data_8S2R
# 
_entry.id   8S2R 
# 
_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   8S2R         pdb_00008s2r 10.2210/pdb8s2r/pdb 
WWPDB D_1292136716 ?            ?                   
# 
_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                        8S2R 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              matthias.boll@biologie.uni-freiburg.de 
_pdbx_contact_author.name_first         Matthias 
_pdbx_contact_author.name_last          Boll 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8062-8049 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ermler, U.' 1 ? 
'Boll, M.'   2 ? 
'Fuchs, J.'  3 ? 
'Demmer, U.' 4 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'X-ray structure of the BzdNO-benzoyl-CoA complex' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ermler, U.' 1 ? 
primary 'Boll, M.'   2 ? 
primary 'Fuchs, J.'  3 ? 
primary 'Demmer, U.' 4 ? 
# 
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 BzdO                                     51272.199 2   ? ? ? ? 
2 polymer     man BzdN                                     43482.336 2   ? ? ? ? 
3 non-polymer syn 'benzoyl coenzyme A'                     871.640   2   ? ? ? ? 
4 non-polymer syn GLYCEROL                                 92.094    3   ? ? ? ? 
5 non-polymer nat 'IRON/SULFUR CLUSTER'                    351.640   2   ? ? ? ? 
6 non-polymer syn 'Double cubane cluster'                  735.345   2   ? ? ? ? 
7 non-polymer syn 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL 122.143   2   ? ? ? ? 
8 water       nat water                                    18.015    793 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MNAMANKYPTEQLKLWGKAKELREQYYMNYARAKEKGGIRWSGSAWALDAIPAGLGEDVYSLTGEPYAAAVAHDRKFAKE
CMDAAEAYGFARDLCSYMRIYWGGMHLNKYAFGGEFPKPDFVFQTQICCSHSKWYQHVAKEEKIPEFYLDVGVGPYRDMT
DARLDYVANQLHDGIAFVEKASGRKFDDELFIKAVKNEMRSTSRWADICALNKVKPAPLDEKTMYSLYVLCTLSKSSQWC
ADFMDELYEEVKDRVARGIAAVPNEAIRLMTDTQPPWSFLKIFRYLETYGAVSIGSLYTFALEGIWEDKPDGSWGGRTLP
WDKGIEINDRDTAVRLYADWNLSKPQWQHFYDPTIKSDMMLRIIKEWQVDGVMLHLNRGCEGLSVGIMENRLAIAKSGTP
VMTFEGNMGDEREFDEVRTQARVDAFMEQLGVRRQAASAWSHPQFEK
;
;MNAMANKYPTEQLKLWGKAKELREQYYMNYARAKEKGGIRWSGSAWALDAIPAGLGEDVYSLTGEPYAAAVAHDRKFAKE
CMDAAEAYGFARDLCSYMRIYWGGMHLNKYAFGGEFPKPDFVFQTQICCSHSKWYQHVAKEEKIPEFYLDVGVGPYRDMT
DARLDYVANQLHDGIAFVEKASGRKFDDELFIKAVKNEMRSTSRWADICALNKVKPAPLDEKTMYSLYVLCTLSKSSQWC
ADFMDELYEEVKDRVARGIAAVPNEAIRLMTDTQPPWSFLKIFRYLETYGAVSIGSLYTFALEGIWEDKPDGSWGGRTLP
WDKGIEINDRDTAVRLYADWNLSKPQWQHFYDPTIKSDMMLRIIKEWQVDGVMLHLNRGCEGLSVGIMENRLAIAKSGTP
VMTFEGNMGDEREFDEVRTQARVDAFMEQLGVRRQAASAWSHPQFEK
;
A,C ? 
2 'polypeptide(L)' no no 
;MSDGLFDQFKTWYEKRHDYARDWKVRTGGQVVATMCTYTPEELLIAAGMLPVRVLGAHEPQNVTEPHIFGMFCPFCRDSL
AQGLLGRFDYAEGVTLTQSCIQYRQTFGSWRLHVPTVKWDYYVPMPNEVQSPHARKAHYEEVQAFRVFLQTLTGKEITDA
MLSDALAVCDENRRLLRELYEYRKAADPKVTGVEALYASLTAQFIDKREHNEMLKKTLAALPNRKVERKTGARFMTIGSE
NDDIAFMGMVESVGATIVIDDQCSGSRYFWNASKPEGDVIKAIAERYCDRPACPTKDYPAHTRFDHVLGMAKEYNVEGAI
FLQQKFCDPHEGDYPDLKRHLEENGIPTLFLEFDITNPIGPFRIRIEAFLETLSEEELF
;
;MSDGLFDQFKTWYEKRHDYARDWKVRTGGQVVATMCTYTPEELLIAAGMLPVRVLGAHEPQNVTEPHIFGMFCPFCRDSL
AQGLLGRFDYAEGVTLTQSCIQYRQTFGSWRLHVPTVKWDYYVPMPNEVQSPHARKAHYEEVQAFRVFLQTLTGKEITDA
MLSDALAVCDENRRLLRELYEYRKAADPKVTGVEALYASLTAQFIDKREHNEMLKKTLAALPNRKVERKTGARFMTIGSE
NDDIAFMGMVESVGATIVIDDQCSGSRYFWNASKPEGDVIKAIAERYCDRPACPTKDYPAHTRFDHVLGMAKEYNVEGAI
FLQQKFCDPHEGDYPDLKRHLEENGIPTLFLEFDITNPIGPFRIRIEAFLETLSEEELF
;
B,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'benzoyl coenzyme A'                     BYC 
4 GLYCEROL                                 GOL 
5 'IRON/SULFUR CLUSTER'                    SF4 
6 'Double cubane cluster'                  BJ8 
7 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL TRS 
8 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASN n 
1 3   ALA n 
1 4   MET n 
1 5   ALA n 
1 6   ASN n 
1 7   LYS n 
1 8   TYR n 
1 9   PRO n 
1 10  THR n 
1 11  GLU n 
1 12  GLN n 
1 13  LEU n 
1 14  LYS n 
1 15  LEU n 
1 16  TRP n 
1 17  GLY n 
1 18  LYS n 
1 19  ALA n 
1 20  LYS n 
1 21  GLU n 
1 22  LEU n 
1 23  ARG n 
1 24  GLU n 
1 25  GLN n 
1 26  TYR n 
1 27  TYR n 
1 28  MET n 
1 29  ASN n 
1 30  TYR n 
1 31  ALA n 
1 32  ARG n 
1 33  ALA n 
1 34  LYS n 
1 35  GLU n 
1 36  LYS n 
1 37  GLY n 
1 38  GLY n 
1 39  ILE n 
1 40  ARG n 
1 41  TRP n 
1 42  SER n 
1 43  GLY n 
1 44  SER n 
1 45  ALA n 
1 46  TRP n 
1 47  ALA n 
1 48  LEU n 
1 49  ASP n 
1 50  ALA n 
1 51  ILE n 
1 52  PRO n 
1 53  ALA n 
1 54  GLY n 
1 55  LEU n 
1 56  GLY n 
1 57  GLU n 
1 58  ASP n 
1 59  VAL n 
1 60  TYR n 
1 61  SER n 
1 62  LEU n 
1 63  THR n 
1 64  GLY n 
1 65  GLU n 
1 66  PRO n 
1 67  TYR n 
1 68  ALA n 
1 69  ALA n 
1 70  ALA n 
1 71  VAL n 
1 72  ALA n 
1 73  HIS n 
1 74  ASP n 
1 75  ARG n 
1 76  LYS n 
1 77  PHE n 
1 78  ALA n 
1 79  LYS n 
1 80  GLU n 
1 81  CYS n 
1 82  MET n 
1 83  ASP n 
1 84  ALA n 
1 85  ALA n 
1 86  GLU n 
1 87  ALA n 
1 88  TYR n 
1 89  GLY n 
1 90  PHE n 
1 91  ALA n 
1 92  ARG n 
1 93  ASP n 
1 94  LEU n 
1 95  CYS n 
1 96  SER n 
1 97  TYR n 
1 98  MET n 
1 99  ARG n 
1 100 ILE n 
1 101 TYR n 
1 102 TRP n 
1 103 GLY n 
1 104 GLY n 
1 105 MET n 
1 106 HIS n 
1 107 LEU n 
1 108 ASN n 
1 109 LYS n 
1 110 TYR n 
1 111 ALA n 
1 112 PHE n 
1 113 GLY n 
1 114 GLY n 
1 115 GLU n 
1 116 PHE n 
1 117 PRO n 
1 118 LYS n 
1 119 PRO n 
1 120 ASP n 
1 121 PHE n 
1 122 VAL n 
1 123 PHE n 
1 124 GLN n 
1 125 THR n 
1 126 GLN n 
1 127 ILE n 
1 128 CYS n 
1 129 CYS n 
1 130 SER n 
1 131 HIS n 
1 132 SER n 
1 133 LYS n 
1 134 TRP n 
1 135 TYR n 
1 136 GLN n 
1 137 HIS n 
1 138 VAL n 
1 139 ALA n 
1 140 LYS n 
1 141 GLU n 
1 142 GLU n 
1 143 LYS n 
1 144 ILE n 
1 145 PRO n 
1 146 GLU n 
1 147 PHE n 
1 148 TYR n 
1 149 LEU n 
1 150 ASP n 
1 151 VAL n 
1 152 GLY n 
1 153 VAL n 
1 154 GLY n 
1 155 PRO n 
1 156 TYR n 
1 157 ARG n 
1 158 ASP n 
1 159 MET n 
1 160 THR n 
1 161 ASP n 
1 162 ALA n 
1 163 ARG n 
1 164 LEU n 
1 165 ASP n 
1 166 TYR n 
1 167 VAL n 
1 168 ALA n 
1 169 ASN n 
1 170 GLN n 
1 171 LEU n 
1 172 HIS n 
1 173 ASP n 
1 174 GLY n 
1 175 ILE n 
1 176 ALA n 
1 177 PHE n 
1 178 VAL n 
1 179 GLU n 
1 180 LYS n 
1 181 ALA n 
1 182 SER n 
1 183 GLY n 
1 184 ARG n 
1 185 LYS n 
1 186 PHE n 
1 187 ASP n 
1 188 ASP n 
1 189 GLU n 
1 190 LEU n 
1 191 PHE n 
1 192 ILE n 
1 193 LYS n 
1 194 ALA n 
1 195 VAL n 
1 196 LYS n 
1 197 ASN n 
1 198 GLU n 
1 199 MET n 
1 200 ARG n 
1 201 SER n 
1 202 THR n 
1 203 SER n 
1 204 ARG n 
1 205 TRP n 
1 206 ALA n 
1 207 ASP n 
1 208 ILE n 
1 209 CYS n 
1 210 ALA n 
1 211 LEU n 
1 212 ASN n 
1 213 LYS n 
1 214 VAL n 
1 215 LYS n 
1 216 PRO n 
1 217 ALA n 
1 218 PRO n 
1 219 LEU n 
1 220 ASP n 
1 221 GLU n 
1 222 LYS n 
1 223 THR n 
1 224 MET n 
1 225 TYR n 
1 226 SER n 
1 227 LEU n 
1 228 TYR n 
1 229 VAL n 
1 230 LEU n 
1 231 CYS n 
1 232 THR n 
1 233 LEU n 
1 234 SER n 
1 235 LYS n 
1 236 SER n 
1 237 SER n 
1 238 GLN n 
1 239 TRP n 
1 240 CYS n 
1 241 ALA n 
1 242 ASP n 
1 243 PHE n 
1 244 MET n 
1 245 ASP n 
1 246 GLU n 
1 247 LEU n 
1 248 TYR n 
1 249 GLU n 
1 250 GLU n 
1 251 VAL n 
1 252 LYS n 
1 253 ASP n 
1 254 ARG n 
1 255 VAL n 
1 256 ALA n 
1 257 ARG n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 ALA n 
1 262 VAL n 
1 263 PRO n 
1 264 ASN n 
1 265 GLU n 
1 266 ALA n 
1 267 ILE n 
1 268 ARG n 
1 269 LEU n 
1 270 MET n 
1 271 THR n 
1 272 ASP n 
1 273 THR n 
1 274 GLN n 
1 275 PRO n 
1 276 PRO n 
1 277 TRP n 
1 278 SER n 
1 279 PHE n 
1 280 LEU n 
1 281 LYS n 
1 282 ILE n 
1 283 PHE n 
1 284 ARG n 
1 285 TYR n 
1 286 LEU n 
1 287 GLU n 
1 288 THR n 
1 289 TYR n 
1 290 GLY n 
1 291 ALA n 
1 292 VAL n 
1 293 SER n 
1 294 ILE n 
1 295 GLY n 
1 296 SER n 
1 297 LEU n 
1 298 TYR n 
1 299 THR n 
1 300 PHE n 
1 301 ALA n 
1 302 LEU n 
1 303 GLU n 
1 304 GLY n 
1 305 ILE n 
1 306 TRP n 
1 307 GLU n 
1 308 ASP n 
1 309 LYS n 
1 310 PRO n 
1 311 ASP n 
1 312 GLY n 
1 313 SER n 
1 314 TRP n 
1 315 GLY n 
1 316 GLY n 
1 317 ARG n 
1 318 THR n 
1 319 LEU n 
1 320 PRO n 
1 321 TRP n 
1 322 ASP n 
1 323 LYS n 
1 324 GLY n 
1 325 ILE n 
1 326 GLU n 
1 327 ILE n 
1 328 ASN n 
1 329 ASP n 
1 330 ARG n 
1 331 ASP n 
1 332 THR n 
1 333 ALA n 
1 334 VAL n 
1 335 ARG n 
1 336 LEU n 
1 337 TYR n 
1 338 ALA n 
1 339 ASP n 
1 340 TRP n 
1 341 ASN n 
1 342 LEU n 
1 343 SER n 
1 344 LYS n 
1 345 PRO n 
1 346 GLN n 
1 347 TRP n 
1 348 GLN n 
1 349 HIS n 
1 350 PHE n 
1 351 TYR n 
1 352 ASP n 
1 353 PRO n 
1 354 THR n 
1 355 ILE n 
1 356 LYS n 
1 357 SER n 
1 358 ASP n 
1 359 MET n 
1 360 MET n 
1 361 LEU n 
1 362 ARG n 
1 363 ILE n 
1 364 ILE n 
1 365 LYS n 
1 366 GLU n 
1 367 TRP n 
1 368 GLN n 
1 369 VAL n 
1 370 ASP n 
1 371 GLY n 
1 372 VAL n 
1 373 MET n 
1 374 LEU n 
1 375 HIS n 
1 376 LEU n 
1 377 ASN n 
1 378 ARG n 
1 379 GLY n 
1 380 CYS n 
1 381 GLU n 
1 382 GLY n 
1 383 LEU n 
1 384 SER n 
1 385 VAL n 
1 386 GLY n 
1 387 ILE n 
1 388 MET n 
1 389 GLU n 
1 390 ASN n 
1 391 ARG n 
1 392 LEU n 
1 393 ALA n 
1 394 ILE n 
1 395 ALA n 
1 396 LYS n 
1 397 SER n 
1 398 GLY n 
1 399 THR n 
1 400 PRO n 
1 401 VAL n 
1 402 MET n 
1 403 THR n 
1 404 PHE n 
1 405 GLU n 
1 406 GLY n 
1 407 ASN n 
1 408 MET n 
1 409 GLY n 
1 410 ASP n 
1 411 GLU n 
1 412 ARG n 
1 413 GLU n 
1 414 PHE n 
1 415 ASP n 
1 416 GLU n 
1 417 VAL n 
1 418 ARG n 
1 419 THR n 
1 420 GLN n 
1 421 ALA n 
1 422 ARG n 
1 423 VAL n 
1 424 ASP n 
1 425 ALA n 
1 426 PHE n 
1 427 MET n 
1 428 GLU n 
1 429 GLN n 
1 430 LEU n 
1 431 GLY n 
1 432 VAL n 
1 433 ARG n 
1 434 ARG n 
1 435 GLN n 
1 436 ALA n 
1 437 ALA n 
1 438 SER n 
1 439 ALA n 
1 440 TRP n 
1 441 SER n 
1 442 HIS n 
1 443 PRO n 
1 444 GLN n 
1 445 PHE n 
1 446 GLU n 
1 447 LYS n 
2 1   MET n 
2 2   SER n 
2 3   ASP n 
2 4   GLY n 
2 5   LEU n 
2 6   PHE n 
2 7   ASP n 
2 8   GLN n 
2 9   PHE n 
2 10  LYS n 
2 11  THR n 
2 12  TRP n 
2 13  TYR n 
2 14  GLU n 
2 15  LYS n 
2 16  ARG n 
2 17  HIS n 
2 18  ASP n 
2 19  TYR n 
2 20  ALA n 
2 21  ARG n 
2 22  ASP n 
2 23  TRP n 
2 24  LYS n 
2 25  VAL n 
2 26  ARG n 
2 27  THR n 
2 28  GLY n 
2 29  GLY n 
2 30  GLN n 
2 31  VAL n 
2 32  VAL n 
2 33  ALA n 
2 34  THR n 
2 35  MET n 
2 36  CYS n 
2 37  THR n 
2 38  TYR n 
2 39  THR n 
2 40  PRO n 
2 41  GLU n 
2 42  GLU n 
2 43  LEU n 
2 44  LEU n 
2 45  ILE n 
2 46  ALA n 
2 47  ALA n 
2 48  GLY n 
2 49  MET n 
2 50  LEU n 
2 51  PRO n 
2 52  VAL n 
2 53  ARG n 
2 54  VAL n 
2 55  LEU n 
2 56  GLY n 
2 57  ALA n 
2 58  HIS n 
2 59  GLU n 
2 60  PRO n 
2 61  GLN n 
2 62  ASN n 
2 63  VAL n 
2 64  THR n 
2 65  GLU n 
2 66  PRO n 
2 67  HIS n 
2 68  ILE n 
2 69  PHE n 
2 70  GLY n 
2 71  MET n 
2 72  PHE n 
2 73  CYS n 
2 74  PRO n 
2 75  PHE n 
2 76  CYS n 
2 77  ARG n 
2 78  ASP n 
2 79  SER n 
2 80  LEU n 
2 81  ALA n 
2 82  GLN n 
2 83  GLY n 
2 84  LEU n 
2 85  LEU n 
2 86  GLY n 
2 87  ARG n 
2 88  PHE n 
2 89  ASP n 
2 90  TYR n 
2 91  ALA n 
2 92  GLU n 
2 93  GLY n 
2 94  VAL n 
2 95  THR n 
2 96  LEU n 
2 97  THR n 
2 98  GLN n 
2 99  SER n 
2 100 CYS n 
2 101 ILE n 
2 102 GLN n 
2 103 TYR n 
2 104 ARG n 
2 105 GLN n 
2 106 THR n 
2 107 PHE n 
2 108 GLY n 
2 109 SER n 
2 110 TRP n 
2 111 ARG n 
2 112 LEU n 
2 113 HIS n 
2 114 VAL n 
2 115 PRO n 
2 116 THR n 
2 117 VAL n 
2 118 LYS n 
2 119 TRP n 
2 120 ASP n 
2 121 TYR n 
2 122 TYR n 
2 123 VAL n 
2 124 PRO n 
2 125 MET n 
2 126 PRO n 
2 127 ASN n 
2 128 GLU n 
2 129 VAL n 
2 130 GLN n 
2 131 SER n 
2 132 PRO n 
2 133 HIS n 
2 134 ALA n 
2 135 ARG n 
2 136 LYS n 
2 137 ALA n 
2 138 HIS n 
2 139 TYR n 
2 140 GLU n 
2 141 GLU n 
2 142 VAL n 
2 143 GLN n 
2 144 ALA n 
2 145 PHE n 
2 146 ARG n 
2 147 VAL n 
2 148 PHE n 
2 149 LEU n 
2 150 GLN n 
2 151 THR n 
2 152 LEU n 
2 153 THR n 
2 154 GLY n 
2 155 LYS n 
2 156 GLU n 
2 157 ILE n 
2 158 THR n 
2 159 ASP n 
2 160 ALA n 
2 161 MET n 
2 162 LEU n 
2 163 SER n 
2 164 ASP n 
2 165 ALA n 
2 166 LEU n 
2 167 ALA n 
2 168 VAL n 
2 169 CYS n 
2 170 ASP n 
2 171 GLU n 
2 172 ASN n 
2 173 ARG n 
2 174 ARG n 
2 175 LEU n 
2 176 LEU n 
2 177 ARG n 
2 178 GLU n 
2 179 LEU n 
2 180 TYR n 
2 181 GLU n 
2 182 TYR n 
2 183 ARG n 
2 184 LYS n 
2 185 ALA n 
2 186 ALA n 
2 187 ASP n 
2 188 PRO n 
2 189 LYS n 
2 190 VAL n 
2 191 THR n 
2 192 GLY n 
2 193 VAL n 
2 194 GLU n 
2 195 ALA n 
2 196 LEU n 
2 197 TYR n 
2 198 ALA n 
2 199 SER n 
2 200 LEU n 
2 201 THR n 
2 202 ALA n 
2 203 GLN n 
2 204 PHE n 
2 205 ILE n 
2 206 ASP n 
2 207 LYS n 
2 208 ARG n 
2 209 GLU n 
2 210 HIS n 
2 211 ASN n 
2 212 GLU n 
2 213 MET n 
2 214 LEU n 
2 215 LYS n 
2 216 LYS n 
2 217 THR n 
2 218 LEU n 
2 219 ALA n 
2 220 ALA n 
2 221 LEU n 
2 222 PRO n 
2 223 ASN n 
2 224 ARG n 
2 225 LYS n 
2 226 VAL n 
2 227 GLU n 
2 228 ARG n 
2 229 LYS n 
2 230 THR n 
2 231 GLY n 
2 232 ALA n 
2 233 ARG n 
2 234 PHE n 
2 235 MET n 
2 236 THR n 
2 237 ILE n 
2 238 GLY n 
2 239 SER n 
2 240 GLU n 
2 241 ASN n 
2 242 ASP n 
2 243 ASP n 
2 244 ILE n 
2 245 ALA n 
2 246 PHE n 
2 247 MET n 
2 248 GLY n 
2 249 MET n 
2 250 VAL n 
2 251 GLU n 
2 252 SER n 
2 253 VAL n 
2 254 GLY n 
2 255 ALA n 
2 256 THR n 
2 257 ILE n 
2 258 VAL n 
2 259 ILE n 
2 260 ASP n 
2 261 ASP n 
2 262 GLN n 
2 263 CYS n 
2 264 SER n 
2 265 GLY n 
2 266 SER n 
2 267 ARG n 
2 268 TYR n 
2 269 PHE n 
2 270 TRP n 
2 271 ASN n 
2 272 ALA n 
2 273 SER n 
2 274 LYS n 
2 275 PRO n 
2 276 GLU n 
2 277 GLY n 
2 278 ASP n 
2 279 VAL n 
2 280 ILE n 
2 281 LYS n 
2 282 ALA n 
2 283 ILE n 
2 284 ALA n 
2 285 GLU n 
2 286 ARG n 
2 287 TYR n 
2 288 CYS n 
2 289 ASP n 
2 290 ARG n 
2 291 PRO n 
2 292 ALA n 
2 293 CYS n 
2 294 PRO n 
2 295 THR n 
2 296 LYS n 
2 297 ASP n 
2 298 TYR n 
2 299 PRO n 
2 300 ALA n 
2 301 HIS n 
2 302 THR n 
2 303 ARG n 
2 304 PHE n 
2 305 ASP n 
2 306 HIS n 
2 307 VAL n 
2 308 LEU n 
2 309 GLY n 
2 310 MET n 
2 311 ALA n 
2 312 LYS n 
2 313 GLU n 
2 314 TYR n 
2 315 ASN n 
2 316 VAL n 
2 317 GLU n 
2 318 GLY n 
2 319 ALA n 
2 320 ILE n 
2 321 PHE n 
2 322 LEU n 
2 323 GLN n 
2 324 GLN n 
2 325 LYS n 
2 326 PHE n 
2 327 CYS n 
2 328 ASP n 
2 329 PRO n 
2 330 HIS n 
2 331 GLU n 
2 332 GLY n 
2 333 ASP n 
2 334 TYR n 
2 335 PRO n 
2 336 ASP n 
2 337 LEU n 
2 338 LYS n 
2 339 ARG n 
2 340 HIS n 
2 341 LEU n 
2 342 GLU n 
2 343 GLU n 
2 344 ASN n 
2 345 GLY n 
2 346 ILE n 
2 347 PRO n 
2 348 THR n 
2 349 LEU n 
2 350 PHE n 
2 351 LEU n 
2 352 GLU n 
2 353 PHE n 
2 354 ASP n 
2 355 ILE n 
2 356 THR n 
2 357 ASN n 
2 358 PRO n 
2 359 ILE n 
2 360 GLY n 
2 361 PRO n 
2 362 PHE n 
2 363 ARG n 
2 364 ILE n 
2 365 ARG n 
2 366 ILE n 
2 367 GLU n 
2 368 ALA n 
2 369 PHE n 
2 370 LEU n 
2 371 GLU n 
2 372 THR n 
2 373 LEU n 
2 374 SER n 
2 375 GLU n 
2 376 GLU n 
2 377 GLU n 
2 378 LEU n 
2 379 PHE n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 447 ? ? bzdO ? ? ? ? ? ? 'Azoarcus sp. CIB' 198107 ? ? ? ? ? ? ? ? 'Escherichia coli K-12' 
83333 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 379 ? ? bzdN ? ? ? ? ? ? 'Azoarcus sp. CIB' 198107 ? ? ? ? ? ? ? ? 'Escherichia coli K-12' 
83333 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                  ?                               'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE                                 ?                               'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE                               ?                               'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                          ?                               'C4 H7 N O4'          133.103 
BJ8 non-polymer         . 'Double cubane cluster'                  ?                               'Fe8 S9'              735.345 
BYC non-polymer         . 'benzoyl coenzyme A'                     ?                               'C28 H40 N7 O17 P3 S' 871.640 
CYS 'L-peptide linking' y CYSTEINE                                 ?                               'C3 H7 N O2 S'        121.158 
DOD non-polymer         . 'DEUTERATED WATER'                       ?                               'D2 O'                20.028  
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  
GOL non-polymer         . GLYCEROL                                 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'            92.094  
HIS 'L-peptide linking' y HISTIDINE                                ?                               'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                    ?                               'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                               ?                               'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                                  ?                               'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                   ?                               'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                               ?                               'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE                            ?                               'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                                  ?                               'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                                   ?                               'C3 H7 N O3'          105.093 
SF4 non-polymer         . 'IRON/SULFUR CLUSTER'                    ?                               'Fe4 S4'              351.640 
THR 'L-peptide linking' y THREONINE                                ?                               'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                               ?                               'C11 H12 N2 O2'       204.225 
TRS non-polymer         . 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL 'TRIS BUFFER'                   'C4 H12 N O3 1'       122.143 
TYR 'L-peptide linking' y TYROSINE                                 ?                               'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                                   ?                               'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ASN 2   2   ?   ?   ?   A . n 
A 1 3   ALA 3   3   ?   ?   ?   A . n 
A 1 4   MET 4   4   ?   ?   ?   A . n 
A 1 5   ALA 5   5   5   ALA ALA A . n 
A 1 6   ASN 6   6   6   ASN ASN A . n 
A 1 7   LYS 7   7   7   LYS LYS A . n 
A 1 8   TYR 8   8   8   TYR TYR A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  THR 10  10  10  THR THR A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  GLN 12  12  12  GLN GLN A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  LYS 14  14  14  LYS LYS A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  ARG 23  23  23  ARG ARG A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  TYR 26  26  26  TYR TYR A . n 
A 1 27  TYR 27  27  27  TYR TYR A . n 
A 1 28  MET 28  28  28  MET MET A . n 
A 1 29  ASN 29  29  29  ASN ASN A . n 
A 1 30  TYR 30  30  30  TYR TYR A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  ARG 32  32  32  ARG ARG A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  ILE 39  39  39  ILE ILE A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  TRP 41  41  41  TRP TRP A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  TRP 46  46  46  TRP TRP A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  LEU 48  48  48  LEU LEU A . n 
A 1 49  ASP 49  49  49  ASP ASP A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  ILE 51  51  51  ILE ILE A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  ASP 58  58  58  ASP ASP A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  TYR 60  60  60  TYR TYR A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  HIS 73  73  73  HIS HIS A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  ARG 75  75  75  ARG ARG A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  PHE 77  77  77  PHE PHE A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  LYS 79  79  79  LYS LYS A . n 
A 1 80  GLU 80  80  80  GLU GLU A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  ALA 85  85  85  ALA ALA A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  ARG 92  92  92  ARG ARG A . n 
A 1 93  ASP 93  93  93  ASP ASP A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  CYS 95  95  95  CYS CYS A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  MET 98  98  98  MET MET A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 TRP 102 102 102 TRP TRP A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 MET 105 105 105 MET MET A . n 
A 1 106 HIS 106 106 106 HIS HIS A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 TYR 110 110 110 TYR TYR A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 PRO 119 119 119 PRO PRO A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 PHE 121 121 121 PHE PHE A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 PHE 123 123 123 PHE PHE A . n 
A 1 124 GLN 124 124 124 GLN GLN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 GLN 126 126 126 GLN GLN A . n 
A 1 127 ILE 127 127 127 ILE ILE A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 CYS 129 129 129 CYS CYS A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 HIS 131 131 131 HIS HIS A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 LYS 133 133 133 LYS LYS A . n 
A 1 134 TRP 134 134 134 TRP TRP A . n 
A 1 135 TYR 135 135 135 TYR TYR A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 HIS 137 137 137 HIS HIS A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 GLU 142 142 142 GLU GLU A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 PRO 145 145 145 PRO PRO A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 TYR 148 148 148 TYR TYR A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 TYR 156 156 156 TYR TYR A . n 
A 1 157 ARG 157 157 157 ARG ARG A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 MET 159 159 159 MET MET A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 ASP 165 165 165 ASP ASP A . n 
A 1 166 TYR 166 166 166 TYR TYR A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 ASN 169 169 169 ASN ASN A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 ILE 175 175 175 ILE ILE A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 GLU 179 179 179 GLU GLU A . n 
A 1 180 LYS 180 180 180 LYS LYS A . n 
A 1 181 ALA 181 181 181 ALA ALA A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 LYS 185 185 185 LYS LYS A . n 
A 1 186 PHE 186 186 186 PHE PHE A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 PHE 191 191 191 PHE PHE A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 LYS 193 193 193 LYS LYS A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 LYS 196 196 196 LYS LYS A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 GLU 198 198 198 GLU GLU A . n 
A 1 199 MET 199 199 199 MET MET A . n 
A 1 200 ARG 200 200 200 ARG ARG A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 TRP 205 205 205 TRP TRP A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 ASP 207 207 207 ASP ASP A . n 
A 1 208 ILE 208 208 208 ILE ILE A . n 
A 1 209 CYS 209 209 209 CYS CYS A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 ASN 212 212 212 ASN ASN A . n 
A 1 213 LYS 213 213 213 LYS LYS A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 PRO 216 216 216 PRO PRO A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 PRO 218 218 218 PRO PRO A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 LYS 222 222 222 LYS LYS A . n 
A 1 223 THR 223 223 223 THR THR A . n 
A 1 224 MET 224 224 224 MET MET A . n 
A 1 225 TYR 225 225 225 TYR TYR A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 TYR 228 228 228 TYR TYR A . n 
A 1 229 VAL 229 229 229 VAL VAL A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 CYS 231 231 231 CYS CYS A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 SER 234 234 234 SER SER A . n 
A 1 235 LYS 235 235 235 LYS LYS A . n 
A 1 236 SER 236 236 236 SER SER A . n 
A 1 237 SER 237 237 237 SER SER A . n 
A 1 238 GLN 238 238 238 GLN GLN A . n 
A 1 239 TRP 239 239 239 TRP TRP A . n 
A 1 240 CYS 240 240 240 CYS CYS A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 PHE 243 243 243 PHE PHE A . n 
A 1 244 MET 244 244 244 MET MET A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 GLU 246 246 246 GLU GLU A . n 
A 1 247 LEU 247 247 247 LEU LEU A . n 
A 1 248 TYR 248 248 248 TYR TYR A . n 
A 1 249 GLU 249 249 249 GLU GLU A . n 
A 1 250 GLU 250 250 250 GLU GLU A . n 
A 1 251 VAL 251 251 251 VAL VAL A . n 
A 1 252 LYS 252 252 252 LYS LYS A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 ARG 254 254 254 ARG ARG A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 ALA 256 256 256 ALA ALA A . n 
A 1 257 ARG 257 257 257 ARG ARG A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 ALA 261 261 261 ALA ALA A . n 
A 1 262 VAL 262 262 262 VAL VAL A . n 
A 1 263 PRO 263 263 263 PRO PRO A . n 
A 1 264 ASN 264 264 264 ASN ASN A . n 
A 1 265 GLU 265 265 265 GLU GLU A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 ARG 268 268 268 ARG ARG A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 MET 270 270 270 MET MET A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 ASP 272 272 272 ASP ASP A . n 
A 1 273 THR 273 273 273 THR THR A . n 
A 1 274 GLN 274 274 274 GLN GLN A . n 
A 1 275 PRO 275 275 275 PRO PRO A . n 
A 1 276 PRO 276 276 276 PRO PRO A . n 
A 1 277 TRP 277 277 277 TRP TRP A . n 
A 1 278 SER 278 278 278 SER SER A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 LYS 281 281 281 LYS LYS A . n 
A 1 282 ILE 282 282 282 ILE ILE A . n 
A 1 283 PHE 283 283 283 PHE PHE A . n 
A 1 284 ARG 284 284 284 ARG ARG A . n 
A 1 285 TYR 285 285 285 TYR TYR A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 GLU 287 287 287 GLU GLU A . n 
A 1 288 THR 288 288 288 THR THR A . n 
A 1 289 TYR 289 289 289 TYR TYR A . n 
A 1 290 GLY 290 290 290 GLY GLY A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 VAL 292 292 292 VAL VAL A . n 
A 1 293 SER 293 293 293 SER SER A . n 
A 1 294 ILE 294 294 294 ILE ILE A . n 
A 1 295 GLY 295 295 295 GLY GLY A . n 
A 1 296 SER 296 296 296 SER SER A . n 
A 1 297 LEU 297 297 297 LEU LEU A . n 
A 1 298 TYR 298 298 298 TYR TYR A . n 
A 1 299 THR 299 299 299 THR THR A . n 
A 1 300 PHE 300 300 300 PHE PHE A . n 
A 1 301 ALA 301 301 301 ALA ALA A . n 
A 1 302 LEU 302 302 302 LEU LEU A . n 
A 1 303 GLU 303 303 303 GLU GLU A . n 
A 1 304 GLY 304 304 304 GLY GLY A . n 
A 1 305 ILE 305 305 305 ILE ILE A . n 
A 1 306 TRP 306 306 306 TRP TRP A . n 
A 1 307 GLU 307 307 307 GLU GLU A . n 
A 1 308 ASP 308 308 308 ASP ASP A . n 
A 1 309 LYS 309 309 309 LYS LYS A . n 
A 1 310 PRO 310 310 310 PRO PRO A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 GLY 312 312 312 GLY GLY A . n 
A 1 313 SER 313 313 313 SER SER A . n 
A 1 314 TRP 314 314 314 TRP TRP A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 GLY 316 316 316 GLY GLY A . n 
A 1 317 ARG 317 317 317 ARG ARG A . n 
A 1 318 THR 318 318 318 THR THR A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 PRO 320 320 320 PRO PRO A . n 
A 1 321 TRP 321 321 321 TRP TRP A . n 
A 1 322 ASP 322 322 322 ASP ASP A . n 
A 1 323 LYS 323 323 323 LYS LYS A . n 
A 1 324 GLY 324 324 324 GLY GLY A . n 
A 1 325 ILE 325 325 325 ILE ILE A . n 
A 1 326 GLU 326 326 326 GLU GLU A . n 
A 1 327 ILE 327 327 327 ILE ILE A . n 
A 1 328 ASN 328 328 328 ASN ASN A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 ARG 330 330 330 ARG ARG A . n 
A 1 331 ASP 331 331 331 ASP ASP A . n 
A 1 332 THR 332 332 332 THR THR A . n 
A 1 333 ALA 333 333 333 ALA ALA A . n 
A 1 334 VAL 334 334 334 VAL VAL A . n 
A 1 335 ARG 335 335 335 ARG ARG A . n 
A 1 336 LEU 336 336 336 LEU LEU A . n 
A 1 337 TYR 337 337 337 TYR TYR A . n 
A 1 338 ALA 338 338 338 ALA ALA A . n 
A 1 339 ASP 339 339 339 ASP ASP A . n 
A 1 340 TRP 340 340 340 TRP TRP A . n 
A 1 341 ASN 341 341 341 ASN ASN A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 SER 343 343 343 SER SER A . n 
A 1 344 LYS 344 344 344 LYS LYS A . n 
A 1 345 PRO 345 345 345 PRO PRO A . n 
A 1 346 GLN 346 346 346 GLN GLN A . n 
A 1 347 TRP 347 347 347 TRP TRP A . n 
A 1 348 GLN 348 348 348 GLN GLN A . n 
A 1 349 HIS 349 349 349 HIS HIS A . n 
A 1 350 PHE 350 350 350 PHE PHE A . n 
A 1 351 TYR 351 351 351 TYR TYR A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 PRO 353 353 353 PRO PRO A . n 
A 1 354 THR 354 354 354 THR THR A . n 
A 1 355 ILE 355 355 355 ILE ILE A . n 
A 1 356 LYS 356 356 356 LYS LYS A . n 
A 1 357 SER 357 357 357 SER SER A . n 
A 1 358 ASP 358 358 358 ASP ASP A . n 
A 1 359 MET 359 359 359 MET MET A . n 
A 1 360 MET 360 360 360 MET MET A . n 
A 1 361 LEU 361 361 361 LEU LEU A . n 
A 1 362 ARG 362 362 362 ARG ARG A . n 
A 1 363 ILE 363 363 363 ILE ILE A . n 
A 1 364 ILE 364 364 364 ILE ILE A . n 
A 1 365 LYS 365 365 365 LYS LYS A . n 
A 1 366 GLU 366 366 366 GLU GLU A . n 
A 1 367 TRP 367 367 367 TRP TRP A . n 
A 1 368 GLN 368 368 368 GLN GLN A . n 
A 1 369 VAL 369 369 369 VAL VAL A . n 
A 1 370 ASP 370 370 370 ASP ASP A . n 
A 1 371 GLY 371 371 371 GLY GLY A . n 
A 1 372 VAL 372 372 372 VAL VAL A . n 
A 1 373 MET 373 373 373 MET MET A . n 
A 1 374 LEU 374 374 374 LEU LEU A . n 
A 1 375 HIS 375 375 375 HIS HIS A . n 
A 1 376 LEU 376 376 376 LEU LEU A . n 
A 1 377 ASN 377 377 377 ASN ASN A . n 
A 1 378 ARG 378 378 378 ARG ARG A . n 
A 1 379 GLY 379 379 379 GLY GLY A . n 
A 1 380 CYS 380 380 380 CYS CYS A . n 
A 1 381 GLU 381 381 381 GLU GLU A . n 
A 1 382 GLY 382 382 382 GLY GLY A . n 
A 1 383 LEU 383 383 383 LEU LEU A . n 
A 1 384 SER 384 384 384 SER SER A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 GLY 386 386 386 GLY GLY A . n 
A 1 387 ILE 387 387 387 ILE ILE A . n 
A 1 388 MET 388 388 388 MET MET A . n 
A 1 389 GLU 389 389 389 GLU GLU A . n 
A 1 390 ASN 390 390 390 ASN ASN A . n 
A 1 391 ARG 391 391 391 ARG ARG A . n 
A 1 392 LEU 392 392 392 LEU LEU A . n 
A 1 393 ALA 393 393 393 ALA ALA A . n 
A 1 394 ILE 394 394 394 ILE ILE A . n 
A 1 395 ALA 395 395 395 ALA ALA A . n 
A 1 396 LYS 396 396 396 LYS LYS A . n 
A 1 397 SER 397 397 397 SER SER A . n 
A 1 398 GLY 398 398 398 GLY GLY A . n 
A 1 399 THR 399 399 399 THR THR A . n 
A 1 400 PRO 400 400 400 PRO PRO A . n 
A 1 401 VAL 401 401 401 VAL VAL A . n 
A 1 402 MET 402 402 402 MET MET A . n 
A 1 403 THR 403 403 403 THR THR A . n 
A 1 404 PHE 404 404 404 PHE PHE A . n 
A 1 405 GLU 405 405 405 GLU GLU A . n 
A 1 406 GLY 406 406 406 GLY GLY A . n 
A 1 407 ASN 407 407 407 ASN ASN A . n 
A 1 408 MET 408 408 408 MET MET A . n 
A 1 409 GLY 409 409 409 GLY GLY A . n 
A 1 410 ASP 410 410 410 ASP ASP A . n 
A 1 411 GLU 411 411 411 GLU GLU A . n 
A 1 412 ARG 412 412 412 ARG ARG A . n 
A 1 413 GLU 413 413 413 GLU GLU A . n 
A 1 414 PHE 414 414 414 PHE PHE A . n 
A 1 415 ASP 415 415 415 ASP ASP A . n 
A 1 416 GLU 416 416 416 GLU GLU A . n 
A 1 417 VAL 417 417 417 VAL VAL A . n 
A 1 418 ARG 418 418 418 ARG ARG A . n 
A 1 419 THR 419 419 419 THR THR A . n 
A 1 420 GLN 420 420 420 GLN GLN A . n 
A 1 421 ALA 421 421 421 ALA ALA A . n 
A 1 422 ARG 422 422 422 ARG ARG A . n 
A 1 423 VAL 423 423 423 VAL VAL A . n 
A 1 424 ASP 424 424 424 ASP ASP A . n 
A 1 425 ALA 425 425 425 ALA ALA A . n 
A 1 426 PHE 426 426 426 PHE PHE A . n 
A 1 427 MET 427 427 427 MET MET A . n 
A 1 428 GLU 428 428 428 GLU GLU A . n 
A 1 429 GLN 429 429 429 GLN GLN A . n 
A 1 430 LEU 430 430 430 LEU LEU A . n 
A 1 431 GLY 431 431 431 GLY GLY A . n 
A 1 432 VAL 432 432 432 VAL VAL A . n 
A 1 433 ARG 433 433 433 ARG ARG A . n 
A 1 434 ARG 434 434 434 ARG ARG A . n 
A 1 435 GLN 435 435 435 GLN GLN A . n 
A 1 436 ALA 436 436 436 ALA ALA A . n 
A 1 437 ALA 437 437 437 ALA ALA A . n 
A 1 438 SER 438 438 438 SER SER A . n 
A 1 439 ALA 439 439 439 ALA ALA A . n 
A 1 440 TRP 440 440 440 TRP TRP A . n 
A 1 441 SER 441 441 441 SER SER A . n 
A 1 442 HIS 442 442 442 HIS HIS A . n 
A 1 443 PRO 443 443 ?   ?   ?   A . n 
A 1 444 GLN 444 444 ?   ?   ?   A . n 
A 1 445 PHE 445 445 ?   ?   ?   A . n 
A 1 446 GLU 446 446 ?   ?   ?   A . n 
A 1 447 LYS 447 447 ?   ?   ?   A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   SER 2   2   2   SER SER B . n 
B 2 3   ASP 3   3   3   ASP ASP B . n 
B 2 4   GLY 4   4   4   GLY GLY B . n 
B 2 5   LEU 5   5   5   LEU LEU B . n 
B 2 6   PHE 6   6   6   PHE PHE B . n 
B 2 7   ASP 7   7   7   ASP ASP B . n 
B 2 8   GLN 8   8   8   GLN GLN B . n 
B 2 9   PHE 9   9   9   PHE PHE B . n 
B 2 10  LYS 10  10  10  LYS LYS B . n 
B 2 11  THR 11  11  11  THR THR B . n 
B 2 12  TRP 12  12  12  TRP TRP B . n 
B 2 13  TYR 13  13  13  TYR TYR B . n 
B 2 14  GLU 14  14  14  GLU GLU B . n 
B 2 15  LYS 15  15  15  LYS LYS B . n 
B 2 16  ARG 16  16  16  ARG ARG B . n 
B 2 17  HIS 17  17  17  HIS HIS B . n 
B 2 18  ASP 18  18  18  ASP ASP B . n 
B 2 19  TYR 19  19  19  TYR TYR B . n 
B 2 20  ALA 20  20  20  ALA ALA B . n 
B 2 21  ARG 21  21  21  ARG ARG B . n 
B 2 22  ASP 22  22  22  ASP ASP B . n 
B 2 23  TRP 23  23  23  TRP TRP B . n 
B 2 24  LYS 24  24  24  LYS LYS B . n 
B 2 25  VAL 25  25  25  VAL VAL B . n 
B 2 26  ARG 26  26  26  ARG ARG B . n 
B 2 27  THR 27  27  27  THR THR B . n 
B 2 28  GLY 28  28  28  GLY GLY B . n 
B 2 29  GLY 29  29  29  GLY GLY B . n 
B 2 30  GLN 30  30  30  GLN GLN B . n 
B 2 31  VAL 31  31  31  VAL VAL B . n 
B 2 32  VAL 32  32  32  VAL VAL B . n 
B 2 33  ALA 33  33  33  ALA ALA B . n 
B 2 34  THR 34  34  34  THR THR B . n 
B 2 35  MET 35  35  35  MET MET B . n 
B 2 36  CYS 36  36  36  CYS CYS B . n 
B 2 37  THR 37  37  37  THR THR B . n 
B 2 38  TYR 38  38  38  TYR TYR B . n 
B 2 39  THR 39  39  39  THR THR B . n 
B 2 40  PRO 40  40  40  PRO PRO B . n 
B 2 41  GLU 41  41  41  GLU GLU B . n 
B 2 42  GLU 42  42  42  GLU GLU B . n 
B 2 43  LEU 43  43  43  LEU LEU B . n 
B 2 44  LEU 44  44  44  LEU LEU B . n 
B 2 45  ILE 45  45  45  ILE ILE B . n 
B 2 46  ALA 46  46  46  ALA ALA B . n 
B 2 47  ALA 47  47  47  ALA ALA B . n 
B 2 48  GLY 48  48  48  GLY GLY B . n 
B 2 49  MET 49  49  49  MET MET B . n 
B 2 50  LEU 50  50  50  LEU LEU B . n 
B 2 51  PRO 51  51  51  PRO PRO B . n 
B 2 52  VAL 52  52  52  VAL VAL B . n 
B 2 53  ARG 53  53  53  ARG ARG B . n 
B 2 54  VAL 54  54  54  VAL VAL B . n 
B 2 55  LEU 55  55  55  LEU LEU B . n 
B 2 56  GLY 56  56  56  GLY GLY B . n 
B 2 57  ALA 57  57  57  ALA ALA B . n 
B 2 58  HIS 58  58  58  HIS HIS B . n 
B 2 59  GLU 59  59  59  GLU GLU B . n 
B 2 60  PRO 60  60  60  PRO PRO B . n 
B 2 61  GLN 61  61  61  GLN GLN B . n 
B 2 62  ASN 62  62  62  ASN ASN B . n 
B 2 63  VAL 63  63  63  VAL VAL B . n 
B 2 64  THR 64  64  64  THR THR B . n 
B 2 65  GLU 65  65  65  GLU GLU B . n 
B 2 66  PRO 66  66  66  PRO PRO B . n 
B 2 67  HIS 67  67  67  HIS HIS B . n 
B 2 68  ILE 68  68  68  ILE ILE B . n 
B 2 69  PHE 69  69  69  PHE PHE B . n 
B 2 70  GLY 70  70  70  GLY GLY B . n 
B 2 71  MET 71  71  71  MET MET B . n 
B 2 72  PHE 72  72  72  PHE PHE B . n 
B 2 73  CYS 73  73  73  CYS CYS B . n 
B 2 74  PRO 74  74  74  PRO PRO B . n 
B 2 75  PHE 75  75  75  PHE PHE B . n 
B 2 76  CYS 76  76  76  CYS CYS B . n 
B 2 77  ARG 77  77  77  ARG ARG B . n 
B 2 78  ASP 78  78  78  ASP ASP B . n 
B 2 79  SER 79  79  79  SER SER B . n 
B 2 80  LEU 80  80  80  LEU LEU B . n 
B 2 81  ALA 81  81  81  ALA ALA B . n 
B 2 82  GLN 82  82  82  GLN GLN B . n 
B 2 83  GLY 83  83  83  GLY GLY B . n 
B 2 84  LEU 84  84  84  LEU LEU B . n 
B 2 85  LEU 85  85  85  LEU LEU B . n 
B 2 86  GLY 86  86  86  GLY GLY B . n 
B 2 87  ARG 87  87  87  ARG ARG B . n 
B 2 88  PHE 88  88  88  PHE PHE B . n 
B 2 89  ASP 89  89  89  ASP ASP B . n 
B 2 90  TYR 90  90  90  TYR TYR B . n 
B 2 91  ALA 91  91  91  ALA ALA B . n 
B 2 92  GLU 92  92  92  GLU GLU B . n 
B 2 93  GLY 93  93  93  GLY GLY B . n 
B 2 94  VAL 94  94  94  VAL VAL B . n 
B 2 95  THR 95  95  95  THR THR B . n 
B 2 96  LEU 96  96  96  LEU LEU B . n 
B 2 97  THR 97  97  97  THR THR B . n 
B 2 98  GLN 98  98  98  GLN GLN B . n 
B 2 99  SER 99  99  99  SER SER B . n 
B 2 100 CYS 100 100 100 CYS CYS B . n 
B 2 101 ILE 101 101 101 ILE ILE B . n 
B 2 102 GLN 102 102 102 GLN GLN B . n 
B 2 103 TYR 103 103 103 TYR TYR B . n 
B 2 104 ARG 104 104 104 ARG ARG B . n 
B 2 105 GLN 105 105 105 GLN GLN B . n 
B 2 106 THR 106 106 106 THR THR B . n 
B 2 107 PHE 107 107 107 PHE PHE B . n 
B 2 108 GLY 108 108 108 GLY GLY B . n 
B 2 109 SER 109 109 109 SER SER B . n 
B 2 110 TRP 110 110 110 TRP TRP B . n 
B 2 111 ARG 111 111 111 ARG ARG B . n 
B 2 112 LEU 112 112 112 LEU LEU B . n 
B 2 113 HIS 113 113 113 HIS HIS B . n 
B 2 114 VAL 114 114 114 VAL VAL B . n 
B 2 115 PRO 115 115 115 PRO PRO B . n 
B 2 116 THR 116 116 116 THR THR B . n 
B 2 117 VAL 117 117 117 VAL VAL B . n 
B 2 118 LYS 118 118 118 LYS LYS B . n 
B 2 119 TRP 119 119 119 TRP TRP B . n 
B 2 120 ASP 120 120 120 ASP ASP B . n 
B 2 121 TYR 121 121 121 TYR TYR B . n 
B 2 122 TYR 122 122 122 TYR TYR B . n 
B 2 123 VAL 123 123 123 VAL VAL B . n 
B 2 124 PRO 124 124 124 PRO PRO B . n 
B 2 125 MET 125 125 125 MET MET B . n 
B 2 126 PRO 126 126 126 PRO PRO B . n 
B 2 127 ASN 127 127 127 ASN ASN B . n 
B 2 128 GLU 128 128 128 GLU GLU B . n 
B 2 129 VAL 129 129 129 VAL VAL B . n 
B 2 130 GLN 130 130 130 GLN GLN B . n 
B 2 131 SER 131 131 131 SER SER B . n 
B 2 132 PRO 132 132 132 PRO PRO B . n 
B 2 133 HIS 133 133 133 HIS HIS B . n 
B 2 134 ALA 134 134 134 ALA ALA B . n 
B 2 135 ARG 135 135 135 ARG ARG B . n 
B 2 136 LYS 136 136 136 LYS LYS B . n 
B 2 137 ALA 137 137 137 ALA ALA B . n 
B 2 138 HIS 138 138 138 HIS HIS B . n 
B 2 139 TYR 139 139 139 TYR TYR B . n 
B 2 140 GLU 140 140 140 GLU GLU B . n 
B 2 141 GLU 141 141 141 GLU GLU B . n 
B 2 142 VAL 142 142 142 VAL VAL B . n 
B 2 143 GLN 143 143 143 GLN GLN B . n 
B 2 144 ALA 144 144 144 ALA ALA B . n 
B 2 145 PHE 145 145 145 PHE PHE B . n 
B 2 146 ARG 146 146 146 ARG ARG B . n 
B 2 147 VAL 147 147 147 VAL VAL B . n 
B 2 148 PHE 148 148 148 PHE PHE B . n 
B 2 149 LEU 149 149 149 LEU LEU B . n 
B 2 150 GLN 150 150 150 GLN GLN B . n 
B 2 151 THR 151 151 151 THR THR B . n 
B 2 152 LEU 152 152 152 LEU LEU B . n 
B 2 153 THR 153 153 153 THR THR B . n 
B 2 154 GLY 154 154 154 GLY GLY B . n 
B 2 155 LYS 155 155 155 LYS LYS B . n 
B 2 156 GLU 156 156 156 GLU GLU B . n 
B 2 157 ILE 157 157 157 ILE ILE B . n 
B 2 158 THR 158 158 158 THR THR B . n 
B 2 159 ASP 159 159 159 ASP ASP B . n 
B 2 160 ALA 160 160 160 ALA ALA B . n 
B 2 161 MET 161 161 161 MET MET B . n 
B 2 162 LEU 162 162 162 LEU LEU B . n 
B 2 163 SER 163 163 163 SER SER B . n 
B 2 164 ASP 164 164 164 ASP ASP B . n 
B 2 165 ALA 165 165 165 ALA ALA B . n 
B 2 166 LEU 166 166 166 LEU LEU B . n 
B 2 167 ALA 167 167 167 ALA ALA B . n 
B 2 168 VAL 168 168 168 VAL VAL B . n 
B 2 169 CYS 169 169 169 CYS CYS B . n 
B 2 170 ASP 170 170 170 ASP ASP B . n 
B 2 171 GLU 171 171 171 GLU GLU B . n 
B 2 172 ASN 172 172 172 ASN ASN B . n 
B 2 173 ARG 173 173 173 ARG ARG B . n 
B 2 174 ARG 174 174 174 ARG ARG B . n 
B 2 175 LEU 175 175 175 LEU LEU B . n 
B 2 176 LEU 176 176 176 LEU LEU B . n 
B 2 177 ARG 177 177 177 ARG ARG B . n 
B 2 178 GLU 178 178 178 GLU GLU B . n 
B 2 179 LEU 179 179 179 LEU LEU B . n 
B 2 180 TYR 180 180 180 TYR TYR B . n 
B 2 181 GLU 181 181 181 GLU GLU B . n 
B 2 182 TYR 182 182 182 TYR TYR B . n 
B 2 183 ARG 183 183 183 ARG ARG B . n 
B 2 184 LYS 184 184 184 LYS LYS B . n 
B 2 185 ALA 185 185 185 ALA ALA B . n 
B 2 186 ALA 186 186 186 ALA ALA B . n 
B 2 187 ASP 187 187 187 ASP ASP B . n 
B 2 188 PRO 188 188 188 PRO PRO B . n 
B 2 189 LYS 189 189 189 LYS LYS B . n 
B 2 190 VAL 190 190 190 VAL VAL B . n 
B 2 191 THR 191 191 191 THR THR B . n 
B 2 192 GLY 192 192 192 GLY GLY B . n 
B 2 193 VAL 193 193 193 VAL VAL B . n 
B 2 194 GLU 194 194 194 GLU GLU B . n 
B 2 195 ALA 195 195 195 ALA ALA B . n 
B 2 196 LEU 196 196 196 LEU LEU B . n 
B 2 197 TYR 197 197 197 TYR TYR B . n 
B 2 198 ALA 198 198 198 ALA ALA B . n 
B 2 199 SER 199 199 199 SER SER B . n 
B 2 200 LEU 200 200 200 LEU LEU B . n 
B 2 201 THR 201 201 201 THR THR B . n 
B 2 202 ALA 202 202 202 ALA ALA B . n 
B 2 203 GLN 203 203 203 GLN GLN B . n 
B 2 204 PHE 204 204 204 PHE PHE B . n 
B 2 205 ILE 205 205 205 ILE ILE B . n 
B 2 206 ASP 206 206 206 ASP ASP B . n 
B 2 207 LYS 207 207 207 LYS LYS B . n 
B 2 208 ARG 208 208 208 ARG ARG B . n 
B 2 209 GLU 209 209 209 GLU GLU B . n 
B 2 210 HIS 210 210 210 HIS HIS B . n 
B 2 211 ASN 211 211 211 ASN ASN B . n 
B 2 212 GLU 212 212 212 GLU GLU B . n 
B 2 213 MET 213 213 213 MET MET B . n 
B 2 214 LEU 214 214 214 LEU LEU B . n 
B 2 215 LYS 215 215 215 LYS LYS B . n 
B 2 216 LYS 216 216 216 LYS LYS B . n 
B 2 217 THR 217 217 217 THR THR B . n 
B 2 218 LEU 218 218 218 LEU LEU B . n 
B 2 219 ALA 219 219 219 ALA ALA B . n 
B 2 220 ALA 220 220 220 ALA ALA B . n 
B 2 221 LEU 221 221 221 LEU LEU B . n 
B 2 222 PRO 222 222 222 PRO PRO B . n 
B 2 223 ASN 223 223 223 ASN ASN B . n 
B 2 224 ARG 224 224 224 ARG ARG B . n 
B 2 225 LYS 225 225 225 LYS LYS B . n 
B 2 226 VAL 226 226 226 VAL VAL B . n 
B 2 227 GLU 227 227 227 GLU GLU B . n 
B 2 228 ARG 228 228 228 ARG ARG B . n 
B 2 229 LYS 229 229 229 LYS LYS B . n 
B 2 230 THR 230 230 230 THR THR B . n 
B 2 231 GLY 231 231 231 GLY GLY B . n 
B 2 232 ALA 232 232 232 ALA ALA B . n 
B 2 233 ARG 233 233 233 ARG ARG B . n 
B 2 234 PHE 234 234 234 PHE PHE B . n 
B 2 235 MET 235 235 235 MET MET B . n 
B 2 236 THR 236 236 236 THR THR B . n 
B 2 237 ILE 237 237 237 ILE ILE B . n 
B 2 238 GLY 238 238 238 GLY GLY B . n 
B 2 239 SER 239 239 239 SER SER B . n 
B 2 240 GLU 240 240 240 GLU GLU B . n 
B 2 241 ASN 241 241 241 ASN ASN B . n 
B 2 242 ASP 242 242 242 ASP ASP B . n 
B 2 243 ASP 243 243 243 ASP ASP B . n 
B 2 244 ILE 244 244 244 ILE ILE B . n 
B 2 245 ALA 245 245 245 ALA ALA B . n 
B 2 246 PHE 246 246 246 PHE PHE B . n 
B 2 247 MET 247 247 247 MET MET B . n 
B 2 248 GLY 248 248 248 GLY GLY B . n 
B 2 249 MET 249 249 249 MET MET B . n 
B 2 250 VAL 250 250 250 VAL VAL B . n 
B 2 251 GLU 251 251 251 GLU GLU B . n 
B 2 252 SER 252 252 252 SER SER B . n 
B 2 253 VAL 253 253 253 VAL VAL B . n 
B 2 254 GLY 254 254 254 GLY GLY B . n 
B 2 255 ALA 255 255 255 ALA ALA B . n 
B 2 256 THR 256 256 256 THR THR B . n 
B 2 257 ILE 257 257 257 ILE ILE B . n 
B 2 258 VAL 258 258 258 VAL VAL B . n 
B 2 259 ILE 259 259 259 ILE ILE B . n 
B 2 260 ASP 260 260 260 ASP ASP B . n 
B 2 261 ASP 261 261 261 ASP ASP B . n 
B 2 262 GLN 262 262 262 GLN GLN B . n 
B 2 263 CYS 263 263 263 CYS CYS B . n 
B 2 264 SER 264 264 264 SER SER B . n 
B 2 265 GLY 265 265 265 GLY GLY B . n 
B 2 266 SER 266 266 266 SER SER B . n 
B 2 267 ARG 267 267 267 ARG ARG B . n 
B 2 268 TYR 268 268 268 TYR TYR B . n 
B 2 269 PHE 269 269 269 PHE PHE B . n 
B 2 270 TRP 270 270 270 TRP TRP B . n 
B 2 271 ASN 271 271 271 ASN ASN B . n 
B 2 272 ALA 272 272 272 ALA ALA B . n 
B 2 273 SER 273 273 273 SER SER B . n 
B 2 274 LYS 274 274 274 LYS LYS B . n 
B 2 275 PRO 275 275 275 PRO PRO B . n 
B 2 276 GLU 276 276 276 GLU GLU B . n 
B 2 277 GLY 277 277 277 GLY GLY B . n 
B 2 278 ASP 278 278 278 ASP ASP B . n 
B 2 279 VAL 279 279 279 VAL VAL B . n 
B 2 280 ILE 280 280 280 ILE ILE B . n 
B 2 281 LYS 281 281 281 LYS LYS B . n 
B 2 282 ALA 282 282 282 ALA ALA B . n 
B 2 283 ILE 283 283 283 ILE ILE B . n 
B 2 284 ALA 284 284 284 ALA ALA B . n 
B 2 285 GLU 285 285 285 GLU GLU B . n 
B 2 286 ARG 286 286 286 ARG ARG B . n 
B 2 287 TYR 287 287 287 TYR TYR B . n 
B 2 288 CYS 288 288 288 CYS CYS B . n 
B 2 289 ASP 289 289 289 ASP ASP B . n 
B 2 290 ARG 290 290 290 ARG ARG B . n 
B 2 291 PRO 291 291 291 PRO PRO B . n 
B 2 292 ALA 292 292 292 ALA ALA B . n 
B 2 293 CYS 293 293 293 CYS CYS B . n 
B 2 294 PRO 294 294 294 PRO PRO B . n 
B 2 295 THR 295 295 295 THR THR B . n 
B 2 296 LYS 296 296 296 LYS LYS B . n 
B 2 297 ASP 297 297 297 ASP ASP B . n 
B 2 298 TYR 298 298 298 TYR TYR B . n 
B 2 299 PRO 299 299 299 PRO PRO B . n 
B 2 300 ALA 300 300 300 ALA ALA B . n 
B 2 301 HIS 301 301 301 HIS HIS B . n 
B 2 302 THR 302 302 302 THR THR B . n 
B 2 303 ARG 303 303 303 ARG ARG B . n 
B 2 304 PHE 304 304 304 PHE PHE B . n 
B 2 305 ASP 305 305 305 ASP ASP B . n 
B 2 306 HIS 306 306 306 HIS HIS B . n 
B 2 307 VAL 307 307 307 VAL VAL B . n 
B 2 308 LEU 308 308 308 LEU LEU B . n 
B 2 309 GLY 309 309 309 GLY GLY B . n 
B 2 310 MET 310 310 310 MET MET B . n 
B 2 311 ALA 311 311 311 ALA ALA B . n 
B 2 312 LYS 312 312 312 LYS LYS B . n 
B 2 313 GLU 313 313 313 GLU GLU B . n 
B 2 314 TYR 314 314 314 TYR TYR B . n 
B 2 315 ASN 315 315 315 ASN ASN B . n 
B 2 316 VAL 316 316 316 VAL VAL B . n 
B 2 317 GLU 317 317 317 GLU GLU B . n 
B 2 318 GLY 318 318 318 GLY GLY B . n 
B 2 319 ALA 319 319 319 ALA ALA B . n 
B 2 320 ILE 320 320 320 ILE ILE B . n 
B 2 321 PHE 321 321 321 PHE PHE B . n 
B 2 322 LEU 322 322 322 LEU LEU B . n 
B 2 323 GLN 323 323 323 GLN GLN B . n 
B 2 324 GLN 324 324 324 GLN GLN B . n 
B 2 325 LYS 325 325 325 LYS LYS B . n 
B 2 326 PHE 326 326 326 PHE PHE B . n 
B 2 327 CYS 327 327 327 CYS CYS B . n 
B 2 328 ASP 328 328 328 ASP ASP B . n 
B 2 329 PRO 329 329 329 PRO PRO B . n 
B 2 330 HIS 330 330 330 HIS HIS B . n 
B 2 331 GLU 331 331 331 GLU GLU B . n 
B 2 332 GLY 332 332 332 GLY GLY B . n 
B 2 333 ASP 333 333 333 ASP ASP B . n 
B 2 334 TYR 334 334 334 TYR TYR B . n 
B 2 335 PRO 335 335 335 PRO PRO B . n 
B 2 336 ASP 336 336 336 ASP ASP B . n 
B 2 337 LEU 337 337 337 LEU LEU B . n 
B 2 338 LYS 338 338 338 LYS LYS B . n 
B 2 339 ARG 339 339 339 ARG ARG B . n 
B 2 340 HIS 340 340 340 HIS HIS B . n 
B 2 341 LEU 341 341 341 LEU LEU B . n 
B 2 342 GLU 342 342 342 GLU GLU B . n 
B 2 343 GLU 343 343 343 GLU GLU B . n 
B 2 344 ASN 344 344 344 ASN ASN B . n 
B 2 345 GLY 345 345 345 GLY GLY B . n 
B 2 346 ILE 346 346 346 ILE ILE B . n 
B 2 347 PRO 347 347 347 PRO PRO B . n 
B 2 348 THR 348 348 348 THR THR B . n 
B 2 349 LEU 349 349 349 LEU LEU B . n 
B 2 350 PHE 350 350 350 PHE PHE B . n 
B 2 351 LEU 351 351 351 LEU LEU B . n 
B 2 352 GLU 352 352 352 GLU GLU B . n 
B 2 353 PHE 353 353 353 PHE PHE B . n 
B 2 354 ASP 354 354 354 ASP ASP B . n 
B 2 355 ILE 355 355 355 ILE ILE B . n 
B 2 356 THR 356 356 356 THR THR B . n 
B 2 357 ASN 357 357 357 ASN ASN B . n 
B 2 358 PRO 358 358 358 PRO PRO B . n 
B 2 359 ILE 359 359 359 ILE ILE B . n 
B 2 360 GLY 360 360 360 GLY GLY B . n 
B 2 361 PRO 361 361 361 PRO PRO B . n 
B 2 362 PHE 362 362 362 PHE PHE B . n 
B 2 363 ARG 363 363 363 ARG ARG B . n 
B 2 364 ILE 364 364 364 ILE ILE B . n 
B 2 365 ARG 365 365 365 ARG ARG B . n 
B 2 366 ILE 366 366 366 ILE ILE B . n 
B 2 367 GLU 367 367 367 GLU GLU B . n 
B 2 368 ALA 368 368 368 ALA ALA B . n 
B 2 369 PHE 369 369 369 PHE PHE B . n 
B 2 370 LEU 370 370 370 LEU LEU B . n 
B 2 371 GLU 371 371 371 GLU GLU B . n 
B 2 372 THR 372 372 372 THR THR B . n 
B 2 373 LEU 373 373 373 LEU LEU B . n 
B 2 374 SER 374 374 374 SER SER B . n 
B 2 375 GLU 375 375 375 GLU GLU B . n 
B 2 376 GLU 376 376 376 GLU GLU B . n 
B 2 377 GLU 377 377 ?   ?   ?   B . n 
B 2 378 LEU 378 378 ?   ?   ?   B . n 
B 2 379 PHE 379 379 ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   ASN 2   2   ?   ?   ?   C . n 
C 1 3   ALA 3   3   ?   ?   ?   C . n 
C 1 4   MET 4   4   ?   ?   ?   C . n 
C 1 5   ALA 5   5   ?   ?   ?   C . n 
C 1 6   ASN 6   6   6   ASN ASN C . n 
C 1 7   LYS 7   7   7   LYS LYS C . n 
C 1 8   TYR 8   8   8   TYR TYR C . n 
C 1 9   PRO 9   9   9   PRO PRO C . n 
C 1 10  THR 10  10  10  THR THR C . n 
C 1 11  GLU 11  11  11  GLU GLU C . n 
C 1 12  GLN 12  12  12  GLN GLN C . n 
C 1 13  LEU 13  13  13  LEU LEU C . n 
C 1 14  LYS 14  14  14  LYS LYS C . n 
C 1 15  LEU 15  15  15  LEU LEU C . n 
C 1 16  TRP 16  16  16  TRP TRP C . n 
C 1 17  GLY 17  17  17  GLY GLY C . n 
C 1 18  LYS 18  18  18  LYS LYS C . n 
C 1 19  ALA 19  19  19  ALA ALA C . n 
C 1 20  LYS 20  20  20  LYS LYS C . n 
C 1 21  GLU 21  21  21  GLU GLU C . n 
C 1 22  LEU 22  22  22  LEU LEU C . n 
C 1 23  ARG 23  23  23  ARG ARG C . n 
C 1 24  GLU 24  24  24  GLU GLU C . n 
C 1 25  GLN 25  25  25  GLN GLN C . n 
C 1 26  TYR 26  26  26  TYR TYR C . n 
C 1 27  TYR 27  27  27  TYR TYR C . n 
C 1 28  MET 28  28  28  MET MET C . n 
C 1 29  ASN 29  29  29  ASN ASN C . n 
C 1 30  TYR 30  30  30  TYR TYR C . n 
C 1 31  ALA 31  31  31  ALA ALA C . n 
C 1 32  ARG 32  32  32  ARG ARG C . n 
C 1 33  ALA 33  33  33  ALA ALA C . n 
C 1 34  LYS 34  34  34  LYS LYS C . n 
C 1 35  GLU 35  35  35  GLU GLU C . n 
C 1 36  LYS 36  36  36  LYS LYS C . n 
C 1 37  GLY 37  37  37  GLY GLY C . n 
C 1 38  GLY 38  38  38  GLY GLY C . n 
C 1 39  ILE 39  39  39  ILE ILE C . n 
C 1 40  ARG 40  40  40  ARG ARG C . n 
C 1 41  TRP 41  41  41  TRP TRP C . n 
C 1 42  SER 42  42  42  SER SER C . n 
C 1 43  GLY 43  43  43  GLY GLY C . n 
C 1 44  SER 44  44  44  SER SER C . n 
C 1 45  ALA 45  45  45  ALA ALA C . n 
C 1 46  TRP 46  46  46  TRP TRP C . n 
C 1 47  ALA 47  47  47  ALA ALA C . n 
C 1 48  LEU 48  48  48  LEU LEU C . n 
C 1 49  ASP 49  49  49  ASP ASP C . n 
C 1 50  ALA 50  50  50  ALA ALA C . n 
C 1 51  ILE 51  51  51  ILE ILE C . n 
C 1 52  PRO 52  52  52  PRO PRO C . n 
C 1 53  ALA 53  53  53  ALA ALA C . n 
C 1 54  GLY 54  54  54  GLY GLY C . n 
C 1 55  LEU 55  55  55  LEU LEU C . n 
C 1 56  GLY 56  56  56  GLY GLY C . n 
C 1 57  GLU 57  57  57  GLU GLU C . n 
C 1 58  ASP 58  58  58  ASP ASP C . n 
C 1 59  VAL 59  59  59  VAL VAL C . n 
C 1 60  TYR 60  60  60  TYR TYR C . n 
C 1 61  SER 61  61  61  SER SER C . n 
C 1 62  LEU 62  62  62  LEU LEU C . n 
C 1 63  THR 63  63  63  THR THR C . n 
C 1 64  GLY 64  64  64  GLY GLY C . n 
C 1 65  GLU 65  65  65  GLU GLU C . n 
C 1 66  PRO 66  66  66  PRO PRO C . n 
C 1 67  TYR 67  67  67  TYR TYR C . n 
C 1 68  ALA 68  68  68  ALA ALA C . n 
C 1 69  ALA 69  69  69  ALA ALA C . n 
C 1 70  ALA 70  70  70  ALA ALA C . n 
C 1 71  VAL 71  71  71  VAL VAL C . n 
C 1 72  ALA 72  72  72  ALA ALA C . n 
C 1 73  HIS 73  73  73  HIS HIS C . n 
C 1 74  ASP 74  74  74  ASP ASP C . n 
C 1 75  ARG 75  75  75  ARG ARG C . n 
C 1 76  LYS 76  76  76  LYS LYS C . n 
C 1 77  PHE 77  77  77  PHE PHE C . n 
C 1 78  ALA 78  78  78  ALA ALA C . n 
C 1 79  LYS 79  79  79  LYS LYS C . n 
C 1 80  GLU 80  80  80  GLU GLU C . n 
C 1 81  CYS 81  81  81  CYS CYS C . n 
C 1 82  MET 82  82  82  MET MET C . n 
C 1 83  ASP 83  83  83  ASP ASP C . n 
C 1 84  ALA 84  84  84  ALA ALA C . n 
C 1 85  ALA 85  85  85  ALA ALA C . n 
C 1 86  GLU 86  86  86  GLU GLU C . n 
C 1 87  ALA 87  87  87  ALA ALA C . n 
C 1 88  TYR 88  88  88  TYR TYR C . n 
C 1 89  GLY 89  89  89  GLY GLY C . n 
C 1 90  PHE 90  90  90  PHE PHE C . n 
C 1 91  ALA 91  91  91  ALA ALA C . n 
C 1 92  ARG 92  92  92  ARG ARG C . n 
C 1 93  ASP 93  93  93  ASP ASP C . n 
C 1 94  LEU 94  94  94  LEU LEU C . n 
C 1 95  CYS 95  95  95  CYS CYS C . n 
C 1 96  SER 96  96  96  SER SER C . n 
C 1 97  TYR 97  97  97  TYR TYR C . n 
C 1 98  MET 98  98  98  MET MET C . n 
C 1 99  ARG 99  99  99  ARG ARG C . n 
C 1 100 ILE 100 100 100 ILE ILE C . n 
C 1 101 TYR 101 101 101 TYR TYR C . n 
C 1 102 TRP 102 102 102 TRP TRP C . n 
C 1 103 GLY 103 103 103 GLY GLY C . n 
C 1 104 GLY 104 104 104 GLY GLY C . n 
C 1 105 MET 105 105 105 MET MET C . n 
C 1 106 HIS 106 106 106 HIS HIS C . n 
C 1 107 LEU 107 107 107 LEU LEU C . n 
C 1 108 ASN 108 108 108 ASN ASN C . n 
C 1 109 LYS 109 109 109 LYS LYS C . n 
C 1 110 TYR 110 110 110 TYR TYR C . n 
C 1 111 ALA 111 111 111 ALA ALA C . n 
C 1 112 PHE 112 112 112 PHE PHE C . n 
C 1 113 GLY 113 113 113 GLY GLY C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 GLU 115 115 115 GLU GLU C . n 
C 1 116 PHE 116 116 116 PHE PHE C . n 
C 1 117 PRO 117 117 117 PRO PRO C . n 
C 1 118 LYS 118 118 118 LYS LYS C . n 
C 1 119 PRO 119 119 119 PRO PRO C . n 
C 1 120 ASP 120 120 120 ASP ASP C . n 
C 1 121 PHE 121 121 121 PHE PHE C . n 
C 1 122 VAL 122 122 122 VAL VAL C . n 
C 1 123 PHE 123 123 123 PHE PHE C . n 
C 1 124 GLN 124 124 124 GLN GLN C . n 
C 1 125 THR 125 125 125 THR THR C . n 
C 1 126 GLN 126 126 126 GLN GLN C . n 
C 1 127 ILE 127 127 127 ILE ILE C . n 
C 1 128 CYS 128 128 128 CYS CYS C . n 
C 1 129 CYS 129 129 129 CYS CYS C . n 
C 1 130 SER 130 130 130 SER SER C . n 
C 1 131 HIS 131 131 131 HIS HIS C . n 
C 1 132 SER 132 132 132 SER SER C . n 
C 1 133 LYS 133 133 133 LYS LYS C . n 
C 1 134 TRP 134 134 134 TRP TRP C . n 
C 1 135 TYR 135 135 135 TYR TYR C . n 
C 1 136 GLN 136 136 136 GLN GLN C . n 
C 1 137 HIS 137 137 137 HIS HIS C . n 
C 1 138 VAL 138 138 138 VAL VAL C . n 
C 1 139 ALA 139 139 139 ALA ALA C . n 
C 1 140 LYS 140 140 140 LYS LYS C . n 
C 1 141 GLU 141 141 141 GLU GLU C . n 
C 1 142 GLU 142 142 142 GLU GLU C . n 
C 1 143 LYS 143 143 143 LYS LYS C . n 
C 1 144 ILE 144 144 144 ILE ILE C . n 
C 1 145 PRO 145 145 145 PRO PRO C . n 
C 1 146 GLU 146 146 146 GLU GLU C . n 
C 1 147 PHE 147 147 147 PHE PHE C . n 
C 1 148 TYR 148 148 148 TYR TYR C . n 
C 1 149 LEU 149 149 149 LEU LEU C . n 
C 1 150 ASP 150 150 150 ASP ASP C . n 
C 1 151 VAL 151 151 151 VAL VAL C . n 
C 1 152 GLY 152 152 152 GLY GLY C . n 
C 1 153 VAL 153 153 153 VAL VAL C . n 
C 1 154 GLY 154 154 154 GLY GLY C . n 
C 1 155 PRO 155 155 155 PRO PRO C . n 
C 1 156 TYR 156 156 156 TYR TYR C . n 
C 1 157 ARG 157 157 157 ARG ARG C . n 
C 1 158 ASP 158 158 158 ASP ASP C . n 
C 1 159 MET 159 159 159 MET MET C . n 
C 1 160 THR 160 160 160 THR THR C . n 
C 1 161 ASP 161 161 161 ASP ASP C . n 
C 1 162 ALA 162 162 162 ALA ALA C . n 
C 1 163 ARG 163 163 163 ARG ARG C . n 
C 1 164 LEU 164 164 164 LEU LEU C . n 
C 1 165 ASP 165 165 165 ASP ASP C . n 
C 1 166 TYR 166 166 166 TYR TYR C . n 
C 1 167 VAL 167 167 167 VAL VAL C . n 
C 1 168 ALA 168 168 168 ALA ALA C . n 
C 1 169 ASN 169 169 169 ASN ASN C . n 
C 1 170 GLN 170 170 170 GLN GLN C . n 
C 1 171 LEU 171 171 171 LEU LEU C . n 
C 1 172 HIS 172 172 172 HIS HIS C . n 
C 1 173 ASP 173 173 173 ASP ASP C . n 
C 1 174 GLY 174 174 174 GLY GLY C . n 
C 1 175 ILE 175 175 175 ILE ILE C . n 
C 1 176 ALA 176 176 176 ALA ALA C . n 
C 1 177 PHE 177 177 177 PHE PHE C . n 
C 1 178 VAL 178 178 178 VAL VAL C . n 
C 1 179 GLU 179 179 179 GLU GLU C . n 
C 1 180 LYS 180 180 180 LYS LYS C . n 
C 1 181 ALA 181 181 181 ALA ALA C . n 
C 1 182 SER 182 182 182 SER SER C . n 
C 1 183 GLY 183 183 183 GLY GLY C . n 
C 1 184 ARG 184 184 184 ARG ARG C . n 
C 1 185 LYS 185 185 185 LYS LYS C . n 
C 1 186 PHE 186 186 186 PHE PHE C . n 
C 1 187 ASP 187 187 187 ASP ASP C . n 
C 1 188 ASP 188 188 188 ASP ASP C . n 
C 1 189 GLU 189 189 189 GLU GLU C . n 
C 1 190 LEU 190 190 190 LEU LEU C . n 
C 1 191 PHE 191 191 191 PHE PHE C . n 
C 1 192 ILE 192 192 192 ILE ILE C . n 
C 1 193 LYS 193 193 193 LYS LYS C . n 
C 1 194 ALA 194 194 194 ALA ALA C . n 
C 1 195 VAL 195 195 195 VAL VAL C . n 
C 1 196 LYS 196 196 196 LYS LYS C . n 
C 1 197 ASN 197 197 197 ASN ASN C . n 
C 1 198 GLU 198 198 198 GLU GLU C . n 
C 1 199 MET 199 199 199 MET MET C . n 
C 1 200 ARG 200 200 200 ARG ARG C . n 
C 1 201 SER 201 201 201 SER SER C . n 
C 1 202 THR 202 202 202 THR THR C . n 
C 1 203 SER 203 203 203 SER SER C . n 
C 1 204 ARG 204 204 204 ARG ARG C . n 
C 1 205 TRP 205 205 205 TRP TRP C . n 
C 1 206 ALA 206 206 206 ALA ALA C . n 
C 1 207 ASP 207 207 207 ASP ASP C . n 
C 1 208 ILE 208 208 208 ILE ILE C . n 
C 1 209 CYS 209 209 209 CYS CYS C . n 
C 1 210 ALA 210 210 210 ALA ALA C . n 
C 1 211 LEU 211 211 211 LEU LEU C . n 
C 1 212 ASN 212 212 212 ASN ASN C . n 
C 1 213 LYS 213 213 213 LYS LYS C . n 
C 1 214 VAL 214 214 214 VAL VAL C . n 
C 1 215 LYS 215 215 215 LYS LYS C . n 
C 1 216 PRO 216 216 216 PRO PRO C . n 
C 1 217 ALA 217 217 217 ALA ALA C . n 
C 1 218 PRO 218 218 218 PRO PRO C . n 
C 1 219 LEU 219 219 219 LEU LEU C . n 
C 1 220 ASP 220 220 220 ASP ASP C . n 
C 1 221 GLU 221 221 221 GLU GLU C . n 
C 1 222 LYS 222 222 222 LYS LYS C . n 
C 1 223 THR 223 223 223 THR THR C . n 
C 1 224 MET 224 224 224 MET MET C . n 
C 1 225 TYR 225 225 225 TYR TYR C . n 
C 1 226 SER 226 226 226 SER SER C . n 
C 1 227 LEU 227 227 227 LEU LEU C . n 
C 1 228 TYR 228 228 228 TYR TYR C . n 
C 1 229 VAL 229 229 229 VAL VAL C . n 
C 1 230 LEU 230 230 230 LEU LEU C . n 
C 1 231 CYS 231 231 231 CYS CYS C . n 
C 1 232 THR 232 232 232 THR THR C . n 
C 1 233 LEU 233 233 233 LEU LEU C . n 
C 1 234 SER 234 234 234 SER SER C . n 
C 1 235 LYS 235 235 235 LYS LYS C . n 
C 1 236 SER 236 236 236 SER SER C . n 
C 1 237 SER 237 237 237 SER SER C . n 
C 1 238 GLN 238 238 238 GLN GLN C . n 
C 1 239 TRP 239 239 239 TRP TRP C . n 
C 1 240 CYS 240 240 240 CYS CYS C . n 
C 1 241 ALA 241 241 241 ALA ALA C . n 
C 1 242 ASP 242 242 242 ASP ASP C . n 
C 1 243 PHE 243 243 243 PHE PHE C . n 
C 1 244 MET 244 244 244 MET MET C . n 
C 1 245 ASP 245 245 245 ASP ASP C . n 
C 1 246 GLU 246 246 246 GLU GLU C . n 
C 1 247 LEU 247 247 247 LEU LEU C . n 
C 1 248 TYR 248 248 248 TYR TYR C . n 
C 1 249 GLU 249 249 249 GLU GLU C . n 
C 1 250 GLU 250 250 250 GLU GLU C . n 
C 1 251 VAL 251 251 251 VAL VAL C . n 
C 1 252 LYS 252 252 252 LYS LYS C . n 
C 1 253 ASP 253 253 253 ASP ASP C . n 
C 1 254 ARG 254 254 254 ARG ARG C . n 
C 1 255 VAL 255 255 255 VAL VAL C . n 
C 1 256 ALA 256 256 256 ALA ALA C . n 
C 1 257 ARG 257 257 257 ARG ARG C . n 
C 1 258 GLY 258 258 258 GLY GLY C . n 
C 1 259 ILE 259 259 259 ILE ILE C . n 
C 1 260 ALA 260 260 260 ALA ALA C . n 
C 1 261 ALA 261 261 261 ALA ALA C . n 
C 1 262 VAL 262 262 262 VAL VAL C . n 
C 1 263 PRO 263 263 263 PRO PRO C . n 
C 1 264 ASN 264 264 264 ASN ASN C . n 
C 1 265 GLU 265 265 265 GLU GLU C . n 
C 1 266 ALA 266 266 266 ALA ALA C . n 
C 1 267 ILE 267 267 267 ILE ILE C . n 
C 1 268 ARG 268 268 268 ARG ARG C . n 
C 1 269 LEU 269 269 269 LEU LEU C . n 
C 1 270 MET 270 270 270 MET MET C . n 
C 1 271 THR 271 271 271 THR THR C . n 
C 1 272 ASP 272 272 272 ASP ASP C . n 
C 1 273 THR 273 273 273 THR THR C . n 
C 1 274 GLN 274 274 274 GLN GLN C . n 
C 1 275 PRO 275 275 275 PRO PRO C . n 
C 1 276 PRO 276 276 276 PRO PRO C . n 
C 1 277 TRP 277 277 277 TRP TRP C . n 
C 1 278 SER 278 278 278 SER SER C . n 
C 1 279 PHE 279 279 279 PHE PHE C . n 
C 1 280 LEU 280 280 280 LEU LEU C . n 
C 1 281 LYS 281 281 281 LYS LYS C . n 
C 1 282 ILE 282 282 282 ILE ILE C . n 
C 1 283 PHE 283 283 283 PHE PHE C . n 
C 1 284 ARG 284 284 284 ARG ARG C . n 
C 1 285 TYR 285 285 285 TYR TYR C . n 
C 1 286 LEU 286 286 286 LEU LEU C . n 
C 1 287 GLU 287 287 287 GLU GLU C . n 
C 1 288 THR 288 288 288 THR THR C . n 
C 1 289 TYR 289 289 289 TYR TYR C . n 
C 1 290 GLY 290 290 290 GLY GLY C . n 
C 1 291 ALA 291 291 291 ALA ALA C . n 
C 1 292 VAL 292 292 292 VAL VAL C . n 
C 1 293 SER 293 293 293 SER SER C . n 
C 1 294 ILE 294 294 294 ILE ILE C . n 
C 1 295 GLY 295 295 295 GLY GLY C . n 
C 1 296 SER 296 296 296 SER SER C . n 
C 1 297 LEU 297 297 297 LEU LEU C . n 
C 1 298 TYR 298 298 298 TYR TYR C . n 
C 1 299 THR 299 299 299 THR THR C . n 
C 1 300 PHE 300 300 300 PHE PHE C . n 
C 1 301 ALA 301 301 301 ALA ALA C . n 
C 1 302 LEU 302 302 302 LEU LEU C . n 
C 1 303 GLU 303 303 303 GLU GLU C . n 
C 1 304 GLY 304 304 304 GLY GLY C . n 
C 1 305 ILE 305 305 305 ILE ILE C . n 
C 1 306 TRP 306 306 306 TRP TRP C . n 
C 1 307 GLU 307 307 307 GLU GLU C . n 
C 1 308 ASP 308 308 308 ASP ASP C . n 
C 1 309 LYS 309 309 309 LYS LYS C . n 
C 1 310 PRO 310 310 310 PRO PRO C . n 
C 1 311 ASP 311 311 311 ASP ASP C . n 
C 1 312 GLY 312 312 312 GLY GLY C . n 
C 1 313 SER 313 313 313 SER SER C . n 
C 1 314 TRP 314 314 314 TRP TRP C . n 
C 1 315 GLY 315 315 315 GLY GLY C . n 
C 1 316 GLY 316 316 316 GLY GLY C . n 
C 1 317 ARG 317 317 317 ARG ARG C . n 
C 1 318 THR 318 318 318 THR THR C . n 
C 1 319 LEU 319 319 319 LEU LEU C . n 
C 1 320 PRO 320 320 320 PRO PRO C . n 
C 1 321 TRP 321 321 321 TRP TRP C . n 
C 1 322 ASP 322 322 322 ASP ASP C . n 
C 1 323 LYS 323 323 323 LYS LYS C . n 
C 1 324 GLY 324 324 324 GLY GLY C . n 
C 1 325 ILE 325 325 325 ILE ILE C . n 
C 1 326 GLU 326 326 326 GLU GLU C . n 
C 1 327 ILE 327 327 327 ILE ILE C . n 
C 1 328 ASN 328 328 328 ASN ASN C . n 
C 1 329 ASP 329 329 329 ASP ASP C . n 
C 1 330 ARG 330 330 330 ARG ARG C . n 
C 1 331 ASP 331 331 331 ASP ASP C . n 
C 1 332 THR 332 332 332 THR THR C . n 
C 1 333 ALA 333 333 333 ALA ALA C . n 
C 1 334 VAL 334 334 334 VAL VAL C . n 
C 1 335 ARG 335 335 335 ARG ARG C . n 
C 1 336 LEU 336 336 336 LEU LEU C . n 
C 1 337 TYR 337 337 337 TYR TYR C . n 
C 1 338 ALA 338 338 338 ALA ALA C . n 
C 1 339 ASP 339 339 339 ASP ASP C . n 
C 1 340 TRP 340 340 340 TRP TRP C . n 
C 1 341 ASN 341 341 341 ASN ASN C . n 
C 1 342 LEU 342 342 342 LEU LEU C . n 
C 1 343 SER 343 343 343 SER SER C . n 
C 1 344 LYS 344 344 344 LYS LYS C . n 
C 1 345 PRO 345 345 345 PRO PRO C . n 
C 1 346 GLN 346 346 346 GLN GLN C . n 
C 1 347 TRP 347 347 347 TRP TRP C . n 
C 1 348 GLN 348 348 348 GLN GLN C . n 
C 1 349 HIS 349 349 349 HIS HIS C . n 
C 1 350 PHE 350 350 350 PHE PHE C . n 
C 1 351 TYR 351 351 351 TYR TYR C . n 
C 1 352 ASP 352 352 352 ASP ASP C . n 
C 1 353 PRO 353 353 353 PRO PRO C . n 
C 1 354 THR 354 354 354 THR THR C . n 
C 1 355 ILE 355 355 355 ILE ILE C . n 
C 1 356 LYS 356 356 356 LYS LYS C . n 
C 1 357 SER 357 357 357 SER SER C . n 
C 1 358 ASP 358 358 358 ASP ASP C . n 
C 1 359 MET 359 359 359 MET MET C . n 
C 1 360 MET 360 360 360 MET MET C . n 
C 1 361 LEU 361 361 361 LEU LEU C . n 
C 1 362 ARG 362 362 362 ARG ARG C . n 
C 1 363 ILE 363 363 363 ILE ILE C . n 
C 1 364 ILE 364 364 364 ILE ILE C . n 
C 1 365 LYS 365 365 365 LYS LYS C . n 
C 1 366 GLU 366 366 366 GLU GLU C . n 
C 1 367 TRP 367 367 367 TRP TRP C . n 
C 1 368 GLN 368 368 368 GLN GLN C . n 
C 1 369 VAL 369 369 369 VAL VAL C . n 
C 1 370 ASP 370 370 370 ASP ASP C . n 
C 1 371 GLY 371 371 371 GLY GLY C . n 
C 1 372 VAL 372 372 372 VAL VAL C . n 
C 1 373 MET 373 373 373 MET MET C . n 
C 1 374 LEU 374 374 374 LEU LEU C . n 
C 1 375 HIS 375 375 375 HIS HIS C . n 
C 1 376 LEU 376 376 376 LEU LEU C . n 
C 1 377 ASN 377 377 377 ASN ASN C . n 
C 1 378 ARG 378 378 378 ARG ARG C . n 
C 1 379 GLY 379 379 379 GLY GLY C . n 
C 1 380 CYS 380 380 380 CYS CYS C . n 
C 1 381 GLU 381 381 381 GLU GLU C . n 
C 1 382 GLY 382 382 382 GLY GLY C . n 
C 1 383 LEU 383 383 383 LEU LEU C . n 
C 1 384 SER 384 384 384 SER SER C . n 
C 1 385 VAL 385 385 385 VAL VAL C . n 
C 1 386 GLY 386 386 386 GLY GLY C . n 
C 1 387 ILE 387 387 387 ILE ILE C . n 
C 1 388 MET 388 388 388 MET MET C . n 
C 1 389 GLU 389 389 389 GLU GLU C . n 
C 1 390 ASN 390 390 390 ASN ASN C . n 
C 1 391 ARG 391 391 391 ARG ARG C . n 
C 1 392 LEU 392 392 392 LEU LEU C . n 
C 1 393 ALA 393 393 393 ALA ALA C . n 
C 1 394 ILE 394 394 394 ILE ILE C . n 
C 1 395 ALA 395 395 395 ALA ALA C . n 
C 1 396 LYS 396 396 396 LYS LYS C . n 
C 1 397 SER 397 397 397 SER SER C . n 
C 1 398 GLY 398 398 398 GLY GLY C . n 
C 1 399 THR 399 399 399 THR THR C . n 
C 1 400 PRO 400 400 400 PRO PRO C . n 
C 1 401 VAL 401 401 401 VAL VAL C . n 
C 1 402 MET 402 402 402 MET MET C . n 
C 1 403 THR 403 403 403 THR THR C . n 
C 1 404 PHE 404 404 404 PHE PHE C . n 
C 1 405 GLU 405 405 405 GLU GLU C . n 
C 1 406 GLY 406 406 406 GLY GLY C . n 
C 1 407 ASN 407 407 407 ASN ASN C . n 
C 1 408 MET 408 408 408 MET MET C . n 
C 1 409 GLY 409 409 409 GLY GLY C . n 
C 1 410 ASP 410 410 410 ASP ASP C . n 
C 1 411 GLU 411 411 411 GLU GLU C . n 
C 1 412 ARG 412 412 412 ARG ARG C . n 
C 1 413 GLU 413 413 413 GLU GLU C . n 
C 1 414 PHE 414 414 414 PHE PHE C . n 
C 1 415 ASP 415 415 415 ASP ASP C . n 
C 1 416 GLU 416 416 416 GLU GLU C . n 
C 1 417 VAL 417 417 417 VAL VAL C . n 
C 1 418 ARG 418 418 418 ARG ARG C . n 
C 1 419 THR 419 419 419 THR THR C . n 
C 1 420 GLN 420 420 420 GLN GLN C . n 
C 1 421 ALA 421 421 421 ALA ALA C . n 
C 1 422 ARG 422 422 422 ARG ARG C . n 
C 1 423 VAL 423 423 423 VAL VAL C . n 
C 1 424 ASP 424 424 424 ASP ASP C . n 
C 1 425 ALA 425 425 425 ALA ALA C . n 
C 1 426 PHE 426 426 426 PHE PHE C . n 
C 1 427 MET 427 427 427 MET MET C . n 
C 1 428 GLU 428 428 428 GLU GLU C . n 
C 1 429 GLN 429 429 429 GLN GLN C . n 
C 1 430 LEU 430 430 430 LEU LEU C . n 
C 1 431 GLY 431 431 431 GLY GLY C . n 
C 1 432 VAL 432 432 432 VAL VAL C . n 
C 1 433 ARG 433 433 433 ARG ARG C . n 
C 1 434 ARG 434 434 434 ARG ARG C . n 
C 1 435 GLN 435 435 ?   ?   ?   C . n 
C 1 436 ALA 436 436 ?   ?   ?   C . n 
C 1 437 ALA 437 437 ?   ?   ?   C . n 
C 1 438 SER 438 438 ?   ?   ?   C . n 
C 1 439 ALA 439 439 ?   ?   ?   C . n 
C 1 440 TRP 440 440 ?   ?   ?   C . n 
C 1 441 SER 441 441 ?   ?   ?   C . n 
C 1 442 HIS 442 442 ?   ?   ?   C . n 
C 1 443 PRO 443 443 ?   ?   ?   C . n 
C 1 444 GLN 444 444 ?   ?   ?   C . n 
C 1 445 PHE 445 445 ?   ?   ?   C . n 
C 1 446 GLU 446 446 ?   ?   ?   C . n 
C 1 447 LYS 447 447 ?   ?   ?   C . n 
D 2 1   MET 1   1   ?   ?   ?   D . n 
D 2 2   SER 2   2   2   SER SER D . n 
D 2 3   ASP 3   3   3   ASP ASP D . n 
D 2 4   GLY 4   4   4   GLY GLY D . n 
D 2 5   LEU 5   5   5   LEU LEU D . n 
D 2 6   PHE 6   6   6   PHE PHE D . n 
D 2 7   ASP 7   7   7   ASP ASP D . n 
D 2 8   GLN 8   8   8   GLN GLN D . n 
D 2 9   PHE 9   9   9   PHE PHE D . n 
D 2 10  LYS 10  10  10  LYS LYS D . n 
D 2 11  THR 11  11  11  THR THR D . n 
D 2 12  TRP 12  12  12  TRP TRP D . n 
D 2 13  TYR 13  13  13  TYR TYR D . n 
D 2 14  GLU 14  14  14  GLU GLU D . n 
D 2 15  LYS 15  15  15  LYS LYS D . n 
D 2 16  ARG 16  16  16  ARG ARG D . n 
D 2 17  HIS 17  17  17  HIS HIS D . n 
D 2 18  ASP 18  18  18  ASP ASP D . n 
D 2 19  TYR 19  19  19  TYR TYR D . n 
D 2 20  ALA 20  20  20  ALA ALA D . n 
D 2 21  ARG 21  21  21  ARG ARG D . n 
D 2 22  ASP 22  22  22  ASP ASP D . n 
D 2 23  TRP 23  23  23  TRP TRP D . n 
D 2 24  LYS 24  24  24  LYS LYS D . n 
D 2 25  VAL 25  25  25  VAL VAL D . n 
D 2 26  ARG 26  26  26  ARG ARG D . n 
D 2 27  THR 27  27  27  THR THR D . n 
D 2 28  GLY 28  28  28  GLY GLY D . n 
D 2 29  GLY 29  29  29  GLY GLY D . n 
D 2 30  GLN 30  30  30  GLN GLN D . n 
D 2 31  VAL 31  31  31  VAL VAL D . n 
D 2 32  VAL 32  32  32  VAL VAL D . n 
D 2 33  ALA 33  33  33  ALA ALA D . n 
D 2 34  THR 34  34  34  THR THR D . n 
D 2 35  MET 35  35  35  MET MET D . n 
D 2 36  CYS 36  36  36  CYS CYS D . n 
D 2 37  THR 37  37  37  THR THR D . n 
D 2 38  TYR 38  38  38  TYR TYR D . n 
D 2 39  THR 39  39  39  THR THR D . n 
D 2 40  PRO 40  40  40  PRO PRO D . n 
D 2 41  GLU 41  41  41  GLU GLU D . n 
D 2 42  GLU 42  42  42  GLU GLU D . n 
D 2 43  LEU 43  43  43  LEU LEU D . n 
D 2 44  LEU 44  44  44  LEU LEU D . n 
D 2 45  ILE 45  45  45  ILE ILE D . n 
D 2 46  ALA 46  46  46  ALA ALA D . n 
D 2 47  ALA 47  47  47  ALA ALA D . n 
D 2 48  GLY 48  48  48  GLY GLY D . n 
D 2 49  MET 49  49  49  MET MET D . n 
D 2 50  LEU 50  50  50  LEU LEU D . n 
D 2 51  PRO 51  51  51  PRO PRO D . n 
D 2 52  VAL 52  52  52  VAL VAL D . n 
D 2 53  ARG 53  53  53  ARG ARG D . n 
D 2 54  VAL 54  54  54  VAL VAL D . n 
D 2 55  LEU 55  55  55  LEU LEU D . n 
D 2 56  GLY 56  56  56  GLY GLY D . n 
D 2 57  ALA 57  57  57  ALA ALA D . n 
D 2 58  HIS 58  58  58  HIS HIS D . n 
D 2 59  GLU 59  59  59  GLU GLU D . n 
D 2 60  PRO 60  60  60  PRO PRO D . n 
D 2 61  GLN 61  61  61  GLN GLN D . n 
D 2 62  ASN 62  62  62  ASN ASN D . n 
D 2 63  VAL 63  63  63  VAL VAL D . n 
D 2 64  THR 64  64  64  THR THR D . n 
D 2 65  GLU 65  65  65  GLU GLU D . n 
D 2 66  PRO 66  66  66  PRO PRO D . n 
D 2 67  HIS 67  67  67  HIS HIS D . n 
D 2 68  ILE 68  68  68  ILE ILE D . n 
D 2 69  PHE 69  69  69  PHE PHE D . n 
D 2 70  GLY 70  70  70  GLY GLY D . n 
D 2 71  MET 71  71  71  MET MET D . n 
D 2 72  PHE 72  72  72  PHE PHE D . n 
D 2 73  CYS 73  73  73  CYS CYS D . n 
D 2 74  PRO 74  74  74  PRO PRO D . n 
D 2 75  PHE 75  75  75  PHE PHE D . n 
D 2 76  CYS 76  76  76  CYS CYS D . n 
D 2 77  ARG 77  77  77  ARG ARG D . n 
D 2 78  ASP 78  78  78  ASP ASP D . n 
D 2 79  SER 79  79  79  SER SER D . n 
D 2 80  LEU 80  80  80  LEU LEU D . n 
D 2 81  ALA 81  81  81  ALA ALA D . n 
D 2 82  GLN 82  82  82  GLN GLN D . n 
D 2 83  GLY 83  83  83  GLY GLY D . n 
D 2 84  LEU 84  84  84  LEU LEU D . n 
D 2 85  LEU 85  85  85  LEU LEU D . n 
D 2 86  GLY 86  86  86  GLY GLY D . n 
D 2 87  ARG 87  87  87  ARG ARG D . n 
D 2 88  PHE 88  88  88  PHE PHE D . n 
D 2 89  ASP 89  89  89  ASP ASP D . n 
D 2 90  TYR 90  90  90  TYR TYR D . n 
D 2 91  ALA 91  91  91  ALA ALA D . n 
D 2 92  GLU 92  92  92  GLU GLU D . n 
D 2 93  GLY 93  93  93  GLY GLY D . n 
D 2 94  VAL 94  94  94  VAL VAL D . n 
D 2 95  THR 95  95  95  THR THR D . n 
D 2 96  LEU 96  96  96  LEU LEU D . n 
D 2 97  THR 97  97  97  THR THR D . n 
D 2 98  GLN 98  98  98  GLN GLN D . n 
D 2 99  SER 99  99  99  SER SER D . n 
D 2 100 CYS 100 100 100 CYS CYS D . n 
D 2 101 ILE 101 101 101 ILE ILE D . n 
D 2 102 GLN 102 102 102 GLN GLN D . n 
D 2 103 TYR 103 103 103 TYR TYR D . n 
D 2 104 ARG 104 104 104 ARG ARG D . n 
D 2 105 GLN 105 105 105 GLN GLN D . n 
D 2 106 THR 106 106 106 THR THR D . n 
D 2 107 PHE 107 107 107 PHE PHE D . n 
D 2 108 GLY 108 108 108 GLY GLY D . n 
D 2 109 SER 109 109 109 SER SER D . n 
D 2 110 TRP 110 110 110 TRP TRP D . n 
D 2 111 ARG 111 111 111 ARG ARG D . n 
D 2 112 LEU 112 112 112 LEU LEU D . n 
D 2 113 HIS 113 113 113 HIS HIS D . n 
D 2 114 VAL 114 114 114 VAL VAL D . n 
D 2 115 PRO 115 115 115 PRO PRO D . n 
D 2 116 THR 116 116 116 THR THR D . n 
D 2 117 VAL 117 117 117 VAL VAL D . n 
D 2 118 LYS 118 118 118 LYS LYS D . n 
D 2 119 TRP 119 119 119 TRP TRP D . n 
D 2 120 ASP 120 120 120 ASP ASP D . n 
D 2 121 TYR 121 121 121 TYR TYR D . n 
D 2 122 TYR 122 122 122 TYR TYR D . n 
D 2 123 VAL 123 123 123 VAL VAL D . n 
D 2 124 PRO 124 124 124 PRO PRO D . n 
D 2 125 MET 125 125 125 MET MET D . n 
D 2 126 PRO 126 126 126 PRO PRO D . n 
D 2 127 ASN 127 127 127 ASN ASN D . n 
D 2 128 GLU 128 128 128 GLU GLU D . n 
D 2 129 VAL 129 129 129 VAL VAL D . n 
D 2 130 GLN 130 130 130 GLN GLN D . n 
D 2 131 SER 131 131 131 SER SER D . n 
D 2 132 PRO 132 132 132 PRO PRO D . n 
D 2 133 HIS 133 133 133 HIS HIS D . n 
D 2 134 ALA 134 134 134 ALA ALA D . n 
D 2 135 ARG 135 135 135 ARG ARG D . n 
D 2 136 LYS 136 136 136 LYS LYS D . n 
D 2 137 ALA 137 137 137 ALA ALA D . n 
D 2 138 HIS 138 138 138 HIS HIS D . n 
D 2 139 TYR 139 139 139 TYR TYR D . n 
D 2 140 GLU 140 140 140 GLU GLU D . n 
D 2 141 GLU 141 141 141 GLU GLU D . n 
D 2 142 VAL 142 142 142 VAL VAL D . n 
D 2 143 GLN 143 143 143 GLN GLN D . n 
D 2 144 ALA 144 144 144 ALA ALA D . n 
D 2 145 PHE 145 145 145 PHE PHE D . n 
D 2 146 ARG 146 146 146 ARG ARG D . n 
D 2 147 VAL 147 147 147 VAL VAL D . n 
D 2 148 PHE 148 148 148 PHE PHE D . n 
D 2 149 LEU 149 149 149 LEU LEU D . n 
D 2 150 GLN 150 150 150 GLN GLN D . n 
D 2 151 THR 151 151 151 THR THR D . n 
D 2 152 LEU 152 152 152 LEU LEU D . n 
D 2 153 THR 153 153 153 THR THR D . n 
D 2 154 GLY 154 154 154 GLY GLY D . n 
D 2 155 LYS 155 155 155 LYS LYS D . n 
D 2 156 GLU 156 156 156 GLU GLU D . n 
D 2 157 ILE 157 157 157 ILE ILE D . n 
D 2 158 THR 158 158 158 THR THR D . n 
D 2 159 ASP 159 159 159 ASP ASP D . n 
D 2 160 ALA 160 160 160 ALA ALA D . n 
D 2 161 MET 161 161 161 MET MET D . n 
D 2 162 LEU 162 162 162 LEU LEU D . n 
D 2 163 SER 163 163 163 SER SER D . n 
D 2 164 ASP 164 164 164 ASP ASP D . n 
D 2 165 ALA 165 165 165 ALA ALA D . n 
D 2 166 LEU 166 166 166 LEU LEU D . n 
D 2 167 ALA 167 167 167 ALA ALA D . n 
D 2 168 VAL 168 168 168 VAL VAL D . n 
D 2 169 CYS 169 169 169 CYS CYS D . n 
D 2 170 ASP 170 170 170 ASP ASP D . n 
D 2 171 GLU 171 171 171 GLU GLU D . n 
D 2 172 ASN 172 172 172 ASN ASN D . n 
D 2 173 ARG 173 173 173 ARG ARG D . n 
D 2 174 ARG 174 174 174 ARG ARG D . n 
D 2 175 LEU 175 175 175 LEU LEU D . n 
D 2 176 LEU 176 176 176 LEU LEU D . n 
D 2 177 ARG 177 177 177 ARG ARG D . n 
D 2 178 GLU 178 178 178 GLU GLU D . n 
D 2 179 LEU 179 179 179 LEU LEU D . n 
D 2 180 TYR 180 180 180 TYR TYR D . n 
D 2 181 GLU 181 181 181 GLU GLU D . n 
D 2 182 TYR 182 182 182 TYR TYR D . n 
D 2 183 ARG 183 183 183 ARG ARG D . n 
D 2 184 LYS 184 184 184 LYS LYS D . n 
D 2 185 ALA 185 185 185 ALA ALA D . n 
D 2 186 ALA 186 186 186 ALA ALA D . n 
D 2 187 ASP 187 187 187 ASP ASP D . n 
D 2 188 PRO 188 188 188 PRO PRO D . n 
D 2 189 LYS 189 189 189 LYS LYS D . n 
D 2 190 VAL 190 190 190 VAL VAL D . n 
D 2 191 THR 191 191 191 THR THR D . n 
D 2 192 GLY 192 192 192 GLY GLY D . n 
D 2 193 VAL 193 193 193 VAL VAL D . n 
D 2 194 GLU 194 194 194 GLU GLU D . n 
D 2 195 ALA 195 195 195 ALA ALA D . n 
D 2 196 LEU 196 196 196 LEU LEU D . n 
D 2 197 TYR 197 197 197 TYR TYR D . n 
D 2 198 ALA 198 198 198 ALA ALA D . n 
D 2 199 SER 199 199 199 SER SER D . n 
D 2 200 LEU 200 200 200 LEU LEU D . n 
D 2 201 THR 201 201 201 THR THR D . n 
D 2 202 ALA 202 202 202 ALA ALA D . n 
D 2 203 GLN 203 203 203 GLN GLN D . n 
D 2 204 PHE 204 204 204 PHE PHE D . n 
D 2 205 ILE 205 205 205 ILE ILE D . n 
D 2 206 ASP 206 206 206 ASP ASP D . n 
D 2 207 LYS 207 207 207 LYS LYS D . n 
D 2 208 ARG 208 208 208 ARG ARG D . n 
D 2 209 GLU 209 209 209 GLU GLU D . n 
D 2 210 HIS 210 210 210 HIS HIS D . n 
D 2 211 ASN 211 211 211 ASN ASN D . n 
D 2 212 GLU 212 212 212 GLU GLU D . n 
D 2 213 MET 213 213 213 MET MET D . n 
D 2 214 LEU 214 214 214 LEU LEU D . n 
D 2 215 LYS 215 215 215 LYS LYS D . n 
D 2 216 LYS 216 216 216 LYS LYS D . n 
D 2 217 THR 217 217 217 THR THR D . n 
D 2 218 LEU 218 218 218 LEU LEU D . n 
D 2 219 ALA 219 219 219 ALA ALA D . n 
D 2 220 ALA 220 220 220 ALA ALA D . n 
D 2 221 LEU 221 221 221 LEU LEU D . n 
D 2 222 PRO 222 222 222 PRO PRO D . n 
D 2 223 ASN 223 223 223 ASN ASN D . n 
D 2 224 ARG 224 224 224 ARG ARG D . n 
D 2 225 LYS 225 225 225 LYS LYS D . n 
D 2 226 VAL 226 226 226 VAL VAL D . n 
D 2 227 GLU 227 227 227 GLU GLU D . n 
D 2 228 ARG 228 228 228 ARG ARG D . n 
D 2 229 LYS 229 229 229 LYS LYS D . n 
D 2 230 THR 230 230 230 THR THR D . n 
D 2 231 GLY 231 231 231 GLY GLY D . n 
D 2 232 ALA 232 232 232 ALA ALA D . n 
D 2 233 ARG 233 233 233 ARG ARG D . n 
D 2 234 PHE 234 234 234 PHE PHE D . n 
D 2 235 MET 235 235 235 MET MET D . n 
D 2 236 THR 236 236 236 THR THR D . n 
D 2 237 ILE 237 237 237 ILE ILE D . n 
D 2 238 GLY 238 238 238 GLY GLY D . n 
D 2 239 SER 239 239 239 SER SER D . n 
D 2 240 GLU 240 240 240 GLU GLU D . n 
D 2 241 ASN 241 241 241 ASN ASN D . n 
D 2 242 ASP 242 242 242 ASP ASP D . n 
D 2 243 ASP 243 243 243 ASP ASP D . n 
D 2 244 ILE 244 244 244 ILE ILE D . n 
D 2 245 ALA 245 245 245 ALA ALA D . n 
D 2 246 PHE 246 246 246 PHE PHE D . n 
D 2 247 MET 247 247 247 MET MET D . n 
D 2 248 GLY 248 248 248 GLY GLY D . n 
D 2 249 MET 249 249 249 MET MET D . n 
D 2 250 VAL 250 250 250 VAL VAL D . n 
D 2 251 GLU 251 251 251 GLU GLU D . n 
D 2 252 SER 252 252 252 SER SER D . n 
D 2 253 VAL 253 253 253 VAL VAL D . n 
D 2 254 GLY 254 254 254 GLY GLY D . n 
D 2 255 ALA 255 255 255 ALA ALA D . n 
D 2 256 THR 256 256 256 THR THR D . n 
D 2 257 ILE 257 257 257 ILE ILE D . n 
D 2 258 VAL 258 258 258 VAL VAL D . n 
D 2 259 ILE 259 259 259 ILE ILE D . n 
D 2 260 ASP 260 260 260 ASP ASP D . n 
D 2 261 ASP 261 261 261 ASP ASP D . n 
D 2 262 GLN 262 262 262 GLN GLN D . n 
D 2 263 CYS 263 263 263 CYS CYS D . n 
D 2 264 SER 264 264 264 SER SER D . n 
D 2 265 GLY 265 265 265 GLY GLY D . n 
D 2 266 SER 266 266 266 SER SER D . n 
D 2 267 ARG 267 267 267 ARG ARG D . n 
D 2 268 TYR 268 268 268 TYR TYR D . n 
D 2 269 PHE 269 269 269 PHE PHE D . n 
D 2 270 TRP 270 270 270 TRP TRP D . n 
D 2 271 ASN 271 271 271 ASN ASN D . n 
D 2 272 ALA 272 272 272 ALA ALA D . n 
D 2 273 SER 273 273 273 SER SER D . n 
D 2 274 LYS 274 274 274 LYS LYS D . n 
D 2 275 PRO 275 275 275 PRO PRO D . n 
D 2 276 GLU 276 276 276 GLU GLU D . n 
D 2 277 GLY 277 277 277 GLY GLY D . n 
D 2 278 ASP 278 278 278 ASP ASP D . n 
D 2 279 VAL 279 279 279 VAL VAL D . n 
D 2 280 ILE 280 280 280 ILE ILE D . n 
D 2 281 LYS 281 281 281 LYS LYS D . n 
D 2 282 ALA 282 282 282 ALA ALA D . n 
D 2 283 ILE 283 283 283 ILE ILE D . n 
D 2 284 ALA 284 284 284 ALA ALA D . n 
D 2 285 GLU 285 285 285 GLU GLU D . n 
D 2 286 ARG 286 286 286 ARG ARG D . n 
D 2 287 TYR 287 287 287 TYR TYR D . n 
D 2 288 CYS 288 288 288 CYS CYS D . n 
D 2 289 ASP 289 289 289 ASP ASP D . n 
D 2 290 ARG 290 290 290 ARG ARG D . n 
D 2 291 PRO 291 291 291 PRO PRO D . n 
D 2 292 ALA 292 292 292 ALA ALA D . n 
D 2 293 CYS 293 293 293 CYS CYS D . n 
D 2 294 PRO 294 294 294 PRO PRO D . n 
D 2 295 THR 295 295 295 THR THR D . n 
D 2 296 LYS 296 296 296 LYS LYS D . n 
D 2 297 ASP 297 297 297 ASP ASP D . n 
D 2 298 TYR 298 298 298 TYR TYR D . n 
D 2 299 PRO 299 299 299 PRO PRO D . n 
D 2 300 ALA 300 300 300 ALA ALA D . n 
D 2 301 HIS 301 301 301 HIS HIS D . n 
D 2 302 THR 302 302 302 THR THR D . n 
D 2 303 ARG 303 303 303 ARG ARG D . n 
D 2 304 PHE 304 304 304 PHE PHE D . n 
D 2 305 ASP 305 305 305 ASP ASP D . n 
D 2 306 HIS 306 306 306 HIS HIS D . n 
D 2 307 VAL 307 307 307 VAL VAL D . n 
D 2 308 LEU 308 308 308 LEU LEU D . n 
D 2 309 GLY 309 309 309 GLY GLY D . n 
D 2 310 MET 310 310 310 MET MET D . n 
D 2 311 ALA 311 311 311 ALA ALA D . n 
D 2 312 LYS 312 312 312 LYS LYS D . n 
D 2 313 GLU 313 313 313 GLU GLU D . n 
D 2 314 TYR 314 314 314 TYR TYR D . n 
D 2 315 ASN 315 315 315 ASN ASN D . n 
D 2 316 VAL 316 316 316 VAL VAL D . n 
D 2 317 GLU 317 317 317 GLU GLU D . n 
D 2 318 GLY 318 318 318 GLY GLY D . n 
D 2 319 ALA 319 319 319 ALA ALA D . n 
D 2 320 ILE 320 320 320 ILE ILE D . n 
D 2 321 PHE 321 321 321 PHE PHE D . n 
D 2 322 LEU 322 322 322 LEU LEU D . n 
D 2 323 GLN 323 323 323 GLN GLN D . n 
D 2 324 GLN 324 324 324 GLN GLN D . n 
D 2 325 LYS 325 325 325 LYS LYS D . n 
D 2 326 PHE 326 326 326 PHE PHE D . n 
D 2 327 CYS 327 327 327 CYS CYS D . n 
D 2 328 ASP 328 328 328 ASP ASP D . n 
D 2 329 PRO 329 329 329 PRO PRO D . n 
D 2 330 HIS 330 330 330 HIS HIS D . n 
D 2 331 GLU 331 331 331 GLU GLU D . n 
D 2 332 GLY 332 332 332 GLY GLY D . n 
D 2 333 ASP 333 333 333 ASP ASP D . n 
D 2 334 TYR 334 334 334 TYR TYR D . n 
D 2 335 PRO 335 335 335 PRO PRO D . n 
D 2 336 ASP 336 336 336 ASP ASP D . n 
D 2 337 LEU 337 337 337 LEU LEU D . n 
D 2 338 LYS 338 338 338 LYS LYS D . n 
D 2 339 ARG 339 339 339 ARG ARG D . n 
D 2 340 HIS 340 340 340 HIS HIS D . n 
D 2 341 LEU 341 341 341 LEU LEU D . n 
D 2 342 GLU 342 342 342 GLU GLU D . n 
D 2 343 GLU 343 343 343 GLU GLU D . n 
D 2 344 ASN 344 344 344 ASN ASN D . n 
D 2 345 GLY 345 345 345 GLY GLY D . n 
D 2 346 ILE 346 346 346 ILE ILE D . n 
D 2 347 PRO 347 347 347 PRO PRO D . n 
D 2 348 THR 348 348 348 THR THR D . n 
D 2 349 LEU 349 349 349 LEU LEU D . n 
D 2 350 PHE 350 350 350 PHE PHE D . n 
D 2 351 LEU 351 351 351 LEU LEU D . n 
D 2 352 GLU 352 352 352 GLU GLU D . n 
D 2 353 PHE 353 353 353 PHE PHE D . n 
D 2 354 ASP 354 354 354 ASP ASP D . n 
D 2 355 ILE 355 355 355 ILE ILE D . n 
D 2 356 THR 356 356 356 THR THR D . n 
D 2 357 ASN 357 357 357 ASN ASN D . n 
D 2 358 PRO 358 358 358 PRO PRO D . n 
D 2 359 ILE 359 359 359 ILE ILE D . n 
D 2 360 GLY 360 360 360 GLY GLY D . n 
D 2 361 PRO 361 361 361 PRO PRO D . n 
D 2 362 PHE 362 362 362 PHE PHE D . n 
D 2 363 ARG 363 363 363 ARG ARG D . n 
D 2 364 ILE 364 364 364 ILE ILE D . n 
D 2 365 ARG 365 365 365 ARG ARG D . n 
D 2 366 ILE 366 366 366 ILE ILE D . n 
D 2 367 GLU 367 367 367 GLU GLU D . n 
D 2 368 ALA 368 368 368 ALA ALA D . n 
D 2 369 PHE 369 369 369 PHE PHE D . n 
D 2 370 LEU 370 370 370 LEU LEU D . n 
D 2 371 GLU 371 371 371 GLU GLU D . n 
D 2 372 THR 372 372 372 THR THR D . n 
D 2 373 LEU 373 373 373 LEU LEU D . n 
D 2 374 SER 374 374 374 SER SER D . n 
D 2 375 GLU 375 375 375 GLU GLU D . n 
D 2 376 GLU 376 376 376 GLU GLU D . n 
D 2 377 GLU 377 377 ?   ?   ?   D . n 
D 2 378 LEU 378 378 ?   ?   ?   D . n 
D 2 379 PHE 379 379 ?   ?   ?   D . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 HOH ? ? HOH ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SF4 ? ? SF4 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
E 3 BYC 1   501 501 BYC BYC A . 
F 4 GOL 1   502 512 GOL GOL A . 
G 5 SF4 1   503 450 SF4 SFO A . 
H 6 BJ8 1   401 450 BJ8 BJ8 B . 
I 7 TRS 1   402 502 TRS TRS B . 
J 3 BYC 1   501 501 BYC BYC C . 
K 4 GOL 1   502 511 GOL GOL C . 
L 4 GOL 1   503 513 GOL GOL C . 
M 5 SF4 1   504 450 SF4 SFO C . 
N 6 BJ8 1   401 450 BJ8 BJ8 D . 
O 7 TRS 1   402 501 TRS TRS D . 
P 8 HOH 1   601 671 HOH HOH A . 
P 8 HOH 2   602 647 HOH HOH A . 
P 8 HOH 3   603 611 HOH HOH A . 
P 8 HOH 4   604 605 HOH HOH A . 
P 8 HOH 5   605 636 HOH HOH A . 
P 8 HOH 6   606 648 HOH HOH A . 
P 8 HOH 7   607 775 HOH HOH A . 
P 8 HOH 8   608 291 HOH HOH A . 
P 8 HOH 9   609 814 HOH HOH A . 
P 8 HOH 10  610 80  HOH HOH A . 
P 8 HOH 11  611 753 HOH HOH A . 
P 8 HOH 12  612 206 HOH HOH A . 
P 8 HOH 13  613 69  HOH HOH A . 
P 8 HOH 14  614 600 HOH HOH A . 
P 8 HOH 15  615 796 HOH HOH A . 
P 8 HOH 16  616 791 HOH HOH A . 
P 8 HOH 17  617 391 HOH HOH A . 
P 8 HOH 18  618 557 HOH HOH A . 
P 8 HOH 19  619 656 HOH HOH A . 
P 8 HOH 20  620 779 HOH HOH A . 
P 8 HOH 21  621 366 HOH HOH A . 
P 8 HOH 22  622 564 HOH HOH A . 
P 8 HOH 23  623 208 HOH HOH A . 
P 8 HOH 24  624 581 HOH HOH A . 
P 8 HOH 25  625 91  HOH HOH A . 
P 8 HOH 26  626 762 HOH HOH A . 
P 8 HOH 27  627 803 HOH HOH A . 
P 8 HOH 28  628 657 HOH HOH A . 
P 8 HOH 29  629 72  HOH HOH A . 
P 8 HOH 30  630 582 HOH HOH A . 
P 8 HOH 31  631 180 HOH HOH A . 
P 8 HOH 32  632 76  HOH HOH A . 
P 8 HOH 33  633 761 HOH HOH A . 
P 8 HOH 34  634 450 HOH SFO A . 
P 8 HOH 35  635 816 HOH HOH A . 
P 8 HOH 36  636 437 HOH HOH A . 
P 8 HOH 37  637 24  HOH HOH A . 
P 8 HOH 38  638 364 HOH HOH A . 
P 8 HOH 39  639 455 HOH HOH A . 
P 8 HOH 40  640 93  HOH HOH A . 
P 8 HOH 41  641 759 HOH HOH A . 
P 8 HOH 42  642 425 HOH HOH A . 
P 8 HOH 43  643 472 HOH HOH A . 
P 8 HOH 44  644 187 HOH HOH A . 
P 8 HOH 45  645 194 HOH HOH A . 
P 8 HOH 46  646 641 HOH HOH A . 
P 8 HOH 47  647 40  HOH HOH A . 
P 8 HOH 48  648 302 HOH HOH A . 
P 8 HOH 49  649 523 HOH HOH A . 
P 8 HOH 50  650 336 HOH HOH A . 
P 8 HOH 51  651 275 HOH HOH A . 
P 8 HOH 52  652 94  HOH HOH A . 
P 8 HOH 53  653 19  HOH HOH A . 
P 8 HOH 54  654 416 HOH HOH A . 
P 8 HOH 55  655 541 HOH HOH A . 
P 8 HOH 56  656 83  HOH HOH A . 
P 8 HOH 57  657 170 HOH HOH A . 
P 8 HOH 58  658 75  HOH HOH A . 
P 8 HOH 59  659 337 HOH HOH A . 
P 8 HOH 60  660 402 HOH HOH A . 
P 8 HOH 61  661 395 HOH HOH A . 
P 8 HOH 62  662 51  HOH HOH A . 
P 8 HOH 63  663 44  HOH HOH A . 
P 8 HOH 64  664 294 HOH HOH A . 
P 8 HOH 65  665 639 HOH HOH A . 
P 8 HOH 66  666 189 HOH HOH A . 
P 8 HOH 67  667 32  HOH HOH A . 
P 8 HOH 68  668 571 HOH HOH A . 
P 8 HOH 69  669 409 HOH HOH A . 
P 8 HOH 70  670 104 HOH HOH A . 
P 8 HOH 71  671 281 HOH HOH A . 
P 8 HOH 72  672 303 HOH HOH A . 
P 8 HOH 73  673 334 HOH HOH A . 
P 8 HOH 74  674 544 HOH HOH A . 
P 8 HOH 75  675 148 HOH HOH A . 
P 8 HOH 76  676 140 HOH HOH A . 
P 8 HOH 77  677 207 HOH HOH A . 
P 8 HOH 78  678 201 HOH HOH A . 
P 8 HOH 79  679 15  HOH HOH A . 
P 8 HOH 80  680 231 HOH HOH A . 
P 8 HOH 81  681 270 HOH HOH A . 
P 8 HOH 82  682 29  HOH HOH A . 
P 8 HOH 83  683 237 HOH HOH A . 
P 8 HOH 84  684 169 HOH HOH A . 
P 8 HOH 85  685 37  HOH HOH A . 
P 8 HOH 86  686 633 HOH HOH A . 
P 8 HOH 87  687 211 HOH HOH A . 
P 8 HOH 88  688 151 HOH HOH A . 
P 8 HOH 89  689 59  HOH HOH A . 
P 8 HOH 90  690 209 HOH HOH A . 
P 8 HOH 91  691 167 HOH HOH A . 
P 8 HOH 92  692 273 HOH HOH A . 
P 8 HOH 93  693 253 HOH HOH A . 
P 8 HOH 94  694 427 HOH HOH A . 
P 8 HOH 95  695 801 HOH HOH A . 
P 8 HOH 96  696 413 HOH HOH A . 
P 8 HOH 97  697 456 HOH HOH A . 
P 8 HOH 98  698 118 HOH HOH A . 
P 8 HOH 99  699 418 HOH HOH A . 
P 8 HOH 100 700 105 HOH HOH A . 
P 8 HOH 101 701 22  HOH HOH A . 
P 8 HOH 102 702 361 HOH HOH A . 
P 8 HOH 103 703 642 HOH HOH A . 
P 8 HOH 104 704 54  HOH HOH A . 
P 8 HOH 105 705 77  HOH HOH A . 
P 8 HOH 106 706 749 HOH HOH A . 
P 8 HOH 107 707 129 HOH HOH A . 
P 8 HOH 108 708 81  HOH HOH A . 
P 8 HOH 109 709 126 HOH HOH A . 
P 8 HOH 110 710 567 HOH HOH A . 
P 8 HOH 111 711 827 HOH HOH A . 
P 8 HOH 112 712 522 HOH HOH A . 
P 8 HOH 113 713 578 HOH HOH A . 
P 8 HOH 114 714 799 HOH HOH A . 
P 8 HOH 115 715 430 HOH HOH A . 
P 8 HOH 116 716 74  HOH HOH A . 
P 8 HOH 117 717 85  HOH HOH A . 
P 8 HOH 118 718 468 HOH HOH A . 
P 8 HOH 119 719 115 HOH HOH A . 
P 8 HOH 120 720 173 HOH HOH A . 
P 8 HOH 121 721 33  HOH HOH A . 
P 8 HOH 122 722 243 HOH HOH A . 
P 8 HOH 123 723 182 HOH HOH A . 
P 8 HOH 124 724 154 HOH HOH A . 
P 8 HOH 125 725 339 HOH HOH A . 
P 8 HOH 126 726 789 HOH HOH A . 
P 8 HOH 127 727 454 HOH HOH A . 
P 8 HOH 128 728 507 HOH HOH A . 
P 8 HOH 129 729 475 HOH HOH A . 
P 8 HOH 130 730 66  HOH HOH A . 
P 8 HOH 131 731 204 HOH HOH A . 
P 8 HOH 132 732 332 HOH HOH A . 
P 8 HOH 133 733 769 HOH HOH A . 
P 8 HOH 134 734 607 HOH HOH A . 
P 8 HOH 135 735 439 HOH HOH A . 
P 8 HOH 136 736 739 HOH HOH A . 
P 8 HOH 137 737 202 HOH HOH A . 
P 8 HOH 138 738 11  HOH HOH A . 
P 8 HOH 139 739 113 HOH HOH A . 
P 8 HOH 140 740 359 HOH HOH A . 
P 8 HOH 141 741 247 HOH HOH A . 
P 8 HOH 142 742 163 HOH HOH A . 
P 8 HOH 143 743 227 HOH HOH A . 
P 8 HOH 144 744 12  HOH HOH A . 
P 8 HOH 145 745 373 HOH HOH A . 
P 8 HOH 146 746 283 HOH HOH A . 
P 8 HOH 147 747 123 HOH HOH A . 
P 8 HOH 148 748 535 HOH HOH A . 
P 8 HOH 149 749 185 HOH HOH A . 
P 8 HOH 150 750 79  HOH HOH A . 
P 8 HOH 151 751 117 HOH HOH A . 
P 8 HOH 152 752 61  HOH HOH A . 
P 8 HOH 153 753 449 HOH HOH A . 
P 8 HOH 154 754 467 HOH HOH A . 
P 8 HOH 155 755 351 HOH HOH A . 
P 8 HOH 156 756 375 HOH HOH A . 
P 8 HOH 157 757 297 HOH HOH A . 
P 8 HOH 158 758 781 HOH HOH A . 
P 8 HOH 159 759 261 HOH HOH A . 
P 8 HOH 160 760 106 HOH HOH A . 
P 8 HOH 161 761 519 HOH HOH A . 
P 8 HOH 162 762 248 HOH HOH A . 
P 8 HOH 163 763 107 HOH HOH A . 
P 8 HOH 164 764 21  HOH HOH A . 
P 8 HOH 165 765 643 HOH HOH A . 
P 8 HOH 166 766 568 HOH HOH A . 
P 8 HOH 167 767 703 HOH HOH A . 
P 8 HOH 168 768 575 HOH HOH A . 
P 8 HOH 169 769 27  HOH HOH A . 
P 8 HOH 170 770 553 HOH HOH A . 
P 8 HOH 171 771 491 HOH HOH A . 
P 8 HOH 172 772 479 HOH HOH A . 
P 8 HOH 173 773 212 HOH HOH A . 
P 8 HOH 174 774 822 HOH HOH A . 
P 8 HOH 175 775 31  HOH HOH A . 
P 8 HOH 176 776 242 HOH HOH A . 
P 8 HOH 177 777 506 HOH HOH A . 
P 8 HOH 178 778 127 HOH HOH A . 
P 8 HOH 179 779 457 HOH HOH A . 
P 8 HOH 180 780 561 HOH HOH A . 
P 8 HOH 181 781 197 HOH HOH A . 
P 8 HOH 182 782 181 HOH HOH A . 
P 8 HOH 183 783 316 HOH HOH A . 
P 8 HOH 184 784 782 HOH HOH A . 
P 8 HOH 185 785 320 HOH HOH A . 
P 8 HOH 186 786 806 HOH HOH A . 
P 8 HOH 187 787 229 HOH HOH A . 
P 8 HOH 188 788 772 HOH HOH A . 
P 8 HOH 189 789 788 HOH HOH A . 
P 8 HOH 190 790 172 HOH HOH A . 
P 8 HOH 191 791 331 HOH HOH A . 
P 8 HOH 192 792 616 HOH HOH A . 
P 8 HOH 193 793 87  HOH HOH A . 
P 8 HOH 194 794 150 HOH HOH A . 
P 8 HOH 195 795 149 HOH HOH A . 
P 8 HOH 196 796 530 HOH HOH A . 
P 8 HOH 197 797 565 HOH HOH A . 
P 8 HOH 198 798 166 HOH HOH A . 
P 8 HOH 199 799 3   HOH HOH A . 
P 8 HOH 200 800 177 HOH HOH A . 
P 8 HOH 201 801 663 HOH HOH A . 
P 8 HOH 202 802 260 HOH HOH A . 
P 8 HOH 203 803 526 HOH HOH A . 
P 8 HOH 204 804 754 HOH HOH A . 
P 8 HOH 205 805 780 HOH HOH A . 
P 8 HOH 206 806 315 HOH HOH A . 
P 8 HOH 207 807 777 HOH HOH A . 
P 8 HOH 208 808 596 HOH HOH A . 
P 8 HOH 209 809 301 HOH HOH A . 
P 8 HOH 210 810 758 HOH HOH A . 
P 8 HOH 211 811 311 HOH HOH A . 
P 8 HOH 212 812 795 HOH HOH A . 
P 8 HOH 213 813 477 HOH HOH A . 
P 8 HOH 214 814 735 HOH HOH A . 
P 8 HOH 215 815 289 HOH HOH A . 
P 8 HOH 216 816 492 HOH HOH A . 
P 8 HOH 217 817 405 HOH HOH A . 
P 8 HOH 218 818 820 HOH HOH A . 
P 8 HOH 219 819 804 HOH HOH A . 
P 8 HOH 220 820 448 HOH HOH A . 
P 8 HOH 221 821 698 HOH HOH A . 
P 8 HOH 222 822 217 HOH HOH A . 
P 8 HOH 223 823 235 HOH HOH A . 
P 8 HOH 224 824 682 HOH HOH A . 
P 8 HOH 225 825 514 HOH HOH A . 
P 8 HOH 226 826 546 HOH HOH A . 
P 8 HOH 227 827 652 HOH HOH A . 
P 8 HOH 228 828 678 HOH HOH A . 
P 8 HOH 229 829 695 HOH HOH A . 
P 8 HOH 230 830 555 HOH HOH A . 
P 8 HOH 231 831 620 HOH HOH A . 
P 8 HOH 232 832 604 HOH HOH A . 
P 8 HOH 233 833 768 HOH HOH A . 
P 8 HOH 234 834 793 HOH HOH A . 
P 8 HOH 235 835 797 HOH HOH A . 
P 8 HOH 236 836 826 HOH HOH A . 
P 8 HOH 237 837 745 HOH HOH A . 
P 8 HOH 238 838 727 HOH HOH A . 
P 8 HOH 239 839 602 HOH HOH A . 
P 8 HOH 240 840 383 HOH HOH A . 
P 8 HOH 241 841 767 HOH HOH A . 
P 8 HOH 242 842 587 HOH HOH A . 
P 8 HOH 243 843 387 HOH HOH A . 
P 8 HOH 244 844 520 HOH HOH A . 
P 8 HOH 245 845 810 HOH HOH A . 
P 8 HOH 246 846 640 HOH HOH A . 
P 8 HOH 247 847 360 HOH HOH A . 
P 8 HOH 248 848 340 HOH HOH A . 
P 8 HOH 249 849 382 HOH HOH A . 
P 8 HOH 250 850 609 HOH HOH A . 
P 8 HOH 251 851 811 HOH HOH A . 
P 8 HOH 252 852 365 HOH HOH A . 
P 8 HOH 253 853 685 HOH HOH A . 
P 8 HOH 254 854 386 HOH HOH A . 
P 8 HOH 255 855 765 HOH HOH A . 
P 8 HOH 256 856 466 HOH HOH A . 
P 8 HOH 257 857 385 HOH HOH A . 
Q 8 HOH 1   501 715 HOH HOH B . 
Q 8 HOH 2   502 590 HOH HOH B . 
Q 8 HOH 3   503 223 HOH HOH B . 
Q 8 HOH 4   504 390 HOH HOH B . 
Q 8 HOH 5   505 606 HOH HOH B . 
Q 8 HOH 6   506 458 HOH HOH B . 
Q 8 HOH 7   507 612 HOH HOH B . 
Q 8 HOH 8   508 393 HOH HOH B . 
Q 8 HOH 9   509 621 HOH HOH B . 
Q 8 HOH 10  510 742 HOH HOH B . 
Q 8 HOH 11  511 64  HOH HOH B . 
Q 8 HOH 12  512 195 HOH HOH B . 
Q 8 HOH 13  513 354 HOH HOH B . 
Q 8 HOH 14  514 300 HOH HOH B . 
Q 8 HOH 15  515 579 HOH HOH B . 
Q 8 HOH 16  516 398 HOH HOH B . 
Q 8 HOH 17  517 447 HOH HOH B . 
Q 8 HOH 18  518 221 HOH HOH B . 
Q 8 HOH 19  519 790 HOH HOH B . 
Q 8 HOH 20  520 798 HOH HOH B . 
Q 8 HOH 21  521 583 HOH HOH B . 
Q 8 HOH 22  522 495 HOH HOH B . 
Q 8 HOH 23  523 49  HOH HOH B . 
Q 8 HOH 24  524 689 HOH HOH B . 
Q 8 HOH 25  525 165 HOH HOH B . 
Q 8 HOH 26  526 39  HOH HOH B . 
Q 8 HOH 27  527 310 HOH HOH B . 
Q 8 HOH 28  528 35  HOH HOH B . 
Q 8 HOH 29  529 7   HOH HOH B . 
Q 8 HOH 30  530 757 HOH HOH B . 
Q 8 HOH 31  531 168 HOH HOH B . 
Q 8 HOH 32  532 452 HOH HOH B . 
Q 8 HOH 33  533 624 HOH HOH B . 
Q 8 HOH 34  534 92  HOH HOH B . 
Q 8 HOH 35  535 128 HOH HOH B . 
Q 8 HOH 36  536 560 HOH HOH B . 
Q 8 HOH 37  537 771 HOH HOH B . 
Q 8 HOH 38  538 46  HOH HOH B . 
Q 8 HOH 39  539 737 HOH HOH B . 
Q 8 HOH 40  540 268 HOH HOH B . 
Q 8 HOH 41  541 708 HOH HOH B . 
Q 8 HOH 42  542 36  HOH HOH B . 
Q 8 HOH 43  543 701 HOH HOH B . 
Q 8 HOH 44  544 422 HOH HOH B . 
Q 8 HOH 45  545 6   HOH HOH B . 
Q 8 HOH 46  546 733 HOH HOH B . 
Q 8 HOH 47  547 634 HOH HOH B . 
Q 8 HOH 48  548 285 HOH HOH B . 
Q 8 HOH 49  549 510 HOH HOH B . 
Q 8 HOH 50  550 442 HOH HOH B . 
Q 8 HOH 51  551 669 HOH HOH B . 
Q 8 HOH 52  552 53  HOH HOH B . 
Q 8 HOH 53  553 693 HOH HOH B . 
Q 8 HOH 54  554 321 HOH HOH B . 
Q 8 HOH 55  555 249 HOH HOH B . 
Q 8 HOH 56  556 494 HOH HOH B . 
Q 8 HOH 57  557 99  HOH HOH B . 
Q 8 HOH 58  558 534 HOH HOH B . 
Q 8 HOH 59  559 589 HOH HOH B . 
Q 8 HOH 60  560 350 HOH HOH B . 
Q 8 HOH 61  561 8   HOH HOH B . 
Q 8 HOH 62  562 414 HOH HOH B . 
Q 8 HOH 63  563 547 HOH HOH B . 
Q 8 HOH 64  564 412 HOH HOH B . 
Q 8 HOH 65  565 14  HOH HOH B . 
Q 8 HOH 66  566 496 HOH HOH B . 
Q 8 HOH 67  567 517 HOH HOH B . 
Q 8 HOH 68  568 220 HOH HOH B . 
Q 8 HOH 69  569 501 HOH HOH B . 
Q 8 HOH 70  570 58  HOH HOH B . 
Q 8 HOH 71  571 271 HOH HOH B . 
Q 8 HOH 72  572 136 HOH HOH B . 
Q 8 HOH 73  573 421 HOH HOH B . 
Q 8 HOH 74  574 525 HOH HOH B . 
Q 8 HOH 75  575 683 HOH HOH B . 
Q 8 HOH 76  576 63  HOH HOH B . 
Q 8 HOH 77  577 654 HOH HOH B . 
Q 8 HOH 78  578 434 HOH HOH B . 
Q 8 HOH 79  579 327 HOH HOH B . 
Q 8 HOH 80  580 529 HOH HOH B . 
Q 8 HOH 81  581 147 HOH HOH B . 
Q 8 HOH 82  582 282 HOH HOH B . 
Q 8 HOH 83  583 485 HOH HOH B . 
Q 8 HOH 84  584 357 HOH HOH B . 
Q 8 HOH 85  585 543 HOH HOH B . 
Q 8 HOH 86  586 577 HOH HOH B . 
Q 8 HOH 87  587 406 HOH HOH B . 
Q 8 HOH 88  588 718 HOH HOH B . 
Q 8 HOH 89  589 299 HOH HOH B . 
Q 8 HOH 90  590 43  HOH HOH B . 
Q 8 HOH 91  591 60  HOH HOH B . 
Q 8 HOH 92  592 108 HOH HOH B . 
Q 8 HOH 93  593 263 HOH HOH B . 
Q 8 HOH 94  594 630 HOH HOH B . 
Q 8 HOH 95  595 216 HOH HOH B . 
Q 8 HOH 96  596 156 HOH HOH B . 
Q 8 HOH 97  597 62  HOH HOH B . 
Q 8 HOH 98  598 125 HOH HOH B . 
Q 8 HOH 99  599 234 HOH HOH B . 
Q 8 HOH 100 600 766 HOH HOH B . 
Q 8 HOH 101 601 805 HOH HOH B . 
Q 8 HOH 102 602 404 HOH HOH B . 
Q 8 HOH 103 603 540 HOH HOH B . 
Q 8 HOH 104 604 286 HOH HOH B . 
Q 8 HOH 105 605 259 HOH HOH B . 
Q 8 HOH 106 606 110 HOH HOH B . 
Q 8 HOH 107 607 192 HOH HOH B . 
Q 8 HOH 108 608 497 HOH HOH B . 
Q 8 HOH 109 609 644 HOH HOH B . 
Q 8 HOH 110 610 232 HOH HOH B . 
Q 8 HOH 111 611 743 HOH HOH B . 
Q 8 HOH 112 612 190 HOH HOH B . 
Q 8 HOH 113 613 527 HOH HOH B . 
Q 8 HOH 114 614 436 HOH HOH B . 
Q 8 HOH 115 615 200 HOH HOH B . 
Q 8 HOH 116 616 131 HOH HOH B . 
Q 8 HOH 117 617 696 HOH HOH B . 
Q 8 HOH 118 618 41  HOH HOH B . 
Q 8 HOH 119 619 717 HOH HOH B . 
Q 8 HOH 120 620 719 HOH HOH B . 
Q 8 HOH 121 621 461 HOH HOH B . 
Q 8 HOH 122 622 371 HOH HOH B . 
Q 8 HOH 123 623 48  HOH HOH B . 
Q 8 HOH 124 624 692 HOH HOH B . 
Q 8 HOH 125 625 323 HOH HOH B . 
Q 8 HOH 126 626 770 HOH HOH B . 
Q 8 HOH 127 627 318 HOH HOH B . 
Q 8 HOH 128 628 109 HOH HOH B . 
Q 8 HOH 129 629 465 HOH HOH B . 
Q 8 HOH 130 630 138 HOH HOH B . 
Q 8 HOH 131 631 619 HOH HOH B . 
Q 8 HOH 132 632 503 HOH HOH B . 
Q 8 HOH 133 633 143 HOH HOH B . 
Q 8 HOH 134 634 435 HOH HOH B . 
Q 8 HOH 135 635 601 HOH HOH B . 
Q 8 HOH 136 636 463 HOH HOH B . 
Q 8 HOH 137 637 258 HOH HOH B . 
Q 8 HOH 138 638 121 HOH HOH B . 
Q 8 HOH 139 639 545 HOH HOH B . 
Q 8 HOH 140 640 521 HOH HOH B . 
Q 8 HOH 141 641 164 HOH HOH B . 
Q 8 HOH 142 642 572 HOH HOH B . 
Q 8 HOH 143 643 246 HOH HOH B . 
Q 8 HOH 144 644 254 HOH HOH B . 
Q 8 HOH 145 645 559 HOH HOH B . 
Q 8 HOH 146 646 191 HOH HOH B . 
Q 8 HOH 147 647 538 HOH HOH B . 
Q 8 HOH 148 648 367 HOH HOH B . 
Q 8 HOH 149 649 603 HOH HOH B . 
Q 8 HOH 150 650 594 HOH HOH B . 
Q 8 HOH 151 651 681 HOH HOH B . 
Q 8 HOH 152 652 176 HOH HOH B . 
Q 8 HOH 153 653 731 HOH HOH B . 
Q 8 HOH 154 654 716 HOH HOH B . 
Q 8 HOH 155 655 130 HOH HOH B . 
Q 8 HOH 156 656 608 HOH HOH B . 
Q 8 HOH 157 657 667 HOH HOH B . 
Q 8 HOH 158 658 650 HOH HOH B . 
Q 8 HOH 159 659 573 HOH HOH B . 
Q 8 HOH 160 660 617 HOH HOH B . 
Q 8 HOH 161 661 230 HOH HOH B . 
R 8 HOH 1   601 637 HOH HOH C . 
R 8 HOH 2   602 763 HOH HOH C . 
R 8 HOH 3   603 760 HOH HOH C . 
R 8 HOH 4   604 720 HOH HOH C . 
R 8 HOH 5   605 674 HOH HOH C . 
R 8 HOH 6   606 823 HOH HOH C . 
R 8 HOH 7   607 622 HOH HOH C . 
R 8 HOH 8   608 570 HOH HOH C . 
R 8 HOH 9   609 764 HOH HOH C . 
R 8 HOH 10  610 114 HOH HOH C . 
R 8 HOH 11  611 569 HOH HOH C . 
R 8 HOH 12  612 661 HOH HOH C . 
R 8 HOH 13  613 551 HOH HOH C . 
R 8 HOH 14  614 794 HOH HOH C . 
R 8 HOH 15  615 392 HOH HOH C . 
R 8 HOH 16  616 374 HOH HOH C . 
R 8 HOH 17  617 706 HOH HOH C . 
R 8 HOH 18  618 755 HOH HOH C . 
R 8 HOH 19  619 103 HOH HOH C . 
R 8 HOH 20  620 17  HOH HOH C . 
R 8 HOH 21  621 493 HOH HOH C . 
R 8 HOH 22  622 178 HOH HOH C . 
R 8 HOH 23  623 312 HOH HOH C . 
R 8 HOH 24  624 313 HOH HOH C . 
R 8 HOH 25  625 335 HOH HOH C . 
R 8 HOH 26  626 825 HOH HOH C . 
R 8 HOH 27  627 5   HOH HOH C . 
R 8 HOH 28  628 153 HOH HOH C . 
R 8 HOH 29  629 516 HOH HOH C . 
R 8 HOH 30  630 713 HOH HOH C . 
R 8 HOH 31  631 518 HOH HOH C . 
R 8 HOH 32  632 88  HOH HOH C . 
R 8 HOH 33  633 625 HOH HOH C . 
R 8 HOH 34  634 431 HOH HOH C . 
R 8 HOH 35  635 244 HOH HOH C . 
R 8 HOH 36  636 272 HOH HOH C . 
R 8 HOH 37  637 34  HOH HOH C . 
R 8 HOH 38  638 451 HOH HOH C . 
R 8 HOH 39  639 401 HOH HOH C . 
R 8 HOH 40  640 95  HOH HOH C . 
R 8 HOH 41  641 65  HOH HOH C . 
R 8 HOH 42  642 687 HOH HOH C . 
R 8 HOH 43  643 598 HOH HOH C . 
R 8 HOH 44  644 137 HOH HOH C . 
R 8 HOH 45  645 13  HOH HOH C . 
R 8 HOH 46  646 238 HOH HOH C . 
R 8 HOH 47  647 25  HOH HOH C . 
R 8 HOH 48  648 196 HOH HOH C . 
R 8 HOH 49  649 403 HOH HOH C . 
R 8 HOH 50  650 288 HOH HOH C . 
R 8 HOH 51  651 236 HOH HOH C . 
R 8 HOH 52  652 813 HOH HOH C . 
R 8 HOH 53  653 307 HOH HOH C . 
R 8 HOH 54  654 369 HOH HOH C . 
R 8 HOH 55  655 588 HOH HOH C . 
R 8 HOH 56  656 296 HOH HOH C . 
R 8 HOH 57  657 655 HOH HOH C . 
R 8 HOH 58  658 325 HOH HOH C . 
R 8 HOH 59  659 256 HOH HOH C . 
R 8 HOH 60  660 96  HOH HOH C . 
R 8 DOD 61  661 450 DOD SFO C . 
R 8 HOH 62  662 145 HOH HOH C . 
R 8 HOH 63  663 233 HOH HOH C . 
R 8 HOH 64  664 84  HOH HOH C . 
R 8 HOH 65  665 702 HOH HOH C . 
R 8 HOH 66  666 70  HOH HOH C . 
R 8 HOH 67  667 158 HOH HOH C . 
R 8 HOH 68  668 183 HOH HOH C . 
R 8 HOH 69  669 142 HOH HOH C . 
R 8 HOH 70  670 141 HOH HOH C . 
R 8 HOH 71  671 20  HOH HOH C . 
R 8 HOH 72  672 111 HOH HOH C . 
R 8 HOH 73  673 778 HOH HOH C . 
R 8 HOH 74  674 82  HOH HOH C . 
R 8 HOH 75  675 241 HOH HOH C . 
R 8 HOH 76  676 186 HOH HOH C . 
R 8 HOH 77  677 119 HOH HOH C . 
R 8 HOH 78  678 818 HOH HOH C . 
R 8 HOH 79  679 67  HOH HOH C . 
R 8 HOH 80  680 239 HOH HOH C . 
R 8 HOH 81  681 225 HOH HOH C . 
R 8 HOH 82  682 264 HOH HOH C . 
R 8 HOH 83  683 161 HOH HOH C . 
R 8 HOH 84  684 505 HOH HOH C . 
R 8 HOH 85  685 345 HOH HOH C . 
R 8 HOH 86  686 78  HOH HOH C . 
R 8 HOH 87  687 490 HOH HOH C . 
R 8 HOH 88  688 314 HOH HOH C . 
R 8 HOH 89  689 56  HOH HOH C . 
R 8 HOH 90  690 690 HOH HOH C . 
R 8 HOH 91  691 740 HOH HOH C . 
R 8 HOH 92  692 344 HOH HOH C . 
R 8 HOH 93  693 257 HOH HOH C . 
R 8 HOH 94  694 89  HOH HOH C . 
R 8 HOH 95  695 342 HOH HOH C . 
R 8 HOH 96  696 776 HOH HOH C . 
R 8 HOH 97  697 585 HOH HOH C . 
R 8 HOH 98  698 419 HOH HOH C . 
R 8 HOH 99  699 218 HOH HOH C . 
R 8 HOH 100 700 298 HOH HOH C . 
R 8 HOH 101 701 785 HOH HOH C . 
R 8 HOH 102 702 397 HOH HOH C . 
R 8 HOH 103 703 515 HOH HOH C . 
R 8 HOH 104 704 537 HOH HOH C . 
R 8 HOH 105 705 462 HOH HOH C . 
R 8 HOH 106 706 120 HOH HOH C . 
R 8 HOH 107 707 352 HOH HOH C . 
R 8 HOH 108 708 215 HOH HOH C . 
R 8 HOH 109 709 71  HOH HOH C . 
R 8 HOH 110 710 734 HOH HOH C . 
R 8 HOH 111 711 155 HOH HOH C . 
R 8 HOH 112 712 134 HOH HOH C . 
R 8 HOH 113 713 124 HOH HOH C . 
R 8 HOH 114 714 446 HOH HOH C . 
R 8 HOH 115 715 532 HOH HOH C . 
R 8 HOH 116 716 445 HOH HOH C . 
R 8 HOH 117 717 179 HOH HOH C . 
R 8 HOH 118 718 319 HOH HOH C . 
R 8 HOH 119 719 631 HOH HOH C . 
R 8 HOH 120 720 677 HOH HOH C . 
R 8 HOH 121 721 304 HOH HOH C . 
R 8 HOH 122 722 524 HOH HOH C . 
R 8 HOH 123 723 50  HOH HOH C . 
R 8 HOH 124 724 252 HOH HOH C . 
R 8 HOH 125 725 278 HOH HOH C . 
R 8 HOH 126 726 480 HOH HOH C . 
R 8 HOH 127 727 341 HOH HOH C . 
R 8 HOH 128 728 277 HOH HOH C . 
R 8 HOH 129 729 580 HOH HOH C . 
R 8 HOH 130 730 783 HOH HOH C . 
R 8 HOH 131 731 226 HOH HOH C . 
R 8 HOH 132 732 324 HOH HOH C . 
R 8 HOH 133 733 428 HOH HOH C . 
R 8 HOH 134 734 347 HOH HOH C . 
R 8 HOH 135 735 356 HOH HOH C . 
R 8 HOH 136 736 132 HOH HOH C . 
R 8 HOH 137 737 133 HOH HOH C . 
R 8 HOH 138 738 623 HOH HOH C . 
R 8 HOH 139 739 267 HOH HOH C . 
R 8 HOH 140 740 722 HOH HOH C . 
R 8 HOH 141 741 697 HOH HOH C . 
R 8 HOH 142 742 305 HOH HOH C . 
R 8 HOH 143 743 408 HOH HOH C . 
R 8 HOH 144 744 213 HOH HOH C . 
R 8 HOH 145 745 152 HOH HOH C . 
R 8 HOH 146 746 26  HOH HOH C . 
R 8 HOH 147 747 42  HOH HOH C . 
R 8 HOH 148 748 433 HOH HOH C . 
R 8 HOH 149 749 787 HOH HOH C . 
R 8 HOH 150 750 276 HOH HOH C . 
R 8 HOH 151 751 240 HOH HOH C . 
R 8 HOH 152 752 638 HOH HOH C . 
R 8 HOH 153 753 184 HOH HOH C . 
R 8 HOH 154 754 47  HOH HOH C . 
R 8 HOH 155 755 488 HOH HOH C . 
R 8 HOH 156 756 482 HOH HOH C . 
R 8 HOH 157 757 700 HOH HOH C . 
R 8 HOH 158 758 691 HOH HOH C . 
R 8 HOH 159 759 500 HOH HOH C . 
R 8 HOH 160 760 509 HOH HOH C . 
R 8 HOH 161 761 528 HOH HOH C . 
R 8 HOH 162 762 160 HOH HOH C . 
R 8 HOH 163 763 832 HOH HOH C . 
R 8 HOH 164 764 626 HOH HOH C . 
R 8 HOH 165 765 174 HOH HOH C . 
R 8 HOH 166 766 550 HOH HOH C . 
R 8 HOH 167 767 420 HOH HOH C . 
R 8 HOH 168 768 306 HOH HOH C . 
R 8 HOH 169 769 833 HOH HOH C . 
R 8 HOH 170 770 450 HOH HOH C . 
R 8 HOH 171 771 338 HOH HOH C . 
R 8 HOH 172 772 443 HOH HOH C . 
R 8 HOH 173 773 802 HOH HOH C . 
R 8 HOH 174 774 210 HOH HOH C . 
R 8 HOH 175 775 293 HOH HOH C . 
R 8 HOH 176 776 474 HOH HOH C . 
R 8 HOH 177 777 262 HOH HOH C . 
R 8 HOH 178 778 738 HOH HOH C . 
R 8 HOH 179 779 68  HOH HOH C . 
R 8 HOH 180 780 343 HOH HOH C . 
R 8 HOH 181 781 549 HOH HOH C . 
R 8 HOH 182 782 498 HOH HOH C . 
R 8 HOH 183 783 295 HOH HOH C . 
R 8 HOH 184 784 175 HOH HOH C . 
R 8 HOH 185 785 274 HOH HOH C . 
R 8 HOH 186 786 552 HOH HOH C . 
R 8 HOH 187 787 792 HOH HOH C . 
R 8 HOH 188 788 705 HOH HOH C . 
R 8 HOH 189 789 486 HOH HOH C . 
R 8 HOH 190 790 380 HOH HOH C . 
R 8 HOH 191 791 660 HOH HOH C . 
R 8 HOH 192 792 665 HOH HOH C . 
R 8 HOH 193 793 576 HOH HOH C . 
R 8 HOH 194 794 824 HOH HOH C . 
R 8 HOH 195 795 831 HOH HOH C . 
R 8 HOH 196 796 426 HOH HOH C . 
R 8 HOH 197 797 828 HOH HOH C . 
R 8 HOH 198 798 784 HOH HOH C . 
R 8 HOH 199 799 632 HOH HOH C . 
R 8 HOH 200 800 645 HOH HOH C . 
R 8 HOH 201 801 292 HOH HOH C . 
R 8 HOH 202 802 746 HOH HOH C . 
R 8 HOH 203 803 721 HOH HOH C . 
R 8 HOH 204 804 723 HOH HOH C . 
R 8 HOH 205 805 821 HOH HOH C . 
R 8 HOH 206 806 750 HOH HOH C . 
R 8 HOH 207 807 593 HOH HOH C . 
R 8 HOH 208 808 635 HOH HOH C . 
R 8 HOH 209 809 704 HOH HOH C . 
R 8 HOH 210 810 728 HOH HOH C . 
R 8 HOH 211 811 112 HOH HOH C . 
R 8 HOH 212 812 384 HOH HOH C . 
R 8 HOH 213 813 664 HOH HOH C . 
R 8 HOH 214 814 714 HOH HOH C . 
R 8 HOH 215 815 326 HOH HOH C . 
R 8 HOH 216 816 819 HOH HOH C . 
R 8 HOH 217 817 389 HOH HOH C . 
R 8 HOH 218 818 372 HOH HOH C . 
R 8 HOH 219 819 800 HOH HOH C . 
S 8 HOH 1   501 680 HOH HOH D . 
S 8 HOH 2   502 394 HOH HOH D . 
S 8 HOH 3   503 729 HOH HOH D . 
S 8 HOH 4   504 651 HOH HOH D . 
S 8 HOH 5   505 595 HOH HOH D . 
S 8 HOH 6   506 399 HOH HOH D . 
S 8 HOH 7   507 752 HOH HOH D . 
S 8 HOH 8   508 614 HOH HOH D . 
S 8 HOH 9   509 116 HOH HOH D . 
S 8 HOH 10  510 471 HOH HOH D . 
S 8 HOH 11  511 592 HOH HOH D . 
S 8 HOH 12  512 556 HOH HOH D . 
S 8 HOH 13  513 30  HOH HOH D . 
S 8 HOH 14  514 786 HOH HOH D . 
S 8 HOH 15  515 358 HOH HOH D . 
S 8 HOH 16  516 710 HOH HOH D . 
S 8 HOH 17  517 18  HOH HOH D . 
S 8 HOH 18  518 726 HOH HOH D . 
S 8 HOH 19  519 214 HOH HOH D . 
S 8 HOH 20  520 653 HOH HOH D . 
S 8 HOH 21  521 830 HOH HOH D . 
S 8 HOH 22  522 429 HOH HOH D . 
S 8 HOH 23  523 628 HOH HOH D . 
S 8 HOH 24  524 676 HOH HOH D . 
S 8 HOH 25  525 308 HOH HOH D . 
S 8 HOH 26  526 55  HOH HOH D . 
S 8 HOH 27  527 756 HOH HOH D . 
S 8 HOH 28  528 481 HOH HOH D . 
S 8 HOH 29  529 662 HOH HOH D . 
S 8 HOH 30  530 615 HOH HOH D . 
S 8 HOH 31  531 162 HOH HOH D . 
S 8 HOH 32  532 407 HOH HOH D . 
S 8 HOH 33  533 411 HOH HOH D . 
S 8 HOH 34  534 322 HOH HOH D . 
S 8 HOH 35  535 512 HOH HOH D . 
S 8 HOH 36  536 224 HOH HOH D . 
S 8 HOH 37  537 829 HOH HOH D . 
S 8 HOH 38  538 16  HOH HOH D . 
S 8 HOH 39  539 362 HOH HOH D . 
S 8 HOH 40  540 666 HOH HOH D . 
S 8 HOH 41  541 599 HOH HOH D . 
S 8 HOH 42  542 379 HOH HOH D . 
S 8 HOH 43  543 712 HOH HOH D . 
S 8 HOH 44  544 23  HOH HOH D . 
S 8 HOH 45  545 4   HOH HOH D . 
S 8 HOH 46  546 28  HOH HOH D . 
S 8 HOH 47  547 562 HOH HOH D . 
S 8 HOH 48  548 649 HOH HOH D . 
S 8 HOH 49  549 610 HOH HOH D . 
S 8 HOH 50  550 98  HOH HOH D . 
S 8 HOH 51  551 280 HOH HOH D . 
S 8 HOH 52  552 38  HOH HOH D . 
S 8 HOH 53  553 100 HOH HOH D . 
S 8 HOH 54  554 9   HOH HOH D . 
S 8 HOH 55  555 348 HOH HOH D . 
S 8 HOH 56  556 222 HOH HOH D . 
S 8 HOH 57  557 287 HOH HOH D . 
S 8 HOH 58  558 508 HOH HOH D . 
S 8 HOH 59  559 122 HOH HOH D . 
S 8 HOH 60  560 511 HOH HOH D . 
S 8 HOH 61  561 444 HOH HOH D . 
S 8 HOH 62  562 10  HOH HOH D . 
S 8 HOH 63  563 747 HOH HOH D . 
S 8 HOH 64  564 730 HOH HOH D . 
S 8 HOH 65  565 424 HOH HOH D . 
S 8 HOH 66  566 817 HOH HOH D . 
S 8 HOH 67  567 388 HOH HOH D . 
S 8 HOH 68  568 483 HOH HOH D . 
S 8 HOH 69  569 812 HOH HOH D . 
S 8 HOH 70  570 157 HOH HOH D . 
S 8 HOH 71  571 400 HOH HOH D . 
S 8 HOH 72  572 144 HOH HOH D . 
S 8 HOH 73  573 199 HOH HOH D . 
S 8 HOH 74  574 353 HOH HOH D . 
S 8 HOH 75  575 646 HOH HOH D . 
S 8 HOH 76  576 255 HOH HOH D . 
S 8 HOH 77  577 102 HOH HOH D . 
S 8 HOH 78  578 90  HOH HOH D . 
S 8 HOH 79  579 658 HOH HOH D . 
S 8 HOH 80  580 748 HOH HOH D . 
S 8 HOH 81  581 73  HOH HOH D . 
S 8 HOH 82  582 377 HOH HOH D . 
S 8 HOH 83  583 171 HOH HOH D . 
S 8 HOH 84  584 251 HOH HOH D . 
S 8 HOH 85  585 355 HOH HOH D . 
S 8 HOH 86  586 709 HOH HOH D . 
S 8 HOH 87  587 724 HOH HOH D . 
S 8 HOH 88  588 45  HOH HOH D . 
S 8 HOH 89  589 159 HOH HOH D . 
S 8 HOH 90  590 438 HOH HOH D . 
S 8 HOH 91  591 245 HOH HOH D . 
S 8 HOH 92  592 86  HOH HOH D . 
S 8 HOH 93  593 423 HOH HOH D . 
S 8 HOH 94  594 135 HOH HOH D . 
S 8 HOH 95  595 381 HOH HOH D . 
S 8 HOH 96  596 219 HOH HOH D . 
S 8 HOH 97  597 531 HOH HOH D . 
S 8 HOH 98  598 328 HOH HOH D . 
S 8 HOH 99  599 52  HOH HOH D . 
S 8 HOH 100 600 228 HOH HOH D . 
S 8 HOH 101 601 97  HOH HOH D . 
S 8 HOH 102 602 368 HOH HOH D . 
S 8 HOH 103 603 460 HOH HOH D . 
S 8 HOH 104 604 279 HOH HOH D . 
S 8 HOH 105 605 317 HOH HOH D . 
S 8 HOH 106 606 205 HOH HOH D . 
S 8 HOH 107 607 290 HOH HOH D . 
S 8 HOH 108 608 487 HOH HOH D . 
S 8 HOH 109 609 410 HOH HOH D . 
S 8 HOH 110 610 707 HOH HOH D . 
S 8 HOH 111 611 396 HOH HOH D . 
S 8 HOH 112 612 499 HOH HOH D . 
S 8 HOH 113 613 330 HOH HOH D . 
S 8 HOH 114 614 269 HOH HOH D . 
S 8 HOH 115 615 193 HOH HOH D . 
S 8 HOH 116 616 566 HOH HOH D . 
S 8 HOH 117 617 558 HOH HOH D . 
S 8 HOH 118 618 146 HOH HOH D . 
S 8 HOH 119 619 329 HOH HOH D . 
S 8 HOH 120 620 459 HOH HOH D . 
S 8 HOH 121 621 539 HOH HOH D . 
S 8 HOH 122 622 725 HOH HOH D . 
S 8 HOH 123 623 548 HOH HOH D . 
S 8 HOH 124 624 478 HOH HOH D . 
S 8 HOH 125 625 773 HOH HOH D . 
S 8 HOH 126 626 618 HOH HOH D . 
S 8 HOH 127 627 502 HOH HOH D . 
S 8 HOH 128 628 284 HOH HOH D . 
S 8 HOH 129 629 464 HOH HOH D . 
S 8 HOH 130 630 250 HOH HOH D . 
S 8 HOH 131 631 473 HOH HOH D . 
S 8 HOH 132 632 309 HOH HOH D . 
S 8 HOH 133 633 476 HOH HOH D . 
S 8 HOH 134 634 668 HOH HOH D . 
S 8 HOH 135 635 489 HOH HOH D . 
S 8 HOH 136 636 378 HOH HOH D . 
S 8 HOH 137 637 440 HOH HOH D . 
S 8 HOH 138 638 597 HOH HOH D . 
S 8 HOH 139 639 659 HOH HOH D . 
S 8 HOH 140 640 563 HOH HOH D . 
S 8 HOH 141 641 694 HOH HOH D . 
S 8 HOH 142 642 542 HOH HOH D . 
S 8 HOH 143 643 684 HOH HOH D . 
S 8 HOH 144 644 536 HOH HOH D . 
S 8 HOH 145 645 613 HOH HOH D . 
S 8 HOH 146 646 711 HOH HOH D . 
S 8 HOH 147 647 774 HOH HOH D . 
S 8 HOH 148 648 139 HOH HOH D . 
S 8 HOH 149 649 679 HOH HOH D . 
S 8 HOH 150 650 346 HOH HOH D . 
S 8 HOH 151 651 808 HOH HOH D . 
S 8 HOH 152 652 699 HOH HOH D . 
S 8 HOH 153 653 686 HOH HOH D . 
S 8 HOH 154 654 627 HOH HOH D . 
S 8 HOH 155 655 266 HOH HOH D . 
S 8 HOH 156 656 809 HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   102.48 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8S2R 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     208.170 
_cell.length_a_esd                 ? 
_cell.length_b                     102.710 
_cell.length_b_esd                 ? 
_cell.length_c                     86.900 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8S2R 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8S2R 
_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             2.39 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.60 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'PEG 3350, bis-tris propane pH 7.5, sodium formate or sodium acetate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.0 
# 
_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 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-06 
_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   1.0 
_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                        'SLS BEAMLINE X10SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8S2R 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.6 
_reflns.d_resolution_low                               50.0 
_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                                     201996 
_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                           86.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.48 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.075 
_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                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.064 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.60  1.7  ? ? ? ? ? ? 16309 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.612                ? ? 1  1 0.735              ? ? ? ? 
0.47700000000000004  ? ? ? ? ? ? ? ? ? 
1.70  1.9  ? ? ? ? ? ? 45741 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.35                 ? ? 2  1 0.9209999999999999 ? ? ? ? 0.29 ? ? ? ? ? 
? ? ? ? 
1.90  2.3  ? ? ? ? ? ? 60843 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.156                ? ? 3  1 0.9840000000000001 ? ? ? ? 0.133 ? ? ? ? 
? ? ? ? ? 
2.30  2.9  ? ? ? ? ? ? 39513 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.084                ? ? 4  1 0.992              ? ? ? ? 
0.07200000000000001  ? ? ? ? ? ? ? ? ? 
2.90  3.8  ? ? ? ? ? ? 21864 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.062                ? ? 5  1 0.9940000000000001 ? ? ? ? 0.053 ? ? ? ? 
? ? ? ? ? 
3.80  4.6  ? ? ? ? ? ? 7680  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.057                ? ? 6  1 0.9940000000000001 ? ? ? ? 0.049 ? ? ? ? 
? ? ? ? ? 
4.60  5.7  ? ? ? ? ? ? 4728  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.057                ? ? 7  1 0.993              ? ? ? ? 0.049 ? ? ? ? 
? ? ? ? ? 
5.70  8.0  ? ? ? ? ? ? 3367  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.062                ? ? 8  1 0.992              ? ? ? ? 
0.052000000000000005 ? ? ? ? ? ? ? ? ? 
8.00  12.0 ? ? ? ? ? ? 1365  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.055999999999999994 ? ? 9  1 0.996              ? ? ? ? 0.048 ? ? ? ? 
? ? ? ? ? 
12.00 50.0 ? ? ? ? ? ? 586   ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.057                ? ? 10 1 0.997              ? ? ? ? 0.048 ? ? ? ? 
? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8S2R 
_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                            1.60 
_refine.ls_d_res_low                             48.45 
_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                     201898 
_refine.ls_number_reflns_R_free                  10116 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    86.09 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1846 
_refine.ls_R_factor_R_free                       0.2111 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1832 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.03 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.17 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        48.45 
_refine_hist.number_atoms_solvent             791 
_refine_hist.number_atoms_total               14020 
_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        13031 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         198 
_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' ? 0.016 ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.959 ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.626 ? 1868 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.083 ? 1908 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.013 ? 2410 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.60 1.62  . . 50  1181 16.00  . . . . 0.6612 . . . . . . . . . . . 0.7775 
'X-RAY DIFFRACTION' 1.62 1.64  . . 141 2646 36.00  . . . . 0.4393 . . . . . . . . . . . 0.4698 
'X-RAY DIFFRACTION' 1.64 1.66  . . 184 3523 47.00  . . . . 0.3351 . . . . . . . . . . . 0.3560 
'X-RAY DIFFRACTION' 1.66 1.68  . . 187 3973 53.00  . . . . 0.3007 . . . . . . . . . . . 0.3536 
'X-RAY DIFFRACTION' 1.68 1.70  . . 235 4285 58.00  . . . . 0.2728 . . . . . . . . . . . 0.3043 
'X-RAY DIFFRACTION' 1.70 1.72  . . 249 4619 63.00  . . . . 0.2519 . . . . . . . . . . . 0.2937 
'X-RAY DIFFRACTION' 1.72 1.75  . . 259 5088 68.00  . . . . 0.2368 . . . . . . . . . . . 0.2736 
'X-RAY DIFFRACTION' 1.75 1.77  . . 301 5547 75.00  . . . . 0.2256 . . . . . . . . . . . 0.3102 
'X-RAY DIFFRACTION' 1.77 1.80  . . 313 6037 82.00  . . . . 0.2171 . . . . . . . . . . . 0.2440 
'X-RAY DIFFRACTION' 1.80 1.83  . . 348 6657 90.00  . . . . 0.2039 . . . . . . . . . . . 0.2463 
'X-RAY DIFFRACTION' 1.83 1.86  . . 384 7373 99.00  . . . . 0.1895 . . . . . . . . . . . 0.2231 
'X-RAY DIFFRACTION' 1.86 1.90  . . 400 7431 100.00 . . . . 0.2014 . . . . . . . . . . . 0.2338 
'X-RAY DIFFRACTION' 1.90 1.93  . . 415 7376 100.00 . . . . 0.1959 . . . . . . . . . . . 0.2093 
'X-RAY DIFFRACTION' 1.93 1.97  . . 390 7395 100.00 . . . . 0.1909 . . . . . . . . . . . 0.2361 
'X-RAY DIFFRACTION' 1.97 2.02  . . 412 7361 100.00 . . . . 0.1842 . . . . . . . . . . . 0.2283 
'X-RAY DIFFRACTION' 2.02 2.06  . . 394 7357 100.00 . . . . 0.1776 . . . . . . . . . . . 0.2120 
'X-RAY DIFFRACTION' 2.06 2.11  . . 388 7373 100.00 . . . . 0.1741 . . . . . . . . . . . 0.2192 
'X-RAY DIFFRACTION' 2.11 2.17  . . 406 7414 100.00 . . . . 0.1682 . . . . . . . . . . . 0.2054 
'X-RAY DIFFRACTION' 2.17 2.24  . . 416 7359 100.00 . . . . 0.1694 . . . . . . . . . . . 0.2079 
'X-RAY DIFFRACTION' 2.24 2.31  . . 363 7395 99.00  . . . . 0.1675 . . . . . . . . . . . 0.1966 
'X-RAY DIFFRACTION' 2.31 2.39  . . 402 7388 100.00 . . . . 0.1772 . . . . . . . . . . . 0.2043 
'X-RAY DIFFRACTION' 2.39 2.49  . . 374 7413 100.00 . . . . 0.1856 . . . . . . . . . . . 0.2224 
'X-RAY DIFFRACTION' 2.49 2.60  . . 398 7380 100.00 . . . . 0.1755 . . . . . . . . . . . 0.2209 
'X-RAY DIFFRACTION' 2.60 2.74  . . 399 7419 100.00 . . . . 0.1799 . . . . . . . . . . . 0.2175 
'X-RAY DIFFRACTION' 2.74 2.91  . . 408 7446 100.00 . . . . 0.1923 . . . . . . . . . . . 0.2245 
'X-RAY DIFFRACTION' 2.91 3.13  . . 353 7423 100.00 . . . . 0.2012 . . . . . . . . . . . 0.2650 
'X-RAY DIFFRACTION' 3.13 3.45  . . 366 7452 99.00  . . . . 0.1938 . . . . . . . . . . . 0.2099 
'X-RAY DIFFRACTION' 3.45 3.95  . . 390 7439 100.00 . . . . 0.1696 . . . . . . . . . . . 0.1803 
'X-RAY DIFFRACTION' 3.95 4.97  . . 393 7470 100.00 . . . . 0.1529 . . . . . . . . . . . 0.1753 
'X-RAY DIFFRACTION' 4.97 48.45 . . 398 7562 99.00  . . . . 0.1814 . . . . . . . . . . . 0.1854 
# 
_struct.entry_id                     8S2R 
_struct.title                        'BzdNO in partially coenzyme A - free state' 
_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        8S2R 
_struct_keywords.text            'Benzoyl-CoA reductase, reductive dearomatization, iron-sulfur clusters, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 7 ? 
J N N 3 ? 
K N N 4 ? 
L N N 4 ? 
M N N 5 ? 
N N N 6 ? 
O N N 7 ? 
P N N 8 ? 
Q N N 8 ? 
R N N 8 ? 
S N N 8 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP Q68VL9_9RHOO Q68VL9 ? 1 
;MNAMANKYPTEQLKLWGKAKELREQYYMNYARAKEKGGIRWSGSAWALDAIPAGLGEDVYSLTGEPYAAAVAHDRKFAKE
CMDAAEAYGFARDLCSYMRIYWGGMHLNKYAFGGEFPKPDFVFQTQICCSHSKWYQHVAKEEKIPEFYLDVGVGPYRDMT
DARLDYVANQLHDGIAFVEKASGRKFDDELFIKAVKNEMRSTSRWADICALNKVKPAPLDEKTMYSLYVLCTLSKSSQWC
ADFMDELYEEVKDRVARGIAAVPNEAIRLMTDTQPPWSFLKIFRYLETYGAVSIGSLYTFALEGIWEDKPDGSWGGRTLP
WDKGIEINDRDTAVRLYADWNLSKPQWQHFYDPTIKSDMMLRIIKEWQVDGVMLHLNRGCEGLSVGIMENRLAIAKSGTP
VMTFEGNMGDEREFDEVRTQARVDAFMEQLGVRRQAA
;
1 
2 UNP Q68VM0_9RHOO Q68VM0 ? 2 
;MSDGLFDQFKTWYEKRHDYARDWKVRTGGQVVATMCTYTPEELLIAAGMLPVRVLGAHEPQNVTEPHIFGMFCPFCRDSL
AQGLLGRFDYAEGVTLTQSCIQYRQTFGSWRLHVPTVKWDYYVPMPNEVQSPHARKAHYEEVQAFRVFLQTLTGKEITDA
MLSDALAVCDENRRLLRELYEYRKAADPKVTGVEALYASLTAQFIDKREHNEMLKKTLAALPNRKVERKTGARFMTIGSE
NDDIAFMGMVESVGATIVIDDQCSGSRYFWNASKPEGDVIKAIAERYCDRPACPTKDYPAHTRFDHVLGMAKEYNVEGAI
FLQQKFCDPHEGDYPDLKRHLEENGIPTLFLEFDITNPIGPFRIRIEAFLETLSEEELF
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8S2R A 1 ? 437 ? Q68VL9 1 ? 437 ? 1 437 
2 2 8S2R B 1 ? 379 ? Q68VM0 1 ? 379 ? 1 379 
3 1 8S2R C 1 ? 437 ? Q68VL9 1 ? 437 ? 1 437 
4 2 8S2R D 1 ? 379 ? Q68VM0 1 ? 379 ? 1 379 
# 
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 8S2R SER A 438 ? UNP Q68VL9 ? ? 'expression tag' 438 1  
1 8S2R ALA A 439 ? UNP Q68VL9 ? ? 'expression tag' 439 2  
1 8S2R TRP A 440 ? UNP Q68VL9 ? ? 'expression tag' 440 3  
1 8S2R SER A 441 ? UNP Q68VL9 ? ? 'expression tag' 441 4  
1 8S2R HIS A 442 ? UNP Q68VL9 ? ? 'expression tag' 442 5  
1 8S2R PRO A 443 ? UNP Q68VL9 ? ? 'expression tag' 443 6  
1 8S2R GLN A 444 ? UNP Q68VL9 ? ? 'expression tag' 444 7  
1 8S2R PHE A 445 ? UNP Q68VL9 ? ? 'expression tag' 445 8  
1 8S2R GLU A 446 ? UNP Q68VL9 ? ? 'expression tag' 446 9  
1 8S2R LYS A 447 ? UNP Q68VL9 ? ? 'expression tag' 447 10 
3 8S2R SER C 438 ? UNP Q68VL9 ? ? 'expression tag' 438 11 
3 8S2R ALA C 439 ? UNP Q68VL9 ? ? 'expression tag' 439 12 
3 8S2R TRP C 440 ? UNP Q68VL9 ? ? 'expression tag' 440 13 
3 8S2R SER C 441 ? UNP Q68VL9 ? ? 'expression tag' 441 14 
3 8S2R HIS C 442 ? UNP Q68VL9 ? ? 'expression tag' 442 15 
3 8S2R PRO C 443 ? UNP Q68VL9 ? ? 'expression tag' 443 16 
3 8S2R GLN C 444 ? UNP Q68VL9 ? ? 'expression tag' 444 17 
3 8S2R PHE C 445 ? UNP Q68VL9 ? ? 'expression tag' 445 18 
3 8S2R GLU C 446 ? UNP Q68VL9 ? ? 'expression tag' 446 19 
3 8S2R LYS C 447 ? UNP Q68VL9 ? ? 'expression tag' 447 20 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4910  ? 
1 MORE         -38   ? 
1 'SSA (A^2)'  28680 ? 
2 'ABSA (A^2)' 4790  ? 
2 MORE         -38   ? 
2 'SSA (A^2)'  27760 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I,P,Q   
2 1 C,D,J,K,L,M,N,O,R,S 
# 
_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 LEU A 15  ? ARG A 32  ? LEU A 15  ARG A 32  1 ? 18 
HELX_P HELX_P2  AA2 ALA A 33  ? GLY A 37  ? ALA A 33  GLY A 37  5 ? 5  
HELX_P HELX_P3  AA3 ASP A 49  ? GLY A 54  ? ASP A 49  GLY A 54  1 ? 6  
HELX_P HELX_P4  AA4 GLY A 64  ? ASP A 74  ? GLY A 64  ASP A 74  1 ? 11 
HELX_P HELX_P5  AA5 ASP A 74  ? GLY A 89  ? ASP A 74  GLY A 89  1 ? 16 
HELX_P HELX_P6  AA6 CYS A 95  ? ASN A 108 ? CYS A 95  ASN A 108 1 ? 14 
HELX_P HELX_P7  AA7 CYS A 128 ? LYS A 143 ? CYS A 128 LYS A 143 1 ? 16 
HELX_P HELX_P8  AA8 PRO A 155 ? MET A 159 ? PRO A 155 MET A 159 5 ? 5  
HELX_P HELX_P9  AA9 THR A 160 ? GLY A 183 ? THR A 160 GLY A 183 1 ? 24 
HELX_P HELX_P10 AB1 ASP A 187 ? LEU A 211 ? ASP A 187 LEU A 211 1 ? 25 
HELX_P HELX_P11 AB2 ASN A 212 ? VAL A 214 ? ASN A 212 VAL A 214 5 ? 3  
HELX_P HELX_P12 AB3 ASP A 220 ? SER A 226 ? ASP A 220 SER A 226 1 ? 7  
HELX_P HELX_P13 AB4 TYR A 228 ? LYS A 235 ? TYR A 228 LYS A 235 1 ? 8  
HELX_P HELX_P14 AB5 SER A 237 ? ARG A 257 ? SER A 237 ARG A 257 1 ? 21 
HELX_P HELX_P15 AB6 PRO A 276 ? SER A 278 ? PRO A 276 SER A 278 5 ? 3  
HELX_P HELX_P16 AB7 PHE A 279 ? THR A 288 ? PHE A 279 THR A 288 1 ? 10 
HELX_P HELX_P17 AB8 LEU A 297 ? LEU A 302 ? LEU A 297 LEU A 302 1 ? 6  
HELX_P HELX_P18 AB9 LEU A 319 ? GLY A 324 ? LEU A 319 GLY A 324 5 ? 6  
HELX_P HELX_P19 AC1 ASP A 329 ? SER A 343 ? ASP A 329 SER A 343 1 ? 15 
HELX_P HELX_P20 AC2 LYS A 344 ? TYR A 351 ? LYS A 344 TYR A 351 5 ? 8  
HELX_P HELX_P21 AC3 ASP A 352 ? TRP A 367 ? ASP A 352 TRP A 367 1 ? 16 
HELX_P HELX_P22 AC4 CYS A 380 ? VAL A 385 ? CYS A 380 VAL A 385 1 ? 6  
HELX_P HELX_P23 AC5 GLY A 386 ? GLY A 398 ? GLY A 386 GLY A 398 1 ? 13 
HELX_P HELX_P24 AC6 ASP A 410 ? PHE A 414 ? ASP A 410 PHE A 414 5 ? 5  
HELX_P HELX_P25 AC7 ASP A 415 ? HIS A 442 ? ASP A 415 HIS A 442 1 ? 28 
HELX_P HELX_P26 AC8 PHE B 6   ? LYS B 15  ? PHE B 6   LYS B 15  1 ? 10 
HELX_P HELX_P27 AC9 LYS B 15  ? GLY B 28  ? LYS B 15  GLY B 28  1 ? 14 
HELX_P HELX_P28 AD1 PRO B 40  ? ALA B 47  ? PRO B 40  ALA B 47  1 ? 8  
HELX_P HELX_P29 AD2 CYS B 73  ? LEU B 85  ? CYS B 73  LEU B 85  1 ? 13 
HELX_P HELX_P30 AD3 CYS B 100 ? VAL B 114 ? CYS B 100 VAL B 114 1 ? 15 
HELX_P HELX_P31 AD4 HIS B 133 ? GLY B 154 ? HIS B 133 GLY B 154 1 ? 22 
HELX_P HELX_P32 AD5 THR B 158 ? TYR B 182 ? THR B 158 TYR B 182 1 ? 25 
HELX_P HELX_P33 AD6 ARG B 183 ? ALA B 185 ? ARG B 183 ALA B 185 5 ? 3  
HELX_P HELX_P34 AD7 THR B 191 ? ALA B 202 ? THR B 191 ALA B 202 1 ? 12 
HELX_P HELX_P35 AD8 ASP B 206 ? LEU B 221 ? ASP B 206 LEU B 221 1 ? 16 
HELX_P HELX_P36 AD9 PRO B 222 ? ARG B 224 ? PRO B 222 ARG B 224 5 ? 3  
HELX_P HELX_P37 AE1 ASP B 243 ? VAL B 253 ? ASP B 243 VAL B 253 1 ? 11 
HELX_P HELX_P38 AE2 GLY B 265 ? TRP B 270 ? GLY B 265 TRP B 270 1 ? 6  
HELX_P HELX_P39 AE3 ASP B 278 ? ARG B 290 ? ASP B 278 ARG B 290 1 ? 13 
HELX_P HELX_P40 AE4 CYS B 293 ? ASP B 297 ? CYS B 293 ASP B 297 5 ? 5  
HELX_P HELX_P41 AE5 HIS B 301 ? TYR B 314 ? HIS B 301 TYR B 314 1 ? 14 
HELX_P HELX_P42 AE6 CYS B 327 ? ASN B 344 ? CYS B 327 ASN B 344 1 ? 18 
HELX_P HELX_P43 AE7 PRO B 358 ? GLU B 375 ? PRO B 358 GLU B 375 1 ? 18 
HELX_P HELX_P44 AE8 LEU C 15  ? ALA C 33  ? LEU C 15  ALA C 33  1 ? 19 
HELX_P HELX_P45 AE9 LYS C 34  ? GLY C 37  ? LYS C 34  GLY C 37  5 ? 4  
HELX_P HELX_P46 AF1 ASP C 49  ? GLY C 54  ? ASP C 49  GLY C 54  1 ? 6  
HELX_P HELX_P47 AF2 GLY C 64  ? HIS C 73  ? GLY C 64  HIS C 73  1 ? 10 
HELX_P HELX_P48 AF3 ASP C 74  ? GLY C 89  ? ASP C 74  GLY C 89  1 ? 16 
HELX_P HELX_P49 AF4 CYS C 95  ? ASN C 108 ? CYS C 95  ASN C 108 1 ? 14 
HELX_P HELX_P50 AF5 CYS C 128 ? LYS C 143 ? CYS C 128 LYS C 143 1 ? 16 
HELX_P HELX_P51 AF6 PRO C 155 ? MET C 159 ? PRO C 155 MET C 159 5 ? 5  
HELX_P HELX_P52 AF7 THR C 160 ? GLY C 183 ? THR C 160 GLY C 183 1 ? 24 
HELX_P HELX_P53 AF8 ASP C 187 ? LEU C 211 ? ASP C 187 LEU C 211 1 ? 25 
HELX_P HELX_P54 AF9 ASN C 212 ? VAL C 214 ? ASN C 212 VAL C 214 5 ? 3  
HELX_P HELX_P55 AG1 ASP C 220 ? LYS C 235 ? ASP C 220 LYS C 235 1 ? 16 
HELX_P HELX_P56 AG2 SER C 237 ? GLY C 258 ? SER C 237 GLY C 258 1 ? 22 
HELX_P HELX_P57 AG3 PRO C 276 ? SER C 278 ? PRO C 276 SER C 278 5 ? 3  
HELX_P HELX_P58 AG4 PHE C 279 ? THR C 288 ? PHE C 279 THR C 288 1 ? 10 
HELX_P HELX_P59 AG5 LEU C 297 ? LEU C 302 ? LEU C 297 LEU C 302 1 ? 6  
HELX_P HELX_P60 AG6 LEU C 319 ? GLY C 324 ? LEU C 319 GLY C 324 5 ? 6  
HELX_P HELX_P61 AG7 ASP C 329 ? SER C 343 ? ASP C 329 SER C 343 1 ? 15 
HELX_P HELX_P62 AG8 LYS C 344 ? TYR C 351 ? LYS C 344 TYR C 351 5 ? 8  
HELX_P HELX_P63 AG9 ASP C 352 ? TRP C 367 ? ASP C 352 TRP C 367 1 ? 16 
HELX_P HELX_P64 AH1 CYS C 380 ? VAL C 385 ? CYS C 380 VAL C 385 1 ? 6  
HELX_P HELX_P65 AH2 GLY C 386 ? GLY C 398 ? GLY C 386 GLY C 398 1 ? 13 
HELX_P HELX_P66 AH3 ASP C 410 ? PHE C 414 ? ASP C 410 PHE C 414 5 ? 5  
HELX_P HELX_P67 AH4 ASP C 415 ? LEU C 430 ? ASP C 415 LEU C 430 1 ? 16 
HELX_P HELX_P68 AH5 PHE D 6   ? LYS D 15  ? PHE D 6   LYS D 15  1 ? 10 
HELX_P HELX_P69 AH6 LYS D 15  ? GLY D 28  ? LYS D 15  GLY D 28  1 ? 14 
HELX_P HELX_P70 AH7 PRO D 40  ? ALA D 47  ? PRO D 40  ALA D 47  1 ? 8  
HELX_P HELX_P71 AH8 CYS D 73  ? LEU D 85  ? CYS D 73  LEU D 85  1 ? 13 
HELX_P HELX_P72 AH9 CYS D 100 ? VAL D 114 ? CYS D 100 VAL D 114 1 ? 15 
HELX_P HELX_P73 AI1 HIS D 133 ? GLY D 154 ? HIS D 133 GLY D 154 1 ? 22 
HELX_P HELX_P74 AI2 THR D 158 ? TYR D 182 ? THR D 158 TYR D 182 1 ? 25 
HELX_P HELX_P75 AI3 ARG D 183 ? ALA D 185 ? ARG D 183 ALA D 185 5 ? 3  
HELX_P HELX_P76 AI4 THR D 191 ? ALA D 202 ? THR D 191 ALA D 202 1 ? 12 
HELX_P HELX_P77 AI5 ASP D 206 ? LEU D 221 ? ASP D 206 LEU D 221 1 ? 16 
HELX_P HELX_P78 AI6 PRO D 222 ? ARG D 224 ? PRO D 222 ARG D 224 5 ? 3  
HELX_P HELX_P79 AI7 ASP D 243 ? GLU D 251 ? ASP D 243 GLU D 251 1 ? 9  
HELX_P HELX_P80 AI8 GLY D 265 ? TRP D 270 ? GLY D 265 TRP D 270 1 ? 6  
HELX_P HELX_P81 AI9 ASP D 278 ? ARG D 290 ? ASP D 278 ARG D 290 1 ? 13 
HELX_P HELX_P82 AJ1 CYS D 293 ? ASP D 297 ? CYS D 293 ASP D 297 5 ? 5  
HELX_P HELX_P83 AJ2 HIS D 301 ? TYR D 314 ? HIS D 301 TYR D 314 1 ? 14 
HELX_P HELX_P84 AJ3 CYS D 327 ? ASN D 344 ? CYS D 327 ASN D 344 1 ? 18 
HELX_P HELX_P85 AJ4 PRO D 358 ? SER D 374 ? PRO D 358 SER D 374 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A CYS 95  SG  ? ? ? 1_555 G SF4 . FE4 ? ? A CYS 95  A SF4 503 1_555 ? ? ? ? ? ? ? 2.313 ? ? 
metalc2  metalc ? ? A CYS 128 SG  ? ? ? 1_555 G SF4 . FE1 ? ? A CYS 128 A SF4 503 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc3  metalc ? ? A CYS 380 SG  ? ? ? 1_555 G SF4 . FE3 ? ? A CYS 380 A SF4 503 1_555 ? ? ? ? ? ? ? 2.282 ? ? 
metalc4  metalc ? ? G SF4 .   FE2 ? ? ? 1_555 P HOH . O   ? ? A SF4 503 A HOH 634 1_555 ? ? ? ? ? ? ? 1.854 ? ? 
metalc5  metalc ? ? B CYS 36  SG  ? ? ? 1_555 H BJ8 . FE5 ? ? B CYS 36  B BJ8 401 1_555 ? ? ? ? ? ? ? 2.277 ? ? 
metalc6  metalc ? ? B CYS 73  SG  ? ? ? 1_555 H BJ8 . FE3 ? ? B CYS 73  B BJ8 401 1_555 ? ? ? ? ? ? ? 2.177 ? ? 
metalc7  metalc ? ? B CYS 100 SG  ? ? ? 1_555 H BJ8 . FE4 ? ? B CYS 100 B BJ8 401 1_555 ? ? ? ? ? ? ? 2.291 ? ? 
metalc8  metalc ? ? B CYS 263 SG  ? ? ? 1_555 H BJ8 . FE7 ? ? B CYS 263 B BJ8 401 1_555 ? ? ? ? ? ? ? 2.286 ? ? 
metalc9  metalc ? ? B CYS 293 SG  ? ? ? 1_555 H BJ8 . FE6 ? ? B CYS 293 B BJ8 401 1_555 ? ? ? ? ? ? ? 2.361 ? ? 
metalc10 metalc ? ? B CYS 327 SG  ? ? ? 1_555 H BJ8 . FE2 ? ? B CYS 327 B BJ8 401 1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc11 metalc ? ? C CYS 95  SG  ? ? ? 1_555 M SF4 . FE4 ? ? C CYS 95  C SF4 504 1_555 ? ? ? ? ? ? ? 2.215 ? ? 
metalc12 metalc ? ? C CYS 128 SG  ? ? ? 1_555 M SF4 . FE1 ? ? C CYS 128 C SF4 504 1_555 ? ? ? ? ? ? ? 2.308 ? ? 
metalc13 metalc ? ? C CYS 380 SG  ? ? ? 1_555 M SF4 . FE3 ? ? C CYS 380 C SF4 504 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc14 metalc ? ? M SF4 .   FE2 ? ? ? 1_555 R DOD . O   ? ? C SF4 504 C DOD 661 1_555 ? ? ? ? ? ? ? 1.913 ? ? 
metalc15 metalc ? ? D CYS 36  SG  ? ? ? 1_555 N BJ8 . FE5 ? ? D CYS 36  D BJ8 401 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc16 metalc ? ? D CYS 73  SG  ? ? ? 1_555 N BJ8 . FE3 ? ? D CYS 73  D BJ8 401 1_555 ? ? ? ? ? ? ? 2.246 ? ? 
metalc17 metalc ? ? D CYS 100 SG  ? ? ? 1_555 N BJ8 . FE4 ? ? D CYS 100 D BJ8 401 1_555 ? ? ? ? ? ? ? 2.339 ? ? 
metalc18 metalc ? ? D CYS 263 SG  ? ? ? 1_555 N BJ8 . FE7 ? ? D CYS 263 D BJ8 401 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc19 metalc ? ? D CYS 293 SG  ? ? ? 1_555 N BJ8 . FE6 ? ? D CYS 293 D BJ8 401 1_555 ? ? ? ? ? ? ? 2.358 ? ? 
metalc20 metalc ? ? D CYS 327 SG  ? ? ? 1_555 N BJ8 . FE2 ? ? D CYS 327 D BJ8 401 1_555 ? ? ? ? ? ? ? 2.286 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   SG ? A CYS 95  ? A CYS 95  ? 1_555 FE4 ? G SF4 . ? A SF4 503 ? 1_555 S1 ? G SF4 . ? A SF4 503 ? 1_555 102.3 ? 
2   SG ? A CYS 95  ? A CYS 95  ? 1_555 FE4 ? G SF4 . ? A SF4 503 ? 1_555 S2 ? G SF4 . ? A SF4 503 ? 1_555 108.2 ? 
3   S1 ? G SF4 .   ? A SF4 503 ? 1_555 FE4 ? G SF4 . ? A SF4 503 ? 1_555 S2 ? G SF4 . ? A SF4 503 ? 1_555 109.4 ? 
4   SG ? A CYS 95  ? A CYS 95  ? 1_555 FE4 ? G SF4 . ? A SF4 503 ? 1_555 S3 ? G SF4 . ? A SF4 503 ? 1_555 127.4 ? 
5   S1 ? G SF4 .   ? A SF4 503 ? 1_555 FE4 ? G SF4 . ? A SF4 503 ? 1_555 S3 ? G SF4 . ? A SF4 503 ? 1_555 103.5 ? 
6   S2 ? G SF4 .   ? A SF4 503 ? 1_555 FE4 ? G SF4 . ? A SF4 503 ? 1_555 S3 ? G SF4 . ? A SF4 503 ? 1_555 105.2 ? 
7   SG ? A CYS 128 ? A CYS 128 ? 1_555 FE1 ? G SF4 . ? A SF4 503 ? 1_555 S2 ? G SF4 . ? A SF4 503 ? 1_555 113.8 ? 
8   SG ? A CYS 128 ? A CYS 128 ? 1_555 FE1 ? G SF4 . ? A SF4 503 ? 1_555 S3 ? G SF4 . ? A SF4 503 ? 1_555 122.2 ? 
9   S2 ? G SF4 .   ? A SF4 503 ? 1_555 FE1 ? G SF4 . ? A SF4 503 ? 1_555 S3 ? G SF4 . ? A SF4 503 ? 1_555 102.5 ? 
10  SG ? A CYS 128 ? A CYS 128 ? 1_555 FE1 ? G SF4 . ? A SF4 503 ? 1_555 S4 ? G SF4 . ? A SF4 503 ? 1_555 108.3 ? 
11  S2 ? G SF4 .   ? A SF4 503 ? 1_555 FE1 ? G SF4 . ? A SF4 503 ? 1_555 S4 ? G SF4 . ? A SF4 503 ? 1_555 102.5 ? 
12  S3 ? G SF4 .   ? A SF4 503 ? 1_555 FE1 ? G SF4 . ? A SF4 503 ? 1_555 S4 ? G SF4 . ? A SF4 503 ? 1_555 105.6 ? 
13  SG ? A CYS 380 ? A CYS 380 ? 1_555 FE3 ? G SF4 . ? A SF4 503 ? 1_555 S1 ? G SF4 . ? A SF4 503 ? 1_555 117.2 ? 
14  SG ? A CYS 380 ? A CYS 380 ? 1_555 FE3 ? G SF4 . ? A SF4 503 ? 1_555 S2 ? G SF4 . ? A SF4 503 ? 1_555 109.8 ? 
15  S1 ? G SF4 .   ? A SF4 503 ? 1_555 FE3 ? G SF4 . ? A SF4 503 ? 1_555 S2 ? G SF4 . ? A SF4 503 ? 1_555 108.7 ? 
16  SG ? A CYS 380 ? A CYS 380 ? 1_555 FE3 ? G SF4 . ? A SF4 503 ? 1_555 S4 ? G SF4 . ? A SF4 503 ? 1_555 114.1 ? 
17  S1 ? G SF4 .   ? A SF4 503 ? 1_555 FE3 ? G SF4 . ? A SF4 503 ? 1_555 S4 ? G SF4 . ? A SF4 503 ? 1_555 104.9 ? 
18  S2 ? G SF4 .   ? A SF4 503 ? 1_555 FE3 ? G SF4 . ? A SF4 503 ? 1_555 S4 ? G SF4 . ? A SF4 503 ? 1_555 100.7 ? 
19  O  ? P HOH .   ? A HOH 634 ? 1_555 FE2 ? G SF4 . ? A SF4 503 ? 1_555 S1 ? G SF4 . ? A SF4 503 ? 1_555 122.6 ? 
20  O  ? P HOH .   ? A HOH 634 ? 1_555 FE2 ? G SF4 . ? A SF4 503 ? 1_555 S3 ? G SF4 . ? A SF4 503 ? 1_555 111.4 ? 
21  S1 ? G SF4 .   ? A SF4 503 ? 1_555 FE2 ? G SF4 . ? A SF4 503 ? 1_555 S3 ? G SF4 . ? A SF4 503 ? 1_555 99.7  ? 
22  O  ? P HOH .   ? A HOH 634 ? 1_555 FE2 ? G SF4 . ? A SF4 503 ? 1_555 S4 ? G SF4 . ? A SF4 503 ? 1_555 106.7 ? 
23  S1 ? G SF4 .   ? A SF4 503 ? 1_555 FE2 ? G SF4 . ? A SF4 503 ? 1_555 S4 ? G SF4 . ? A SF4 503 ? 1_555 106.3 ? 
24  S3 ? G SF4 .   ? A SF4 503 ? 1_555 FE2 ? G SF4 . ? A SF4 503 ? 1_555 S4 ? G SF4 . ? A SF4 503 ? 1_555 109.5 ? 
25  SG ? B CYS 36  ? B CYS 36  ? 1_555 FE5 ? H BJ8 . ? B BJ8 401 ? 1_555 S6 ? H BJ8 . ? B BJ8 401 ? 1_555 118.2 ? 
26  SG ? B CYS 36  ? B CYS 36  ? 1_555 FE5 ? H BJ8 . ? B BJ8 401 ? 1_555 S7 ? H BJ8 . ? B BJ8 401 ? 1_555 119.6 ? 
27  S6 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE5 ? H BJ8 . ? B BJ8 401 ? 1_555 S7 ? H BJ8 . ? B BJ8 401 ? 1_555 103.7 ? 
28  SG ? B CYS 36  ? B CYS 36  ? 1_555 FE5 ? H BJ8 . ? B BJ8 401 ? 1_555 S8 ? H BJ8 . ? B BJ8 401 ? 1_555 106.9 ? 
29  S6 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE5 ? H BJ8 . ? B BJ8 401 ? 1_555 S8 ? H BJ8 . ? B BJ8 401 ? 1_555 103.1 ? 
30  S7 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE5 ? H BJ8 . ? B BJ8 401 ? 1_555 S8 ? H BJ8 . ? B BJ8 401 ? 1_555 103.2 ? 
31  SG ? B CYS 73  ? B CYS 73  ? 1_555 FE3 ? H BJ8 . ? B BJ8 401 ? 1_555 S1 ? H BJ8 . ? B BJ8 401 ? 1_555 110.9 ? 
32  SG ? B CYS 73  ? B CYS 73  ? 1_555 FE3 ? H BJ8 . ? B BJ8 401 ? 1_555 S2 ? H BJ8 . ? B BJ8 401 ? 1_555 116.4 ? 
33  S1 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE3 ? H BJ8 . ? B BJ8 401 ? 1_555 S2 ? H BJ8 . ? B BJ8 401 ? 1_555 106.8 ? 
34  SG ? B CYS 73  ? B CYS 73  ? 1_555 FE3 ? H BJ8 . ? B BJ8 401 ? 1_555 S4 ? H BJ8 . ? B BJ8 401 ? 1_555 114.1 ? 
35  S1 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE3 ? H BJ8 . ? B BJ8 401 ? 1_555 S4 ? H BJ8 . ? B BJ8 401 ? 1_555 104.0 ? 
36  S2 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE3 ? H BJ8 . ? B BJ8 401 ? 1_555 S4 ? H BJ8 . ? B BJ8 401 ? 1_555 103.6 ? 
37  SG ? B CYS 100 ? B CYS 100 ? 1_555 FE4 ? H BJ8 . ? B BJ8 401 ? 1_555 S1 ? H BJ8 . ? B BJ8 401 ? 1_555 106.9 ? 
38  SG ? B CYS 100 ? B CYS 100 ? 1_555 FE4 ? H BJ8 . ? B BJ8 401 ? 1_555 S2 ? H BJ8 . ? B BJ8 401 ? 1_555 116.6 ? 
39  S1 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE4 ? H BJ8 . ? B BJ8 401 ? 1_555 S2 ? H BJ8 . ? B BJ8 401 ? 1_555 106.9 ? 
40  SG ? B CYS 100 ? B CYS 100 ? 1_555 FE4 ? H BJ8 . ? B BJ8 401 ? 1_555 S3 ? H BJ8 . ? B BJ8 401 ? 1_555 112.7 ? 
41  S1 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE4 ? H BJ8 . ? B BJ8 401 ? 1_555 S3 ? H BJ8 . ? B BJ8 401 ? 1_555 104.0 ? 
42  S2 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE4 ? H BJ8 . ? B BJ8 401 ? 1_555 S3 ? H BJ8 . ? B BJ8 401 ? 1_555 108.7 ? 
43  SG ? B CYS 263 ? B CYS 263 ? 1_555 FE7 ? H BJ8 . ? B BJ8 401 ? 1_555 S5 ? H BJ8 . ? B BJ8 401 ? 1_555 116.5 ? 
44  SG ? B CYS 263 ? B CYS 263 ? 1_555 FE7 ? H BJ8 . ? B BJ8 401 ? 1_555 S6 ? H BJ8 . ? B BJ8 401 ? 1_555 108.9 ? 
45  S5 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE7 ? H BJ8 . ? B BJ8 401 ? 1_555 S6 ? H BJ8 . ? B BJ8 401 ? 1_555 108.9 ? 
46  SG ? B CYS 263 ? B CYS 263 ? 1_555 FE7 ? H BJ8 . ? B BJ8 401 ? 1_555 S8 ? H BJ8 . ? B BJ8 401 ? 1_555 113.0 ? 
47  S5 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE7 ? H BJ8 . ? B BJ8 401 ? 1_555 S8 ? H BJ8 . ? B BJ8 401 ? 1_555 103.5 ? 
48  S6 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE7 ? H BJ8 . ? B BJ8 401 ? 1_555 S8 ? H BJ8 . ? B BJ8 401 ? 1_555 105.4 ? 
49  SG ? B CYS 293 ? B CYS 293 ? 1_555 FE6 ? H BJ8 . ? B BJ8 401 ? 1_555 S5 ? H BJ8 . ? B BJ8 401 ? 1_555 120.5 ? 
50  SG ? B CYS 293 ? B CYS 293 ? 1_555 FE6 ? H BJ8 . ? B BJ8 401 ? 1_555 S7 ? H BJ8 . ? B BJ8 401 ? 1_555 116.1 ? 
51  S5 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE6 ? H BJ8 . ? B BJ8 401 ? 1_555 S7 ? H BJ8 . ? B BJ8 401 ? 1_555 107.6 ? 
52  SG ? B CYS 293 ? B CYS 293 ? 1_555 FE6 ? H BJ8 . ? B BJ8 401 ? 1_555 S8 ? H BJ8 . ? B BJ8 401 ? 1_555 105.1 ? 
53  S5 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE6 ? H BJ8 . ? B BJ8 401 ? 1_555 S8 ? H BJ8 . ? B BJ8 401 ? 1_555 102.0 ? 
54  S7 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE6 ? H BJ8 . ? B BJ8 401 ? 1_555 S8 ? H BJ8 . ? B BJ8 401 ? 1_555 103.1 ? 
55  SG ? B CYS 327 ? B CYS 327 ? 1_555 FE2 ? H BJ8 . ? B BJ8 401 ? 1_555 S1 ? H BJ8 . ? B BJ8 401 ? 1_555 109.6 ? 
56  SG ? B CYS 327 ? B CYS 327 ? 1_555 FE2 ? H BJ8 . ? B BJ8 401 ? 1_555 S3 ? H BJ8 . ? B BJ8 401 ? 1_555 110.7 ? 
57  S1 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE2 ? H BJ8 . ? B BJ8 401 ? 1_555 S3 ? H BJ8 . ? B BJ8 401 ? 1_555 105.2 ? 
58  SG ? B CYS 327 ? B CYS 327 ? 1_555 FE2 ? H BJ8 . ? B BJ8 401 ? 1_555 S4 ? H BJ8 . ? B BJ8 401 ? 1_555 115.7 ? 
59  S1 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE2 ? H BJ8 . ? B BJ8 401 ? 1_555 S4 ? H BJ8 . ? B BJ8 401 ? 1_555 106.5 ? 
60  S3 ? H BJ8 .   ? B BJ8 401 ? 1_555 FE2 ? H BJ8 . ? B BJ8 401 ? 1_555 S4 ? H BJ8 . ? B BJ8 401 ? 1_555 108.5 ? 
61  SG ? C CYS 95  ? C CYS 95  ? 1_555 FE4 ? M SF4 . ? C SF4 504 ? 1_555 S1 ? M SF4 . ? C SF4 504 ? 1_555 104.2 ? 
62  SG ? C CYS 95  ? C CYS 95  ? 1_555 FE4 ? M SF4 . ? C SF4 504 ? 1_555 S2 ? M SF4 . ? C SF4 504 ? 1_555 109.6 ? 
63  S1 ? M SF4 .   ? C SF4 504 ? 1_555 FE4 ? M SF4 . ? C SF4 504 ? 1_555 S2 ? M SF4 . ? C SF4 504 ? 1_555 111.0 ? 
64  SG ? C CYS 95  ? C CYS 95  ? 1_555 FE4 ? M SF4 . ? C SF4 504 ? 1_555 S3 ? M SF4 . ? C SF4 504 ? 1_555 126.6 ? 
65  S1 ? M SF4 .   ? C SF4 504 ? 1_555 FE4 ? M SF4 . ? C SF4 504 ? 1_555 S3 ? M SF4 . ? C SF4 504 ? 1_555 102.4 ? 
66  S2 ? M SF4 .   ? C SF4 504 ? 1_555 FE4 ? M SF4 . ? C SF4 504 ? 1_555 S3 ? M SF4 . ? C SF4 504 ? 1_555 102.6 ? 
67  SG ? C CYS 128 ? C CYS 128 ? 1_555 FE1 ? M SF4 . ? C SF4 504 ? 1_555 S2 ? M SF4 . ? C SF4 504 ? 1_555 112.5 ? 
68  SG ? C CYS 128 ? C CYS 128 ? 1_555 FE1 ? M SF4 . ? C SF4 504 ? 1_555 S3 ? M SF4 . ? C SF4 504 ? 1_555 122.5 ? 
69  S2 ? M SF4 .   ? C SF4 504 ? 1_555 FE1 ? M SF4 . ? C SF4 504 ? 1_555 S3 ? M SF4 . ? C SF4 504 ? 1_555 103.6 ? 
70  SG ? C CYS 128 ? C CYS 128 ? 1_555 FE1 ? M SF4 . ? C SF4 504 ? 1_555 S4 ? M SF4 . ? C SF4 504 ? 1_555 105.9 ? 
71  S2 ? M SF4 .   ? C SF4 504 ? 1_555 FE1 ? M SF4 . ? C SF4 504 ? 1_555 S4 ? M SF4 . ? C SF4 504 ? 1_555 103.7 ? 
72  S3 ? M SF4 .   ? C SF4 504 ? 1_555 FE1 ? M SF4 . ? C SF4 504 ? 1_555 S4 ? M SF4 . ? C SF4 504 ? 1_555 107.1 ? 
73  SG ? C CYS 380 ? C CYS 380 ? 1_555 FE3 ? M SF4 . ? C SF4 504 ? 1_555 S1 ? M SF4 . ? C SF4 504 ? 1_555 114.9 ? 
74  SG ? C CYS 380 ? C CYS 380 ? 1_555 FE3 ? M SF4 . ? C SF4 504 ? 1_555 S2 ? M SF4 . ? C SF4 504 ? 1_555 111.0 ? 
75  S1 ? M SF4 .   ? C SF4 504 ? 1_555 FE3 ? M SF4 . ? C SF4 504 ? 1_555 S2 ? M SF4 . ? C SF4 504 ? 1_555 110.5 ? 
76  SG ? C CYS 380 ? C CYS 380 ? 1_555 FE3 ? M SF4 . ? C SF4 504 ? 1_555 S4 ? M SF4 . ? C SF4 504 ? 1_555 113.3 ? 
77  S1 ? M SF4 .   ? C SF4 504 ? 1_555 FE3 ? M SF4 . ? C SF4 504 ? 1_555 S4 ? M SF4 . ? C SF4 504 ? 1_555 106.1 ? 
78  S2 ? M SF4 .   ? C SF4 504 ? 1_555 FE3 ? M SF4 . ? C SF4 504 ? 1_555 S4 ? M SF4 . ? C SF4 504 ? 1_555 99.9  ? 
79  O  ? R DOD .   ? C DOD 661 ? 1_555 FE2 ? M SF4 . ? C SF4 504 ? 1_555 S1 ? M SF4 . ? C SF4 504 ? 1_555 122.5 ? 
80  O  ? R DOD .   ? C DOD 661 ? 1_555 FE2 ? M SF4 . ? C SF4 504 ? 1_555 S3 ? M SF4 . ? C SF4 504 ? 1_555 112.5 ? 
81  S1 ? M SF4 .   ? C SF4 504 ? 1_555 FE2 ? M SF4 . ? C SF4 504 ? 1_555 S3 ? M SF4 . ? C SF4 504 ? 1_555 102.0 ? 
82  O  ? R DOD .   ? C DOD 661 ? 1_555 FE2 ? M SF4 . ? C SF4 504 ? 1_555 S4 ? M SF4 . ? C SF4 504 ? 1_555 101.6 ? 
83  S1 ? M SF4 .   ? C SF4 504 ? 1_555 FE2 ? M SF4 . ? C SF4 504 ? 1_555 S4 ? M SF4 . ? C SF4 504 ? 1_555 108.4 ? 
84  S3 ? M SF4 .   ? C SF4 504 ? 1_555 FE2 ? M SF4 . ? C SF4 504 ? 1_555 S4 ? M SF4 . ? C SF4 504 ? 1_555 109.5 ? 
85  SG ? D CYS 36  ? D CYS 36  ? 1_555 FE5 ? N BJ8 . ? D BJ8 401 ? 1_555 S6 ? N BJ8 . ? D BJ8 401 ? 1_555 117.6 ? 
86  SG ? D CYS 36  ? D CYS 36  ? 1_555 FE5 ? N BJ8 . ? D BJ8 401 ? 1_555 S7 ? N BJ8 . ? D BJ8 401 ? 1_555 119.4 ? 
87  S6 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE5 ? N BJ8 . ? D BJ8 401 ? 1_555 S7 ? N BJ8 . ? D BJ8 401 ? 1_555 104.9 ? 
88  SG ? D CYS 36  ? D CYS 36  ? 1_555 FE5 ? N BJ8 . ? D BJ8 401 ? 1_555 S8 ? N BJ8 . ? D BJ8 401 ? 1_555 105.2 ? 
89  S6 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE5 ? N BJ8 . ? D BJ8 401 ? 1_555 S8 ? N BJ8 . ? D BJ8 401 ? 1_555 104.2 ? 
90  S7 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE5 ? N BJ8 . ? D BJ8 401 ? 1_555 S8 ? N BJ8 . ? D BJ8 401 ? 1_555 103.5 ? 
91  SG ? D CYS 73  ? D CYS 73  ? 1_555 FE3 ? N BJ8 . ? D BJ8 401 ? 1_555 S1 ? N BJ8 . ? D BJ8 401 ? 1_555 108.0 ? 
92  SG ? D CYS 73  ? D CYS 73  ? 1_555 FE3 ? N BJ8 . ? D BJ8 401 ? 1_555 S2 ? N BJ8 . ? D BJ8 401 ? 1_555 116.9 ? 
93  S1 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE3 ? N BJ8 . ? D BJ8 401 ? 1_555 S2 ? N BJ8 . ? D BJ8 401 ? 1_555 106.9 ? 
94  SG ? D CYS 73  ? D CYS 73  ? 1_555 FE3 ? N BJ8 . ? D BJ8 401 ? 1_555 S4 ? N BJ8 . ? D BJ8 401 ? 1_555 113.0 ? 
95  S1 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE3 ? N BJ8 . ? D BJ8 401 ? 1_555 S4 ? N BJ8 . ? D BJ8 401 ? 1_555 107.6 ? 
96  S2 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE3 ? N BJ8 . ? D BJ8 401 ? 1_555 S4 ? N BJ8 . ? D BJ8 401 ? 1_555 103.9 ? 
97  SG ? D CYS 100 ? D CYS 100 ? 1_555 FE4 ? N BJ8 . ? D BJ8 401 ? 1_555 S1 ? N BJ8 . ? D BJ8 401 ? 1_555 106.5 ? 
98  SG ? D CYS 100 ? D CYS 100 ? 1_555 FE4 ? N BJ8 . ? D BJ8 401 ? 1_555 S2 ? N BJ8 . ? D BJ8 401 ? 1_555 114.3 ? 
99  S1 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE4 ? N BJ8 . ? D BJ8 401 ? 1_555 S2 ? N BJ8 . ? D BJ8 401 ? 1_555 106.7 ? 
100 SG ? D CYS 100 ? D CYS 100 ? 1_555 FE4 ? N BJ8 . ? D BJ8 401 ? 1_555 S3 ? N BJ8 . ? D BJ8 401 ? 1_555 114.3 ? 
101 S1 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE4 ? N BJ8 . ? D BJ8 401 ? 1_555 S3 ? N BJ8 . ? D BJ8 401 ? 1_555 106.1 ? 
102 S2 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE4 ? N BJ8 . ? D BJ8 401 ? 1_555 S3 ? N BJ8 . ? D BJ8 401 ? 1_555 108.4 ? 
103 SG ? D CYS 263 ? D CYS 263 ? 1_555 FE7 ? N BJ8 . ? D BJ8 401 ? 1_555 S5 ? N BJ8 . ? D BJ8 401 ? 1_555 118.7 ? 
104 SG ? D CYS 263 ? D CYS 263 ? 1_555 FE7 ? N BJ8 . ? D BJ8 401 ? 1_555 S6 ? N BJ8 . ? D BJ8 401 ? 1_555 106.1 ? 
105 S5 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE7 ? N BJ8 . ? D BJ8 401 ? 1_555 S6 ? N BJ8 . ? D BJ8 401 ? 1_555 109.5 ? 
106 SG ? D CYS 263 ? D CYS 263 ? 1_555 FE7 ? N BJ8 . ? D BJ8 401 ? 1_555 S8 ? N BJ8 . ? D BJ8 401 ? 1_555 113.4 ? 
107 S5 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE7 ? N BJ8 . ? D BJ8 401 ? 1_555 S8 ? N BJ8 . ? D BJ8 401 ? 1_555 104.1 ? 
108 S6 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE7 ? N BJ8 . ? D BJ8 401 ? 1_555 S8 ? N BJ8 . ? D BJ8 401 ? 1_555 104.2 ? 
109 SG ? D CYS 293 ? D CYS 293 ? 1_555 FE6 ? N BJ8 . ? D BJ8 401 ? 1_555 S5 ? N BJ8 . ? D BJ8 401 ? 1_555 120.8 ? 
110 SG ? D CYS 293 ? D CYS 293 ? 1_555 FE6 ? N BJ8 . ? D BJ8 401 ? 1_555 S7 ? N BJ8 . ? D BJ8 401 ? 1_555 114.7 ? 
111 S5 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE6 ? N BJ8 . ? D BJ8 401 ? 1_555 S7 ? N BJ8 . ? D BJ8 401 ? 1_555 107.4 ? 
112 SG ? D CYS 293 ? D CYS 293 ? 1_555 FE6 ? N BJ8 . ? D BJ8 401 ? 1_555 S8 ? N BJ8 . ? D BJ8 401 ? 1_555 104.3 ? 
113 S5 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE6 ? N BJ8 . ? D BJ8 401 ? 1_555 S8 ? N BJ8 . ? D BJ8 401 ? 1_555 104.8 ? 
114 S7 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE6 ? N BJ8 . ? D BJ8 401 ? 1_555 S8 ? N BJ8 . ? D BJ8 401 ? 1_555 102.8 ? 
115 SG ? D CYS 327 ? D CYS 327 ? 1_555 FE2 ? N BJ8 . ? D BJ8 401 ? 1_555 S1 ? N BJ8 . ? D BJ8 401 ? 1_555 112.0 ? 
116 SG ? D CYS 327 ? D CYS 327 ? 1_555 FE2 ? N BJ8 . ? D BJ8 401 ? 1_555 S3 ? N BJ8 . ? D BJ8 401 ? 1_555 111.4 ? 
117 S1 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE2 ? N BJ8 . ? D BJ8 401 ? 1_555 S3 ? N BJ8 . ? D BJ8 401 ? 1_555 106.8 ? 
118 SG ? D CYS 327 ? D CYS 327 ? 1_555 FE2 ? N BJ8 . ? D BJ8 401 ? 1_555 S4 ? N BJ8 . ? D BJ8 401 ? 1_555 116.0 ? 
119 S1 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE2 ? N BJ8 . ? D BJ8 401 ? 1_555 S4 ? N BJ8 . ? D BJ8 401 ? 1_555 105.2 ? 
120 S3 ? N BJ8 .   ? D BJ8 401 ? 1_555 FE2 ? N BJ8 . ? D BJ8 401 ? 1_555 S4 ? N BJ8 . ? D BJ8 401 ? 1_555 104.6 ? 
# 
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 LYS 215 A . ? LYS 215 A PRO 216 A ? PRO 216 A 1 -1.71 
2 TYR 298 B . ? TYR 298 B PRO 299 B ? PRO 299 B 1 0.03  
3 LYS 215 C . ? LYS 215 C PRO 216 C ? PRO 216 C 1 -2.62 
4 TYR 298 D . ? TYR 298 D PRO 299 D ? PRO 299 D 1 -1.96 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 2 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA8 1 2 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? parallel      
AA9 3 4 ? parallel      
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? 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 VAL A 59  ? THR A 63  ? VAL A 59  THR A 63  
AA1 2 ILE A 39  ? GLY A 43  ? ILE A 39  GLY A 43  
AA1 3 PHE A 121 ? GLN A 126 ? PHE A 121 GLN A 126 
AA1 4 GLU A 146 ? ASP A 150 ? GLU A 146 ASP A 150 
AA2 1 ALA A 291 ? SER A 296 ? ALA A 291 SER A 296 
AA2 2 ILE A 267 ? THR A 271 ? ILE A 267 THR A 271 
AA2 3 GLY A 371 ? ASN A 377 ? GLY A 371 ASN A 377 
AA2 4 VAL A 401 ? GLY A 406 ? VAL A 401 GLY A 406 
AA3 1 TRP A 306 ? ASP A 308 ? TRP A 306 ASP A 308 
AA3 2 TRP A 314 ? GLY A 316 ? TRP A 314 GLY A 316 
AA4 1 LEU B 50  ? ARG B 53  ? LEU B 50  ARG B 53  
AA4 2 VAL B 31  ? MET B 35  ? VAL B 31  MET B 35  
AA4 3 GLY B 93  ? THR B 97  ? GLY B 93  THR B 97  
AA4 4 TRP B 119 ? VAL B 123 ? TRP B 119 VAL B 123 
AA5 1 ALA B 255 ? ASP B 261 ? ALA B 255 ASP B 261 
AA5 2 ALA B 232 ? ILE B 237 ? ALA B 232 ILE B 237 
AA5 3 GLY B 318 ? GLN B 324 ? GLY B 318 GLN B 324 
AA5 4 THR B 348 ? PHE B 353 ? THR B 348 PHE B 353 
AA6 1 VAL C 59  ? THR C 63  ? VAL C 59  THR C 63  
AA6 2 ILE C 39  ? GLY C 43  ? ILE C 39  GLY C 43  
AA6 3 PHE C 121 ? GLN C 126 ? PHE C 121 GLN C 126 
AA6 4 GLU C 146 ? ASP C 150 ? GLU C 146 ASP C 150 
AA7 1 ALA C 291 ? SER C 296 ? ALA C 291 SER C 296 
AA7 2 ILE C 267 ? THR C 271 ? ILE C 267 THR C 271 
AA7 3 GLY C 371 ? ASN C 377 ? GLY C 371 ASN C 377 
AA7 4 VAL C 401 ? GLY C 406 ? VAL C 401 GLY C 406 
AA8 1 TRP C 306 ? ASP C 308 ? TRP C 306 ASP C 308 
AA8 2 TRP C 314 ? GLY C 316 ? TRP C 314 GLY C 316 
AA9 1 LEU D 50  ? ARG D 53  ? LEU D 50  ARG D 53  
AA9 2 VAL D 31  ? MET D 35  ? VAL D 31  MET D 35  
AA9 3 GLY D 93  ? THR D 97  ? GLY D 93  THR D 97  
AA9 4 TRP D 119 ? VAL D 123 ? TRP D 119 VAL D 123 
AB1 1 ALA D 255 ? ASP D 261 ? ALA D 255 ASP D 261 
AB1 2 ALA D 232 ? ILE D 237 ? ALA D 232 ILE D 237 
AB1 3 GLY D 318 ? GLN D 324 ? GLY D 318 GLN D 324 
AB1 4 THR D 348 ? PHE D 353 ? THR D 348 PHE D 353 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O TYR A 60  ? O TYR A 60  N ILE A 39  ? N ILE A 39  
AA1 2 3 N SER A 42  ? N SER A 42  O PHE A 123 ? O PHE A 123 
AA1 3 4 N GLN A 126 ? N GLN A 126 O LEU A 149 ? O LEU A 149 
AA2 1 2 O VAL A 292 ? O VAL A 292 N LEU A 269 ? N LEU A 269 
AA2 2 3 N MET A 270 ? N MET A 270 O MET A 373 ? O MET A 373 
AA2 3 4 N LEU A 374 ? N LEU A 374 O MET A 402 ? O MET A 402 
AA3 1 2 N GLU A 307 ? N GLU A 307 O GLY A 315 ? O GLY A 315 
AA4 1 2 O VAL B 52  ? O VAL B 52  N VAL B 32  ? N VAL B 32  
AA4 2 3 N ALA B 33  ? N ALA B 33  O GLY B 93  ? O GLY B 93  
AA4 3 4 N LEU B 96  ? N LEU B 96  O VAL B 123 ? O VAL B 123 
AA5 1 2 O THR B 256 ? O THR B 256 N PHE B 234 ? N PHE B 234 
AA5 2 3 N MET B 235 ? N MET B 235 O ILE B 320 ? O ILE B 320 
AA5 3 4 N GLN B 323 ? N GLN B 323 O LEU B 351 ? O LEU B 351 
AA6 1 2 O TYR C 60  ? O TYR C 60  N ILE C 39  ? N ILE C 39  
AA6 2 3 N SER C 42  ? N SER C 42  O PHE C 123 ? O PHE C 123 
AA6 3 4 N GLN C 126 ? N GLN C 126 O LEU C 149 ? O LEU C 149 
AA7 1 2 O VAL C 292 ? O VAL C 292 N LEU C 269 ? N LEU C 269 
AA7 2 3 N MET C 270 ? N MET C 270 O MET C 373 ? O MET C 373 
AA7 3 4 N LEU C 374 ? N LEU C 374 O MET C 402 ? O MET C 402 
AA8 1 2 N GLU C 307 ? N GLU C 307 O GLY C 315 ? O GLY C 315 
AA9 1 2 O VAL D 52  ? O VAL D 52  N VAL D 32  ? N VAL D 32  
AA9 2 3 N ALA D 33  ? N ALA D 33  O GLY D 93  ? O GLY D 93  
AA9 3 4 N LEU D 96  ? N LEU D 96  O VAL D 123 ? O VAL D 123 
AB1 1 2 O THR D 256 ? O THR D 256 N PHE D 234 ? N PHE D 234 
AB1 2 3 N ILE D 237 ? N ILE D 237 O LEU D 322 ? O LEU D 322 
AB1 3 4 N PHE D 321 ? N PHE D 321 O LEU D 349 ? O LEU D 349 
# 
_pdbx_entry_details.entry_id                   8S2R 
_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   N 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLN 
_pdbx_validate_rmsd_bond.auth_seq_id_1             274 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            N 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_2             275 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.484 
_pdbx_validate_rmsd_bond.bond_target_value         1.338 
_pdbx_validate_rmsd_bond.bond_deviation            0.146 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.019 
_pdbx_validate_rmsd_bond.linker_flag               Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C  A GLN 274 ? ? N  A PRO 275 ? ? CA A PRO 275 ? ? 129.13 119.30 9.83 1.50 Y 
2 1 CA B CYS 76  ? ? CB B CYS 76  ? ? SG B CYS 76  ? ? 121.42 114.20 7.22 1.10 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU A 11  ? ? -172.11 136.91  
2  1 ASP A 58  ? ? -109.73 45.46   
3  1 CYS A 95  ? ? -38.43  124.26  
4  1 ILE A 127 ? ? -138.82 -38.43  
5  1 SER A 234 ? ? -156.27 79.55   
6  1 ASP A 272 ? ? -126.68 -114.68 
7  1 CYS B 36  ? ? 65.31   143.92  
8  1 SER B 99  ? A -156.13 -118.28 
9  1 SER B 99  ? B -152.58 -119.40 
10 1 PHE B 204 ? ? -151.90 20.74   
11 1 SER B 239 ? ? -85.96  -77.78  
12 1 GLU B 276 ? ? -172.94 134.31  
13 1 ASP B 297 ? ? -116.03 78.85   
14 1 CYS C 95  ? ? -36.71  120.49  
15 1 ILE C 127 ? ? -139.91 -40.88  
16 1 SER C 234 ? ? -153.30 79.00   
17 1 THR C 271 ? ? -107.94 -167.11 
18 1 ASP C 272 ? ? -133.42 -115.64 
19 1 CYS D 36  ? ? 62.76   139.17  
20 1 SER D 99  ? A -155.46 -119.84 
21 1 SER D 99  ? B -159.03 -113.17 
22 1 PHE D 204 ? ? -151.29 13.95   
23 1 SER D 239 ? ? -79.12  -83.54  
24 1 GLU D 276 ? ? -170.86 133.09  
25 1 ASP D 354 ? ? -104.36 -166.16 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     810 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   P 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 32.0108 -4.0374  -7.4706  0.2649 ? -0.0555 ? 0.0241  ? 0.2656 ? -0.0363 ? 0.1948 ? 1.4054 ? 
-1.2146 ? 1.1548  ? 3.3898 ? -2.0467 ? 3.8055 ? 0.0593  ? 0.2715  ? -0.1935 ? -0.6073 ? 0.1202  ? 0.1364  ? 0.4252  ? -0.2128 ? 
-0.1214 ? 
2  'X-RAY DIFFRACTION' ? refined 43.2278 -7.9742  11.2912  0.1897 ? 0.0016  ? 0.0237  ? 0.2087 ? -0.0127 ? 0.2133 ? 2.3075 ? 
-0.8729 ? -0.1188 ? 2.4739 ? 0.4187  ? 0.5550 ? -0.0152 ? 0.0365  ? -0.1980 ? -0.1801 ? 0.0197  ? -0.1261 ? -0.0565 ? 0.0922  ? 
-0.0339 ? 
3  'X-RAY DIFFRACTION' ? refined 28.6063 -10.8270 15.8565  0.1816 ? 0.0092  ? -0.0120 ? 0.1856 ? -0.0042 ? 0.2071 ? 0.5042 ? 
0.5572  ? 0.0551  ? 1.6276 ? 0.2226  ? 0.5866 ? 0.0206  ? 0.0217  ? -0.0731 ? 0.0033  ? -0.0086 ? -0.0277 ? 0.0507  ? 0.0038  ? 
0.0013  ? 
4  'X-RAY DIFFRACTION' ? refined 44.6215 1.7583   23.3156  0.1689 ? -0.0081 ? 0.0031  ? 0.2454 ? 0.0041  ? 0.2212 ? 1.2875 ? 
-1.3195 ? -0.6638 ? 1.9715 ? 0.9278  ? 1.1910 ? -0.0447 ? -0.1129 ? 0.0835  ? 0.0485  ? 0.0552  ? -0.2428 ? 0.0103  ? 0.2078  ? 
-0.0315 ? 
5  'X-RAY DIFFRACTION' ? refined 39.8745 8.0906   4.3625   0.2291 ? -0.0171 ? 0.0307  ? 0.2110 ? 0.0071  ? 0.2094 ? 2.9264 ? 
-1.0839 ? 2.1416  ? 0.8642 ? -0.7214 ? 2.0271 ? -0.0685 ? 0.1433  ? 0.0463  ? -0.0269 ? 0.0322  ? -0.0903 ? -0.0853 ? 0.1287  ? 
0.0886  ? 
6  'X-RAY DIFFRACTION' ? refined 28.2103 2.7101   -2.0339  0.2820 ? 0.0109  ? 0.0389  ? 0.2636 ? 0.0074  ? 0.2411 ? 1.4749 ? 
-0.9529 ? 1.7077  ? 1.4326 ? -1.6125 ? 2.2903 ? -0.0134 ? -0.1127 ? -0.1338 ? -0.1298 ? 0.1592  ? 0.1124  ? -0.0443 ? -0.2228 ? 
-0.1123 ? 
7  'X-RAY DIFFRACTION' ? refined 27.8058 6.6333   -6.7881  0.3378 ? -0.0232 ? 0.0235  ? 0.2643 ? 0.0032  ? 0.1957 ? 1.3731 ? 
-0.5761 ? 0.3056  ? 0.6448 ? 0.0508  ? 0.5851 ? 0.0396  ? 0.2088  ? 0.0678  ? -0.1536 ? -0.0726 ? -0.0368 ? -0.0806 ? 0.0601  ? 
0.0466  ? 
8  'X-RAY DIFFRACTION' ? refined 30.2790 9.3724   5.2408   0.2004 ? -0.0026 ? 0.0315  ? 0.1749 ? 0.0047  ? 0.1762 ? 0.9045 ? 
-0.6902 ? 0.4535  ? 0.7248 ? -0.2870 ? 1.6950 ? 0.0009  ? 0.1278  ? 0.0052  ? -0.0861 ? -0.0518 ? -0.0650 ? -0.0349 ? -0.0510 ? 
0.0609  ? 
9  'X-RAY DIFFRACTION' ? refined 16.2765 9.6647   10.4581  0.2065 ? 0.0100  ? -0.0073 ? 0.2210 ? -0.0154 ? 0.2373 ? 0.5444 ? 
0.0325  ? 0.2326  ? 0.5061 ? 0.0345  ? 0.8256 ? -0.0377 ? 0.0069  ? 0.0846  ? -0.0450 ? -0.0108 ? 0.0750  ? 0.0156  ? -0.0478 ? 
0.0440  ? 
10 'X-RAY DIFFRACTION' ? refined 5.3912  3.5823   -0.2184  0.1719 ? -0.0148 ? -0.0262 ? 0.2400 ? -0.0376 ? 0.2197 ? 2.0124 ? 
-0.7274 ? 0.6345  ? 1.7626 ? -1.0881 ? 1.4863 ? 0.0128  ? 0.1193  ? -0.0038 ? -0.1095 ? 0.0943  ? 0.2126  ? 0.0533  ? -0.1089 ? 
-0.1129 ? 
11 'X-RAY DIFFRACTION' ? refined 2.5991  8.3629   49.1997  0.2283 ? 0.0295  ? 0.0397  ? 0.4069 ? -0.0234 ? 0.2570 ? 1.1534 ? 
-0.9367 ? 0.5160  ? 2.9703 ? -1.3769 ? 2.2868 ? -0.0679 ? -0.1569 ? -0.0013 ? 0.2666  ? 0.2633  ? 0.5976  ? 0.0154  ? -0.5336 ? 
-0.1848 ? 
12 'X-RAY DIFFRACTION' ? refined 11.8718 9.8163   37.9305  0.2504 ? 0.0230  ? 0.0188  ? 0.2462 ? -0.0194 ? 0.2437 ? 1.3027 ? 
0.5947  ? 0.5116  ? 0.8692 ? -0.0431 ? 1.1469 ? -0.0618 ? -0.0195 ? 0.1242  ? -0.0394 ? -0.0541 ? 0.2377  ? -0.0312 ? -0.1682 ? 
0.0925  ? 
13 'X-RAY DIFFRACTION' ? refined 13.4772 8.3555   28.4851  0.2143 ? 0.0200  ? 0.0078  ? 0.2265 ? -0.0121 ? 0.2294 ? 0.5969 ? 
-0.2280 ? 0.1145  ? 0.5138 ? -0.0120 ? 0.7150 ? -0.0221 ? 0.0067  ? -0.0222 ? -0.0086 ? -0.0094 ? 0.1214  ? -0.0209 ? -0.1499 ? 
0.0260  ? 
14 'X-RAY DIFFRACTION' ? refined 27.6713 18.7714  38.5000  0.2539 ? -0.0063 ? -0.0129 ? 0.2043 ? -0.0077 ? 0.2047 ? 1.7171 ? 
-0.4381 ? 0.4324  ? 1.7403 ? -0.4373 ? 1.1326 ? 0.0003  ? -0.0136 ? 0.2421  ? 0.2156  ? -0.0572 ? -0.1098 ? -0.2919 ? -0.0000 ? 
0.0062  ? 
15 'X-RAY DIFFRACTION' ? refined 16.1119 0.4303   51.7472  0.2852 ? -0.0052 ? 0.0353  ? 0.2763 ? -0.0221 ? 0.1699 ? 1.0949 ? 
0.1609  ? -0.2637 ? 1.6574 ? -0.3588 ? 1.2094 ? -0.0233 ? -0.1077 ? -0.0341 ? 0.2420  ? 0.0264  ? 0.1034  ? 0.1159  ? -0.1439 ? 
0.0135  ? 
16 'X-RAY DIFFRACTION' ? refined 10.2148 -4.7627  53.3181  0.2994 ? 0.0056  ? 0.0498  ? 0.3302 ? 0.0144  ? 0.2066 ? 0.7003 ? 
-0.3012 ? -0.1093 ? 1.5843 ? 1.2324  ? 1.8753 ? -0.0564 ? -0.2347 ? -0.0518 ? 0.2447  ? 0.0184  ? 0.0880  ? 0.0104  ? -0.2705 ? 
0.0190  ? 
17 'X-RAY DIFFRACTION' ? refined 20.5013 -8.4093  39.3632  0.2680 ? -0.0030 ? 0.0120  ? 0.2155 ? 0.0161  ? 0.2085 ? 0.5368 ? 
0.2505  ? 0.3624  ? 1.2274 ? 0.6652  ? 0.7723 ? 0.0133  ? -0.0446 ? -0.1117 ? 0.1225  ? -0.0057 ? 0.0924  ? 0.1572  ? -0.0757 ? 
0.0005  ? 
18 'X-RAY DIFFRACTION' ? refined 6.1528  -20.0734 36.1382  0.3364 ? -0.0850 ? 0.0192  ? 0.3114 ? 0.0109  ? 0.3793 ? 3.2652 ? 
0.7963  ? -0.3405 ? 1.2870 ? 0.1387  ? 2.5164 ? 0.0899  ? 0.0418  ? -0.0164 ? -0.0770 ? -0.0081 ? 0.4585  ? 0.5501  ? -0.4661 ? 
-0.1135 ? 
19 'X-RAY DIFFRACTION' ? refined 21.7399 -46.5327 40.5766  0.3751 ? 0.0317  ? 0.0420  ? 0.3351 ? -0.0140 ? 0.2276 ? 3.1200 ? 
2.4932  ? -1.9532 ? 3.3614 ? -1.6590 ? 1.8424 ? 0.0872  ? -0.1555 ? 0.2717  ? 0.5967  ? 0.0967  ? 0.3004  ? -0.1904 ? -0.2649 ? 
-0.1713 ? 
20 'X-RAY DIFFRACTION' ? refined 30.2882 -40.3217 20.1928  0.2021 ? 0.0006  ? -0.0104 ? 0.1804 ? -0.0053 ? 0.2125 ? 0.5515 ? 
-0.2905 ? -0.1141 ? 1.1409 ? -0.1377 ? 0.6961 ? -0.0164 ? -0.0465 ? 0.0629  ? 0.0523  ? 0.0158  ? -0.0165 ? -0.0291 ? -0.0450 ? 
0.0153  ? 
21 'X-RAY DIFFRACTION' ? refined 45.7466 -52.5186 18.1835  0.2152 ? 0.0247  ? -0.0063 ? 0.2419 ? 0.0040  ? 0.2212 ? 0.8408 ? 
0.8189  ? 0.3791  ? 1.8162 ? 0.9601  ? 1.4761 ? 0.0039  ? -0.0332 ? -0.0407 ? 0.0306  ? -0.0393 ? -0.0824 ? -0.0411 ? 0.1021  ? 
-0.0333 ? 
22 'X-RAY DIFFRACTION' ? refined 26.9134 -56.4700 33.6563  0.3501 ? 0.0041  ? 0.0196  ? 0.2101 ? 0.0100  ? 0.1807 ? 1.9202 ? 
0.5145  ? -0.8782 ? 1.1039 ? -0.1971 ? 0.9828 ? -0.1105 ? -0.0622 ? 0.0484  ? 0.2055  ? 0.0815  ? 0.1447  ? 0.1184  ? -0.1319 ? 
0.0152  ? 
23 'X-RAY DIFFRACTION' ? refined 17.6661 -57.4080 38.2009  0.4493 ? 0.0178  ? 0.0752  ? 0.2736 ? 0.0172  ? 0.2306 ? 1.7604 ? 
0.4496  ? -0.0915 ? 0.6221 ? 0.3716  ? 0.7289 ? -0.0319 ? -0.2401 ? -0.0733 ? 0.1572  ? -0.0229 ? 0.0885  ? 0.0615  ? -0.1022 ? 
0.0469  ? 
24 'X-RAY DIFFRACTION' ? refined 12.4026 -54.2258 29.6725  0.3079 ? 0.0386  ? 0.0618  ? 0.2833 ? -0.0092 ? 0.3071 ? 1.3738 ? 
0.2962  ? -0.1281 ? 2.2143 ? 0.0876  ? 1.6854 ? -0.0072 ? -0.0087 ? 0.2237  ? 0.2422  ? -0.0568 ? 0.4424  ? -0.1735 ? -0.4379 ? 
0.0403  ? 
25 'X-RAY DIFFRACTION' ? refined 37.0682 -65.7123 27.2204  0.3032 ? 0.0300  ? -0.0066 ? 0.2328 ? 0.0299  ? 0.2893 ? 1.7509 ? 
1.3157  ? -1.1341 ? 1.4365 ? -0.5437 ? 0.9352 ? -0.0008 ? -0.1808 ? -0.4324 ? 0.1862  ? -0.0775 ? -0.2401 ? 0.1259  ? 0.1033  ? 
0.0562  ? 
26 'X-RAY DIFFRACTION' ? refined 14.9466 -60.2452 17.8089  0.2504 ? -0.0291 ? 0.0107  ? 0.2590 ? -0.0115 ? 0.2602 ? 1.0472 ? 
0.2050  ? -0.3523 ? 0.6289 ? -0.1092 ? 0.9646 ? -0.0288 ? 0.0976  ? -0.0614 ? 0.0576  ? 0.0188  ? 0.1073  ? 0.0681  ? -0.2007 ? 
0.0248  ? 
27 'X-RAY DIFFRACTION' ? refined 1.7781  -50.3664 22.3169  0.3357 ? -0.0342 ? 0.0897  ? 0.4974 ? -0.0544 ? 0.5229 ? 1.6122 ? 
0.7047  ? 0.1283  ? 3.5632 ? -0.4511 ? 0.4568 ? 0.0252  ? -0.1755 ? 0.2361  ? 0.3779  ? 0.0021  ? 0.9890  ? -0.1144 ? -0.5208 ? 
-0.0802 ? 
28 'X-RAY DIFFRACTION' ? refined 19.0990 -58.7215 -23.3542 0.3374 ? -0.0318 ? -0.0715 ? 0.5247 ? -0.0366 ? 0.2606 ? 2.0439 ? 
1.0198  ? -1.1111 ? 4.2627 ? -1.0933 ? 2.0813 ? -0.0998 ? 0.4579  ? 0.0152  ? -0.8294 ? 0.2567  ? 0.4768  ? 0.2110  ? -0.7007 ? 
-0.1525 ? 
29 'X-RAY DIFFRACTION' ? refined 25.8342 -58.7752 -7.0822  0.2261 ? -0.0138 ? -0.0100 ? 0.2389 ? -0.0184 ? 0.2120 ? 0.4103 ? 
-0.1021 ? -0.1788 ? 0.6937 ? 0.0194  ? 0.8462 ? 0.0124  ? 0.1250  ? -0.0633 ? -0.0840 ? -0.0293 ? 0.0924  ? 0.0235  ? -0.1713 ? 
0.0134  ? 
30 'X-RAY DIFFRACTION' ? refined 27.2696 -45.0117 -23.5227 0.3885 ? 0.0263  ? -0.0043 ? 0.3671 ? 0.0360  ? 0.2317 ? 1.0911 ? 
-0.3640 ? -0.4173 ? 1.4003 ? 0.8059  ? 1.8175 ? 0.0688  ? 0.3902  ? 0.0546  ? -0.2095 ? -0.1116 ? 0.0364  ? -0.2138 ? -0.3358 ? 
0.0320  ? 
31 'X-RAY DIFFRACTION' ? refined 31.3316 -43.9959 -8.3114  0.2787 ? 0.0090  ? -0.0017 ? 0.2466 ? 0.0178  ? 0.2324 ? 0.5269 ? 
-0.3128 ? -0.4685 ? 0.9876 ? 0.2108  ? 0.8719 ? 0.0762  ? 0.1336  ? 0.0871  ? -0.1696 ? -0.0248 ? 0.0241  ? -0.1616 ? -0.1385 ? 
-0.0449 ? 
32 'X-RAY DIFFRACTION' ? refined 20.8133 -31.8411 -5.9791  0.3868 ? 0.0878  ? 0.0072  ? 0.2893 ? 0.0178  ? 0.3342 ? 2.8438 ? 
-0.8166 ? 0.8319  ? 1.6885 ? -0.7784 ? 2.7093 ? 0.1418  ? 0.1437  ? 0.2576  ? -0.0919 ? 0.0555  ? 0.3780  ? -0.4182 ? -0.3804 ? 
-0.1552 ? 
# 
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  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 5 through 31 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 32 through 58 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 59 through 160 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 161 through 187 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 188 through 213 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 214 through 237 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 238 through 276 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 277 through 343 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 344 through 397 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 398 through 442 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 2 through 27 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 28 through 63 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 64 through 133 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 134 through 158 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 159 through 206 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 207 through 243 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 244 through 344 )
;
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 345 through 376 )
;
19 'X-RAY DIFFRACTION' 19 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 6 through 31 )
;
20 'X-RAY DIFFRACTION' 20 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 32 through 160 )
;
21 'X-RAY DIFFRACTION' 21 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 161 through 187 )
;
22 'X-RAY DIFFRACTION' 22 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 188 through 237 )
;
23 'X-RAY DIFFRACTION' 23 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 238 through 276 )
;
24 'X-RAY DIFFRACTION' 24 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 277 through 308 )
;
25 'X-RAY DIFFRACTION' 25 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 309 through 343 )
;
26 'X-RAY DIFFRACTION' 26 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 344 through 396 )
;
27 'X-RAY DIFFRACTION' 27 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 397 through 434 )
;
28 'X-RAY DIFFRACTION' 28 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 2 through 27 )
;
29 'X-RAY DIFFRACTION' 29 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 28 through 206 )
;
30 'X-RAY DIFFRACTION' 30 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 207 through 243 )
;
31 'X-RAY DIFFRACTION' 31 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 244 through 327 )
;
32 'X-RAY DIFFRACTION' 32 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 328 through 376 )
;
# 
_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                      D 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       656 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.57 
_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 MET 1   ? A MET 1   
2  1 Y 1 A ASN 2   ? A ASN 2   
3  1 Y 1 A ALA 3   ? A ALA 3   
4  1 Y 1 A MET 4   ? A MET 4   
5  1 Y 1 A PRO 443 ? A PRO 443 
6  1 Y 1 A GLN 444 ? A GLN 444 
7  1 Y 1 A PHE 445 ? A PHE 445 
8  1 Y 1 A GLU 446 ? A GLU 446 
9  1 Y 1 A LYS 447 ? A LYS 447 
10 1 Y 1 B MET 1   ? B MET 1   
11 1 Y 1 B GLU 377 ? B GLU 377 
12 1 Y 1 B LEU 378 ? B LEU 378 
13 1 Y 1 B PHE 379 ? B PHE 379 
14 1 Y 1 C MET 1   ? C MET 1   
15 1 Y 1 C ASN 2   ? C ASN 2   
16 1 Y 1 C ALA 3   ? C ALA 3   
17 1 Y 1 C MET 4   ? C MET 4   
18 1 Y 1 C ALA 5   ? C ALA 5   
19 1 Y 1 C GLN 435 ? C GLN 435 
20 1 Y 1 C ALA 436 ? C ALA 436 
21 1 Y 1 C ALA 437 ? C ALA 437 
22 1 Y 1 C SER 438 ? C SER 438 
23 1 Y 1 C ALA 439 ? C ALA 439 
24 1 Y 1 C TRP 440 ? C TRP 440 
25 1 Y 1 C SER 441 ? C SER 441 
26 1 Y 1 C HIS 442 ? C HIS 442 
27 1 Y 1 C PRO 443 ? C PRO 443 
28 1 Y 1 C GLN 444 ? C GLN 444 
29 1 Y 1 C PHE 445 ? C PHE 445 
30 1 Y 1 C GLU 446 ? C GLU 446 
31 1 Y 1 C LYS 447 ? C LYS 447 
32 1 Y 1 D MET 1   ? D MET 1   
33 1 Y 1 D GLU 377 ? D GLU 377 
34 1 Y 1 D LEU 378 ? D LEU 378 
35 1 Y 1 D PHE 379 ? D PHE 379 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BJ8 S1   S  N N 74  
BJ8 S2   S  N N 75  
BJ8 S3   S  N N 76  
BJ8 S4   S  N N 77  
BJ8 S5   S  N N 78  
BJ8 S6   S  N N 79  
BJ8 S7   S  N N 80  
BJ8 S8   S  N N 81  
BJ8 S9   S  N N 82  
BJ8 FE1  FE N N 83  
BJ8 FE2  FE N N 84  
BJ8 FE3  FE N N 85  
BJ8 FE4  FE N N 86  
BJ8 FE5  FE N N 87  
BJ8 FE6  FE N N 88  
BJ8 FE7  FE N N 89  
BJ8 FE8  FE N N 90  
BYC N1A  N  Y N 91  
BYC O1A  O  N N 92  
BYC P1A  P  N N 93  
BYC C1B  C  N N 94  
BYC C1D  C  N R 95  
BYC S1P  S  N N 96  
BYC C2A  C  Y N 97  
BYC O2A  O  N N 98  
BYC P2A  P  N N 99  
BYC C2B  C  Y N 100 
BYC C2D  C  N R 101 
BYC O2D  O  N N 102 
BYC C2P  C  N N 103 
BYC N3A  N  Y N 104 
BYC O3A  O  N N 105 
BYC C3B  C  Y N 106 
BYC C3D  C  N S 107 
BYC O3D  O  N N 108 
BYC P3D  P  N N 109 
BYC C3P  C  N N 110 
BYC C4A  C  Y N 111 
BYC O4A  O  N N 112 
BYC C4B  C  Y N 113 
BYC C4D  C  N R 114 
BYC O4D  O  N N 115 
BYC N4P  N  N N 116 
BYC O57  O  N N 117 
BYC O5A  O  N N 118 
BYC C5B  C  Y N 119 
BYC C5D  C  N N 120 
BYC O5D  O  N N 121 
BYC C5M  C  Y N 122 
BYC C5P  C  N N 123 
BYC O5P  O  N N 124 
BYC C6A  C  Y N 125 
BYC N6A  N  N N 126 
BYC O6A  O  N N 127 
BYC C6B  C  Y N 128 
BYC C6P  C  N N 129 
BYC N7A  N  Y N 130 
BYC O7A  O  N N 131 
BYC C7B  C  Y N 132 
BYC C7P  C  N N 133 
BYC C8A  C  Y N 134 
BYC O8A  O  N N 135 
BYC N8P  N  N N 136 
BYC N9A  N  Y N 137 
BYC O9A  O  N N 138 
BYC C9P  C  N N 139 
BYC O9P  O  N N 140 
BYC CAP  C  N R 141 
BYC OAP  O  N N 142 
BYC CBP  C  N N 143 
BYC CCP  C  N N 144 
BYC CDP  C  N N 145 
BYC CEP  C  N N 146 
BYC H1D  H  N N 147 
BYC H2A  H  N N 148 
BYC HO2A H  N N 149 
BYC H2D  H  N N 150 
BYC HO2D H  N N 151 
BYC H2P  H  N N 152 
BYC H2PA H  N N 153 
BYC H3B  H  N N 154 
BYC H3D  H  N N 155 
BYC H3P  H  N N 156 
BYC H3PA H  N N 157 
BYC HO4A H  N N 158 
BYC H4B  H  N N 159 
BYC H4D  H  N N 160 
BYC HN4P H  N N 161 
BYC H5B  H  N N 162 
BYC H5D  H  N N 163 
BYC H5DA H  N N 164 
BYC HN6A H  N N 165 
BYC HN6B H  N N 166 
BYC H6B  H  N N 167 
BYC H6P  H  N N 168 
BYC H6PA H  N N 169 
BYC HO7A H  N N 170 
BYC H7B  H  N N 171 
BYC H7P  H  N N 172 
BYC H7PA H  N N 173 
BYC H8A  H  N N 174 
BYC HN8P H  N N 175 
BYC HO9A H  N N 176 
BYC HAP  H  N N 177 
BYC HOAP H  N N 178 
BYC HCP  H  N N 179 
BYC HCPA H  N N 180 
BYC HDP  H  N N 181 
BYC HDPA H  N N 182 
BYC HDPB H  N N 183 
BYC HEP  H  N N 184 
BYC HEPA H  N N 185 
BYC HEPB H  N N 186 
CYS N    N  N N 187 
CYS CA   C  N R 188 
CYS C    C  N N 189 
CYS O    O  N N 190 
CYS CB   C  N N 191 
CYS SG   S  N N 192 
CYS OXT  O  N N 193 
CYS H    H  N N 194 
CYS H2   H  N N 195 
CYS HA   H  N N 196 
CYS HB2  H  N N 197 
CYS HB3  H  N N 198 
CYS HG   H  N N 199 
CYS HXT  H  N N 200 
DOD O    O  N N 201 
DOD D1   D  N N 202 
DOD D2   D  N N 203 
GLN N    N  N N 204 
GLN CA   C  N S 205 
GLN C    C  N N 206 
GLN O    O  N N 207 
GLN CB   C  N N 208 
GLN CG   C  N N 209 
GLN CD   C  N N 210 
GLN OE1  O  N N 211 
GLN NE2  N  N N 212 
GLN OXT  O  N N 213 
GLN H    H  N N 214 
GLN H2   H  N N 215 
GLN HA   H  N N 216 
GLN HB2  H  N N 217 
GLN HB3  H  N N 218 
GLN HG2  H  N N 219 
GLN HG3  H  N N 220 
GLN HE21 H  N N 221 
GLN HE22 H  N N 222 
GLN HXT  H  N N 223 
GLU N    N  N N 224 
GLU CA   C  N S 225 
GLU C    C  N N 226 
GLU O    O  N N 227 
GLU CB   C  N N 228 
GLU CG   C  N N 229 
GLU CD   C  N N 230 
GLU OE1  O  N N 231 
GLU OE2  O  N N 232 
GLU OXT  O  N N 233 
GLU H    H  N N 234 
GLU H2   H  N N 235 
GLU HA   H  N N 236 
GLU HB2  H  N N 237 
GLU HB3  H  N N 238 
GLU HG2  H  N N 239 
GLU HG3  H  N N 240 
GLU HE2  H  N N 241 
GLU HXT  H  N N 242 
GLY N    N  N N 243 
GLY CA   C  N N 244 
GLY C    C  N N 245 
GLY O    O  N N 246 
GLY OXT  O  N N 247 
GLY H    H  N N 248 
GLY H2   H  N N 249 
GLY HA2  H  N N 250 
GLY HA3  H  N N 251 
GLY HXT  H  N N 252 
GOL C1   C  N N 253 
GOL O1   O  N N 254 
GOL C2   C  N N 255 
GOL O2   O  N N 256 
GOL C3   C  N N 257 
GOL O3   O  N N 258 
GOL H11  H  N N 259 
GOL H12  H  N N 260 
GOL HO1  H  N N 261 
GOL H2   H  N N 262 
GOL HO2  H  N N 263 
GOL H31  H  N N 264 
GOL H32  H  N N 265 
GOL HO3  H  N N 266 
HIS N    N  N N 267 
HIS CA   C  N S 268 
HIS C    C  N N 269 
HIS O    O  N N 270 
HIS CB   C  N N 271 
HIS CG   C  Y N 272 
HIS ND1  N  Y N 273 
HIS CD2  C  Y N 274 
HIS CE1  C  Y N 275 
HIS NE2  N  Y N 276 
HIS OXT  O  N N 277 
HIS H    H  N N 278 
HIS H2   H  N N 279 
HIS HA   H  N N 280 
HIS HB2  H  N N 281 
HIS HB3  H  N N 282 
HIS HD1  H  N N 283 
HIS HD2  H  N N 284 
HIS HE1  H  N N 285 
HIS HE2  H  N N 286 
HIS HXT  H  N N 287 
HOH O    O  N N 288 
HOH H1   H  N N 289 
HOH H2   H  N N 290 
ILE N    N  N N 291 
ILE CA   C  N S 292 
ILE C    C  N N 293 
ILE O    O  N N 294 
ILE CB   C  N S 295 
ILE CG1  C  N N 296 
ILE CG2  C  N N 297 
ILE CD1  C  N N 298 
ILE OXT  O  N N 299 
ILE H    H  N N 300 
ILE H2   H  N N 301 
ILE HA   H  N N 302 
ILE HB   H  N N 303 
ILE HG12 H  N N 304 
ILE HG13 H  N N 305 
ILE HG21 H  N N 306 
ILE HG22 H  N N 307 
ILE HG23 H  N N 308 
ILE HD11 H  N N 309 
ILE HD12 H  N N 310 
ILE HD13 H  N N 311 
ILE HXT  H  N N 312 
LEU N    N  N N 313 
LEU CA   C  N S 314 
LEU C    C  N N 315 
LEU O    O  N N 316 
LEU CB   C  N N 317 
LEU CG   C  N N 318 
LEU CD1  C  N N 319 
LEU CD2  C  N N 320 
LEU OXT  O  N N 321 
LEU H    H  N N 322 
LEU H2   H  N N 323 
LEU HA   H  N N 324 
LEU HB2  H  N N 325 
LEU HB3  H  N N 326 
LEU HG   H  N N 327 
LEU HD11 H  N N 328 
LEU HD12 H  N N 329 
LEU HD13 H  N N 330 
LEU HD21 H  N N 331 
LEU HD22 H  N N 332 
LEU HD23 H  N N 333 
LEU HXT  H  N N 334 
LYS N    N  N N 335 
LYS CA   C  N S 336 
LYS C    C  N N 337 
LYS O    O  N N 338 
LYS CB   C  N N 339 
LYS CG   C  N N 340 
LYS CD   C  N N 341 
LYS CE   C  N N 342 
LYS NZ   N  N N 343 
LYS OXT  O  N N 344 
LYS H    H  N N 345 
LYS H2   H  N N 346 
LYS HA   H  N N 347 
LYS HB2  H  N N 348 
LYS HB3  H  N N 349 
LYS HG2  H  N N 350 
LYS HG3  H  N N 351 
LYS HD2  H  N N 352 
LYS HD3  H  N N 353 
LYS HE2  H  N N 354 
LYS HE3  H  N N 355 
LYS HZ1  H  N N 356 
LYS HZ2  H  N N 357 
LYS HZ3  H  N N 358 
LYS HXT  H  N N 359 
MET N    N  N N 360 
MET CA   C  N S 361 
MET C    C  N N 362 
MET O    O  N N 363 
MET CB   C  N N 364 
MET CG   C  N N 365 
MET SD   S  N N 366 
MET CE   C  N N 367 
MET OXT  O  N N 368 
MET H    H  N N 369 
MET H2   H  N N 370 
MET HA   H  N N 371 
MET HB2  H  N N 372 
MET HB3  H  N N 373 
MET HG2  H  N N 374 
MET HG3  H  N N 375 
MET HE1  H  N N 376 
MET HE2  H  N N 377 
MET HE3  H  N N 378 
MET HXT  H  N N 379 
PHE N    N  N N 380 
PHE CA   C  N S 381 
PHE C    C  N N 382 
PHE O    O  N N 383 
PHE CB   C  N N 384 
PHE CG   C  Y N 385 
PHE CD1  C  Y N 386 
PHE CD2  C  Y N 387 
PHE CE1  C  Y N 388 
PHE CE2  C  Y N 389 
PHE CZ   C  Y N 390 
PHE OXT  O  N N 391 
PHE H    H  N N 392 
PHE H2   H  N N 393 
PHE HA   H  N N 394 
PHE HB2  H  N N 395 
PHE HB3  H  N N 396 
PHE HD1  H  N N 397 
PHE HD2  H  N N 398 
PHE HE1  H  N N 399 
PHE HE2  H  N N 400 
PHE HZ   H  N N 401 
PHE HXT  H  N N 402 
PRO N    N  N N 403 
PRO CA   C  N S 404 
PRO C    C  N N 405 
PRO O    O  N N 406 
PRO CB   C  N N 407 
PRO CG   C  N N 408 
PRO CD   C  N N 409 
PRO OXT  O  N N 410 
PRO H    H  N N 411 
PRO HA   H  N N 412 
PRO HB2  H  N N 413 
PRO HB3  H  N N 414 
PRO HG2  H  N N 415 
PRO HG3  H  N N 416 
PRO HD2  H  N N 417 
PRO HD3  H  N N 418 
PRO HXT  H  N N 419 
SER N    N  N N 420 
SER CA   C  N S 421 
SER C    C  N N 422 
SER O    O  N N 423 
SER CB   C  N N 424 
SER OG   O  N N 425 
SER OXT  O  N N 426 
SER H    H  N N 427 
SER H2   H  N N 428 
SER HA   H  N N 429 
SER HB2  H  N N 430 
SER HB3  H  N N 431 
SER HG   H  N N 432 
SER HXT  H  N N 433 
SF4 FE1  FE N N 434 
SF4 FE2  FE N N 435 
SF4 FE3  FE N N 436 
SF4 FE4  FE N N 437 
SF4 S1   S  N N 438 
SF4 S2   S  N N 439 
SF4 S3   S  N N 440 
SF4 S4   S  N N 441 
THR N    N  N N 442 
THR CA   C  N S 443 
THR C    C  N N 444 
THR O    O  N N 445 
THR CB   C  N R 446 
THR OG1  O  N N 447 
THR CG2  C  N N 448 
THR OXT  O  N N 449 
THR H    H  N N 450 
THR H2   H  N N 451 
THR HA   H  N N 452 
THR HB   H  N N 453 
THR HG1  H  N N 454 
THR HG21 H  N N 455 
THR HG22 H  N N 456 
THR HG23 H  N N 457 
THR HXT  H  N N 458 
TRP N    N  N N 459 
TRP CA   C  N S 460 
TRP C    C  N N 461 
TRP O    O  N N 462 
TRP CB   C  N N 463 
TRP CG   C  Y N 464 
TRP CD1  C  Y N 465 
TRP CD2  C  Y N 466 
TRP NE1  N  Y N 467 
TRP CE2  C  Y N 468 
TRP CE3  C  Y N 469 
TRP CZ2  C  Y N 470 
TRP CZ3  C  Y N 471 
TRP CH2  C  Y N 472 
TRP OXT  O  N N 473 
TRP H    H  N N 474 
TRP H2   H  N N 475 
TRP HA   H  N N 476 
TRP HB2  H  N N 477 
TRP HB3  H  N N 478 
TRP HD1  H  N N 479 
TRP HE1  H  N N 480 
TRP HE3  H  N N 481 
TRP HZ2  H  N N 482 
TRP HZ3  H  N N 483 
TRP HH2  H  N N 484 
TRP HXT  H  N N 485 
TRS C    C  N N 486 
TRS C1   C  N N 487 
TRS C2   C  N N 488 
TRS C3   C  N N 489 
TRS N    N  N N 490 
TRS O1   O  N N 491 
TRS O2   O  N N 492 
TRS O3   O  N N 493 
TRS H11  H  N N 494 
TRS H12  H  N N 495 
TRS H21  H  N N 496 
TRS H22  H  N N 497 
TRS H31  H  N N 498 
TRS H32  H  N N 499 
TRS HN1  H  N N 500 
TRS HN2  H  N N 501 
TRS HN3  H  N N 502 
TRS HO1  H  N N 503 
TRS HO2  H  N N 504 
TRS HO3  H  N N 505 
TYR N    N  N N 506 
TYR CA   C  N S 507 
TYR C    C  N N 508 
TYR O    O  N N 509 
TYR CB   C  N N 510 
TYR CG   C  Y N 511 
TYR CD1  C  Y N 512 
TYR CD2  C  Y N 513 
TYR CE1  C  Y N 514 
TYR CE2  C  Y N 515 
TYR CZ   C  Y N 516 
TYR OH   O  N N 517 
TYR OXT  O  N N 518 
TYR H    H  N N 519 
TYR H2   H  N N 520 
TYR HA   H  N N 521 
TYR HB2  H  N N 522 
TYR HB3  H  N N 523 
TYR HD1  H  N N 524 
TYR HD2  H  N N 525 
TYR HE1  H  N N 526 
TYR HE2  H  N N 527 
TYR HH   H  N N 528 
TYR HXT  H  N N 529 
VAL N    N  N N 530 
VAL CA   C  N S 531 
VAL C    C  N N 532 
VAL O    O  N N 533 
VAL CB   C  N N 534 
VAL CG1  C  N N 535 
VAL CG2  C  N N 536 
VAL OXT  O  N N 537 
VAL H    H  N N 538 
VAL H2   H  N N 539 
VAL HA   H  N N 540 
VAL HB   H  N N 541 
VAL HG11 H  N N 542 
VAL HG12 H  N N 543 
VAL HG13 H  N N 544 
VAL HG21 H  N N 545 
VAL HG22 H  N N 546 
VAL HG23 H  N N 547 
VAL HXT  H  N N 548 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BJ8 S1  FE2  sing N N 70  
BJ8 S1  FE3  sing N N 71  
BJ8 S1  FE4  sing N N 72  
BJ8 S2  FE1  sing N N 73  
BJ8 S2  FE3  sing N N 74  
BJ8 S2  FE4  sing N N 75  
BJ8 S3  FE1  sing N N 76  
BJ8 S3  FE2  sing N N 77  
BJ8 S3  FE4  sing N N 78  
BJ8 S4  FE1  sing N N 79  
BJ8 S4  FE2  sing N N 80  
BJ8 S4  FE3  sing N N 81  
BJ8 S5  FE6  sing N N 82  
BJ8 S5  FE7  sing N N 83  
BJ8 S6  FE5  sing N N 84  
BJ8 S6  FE7  sing N N 85  
BJ8 S6  FE8  sing N N 86  
BJ8 S7  FE5  sing N N 87  
BJ8 S7  FE6  sing N N 88  
BJ8 S7  FE8  sing N N 89  
BJ8 S8  FE5  sing N N 90  
BJ8 S8  FE6  sing N N 91  
BJ8 S8  FE7  sing N N 92  
BJ8 S9  FE1  sing N N 93  
BJ8 S9  FE8  sing N N 94  
BJ8 S5  FE8  sing N N 95  
BYC C6A N1A  doub Y N 96  
BYC N1A C2A  sing Y N 97  
BYC O1A P1A  doub N N 98  
BYC O2A P1A  sing N N 99  
BYC P1A O3A  sing N N 100 
BYC P1A O5D  sing N N 101 
BYC S1P C1B  sing N N 102 
BYC C1B O57  doub N N 103 
BYC C1B C2B  sing N N 104 
BYC C2D C1D  sing N N 105 
BYC O4D C1D  sing N N 106 
BYC C1D N9A  sing N N 107 
BYC C1D H1D  sing N N 108 
BYC C2P S1P  sing N N 109 
BYC N3A C2A  doub Y N 110 
BYC C2A H2A  sing N N 111 
BYC O2A HO2A sing N N 112 
BYC O5A P2A  doub N N 113 
BYC P2A O6A  sing N N 114 
BYC P2A O4A  sing N N 115 
BYC P2A O3A  sing N N 116 
BYC C3B C2B  doub Y N 117 
BYC C2B C7B  sing Y N 118 
BYC C3D C2D  sing N N 119 
BYC C2D O2D  sing N N 120 
BYC C2D H2D  sing N N 121 
BYC O2D HO2D sing N N 122 
BYC C3P C2P  sing N N 123 
BYC C2P H2P  sing N N 124 
BYC C2P H2PA sing N N 125 
BYC C4A N3A  sing Y N 126 
BYC C3B C4B  sing Y N 127 
BYC C3B H3B  sing N N 128 
BYC C3D C4D  sing N N 129 
BYC C3D O3D  sing N N 130 
BYC C3D H3D  sing N N 131 
BYC P3D O3D  sing N N 132 
BYC O8A P3D  doub N N 133 
BYC P3D O9A  sing N N 134 
BYC P3D O7A  sing N N 135 
BYC N4P C3P  sing N N 136 
BYC C3P H3P  sing N N 137 
BYC C3P H3PA sing N N 138 
BYC N9A C4A  sing Y N 139 
BYC C5M C4A  doub Y N 140 
BYC O4A HO4A sing N N 141 
BYC C4B C5B  doub Y N 142 
BYC C4B H4B  sing N N 143 
BYC C5D C4D  sing N N 144 
BYC C4D O4D  sing N N 145 
BYC C4D H4D  sing N N 146 
BYC C5P N4P  sing N N 147 
BYC N4P HN4P sing N N 148 
BYC C5B C6B  sing Y N 149 
BYC C5B H5B  sing N N 150 
BYC O5D C5D  sing N N 151 
BYC C5D H5D  sing N N 152 
BYC C5D H5DA sing N N 153 
BYC N7A C5M  sing Y N 154 
BYC C5M C6A  sing Y N 155 
BYC C6P C5P  sing N N 156 
BYC C5P O5P  doub N N 157 
BYC N6A C6A  sing N N 158 
BYC N6A HN6A sing N N 159 
BYC N6A HN6B sing N N 160 
BYC O6A CCP  sing N N 161 
BYC C7B C6B  doub Y N 162 
BYC C6B H6B  sing N N 163 
BYC C7P C6P  sing N N 164 
BYC C6P H6P  sing N N 165 
BYC C6P H6PA sing N N 166 
BYC C8A N7A  doub Y N 167 
BYC O7A HO7A sing N N 168 
BYC C7B H7B  sing N N 169 
BYC N8P C7P  sing N N 170 
BYC C7P H7P  sing N N 171 
BYC C7P H7PA sing N N 172 
BYC C8A N9A  sing Y N 173 
BYC C8A H8A  sing N N 174 
BYC C9P N8P  sing N N 175 
BYC N8P HN8P sing N N 176 
BYC O9A HO9A sing N N 177 
BYC O9P C9P  doub N N 178 
BYC CAP C9P  sing N N 179 
BYC CAP CBP  sing N N 180 
BYC CAP OAP  sing N N 181 
BYC CAP HAP  sing N N 182 
BYC OAP HOAP sing N N 183 
BYC CEP CBP  sing N N 184 
BYC CCP CBP  sing N N 185 
BYC CBP CDP  sing N N 186 
BYC CCP HCP  sing N N 187 
BYC CCP HCPA sing N N 188 
BYC CDP HDP  sing N N 189 
BYC CDP HDPA sing N N 190 
BYC CDP HDPB sing N N 191 
BYC CEP HEP  sing N N 192 
BYC CEP HEPA sing N N 193 
BYC CEP HEPB sing N N 194 
CYS N   CA   sing N N 195 
CYS N   H    sing N N 196 
CYS N   H2   sing N N 197 
CYS CA  C    sing N N 198 
CYS CA  CB   sing N N 199 
CYS CA  HA   sing N N 200 
CYS C   O    doub N N 201 
CYS C   OXT  sing N N 202 
CYS CB  SG   sing N N 203 
CYS CB  HB2  sing N N 204 
CYS CB  HB3  sing N N 205 
CYS SG  HG   sing N N 206 
CYS OXT HXT  sing N N 207 
DOD O   D1   sing N N 208 
DOD O   D2   sing N N 209 
GLN N   CA   sing N N 210 
GLN N   H    sing N N 211 
GLN N   H2   sing N N 212 
GLN CA  C    sing N N 213 
GLN CA  CB   sing N N 214 
GLN CA  HA   sing N N 215 
GLN C   O    doub N N 216 
GLN C   OXT  sing N N 217 
GLN CB  CG   sing N N 218 
GLN CB  HB2  sing N N 219 
GLN CB  HB3  sing N N 220 
GLN CG  CD   sing N N 221 
GLN CG  HG2  sing N N 222 
GLN CG  HG3  sing N N 223 
GLN CD  OE1  doub N N 224 
GLN CD  NE2  sing N N 225 
GLN NE2 HE21 sing N N 226 
GLN NE2 HE22 sing N N 227 
GLN OXT HXT  sing N N 228 
GLU N   CA   sing N N 229 
GLU N   H    sing N N 230 
GLU N   H2   sing N N 231 
GLU CA  C    sing N N 232 
GLU CA  CB   sing N N 233 
GLU CA  HA   sing N N 234 
GLU C   O    doub N N 235 
GLU C   OXT  sing N N 236 
GLU CB  CG   sing N N 237 
GLU CB  HB2  sing N N 238 
GLU CB  HB3  sing N N 239 
GLU CG  CD   sing N N 240 
GLU CG  HG2  sing N N 241 
GLU CG  HG3  sing N N 242 
GLU CD  OE1  doub N N 243 
GLU CD  OE2  sing N N 244 
GLU OE2 HE2  sing N N 245 
GLU OXT HXT  sing N N 246 
GLY N   CA   sing N N 247 
GLY N   H    sing N N 248 
GLY N   H2   sing N N 249 
GLY CA  C    sing N N 250 
GLY CA  HA2  sing N N 251 
GLY CA  HA3  sing N N 252 
GLY C   O    doub N N 253 
GLY C   OXT  sing N N 254 
GLY OXT HXT  sing N N 255 
GOL C1  O1   sing N N 256 
GOL C1  C2   sing N N 257 
GOL C1  H11  sing N N 258 
GOL C1  H12  sing N N 259 
GOL O1  HO1  sing N N 260 
GOL C2  O2   sing N N 261 
GOL C2  C3   sing N N 262 
GOL C2  H2   sing N N 263 
GOL O2  HO2  sing N N 264 
GOL C3  O3   sing N N 265 
GOL C3  H31  sing N N 266 
GOL C3  H32  sing N N 267 
GOL O3  HO3  sing N N 268 
HIS N   CA   sing N N 269 
HIS N   H    sing N N 270 
HIS N   H2   sing N N 271 
HIS CA  C    sing N N 272 
HIS CA  CB   sing N N 273 
HIS CA  HA   sing N N 274 
HIS C   O    doub N N 275 
HIS C   OXT  sing N N 276 
HIS CB  CG   sing N N 277 
HIS CB  HB2  sing N N 278 
HIS CB  HB3  sing N N 279 
HIS CG  ND1  sing Y N 280 
HIS CG  CD2  doub Y N 281 
HIS ND1 CE1  doub Y N 282 
HIS ND1 HD1  sing N N 283 
HIS CD2 NE2  sing Y N 284 
HIS CD2 HD2  sing N N 285 
HIS CE1 NE2  sing Y N 286 
HIS CE1 HE1  sing N N 287 
HIS NE2 HE2  sing N N 288 
HIS OXT HXT  sing N N 289 
HOH O   H1   sing N N 290 
HOH O   H2   sing N N 291 
ILE N   CA   sing N N 292 
ILE N   H    sing N N 293 
ILE N   H2   sing N N 294 
ILE CA  C    sing N N 295 
ILE CA  CB   sing N N 296 
ILE CA  HA   sing N N 297 
ILE C   O    doub N N 298 
ILE C   OXT  sing N N 299 
ILE CB  CG1  sing N N 300 
ILE CB  CG2  sing N N 301 
ILE CB  HB   sing N N 302 
ILE CG1 CD1  sing N N 303 
ILE CG1 HG12 sing N N 304 
ILE CG1 HG13 sing N N 305 
ILE CG2 HG21 sing N N 306 
ILE CG2 HG22 sing N N 307 
ILE CG2 HG23 sing N N 308 
ILE CD1 HD11 sing N N 309 
ILE CD1 HD12 sing N N 310 
ILE CD1 HD13 sing N N 311 
ILE OXT HXT  sing N N 312 
LEU N   CA   sing N N 313 
LEU N   H    sing N N 314 
LEU N   H2   sing N N 315 
LEU CA  C    sing N N 316 
LEU CA  CB   sing N N 317 
LEU CA  HA   sing N N 318 
LEU C   O    doub N N 319 
LEU C   OXT  sing N N 320 
LEU CB  CG   sing N N 321 
LEU CB  HB2  sing N N 322 
LEU CB  HB3  sing N N 323 
LEU CG  CD1  sing N N 324 
LEU CG  CD2  sing N N 325 
LEU CG  HG   sing N N 326 
LEU CD1 HD11 sing N N 327 
LEU CD1 HD12 sing N N 328 
LEU CD1 HD13 sing N N 329 
LEU CD2 HD21 sing N N 330 
LEU CD2 HD22 sing N N 331 
LEU CD2 HD23 sing N N 332 
LEU OXT HXT  sing N N 333 
LYS N   CA   sing N N 334 
LYS N   H    sing N N 335 
LYS N   H2   sing N N 336 
LYS CA  C    sing N N 337 
LYS CA  CB   sing N N 338 
LYS CA  HA   sing N N 339 
LYS C   O    doub N N 340 
LYS C   OXT  sing N N 341 
LYS CB  CG   sing N N 342 
LYS CB  HB2  sing N N 343 
LYS CB  HB3  sing N N 344 
LYS CG  CD   sing N N 345 
LYS CG  HG2  sing N N 346 
LYS CG  HG3  sing N N 347 
LYS CD  CE   sing N N 348 
LYS CD  HD2  sing N N 349 
LYS CD  HD3  sing N N 350 
LYS CE  NZ   sing N N 351 
LYS CE  HE2  sing N N 352 
LYS CE  HE3  sing N N 353 
LYS NZ  HZ1  sing N N 354 
LYS NZ  HZ2  sing N N 355 
LYS NZ  HZ3  sing N N 356 
LYS OXT HXT  sing N N 357 
MET N   CA   sing N N 358 
MET N   H    sing N N 359 
MET N   H2   sing N N 360 
MET CA  C    sing N N 361 
MET CA  CB   sing N N 362 
MET CA  HA   sing N N 363 
MET C   O    doub N N 364 
MET C   OXT  sing N N 365 
MET CB  CG   sing N N 366 
MET CB  HB2  sing N N 367 
MET CB  HB3  sing N N 368 
MET CG  SD   sing N N 369 
MET CG  HG2  sing N N 370 
MET CG  HG3  sing N N 371 
MET SD  CE   sing N N 372 
MET CE  HE1  sing N N 373 
MET CE  HE2  sing N N 374 
MET CE  HE3  sing N N 375 
MET OXT HXT  sing N N 376 
PHE N   CA   sing N N 377 
PHE N   H    sing N N 378 
PHE N   H2   sing N N 379 
PHE CA  C    sing N N 380 
PHE CA  CB   sing N N 381 
PHE CA  HA   sing N N 382 
PHE C   O    doub N N 383 
PHE C   OXT  sing N N 384 
PHE CB  CG   sing N N 385 
PHE CB  HB2  sing N N 386 
PHE CB  HB3  sing N N 387 
PHE CG  CD1  doub Y N 388 
PHE CG  CD2  sing Y N 389 
PHE CD1 CE1  sing Y N 390 
PHE CD1 HD1  sing N N 391 
PHE CD2 CE2  doub Y N 392 
PHE CD2 HD2  sing N N 393 
PHE CE1 CZ   doub Y N 394 
PHE CE1 HE1  sing N N 395 
PHE CE2 CZ   sing Y N 396 
PHE CE2 HE2  sing N N 397 
PHE CZ  HZ   sing N N 398 
PHE OXT HXT  sing N N 399 
PRO N   CA   sing N N 400 
PRO N   CD   sing N N 401 
PRO N   H    sing N N 402 
PRO CA  C    sing N N 403 
PRO CA  CB   sing N N 404 
PRO CA  HA   sing N N 405 
PRO C   O    doub N N 406 
PRO C   OXT  sing N N 407 
PRO CB  CG   sing N N 408 
PRO CB  HB2  sing N N 409 
PRO CB  HB3  sing N N 410 
PRO CG  CD   sing N N 411 
PRO CG  HG2  sing N N 412 
PRO CG  HG3  sing N N 413 
PRO CD  HD2  sing N N 414 
PRO CD  HD3  sing N N 415 
PRO OXT HXT  sing N N 416 
SER N   CA   sing N N 417 
SER N   H    sing N N 418 
SER N   H2   sing N N 419 
SER CA  C    sing N N 420 
SER CA  CB   sing N N 421 
SER CA  HA   sing N N 422 
SER C   O    doub N N 423 
SER C   OXT  sing N N 424 
SER CB  OG   sing N N 425 
SER CB  HB2  sing N N 426 
SER CB  HB3  sing N N 427 
SER OG  HG   sing N N 428 
SER OXT HXT  sing N N 429 
SF4 FE1 S2   sing N N 430 
SF4 FE1 S3   sing N N 431 
SF4 FE1 S4   sing N N 432 
SF4 FE2 S1   sing N N 433 
SF4 FE2 S3   sing N N 434 
SF4 FE2 S4   sing N N 435 
SF4 FE3 S1   sing N N 436 
SF4 FE3 S2   sing N N 437 
SF4 FE3 S4   sing N N 438 
SF4 FE4 S1   sing N N 439 
SF4 FE4 S2   sing N N 440 
SF4 FE4 S3   sing N N 441 
THR N   CA   sing N N 442 
THR N   H    sing N N 443 
THR N   H2   sing N N 444 
THR CA  C    sing N N 445 
THR CA  CB   sing N N 446 
THR CA  HA   sing N N 447 
THR C   O    doub N N 448 
THR C   OXT  sing N N 449 
THR CB  OG1  sing N N 450 
THR CB  CG2  sing N N 451 
THR CB  HB   sing N N 452 
THR OG1 HG1  sing N N 453 
THR CG2 HG21 sing N N 454 
THR CG2 HG22 sing N N 455 
THR CG2 HG23 sing N N 456 
THR OXT HXT  sing N N 457 
TRP N   CA   sing N N 458 
TRP N   H    sing N N 459 
TRP N   H2   sing N N 460 
TRP CA  C    sing N N 461 
TRP CA  CB   sing N N 462 
TRP CA  HA   sing N N 463 
TRP C   O    doub N N 464 
TRP C   OXT  sing N N 465 
TRP CB  CG   sing N N 466 
TRP CB  HB2  sing N N 467 
TRP CB  HB3  sing N N 468 
TRP CG  CD1  doub Y N 469 
TRP CG  CD2  sing Y N 470 
TRP CD1 NE1  sing Y N 471 
TRP CD1 HD1  sing N N 472 
TRP CD2 CE2  doub Y N 473 
TRP CD2 CE3  sing Y N 474 
TRP NE1 CE2  sing Y N 475 
TRP NE1 HE1  sing N N 476 
TRP CE2 CZ2  sing Y N 477 
TRP CE3 CZ3  doub Y N 478 
TRP CE3 HE3  sing N N 479 
TRP CZ2 CH2  doub Y N 480 
TRP CZ2 HZ2  sing N N 481 
TRP CZ3 CH2  sing Y N 482 
TRP CZ3 HZ3  sing N N 483 
TRP CH2 HH2  sing N N 484 
TRP OXT HXT  sing N N 485 
TRS C   C1   sing N N 486 
TRS C   C2   sing N N 487 
TRS C   C3   sing N N 488 
TRS C   N    sing N N 489 
TRS C1  O1   sing N N 490 
TRS C1  H11  sing N N 491 
TRS C1  H12  sing N N 492 
TRS C2  O2   sing N N 493 
TRS C2  H21  sing N N 494 
TRS C2  H22  sing N N 495 
TRS C3  O3   sing N N 496 
TRS C3  H31  sing N N 497 
TRS C3  H32  sing N N 498 
TRS N   HN1  sing N N 499 
TRS N   HN2  sing N N 500 
TRS N   HN3  sing N N 501 
TRS O1  HO1  sing N N 502 
TRS O2  HO2  sing N N 503 
TRS O3  HO3  sing N N 504 
TYR N   CA   sing N N 505 
TYR N   H    sing N N 506 
TYR N   H2   sing N N 507 
TYR CA  C    sing N N 508 
TYR CA  CB   sing N N 509 
TYR CA  HA   sing N N 510 
TYR C   O    doub N N 511 
TYR C   OXT  sing N N 512 
TYR CB  CG   sing N N 513 
TYR CB  HB2  sing N N 514 
TYR CB  HB3  sing N N 515 
TYR CG  CD1  doub Y N 516 
TYR CG  CD2  sing Y N 517 
TYR CD1 CE1  sing Y N 518 
TYR CD1 HD1  sing N N 519 
TYR CD2 CE2  doub Y N 520 
TYR CD2 HD2  sing N N 521 
TYR CE1 CZ   doub Y N 522 
TYR CE1 HE1  sing N N 523 
TYR CE2 CZ   sing Y N 524 
TYR CE2 HE2  sing N N 525 
TYR CZ  OH   sing N N 526 
TYR OH  HH   sing N N 527 
TYR OXT HXT  sing N N 528 
VAL N   CA   sing N N 529 
VAL N   H    sing N N 530 
VAL N   H2   sing N N 531 
VAL CA  C    sing N N 532 
VAL CA  CB   sing N N 533 
VAL CA  HA   sing N N 534 
VAL C   O    doub N N 535 
VAL C   OXT  sing N N 536 
VAL CB  CG1  sing N N 537 
VAL CB  CG2  sing N N 538 
VAL CB  HB   sing N N 539 
VAL CG1 HG11 sing N N 540 
VAL CG1 HG12 sing N N 541 
VAL CG1 HG13 sing N N 542 
VAL CG2 HG21 sing N N 543 
VAL CG2 HG22 sing N N 544 
VAL CG2 HG23 sing N N 545 
VAL OXT HXT  sing N N 546 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8S2R 
_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]   0.004804 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001063 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009736 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.011786 
_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  
FE 
N  
O  
P  
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   . ALA A 1 5   ? 14.311  5.030   -19.977 1.00 65.09  ? 5   ALA A N   1 
ATOM   2     C  CA  . ALA A 1 5   ? 13.382  5.541   -20.974 1.00 75.69  ? 5   ALA A CA  1 
ATOM   3     C  C   . ALA A 1 5   ? 13.741  6.961   -21.445 1.00 81.68  ? 5   ALA A C   1 
ATOM   4     O  O   . ALA A 1 5   ? 12.988  7.915   -21.222 1.00 82.66  ? 5   ALA A O   1 
ATOM   5     C  CB  . ALA A 1 5   ? 11.955  5.499   -20.436 1.00 71.84  ? 5   ALA A CB  1 
ATOM   6     N  N   . ASN A 1 6   ? 14.917  7.076   -22.071 1.00 83.26  ? 6   ASN A N   1 
ATOM   7     C  CA  . ASN A 1 6   ? 15.290  8.118   -23.034 1.00 87.49  ? 6   ASN A CA  1 
ATOM   8     C  C   . ASN A 1 6   ? 15.418  9.528   -22.467 1.00 79.19  ? 6   ASN A C   1 
ATOM   9     O  O   . ASN A 1 6   ? 15.615  10.466  -23.252 1.00 87.99  ? 6   ASN A O   1 
ATOM   10    C  CB  . ASN A 1 6   ? 14.323  8.194   -24.234 1.00 91.83  ? 6   ASN A CB  1 
ATOM   11    C  CG  . ASN A 1 6   ? 14.882  7.566   -25.510 1.00 97.81  ? 6   ASN A CG  1 
ATOM   12    O  OD1 . ASN A 1 6   ? 15.064  6.347   -25.597 1.00 99.19  ? 6   ASN A OD1 1 
ATOM   13    N  ND2 . ASN A 1 6   ? 15.108  8.401   -26.528 1.00 89.64  ? 6   ASN A ND2 1 
ATOM   14    N  N   . LYS A 1 7   ? 15.319  9.738   -21.153 1.00 65.83  ? 7   LYS A N   1 
ATOM   15    C  CA  . LYS A 1 7   ? 15.525  11.111  -20.700 1.00 60.82  ? 7   LYS A CA  1 
ATOM   16    C  C   . LYS A 1 7   ? 17.024  11.397  -20.556 1.00 54.18  ? 7   LYS A C   1 
ATOM   17    O  O   . LYS A 1 7   ? 17.522  12.417  -21.058 1.00 55.96  ? 7   LYS A O   1 
ATOM   18    C  CB  . LYS A 1 7   ? 14.754  11.363  -19.393 1.00 63.86  ? 7   LYS A CB  1 
ATOM   19    C  CG  . LYS A 1 7   ? 14.875  12.763  -18.698 1.00 58.86  ? 7   LYS A CG  1 
ATOM   20    C  CD  . LYS A 1 7   ? 15.273  13.908  -19.636 1.00 61.83  ? 7   LYS A CD  1 
ATOM   21    C  CE  . LYS A 1 7   ? 14.789  15.274  -19.135 1.00 68.27  ? 7   LYS A CE  1 
ATOM   22    N  NZ  . LYS A 1 7   ? 15.659  16.393  -19.627 1.00 66.78  ? 7   LYS A NZ  1 
ATOM   23    N  N   . TYR A 1 8   ? 17.770  10.483  -19.928 1.00 49.03  ? 8   TYR A N   1 
ATOM   24    C  CA  . TYR A 1 8   ? 19.187  10.668  -19.638 1.00 44.22  ? 8   TYR A CA  1 
ATOM   25    C  C   . TYR A 1 8   ? 20.002  9.525   -20.224 1.00 43.53  ? 8   TYR A C   1 
ATOM   26    O  O   . TYR A 1 8   ? 19.558  8.373   -20.241 1.00 43.07  ? 8   TYR A O   1 
ATOM   27    C  CB  . TYR A 1 8   ? 19.493  10.734  -18.122 1.00 38.72  ? 8   TYR A CB  1 
ATOM   28    C  CG  . TYR A 1 8   ? 18.752  11.836  -17.414 1.00 43.32  ? 8   TYR A CG  1 
ATOM   29    C  CD1 . TYR A 1 8   ? 19.124  13.171  -17.563 1.00 45.78  ? 8   TYR A CD1 1 
ATOM   30    C  CD2 . TYR A 1 8   ? 17.626  11.550  -16.657 1.00 44.84  ? 8   TYR A CD2 1 
ATOM   31    C  CE1 . TYR A 1 8   ? 18.399  14.184  -16.951 1.00 44.64  ? 8   TYR A CE1 1 
ATOM   32    C  CE2 . TYR A 1 8   ? 16.919  12.546  -16.029 1.00 44.24  ? 8   TYR A CE2 1 
ATOM   33    C  CZ  . TYR A 1 8   ? 17.303  13.862  -16.185 1.00 44.23  ? 8   TYR A CZ  1 
ATOM   34    O  OH  . TYR A 1 8   ? 16.587  14.844  -15.524 1.00 48.70  ? 8   TYR A OH  1 
ATOM   35    N  N   . PRO A 1 9   ? 21.234  9.808   -20.620 1.00 42.56  ? 9   PRO A N   1 
ATOM   36    C  CA  . PRO A 1 9   ? 22.211  8.735   -20.860 1.00 41.31  ? 9   PRO A CA  1 
ATOM   37    C  C   . PRO A 1 9   ? 22.514  7.918   -19.620 1.00 39.03  ? 9   PRO A C   1 
ATOM   38    O  O   . PRO A 1 9   ? 22.583  8.427   -18.500 1.00 36.51  ? 9   PRO A O   1 
ATOM   39    C  CB  . PRO A 1 9   ? 23.475  9.489   -21.298 1.00 43.33  ? 9   PRO A CB  1 
ATOM   40    C  CG  . PRO A 1 9   ? 23.313  10.869  -20.726 1.00 43.55  ? 9   PRO A CG  1 
ATOM   41    C  CD  . PRO A 1 9   ? 21.819  11.156  -20.726 1.00 40.41  ? 9   PRO A CD  1 
ATOM   42    N  N   . THR A 1 10  ? 22.808  6.646   -19.844 1.00 37.34  ? 10  THR A N   1 
ATOM   43    C  CA  . THR A 1 10  ? 23.140  5.723   -18.780 1.00 37.33  ? 10  THR A CA  1 
ATOM   44    C  C   . THR A 1 10  ? 24.400  4.951   -19.169 1.00 35.39  ? 10  THR A C   1 
ATOM   45    O  O   . THR A 1 10  ? 24.831  4.945   -20.334 1.00 41.11  ? 10  THR A O   1 
ATOM   46    C  CB  . THR A 1 10  ? 21.943  4.790   -18.516 1.00 36.74  ? 10  THR A CB  1 
ATOM   47    O  OG1 . THR A 1 10  ? 21.955  4.304   -17.174 1.00 45.78  ? 10  THR A OG1 1 
ATOM   48    C  CG2 . THR A 1 10  ? 21.923  3.639   -19.524 1.00 39.53  ? 10  THR A CG2 1 
ATOM   49    N  N   . GLU A 1 11  ? 24.975  4.281   -18.185 1.00 37.48  ? 11  GLU A N   1 
ATOM   50    C  CA  . GLU A 1 11  ? 26.185  3.493   -18.347 1.00 37.63  ? 11  GLU A CA  1 
ATOM   51    C  C   . GLU A 1 11  ? 26.476  2.695   -17.079 1.00 33.14  ? 11  GLU A C   1 
ATOM   52    O  O   . GLU A 1 11  ? 26.338  3.211   -15.984 1.00 33.30  ? 11  GLU A O   1 
ATOM   53    C  CB  . GLU A 1 11  ? 27.336  4.423   -18.720 1.00 40.16  ? 11  GLU A CB  1 
ATOM   54    C  CG  . GLU A 1 11  ? 28.633  4.097   -18.111 1.00 41.21  ? 11  GLU A CG  1 
ATOM   55    C  CD  . GLU A 1 11  ? 29.734  5.051   -18.568 1.00 51.16  ? 11  GLU A CD  1 
ATOM   56    O  OE1 . GLU A 1 11  ? 29.442  6.077   -19.277 1.00 49.90  ? 11  GLU A OE1 1 
ATOM   57    O  OE2 . GLU A 1 11  ? 30.873  4.824   -18.097 1.00 43.30  ? 11  GLU A OE2 1 
ATOM   58    N  N   . GLN A 1 12  ? 26.858  1.433   -17.250 1.00 31.71  ? 12  GLN A N   1 
ATOM   59    C  CA  . GLN A 1 12  ? 27.198  0.598   -16.111 1.00 33.85  ? 12  GLN A CA  1 
ATOM   60    C  C   . GLN A 1 12  ? 28.535  1.056   -15.526 1.00 37.46  ? 12  GLN A C   1 
ATOM   61    O  O   . GLN A 1 12  ? 29.409  1.556   -16.247 1.00 41.79  ? 12  GLN A O   1 
ATOM   62    C  CB  . GLN A 1 12  ? 27.231  -0.862  -16.547 1.00 29.50  ? 12  GLN A CB  1 
ATOM   63    C  CG  . GLN A 1 12  ? 25.876  -1.585  -16.284 1.00 39.65  ? 12  GLN A CG  1 
ATOM   64    C  CD  . GLN A 1 12  ? 25.695  -2.885  -17.065 1.00 45.81  ? 12  GLN A CD  1 
ATOM   65    O  OE1 . GLN A 1 12  ? 24.735  -3.049  -17.841 1.00 45.53  ? 12  GLN A OE1 1 
ATOM   66    N  NE2 . GLN A 1 12  ? 26.579  -3.854  -16.800 1.00 49.01  ? 12  GLN A NE2 1 
ATOM   67    N  N   . LEU A 1 13  ? 28.629  1.006   -14.204 1.00 32.89  ? 13  LEU A N   1 
ATOM   68    C  CA  . LEU A 1 13  ? 29.844  1.480   -13.506 1.00 31.97  ? 13  LEU A CA  1 
ATOM   69    C  C   . LEU A 1 13  ? 31.016  0.606   -13.943 1.00 37.35  ? 13  LEU A C   1 
ATOM   70    O  O   . LEU A 1 13  ? 30.881  -0.602  -13.899 1.00 39.08  ? 13  LEU A O   1 
ATOM   71    C  CB  . LEU A 1 13  ? 29.573  1.400   -12.003 1.00 31.23  ? 13  LEU A CB  1 
ATOM   72    C  CG  . LEU A 1 13  ? 30.561  2.134   -11.108 1.00 39.86  ? 13  LEU A CG  1 
ATOM   73    C  CD1 . LEU A 1 13  ? 30.377  3.631   -11.197 1.00 34.06  ? 13  LEU A CD1 1 
ATOM   74    C  CD2 . LEU A 1 13  ? 30.404  1.669   -9.681  1.00 33.84  ? 13  LEU A CD2 1 
ATOM   75    N  N   . LYS A 1 14  ? 32.132  1.214   -14.320 1.00 33.67  ? 14  LYS A N   1 
ATOM   76    C  CA  . LYS A 1 14  ? 33.248  0.427   -14.838 1.00 35.10  ? 14  LYS A CA  1 
ATOM   77    C  C   . LYS A 1 14  ? 34.053  -0.228  -13.716 1.00 34.15  ? 14  LYS A C   1 
ATOM   78    O  O   . LYS A 1 14  ? 34.650  -1.288  -13.933 1.00 39.48  ? 14  LYS A O   1 
ATOM   79    C  CB  . LYS A 1 14  ? 34.163  1.293   -15.703 1.00 36.50  ? 14  LYS A CB  1 
ATOM   80    C  CG  . LYS A 1 14  ? 33.502  1.835   -16.964 1.00 40.59  ? 14  LYS A CG  1 
ATOM   81    C  CD  . LYS A 1 14  ? 34.393  2.920   -17.557 1.00 43.04  ? 14  LYS A CD  1 
ATOM   82    C  CE  . LYS A 1 14  ? 33.602  4.176   -17.695 1.00 46.38  ? 14  LYS A CE  1 
ATOM   83    N  NZ  . LYS A 1 14  ? 33.433  4.635   -19.123 1.00 51.29  ? 14  LYS A NZ  1 
ATOM   84    N  N   . LEU A 1 15  ? 34.055  0.363   -12.523 1.00 32.06  ? 15  LEU A N   1 
ATOM   85    C  CA  . LEU A 1 15  ? 34.786  -0.154  -11.360 1.00 32.29  ? 15  LEU A CA  1 
ATOM   86    C  C   . LEU A 1 15  ? 33.971  -1.156  -10.554 1.00 31.17  ? 15  LEU A C   1 
ATOM   87    O  O   . LEU A 1 15  ? 34.442  -1.612  -9.507  1.00 32.36  ? 15  LEU A O   1 
ATOM   88    C  CB  . LEU A 1 15  ? 35.292  1.009   -10.468 1.00 29.65  ? 15  LEU A CB  1 
ATOM   89    C  CG  . LEU A 1 15  ? 36.443  1.868   -10.996 1.00 34.60  ? 15  LEU A CG  1 
ATOM   90    C  CD1 . LEU A 1 15  ? 36.511  3.225   -10.260 1.00 33.37  ? 15  LEU A CD1 1 
ATOM   91    C  CD2 . LEU A 1 15  ? 37.804  1.151   -10.903 1.00 33.09  ? 15  LEU A CD2 1 
ATOM   92    N  N   . TRP A 1 16  ? 32.756  -1.467  -11.010 1.00 32.36  ? 16  TRP A N   1 
ATOM   93    C  CA  . TRP A 1 16  ? 31.929  -2.518  -10.423 1.00 34.99  ? 16  TRP A CA  1 
ATOM   94    C  C   . TRP A 1 16  ? 32.725  -3.783  -10.119 1.00 29.41  ? 16  TRP A C   1 
ATOM   95    O  O   . TRP A 1 16  ? 32.709  -4.288  -9.001  1.00 31.25  ? 16  TRP A O   1 
ATOM   96    C  CB  . TRP A 1 16  ? 30.815  -2.862  -11.405 1.00 37.40  ? 16  TRP A CB  1 
ATOM   97    C  CG  . TRP A 1 16  ? 29.684  -3.613  -10.769 1.00 42.97  ? 16  TRP A CG  1 
ATOM   98    C  CD1 . TRP A 1 16  ? 29.213  -4.871  -11.092 1.00 45.58  ? 16  TRP A CD1 1 
ATOM   99    C  CD2 . TRP A 1 16  ? 28.890  -3.138  -9.696  1.00 41.98  ? 16  TRP A CD2 1 
ATOM   100   N  NE1 . TRP A 1 16  ? 28.157  -5.196  -10.258 1.00 48.74  ? 16  TRP A NE1 1 
ATOM   101   C  CE2 . TRP A 1 16  ? 27.947  -4.138  -9.396  1.00 45.34  ? 16  TRP A CE2 1 
ATOM   102   C  CE3 . TRP A 1 16  ? 28.898  -1.942  -8.940  1.00 43.74  ? 16  TRP A CE3 1 
ATOM   103   C  CZ2 . TRP A 1 16  ? 26.998  -3.969  -8.385  1.00 47.84  ? 16  TRP A CZ2 1 
ATOM   104   C  CZ3 . TRP A 1 16  ? 27.972  -1.772  -7.948  1.00 33.80  ? 16  TRP A CZ3 1 
ATOM   105   C  CH2 . TRP A 1 16  ? 27.028  -2.782  -7.679  1.00 38.81  ? 16  TRP A CH2 1 
ATOM   106   N  N   . GLY A 1 17  ? 33.409  -4.305  -11.123 1.00 31.69  ? 17  GLY A N   1 
ATOM   107   C  CA  . GLY A 1 17  ? 34.091  -5.579  -10.969 1.00 32.61  ? 17  GLY A CA  1 
ATOM   108   C  C   . GLY A 1 17  ? 35.156  -5.507  -9.897  1.00 33.64  ? 17  GLY A C   1 
ATOM   109   O  O   . GLY A 1 17  ? 35.301  -6.428  -9.082  1.00 29.97  ? 17  GLY A O   1 
ATOM   110   N  N   . LYS A 1 18  ? 35.923  -4.407  -9.887  1.00 29.77  ? 18  LYS A N   1 
ATOM   111   C  CA  . LYS A 1 18  ? 36.941  -4.221  -8.864  1.00 30.55  ? 18  LYS A CA  1 
ATOM   112   C  C   . LYS A 1 18  ? 36.334  -4.120  -7.457  1.00 28.68  ? 18  LYS A C   1 
ATOM   113   O  O   . LYS A 1 18  ? 36.882  -4.690  -6.508  1.00 29.16  ? 18  LYS A O   1 
ATOM   114   C  CB  . LYS A 1 18  ? 37.769  -2.978  -9.162  1.00 29.28  ? 18  LYS A CB  1 
ATOM   115   C  CG  . LYS A 1 18  ? 38.946  -2.834  -8.174  1.00 32.25  ? 18  LYS A CG  1 
ATOM   116   C  CD  . LYS A 1 18  ? 40.001  -1.900  -8.713  1.00 38.90  ? 18  LYS A CD  1 
ATOM   117   C  CE  . LYS A 1 18  ? 41.241  -1.905  -7.842  1.00 38.28  ? 18  LYS A CE  1 
ATOM   118   N  NZ  . LYS A 1 18  ? 42.190  -0.897  -8.399  1.00 40.09  ? 18  LYS A NZ  1 
ATOM   119   N  N   . ALA A 1 19  ? 35.196  -3.406  -7.287  1.00 27.92  ? 19  ALA A N   1 
ATOM   120   C  CA  . ALA A 1 19  ? 34.545  -3.366  -5.973  1.00 28.89  ? 19  ALA A CA  1 
ATOM   121   C  C   . ALA A 1 19  ? 34.179  -4.776  -5.513  1.00 26.54  ? 19  ALA A C   1 
ATOM   122   O  O   . ALA A 1 19  ? 34.339  -5.111  -4.336  1.00 27.79  ? 19  ALA A O   1 
ATOM   123   C  CB  . ALA A 1 19  ? 33.265  -2.515  -6.008  1.00 27.27  ? 19  ALA A CB  1 
ATOM   124   N  N   . LYS A 1 20  ? 33.672  -5.597  -6.441  1.00 28.03  ? 20  LYS A N   1 
ATOM   125   C  CA  . LYS A 1 20  ? 33.296  -6.969  -6.108  1.00 31.12  ? 20  LYS A CA  1 
ATOM   126   C  C   . LYS A 1 20  ? 34.527  -7.780  -5.738  1.00 27.63  ? 20  LYS A C   1 
ATOM   127   O  O   . LYS A 1 20  ? 34.485  -8.585  -4.801  1.00 28.31  ? 20  LYS A O   1 
ATOM   128   C  CB  . LYS A 1 20  ? 32.579  -7.612  -7.298  1.00 34.14  ? 20  LYS A CB  1 
ATOM   129   C  CG  . LYS A 1 20  ? 31.167  -7.066  -7.594  1.00 36.31  ? 20  LYS A CG  1 
ATOM   130   C  CD  . LYS A 1 20  ? 30.239  -7.193  -6.386  1.00 37.71  ? 20  LYS A CD  1 
ATOM   131   C  CE  . LYS A 1 20  ? 28.808  -7.535  -6.794  1.00 48.15  ? 20  LYS A CE  1 
ATOM   132   N  NZ  . LYS A 1 20  ? 27.745  -6.750  -6.043  1.00 38.51  ? 20  LYS A NZ  1 
ATOM   133   N  N   . GLU A 1 21  ? 35.596  -7.652  -6.531  1.00 29.15  ? 21  GLU A N   1 
ATOM   134   C  CA  . GLU A 1 21  ? 36.822  -8.412  -6.288  1.00 29.57  ? 21  GLU A CA  1 
ATOM   135   C  C   . GLU A 1 21  ? 37.485  -8.019  -4.969  1.00 28.22  ? 21  GLU A C   1 
ATOM   136   O  O   . GLU A 1 21  ? 37.942  -8.898  -4.223  1.00 28.22  ? 21  GLU A O   1 
ATOM   137   C  CB  . GLU A 1 21  ? 37.803  -8.225  -7.430  1.00 33.22  ? 21  GLU A CB  1 
ATOM   138   C  CG  . GLU A 1 21  ? 39.128  -8.887  -7.188  1.00 40.16  ? 21  GLU A CG  1 
ATOM   139   C  CD  . GLU A 1 21  ? 40.018  -8.822  -8.440  1.00 54.22  ? 21  GLU A CD  1 
ATOM   140   O  OE1 . GLU A 1 21  ? 40.526  -9.879  -8.886  1.00 58.38  ? 21  GLU A OE1 1 
ATOM   141   O  OE2 . GLU A 1 21  ? 40.171  -7.694  -8.984  1.00 56.45  ? 21  GLU A OE2 1 
ATOM   142   N  N   . LEU A 1 22  ? 37.492  -6.734  -4.635  1.00 25.19  ? 22  LEU A N   1 
ATOM   143   C  CA  . LEU A 1 22  ? 38.085  -6.311  -3.340  1.00 22.45  ? 22  LEU A CA  1 
ATOM   144   C  C   . LEU A 1 22  ? 37.327  -6.956  -2.175  1.00 25.28  ? 22  LEU A C   1 
ATOM   145   O  O   . LEU A 1 22  ? 37.964  -7.344  -1.227  1.00 25.51  ? 22  LEU A O   1 
ATOM   146   C  CB  . LEU A 1 22  ? 38.038  -4.791  -3.223  1.00 24.72  ? 22  LEU A CB  1 
ATOM   147   C  CG  . LEU A 1 22  ? 39.022  -4.030  -4.099  1.00 23.67  ? 22  LEU A CG  1 
ATOM   148   C  CD1 . LEU A 1 22  ? 38.660  -2.558  -4.149  1.00 27.07  ? 22  LEU A CD1 1 
ATOM   149   C  CD2 . LEU A 1 22  ? 40.448  -4.223  -3.636  1.00 25.37  ? 22  LEU A CD2 1 
ATOM   150   N  N   . ARG A 1 23  ? 36.005  -7.016  -2.263  1.00 21.49  ? 23  ARG A N   1 
ATOM   151   C  CA  . ARG A 1 23  ? 35.198  -7.619  -1.207  1.00 23.06  ? 23  ARG A CA  1 
ATOM   152   C  C   . ARG A 1 23  ? 35.487  -9.099  -1.100  1.00 27.37  ? 23  ARG A C   1 
ATOM   153   O  O   . ARG A 1 23  ? 35.624  -9.641  0.004   1.00 25.59  ? 23  ARG A O   1 
ATOM   154   C  CB  . ARG A 1 23  ? 33.728  -7.411  -1.516  1.00 24.20  ? 23  ARG A CB  1 
ATOM   155   C  CG  . ARG A 1 23  ? 32.795  -8.051  -0.552  1.00 26.73  ? 23  ARG A CG  1 
ATOM   156   C  CD  . ARG A 1 23  ? 31.353  -7.675  -0.843  1.00 28.27  ? 23  ARG A CD  1 
ATOM   157   N  NE  . ARG A 1 23  ? 30.435  -8.490  -0.048  1.00 29.45  ? 23  ARG A NE  1 
ATOM   158   C  CZ  . ARG A 1 23  ? 29.924  -9.646  -0.451  1.00 29.15  ? 23  ARG A CZ  1 
ATOM   159   N  NH1 . ARG A 1 23  ? 30.251  -10.184 -1.612  1.00 34.52  ? 23  ARG A NH1 1 
ATOM   160   N  NH2 . ARG A 1 23  ? 29.087  -10.311 0.342   1.00 33.88  ? 23  ARG A NH2 1 
ATOM   161   N  N   . GLU A 1 24  ? 35.528  -9.784  -2.245  1.00 26.07  ? 24  GLU A N   1 
ATOM   162   C  CA  . GLU A 1 24  ? 35.825  -11.224 -2.231  1.00 27.50  ? 24  GLU A CA  1 
ATOM   163   C  C   . GLU A 1 24  ? 37.193  -11.490 -1.621  1.00 28.24  ? 24  GLU A C   1 
ATOM   164   O  O   . GLU A 1 24  ? 37.360  -12.431 -0.817  1.00 28.49  ? 24  GLU A O   1 
ATOM   165   C  CB  . GLU A 1 24  ? 35.790  -11.802 -3.653  1.00 30.94  ? 24  GLU A CB  1 
ATOM   166   C  CG  . GLU A 1 24  ? 34.445  -11.859 -4.365  1.00 38.50  ? 24  GLU A CG  1 
ATOM   167   C  CD  . GLU A 1 24  ? 33.412  -12.856 -3.773  1.00 51.66  ? 24  GLU A CD  1 
ATOM   168   O  OE1 . GLU A 1 24  ? 33.776  -13.797 -3.022  1.00 51.46  ? 24  GLU A OE1 1 
ATOM   169   O  OE2 . GLU A 1 24  ? 32.210  -12.711 -4.104  1.00 56.49  ? 24  GLU A OE2 1 
ATOM   170   N  N   . GLN A 1 25  ? 38.182  -10.682 -2.003  1.00 27.09  ? 25  GLN A N   1 
ATOM   171   C  CA  . GLN A 1 25  ? 39.542  -10.838 -1.479  1.00 29.38  ? 25  GLN A CA  1 
ATOM   172   C  C   . GLN A 1 25  ? 39.575  -10.631 0.033   1.00 27.81  ? 25  GLN A C   1 
ATOM   173   O  O   . GLN A 1 25  ? 40.327  -11.306 0.753   1.00 29.22  ? 25  GLN A O   1 
ATOM   174   C  CB  . GLN A 1 25  ? 40.490  -9.843  -2.141  1.00 26.06  ? 25  GLN A CB  1 
ATOM   175   C  CG  . GLN A 1 25  ? 41.990  -10.263 -1.972  1.00 37.20  ? 25  GLN A CG  1 
ATOM   176   C  CD  . GLN A 1 25  ? 42.339  -11.614 -2.662  1.00 47.38  ? 25  GLN A CD  1 
ATOM   177   O  OE1 . GLN A 1 25  ? 42.823  -12.577 -2.031  1.00 50.10  ? 25  GLN A OE1 1 
ATOM   178   N  NE2 . GLN A 1 25  ? 42.195  -11.638 -3.973  1.00 46.30  ? 25  GLN A NE2 1 
ATOM   179   N  N   . TYR A 1 26  ? 38.828  -9.648  0.528   1.00 23.44  ? 26  TYR A N   1 
ATOM   180   C  CA  . TYR A 1 26  ? 38.779  -9.433  1.983   1.00 21.66  ? 26  TYR A CA  1 
ATOM   181   C  C   . TYR A 1 26  ? 38.356  -10.695 2.719   1.00 25.02  ? 26  TYR A C   1 
ATOM   182   O  O   . TYR A 1 26  ? 39.022  -11.108 3.670   1.00 23.20  ? 26  TYR A O   1 
ATOM   183   C  CB  . TYR A 1 26  ? 37.867  -8.258  2.275   1.00 23.43  ? 26  TYR A CB  1 
ATOM   184   C  CG  . TYR A 1 26  ? 37.467  -8.128  3.715   1.00 23.42  ? 26  TYR A CG  1 
ATOM   185   C  CD1 . TYR A 1 26  ? 38.271  -7.369  4.619   1.00 21.48  ? 26  TYR A CD1 1 
ATOM   186   C  CD2 . TYR A 1 26  ? 36.272  -8.717  4.182   1.00 21.01  ? 26  TYR A CD2 1 
ATOM   187   C  CE1 . TYR A 1 26  ? 37.927  -7.203  5.939   1.00 22.40  ? 26  TYR A CE1 1 
ATOM   188   C  CE2 . TYR A 1 26  ? 35.864  -8.534  5.549   1.00 22.46  ? 26  TYR A CE2 1 
ATOM   189   C  CZ  . TYR A 1 26  ? 36.691  -7.751  6.415   1.00 22.40  ? 26  TYR A CZ  1 
ATOM   190   O  OH  . TYR A 1 26  ? 36.303  -7.587  7.745   1.00 23.26  ? 26  TYR A OH  1 
ATOM   191   N  N   . TYR A 1 27  ? 37.272  -11.345 2.269   1.00 25.20  ? 27  TYR A N   1 
ATOM   192   C  CA  . TYR A 1 27  ? 36.770  -12.542 2.943   1.00 25.38  ? 27  TYR A CA  1 
ATOM   193   C  C   . TYR A 1 27  ? 37.726  -13.706 2.755   1.00 27.58  ? 27  TYR A C   1 
ATOM   194   O  O   . TYR A 1 27  ? 37.909  -14.519 3.671   1.00 26.27  ? 27  TYR A O   1 
ATOM   195   C  CB  . TYR A 1 27  ? 35.360  -12.895 2.437   1.00 22.38  ? 27  TYR A CB  1 
ATOM   196   C  CG  . TYR A 1 27  ? 34.345  -11.891 2.969   1.00 25.28  ? 27  TYR A CG  1 
ATOM   197   C  CD1 . TYR A 1 27  ? 34.095  -11.801 4.354   1.00 24.48  ? 27  TYR A CD1 1 
ATOM   198   C  CD2 . TYR A 1 27  ? 33.678  -11.009 2.126   1.00 25.95  ? 27  TYR A CD2 1 
ATOM   199   C  CE1 . TYR A 1 27  ? 33.168  -10.887 4.898   1.00 22.80  ? 27  TYR A CE1 1 
ATOM   200   C  CE2 . TYR A 1 27  ? 32.732  -10.081 2.654   1.00 23.23  ? 27  TYR A CE2 1 
ATOM   201   C  CZ  . TYR A 1 27  ? 32.471  -10.050 4.035   1.00 22.18  ? 27  TYR A CZ  1 
ATOM   202   O  OH  . TYR A 1 27  ? 31.568  -9.194  4.613   1.00 24.24  ? 27  TYR A OH  1 
ATOM   203   N  N   A MET A 1 28  ? 38.325  -13.834 1.569   0.54 26.79  ? 28  MET A N   1 
ATOM   204   N  N   B MET A 1 28  ? 38.316  -13.845 1.556   0.46 26.79  ? 28  MET A N   1 
ATOM   205   C  CA  A MET A 1 28  ? 39.283  -14.915 1.386   0.54 28.23  ? 28  MET A CA  1 
ATOM   206   C  CA  B MET A 1 28  ? 39.312  -14.899 1.347   0.46 28.24  ? 28  MET A CA  1 
ATOM   207   C  C   A MET A 1 28  ? 40.544  -14.687 2.231   0.54 28.42  ? 28  MET A C   1 
ATOM   208   C  C   B MET A 1 28  ? 40.567  -14.685 2.196   0.46 28.43  ? 28  MET A C   1 
ATOM   209   O  O   A MET A 1 28  ? 41.054  -15.624 2.857   0.54 29.94  ? 28  MET A O   1 
ATOM   210   O  O   B MET A 1 28  ? 41.111  -15.642 2.761   0.46 29.97  ? 28  MET A O   1 
ATOM   211   C  CB  A MET A 1 28  ? 39.574  -15.070 -0.109  0.54 31.90  ? 28  MET A CB  1 
ATOM   212   C  CB  B MET A 1 28  ? 39.640  -15.009 -0.147  0.46 31.89  ? 28  MET A CB  1 
ATOM   213   C  CG  A MET A 1 28  ? 38.904  -16.290 -0.788  0.54 35.82  ? 28  MET A CG  1 
ATOM   214   C  CG  B MET A 1 28  ? 40.328  -16.294 -0.553  0.46 36.33  ? 28  MET A CG  1 
ATOM   215   S  SD  A MET A 1 28  ? 37.339  -17.050 -0.178  0.54 42.10  ? 28  MET A SD  1 
ATOM   216   S  SD  B MET A 1 28  ? 41.202  -16.067 -2.110  0.46 44.41  ? 28  MET A SD  1 
ATOM   217   C  CE  A MET A 1 28  ? 37.882  -18.124 1.159   0.54 34.54  ? 28  MET A CE  1 
ATOM   218   C  CE  B MET A 1 28  ? 42.873  -15.707 -1.618  0.46 39.45  ? 28  MET A CE  1 
ATOM   219   N  N   . ASN A 1 29  ? 41.039  -13.447 2.307   1.00 27.52  ? 29  ASN A N   1 
ATOM   220   C  CA  . ASN A 1 29  ? 42.207  -13.175 3.150   1.00 26.50  ? 29  ASN A CA  1 
ATOM   221   C  C   . ASN A 1 29  ? 41.934  -13.520 4.620   1.00 27.86  ? 29  ASN A C   1 
ATOM   222   O  O   . ASN A 1 29  ? 42.828  -14.017 5.322   1.00 28.17  ? 29  ASN A O   1 
ATOM   223   C  CB  . ASN A 1 29  ? 42.594  -11.697 3.060   1.00 27.39  ? 29  ASN A CB  1 
ATOM   224   C  CG  . ASN A 1 29  ? 43.227  -11.343 1.725   1.00 28.36  ? 29  ASN A CG  1 
ATOM   225   O  OD1 . ASN A 1 29  ? 43.726  -12.202 1.003   1.00 35.07  ? 29  ASN A OD1 1 
ATOM   226   N  ND2 . ASN A 1 29  ? 43.188  -10.051 1.392   1.00 37.69  ? 29  ASN A ND2 1 
ATOM   227   N  N   . TYR A 1 30  ? 40.719  -13.271 5.107   1.00 26.04  ? 30  TYR A N   1 
ATOM   228   C  CA  . TYR A 1 30  ? 40.442  -13.647 6.505   1.00 23.73  ? 30  TYR A CA  1 
ATOM   229   C  C   . TYR A 1 30  ? 40.568  -15.154 6.677   1.00 26.33  ? 30  TYR A C   1 
ATOM   230   O  O   . TYR A 1 30  ? 41.214  -15.646 7.624   1.00 27.90  ? 30  TYR A O   1 
ATOM   231   C  CB  . TYR A 1 30  ? 39.047  -13.197 6.917   1.00 22.25  ? 30  TYR A CB  1 
ATOM   232   C  CG  . TYR A 1 30  ? 38.710  -13.452 8.373   1.00 24.91  ? 30  TYR A CG  1 
ATOM   233   C  CD1 . TYR A 1 30  ? 39.230  -12.625 9.383   1.00 25.25  ? 30  TYR A CD1 1 
ATOM   234   C  CD2 . TYR A 1 30  ? 37.861  -14.489 8.734   1.00 25.03  ? 30  TYR A CD2 1 
ATOM   235   C  CE1 . TYR A 1 30  ? 38.890  -12.832 10.724  1.00 24.72  ? 30  TYR A CE1 1 
ATOM   236   C  CE2 . TYR A 1 30  ? 37.528  -14.707 10.096  1.00 27.78  ? 30  TYR A CE2 1 
ATOM   237   C  CZ  . TYR A 1 30  ? 38.063  -13.857 11.064  1.00 27.14  ? 30  TYR A CZ  1 
ATOM   238   O  OH  . TYR A 1 30  ? 37.775  -14.049 12.414  1.00 34.11  ? 30  TYR A OH  1 
ATOM   239   N  N   . ALA A 1 31  ? 39.983  -15.911 5.744   1.00 25.84  ? 31  ALA A N   1 
ATOM   240   C  CA  . ALA A 1 31  ? 40.031  -17.368 5.846   1.00 28.13  ? 31  ALA A CA  1 
ATOM   241   C  C   . ALA A 1 31  ? 41.456  -17.912 5.737   1.00 29.24  ? 31  ALA A C   1 
ATOM   242   O  O   . ALA A 1 31  ? 41.784  -18.921 6.380   1.00 30.25  ? 31  ALA A O   1 
ATOM   243   C  CB  . ALA A 1 31  ? 39.119  -17.999 4.803   1.00 29.22  ? 31  ALA A CB  1 
ATOM   244   N  N   . ARG A 1 32  ? 42.296  -17.309 4.896   1.00 25.77  ? 32  ARG A N   1 
ATOM   245   C  CA  . ARG A 1 32  ? 43.661  -17.768 4.685   1.00 29.41  ? 32  ARG A CA  1 
ATOM   246   C  C   . ARG A 1 32  ? 44.706  -17.078 5.540   1.00 27.78  ? 32  ARG A C   1 
ATOM   247   O  O   . ARG A 1 32  ? 45.915  -17.277 5.302   1.00 30.65  ? 32  ARG A O   1 
ATOM   248   C  CB  . ARG A 1 32  ? 44.041  -17.652 3.199   1.00 35.31  ? 32  ARG A CB  1 
ATOM   249   C  CG  . ARG A 1 32  ? 42.984  -18.240 2.273   1.00 36.90  ? 32  ARG A CG  1 
ATOM   250   C  CD  . ARG A 1 32  ? 43.344  -18.056 0.828   1.00 37.93  ? 32  ARG A CD  1 
ATOM   251   N  NE  . ARG A 1 32  ? 44.552  -18.812 0.533   1.00 49.97  ? 32  ARG A NE  1 
ATOM   252   C  CZ  . ARG A 1 32  ? 45.260  -18.721 -0.585  1.00 50.58  ? 32  ARG A CZ  1 
ATOM   253   N  NH1 . ARG A 1 32  ? 44.890  -17.925 -1.574  1.00 54.55  ? 32  ARG A NH1 1 
ATOM   254   N  NH2 . ARG A 1 32  ? 46.361  -19.454 -0.712  1.00 47.64  ? 32  ARG A NH2 1 
ATOM   255   N  N   . ALA A 1 33  ? 44.282  -16.319 6.568   1.00 28.35  ? 33  ALA A N   1 
ATOM   256   C  CA  . ALA A 1 33  ? 45.200  -15.492 7.346   1.00 30.69  ? 33  ALA A CA  1 
ATOM   257   C  C   . ALA A 1 33  ? 46.387  -16.276 7.899   1.00 30.90  ? 33  ALA A C   1 
ATOM   258   O  O   . ALA A 1 33  ? 47.499  -15.751 7.980   1.00 31.63  ? 33  ALA A O   1 
ATOM   259   C  CB  . ALA A 1 33  ? 44.427  -14.845 8.497   1.00 28.09  ? 33  ALA A CB  1 
ATOM   260   N  N   . LYS A 1 34  ? 46.168  -17.516 8.346   1.00 28.35  ? 34  LYS A N   1 
ATOM   261   C  CA  . LYS A 1 34  ? 47.236  -18.250 9.035   1.00 32.66  ? 34  LYS A CA  1 
ATOM   262   C  C   . LYS A 1 34  ? 48.207  -18.945 8.104   1.00 33.54  ? 34  LYS A C   1 
ATOM   263   O  O   . LYS A 1 34  ? 49.276  -19.376 8.567   1.00 33.92  ? 34  LYS A O   1 
ATOM   264   C  CB  . LYS A 1 34  ? 46.618  -19.293 9.972   1.00 32.93  ? 34  LYS A CB  1 
ATOM   265   C  CG  . LYS A 1 34  ? 45.830  -18.628 11.073  1.00 29.62  ? 34  LYS A CG  1 
ATOM   266   C  CD  . LYS A 1 34  ? 46.728  -17.680 11.886  1.00 32.18  ? 34  LYS A CD  1 
ATOM   267   C  CE  . LYS A 1 34  ? 45.971  -16.956 13.026  1.00 31.25  ? 34  LYS A CE  1 
ATOM   268   N  NZ  . LYS A 1 34  ? 46.888  -16.137 13.932  1.00 29.58  ? 34  LYS A NZ  1 
ATOM   269   N  N   . GLU A 1 35  ? 47.892  -19.051 6.808   1.00 31.31  ? 35  GLU A N   1 
ATOM   270   C  CA  . GLU A 1 35  ? 48.839  -19.681 5.880   1.00 34.92  ? 35  GLU A CA  1 
ATOM   271   C  C   . GLU A 1 35  ? 50.234  -19.070 5.960   1.00 34.02  ? 35  GLU A C   1 
ATOM   272   O  O   . GLU A 1 35  ? 51.236  -19.775 5.808   1.00 31.94  ? 35  GLU A O   1 
ATOM   273   C  CB  . GLU A 1 35  ? 48.307  -19.614 4.453   1.00 34.36  ? 35  GLU A CB  1 
ATOM   274   C  CG  . GLU A 1 35  ? 47.041  -20.474 4.286   1.00 38.22  ? 35  GLU A CG  1 
ATOM   275   C  CD  . GLU A 1 35  ? 46.472  -20.447 2.876   1.00 43.80  ? 35  GLU A CD  1 
ATOM   276   O  OE1 . GLU A 1 35  ? 47.179  -19.956 1.956   1.00 47.03  ? 35  GLU A OE1 1 
ATOM   277   O  OE2 . GLU A 1 35  ? 45.307  -20.886 2.712   1.00 41.62  ? 35  GLU A OE2 1 
ATOM   278   N  N   . LYS A 1 36  ? 50.331  -17.765 6.179   1.00 31.42  ? 36  LYS A N   1 
ATOM   279   C  CA  . LYS A 1 36  ? 51.620  -17.093 6.277   1.00 30.21  ? 36  LYS A CA  1 
ATOM   280   C  C   . LYS A 1 36  ? 51.780  -16.400 7.641   1.00 32.38  ? 36  LYS A C   1 
ATOM   281   O  O   . LYS A 1 36  ? 52.520  -15.415 7.774   1.00 31.89  ? 36  LYS A O   1 
ATOM   282   C  CB  . LYS A 1 36  ? 51.751  -16.071 5.144   1.00 32.35  ? 36  LYS A CB  1 
ATOM   283   C  CG  . LYS A 1 36  ? 51.938  -16.662 3.757   1.00 36.28  ? 36  LYS A CG  1 
ATOM   284   C  CD  . LYS A 1 36  ? 52.913  -17.881 3.701   1.00 45.83  ? 36  LYS A CD  1 
ATOM   285   C  CE  . LYS A 1 36  ? 54.387  -17.544 4.127   1.00 40.51  ? 36  LYS A CE  1 
ATOM   286   N  NZ  . LYS A 1 36  ? 55.385  -18.629 3.769   1.00 44.22  ? 36  LYS A NZ  1 
ATOM   287   N  N   . GLY A 1 37  ? 51.107  -16.923 8.660   1.00 30.86  ? 37  GLY A N   1 
ATOM   288   C  CA  . GLY A 1 37  ? 51.261  -16.450 10.012  1.00 28.06  ? 37  GLY A CA  1 
ATOM   289   C  C   . GLY A 1 37  ? 50.656  -15.080 10.239  1.00 27.95  ? 37  GLY A C   1 
ATOM   290   O  O   . GLY A 1 37  ? 51.111  -14.365 11.118  1.00 26.48  ? 37  GLY A O   1 
ATOM   291   N  N   . GLY A 1 38  ? 49.572  -14.744 9.529   1.00 26.31  ? 38  GLY A N   1 
ATOM   292   C  CA  . GLY A 1 38  ? 48.856  -13.504 9.746   1.00 28.60  ? 38  GLY A CA  1 
ATOM   293   C  C   . GLY A 1 38  ? 48.038  -13.545 11.015  1.00 29.21  ? 38  GLY A C   1 
ATOM   294   O  O   . GLY A 1 38  ? 47.953  -14.559 11.710  1.00 26.07  ? 38  GLY A O   1 
ATOM   295   N  N   . ILE A 1 39  ? 47.433  -12.397 11.323  1.00 23.40  ? 39  ILE A N   1 
ATOM   296   C  CA  . ILE A 1 39  ? 46.542  -12.219 12.473  1.00 24.63  ? 39  ILE A CA  1 
ATOM   297   C  C   . ILE A 1 39  ? 45.108  -12.088 11.950  1.00 24.47  ? 39  ILE A C   1 
ATOM   298   O  O   . ILE A 1 39  ? 44.876  -11.482 10.895  1.00 29.09  ? 39  ILE A O   1 
ATOM   299   C  CB  . ILE A 1 39  ? 46.930  -10.956 13.264  1.00 26.97  ? 39  ILE A CB  1 
ATOM   300   C  CG1 . ILE A 1 39  ? 48.301  -11.153 13.921  1.00 29.92  ? 39  ILE A CG1 1 
ATOM   301   C  CG2 . ILE A 1 39  ? 45.865  -10.624 14.377  1.00 29.23  ? 39  ILE A CG2 1 
ATOM   302   C  CD1 . ILE A 1 39  ? 48.803  -9.953  14.619  1.00 32.34  ? 39  ILE A CD1 1 
ATOM   303   N  N   . ARG A 1 40  ? 44.170  -12.682 12.656  1.00 22.94  ? 40  ARG A N   1 
ATOM   304   C  CA  . ARG A 1 40  ? 42.729  -12.561 12.413  1.00 25.65  ? 40  ARG A CA  1 
ATOM   305   C  C   . ARG A 1 40  ? 42.100  -11.916 13.636  1.00 25.48  ? 40  ARG A C   1 
ATOM   306   O  O   . ARG A 1 40  ? 42.377  -12.352 14.752  1.00 24.50  ? 40  ARG A O   1 
ATOM   307   C  CB  . ARG A 1 40  ? 42.037  -13.929 12.298  1.00 25.70  ? 40  ARG A CB  1 
ATOM   308   C  CG  . ARG A 1 40  ? 42.275  -14.678 11.092  1.00 28.35  ? 40  ARG A CG  1 
ATOM   309   C  CD  . ARG A 1 40  ? 41.190  -15.738 10.940  1.00 28.29  ? 40  ARG A CD  1 
ATOM   310   N  NE  . ARG A 1 40  ? 41.612  -16.960 11.576  1.00 38.63  ? 40  ARG A NE  1 
ATOM   311   C  CZ  . ARG A 1 40  ? 42.008  -18.047 10.931  1.00 34.22  ? 40  ARG A CZ  1 
ATOM   312   N  NH1 . ARG A 1 40  ? 42.155  -18.059 9.613   1.00 34.46  ? 40  ARG A NH1 1 
ATOM   313   N  NH2 . ARG A 1 40  ? 42.313  -19.131 11.626  1.00 35.05  ? 40  ARG A NH2 1 
ATOM   314   N  N   . TRP A 1 41  ? 41.189  -10.960 13.449  1.00 24.25  ? 41  TRP A N   1 
ATOM   315   C  CA  . TRP A 1 41  ? 40.379  -10.481 14.559  1.00 22.21  ? 41  TRP A CA  1 
ATOM   316   C  C   . TRP A 1 41  ? 38.956  -10.202 14.094  1.00 21.57  ? 41  TRP A C   1 
ATOM   317   O  O   . TRP A 1 41  ? 38.707  -10.015 12.902  1.00 23.65  ? 41  TRP A O   1 
ATOM   318   C  CB  . TRP A 1 41  ? 41.015  -9.234  15.210  1.00 23.80  ? 41  TRP A CB  1 
ATOM   319   C  CG  . TRP A 1 41  ? 41.112  -8.066  14.312  1.00 23.47  ? 41  TRP A CG  1 
ATOM   320   C  CD1 . TRP A 1 41  ? 42.137  -7.737  13.467  1.00 23.73  ? 41  TRP A CD1 1 
ATOM   321   C  CD2 . TRP A 1 41  ? 40.139  -6.991  14.217  1.00 25.30  ? 41  TRP A CD2 1 
ATOM   322   N  NE1 . TRP A 1 41  ? 41.837  -6.525  12.813  1.00 24.58  ? 41  TRP A NE1 1 
ATOM   323   C  CE2 . TRP A 1 41  ? 40.627  -6.058  13.279  1.00 24.74  ? 41  TRP A CE2 1 
ATOM   324   C  CE3 . TRP A 1 41  ? 38.901  -6.759  14.840  1.00 22.84  ? 41  TRP A CE3 1 
ATOM   325   C  CZ2 . TRP A 1 41  ? 39.898  -4.895  12.919  1.00 22.80  ? 41  TRP A CZ2 1 
ATOM   326   C  CZ3 . TRP A 1 41  ? 38.181  -5.607  14.515  1.00 27.88  ? 41  TRP A CZ3 1 
ATOM   327   C  CH2 . TRP A 1 41  ? 38.679  -4.686  13.560  1.00 24.07  ? 41  TRP A CH2 1 
ATOM   328   N  N   . SER A 1 42  ? 38.010  -10.158 15.040  1.00 20.32  ? 42  SER A N   1 
ATOM   329   C  CA  . SER A 1 42  ? 36.630  -9.881  14.654  1.00 19.05  ? 42  SER A CA  1 
ATOM   330   C  C   . SER A 1 42  ? 36.052  -8.773  15.525  1.00 22.94  ? 42  SER A C   1 
ATOM   331   O  O   . SER A 1 42  ? 36.398  -8.608  16.702  1.00 23.35  ? 42  SER A O   1 
ATOM   332   C  CB  . SER A 1 42  ? 35.717  -11.109 14.721  1.00 28.29  ? 42  SER A CB  1 
ATOM   333   O  OG  . SER A 1 42  ? 35.885  -11.755 15.964  1.00 37.80  ? 42  SER A OG  1 
ATOM   334   N  N   . GLY A 1 43  ? 35.040  -8.130  14.980  1.00 21.91  ? 43  GLY A N   1 
ATOM   335   C  CA  . GLY A 1 43  ? 34.399  -7.009  15.654  1.00 20.62  ? 43  GLY A CA  1 
ATOM   336   C  C   . GLY A 1 43  ? 33.494  -6.336  14.645  1.00 22.06  ? 43  GLY A C   1 
ATOM   337   O  O   . GLY A 1 43  ? 33.470  -6.698  13.451  1.00 21.02  ? 43  GLY A O   1 
ATOM   338   N  N   . SER A 1 44  ? 32.825  -5.300  15.115  1.00 21.41  ? 44  SER A N   1 
ATOM   339   C  CA  . SER A 1 44  ? 31.868  -4.572  14.315  1.00 19.61  ? 44  SER A CA  1 
ATOM   340   C  C   . SER A 1 44  ? 32.581  -3.840  13.164  1.00 19.91  ? 44  SER A C   1 
ATOM   341   O  O   . SER A 1 44  ? 33.790  -3.502  13.205  1.00 19.98  ? 44  SER A O   1 
ATOM   342   C  CB  . SER A 1 44  ? 31.145  -3.511  15.170  1.00 20.54  ? 44  SER A CB  1 
ATOM   343   O  OG  . SER A 1 44  ? 30.344  -2.625  14.434  1.00 20.56  ? 44  SER A OG  1 
ATOM   344   N  N   . ALA A 1 45  ? 31.806  -3.576  12.137  1.00 19.34  ? 45  ALA A N   1 
ATOM   345   C  CA  . ALA A 1 45  ? 32.216  -2.557  11.164  1.00 19.97  ? 45  ALA A CA  1 
ATOM   346   C  C   . ALA A 1 45  ? 32.525  -1.219  11.793  1.00 23.94  ? 45  ALA A C   1 
ATOM   347   O  O   . ALA A 1 45  ? 33.200  -0.404  11.162  1.00 23.75  ? 45  ALA A O   1 
ATOM   348   C  CB  . ALA A 1 45  ? 31.125  -2.319  10.177  1.00 21.20  ? 45  ALA A CB  1 
ATOM   349   N  N   . TRP A 1 46  ? 32.021  -0.945  12.979  1.00 20.03  ? 46  TRP A N   1 
ATOM   350   C  CA  . TRP A 1 46  ? 32.327  0.289   13.676  1.00 21.66  ? 46  TRP A CA  1 
ATOM   351   C  C   . TRP A 1 46  ? 33.547  0.150   14.580  1.00 22.78  ? 46  TRP A C   1 
ATOM   352   O  O   . TRP A 1 46  ? 33.850  1.070   15.339  1.00 19.09  ? 46  TRP A O   1 
ATOM   353   C  CB  . TRP A 1 46  ? 31.100  0.695   14.484  1.00 21.23  ? 46  TRP A CB  1 
ATOM   354   C  CG  . TRP A 1 46  ? 30.067  1.346   13.679  1.00 20.29  ? 46  TRP A CG  1 
ATOM   355   C  CD1 . TRP A 1 46  ? 30.196  1.894   12.414  1.00 20.63  ? 46  TRP A CD1 1 
ATOM   356   C  CD2 . TRP A 1 46  ? 28.681  1.498   14.048  1.00 21.49  ? 46  TRP A CD2 1 
ATOM   357   N  NE1 . TRP A 1 46  ? 28.966  2.448   12.016  1.00 22.33  ? 46  TRP A NE1 1 
ATOM   358   C  CE2 . TRP A 1 46  ? 28.043  2.246   13.020  1.00 22.12  ? 46  TRP A CE2 1 
ATOM   359   C  CE3 . TRP A 1 46  ? 27.956  1.208   15.231  1.00 20.56  ? 46  TRP A CE3 1 
ATOM   360   C  CZ2 . TRP A 1 46  ? 26.689  2.608   13.078  1.00 23.40  ? 46  TRP A CZ2 1 
ATOM   361   C  CZ3 . TRP A 1 46  ? 26.635  1.577   15.307  1.00 19.74  ? 46  TRP A CZ3 1 
ATOM   362   C  CH2 . TRP A 1 46  ? 26.007  2.278   14.238  1.00 24.24  ? 46  TRP A CH2 1 
ATOM   363   N  N   . ALA A 1 47  ? 34.166  -1.027  14.640  1.00 17.94  ? 47  ALA A N   1 
ATOM   364   C  CA  . ALA A 1 47  ? 35.423  -1.149  15.396  1.00 18.33  ? 47  ALA A CA  1 
ATOM   365   C  C   . ALA A 1 47  ? 36.427  -0.151  14.848  1.00 20.00  ? 47  ALA A C   1 
ATOM   366   O  O   . ALA A 1 47  ? 36.431  0.169   13.656  1.00 21.67  ? 47  ALA A O   1 
ATOM   367   C  CB  . ALA A 1 47  ? 35.991  -2.590  15.248  1.00 20.62  ? 47  ALA A CB  1 
ATOM   368   N  N   . LEU A 1 48  ? 37.327  0.298   15.712  1.00 20.40  ? 48  LEU A N   1 
ATOM   369   C  CA  . LEU A 1 48  ? 38.373  1.237   15.301  1.00 21.23  ? 48  LEU A CA  1 
ATOM   370   C  C   . LEU A 1 48  ? 39.571  0.431   14.790  1.00 20.12  ? 48  LEU A C   1 
ATOM   371   O  O   . LEU A 1 48  ? 40.602  0.257   15.447  1.00 20.12  ? 48  LEU A O   1 
ATOM   372   C  CB  . LEU A 1 48  ? 38.713  2.196   16.445  1.00 21.51  ? 48  LEU A CB  1 
ATOM   373   C  CG  . LEU A 1 48  ? 37.961  3.545   16.298  1.00 23.16  ? 48  LEU A CG  1 
ATOM   374   C  CD1 . LEU A 1 48  ? 36.426  3.346   16.359  1.00 22.01  ? 48  LEU A CD1 1 
ATOM   375   C  CD2 . LEU A 1 48  ? 38.395  4.601   17.291  1.00 22.70  ? 48  LEU A CD2 1 
ATOM   376   N  N   . ASP A 1 49  ? 39.458  0.021   13.537  1.00 21.77  ? 49  ASP A N   1 
ATOM   377   C  CA  . ASP A 1 49  ? 40.350  -0.956  12.934  1.00 20.89  ? 49  ASP A CA  1 
ATOM   378   C  C   . ASP A 1 49  ? 41.763  -0.482  12.630  1.00 21.27  ? 49  ASP A C   1 
ATOM   379   O  O   . ASP A 1 49  ? 42.641  -1.337  12.448  1.00 22.30  ? 49  ASP A O   1 
ATOM   380   C  CB  . ASP A 1 49  ? 39.659  -1.553  11.709  1.00 25.09  ? 49  ASP A CB  1 
ATOM   381   C  CG  . ASP A 1 49  ? 39.176  -0.518  10.749  1.00 24.60  ? 49  ASP A CG  1 
ATOM   382   O  OD1 . ASP A 1 49  ? 38.046  -0.001  10.969  1.00 27.92  ? 49  ASP A OD1 1 
ATOM   383   O  OD2 . ASP A 1 49  ? 39.788  -0.332  9.694   1.00 23.52  ? 49  ASP A OD2 1 
ATOM   384   N  N   . ALA A 1 50  ? 42.061  0.827   12.687  1.00 20.37  ? 50  ALA A N   1 
ATOM   385   C  CA  . ALA A 1 50  ? 43.472  1.192   12.646  1.00 19.71  ? 50  ALA A CA  1 
ATOM   386   C  C   . ALA A 1 50  ? 44.267  0.697   13.842  1.00 19.27  ? 50  ALA A C   1 
ATOM   387   O  O   . ALA A 1 50  ? 45.514  0.664   13.743  1.00 21.54  ? 50  ALA A O   1 
ATOM   388   C  CB  . ALA A 1 50  ? 43.626  2.734   12.601  1.00 18.32  ? 50  ALA A CB  1 
ATOM   389   N  N   . ILE A 1 51  ? 43.643  0.434   15.010  1.00 20.86  ? 51  ILE A N   1 
ATOM   390   C  CA  . ILE A 1 51  ? 44.436  0.005   16.168  1.00 20.24  ? 51  ILE A CA  1 
ATOM   391   C  C   . ILE A 1 51  ? 45.017  -1.379  15.867  1.00 20.43  ? 51  ILE A C   1 
ATOM   392   O  O   . ILE A 1 51  ? 46.248  -1.542  15.951  1.00 23.19  ? 51  ILE A O   1 
ATOM   393   C  CB  . ILE A 1 51  ? 43.624  0.011   17.491  1.00 19.17  ? 51  ILE A CB  1 
ATOM   394   C  CG1 . ILE A 1 51  ? 43.205  1.450   17.865  1.00 23.03  ? 51  ILE A CG1 1 
ATOM   395   C  CG2 . ILE A 1 51  ? 44.486  -0.609  18.607  1.00 23.40  ? 51  ILE A CG2 1 
ATOM   396   C  CD1 . ILE A 1 51  ? 44.284  2.219   18.400  1.00 22.75  ? 51  ILE A CD1 1 
ATOM   397   N  N   . PRO A 1 52  ? 44.216  -2.391  15.507  1.00 23.18  ? 52  PRO A N   1 
ATOM   398   C  CA  . PRO A 1 52  ? 44.822  -3.673  15.070  1.00 24.15  ? 52  PRO A CA  1 
ATOM   399   C  C   . PRO A 1 52  ? 45.780  -3.537  13.876  1.00 24.81  ? 52  PRO A C   1 
ATOM   400   O  O   . PRO A 1 52  ? 46.784  -4.271  13.818  1.00 25.19  ? 52  PRO A O   1 
ATOM   401   C  CB  . PRO A 1 52  ? 43.608  -4.547  14.712  1.00 24.90  ? 52  PRO A CB  1 
ATOM   402   C  CG  . PRO A 1 52  ? 42.487  -3.993  15.428  1.00 26.27  ? 52  PRO A CG  1 
ATOM   403   C  CD  . PRO A 1 52  ? 42.745  -2.488  15.578  1.00 21.10  ? 52  PRO A CD  1 
ATOM   404   N  N   . ALA A 1 53  ? 45.562  -2.557  12.964  1.00 23.04  ? 53  ALA A N   1 
ATOM   405   C  CA  . ALA A 1 53  ? 46.479  -2.342  11.843  1.00 24.73  ? 53  ALA A CA  1 
ATOM   406   C  C   . ALA A 1 53  ? 47.908  -1.952  12.289  1.00 24.92  ? 53  ALA A C   1 
ATOM   407   O  O   . ALA A 1 53  ? 48.873  -2.088  11.509  1.00 25.65  ? 53  ALA A O   1 
ATOM   408   C  CB  . ALA A 1 53  ? 45.913  -1.278  10.898  1.00 21.54  ? 53  ALA A CB  1 
ATOM   409   N  N   . GLY A 1 54  ? 48.064  -1.459  13.517  1.00 21.64  ? 54  GLY A N   1 
ATOM   410   C  CA  . GLY A 1 54  ? 49.423  -1.153  13.931  1.00 22.08  ? 54  GLY A CA  1 
ATOM   411   C  C   . GLY A 1 54  ? 50.259  -2.386  14.145  1.00 23.31  ? 54  GLY A C   1 
ATOM   412   O  O   . GLY A 1 54  ? 51.459  -2.274  14.391  1.00 25.83  ? 54  GLY A O   1 
ATOM   413   N  N   . LEU A 1 55  ? 49.641  -3.538  14.107  1.00 23.21  ? 55  LEU A N   1 
ATOM   414   C  CA  . LEU A 1 55  ? 50.325  -4.793  14.318  1.00 24.01  ? 55  LEU A CA  1 
ATOM   415   C  C   . LEU A 1 55  ? 50.839  -5.407  13.017  1.00 27.56  ? 55  LEU A C   1 
ATOM   416   O  O   . LEU A 1 55  ? 51.469  -6.473  13.054  1.00 26.15  ? 55  LEU A O   1 
ATOM   417   C  CB  . LEU A 1 55  ? 49.363  -5.771  14.976  1.00 24.59  ? 55  LEU A CB  1 
ATOM   418   C  CG  . LEU A 1 55  ? 48.796  -5.460  16.358  1.00 26.04  ? 55  LEU A CG  1 
ATOM   419   C  CD1 . LEU A 1 55  ? 47.922  -6.665  16.780  1.00 23.86  ? 55  LEU A CD1 1 
ATOM   420   C  CD2 . LEU A 1 55  ? 49.874  -5.223  17.343  1.00 25.42  ? 55  LEU A CD2 1 
ATOM   421   N  N   . GLY A 1 56  ? 50.613  -4.764  11.875  1.00 27.44  ? 56  GLY A N   1 
ATOM   422   C  CA  . GLY A 1 56  ? 51.188  -5.257  10.641  1.00 25.06  ? 56  GLY A CA  1 
ATOM   423   C  C   . GLY A 1 56  ? 50.244  -5.150  9.469   1.00 28.33  ? 56  GLY A C   1 
ATOM   424   O  O   . GLY A 1 56  ? 49.046  -4.890  9.666   1.00 27.45  ? 56  GLY A O   1 
ATOM   425   N  N   . GLU A 1 57  ? 50.781  -5.341  8.254   1.00 29.21  ? 57  GLU A N   1 
ATOM   426   C  CA  . GLU A 1 57  ? 50.010  -5.381  7.023   1.00 32.25  ? 57  GLU A CA  1 
ATOM   427   C  C   . GLU A 1 57  ? 49.280  -6.688  6.818   1.00 32.47  ? 57  GLU A C   1 
ATOM   428   O  O   . GLU A 1 57  ? 48.449  -6.769  5.912   1.00 35.04  ? 57  GLU A O   1 
ATOM   429   C  CB  . GLU A 1 57  ? 50.904  -5.180  5.793   1.00 32.61  ? 57  GLU A CB  1 
ATOM   430   C  CG  . GLU A 1 57  ? 52.014  -4.195  5.930   1.00 42.03  ? 57  GLU A CG  1 
ATOM   431   C  CD  . GLU A 1 57  ? 51.483  -2.801  5.769   1.00 45.13  ? 57  GLU A CD  1 
ATOM   432   O  OE1 . GLU A 1 57  ? 52.260  -1.856  5.415   1.00 52.13  ? 57  GLU A OE1 1 
ATOM   433   O  OE2 . GLU A 1 57  ? 50.263  -2.653  6.016   1.00 45.67  ? 57  GLU A OE2 1 
ATOM   434   N  N   . ASP A 1 58  ? 49.555  -7.684  7.635   1.00 26.42  ? 58  ASP A N   1 
ATOM   435   C  CA  . ASP A 1 58  ? 48.943  -9.001  7.516   1.00 27.53  ? 58  ASP A CA  1 
ATOM   436   C  C   . ASP A 1 58  ? 47.973  -9.236  8.672   1.00 27.50  ? 58  ASP A C   1 
ATOM   437   O  O   . ASP A 1 58  ? 47.967  -10.296 9.278   1.00 26.17  ? 58  ASP A O   1 
ATOM   438   C  CB  . ASP A 1 58  ? 50.018  -10.068 7.467   1.00 28.28  ? 58  ASP A CB  1 
ATOM   439   C  CG  . ASP A 1 58  ? 50.881  -10.099 8.724   1.00 29.48  ? 58  ASP A CG  1 
ATOM   440   O  OD1 . ASP A 1 58  ? 51.021  -9.044  9.353   1.00 28.93  ? 58  ASP A OD1 1 
ATOM   441   O  OD2 . ASP A 1 58  ? 51.450  -11.165 9.057   1.00 28.37  ? 58  ASP A OD2 1 
ATOM   442   N  N   . VAL A 1 59  ? 47.146  -8.225  8.958   1.00 25.61  ? 59  VAL A N   1 
ATOM   443   C  CA  . VAL A 1 59  ? 46.166  -8.250  10.027  1.00 24.20  ? 59  VAL A CA  1 
ATOM   444   C  C   . VAL A 1 59  ? 44.817  -8.142  9.342   1.00 26.54  ? 59  VAL A C   1 
ATOM   445   O  O   . VAL A 1 59  ? 44.518  -7.126  8.687   1.00 26.62  ? 59  VAL A O   1 
ATOM   446   C  CB  . VAL A 1 59  ? 46.400  -7.108  11.024  1.00 28.86  ? 59  VAL A CB  1 
ATOM   447   C  CG1 . VAL A 1 59  ? 45.293  -7.116  12.147  1.00 26.47  ? 59  VAL A CG1 1 
ATOM   448   C  CG2 . VAL A 1 59  ? 47.823  -7.230  11.632  1.00 25.88  ? 59  VAL A CG2 1 
ATOM   449   N  N   . TYR A 1 60  ? 44.014  -9.172  9.481   1.00 23.23  ? 60  TYR A N   1 
ATOM   450   C  CA  . TYR A 1 60  ? 42.787  -9.314  8.713   1.00 24.38  ? 60  TYR A CA  1 
ATOM   451   C  C   . TYR A 1 60  ? 41.616  -9.370  9.663   1.00 26.70  ? 60  TYR A C   1 
ATOM   452   O  O   . TYR A 1 60  ? 41.567  -10.256 10.543  1.00 25.13  ? 60  TYR A O   1 
ATOM   453   C  CB  . TYR A 1 60  ? 42.828  -10.599 7.880   1.00 25.00  ? 60  TYR A CB  1 
ATOM   454   C  CG  . TYR A 1 60  ? 44.061  -10.651 7.012   1.00 26.21  ? 60  TYR A CG  1 
ATOM   455   C  CD1 . TYR A 1 60  ? 44.148  -9.909  5.834   1.00 30.32  ? 60  TYR A CD1 1 
ATOM   456   C  CD2 . TYR A 1 60  ? 45.163  -11.416 7.380   1.00 29.80  ? 60  TYR A CD2 1 
ATOM   457   C  CE1 . TYR A 1 60  ? 45.298  -9.937  5.054   1.00 32.55  ? 60  TYR A CE1 1 
ATOM   458   C  CE2 . TYR A 1 60  ? 46.328  -11.442 6.599   1.00 32.30  ? 60  TYR A CE2 1 
ATOM   459   C  CZ  . TYR A 1 60  ? 46.386  -10.700 5.438   1.00 33.77  ? 60  TYR A CZ  1 
ATOM   460   O  OH  . TYR A 1 60  ? 47.508  -10.751 4.657   1.00 38.20  ? 60  TYR A OH  1 
ATOM   461   N  N   . SER A 1 61  ? 40.648  -8.470  9.458   1.00 23.78  ? 61  SER A N   1 
ATOM   462   C  CA  . SER A 1 61  ? 39.410  -8.470  10.203  1.00 22.82  ? 61  SER A CA  1 
ATOM   463   C  C   . SER A 1 61  ? 38.323  -9.280  9.501   1.00 22.30  ? 61  SER A C   1 
ATOM   464   O  O   . SER A 1 61  ? 38.394  -9.592  8.300   1.00 22.65  ? 61  SER A O   1 
ATOM   465   C  CB  . SER A 1 61  ? 38.883  -7.034  10.413  1.00 23.57  ? 61  SER A CB  1 
ATOM   466   O  OG  . SER A 1 61  ? 38.372  -6.542  9.157   1.00 23.82  ? 61  SER A OG  1 
ATOM   467   N  N   . LEU A 1 62  ? 37.337  -9.663  10.287  1.00 19.67  ? 62  LEU A N   1 
ATOM   468   C  CA  . LEU A 1 62  ? 36.011  -10.043 9.801   1.00 18.79  ? 62  LEU A CA  1 
ATOM   469   C  C   . LEU A 1 62  ? 35.032  -9.176  10.550  1.00 21.81  ? 62  LEU A C   1 
ATOM   470   O  O   . LEU A 1 62  ? 34.860  -9.359  11.773  1.00 21.50  ? 62  LEU A O   1 
ATOM   471   C  CB  . LEU A 1 62  ? 35.742  -11.530 10.052  1.00 21.78  ? 62  LEU A CB  1 
ATOM   472   C  CG  . LEU A 1 62  ? 34.384  -11.981 9.524   1.00 19.62  ? 62  LEU A CG  1 
ATOM   473   C  CD1 . LEU A 1 62  ? 34.429  -12.073 7.964   1.00 21.24  ? 62  LEU A CD1 1 
ATOM   474   C  CD2 . LEU A 1 62  ? 33.997  -13.318 10.141  1.00 20.67  ? 62  LEU A CD2 1 
ATOM   475   N  N   . THR A 1 63  ? 34.416  -8.215  9.854   1.00 21.75  ? 63  THR A N   1 
ATOM   476   C  CA  . THR A 1 63  ? 33.463  -7.341  10.519  1.00 21.22  ? 63  THR A CA  1 
ATOM   477   C  C   . THR A 1 63  ? 32.084  -8.021  10.577  1.00 20.62  ? 63  THR A C   1 
ATOM   478   O  O   . THR A 1 63  ? 31.620  -8.647  9.607   1.00 19.99  ? 63  THR A O   1 
ATOM   479   C  CB  . THR A 1 63  ? 33.405  -5.970  9.824   1.00 20.78  ? 63  THR A CB  1 
ATOM   480   O  OG1 . THR A 1 63  ? 33.256  -6.139  8.402   1.00 20.91  ? 63  THR A OG1 1 
ATOM   481   C  CG2 . THR A 1 63  ? 34.748  -5.280  10.053  1.00 22.73  ? 63  THR A CG2 1 
ATOM   482   N  N   . GLY A 1 64  ? 31.462  -7.964  11.734  1.00 20.53  ? 64  GLY A N   1 
ATOM   483   C  CA  . GLY A 1 64  ? 30.357  -8.874  11.992  1.00 19.79  ? 64  GLY A CA  1 
ATOM   484   C  C   . GLY A 1 64  ? 29.090  -8.555  11.220  1.00 20.40  ? 64  GLY A C   1 
ATOM   485   O  O   . GLY A 1 64  ? 28.438  -9.451  10.715  1.00 20.66  ? 64  GLY A O   1 
ATOM   486   N  N   . GLU A 1 65  ? 28.718  -7.257  11.102  1.00 17.95  ? 65  GLU A N   1 
ATOM   487   C  CA  . GLU A 1 65  ? 27.452  -6.971  10.447  1.00 19.93  ? 65  GLU A CA  1 
ATOM   488   C  C   . GLU A 1 65  ? 27.513  -7.179  8.924   1.00 21.16  ? 65  GLU A C   1 
ATOM   489   O  O   . GLU A 1 65  ? 26.586  -7.772  8.355   1.00 20.32  ? 65  GLU A O   1 
ATOM   490   C  CB  . GLU A 1 65  ? 27.008  -5.530  10.761  1.00 21.56  ? 65  GLU A CB  1 
ATOM   491   C  CG  . GLU A 1 65  ? 26.970  -5.142  12.240  1.00 19.68  ? 65  GLU A CG  1 
ATOM   492   C  CD  . GLU A 1 65  ? 28.284  -4.683  12.784  1.00 20.70  ? 65  GLU A CD  1 
ATOM   493   O  OE1 . GLU A 1 65  ? 29.315  -4.720  12.029  1.00 22.87  ? 65  GLU A OE1 1 
ATOM   494   O  OE2 . GLU A 1 65  ? 28.259  -4.273  13.991  1.00 20.49  ? 65  GLU A OE2 1 
ATOM   495   N  N   . PRO A 1 66  ? 28.569  -6.738  8.215   1.00 19.26  ? 66  PRO A N   1 
ATOM   496   C  CA  . PRO A 1 66  ? 28.623  -7.040  6.769   1.00 19.36  ? 66  PRO A CA  1 
ATOM   497   C  C   . PRO A 1 66  ? 28.704  -8.525  6.488   1.00 20.84  ? 66  PRO A C   1 
ATOM   498   O  O   . PRO A 1 66  ? 28.113  -8.946  5.500   1.00 22.26  ? 66  PRO A O   1 
ATOM   499   C  CB  . PRO A 1 66  ? 29.890  -6.302  6.286   1.00 23.48  ? 66  PRO A CB  1 
ATOM   500   C  CG  . PRO A 1 66  ? 30.082  -5.170  7.371   1.00 18.05  ? 66  PRO A CG  1 
ATOM   501   C  CD  . PRO A 1 66  ? 29.717  -5.907  8.648   1.00 21.32  ? 66  PRO A CD  1 
ATOM   502   N  N   . TYR A 1 67  ? 29.405  -9.294  7.337   1.00 20.77  ? 67  TYR A N   1 
ATOM   503   C  CA  . TYR A 1 67  ? 29.469  -10.739 7.127   1.00 18.46  ? 67  TYR A CA  1 
ATOM   504   C  C   . TYR A 1 67  ? 28.073  -11.328 7.274   1.00 20.04  ? 67  TYR A C   1 
ATOM   505   O  O   . TYR A 1 67  ? 27.612  -12.079 6.398   1.00 20.88  ? 67  TYR A O   1 
ATOM   506   C  CB  . TYR A 1 67  ? 30.508  -11.349 8.091   1.00 19.01  ? 67  TYR A CB  1 
ATOM   507   C  CG  . TYR A 1 67  ? 30.491  -12.853 7.977   1.00 18.99  ? 67  TYR A CG  1 
ATOM   508   C  CD1 . TYR A 1 67  ? 30.931  -13.465 6.802   1.00 23.08  ? 67  TYR A CD1 1 
ATOM   509   C  CD2 . TYR A 1 67  ? 29.932  -13.621 8.975   1.00 20.35  ? 67  TYR A CD2 1 
ATOM   510   C  CE1 . TYR A 1 67  ? 30.865  -14.878 6.663   1.00 20.71  ? 67  TYR A CE1 1 
ATOM   511   C  CE2 . TYR A 1 67  ? 29.873  -15.051 8.847   1.00 20.47  ? 67  TYR A CE2 1 
ATOM   512   C  CZ  . TYR A 1 67  ? 30.336  -15.625 7.686   1.00 23.09  ? 67  TYR A CZ  1 
ATOM   513   O  OH  . TYR A 1 67  ? 30.220  -16.989 7.518   1.00 23.02  ? 67  TYR A OH  1 
ATOM   514   N  N   . ALA A 1 68  ? 27.368  -10.965 8.357   1.00 19.49  ? 68  ALA A N   1 
ATOM   515   C  CA  . ALA A 1 68  ? 26.004  -11.448 8.565   1.00 22.04  ? 68  ALA A CA  1 
ATOM   516   C  C   . ALA A 1 68  ? 25.093  -11.052 7.421   1.00 21.04  ? 68  ALA A C   1 
ATOM   517   O  O   . ALA A 1 68  ? 24.218  -11.841 7.026   1.00 22.93  ? 68  ALA A O   1 
ATOM   518   C  CB  . ALA A 1 68  ? 25.436  -10.934 9.911   1.00 18.66  ? 68  ALA A CB  1 
ATOM   519   N  N   . ALA A 1 69  ? 25.253  -9.823  6.873   1.00 19.46  ? 69  ALA A N   1 
ATOM   520   C  CA  . ALA A 1 69  ? 24.422  -9.448  5.711   1.00 19.91  ? 69  ALA A CA  1 
ATOM   521   C  C   . ALA A 1 69  ? 24.737  -10.300 4.493   1.00 19.56  ? 69  ALA A C   1 
ATOM   522   O  O   . ALA A 1 69  ? 23.848  -10.643 3.717   1.00 22.63  ? 69  ALA A O   1 
ATOM   523   C  CB  . ALA A 1 69  ? 24.645  -7.976  5.339   1.00 21.27  ? 69  ALA A CB  1 
ATOM   524   N  N   . ALA A 1 70  ? 25.984  -10.709 4.355   1.00 20.39  ? 70  ALA A N   1 
ATOM   525   C  CA  . ALA A 1 70  ? 26.354  -11.589 3.256   1.00 21.05  ? 70  ALA A CA  1 
ATOM   526   C  C   . ALA A 1 70  ? 25.706  -12.951 3.437   1.00 21.61  ? 70  ALA A C   1 
ATOM   527   O  O   . ALA A 1 70  ? 25.259  -13.541 2.457   1.00 25.03  ? 70  ALA A O   1 
ATOM   528   C  CB  . ALA A 1 70  ? 27.884  -11.692 3.181   1.00 22.48  ? 70  ALA A CB  1 
ATOM   529   N  N   . VAL A 1 71  ? 25.610  -13.438 4.682   1.00 22.30  ? 71  VAL A N   1 
ATOM   530   C  CA  . VAL A 1 71  ? 24.880  -14.700 4.923   1.00 20.05  ? 71  VAL A CA  1 
ATOM   531   C  C   . VAL A 1 71  ? 23.391  -14.487 4.645   1.00 21.37  ? 71  VAL A C   1 
ATOM   532   O  O   . VAL A 1 71  ? 22.731  -15.317 4.050   1.00 23.67  ? 71  VAL A O   1 
ATOM   533   C  CB  . VAL A 1 71  ? 25.103  -15.140 6.370   1.00 18.65  ? 71  VAL A CB  1 
ATOM   534   C  CG1 . VAL A 1 71  ? 24.216  -16.353 6.725   1.00 21.53  ? 71  VAL A CG1 1 
ATOM   535   C  CG2 . VAL A 1 71  ? 26.622  -15.509 6.616   1.00 23.99  ? 71  VAL A CG2 1 
ATOM   536   N  N   . ALA A 1 72  ? 22.831  -13.376 5.120   1.00 23.72  ? 72  ALA A N   1 
ATOM   537   C  CA  . ALA A 1 72  ? 21.424  -13.084 4.861   1.00 23.13  ? 72  ALA A CA  1 
ATOM   538   C  C   . ALA A 1 72  ? 21.057  -13.116 3.390   1.00 26.54  ? 72  ALA A C   1 
ATOM   539   O  O   . ALA A 1 72  ? 19.903  -13.398 3.064   1.00 28.46  ? 72  ALA A O   1 
ATOM   540   C  CB  . ALA A 1 72  ? 21.050  -11.711 5.443   1.00 24.63  ? 72  ALA A CB  1 
ATOM   541   N  N   . HIS A 1 73  ? 21.999  -12.827 2.481   1.00 23.69  ? 73  HIS A N   1 
ATOM   542   C  CA  . HIS A 1 73  ? 21.718  -12.939 1.051   1.00 29.46  ? 73  HIS A CA  1 
ATOM   543   C  C   . HIS A 1 73  ? 21.394  -14.369 0.655   1.00 28.79  ? 73  HIS A C   1 
ATOM   544   O  O   . HIS A 1 73  ? 20.651  -14.599 -0.309  1.00 31.98  ? 73  HIS A O   1 
ATOM   545   C  CB  . HIS A 1 73  ? 22.924  -12.433 0.261   1.00 34.30  ? 73  HIS A CB  1 
ATOM   546   C  CG  . HIS A 1 73  ? 22.688  -12.323 -1.213  1.00 35.15  ? 73  HIS A CG  1 
ATOM   547   N  ND1 . HIS A 1 73  ? 22.121  -11.210 -1.804  1.00 41.04  ? 73  HIS A ND1 1 
ATOM   548   C  CD2 . HIS A 1 73  ? 22.944  -13.194 -2.211  1.00 35.39  ? 73  HIS A CD2 1 
ATOM   549   C  CE1 . HIS A 1 73  ? 22.059  -11.400 -3.110  1.00 37.01  ? 73  HIS A CE1 1 
ATOM   550   N  NE2 . HIS A 1 73  ? 22.534  -12.602 -3.380  1.00 39.39  ? 73  HIS A NE2 1 
ATOM   551   N  N   . ASP A 1 74  ? 21.953  -15.343 1.371   1.00 30.81  ? 74  ASP A N   1 
ATOM   552   C  CA  . ASP A 1 74  ? 21.670  -16.774 1.159   1.00 26.66  ? 74  ASP A CA  1 
ATOM   553   C  C   . ASP A 1 74  ? 20.588  -17.154 2.168   1.00 26.68  ? 74  ASP A C   1 
ATOM   554   O  O   . ASP A 1 74  ? 20.884  -17.577 3.294   1.00 26.34  ? 74  ASP A O   1 
ATOM   555   C  CB  . ASP A 1 74  ? 22.957  -17.578 1.318   1.00 29.67  ? 74  ASP A CB  1 
ATOM   556   C  CG  . ASP A 1 74  ? 22.740  -19.102 1.221   1.00 29.13  ? 74  ASP A CG  1 
ATOM   557   O  OD1 . ASP A 1 74  ? 21.602  -19.600 1.191   1.00 33.66  ? 74  ASP A OD1 1 
ATOM   558   O  OD2 . ASP A 1 74  ? 23.733  -19.826 1.132   1.00 36.06  ? 74  ASP A OD2 1 
ATOM   559   N  N   . ARG A 1 75  ? 19.314  -17.015 1.745   1.00 27.64  ? 75  ARG A N   1 
ATOM   560   C  CA  . ARG A 1 75  ? 18.171  -17.164 2.645   1.00 27.24  ? 75  ARG A CA  1 
ATOM   561   C  C   . ARG A 1 75  ? 18.241  -18.497 3.405   1.00 25.48  ? 75  ARG A C   1 
ATOM   562   O  O   . ARG A 1 75  ? 18.047  -18.558 4.643   1.00 25.51  ? 75  ARG A O   1 
ATOM   563   C  CB  . ARG A 1 75  ? 16.887  -17.056 1.815   1.00 29.63  ? 75  ARG A CB  1 
ATOM   564   C  CG  . ARG A 1 75  ? 16.267  -15.637 1.843   1.00 35.04  ? 75  ARG A CG  1 
ATOM   565   C  CD  . ARG A 1 75  ? 17.177  -14.495 1.381   1.00 40.28  ? 75  ARG A CD  1 
ATOM   566   N  NE  . ARG A 1 75  ? 16.495  -13.394 0.681   1.00 42.96  ? 75  ARG A NE  1 
ATOM   567   C  CZ  . ARG A 1 75  ? 16.979  -12.762 -0.391  1.00 46.02  ? 75  ARG A CZ  1 
ATOM   568   N  NH1 . ARG A 1 75  ? 18.176  -13.060 -0.898  1.00 43.05  ? 75  ARG A NH1 1 
ATOM   569   N  NH2 . ARG A 1 75  ? 16.255  -11.790 -0.963  1.00 45.00  ? 75  ARG A NH2 1 
ATOM   570   N  N   . LYS A 1 76  ? 18.612  -19.546 2.700   1.00 25.47  ? 76  LYS A N   1 
ATOM   571   C  CA  . LYS A 1 76  ? 18.644  -20.860 3.315   1.00 24.96  ? 76  LYS A CA  1 
ATOM   572   C  C   . LYS A 1 76  ? 19.721  -20.954 4.376   1.00 27.39  ? 76  LYS A C   1 
ATOM   573   O  O   . LYS A 1 76  ? 19.457  -21.455 5.471   1.00 27.83  ? 76  LYS A O   1 
ATOM   574   C  CB  . LYS A 1 76  ? 18.849  -21.928 2.248   1.00 25.78  ? 76  LYS A CB  1 
ATOM   575   C  CG  . LYS A 1 76  ? 19.378  -23.254 2.791   1.00 33.39  ? 76  LYS A CG  1 
ATOM   576   C  CD  . LYS A 1 76  ? 18.334  -24.105 3.394   1.00 39.65  ? 76  LYS A CD  1 
ATOM   577   C  CE  . LYS A 1 76  ? 18.760  -25.637 3.353   1.00 45.65  ? 76  LYS A CE  1 
ATOM   578   N  NZ  . LYS A 1 76  ? 20.190  -26.028 2.967   1.00 45.48  ? 76  LYS A NZ  1 
ATOM   579   N  N   . PHE A 1 77  ? 20.950  -20.503 4.069   1.00 23.34  ? 77  PHE A N   1 
ATOM   580   C  CA  . PHE A 1 77  ? 22.019  -20.563 5.069   1.00 23.13  ? 77  PHE A CA  1 
ATOM   581   C  C   . PHE A 1 77  ? 21.697  -19.656 6.243   1.00 23.37  ? 77  PHE A C   1 
ATOM   582   O  O   . PHE A 1 77  ? 21.966  -19.994 7.405   1.00 22.20  ? 77  PHE A O   1 
ATOM   583   C  CB  . PHE A 1 77  ? 23.365  -20.159 4.477   1.00 24.74  ? 77  PHE A CB  1 
ATOM   584   C  CG  . PHE A 1 77  ? 24.544  -20.334 5.395   1.00 26.14  ? 77  PHE A CG  1 
ATOM   585   C  CD1 . PHE A 1 77  ? 24.677  -21.494 6.186   1.00 25.16  ? 77  PHE A CD1 1 
ATOM   586   C  CD2 . PHE A 1 77  ? 25.539  -19.404 5.448   1.00 26.25  ? 77  PHE A CD2 1 
ATOM   587   C  CE1 . PHE A 1 77  ? 25.758  -21.670 7.020   1.00 23.84  ? 77  PHE A CE1 1 
ATOM   588   C  CE2 . PHE A 1 77  ? 26.634  -19.564 6.307   1.00 24.04  ? 77  PHE A CE2 1 
ATOM   589   C  CZ  . PHE A 1 77  ? 26.751  -20.712 7.097   1.00 28.32  ? 77  PHE A CZ  1 
ATOM   590   N  N   . ALA A 1 78  ? 21.115  -18.493 5.966   1.00 22.04  ? 78  ALA A N   1 
ATOM   591   C  CA  . ALA A 1 78  ? 20.781  -17.612 7.070   1.00 23.07  ? 78  ALA A CA  1 
ATOM   592   C  C   . ALA A 1 78  ? 19.759  -18.258 8.003   1.00 22.98  ? 78  ALA A C   1 
ATOM   593   O  O   . ALA A 1 78  ? 19.870  -18.124 9.229   1.00 22.50  ? 78  ALA A O   1 
ATOM   594   C  CB  . ALA A 1 78  ? 20.290  -16.269 6.529   1.00 21.72  ? 78  ALA A CB  1 
ATOM   595   N  N   A LYS A 1 79  ? 18.750  -18.932 7.436   0.49 22.61  ? 79  LYS A N   1 
ATOM   596   N  N   B LYS A 1 79  ? 18.735  -18.913 7.446   0.51 22.61  ? 79  LYS A N   1 
ATOM   597   C  CA  A LYS A 1 79  ? 17.758  -19.640 8.246   0.49 24.75  ? 79  LYS A CA  1 
ATOM   598   C  CA  B LYS A 1 79  ? 17.766  -19.623 8.283   0.51 24.76  ? 79  LYS A CA  1 
ATOM   599   C  C   A LYS A 1 79  ? 18.419  -20.698 9.121   0.49 25.33  ? 79  LYS A C   1 
ATOM   600   C  C   B LYS A 1 79  ? 18.450  -20.678 9.145   0.51 25.33  ? 79  LYS A C   1 
ATOM   601   O  O   A LYS A 1 79  ? 18.130  -20.791 10.320  0.49 23.20  ? 79  LYS A O   1 
ATOM   602   O  O   B LYS A 1 79  ? 18.199  -20.762 10.353  0.51 23.19  ? 79  LYS A O   1 
ATOM   603   C  CB  A LYS A 1 79  ? 16.696  -20.273 7.355   0.49 26.20  ? 79  LYS A CB  1 
ATOM   604   C  CB  B LYS A 1 79  ? 16.671  -20.261 7.440   0.51 26.19  ? 79  LYS A CB  1 
ATOM   605   C  CG  A LYS A 1 79  ? 15.995  -21.453 7.992   0.49 29.51  ? 79  LYS A CG  1 
ATOM   606   C  CG  B LYS A 1 79  ? 15.955  -21.353 8.211   0.51 29.57  ? 79  LYS A CG  1 
ATOM   607   C  CD  A LYS A 1 79  ? 14.633  -21.737 7.349   0.49 31.67  ? 79  LYS A CD  1 
ATOM   608   C  CD  B LYS A 1 79  ? 14.689  -21.900 7.545   0.51 31.80  ? 79  LYS A CD  1 
ATOM   609   C  CE  A LYS A 1 79  ? 14.038  -23.060 7.872   0.49 33.74  ? 79  LYS A CE  1 
ATOM   610   C  CE  B LYS A 1 79  ? 14.135  -23.078 8.398   0.51 33.10  ? 79  LYS A CE  1 
ATOM   611   N  NZ  A LYS A 1 79  ? 14.315  -24.183 6.977   0.49 28.23  ? 79  LYS A NZ  1 
ATOM   612   N  NZ  B LYS A 1 79  ? 13.883  -22.657 9.804   0.51 27.00  ? 79  LYS A NZ  1 
ATOM   613   N  N   . GLU A 1 80  ? 19.341  -21.473 8.541   1.00 23.97  ? 80  GLU A N   1 
ATOM   614   C  CA  . GLU A 1 80  ? 20.076  -22.499 9.300   1.00 24.46  ? 80  GLU A CA  1 
ATOM   615   C  C   . GLU A 1 80  ? 20.863  -21.882 10.438  1.00 22.14  ? 80  GLU A C   1 
ATOM   616   O  O   . GLU A 1 80  ? 20.795  -22.367 11.574  1.00 21.48  ? 80  GLU A O   1 
ATOM   617   C  CB  . GLU A 1 80  ? 21.009  -23.268 8.361   1.00 23.18  ? 80  GLU A CB  1 
ATOM   618   C  CG  . GLU A 1 80  ? 20.285  -24.075 7.317   1.00 26.63  ? 80  GLU A CG  1 
ATOM   619   C  CD  . GLU A 1 80  ? 21.220  -24.567 6.188   1.00 32.30  ? 80  GLU A CD  1 
ATOM   620   O  OE1 . GLU A 1 80  ? 22.247  -23.904 5.844   1.00 28.22  ? 80  GLU A OE1 1 
ATOM   621   O  OE2 . GLU A 1 80  ? 20.921  -25.650 5.657   1.00 31.31  ? 80  GLU A OE2 1 
ATOM   622   N  N   . CYS A 1 81  ? 21.589  -20.761 10.172  1.00 19.97  ? 81  CYS A N   1 
ATOM   623   C  CA  . CYS A 1 81  ? 22.354  -20.105 11.223  1.00 20.58  ? 81  CYS A CA  1 
ATOM   624   C  C   . CYS A 1 81  ? 21.446  -19.634 12.362  1.00 21.39  ? 81  CYS A C   1 
ATOM   625   O  O   . CYS A 1 81  ? 21.692  -19.941 13.540  1.00 22.11  ? 81  CYS A O   1 
ATOM   626   C  CB  . CYS A 1 81  ? 23.105  -18.887 10.639  1.00 22.92  ? 81  CYS A CB  1 
ATOM   627   S  SG  . CYS A 1 81  ? 24.514  -19.363 9.647   1.00 22.43  ? 81  CYS A SG  1 
ATOM   628   N  N   . MET A 1 82  ? 20.340  -18.966 12.014  1.00 22.24  ? 82  MET A N   1 
ATOM   629   C  CA  . MET A 1 82  ? 19.424  -18.474 13.046  1.00 21.41  ? 82  MET A CA  1 
ATOM   630   C  C   . MET A 1 82  ? 18.798  -19.644 13.806  1.00 21.68  ? 82  MET A C   1 
ATOM   631   O  O   . MET A 1 82  ? 18.544  -19.547 15.014  1.00 21.36  ? 82  MET A O   1 
ATOM   632   C  CB  . MET A 1 82  ? 18.324  -17.639 12.423  1.00 22.38  ? 82  MET A CB  1 
ATOM   633   C  CG  . MET A 1 82  ? 18.874  -16.310 12.029  1.00 21.32  ? 82  MET A CG  1 
ATOM   634   S  SD  . MET A 1 82  ? 17.623  -15.193 11.285  1.00 25.39  ? 82  MET A SD  1 
ATOM   635   C  CE  . MET A 1 82  ? 17.328  -16.035 9.722   1.00 26.77  ? 82  MET A CE  1 
ATOM   636   N  N   . ASP A 1 83  ? 18.569  -20.759 13.119  1.00 20.90  ? 83  ASP A N   1 
ATOM   637   C  CA  . ASP A 1 83  ? 18.039  -21.950 13.800  1.00 23.12  ? 83  ASP A CA  1 
ATOM   638   C  C   . ASP A 1 83  ? 19.031  -22.496 14.812  1.00 24.55  ? 83  ASP A C   1 
ATOM   639   O  O   . ASP A 1 83  ? 18.625  -22.929 15.899  1.00 22.61  ? 83  ASP A O   1 
ATOM   640   C  CB  . ASP A 1 83  ? 17.647  -23.015 12.784  1.00 24.43  ? 83  ASP A CB  1 
ATOM   641   C  CG  . ASP A 1 83  ? 16.302  -22.690 12.088  1.00 27.21  ? 83  ASP A CG  1 
ATOM   642   O  OD1 . ASP A 1 83  ? 15.562  -21.764 12.556  1.00 29.63  ? 83  ASP A OD1 1 
ATOM   643   O  OD2 . ASP A 1 83  ? 16.019  -23.318 11.058  1.00 28.53  ? 83  ASP A OD2 1 
ATOM   644   N  N   . ALA A 1 84  ? 20.331  -22.457 14.488  1.00 22.67  ? 84  ALA A N   1 
ATOM   645   C  CA  . ALA A 1 84  ? 21.341  -22.920 15.431  1.00 22.68  ? 84  ALA A CA  1 
ATOM   646   C  C   . ALA A 1 84  ? 21.421  -22.006 16.645  1.00 22.83  ? 84  ALA A C   1 
ATOM   647   O  O   . ALA A 1 84  ? 21.491  -22.499 17.782  1.00 23.47  ? 84  ALA A O   1 
ATOM   648   C  CB  . ALA A 1 84  ? 22.703  -23.050 14.749  1.00 21.98  ? 84  ALA A CB  1 
ATOM   649   N  N   . ALA A 1 85  ? 21.436  -20.662 16.424  1.00 23.17  ? 85  ALA A N   1 
ATOM   650   C  CA  . ALA A 1 85  ? 21.402  -19.747 17.552  1.00 20.24  ? 85  ALA A CA  1 
ATOM   651   C  C   . ALA A 1 85  ? 20.152  -19.919 18.431  1.00 19.04  ? 85  ALA A C   1 
ATOM   652   O  O   . ALA A 1 85  ? 20.231  -19.790 19.675  1.00 21.29  ? 85  ALA A O   1 
ATOM   653   C  CB  . ALA A 1 85  ? 21.507  -18.298 17.051  1.00 20.10  ? 85  ALA A CB  1 
ATOM   654   N  N   . GLU A 1 86  ? 18.990  -20.187 17.830  1.00 20.41  ? 86  GLU A N   1 
ATOM   655   C  CA  . GLU A 1 86  ? 17.791  -20.388 18.631  1.00 22.42  ? 86  GLU A CA  1 
ATOM   656   C  C   . GLU A 1 86  ? 17.880  -21.676 19.444  1.00 23.18  ? 86  GLU A C   1 
ATOM   657   O  O   . GLU A 1 86  ? 17.484  -21.713 20.612  1.00 23.89  ? 86  GLU A O   1 
ATOM   658   C  CB  . GLU A 1 86  ? 16.582  -20.420 17.727  1.00 24.36  ? 86  GLU A CB  1 
ATOM   659   C  CG  . GLU A 1 86  ? 15.270  -20.689 18.410  1.00 24.54  ? 86  GLU A CG  1 
ATOM   660   C  CD  . GLU A 1 86  ? 14.121  -20.065 17.680  1.00 29.36  ? 86  GLU A CD  1 
ATOM   661   O  OE1 . GLU A 1 86  ? 14.300  -19.012 17.000  1.00 29.15  ? 86  GLU A OE1 1 
ATOM   662   O  OE2 . GLU A 1 86  ? 13.039  -20.643 17.725  1.00 32.79  ? 86  GLU A OE2 1 
ATOM   663   N  N   . ALA A 1 87  ? 18.452  -22.719 18.847  1.00 23.15  ? 87  ALA A N   1 
ATOM   664   C  CA  . ALA A 1 87  ? 18.689  -23.977 19.554  1.00 22.51  ? 87  ALA A CA  1 
ATOM   665   C  C   . ALA A 1 87  ? 19.562  -23.780 20.791  1.00 25.14  ? 87  ALA A C   1 
ATOM   666   O  O   . ALA A 1 87  ? 19.341  -24.427 21.830  1.00 23.58  ? 87  ALA A O   1 
ATOM   667   C  CB  . ALA A 1 87  ? 19.336  -24.968 18.573  1.00 21.85  ? 87  ALA A CB  1 
ATOM   668   N  N   . TYR A 1 88  ? 20.582  -22.932 20.684  1.00 22.52  ? 88  TYR A N   1 
ATOM   669   C  CA  . TYR A 1 88  ? 21.414  -22.626 21.834  1.00 22.76  ? 88  TYR A CA  1 
ATOM   670   C  C   . TYR A 1 88  ? 20.581  -22.021 22.961  1.00 24.63  ? 88  TYR A C   1 
ATOM   671   O  O   . TYR A 1 88  ? 20.781  -22.357 24.117  1.00 23.23  ? 88  TYR A O   1 
ATOM   672   C  CB  . TYR A 1 88  ? 22.547  -21.698 21.464  1.00 21.37  ? 88  TYR A CB  1 
ATOM   673   C  CG  . TYR A 1 88  ? 23.511  -21.455 22.612  1.00 23.81  ? 88  TYR A CG  1 
ATOM   674   C  CD1 . TYR A 1 88  ? 23.294  -20.444 23.573  1.00 22.71  ? 88  TYR A CD1 1 
ATOM   675   C  CD2 . TYR A 1 88  ? 24.624  -22.295 22.784  1.00 23.15  ? 88  TYR A CD2 1 
ATOM   676   C  CE1 . TYR A 1 88  ? 24.214  -20.234 24.604  1.00 25.00  ? 88  TYR A CE1 1 
ATOM   677   C  CE2 . TYR A 1 88  ? 25.536  -22.099 23.816  1.00 24.57  ? 88  TYR A CE2 1 
ATOM   678   C  CZ  . TYR A 1 88  ? 25.323  -21.039 24.725  1.00 26.03  ? 88  TYR A CZ  1 
ATOM   679   O  OH  . TYR A 1 88  ? 26.190  -20.815 25.771  1.00 26.15  ? 88  TYR A OH  1 
ATOM   680   N  N   . GLY A 1 89  ? 19.641  -21.132 22.630  1.00 24.28  ? 89  GLY A N   1 
ATOM   681   C  CA  . GLY A 1 89  ? 18.594  -20.686 23.540  1.00 21.12  ? 89  GLY A CA  1 
ATOM   682   C  C   . GLY A 1 89  ? 18.370  -19.194 23.438  1.00 24.44  ? 89  GLY A C   1 
ATOM   683   O  O   . GLY A 1 89  ? 17.675  -18.637 24.273  1.00 23.87  ? 89  GLY A O   1 
ATOM   684   N  N   . PHE A 1 90  ? 18.939  -18.540 22.427  1.00 22.12  ? 90  PHE A N   1 
ATOM   685   C  CA  . PHE A 1 90  ? 18.778  -17.090 22.346  1.00 21.32  ? 90  PHE A CA  1 
ATOM   686   C  C   . PHE A 1 90  ? 17.393  -16.750 21.798  1.00 24.59  ? 90  PHE A C   1 
ATOM   687   O  O   . PHE A 1 90  ? 16.874  -17.444 20.941  1.00 24.38  ? 90  PHE A O   1 
ATOM   688   C  CB  . PHE A 1 90  ? 19.872  -16.498 21.454  1.00 21.76  ? 90  PHE A CB  1 
ATOM   689   C  CG  . PHE A 1 90  ? 21.186  -16.371 22.156  1.00 21.85  ? 90  PHE A CG  1 
ATOM   690   C  CD1 . PHE A 1 90  ? 21.367  -15.423 23.140  1.00 23.06  ? 90  PHE A CD1 1 
ATOM   691   C  CD2 . PHE A 1 90  ? 22.238  -17.208 21.825  1.00 24.06  ? 90  PHE A CD2 1 
ATOM   692   C  CE1 . PHE A 1 90  ? 22.604  -15.303 23.789  1.00 25.76  ? 90  PHE A CE1 1 
ATOM   693   C  CE2 . PHE A 1 90  ? 23.478  -17.052 22.474  1.00 23.98  ? 90  PHE A CE2 1 
ATOM   694   C  CZ  . PHE A 1 90  ? 23.631  -16.150 23.446  1.00 24.23  ? 90  PHE A CZ  1 
ATOM   695   N  N   . ALA A 1 91  ? 16.837  -15.625 22.262  1.00 21.27  ? 91  ALA A N   1 
ATOM   696   C  CA  . ALA A 1 91  ? 15.536  -15.133 21.812  1.00 20.96  ? 91  ALA A CA  1 
ATOM   697   C  C   . ALA A 1 91  ? 15.581  -14.777 20.329  1.00 22.86  ? 91  ALA A C   1 
ATOM   698   O  O   . ALA A 1 91  ? 16.568  -14.215 19.849  1.00 23.01  ? 91  ALA A O   1 
ATOM   699   C  CB  . ALA A 1 91  ? 15.191  -13.832 22.578  1.00 20.72  ? 91  ALA A CB  1 
ATOM   700   N  N   . ARG A 1 92  ? 14.489  -15.073 19.625  1.00 23.06  ? 92  ARG A N   1 
ATOM   701   C  CA  . ARG A 1 92  ? 14.464  -14.817 18.187  1.00 21.28  ? 92  ARG A CA  1 
ATOM   702   C  C   . ARG A 1 92  ? 14.345  -13.336 17.875  1.00 23.24  ? 92  ARG A C   1 
ATOM   703   O  O   . ARG A 1 92  ? 14.581  -12.948 16.724  1.00 24.92  ? 92  ARG A O   1 
ATOM   704   C  CB  . ARG A 1 92  ? 13.334  -15.617 17.520  1.00 24.18  ? 92  ARG A CB  1 
ATOM   705   C  CG  . ARG A 1 92  ? 13.468  -15.716 15.975  1.00 27.41  ? 92  ARG A CG  1 
ATOM   706   C  CD  . ARG A 1 92  ? 12.201  -16.319 15.359  1.00 27.16  ? 92  ARG A CD  1 
ATOM   707   N  NE  . ARG A 1 92  ? 12.102  -17.733 15.726  1.00 25.36  ? 92  ARG A NE  1 
ATOM   708   C  CZ  . ARG A 1 92  ? 11.098  -18.508 15.353  1.00 30.15  ? 92  ARG A CZ  1 
ATOM   709   N  NH1 . ARG A 1 92  ? 10.087  -18.033 14.641  1.00 28.40  ? 92  ARG A NH1 1 
ATOM   710   N  NH2 . ARG A 1 92  ? 11.102  -19.797 15.703  1.00 27.57  ? 92  ARG A NH2 1 
ATOM   711   N  N   . ASP A 1 93  ? 13.985  -12.504 18.833  1.00 22.78  ? 93  ASP A N   1 
ATOM   712   C  CA  . ASP A 1 93  ? 13.878  -11.082 18.530  1.00 20.21  ? 93  ASP A CA  1 
ATOM   713   C  C   . ASP A 1 93  ? 15.126  -10.318 18.826  1.00 19.58  ? 93  ASP A C   1 
ATOM   714   O  O   . ASP A 1 93  ? 15.143  -9.073  18.655  1.00 21.23  ? 93  ASP A O   1 
ATOM   715   C  CB  . ASP A 1 93  ? 12.710  -10.485 19.235  1.00 22.63  ? 93  ASP A CB  1 
ATOM   716   C  CG  . ASP A 1 93  ? 12.742  -10.751 20.710  1.00 26.80  ? 93  ASP A CG  1 
ATOM   717   O  OD1 . ASP A 1 93  ? 12.231  -11.820 21.165  1.00 29.97  ? 93  ASP A OD1 1 
ATOM   718   O  OD2 . ASP A 1 93  ? 13.298  -9.909  21.399  1.00 30.15  ? 93  ASP A OD2 1 
ATOM   719   N  N   . LEU A 1 94  ? 16.197  -10.998 19.219  1.00 21.37  ? 94  LEU A N   1 
ATOM   720   C  CA  . LEU A 1 94  ? 17.483  -10.351 19.255  1.00 18.64  ? 94  LEU A CA  1 
ATOM   721   C  C   . LEU A 1 94  ? 17.946  -10.002 17.814  1.00 19.40  ? 94  LEU A C   1 
ATOM   722   O  O   . LEU A 1 94  ? 17.466  -10.574 16.819  1.00 21.99  ? 94  LEU A O   1 
ATOM   723   C  CB  . LEU A 1 94  ? 18.547  -11.231 19.905  1.00 18.15  ? 94  LEU A CB  1 
ATOM   724   C  CG  . LEU A 1 94  ? 18.529  -11.317 21.440  1.00 20.36  ? 94  LEU A CG  1 
ATOM   725   C  CD1 . LEU A 1 94  ? 19.399  -12.495 21.845  1.00 21.18  ? 94  LEU A CD1 1 
ATOM   726   C  CD2 . LEU A 1 94  ? 19.035  -9.967  22.094  1.00 22.24  ? 94  LEU A CD2 1 
ATOM   727   N  N   . CYS A 1 95  ? 18.871  -9.060  17.743  1.00 19.98  ? 95  CYS A N   1 
ATOM   728   C  CA  . CYS A 1 95  ? 19.439  -8.566  16.487  1.00 20.12  ? 95  CYS A CA  1 
ATOM   729   C  C   . CYS A 1 95  ? 19.632  -9.711  15.492  1.00 21.95  ? 95  CYS A C   1 
ATOM   730   O  O   . CYS A 1 95  ? 20.323  -10.689 15.786  1.00 20.93  ? 95  CYS A O   1 
ATOM   731   C  CB  . CYS A 1 95  ? 20.807  -7.939  16.774  1.00 21.85  ? 95  CYS A CB  1 
ATOM   732   S  SG  . CYS A 1 95  ? 21.834  -7.543  15.274  1.00 20.23  ? 95  CYS A SG  1 
ATOM   733   N  N   . SER A 1 96  ? 19.056  -9.587  14.310  1.00 18.97  ? 96  SER A N   1 
ATOM   734   C  CA  . SER A 1 96  ? 19.155  -10.734 13.374  1.00 19.73  ? 96  SER A CA  1 
ATOM   735   C  C   . SER A 1 96  ? 20.596  -10.959 12.859  1.00 21.65  ? 96  SER A C   1 
ATOM   736   O  O   . SER A 1 96  ? 20.975  -12.106 12.542  1.00 19.66  ? 96  SER A O   1 
ATOM   737   C  CB  . SER A 1 96  ? 18.157  -10.536 12.233  1.00 21.74  ? 96  SER A CB  1 
ATOM   738   O  OG  . SER A 1 96  ? 18.445  -9.342  11.525  1.00 23.67  ? 96  SER A OG  1 
ATOM   739   N  N   . TYR A 1 97  ? 21.419  -9.929  12.698  1.00 20.06  ? 97  TYR A N   1 
ATOM   740   C  CA  . TYR A 1 97  ? 22.824  -10.140 12.316  1.00 21.15  ? 97  TYR A CA  1 
ATOM   741   C  C   . TYR A 1 97  ? 23.592  -10.889 13.403  1.00 19.54  ? 97  TYR A C   1 
ATOM   742   O  O   . TYR A 1 97  ? 24.313  -11.846 13.096  1.00 19.83  ? 97  TYR A O   1 
ATOM   743   C  CB  . TYR A 1 97  ? 23.518  -8.790  12.031  1.00 20.31  ? 97  TYR A CB  1 
ATOM   744   C  CG  . TYR A 1 97  ? 23.174  -8.147  10.709  1.00 20.84  ? 97  TYR A CG  1 
ATOM   745   C  CD1 . TYR A 1 97  ? 22.603  -8.896  9.657   1.00 23.00  ? 97  TYR A CD1 1 
ATOM   746   C  CD2 . TYR A 1 97  ? 23.421  -6.784  10.505  1.00 21.08  ? 97  TYR A CD2 1 
ATOM   747   C  CE1 . TYR A 1 97  ? 22.278  -8.290  8.443   1.00 26.48  ? 97  TYR A CE1 1 
ATOM   748   C  CE2 . TYR A 1 97  ? 23.110  -6.197  9.274   1.00 22.23  ? 97  TYR A CE2 1 
ATOM   749   C  CZ  . TYR A 1 97  ? 22.556  -6.963  8.263   1.00 29.01  ? 97  TYR A CZ  1 
ATOM   750   O  OH  . TYR A 1 97  ? 22.230  -6.328  7.092   1.00 30.16  ? 97  TYR A OH  1 
ATOM   751   N  N   . MET A 1 98  ? 23.387  -10.527 14.678  1.00 18.10  ? 98  MET A N   1 
ATOM   752   C  CA  . MET A 1 98  ? 24.033  -11.182 15.793  1.00 17.22  ? 98  MET A CA  1 
ATOM   753   C  C   . MET A 1 98  ? 23.611  -12.655 15.825  1.00 17.82  ? 98  MET A C   1 
ATOM   754   O  O   . MET A 1 98  ? 24.454  -13.532 15.962  1.00 20.03  ? 98  MET A O   1 
ATOM   755   C  CB  . MET A 1 98  ? 23.591  -10.470 17.053  1.00 16.97  ? 98  MET A CB  1 
ATOM   756   C  CG  . MET A 1 98  ? 23.948  -10.982 18.382  1.00 18.87  ? 98  MET A CG  1 
ATOM   757   S  SD  . MET A 1 98  ? 24.089  -9.852  19.750  1.00 21.24  ? 98  MET A SD  1 
ATOM   758   C  CE  . MET A 1 98  ? 22.405  -9.959  20.171  1.00 20.91  ? 98  MET A CE  1 
ATOM   759   N  N   . ARG A 1 99  ? 22.319  -12.938 15.603  1.00 19.07  ? 99  ARG A N   1 
ATOM   760   C  CA  . ARG A 1 99  ? 21.864  -14.323 15.676  1.00 18.42  ? 99  ARG A CA  1 
ATOM   761   C  C   . ARG A 1 99  ? 22.446  -15.121 14.514  1.00 18.44  ? 99  ARG A C   1 
ATOM   762   O  O   . ARG A 1 99  ? 22.857  -16.273 14.688  1.00 19.64  ? 99  ARG A O   1 
ATOM   763   C  CB  . ARG A 1 99  ? 20.329  -14.393 15.630  1.00 19.85  ? 99  ARG A CB  1 
ATOM   764   C  CG  . ARG A 1 99  ? 19.694  -13.699 16.902  1.00 21.34  ? 99  ARG A CG  1 
ATOM   765   C  CD  . ARG A 1 99  ? 18.147  -13.873 16.945  1.00 20.74  ? 99  ARG A CD  1 
ATOM   766   N  NE  . ARG A 1 99  ? 17.484  -13.139 15.866  1.00 19.82  ? 99  ARG A NE  1 
ATOM   767   C  CZ  . ARG A 1 99  ? 16.864  -13.649 14.810  1.00 21.90  ? 99  ARG A CZ  1 
ATOM   768   N  NH1 . ARG A 1 99  ? 16.899  -14.984 14.525  1.00 22.27  ? 99  ARG A NH1 1 
ATOM   769   N  NH2 . ARG A 1 99  ? 16.159  -12.824 14.029  1.00 22.16  ? 99  ARG A NH2 1 
ATOM   770   N  N   . ILE A 1 100 ? 22.470  -14.526 13.318  1.00 18.87  ? 100 ILE A N   1 
ATOM   771   C  CA  . ILE A 1 100 ? 23.116  -15.195 12.180  1.00 19.74  ? 100 ILE A CA  1 
ATOM   772   C  C   . ILE A 1 100 ? 24.569  -15.503 12.486  1.00 18.93  ? 100 ILE A C   1 
ATOM   773   O  O   . ILE A 1 100 ? 25.053  -16.625 12.230  1.00 19.92  ? 100 ILE A O   1 
ATOM   774   C  CB  . ILE A 1 100 ? 23.001  -14.319 10.924  1.00 20.53  ? 100 ILE A CB  1 
ATOM   775   C  CG1 . ILE A 1 100 ? 21.533  -14.351 10.415  1.00 20.25  ? 100 ILE A CG1 1 
ATOM   776   C  CG2 . ILE A 1 100 ? 23.971  -14.801 9.838   1.00 19.40  ? 100 ILE A CG2 1 
ATOM   777   C  CD1 . ILE A 1 100 ? 21.248  -13.315 9.255   1.00 22.04  ? 100 ILE A CD1 1 
ATOM   778   N  N   . TYR A 1 101 ? 25.293  -14.512 13.013  1.00 17.10  ? 101 TYR A N   1 
ATOM   779   C  CA  . TYR A 1 101 ? 26.722  -14.690 13.278  1.00 16.60  ? 101 TYR A CA  1 
ATOM   780   C  C   . TYR A 1 101 ? 26.963  -15.809 14.297  1.00 21.36  ? 101 TYR A C   1 
ATOM   781   O  O   . TYR A 1 101 ? 27.798  -16.704 14.080  1.00 21.24  ? 101 TYR A O   1 
ATOM   782   C  CB  . TYR A 1 101 ? 27.297  -13.350 13.758  1.00 18.81  ? 101 TYR A CB  1 
ATOM   783   C  CG  . TYR A 1 101 ? 28.798  -13.335 13.781  1.00 18.21  ? 101 TYR A CG  1 
ATOM   784   C  CD1 . TYR A 1 101 ? 29.488  -13.938 14.814  1.00 20.82  ? 101 TYR A CD1 1 
ATOM   785   C  CD2 . TYR A 1 101 ? 29.515  -12.738 12.761  1.00 18.05  ? 101 TYR A CD2 1 
ATOM   786   C  CE1 . TYR A 1 101 ? 30.888  -13.922 14.872  1.00 20.35  ? 101 TYR A CE1 1 
ATOM   787   C  CE2 . TYR A 1 101 ? 30.874  -12.721 12.789  1.00 21.39  ? 101 TYR A CE2 1 
ATOM   788   C  CZ  . TYR A 1 101 ? 31.551  -13.254 13.809  1.00 22.54  ? 101 TYR A CZ  1 
ATOM   789   O  OH  . TYR A 1 101 ? 32.943  -13.155 13.738  1.00 23.63  ? 101 TYR A OH  1 
ATOM   790   N  N   . TRP A 1 102 ? 26.231  -15.771 15.418  1.00 19.75  ? 102 TRP A N   1 
ATOM   791   C  CA  . TRP A 1 102 ? 26.326  -16.841 16.406  1.00 18.21  ? 102 TRP A CA  1 
ATOM   792   C  C   . TRP A 1 102 ? 26.058  -18.204 15.763  1.00 20.08  ? 102 TRP A C   1 
ATOM   793   O  O   . TRP A 1 102 ? 26.772  -19.169 16.013  1.00 21.19  ? 102 TRP A O   1 
ATOM   794   C  CB  . TRP A 1 102 ? 25.311  -16.577 17.470  1.00 18.01  ? 102 TRP A CB  1 
ATOM   795   C  CG  . TRP A 1 102 ? 25.696  -15.464 18.355  1.00 20.25  ? 102 TRP A CG  1 
ATOM   796   C  CD1 . TRP A 1 102 ? 26.942  -14.964 18.602  1.00 18.69  ? 102 TRP A CD1 1 
ATOM   797   C  CD2 . TRP A 1 102 ? 24.806  -14.823 19.248  1.00 22.99  ? 102 TRP A CD2 1 
ATOM   798   N  NE1 . TRP A 1 102 ? 26.865  -13.962 19.595  1.00 20.81  ? 102 TRP A NE1 1 
ATOM   799   C  CE2 . TRP A 1 102 ? 25.549  -13.851 19.974  1.00 21.42  ? 102 TRP A CE2 1 
ATOM   800   C  CE3 . TRP A 1 102 ? 23.409  -14.913 19.435  1.00 19.50  ? 102 TRP A CE3 1 
ATOM   801   C  CZ2 . TRP A 1 102 ? 24.957  -13.054 20.973  1.00 18.53  ? 102 TRP A CZ2 1 
ATOM   802   C  CZ3 . TRP A 1 102 ? 22.800  -14.053 20.404  1.00 18.98  ? 102 TRP A CZ3 1 
ATOM   803   C  CH2 . TRP A 1 102 ? 23.569  -13.185 21.143  1.00 18.90  ? 102 TRP A CH2 1 
ATOM   804   N  N   . GLY A 1 103 ? 24.959  -18.318 15.004  1.00 20.18  ? 103 GLY A N   1 
ATOM   805   C  CA  . GLY A 1 103 ? 24.600  -19.632 14.478  1.00 23.12  ? 103 GLY A CA  1 
ATOM   806   C  C   . GLY A 1 103 ? 25.647  -20.177 13.526  1.00 23.40  ? 103 GLY A C   1 
ATOM   807   O  O   . GLY A 1 103 ? 25.944  -21.380 13.540  1.00 22.70  ? 103 GLY A O   1 
ATOM   808   N  N   . GLY A 1 104 ? 26.216  -19.308 12.675  1.00 20.93  ? 104 GLY A N   1 
ATOM   809   C  CA  . GLY A 1 104 ? 27.297  -19.728 11.782  1.00 22.07  ? 104 GLY A CA  1 
ATOM   810   C  C   . GLY A 1 104 ? 28.536  -20.169 12.542  1.00 24.01  ? 104 GLY A C   1 
ATOM   811   O  O   . GLY A 1 104 ? 29.238  -21.087 12.135  1.00 24.01  ? 104 GLY A O   1 
ATOM   812   N  N   . MET A 1 105 ? 28.771  -19.588 13.705  1.00 20.95  ? 105 MET A N   1 
ATOM   813   C  CA  . MET A 1 105 ? 29.913  -20.003 14.507  1.00 18.75  ? 105 MET A CA  1 
ATOM   814   C  C   . MET A 1 105 ? 29.678  -21.389 15.096  1.00 21.68  ? 105 MET A C   1 
ATOM   815   O  O   . MET A 1 105 ? 30.544  -22.274 15.007  1.00 22.56  ? 105 MET A O   1 
ATOM   816   C  CB  . MET A 1 105 ? 30.112  -18.934 15.609  1.00 20.73  ? 105 MET A CB  1 
ATOM   817   C  CG  . MET A 1 105 ? 31.364  -19.151 16.463  1.00 25.46  ? 105 MET A CG  1 
ATOM   818   S  SD  . MET A 1 105 ? 31.380  -18.235 18.070  1.00 25.50  ? 105 MET A SD  1 
ATOM   819   C  CE  . MET A 1 105 ? 29.626  -18.273 18.490  1.00 26.25  ? 105 MET A CE  1 
ATOM   820   N  N   . HIS A 1 106 ? 28.491  -21.598 15.675  1.00 20.97  ? 106 HIS A N   1 
ATOM   821   C  CA  . HIS A 1 106 ? 28.137  -22.907 16.219  1.00 21.03  ? 106 HIS A CA  1 
ATOM   822   C  C   . HIS A 1 106 ? 28.114  -23.969 15.114  1.00 20.53  ? 106 HIS A C   1 
ATOM   823   O  O   . HIS A 1 106 ? 28.578  -25.092 15.334  1.00 20.69  ? 106 HIS A O   1 
ATOM   824   C  CB  . HIS A 1 106 ? 26.798  -22.807 16.942  1.00 20.07  ? 106 HIS A CB  1 
ATOM   825   C  CG  . HIS A 1 106 ? 26.935  -22.157 18.298  1.00 22.78  ? 106 HIS A CG  1 
ATOM   826   N  ND1 . HIS A 1 106 ? 27.346  -22.849 19.410  1.00 22.43  ? 106 HIS A ND1 1 
ATOM   827   C  CD2 . HIS A 1 106 ? 26.710  -20.880 18.716  1.00 21.46  ? 106 HIS A CD2 1 
ATOM   828   C  CE1 . HIS A 1 106 ? 27.355  -22.043 20.463  1.00 23.71  ? 106 HIS A CE1 1 
ATOM   829   N  NE2 . HIS A 1 106 ? 26.993  -20.834 20.060  1.00 20.76  ? 106 HIS A NE2 1 
ATOM   830   N  N   . LEU A 1 107 ? 27.589  -23.624 13.928  1.00 21.36  ? 107 LEU A N   1 
ATOM   831   C  CA  . LEU A 1 107 ? 27.616  -24.595 12.823  1.00 21.97  ? 107 LEU A CA  1 
ATOM   832   C  C   . LEU A 1 107 ? 29.023  -24.802 12.282  1.00 21.87  ? 107 LEU A C   1 
ATOM   833   O  O   . LEU A 1 107 ? 29.257  -25.806 11.572  1.00 23.49  ? 107 LEU A O   1 
ATOM   834   C  CB  . LEU A 1 107 ? 26.665  -24.139 11.705  1.00 22.88  ? 107 LEU A CB  1 
ATOM   835   C  CG  . LEU A 1 107 ? 25.183  -24.120 12.099  1.00 20.96  ? 107 LEU A CG  1 
ATOM   836   C  CD1 . LEU A 1 107 ? 24.352  -23.572 10.981  1.00 25.34  ? 107 LEU A CD1 1 
ATOM   837   C  CD2 . LEU A 1 107 ? 24.694  -25.538 12.459  1.00 19.55  ? 107 LEU A CD2 1 
ATOM   838   N  N   . ASN A 1 108 ? 29.947  -23.871 12.558  1.00 21.56  ? 108 ASN A N   1 
ATOM   839   C  CA  . ASN A 1 108 ? 31.343  -23.934 12.093  1.00 24.53  ? 108 ASN A CA  1 
ATOM   840   C  C   . ASN A 1 108 ? 31.413  -23.914 10.565  1.00 22.56  ? 108 ASN A C   1 
ATOM   841   O  O   . ASN A 1 108 ? 32.129  -24.729 9.934   1.00 23.71  ? 108 ASN A O   1 
ATOM   842   C  CB  . ASN A 1 108 ? 32.067  -25.177 12.636  1.00 25.54  ? 108 ASN A CB  1 
ATOM   843   C  CG  . ASN A 1 108 ? 33.573  -25.100 12.445  1.00 26.71  ? 108 ASN A CG  1 
ATOM   844   O  OD1 . ASN A 1 108 ? 34.149  -24.005 12.312  1.00 27.81  ? 108 ASN A OD1 1 
ATOM   845   N  ND2 . ASN A 1 108 ? 34.226  -26.255 12.476  1.00 28.21  ? 108 ASN A ND2 1 
ATOM   846   N  N   . LYS A 1 109 ? 30.659  -22.983 9.957   1.00 23.85  ? 109 LYS A N   1 
ATOM   847   C  CA  . LYS A 1 109 ? 30.598  -22.873 8.499   1.00 21.19  ? 109 LYS A CA  1 
ATOM   848   C  C   . LYS A 1 109 ? 30.824  -21.422 8.124   1.00 21.77  ? 109 LYS A C   1 
ATOM   849   O  O   . LYS A 1 109 ? 30.203  -20.524 8.698   1.00 24.17  ? 109 LYS A O   1 
ATOM   850   C  CB  . LYS A 1 109 ? 29.250  -23.328 7.904   1.00 21.50  ? 109 LYS A CB  1 
ATOM   851   C  CG  . LYS A 1 109 ? 29.010  -24.843 8.162   1.00 21.73  ? 109 LYS A CG  1 
ATOM   852   C  CD  . LYS A 1 109 ? 27.594  -25.220 7.736   1.00 25.61  ? 109 LYS A CD  1 
ATOM   853   C  CE  . LYS A 1 109 ? 27.387  -25.102 6.254   1.00 27.59  ? 109 LYS A CE  1 
ATOM   854   N  NZ  . LYS A 1 109 ? 26.053  -25.796 5.786   1.00 28.48  ? 109 LYS A NZ  1 
ATOM   855   N  N   . TYR A 1 110 ? 31.753  -21.207 7.203   1.00 23.41  ? 110 TYR A N   1 
ATOM   856   C  CA  . TYR A 1 110 ? 32.006  -19.871 6.665   1.00 22.67  ? 110 TYR A CA  1 
ATOM   857   C  C   . TYR A 1 110 ? 31.174  -19.699 5.416   1.00 24.72  ? 110 TYR A C   1 
ATOM   858   O  O   . TYR A 1 110 ? 31.051  -20.628 4.595   1.00 26.63  ? 110 TYR A O   1 
ATOM   859   C  CB  . TYR A 1 110 ? 33.496  -19.731 6.353   1.00 22.86  ? 110 TYR A CB  1 
ATOM   860   C  CG  . TYR A 1 110 ? 34.058  -18.364 6.113   1.00 22.24  ? 110 TYR A CG  1 
ATOM   861   C  CD1 . TYR A 1 110 ? 33.751  -17.274 6.948   1.00 22.32  ? 110 TYR A CD1 1 
ATOM   862   C  CD2 . TYR A 1 110 ? 34.958  -18.167 5.045   1.00 26.06  ? 110 TYR A CD2 1 
ATOM   863   C  CE1 . TYR A 1 110 ? 34.357  -16.027 6.720   1.00 22.80  ? 110 TYR A CE1 1 
ATOM   864   C  CE2 . TYR A 1 110 ? 35.593  -16.911 4.847   1.00 24.68  ? 110 TYR A CE2 1 
ATOM   865   C  CZ  . TYR A 1 110 ? 35.252  -15.875 5.681   1.00 23.11  ? 110 TYR A CZ  1 
ATOM   866   O  OH  . TYR A 1 110 ? 35.838  -14.631 5.469   1.00 24.92  ? 110 TYR A OH  1 
ATOM   867   N  N   . ALA A 1 111 ? 30.640  -18.484 5.234   1.00 25.08  ? 111 ALA A N   1 
ATOM   868   C  CA  . ALA A 1 111 ? 29.784  -18.244 4.083   1.00 26.14  ? 111 ALA A CA  1 
ATOM   869   C  C   . ALA A 1 111 ? 30.546  -18.372 2.777   1.00 27.12  ? 111 ALA A C   1 
ATOM   870   O  O   . ALA A 1 111 ? 29.936  -18.655 1.743   1.00 29.98  ? 111 ALA A O   1 
ATOM   871   C  CB  . ALA A 1 111 ? 29.164  -16.838 4.206   1.00 26.95  ? 111 ALA A CB  1 
ATOM   872   N  N   . PHE A 1 112 ? 31.867  -18.171 2.790   1.00 27.22  ? 112 PHE A N   1 
ATOM   873   C  CA  . PHE A 1 112 ? 32.668  -18.237 1.578   1.00 29.54  ? 112 PHE A CA  1 
ATOM   874   C  C   . PHE A 1 112 ? 33.441  -19.561 1.474   1.00 34.24  ? 112 PHE A C   1 
ATOM   875   O  O   . PHE A 1 112 ? 34.381  -19.679 0.688   1.00 36.73  ? 112 PHE A O   1 
ATOM   876   C  CB  . PHE A 1 112 ? 33.571  -16.998 1.530   1.00 29.60  ? 112 PHE A CB  1 
ATOM   877   C  CG  . PHE A 1 112 ? 32.787  -15.675 1.525   1.00 30.88  ? 112 PHE A CG  1 
ATOM   878   C  CD1 . PHE A 1 112 ? 32.331  -15.114 2.705   1.00 26.07  ? 112 PHE A CD1 1 
ATOM   879   C  CD2 . PHE A 1 112 ? 32.523  -15.011 0.327   1.00 35.02  ? 112 PHE A CD2 1 
ATOM   880   C  CE1 . PHE A 1 112 ? 31.629  -13.964 2.735   1.00 29.07  ? 112 PHE A CE1 1 
ATOM   881   C  CE2 . PHE A 1 112 ? 31.811  -13.820 0.347   1.00 32.78  ? 112 PHE A CE2 1 
ATOM   882   C  CZ  . PHE A 1 112 ? 31.350  -13.319 1.584   1.00 33.13  ? 112 PHE A CZ  1 
ATOM   883   N  N   . GLY A 1 113 ? 33.027  -20.566 2.230   1.00 30.20  ? 113 GLY A N   1 
ATOM   884   C  CA  . GLY A 1 113 ? 33.638  -21.879 2.101   1.00 32.28  ? 113 GLY A CA  1 
ATOM   885   C  C   . GLY A 1 113 ? 34.462  -22.215 3.331   1.00 32.45  ? 113 GLY A C   1 
ATOM   886   O  O   . GLY A 1 113 ? 35.194  -21.376 3.851   1.00 31.96  ? 113 GLY A O   1 
ATOM   887   N  N   . GLY A 1 114 ? 34.405  -23.490 3.763   1.00 27.00  ? 114 GLY A N   1 
ATOM   888   C  CA  . GLY A 1 114 ? 35.324  -23.934 4.799   1.00 27.26  ? 114 GLY A CA  1 
ATOM   889   C  C   . GLY A 1 114 ? 34.732  -23.733 6.193   1.00 25.60  ? 114 GLY A C   1 
ATOM   890   O  O   . GLY A 1 114 ? 33.570  -23.350 6.362   1.00 26.10  ? 114 GLY A O   1 
ATOM   891   N  N   . GLU A 1 115 ? 35.532  -24.067 7.202   1.00 23.63  ? 115 GLU A N   1 
ATOM   892   C  CA  . GLU A 1 115 ? 35.132  -23.895 8.601   1.00 25.52  ? 115 GLU A CA  1 
ATOM   893   C  C   . GLU A 1 115 ? 34.980  -22.415 8.904   1.00 25.89  ? 115 GLU A C   1 
ATOM   894   O  O   . GLU A 1 115 ? 35.496  -21.543 8.177   1.00 24.35  ? 115 GLU A O   1 
ATOM   895   C  CB  . GLU A 1 115 ? 36.203  -24.458 9.545   1.00 28.29  ? 115 GLU A CB  1 
ATOM   896   C  CG  . GLU A 1 115 ? 37.560  -23.780 9.371   1.00 34.17  ? 115 GLU A CG  1 
ATOM   897   C  CD  . GLU A 1 115 ? 38.679  -24.340 10.247  1.00 40.30  ? 115 GLU A CD  1 
ATOM   898   O  OE1 . GLU A 1 115 ? 38.579  -25.507 10.641  1.00 39.38  ? 115 GLU A OE1 1 
ATOM   899   O  OE2 . GLU A 1 115 ? 39.666  -23.621 10.507  1.00 41.27  ? 115 GLU A OE2 1 
ATOM   900   N  N   . PHE A 1 116 ? 34.300  -22.123 9.997   1.00 23.55  ? 116 PHE A N   1 
ATOM   901   C  CA  . PHE A 1 116 ? 34.250  -20.724 10.428  1.00 23.70  ? 116 PHE A CA  1 
ATOM   902   C  C   . PHE A 1 116 ? 35.597  -20.352 11.035  1.00 25.24  ? 116 PHE A C   1 
ATOM   903   O  O   . PHE A 1 116 ? 36.005  -20.985 12.017  1.00 27.71  ? 116 PHE A O   1 
ATOM   904   C  CB  . PHE A 1 116 ? 33.154  -20.452 11.443  1.00 21.43  ? 116 PHE A CB  1 
ATOM   905   C  CG  . PHE A 1 116 ? 32.974  -18.989 11.665  1.00 23.42  ? 116 PHE A CG  1 
ATOM   906   C  CD1 . PHE A 1 116 ? 32.598  -18.205 10.592  1.00 25.69  ? 116 PHE A CD1 1 
ATOM   907   C  CD2 . PHE A 1 116 ? 33.254  -18.408 12.881  1.00 24.44  ? 116 PHE A CD2 1 
ATOM   908   C  CE1 . PHE A 1 116 ? 32.444  -16.823 10.719  1.00 25.29  ? 116 PHE A CE1 1 
ATOM   909   C  CE2 . PHE A 1 116 ? 33.081  -16.965 13.033  1.00 24.17  ? 116 PHE A CE2 1 
ATOM   910   C  CZ  . PHE A 1 116 ? 32.685  -16.226 11.955  1.00 27.37  ? 116 PHE A CZ  1 
ATOM   911   N  N   . PRO A 1 117 ? 36.351  -19.398 10.471  1.00 24.88  ? 117 PRO A N   1 
ATOM   912   C  CA  . PRO A 1 117 ? 37.747  -19.251 10.930  1.00 26.51  ? 117 PRO A CA  1 
ATOM   913   C  C   . PRO A 1 117 ? 37.792  -18.675 12.339  1.00 29.78  ? 117 PRO A C   1 
ATOM   914   O  O   . PRO A 1 117 ? 37.087  -17.714 12.647  1.00 31.55  ? 117 PRO A O   1 
ATOM   915   C  CB  . PRO A 1 117 ? 38.390  -18.305 9.895   1.00 25.98  ? 117 PRO A CB  1 
ATOM   916   C  CG  . PRO A 1 117 ? 37.518  -18.357 8.720   1.00 27.56  ? 117 PRO A CG  1 
ATOM   917   C  CD  . PRO A 1 117 ? 36.099  -18.576 9.269   1.00 26.12  ? 117 PRO A CD  1 
ATOM   918   N  N   . LYS A 1 118 ? 38.682  -19.231 13.175  1.00 28.75  ? 118 LYS A N   1 
ATOM   919   C  CA  . LYS A 1 118 ? 38.784  -18.728 14.555  1.00 32.37  ? 118 LYS A CA  1 
ATOM   920   C  C   . LYS A 1 118 ? 39.539  -17.400 14.590  1.00 28.33  ? 118 LYS A C   1 
ATOM   921   O  O   . LYS A 1 118 ? 40.660  -17.320 14.080  1.00 27.93  ? 118 LYS A O   1 
ATOM   922   C  CB  . LYS A 1 118 ? 39.478  -19.724 15.462  1.00 33.45  ? 118 LYS A CB  1 
ATOM   923   C  CG  . LYS A 1 118 ? 39.363  -19.298 16.925  1.00 34.09  ? 118 LYS A CG  1 
ATOM   924   C  CD  . LYS A 1 118 ? 40.077  -20.246 17.838  1.00 35.78  ? 118 LYS A CD  1 
ATOM   925   C  CE  . LYS A 1 118 ? 41.555  -19.891 18.120  1.00 38.63  ? 118 LYS A CE  1 
ATOM   926   N  NZ  . LYS A 1 118 ? 41.941  -18.456 18.165  1.00 38.62  ? 118 LYS A NZ  1 
ATOM   927   N  N   . PRO A 1 119 ? 38.967  -16.372 15.188  1.00 30.61  ? 119 PRO A N   1 
ATOM   928   C  CA  . PRO A 1 119 ? 39.715  -15.123 15.397  1.00 25.44  ? 119 PRO A CA  1 
ATOM   929   C  C   . PRO A 1 119 ? 40.732  -15.260 16.491  1.00 26.92  ? 119 PRO A C   1 
ATOM   930   O  O   . PRO A 1 119 ? 40.594  -16.084 17.389  1.00 29.05  ? 119 PRO A O   1 
ATOM   931   C  CB  . PRO A 1 119 ? 38.632  -14.106 15.770  1.00 27.94  ? 119 PRO A CB  1 
ATOM   932   C  CG  . PRO A 1 119 ? 37.431  -14.877 16.174  1.00 32.23  ? 119 PRO A CG  1 
ATOM   933   C  CD  . PRO A 1 119 ? 37.534  -16.275 15.569  1.00 31.19  ? 119 PRO A CD  1 
ATOM   934   N  N   . ASP A 1 120 ? 41.790  -14.450 16.412  1.00 23.01  ? 120 ASP A N   1 
ATOM   935   C  CA  . ASP A 1 120 ? 42.768  -14.455 17.488  1.00 24.22  ? 120 ASP A CA  1 
ATOM   936   C  C   . ASP A 1 120 ? 42.272  -13.633 18.662  1.00 25.20  ? 120 ASP A C   1 
ATOM   937   O  O   . ASP A 1 120 ? 42.682  -13.890 19.800  1.00 25.69  ? 120 ASP A O   1 
ATOM   938   C  CB  . ASP A 1 120 ? 44.106  -13.885 17.018  1.00 24.46  ? 120 ASP A CB  1 
ATOM   939   C  CG  . ASP A 1 120 ? 44.736  -14.768 15.976  1.00 31.07  ? 120 ASP A CG  1 
ATOM   940   O  OD1 . ASP A 1 120 ? 44.688  -16.013 16.145  1.00 30.21  ? 120 ASP A OD1 1 
ATOM   941   O  OD2 . ASP A 1 120 ? 45.271  -14.231 14.991  1.00 28.89  ? 120 ASP A OD2 1 
ATOM   942   N  N   . PHE A 1 121 ? 41.439  -12.629 18.380  1.00 22.06  ? 121 PHE A N   1 
ATOM   943   C  CA  . PHE A 1 121 ? 40.873  -11.778 19.429  1.00 23.69  ? 121 PHE A CA  1 
ATOM   944   C  C   . PHE A 1 121 ? 39.661  -11.035 18.905  1.00 22.67  ? 121 PHE A C   1 
ATOM   945   O  O   . PHE A 1 121 ? 39.444  -10.910 17.691  1.00 19.98  ? 121 PHE A O   1 
ATOM   946   C  CB  . PHE A 1 121 ? 41.902  -10.805 20.007  1.00 21.14  ? 121 PHE A CB  1 
ATOM   947   C  CG  . PHE A 1 121 ? 42.575  -9.897  19.009  1.00 21.78  ? 121 PHE A CG  1 
ATOM   948   C  CD1 . PHE A 1 121 ? 41.975  -8.680  18.655  1.00 23.82  ? 121 PHE A CD1 1 
ATOM   949   C  CD2 . PHE A 1 121 ? 43.851  -10.229 18.511  1.00 24.87  ? 121 PHE A CD2 1 
ATOM   950   C  CE1 . PHE A 1 121 ? 42.609  -7.831  17.758  1.00 23.79  ? 121 PHE A CE1 1 
ATOM   951   C  CE2 . PHE A 1 121 ? 44.517  -9.369  17.617  1.00 23.85  ? 121 PHE A CE2 1 
ATOM   952   C  CZ  . PHE A 1 121 ? 43.848  -8.158  17.255  1.00 23.18  ? 121 PHE A CZ  1 
ATOM   953   N  N   . VAL A 1 122 ? 38.892  -10.521 19.845  1.00 22.38  ? 122 VAL A N   1 
ATOM   954   C  CA  . VAL A 1 122 ? 37.769  -9.600  19.590  1.00 19.83  ? 122 VAL A CA  1 
ATOM   955   C  C   . VAL A 1 122 ? 38.257  -8.180  19.838  1.00 23.98  ? 122 VAL A C   1 
ATOM   956   O  O   . VAL A 1 122 ? 38.915  -7.914  20.844  1.00 21.85  ? 122 VAL A O   1 
ATOM   957   C  CB  . VAL A 1 122 ? 36.587  -9.928  20.517  1.00 22.68  ? 122 VAL A CB  1 
ATOM   958   C  CG1 . VAL A 1 122 ? 35.583  -8.735  20.581  1.00 23.85  ? 122 VAL A CG1 1 
ATOM   959   C  CG2 . VAL A 1 122 ? 35.959  -11.237 20.097  1.00 24.15  ? 122 VAL A CG2 1 
ATOM   960   N  N   . PHE A 1 123 ? 37.980  -7.271  18.901  1.00 19.72  ? 123 PHE A N   1 
ATOM   961   C  CA  . PHE A 1 123 ? 38.200  -5.837  19.104  1.00 21.22  ? 123 PHE A CA  1 
ATOM   962   C  C   . PHE A 1 123 ? 36.925  -5.151  18.646  1.00 20.26  ? 123 PHE A C   1 
ATOM   963   O  O   . PHE A 1 123 ? 36.618  -5.144  17.449  1.00 22.15  ? 123 PHE A O   1 
ATOM   964   C  CB  . PHE A 1 123 ? 39.405  -5.352  18.302  1.00 22.63  ? 123 PHE A CB  1 
ATOM   965   C  CG  . PHE A 1 123 ? 39.889  -3.975  18.684  1.00 23.61  ? 123 PHE A CG  1 
ATOM   966   C  CD1 . PHE A 1 123 ? 40.798  -3.790  19.720  1.00 23.94  ? 123 PHE A CD1 1 
ATOM   967   C  CD2 . PHE A 1 123 ? 39.461  -2.880  17.938  1.00 25.36  ? 123 PHE A CD2 1 
ATOM   968   C  CE1 . PHE A 1 123 ? 41.268  -2.527  20.046  1.00 24.71  ? 123 PHE A CE1 1 
ATOM   969   C  CE2 . PHE A 1 123 ? 39.897  -1.602  18.272  1.00 23.40  ? 123 PHE A CE2 1 
ATOM   970   C  CZ  . PHE A 1 123 ? 40.809  -1.417  19.312  1.00 23.81  ? 123 PHE A CZ  1 
ATOM   971   N  N   . GLN A 1 124 ? 36.233  -4.523  19.565  1.00 21.06  ? 124 GLN A N   1 
ATOM   972   C  CA  . GLN A 1 124 ? 34.847  -4.139  19.353  1.00 17.62  ? 124 GLN A CA  1 
ATOM   973   C  C   . GLN A 1 124 ? 34.604  -2.710  19.803  1.00 18.93  ? 124 GLN A C   1 
ATOM   974   O  O   . GLN A 1 124 ? 35.275  -2.205  20.706  1.00 22.65  ? 124 GLN A O   1 
ATOM   975   C  CB  . GLN A 1 124 ? 33.922  -5.117  20.133  1.00 20.38  ? 124 GLN A CB  1 
ATOM   976   C  CG  . GLN A 1 124 ? 32.404  -4.820  20.130  1.00 17.65  ? 124 GLN A CG  1 
ATOM   977   C  CD  . GLN A 1 124 ? 31.749  -4.772  18.765  1.00 19.95  ? 124 GLN A CD  1 
ATOM   978   O  OE1 . GLN A 1 124 ? 32.349  -4.304  17.770  1.00 20.58  ? 124 GLN A OE1 1 
ATOM   979   N  NE2 . GLN A 1 124 ? 30.456  -5.225  18.701  1.00 19.03  ? 124 GLN A NE2 1 
ATOM   980   N  N   . THR A 1 125 ? 33.576  -2.105  19.208  1.00 17.99  ? 125 THR A N   1 
ATOM   981   C  CA  . THR A 1 125 ? 33.084  -0.800  19.633  1.00 19.69  ? 125 THR A CA  1 
ATOM   982   C  C   . THR A 1 125 ? 31.733  -1.062  20.263  1.00 22.12  ? 125 THR A C   1 
ATOM   983   O  O   . THR A 1 125 ? 30.939  -1.848  19.704  1.00 20.33  ? 125 THR A O   1 
ATOM   984   C  CB  . THR A 1 125 ? 32.954  0.159   18.450  1.00 20.59  ? 125 THR A CB  1 
ATOM   985   O  OG1 . THR A 1 125 ? 34.237  0.658   18.053  1.00 20.15  ? 125 THR A OG1 1 
ATOM   986   C  CG2 . THR A 1 125 ? 32.011  1.344   18.772  1.00 21.96  ? 125 THR A CG2 1 
ATOM   987   N  N   . GLN A 1 126 ? 31.451  -0.379  21.391  1.00 20.29  ? 126 GLN A N   1 
ATOM   988   C  CA  . GLN A 1 126 ? 30.185  -0.589  22.102  1.00 20.94  ? 126 GLN A CA  1 
ATOM   989   C  C   . GLN A 1 126 ? 29.404  0.714   22.070  1.00 21.13  ? 126 GLN A C   1 
ATOM   990   O  O   . GLN A 1 126 ? 29.798  1.669   22.732  1.00 21.28  ? 126 GLN A O   1 
ATOM   991   C  CB  . GLN A 1 126 ? 30.389  -1.064  23.551  1.00 19.69  ? 126 GLN A CB  1 
ATOM   992   C  CG  . GLN A 1 126 ? 29.099  -1.633  24.140  1.00 19.45  ? 126 GLN A CG  1 
ATOM   993   C  CD  . GLN A 1 126 ? 28.178  -0.555  24.679  1.00 19.60  ? 126 GLN A CD  1 
ATOM   994   O  OE1 . GLN A 1 126 ? 28.550  0.163   25.603  1.00 20.45  ? 126 GLN A OE1 1 
ATOM   995   N  NE2 . GLN A 1 126 ? 26.938  -0.444  24.102  1.00 20.88  ? 126 GLN A NE2 1 
ATOM   996   N  N   . ILE A 1 127 ? 28.282  0.742   21.322  1.00 17.50  ? 127 ILE A N   1 
ATOM   997   C  CA  . ILE A 1 127 ? 27.381  1.891   21.426  1.00 16.65  ? 127 ILE A CA  1 
ATOM   998   C  C   . ILE A 1 127 ? 25.950  1.371   21.423  1.00 23.64  ? 127 ILE A C   1 
ATOM   999   O  O   . ILE A 1 127 ? 25.122  1.843   22.215  1.00 20.42  ? 127 ILE A O   1 
ATOM   1000  C  CB  . ILE A 1 127 ? 27.627  2.929   20.299  1.00 18.76  ? 127 ILE A CB  1 
ATOM   1001  C  CG1 . ILE A 1 127 ? 26.686  4.137   20.472  1.00 21.76  ? 127 ILE A CG1 1 
ATOM   1002  C  CG2 . ILE A 1 127 ? 27.555  2.343   18.938  1.00 19.70  ? 127 ILE A CG2 1 
ATOM   1003  C  CD1 . ILE A 1 127 ? 27.112  5.383   19.652  1.00 19.85  ? 127 ILE A CD1 1 
ATOM   1004  N  N   . CYS A 1 128 ? 25.688  0.337   20.606  1.00 16.92  ? 128 CYS A N   1 
ATOM   1005  C  CA  . CYS A 1 128 ? 24.437  -0.405  20.703  1.00 18.00  ? 128 CYS A CA  1 
ATOM   1006  C  C   . CYS A 1 128 ? 24.610  -1.404  21.854  1.00 18.49  ? 128 CYS A C   1 
ATOM   1007  O  O   . CYS A 1 128 ? 25.710  -1.974  22.031  1.00 20.24  ? 128 CYS A O   1 
ATOM   1008  C  CB  . CYS A 1 128 ? 24.207  -1.223  19.371  1.00 18.55  ? 128 CYS A CB  1 
ATOM   1009  S  SG  . CYS A 1 128 ? 22.738  -2.261  19.480  1.00 21.19  ? 128 CYS A SG  1 
ATOM   1010  N  N   . CYS A 1 129 ? 23.544  -1.653  22.599  1.00 19.02  ? 129 CYS A N   1 
ATOM   1011  C  CA  . CYS A 1 129 ? 23.643  -2.596  23.739  1.00 19.81  ? 129 CYS A CA  1 
ATOM   1012  C  C   . CYS A 1 129 ? 24.064  -3.957  23.258  1.00 19.99  ? 129 CYS A C   1 
ATOM   1013  O  O   . CYS A 1 129 ? 24.836  -4.650  23.942  1.00 23.90  ? 129 CYS A O   1 
ATOM   1014  C  CB  . CYS A 1 129 ? 22.306  -2.707  24.468  1.00 19.10  ? 129 CYS A CB  1 
ATOM   1015  S  SG  . CYS A 1 129 ? 21.830  -1.167  25.264  1.00 22.13  ? 129 CYS A SG  1 
ATOM   1016  N  N   . SER A 1 130 ? 23.611  -4.340  22.056  1.00 19.79  ? 130 SER A N   1 
ATOM   1017  C  CA  . SER A 1 130 ? 23.934  -5.702  21.566  1.00 18.14  ? 130 SER A CA  1 
ATOM   1018  C  C   . SER A 1 130 ? 25.392  -5.839  21.148  1.00 20.29  ? 130 SER A C   1 
ATOM   1019  O  O   . SER A 1 130 ? 25.872  -6.976  20.924  1.00 18.41  ? 130 SER A O   1 
ATOM   1020  C  CB  . SER A 1 130 ? 23.028  -6.047  20.410  1.00 19.68  ? 130 SER A CB  1 
ATOM   1021  O  OG  . SER A 1 130 ? 21.699  -6.081  20.884  1.00 21.44  ? 130 SER A OG  1 
ATOM   1022  N  N   . HIS A 1 131 ? 26.135  -4.729  21.076  1.00 21.10  ? 131 HIS A N   1 
ATOM   1023  C  CA  . HIS A 1 131 ? 27.538  -4.778  20.659  1.00 19.71  ? 131 HIS A CA  1 
ATOM   1024  C  C   . HIS A 1 131 ? 28.380  -5.562  21.624  1.00 20.56  ? 131 HIS A C   1 
ATOM   1025  O  O   . HIS A 1 131 ? 29.270  -6.305  21.196  1.00 20.22  ? 131 HIS A O   1 
ATOM   1026  C  CB  . HIS A 1 131 ? 28.122  -3.393  20.560  1.00 19.96  ? 131 HIS A CB  1 
ATOM   1027  C  CG  . HIS A 1 131 ? 27.731  -2.699  19.326  1.00 17.72  ? 131 HIS A CG  1 
ATOM   1028  N  ND1 . HIS A 1 131 ? 27.671  -1.325  19.268  1.00 19.01  ? 131 HIS A ND1 1 
ATOM   1029  C  CD2 . HIS A 1 131 ? 27.446  -3.162  18.075  1.00 18.04  ? 131 HIS A CD2 1 
ATOM   1030  C  CE1 . HIS A 1 131 ? 27.291  -0.973  18.051  1.00 18.83  ? 131 HIS A CE1 1 
ATOM   1031  N  NE2 . HIS A 1 131 ? 27.181  -2.067  17.305  1.00 20.89  ? 131 HIS A NE2 1 
ATOM   1032  N  N   . SER A 1 132 ? 28.104  -5.430  22.934  1.00 21.77  ? 132 SER A N   1 
ATOM   1033  C  CA  . SER A 1 132 ? 28.843  -6.217  23.916  1.00 19.09  ? 132 SER A CA  1 
ATOM   1034  C  C   . SER A 1 132 ? 28.398  -7.666  23.880  1.00 20.49  ? 132 SER A C   1 
ATOM   1035  O  O   . SER A 1 132 ? 29.228  -8.577  23.789  1.00 21.73  ? 132 SER A O   1 
ATOM   1036  C  CB  . SER A 1 132 ? 28.678  -5.670  25.362  1.00 18.03  ? 132 SER A CB  1 
ATOM   1037  O  OG  . SER A 1 132 ? 27.291  -5.695  25.694  1.00 22.57  ? 132 SER A OG  1 
ATOM   1038  N  N   . LYS A 1 133 ? 27.082  -7.888  23.931  1.00 18.93  ? 133 LYS A N   1 
ATOM   1039  C  CA  . LYS A 1 133 ? 26.576  -9.248  24.059  1.00 19.58  ? 133 LYS A CA  1 
ATOM   1040  C  C   . LYS A 1 133 ? 27.012  -10.083 22.874  1.00 20.80  ? 133 LYS A C   1 
ATOM   1041  O  O   . LYS A 1 133 ? 27.277  -11.276 23.034  1.00 21.28  ? 133 LYS A O   1 
ATOM   1042  C  CB  . LYS A 1 133 ? 25.053  -9.225  24.179  1.00 22.82  ? 133 LYS A CB  1 
ATOM   1043  C  CG  . LYS A 1 133 ? 24.561  -8.341  25.371  1.00 20.29  ? 133 LYS A CG  1 
ATOM   1044  C  CD  . LYS A 1 133 ? 25.067  -8.846  26.686  1.00 21.77  ? 133 LYS A CD  1 
ATOM   1045  C  CE  . LYS A 1 133 ? 24.995  -7.789  27.824  1.00 23.45  ? 133 LYS A CE  1 
ATOM   1046  N  NZ  . LYS A 1 133 ? 25.905  -8.224  28.970  1.00 25.05  ? 133 LYS A NZ  1 
ATOM   1047  N  N   . TRP A 1 134 ? 27.016  -9.498  21.674  1.00 18.65  ? 134 TRP A N   1 
ATOM   1048  C  CA  . TRP A 1 134 ? 27.402  -10.276 20.472  1.00 16.84  ? 134 TRP A CA  1 
ATOM   1049  C  C   . TRP A 1 134 ? 28.730  -10.964 20.683  1.00 20.29  ? 134 TRP A C   1 
ATOM   1050  O  O   . TRP A 1 134 ? 28.862  -12.190 20.482  1.00 21.02  ? 134 TRP A O   1 
ATOM   1051  C  CB  . TRP A 1 134 ? 27.515  -9.286  19.326  1.00 17.74  ? 134 TRP A CB  1 
ATOM   1052  C  CG  . TRP A 1 134 ? 27.853  -9.810  17.954  1.00 19.20  ? 134 TRP A CG  1 
ATOM   1053  C  CD1 . TRP A 1 134 ? 28.693  -10.874 17.602  1.00 20.17  ? 134 TRP A CD1 1 
ATOM   1054  C  CD2 . TRP A 1 134 ? 27.346  -9.273  16.725  1.00 19.42  ? 134 TRP A CD2 1 
ATOM   1055  N  NE1 . TRP A 1 134 ? 28.750  -10.958 16.196  1.00 19.98  ? 134 TRP A NE1 1 
ATOM   1056  C  CE2 . TRP A 1 134 ? 27.923  -10.001 15.648  1.00 22.38  ? 134 TRP A CE2 1 
ATOM   1057  C  CE3 . TRP A 1 134 ? 26.431  -8.253  16.434  1.00 18.22  ? 134 TRP A CE3 1 
ATOM   1058  C  CZ2 . TRP A 1 134 ? 27.653  -9.705  14.294  1.00 20.09  ? 134 TRP A CZ2 1 
ATOM   1059  C  CZ3 . TRP A 1 134 ? 26.160  -7.906  15.086  1.00 18.22  ? 134 TRP A CZ3 1 
ATOM   1060  C  CH2 . TRP A 1 134 ? 26.749  -8.673  13.995  1.00 19.34  ? 134 TRP A CH2 1 
ATOM   1061  N  N   . TYR A 1 135 ? 29.756  -10.170 21.035  1.00 18.76  ? 135 TYR A N   1 
ATOM   1062  C  CA  . TYR A 1 135 ? 31.102  -10.735 21.128  1.00 18.68  ? 135 TYR A CA  1 
ATOM   1063  C  C   . TYR A 1 135 ? 31.489  -11.289 22.488  1.00 19.30  ? 135 TYR A C   1 
ATOM   1064  O  O   . TYR A 1 135 ? 32.425  -12.099 22.541  1.00 21.85  ? 135 TYR A O   1 
ATOM   1065  C  CB  . TYR A 1 135 ? 32.130  -9.732  20.628  1.00 17.75  ? 135 TYR A CB  1 
ATOM   1066  C  CG  . TYR A 1 135 ? 32.051  -9.580  19.134  1.00 21.86  ? 135 TYR A CG  1 
ATOM   1067  C  CD1 . TYR A 1 135 ? 32.570  -10.539 18.291  1.00 21.98  ? 135 TYR A CD1 1 
ATOM   1068  C  CD2 . TYR A 1 135 ? 31.387  -8.472  18.561  1.00 23.16  ? 135 TYR A CD2 1 
ATOM   1069  C  CE1 . TYR A 1 135 ? 32.454  -10.424 16.903  1.00 22.38  ? 135 TYR A CE1 1 
ATOM   1070  C  CE2 . TYR A 1 135 ? 31.259  -8.373  17.158  1.00 22.48  ? 135 TYR A CE2 1 
ATOM   1071  C  CZ  . TYR A 1 135 ? 31.801  -9.330  16.357  1.00 24.44  ? 135 TYR A CZ  1 
ATOM   1072  O  OH  . TYR A 1 135 ? 31.644  -9.130  14.999  1.00 24.35  ? 135 TYR A OH  1 
ATOM   1073  N  N   . GLN A 1 136 ? 30.742  -10.988 23.551  1.00 18.56  ? 136 GLN A N   1 
ATOM   1074  C  CA  . GLN A 1 136 ? 30.900  -11.755 24.773  1.00 20.71  ? 136 GLN A CA  1 
ATOM   1075  C  C   . GLN A 1 136 ? 30.631  -13.239 24.495  1.00 18.59  ? 136 GLN A C   1 
ATOM   1076  O  O   . GLN A 1 136 ? 31.355  -14.105 24.982  1.00 23.02  ? 136 GLN A O   1 
ATOM   1077  C  CB  . GLN A 1 136 ? 29.972  -11.249 25.852  1.00 20.09  ? 136 GLN A CB  1 
ATOM   1078  C  CG  . GLN A 1 136 ? 30.509  -9.933  26.444  1.00 21.48  ? 136 GLN A CG  1 
ATOM   1079  C  CD  . GLN A 1 136 ? 29.609  -9.427  27.546  1.00 20.65  ? 136 GLN A CD  1 
ATOM   1080  O  OE1 . GLN A 1 136 ? 28.466  -9.052  27.292  1.00 25.03  ? 136 GLN A OE1 1 
ATOM   1081  N  NE2 . GLN A 1 136 ? 30.114  -9.432  28.775  1.00 20.47  ? 136 GLN A NE2 1 
ATOM   1082  N  N   . HIS A 1 137 ? 29.544  -13.545 23.771  1.00 17.12  ? 137 HIS A N   1 
ATOM   1083  C  CA  . HIS A 1 137 ? 29.290  -14.973 23.477  1.00 19.04  ? 137 HIS A CA  1 
ATOM   1084  C  C   . HIS A 1 137 ? 30.381  -15.573 22.571  1.00 21.74  ? 137 HIS A C   1 
ATOM   1085  O  O   . HIS A 1 137 ? 30.862  -16.692 22.805  1.00 22.05  ? 137 HIS A O   1 
ATOM   1086  C  CB  . HIS A 1 137 ? 27.882  -15.115 22.829  1.00 18.58  ? 137 HIS A CB  1 
ATOM   1087  C  CG  . HIS A 1 137 ? 27.512  -16.559 22.576  1.00 19.23  ? 137 HIS A CG  1 
ATOM   1088  N  ND1 . HIS A 1 137 ? 27.326  -17.443 23.601  1.00 22.02  ? 137 HIS A ND1 1 
ATOM   1089  C  CD2 . HIS A 1 137 ? 27.375  -17.260 21.420  1.00 22.53  ? 137 HIS A CD2 1 
ATOM   1090  C  CE1 . HIS A 1 137 ? 27.070  -18.649 23.096  1.00 22.53  ? 137 HIS A CE1 1 
ATOM   1091  N  NE2 . HIS A 1 137 ? 27.085  -18.566 21.771  1.00 21.46  ? 137 HIS A NE2 1 
ATOM   1092  N  N   . VAL A 1 138 ? 30.781  -14.816 21.527  1.00 20.44  ? 138 VAL A N   1 
ATOM   1093  C  CA  . VAL A 1 138 ? 31.834  -15.265 20.628  1.00 21.81  ? 138 VAL A CA  1 
ATOM   1094  C  C   . VAL A 1 138 ? 33.142  -15.514 21.386  1.00 23.04  ? 138 VAL A C   1 
ATOM   1095  O  O   . VAL A 1 138 ? 33.802  -16.537 21.190  1.00 20.92  ? 138 VAL A O   1 
ATOM   1096  C  CB  . VAL A 1 138 ? 32.021  -14.232 19.491  1.00 20.43  ? 138 VAL A CB  1 
ATOM   1097  C  CG1 . VAL A 1 138 ? 33.317  -14.532 18.760  1.00 25.23  ? 138 VAL A CG1 1 
ATOM   1098  C  CG2 . VAL A 1 138 ? 30.759  -14.143 18.563  1.00 19.01  ? 138 VAL A CG2 1 
ATOM   1099  N  N   . ALA A 1 139 ? 33.559  -14.588 22.253  1.00 19.29  ? 139 ALA A N   1 
ATOM   1100  C  CA  . ALA A 1 139 ? 34.878  -14.734 22.892  1.00 20.56  ? 139 ALA A CA  1 
ATOM   1101  C  C   . ALA A 1 139 ? 34.888  -15.901 23.856  1.00 24.65  ? 139 ALA A C   1 
ATOM   1102  O  O   . ALA A 1 139 ? 35.913  -16.590 24.010  1.00 23.46  ? 139 ALA A O   1 
ATOM   1103  C  CB  . ALA A 1 139 ? 35.260  -13.414 23.609  1.00 22.79  ? 139 ALA A CB  1 
ATOM   1104  N  N   . LYS A 1 140 ? 33.724  -16.169 24.465  1.00 22.63  ? 140 LYS A N   1 
ATOM   1105  C  CA  . LYS A 1 140 ? 33.560  -17.314 25.329  1.00 24.14  ? 140 LYS A CA  1 
ATOM   1106  C  C   . LYS A 1 140 ? 33.578  -18.625 24.538  1.00 25.25  ? 140 LYS A C   1 
ATOM   1107  O  O   . LYS A 1 140 ? 34.223  -19.599 24.951  1.00 26.81  ? 140 LYS A O   1 
ATOM   1108  C  CB  . LYS A 1 140 ? 32.245  -17.146 26.084  1.00 27.42  ? 140 LYS A CB  1 
ATOM   1109  C  CG  . LYS A 1 140 ? 32.037  -18.179 27.123  1.00 30.69  ? 140 LYS A CG  1 
ATOM   1110  C  CD  . LYS A 1 140 ? 31.151  -19.265 26.630  1.00 30.70  ? 140 LYS A CD  1 
ATOM   1111  C  CE  . LYS A 1 140 ? 29.792  -18.754 26.350  1.00 32.59  ? 140 LYS A CE  1 
ATOM   1112  N  NZ  . LYS A 1 140 ? 28.930  -19.947 26.189  1.00 33.03  ? 140 LYS A NZ  1 
ATOM   1113  N  N   . GLU A 1 141 ? 32.855  -18.686 23.413  1.00 24.15  ? 141 GLU A N   1 
ATOM   1114  C  CA  . GLU A 1 141 ? 32.876  -19.943 22.631  1.00 23.46  ? 141 GLU A CA  1 
ATOM   1115  C  C   . GLU A 1 141 ? 34.226  -20.219 21.949  1.00 26.50  ? 141 GLU A C   1 
ATOM   1116  O  O   . GLU A 1 141 ? 34.562  -21.398 21.698  1.00 28.02  ? 141 GLU A O   1 
ATOM   1117  C  CB  . GLU A 1 141 ? 31.787  -19.935 21.589  1.00 24.09  ? 141 GLU A CB  1 
ATOM   1118  C  CG  . GLU A 1 141 ? 30.391  -19.982 22.162  1.00 24.97  ? 141 GLU A CG  1 
ATOM   1119  C  CD  . GLU A 1 141 ? 30.096  -21.302 22.826  1.00 28.11  ? 141 GLU A CD  1 
ATOM   1120  O  OE1 . GLU A 1 141 ? 30.548  -22.304 22.262  1.00 28.12  ? 141 GLU A OE1 1 
ATOM   1121  O  OE2 . GLU A 1 141 ? 29.499  -21.329 23.940  1.00 28.50  ? 141 GLU A OE2 1 
ATOM   1122  N  N   . GLU A 1 142 ? 34.978  -19.182 21.592  1.00 25.53  ? 142 GLU A N   1 
ATOM   1123  C  CA  . GLU A 1 142 ? 36.265  -19.337 20.927  1.00 23.12  ? 142 GLU A CA  1 
ATOM   1124  C  C   . GLU A 1 142 ? 37.427  -19.347 21.913  1.00 26.93  ? 142 GLU A C   1 
ATOM   1125  O  O   . GLU A 1 142 ? 38.548  -19.671 21.509  1.00 26.32  ? 142 GLU A O   1 
ATOM   1126  C  CB  . GLU A 1 142 ? 36.458  -18.175 19.886  1.00 21.97  ? 142 GLU A CB  1 
ATOM   1127  C  CG  . GLU A 1 142 ? 35.383  -18.146 18.844  1.00 25.30  ? 142 GLU A CG  1 
ATOM   1128  C  CD  . GLU A 1 142 ? 35.635  -19.165 17.716  1.00 33.46  ? 142 GLU A CD  1 
ATOM   1129  O  OE1 . GLU A 1 142 ? 36.317  -20.186 18.001  1.00 30.66  ? 142 GLU A OE1 1 
ATOM   1130  O  OE2 . GLU A 1 142 ? 35.175  -18.908 16.570  1.00 30.97  ? 142 GLU A OE2 1 
ATOM   1131  N  N   A LYS A 1 143 ? 37.200  -18.914 23.170  0.52 25.55  ? 143 LYS A N   1 
ATOM   1132  N  N   B LYS A 1 143 ? 37.177  -19.049 23.204  0.48 25.63  ? 143 LYS A N   1 
ATOM   1133  C  CA  A LYS A 1 143 ? 38.217  -18.824 24.221  0.52 25.52  ? 143 LYS A CA  1 
ATOM   1134  C  CA  B LYS A 1 143 ? 38.207  -18.825 24.215  0.48 25.52  ? 143 LYS A CA  1 
ATOM   1135  C  C   A LYS A 1 143 ? 39.368  -17.900 23.811  0.52 25.82  ? 143 LYS A C   1 
ATOM   1136  C  C   B LYS A 1 143 ? 39.317  -17.944 23.670  0.48 25.80  ? 143 LYS A C   1 
ATOM   1137  O  O   A LYS A 1 143 ? 40.559  -18.250 23.892  0.52 25.21  ? 143 LYS A O   1 
ATOM   1138  O  O   B LYS A 1 143 ? 40.447  -18.406 23.468  0.48 25.27  ? 143 LYS A O   1 
ATOM   1139  C  CB  A LYS A 1 143 ? 38.716  -20.218 24.635  0.52 28.00  ? 143 LYS A CB  1 
ATOM   1140  C  CB  B LYS A 1 143 ? 38.818  -20.124 24.764  0.48 28.01  ? 143 LYS A CB  1 
ATOM   1141  C  CG  A LYS A 1 143 ? 37.571  -21.187 24.862  0.52 31.97  ? 143 LYS A CG  1 
ATOM   1142  C  CG  B LYS A 1 143 ? 37.827  -21.169 25.202  0.48 32.03  ? 143 LYS A CG  1 
ATOM   1143  C  CD  A LYS A 1 143 ? 38.089  -22.573 25.224  0.52 33.42  ? 143 LYS A CD  1 
ATOM   1144  C  CD  B LYS A 1 143 ? 38.587  -22.336 25.828  0.48 33.89  ? 143 LYS A CD  1 
ATOM   1145  C  CE  A LYS A 1 143 ? 37.230  -23.296 26.310  0.52 36.45  ? 143 LYS A CE  1 
ATOM   1146  C  CE  B LYS A 1 143 ? 38.165  -23.709 25.309  0.48 35.65  ? 143 LYS A CE  1 
ATOM   1147  N  NZ  A LYS A 1 143 ? 36.745  -22.445 27.425  0.52 30.71  ? 143 LYS A NZ  1 
ATOM   1148  N  NZ  B LYS A 1 143 ? 38.693  -24.768 26.168  0.48 40.31  ? 143 LYS A NZ  1 
ATOM   1149  N  N   . ILE A 1 144 ? 38.983  -16.680 23.427  1.00 24.29  ? 144 ILE A N   1 
ATOM   1150  C  CA  . ILE A 1 144 ? 39.938  -15.669 22.968  1.00 23.83  ? 144 ILE A CA  1 
ATOM   1151  C  C   . ILE A 1 144 ? 39.816  -14.384 23.775  1.00 24.22  ? 144 ILE A C   1 
ATOM   1152  O  O   . ILE A 1 144 ? 38.735  -14.081 24.297  1.00 25.56  ? 144 ILE A O   1 
ATOM   1153  C  CB  . ILE A 1 144 ? 39.781  -15.373 21.469  1.00 25.12  ? 144 ILE A CB  1 
ATOM   1154  C  CG1 . ILE A 1 144 ? 38.342  -14.944 21.128  1.00 22.47  ? 144 ILE A CG1 1 
ATOM   1155  C  CG2 . ILE A 1 144 ? 40.165  -16.593 20.620  1.00 24.70  ? 144 ILE A CG2 1 
ATOM   1156  C  CD1 . ILE A 1 144 ? 38.224  -14.519 19.696  1.00 25.70  ? 144 ILE A CD1 1 
ATOM   1157  N  N   . PRO A 1 145 ? 40.890  -13.594 23.829  1.00 23.55  ? 145 PRO A N   1 
ATOM   1158  C  CA  . PRO A 1 145 ? 40.824  -12.254 24.435  1.00 24.62  ? 145 PRO A CA  1 
ATOM   1159  C  C   . PRO A 1 145 ? 39.811  -11.359 23.752  1.00 19.79  ? 145 PRO A C   1 
ATOM   1160  O  O   . PRO A 1 145 ? 39.565  -11.460 22.538  1.00 21.49  ? 145 PRO A O   1 
ATOM   1161  C  CB  . PRO A 1 145 ? 42.246  -11.705 24.246  1.00 24.35  ? 145 PRO A CB  1 
ATOM   1162  C  CG  . PRO A 1 145 ? 43.067  -12.834 23.910  1.00 27.22  ? 145 PRO A CG  1 
ATOM   1163  C  CD  . PRO A 1 145 ? 42.232  -13.861 23.273  1.00 24.00  ? 145 PRO A CD  1 
ATOM   1164  N  N   . GLU A 1 146 ? 39.294  -10.371 24.514  1.00 21.04  ? 146 GLU A N   1 
ATOM   1165  C  CA  . GLU A 1 146 ? 38.262  -9.494  23.973  1.00 22.73  ? 146 GLU A CA  1 
ATOM   1166  C  C   . GLU A 1 146 ? 38.434  -8.090  24.546  1.00 22.12  ? 146 GLU A C   1 
ATOM   1167  O  O   . GLU A 1 146 ? 38.659  -7.934  25.744  1.00 23.54  ? 146 GLU A O   1 
ATOM   1168  C  CB  . GLU A 1 146 ? 36.831  -10.026 24.308  1.00 22.39  ? 146 GLU A CB  1 
ATOM   1169  C  CG  . GLU A 1 146 ? 36.583  -10.271 25.804  1.00 23.29  ? 146 GLU A CG  1 
ATOM   1170  C  CD  . GLU A 1 146 ? 35.273  -10.971 26.101  1.00 27.24  ? 146 GLU A CD  1 
ATOM   1171  O  OE1 . GLU A 1 146 ? 34.243  -10.713 25.456  1.00 24.34  ? 146 GLU A OE1 1 
ATOM   1172  O  OE2 . GLU A 1 146 ? 35.274  -11.873 26.959  1.00 32.28  ? 146 GLU A OE2 1 
ATOM   1173  N  N   . PHE A 1 147 ? 38.305  -7.076  23.677  1.00 20.11  ? 147 PHE A N   1 
ATOM   1174  C  CA  . PHE A 1 147 ? 38.411  -5.688  24.083  1.00 22.83  ? 147 PHE A CA  1 
ATOM   1175  C  C   . PHE A 1 147 ? 37.226  -4.903  23.524  1.00 20.92  ? 147 PHE A C   1 
ATOM   1176  O  O   . PHE A 1 147 ? 36.821  -5.102  22.375  1.00 21.16  ? 147 PHE A O   1 
ATOM   1177  C  CB  . PHE A 1 147 ? 39.735  -5.100  23.604  1.00 21.71  ? 147 PHE A CB  1 
ATOM   1178  C  CG  . PHE A 1 147 ? 39.924  -3.655  23.989  1.00 21.91  ? 147 PHE A CG  1 
ATOM   1179  C  CD1 . PHE A 1 147 ? 40.464  -3.321  25.219  1.00 25.41  ? 147 PHE A CD1 1 
ATOM   1180  C  CD2 . PHE A 1 147 ? 39.551  -2.668  23.097  1.00 24.89  ? 147 PHE A CD2 1 
ATOM   1181  C  CE1 . PHE A 1 147 ? 40.614  -1.970  25.604  1.00 25.54  ? 147 PHE A CE1 1 
ATOM   1182  C  CE2 . PHE A 1 147 ? 39.695  -1.287  23.465  1.00 24.62  ? 147 PHE A CE2 1 
ATOM   1183  C  CZ  . PHE A 1 147 ? 40.250  -0.979  24.716  1.00 23.22  ? 147 PHE A CZ  1 
ATOM   1184  N  N   . TYR A 1 148 ? 36.711  -3.954  24.309  1.00 20.00  ? 148 TYR A N   1 
ATOM   1185  C  CA  . TYR A 1 148 ? 35.521  -3.198  23.927  1.00 18.40  ? 148 TYR A CA  1 
ATOM   1186  C  C   . TYR A 1 148 ? 35.836  -1.742  24.173  1.00 20.05  ? 148 TYR A C   1 
ATOM   1187  O  O   . TYR A 1 148 ? 36.247  -1.377  25.286  1.00 20.87  ? 148 TYR A O   1 
ATOM   1188  C  CB  . TYR A 1 148 ? 34.246  -3.566  24.732  1.00 18.75  ? 148 TYR A CB  1 
ATOM   1189  C  CG  . TYR A 1 148 ? 33.870  -4.992  24.552  1.00 17.44  ? 148 TYR A CG  1 
ATOM   1190  C  CD1 . TYR A 1 148 ? 34.488  -5.970  25.321  1.00 21.28  ? 148 TYR A CD1 1 
ATOM   1191  C  CD2 . TYR A 1 148 ? 32.953  -5.361  23.568  1.00 18.05  ? 148 TYR A CD2 1 
ATOM   1192  C  CE1 . TYR A 1 148 ? 34.198  -7.293  25.112  1.00 20.40  ? 148 TYR A CE1 1 
ATOM   1193  C  CE2 . TYR A 1 148 ? 32.636  -6.705  23.336  1.00 21.39  ? 148 TYR A CE2 1 
ATOM   1194  C  CZ  . TYR A 1 148 ? 33.239  -7.636  24.115  1.00 20.42  ? 148 TYR A CZ  1 
ATOM   1195  O  OH  . TYR A 1 148 ? 32.941  -8.959  23.861  1.00 22.45  ? 148 TYR A OH  1 
ATOM   1196  N  N   . LEU A 1 149 ? 35.676  -0.943  23.130  1.00 18.36  ? 149 LEU A N   1 
ATOM   1197  C  CA  . LEU A 1 149 ? 35.776  0.520   23.222  1.00 18.52  ? 149 LEU A CA  1 
ATOM   1198  C  C   . LEU A 1 149 ? 34.380  1.098   23.477  1.00 18.75  ? 149 LEU A C   1 
ATOM   1199  O  O   . LEU A 1 149 ? 33.505  1.015   22.617  1.00 19.79  ? 149 LEU A O   1 
ATOM   1200  C  CB  . LEU A 1 149 ? 36.370  1.040   21.910  1.00 19.04  ? 149 LEU A CB  1 
ATOM   1201  C  CG  . LEU A 1 149 ? 36.522  2.579   21.851  1.00 19.38  ? 149 LEU A CG  1 
ATOM   1202  C  CD1 . LEU A 1 149 ? 37.656  2.985   22.819  1.00 20.15  ? 149 LEU A CD1 1 
ATOM   1203  C  CD2 . LEU A 1 149 ? 36.747  3.010   20.403  1.00 20.75  ? 149 LEU A CD2 1 
ATOM   1204  N  N   . ASP A 1 150 ? 34.179  1.745   24.643  1.00 21.15  ? 150 ASP A N   1 
ATOM   1205  C  CA  . ASP A 1 150 ? 32.901  2.376   24.971  1.00 20.17  ? 150 ASP A CA  1 
ATOM   1206  C  C   . ASP A 1 150 ? 32.900  3.792   24.400  1.00 20.93  ? 150 ASP A C   1 
ATOM   1207  O  O   . ASP A 1 150 ? 33.640  4.638   24.888  1.00 21.87  ? 150 ASP A O   1 
ATOM   1208  C  CB  . ASP A 1 150 ? 32.791  2.399   26.500  1.00 20.88  ? 150 ASP A CB  1 
ATOM   1209  C  CG  . ASP A 1 150 ? 31.598  3.201   27.038  1.00 22.87  ? 150 ASP A CG  1 
ATOM   1210  O  OD1 . ASP A 1 150 ? 30.694  3.571   26.228  1.00 23.59  ? 150 ASP A OD1 1 
ATOM   1211  O  OD2 . ASP A 1 150 ? 31.561  3.388   28.289  1.00 21.32  ? 150 ASP A OD2 1 
ATOM   1212  N  N   . VAL A 1 151 ? 32.153  4.014   23.323  1.00 19.28  ? 151 VAL A N   1 
ATOM   1213  C  CA  . VAL A 1 151 ? 32.136  5.355   22.712  1.00 20.75  ? 151 VAL A CA  1 
ATOM   1214  C  C   . VAL A 1 151 ? 30.912  6.160   23.144  1.00 25.71  ? 151 VAL A C   1 
ATOM   1215  O  O   . VAL A 1 151 ? 30.642  7.210   22.550  1.00 23.74  ? 151 VAL A O   1 
ATOM   1216  C  CB  . VAL A 1 151 ? 32.218  5.275   21.177  1.00 17.70  ? 151 VAL A CB  1 
ATOM   1217  C  CG1 . VAL A 1 151 ? 33.485  4.553   20.708  1.00 20.24  ? 151 VAL A CG1 1 
ATOM   1218  C  CG2 . VAL A 1 151 ? 30.980  4.579   20.651  1.00 19.72  ? 151 VAL A CG2 1 
ATOM   1219  N  N   . GLY A 1 152 ? 30.193  5.730   24.185  1.00 23.76  ? 152 GLY A N   1 
ATOM   1220  C  CA  . GLY A 1 152 ? 28.983  6.395   24.637  1.00 23.46  ? 152 GLY A CA  1 
ATOM   1221  C  C   . GLY A 1 152 ? 29.251  7.653   25.457  1.00 21.18  ? 152 GLY A C   1 
ATOM   1222  O  O   . GLY A 1 152 ? 29.115  7.680   26.695  1.00 25.49  ? 152 GLY A O   1 
ATOM   1223  N  N   . VAL A 1 153 ? 29.635  8.715   24.763  1.00 20.05  ? 153 VAL A N   1 
ATOM   1224  C  CA  . VAL A 1 153 ? 29.973  9.980   25.409  1.00 22.02  ? 153 VAL A CA  1 
ATOM   1225  C  C   . VAL A 1 153 ? 29.031  11.079  24.943  1.00 21.24  ? 153 VAL A C   1 
ATOM   1226  O  O   . VAL A 1 153 ? 29.224  12.265  25.281  1.00 26.07  ? 153 VAL A O   1 
ATOM   1227  C  CB  . VAL A 1 153 ? 31.448  10.393  25.197  1.00 23.77  ? 153 VAL A CB  1 
ATOM   1228  C  CG1 . VAL A 1 153 ? 32.407  9.452   25.915  1.00 22.69  ? 153 VAL A CG1 1 
ATOM   1229  C  CG2 . VAL A 1 153 ? 31.816  10.520  23.676  1.00 22.39  ? 153 VAL A CG2 1 
ATOM   1230  N  N   . GLY A 1 154 ? 27.936  10.702  24.290  1.00 24.00  ? 154 GLY A N   1 
ATOM   1231  C  CA  . GLY A 1 154 ? 26.922  11.676  23.948  1.00 23.13  ? 154 GLY A CA  1 
ATOM   1232  C  C   . GLY A 1 154 ? 27.220  12.345  22.622  1.00 23.43  ? 154 GLY A C   1 
ATOM   1233  O  O   . GLY A 1 154 ? 28.211  12.033  21.958  1.00 22.13  ? 154 GLY A O   1 
ATOM   1234  N  N   . PRO A 1 155 ? 26.382  13.297  22.227  1.00 23.51  ? 155 PRO A N   1 
ATOM   1235  C  CA  . PRO A 1 155 ? 26.487  13.871  20.856  1.00 23.68  ? 155 PRO A CA  1 
ATOM   1236  C  C   . PRO A 1 155 ? 27.827  14.550  20.640  1.00 23.48  ? 155 PRO A C   1 
ATOM   1237  O  O   . PRO A 1 155 ? 28.318  15.301  21.498  1.00 22.28  ? 155 PRO A O   1 
ATOM   1238  C  CB  . PRO A 1 155 ? 25.343  14.901  20.809  1.00 27.31  ? 155 PRO A CB  1 
ATOM   1239  C  CG  . PRO A 1 155 ? 24.352  14.390  21.818  1.00 29.14  ? 155 PRO A CG  1 
ATOM   1240  C  CD  . PRO A 1 155 ? 25.194  13.750  22.940  1.00 25.07  ? 155 PRO A CD  1 
ATOM   1241  N  N   . TYR A 1 156 ? 28.326  14.399  19.423  1.00 22.12  ? 156 TYR A N   1 
ATOM   1242  C  CA  . TYR A 1 156 ? 29.567  15.045  19.021  1.00 19.50  ? 156 TYR A CA  1 
ATOM   1243  C  C   . TYR A 1 156 ? 29.494  16.556  19.224  1.00 21.73  ? 156 TYR A C   1 
ATOM   1244  O  O   . TYR A 1 156 ? 30.472  17.186  19.654  1.00 23.41  ? 156 TYR A O   1 
ATOM   1245  C  CB  . TYR A 1 156 ? 29.824  14.751  17.538  1.00 23.30  ? 156 TYR A CB  1 
ATOM   1246  C  CG  . TYR A 1 156 ? 31.173  15.262  17.058  1.00 19.46  ? 156 TYR A CG  1 
ATOM   1247  C  CD1 . TYR A 1 156 ? 32.349  14.712  17.572  1.00 22.83  ? 156 TYR A CD1 1 
ATOM   1248  C  CD2 . TYR A 1 156 ? 31.273  16.298  16.160  1.00 22.83  ? 156 TYR A CD2 1 
ATOM   1249  C  CE1 . TYR A 1 156 ? 33.598  15.175  17.203  1.00 22.80  ? 156 TYR A CE1 1 
ATOM   1250  C  CE2 . TYR A 1 156 ? 32.550  16.768  15.719  1.00 26.56  ? 156 TYR A CE2 1 
ATOM   1251  C  CZ  . TYR A 1 156 ? 33.695  16.169  16.244  1.00 25.11  ? 156 TYR A CZ  1 
ATOM   1252  O  OH  . TYR A 1 156 ? 34.951  16.598  15.911  1.00 28.92  ? 156 TYR A OH  1 
ATOM   1253  N  N   A ARG A 1 157 ? 28.332  17.136  18.965  0.60 23.27  ? 157 ARG A N   1 
ATOM   1254  N  N   B ARG A 1 157 ? 28.332  17.152  18.957  0.40 23.29  ? 157 ARG A N   1 
ATOM   1255  C  CA  A ARG A 1 157 ? 28.199  18.589  19.056  0.60 22.60  ? 157 ARG A CA  1 
ATOM   1256  C  CA  B ARG A 1 157 ? 28.220  18.610  19.058  0.40 22.65  ? 157 ARG A CA  1 
ATOM   1257  C  C   A ARG A 1 157 ? 28.356  19.093  20.493  0.60 23.61  ? 157 ARG A C   1 
ATOM   1258  C  C   B ARG A 1 157 ? 28.241  19.111  20.506  0.40 23.65  ? 157 ARG A C   1 
ATOM   1259  O  O   A ARG A 1 157 ? 28.630  20.287  20.691  0.60 25.92  ? 157 ARG A O   1 
ATOM   1260  O  O   B ARG A 1 157 ? 28.279  20.329  20.727  0.40 25.79  ? 157 ARG A O   1 
ATOM   1261  C  CB  A ARG A 1 157 ? 26.835  19.014  18.526  0.60 27.09  ? 157 ARG A CB  1 
ATOM   1262  C  CB  B ARG A 1 157 ? 26.934  19.114  18.394  0.40 27.07  ? 157 ARG A CB  1 
ATOM   1263  C  CG  A ARG A 1 157 ? 25.695  18.322  19.273  0.60 27.64  ? 157 ARG A CG  1 
ATOM   1264  C  CG  B ARG A 1 157 ? 25.678  18.528  19.025  0.40 27.65  ? 157 ARG A CG  1 
ATOM   1265  C  CD  A ARG A 1 157 ? 24.375  19.137  19.351  0.60 31.46  ? 157 ARG A CD  1 
ATOM   1266  C  CD  B ARG A 1 157 ? 24.365  19.261  18.680  0.40 30.12  ? 157 ARG A CD  1 
ATOM   1267  N  NE  A ARG A 1 157 ? 23.708  19.169  18.058  0.60 33.44  ? 157 ARG A NE  1 
ATOM   1268  N  NE  B ARG A 1 157 ? 23.266  18.594  19.376  0.40 29.27  ? 157 ARG A NE  1 
ATOM   1269  C  CZ  A ARG A 1 157 ? 22.393  19.125  17.840  0.60 30.82  ? 157 ARG A CZ  1 
ATOM   1270  C  CZ  B ARG A 1 157 ? 23.039  18.683  20.685  0.40 28.46  ? 157 ARG A CZ  1 
ATOM   1271  N  NH1 A ARG A 1 157 ? 21.521  18.919  18.810  0.60 28.92  ? 157 ARG A NH1 1 
ATOM   1272  N  NH1 B ARG A 1 157 ? 23.638  19.594  21.431  0.40 32.01  ? 157 ARG A NH1 1 
ATOM   1273  N  NH2 A ARG A 1 157 ? 21.952  19.257  16.602  0.60 29.10  ? 157 ARG A NH2 1 
ATOM   1274  N  NH2 B ARG A 1 157 ? 22.218  17.813  21.263  0.40 29.53  ? 157 ARG A NH2 1 
ATOM   1275  N  N   . ASP A 1 158 ? 28.177  18.212  21.492  1.00 23.02  ? 158 ASP A N   1 
ATOM   1276  C  CA  . ASP A 1 158 ? 28.265  18.549  22.920  1.00 23.91  ? 158 ASP A CA  1 
ATOM   1277  C  C   . ASP A 1 158 ? 29.580  18.099  23.529  1.00 25.02  ? 158 ASP A C   1 
ATOM   1278  O  O   . ASP A 1 158 ? 29.711  18.100  24.759  1.00 25.58  ? 158 ASP A O   1 
ATOM   1279  C  CB  . ASP A 1 158 ? 27.133  17.882  23.704  1.00 23.80  ? 158 ASP A CB  1 
ATOM   1280  C  CG  . ASP A 1 158 ? 25.742  18.322  23.233  1.00 24.97  ? 158 ASP A CG  1 
ATOM   1281  O  OD1 . ASP A 1 158 ? 25.603  19.447  22.694  1.00 30.67  ? 158 ASP A OD1 1 
ATOM   1282  O  OD2 . ASP A 1 158 ? 24.787  17.613  23.518  1.00 32.85  ? 158 ASP A OD2 1 
ATOM   1283  N  N   . MET A 1 159 ? 30.520  17.648  22.705  1.00 23.13  ? 159 MET A N   1 
ATOM   1284  C  CA  . MET A 1 159 ? 31.739  16.988  23.174  1.00 26.34  ? 159 MET A CA  1 
ATOM   1285  C  C   . MET A 1 159 ? 32.502  17.893  24.158  1.00 26.40  ? 159 MET A C   1 
ATOM   1286  O  O   . MET A 1 159 ? 32.531  19.139  24.032  1.00 27.45  ? 159 MET A O   1 
ATOM   1287  C  CB  . MET A 1 159 ? 32.640  16.746  21.979  1.00 30.31  ? 159 MET A CB  1 
ATOM   1288  C  CG  . MET A 1 159 ? 33.745  15.752  22.020  1.00 32.17  ? 159 MET A CG  1 
ATOM   1289  S  SD  . MET A 1 159 ? 33.372  14.179  22.858  1.00 31.73  ? 159 MET A SD  1 
ATOM   1290  C  CE  . MET A 1 159 ? 31.911  13.734  21.974  1.00 28.73  ? 159 MET A CE  1 
ATOM   1291  N  N   . THR A 1 160 ? 33.076  17.288  25.202  1.00 22.93  ? 160 THR A N   1 
ATOM   1292  C  CA  . THR A 1 160 ? 33.961  17.975  26.139  1.00 25.73  ? 160 THR A CA  1 
ATOM   1293  C  C   . THR A 1 160 ? 35.357  17.353  26.070  1.00 25.42  ? 160 THR A C   1 
ATOM   1294  O  O   . THR A 1 160 ? 35.511  16.229  25.561  1.00 22.12  ? 160 THR A O   1 
ATOM   1295  C  CB  . THR A 1 160 ? 33.435  17.849  27.564  1.00 24.58  ? 160 THR A CB  1 
ATOM   1296  O  OG1 . THR A 1 160 ? 33.527  16.467  27.943  1.00 23.24  ? 160 THR A OG1 1 
ATOM   1297  C  CG2 . THR A 1 160 ? 31.968  18.272  27.692  1.00 25.35  ? 160 THR A CG2 1 
ATOM   1298  N  N   . ASP A 1 161 ? 36.356  18.060  26.639  1.00 24.90  ? 161 ASP A N   1 
ATOM   1299  C  CA  . ASP A 1 161 ? 37.701  17.494  26.754  1.00 25.38  ? 161 ASP A CA  1 
ATOM   1300  C  C   . ASP A 1 161 ? 37.672  16.151  27.498  1.00 24.07  ? 161 ASP A C   1 
ATOM   1301  O  O   . ASP A 1 161 ? 38.356  15.195  27.097  1.00 24.52  ? 161 ASP A O   1 
ATOM   1302  C  CB  . ASP A 1 161 ? 38.650  18.434  27.501  1.00 29.20  ? 161 ASP A CB  1 
ATOM   1303  C  CG  . ASP A 1 161 ? 38.952  19.740  26.745  1.00 33.28  ? 161 ASP A CG  1 
ATOM   1304  O  OD1 . ASP A 1 161 ? 39.058  19.727  25.495  1.00 35.33  ? 161 ASP A OD1 1 
ATOM   1305  O  OD2 . ASP A 1 161 ? 39.138  20.771  27.432  1.00 37.27  ? 161 ASP A OD2 1 
ATOM   1306  N  N   . ALA A 1 162 ? 36.934  16.092  28.621  1.00 22.97  ? 162 ALA A N   1 
ATOM   1307  C  CA  . ALA A 1 162 ? 36.892  14.860  29.417  1.00 24.88  ? 162 ALA A CA  1 
ATOM   1308  C  C   . ALA A 1 162 ? 36.259  13.719  28.641  1.00 22.82  ? 162 ALA A C   1 
ATOM   1309  O  O   . ALA A 1 162 ? 36.689  12.555  28.753  1.00 23.73  ? 162 ALA A O   1 
ATOM   1310  C  CB  . ALA A 1 162 ? 36.147  15.128  30.737  1.00 25.60  ? 162 ALA A CB  1 
ATOM   1311  N  N   . ARG A 1 163 ? 35.182  13.992  27.901  1.00 21.65  ? 163 ARG A N   1 
ATOM   1312  C  CA  . ARG A 1 163 ? 34.581  12.935  27.097  1.00 23.31  ? 163 ARG A CA  1 
ATOM   1313  C  C   . ARG A 1 163 ? 35.573  12.387  26.075  1.00 23.72  ? 163 ARG A C   1 
ATOM   1314  O  O   . ARG A 1 163 ? 35.675  11.168  25.885  1.00 21.93  ? 163 ARG A O   1 
ATOM   1315  C  CB  . ARG A 1 163 ? 33.308  13.455  26.409  1.00 22.17  ? 163 ARG A CB  1 
ATOM   1316  C  CG  . ARG A 1 163 ? 32.171  13.671  27.413  1.00 25.02  ? 163 ARG A CG  1 
ATOM   1317  C  CD  . ARG A 1 163 ? 30.948  14.412  26.751  1.00 21.83  ? 163 ARG A CD  1 
ATOM   1318  N  NE  . ARG A 1 163 ? 29.914  14.495  27.760  1.00 26.16  ? 163 ARG A NE  1 
ATOM   1319  C  CZ  . ARG A 1 163 ? 28.757  15.115  27.613  1.00 26.58  ? 163 ARG A CZ  1 
ATOM   1320  N  NH1 . ARG A 1 163 ? 28.418  15.674  26.467  1.00 24.44  ? 163 ARG A NH1 1 
ATOM   1321  N  NH2 . ARG A 1 163 ? 27.919  15.159  28.643  1.00 22.69  ? 163 ARG A NH2 1 
ATOM   1322  N  N   . LEU A 1 164 ? 36.294  13.275  25.387  1.00 22.43  ? 164 LEU A N   1 
ATOM   1323  C  CA  . LEU A 1 164 ? 37.274  12.828  24.402  1.00 23.39  ? 164 LEU A CA  1 
ATOM   1324  C  C   . LEU A 1 164 ? 38.431  12.117  25.100  1.00 25.90  ? 164 LEU A C   1 
ATOM   1325  O  O   . LEU A 1 164 ? 38.933  11.114  24.585  1.00 23.07  ? 164 LEU A O   1 
ATOM   1326  C  CB  . LEU A 1 164 ? 37.736  14.023  23.555  1.00 24.73  ? 164 LEU A CB  1 
ATOM   1327  C  CG  . LEU A 1 164 ? 38.765  13.798  22.451  1.00 24.41  ? 164 LEU A CG  1 
ATOM   1328  C  CD1 . LEU A 1 164 ? 38.364  12.714  21.469  1.00 27.54  ? 164 LEU A CD1 1 
ATOM   1329  C  CD2 . LEU A 1 164 ? 39.101  15.141  21.733  1.00 24.34  ? 164 LEU A CD2 1 
ATOM   1330  N  N   . ASP A 1 165 ? 38.819  12.589  26.288  1.00 23.34  ? 165 ASP A N   1 
ATOM   1331  C  CA  . ASP A 1 165 ? 39.820  11.893  27.116  1.00 22.83  ? 165 ASP A CA  1 
ATOM   1332  C  C   . ASP A 1 165 ? 39.420  10.431  27.351  1.00 22.83  ? 165 ASP A C   1 
ATOM   1333  O  O   . ASP A 1 165 ? 40.264  9.522   27.292  1.00 23.83  ? 165 ASP A O   1 
ATOM   1334  C  CB  . ASP A 1 165 ? 39.962  12.562  28.480  1.00 25.67  ? 165 ASP A CB  1 
ATOM   1335  C  CG  . ASP A 1 165 ? 40.722  13.893  28.448  1.00 28.17  ? 165 ASP A CG  1 
ATOM   1336  O  OD1 . ASP A 1 165 ? 41.281  14.272  27.380  1.00 28.14  ? 165 ASP A OD1 1 
ATOM   1337  O  OD2 . ASP A 1 165 ? 40.734  14.576  29.521  1.00 27.02  ? 165 ASP A OD2 1 
ATOM   1338  N  N   . TYR A 1 166 ? 38.132  10.200  27.636  1.00 20.78  ? 166 TYR A N   1 
ATOM   1339  C  CA  . TYR A 1 166 ? 37.679  8.857   27.996  1.00 17.48  ? 166 TYR A CA  1 
ATOM   1340  C  C   . TYR A 1 166 ? 37.880  7.916   26.830  1.00 20.05  ? 166 TYR A C   1 
ATOM   1341  O  O   . TYR A 1 166 ? 38.405  6.824   26.988  1.00 21.49  ? 166 TYR A O   1 
ATOM   1342  C  CB  . TYR A 1 166 ? 36.210  8.916   28.375  1.00 19.97  ? 166 TYR A CB  1 
ATOM   1343  C  CG  . TYR A 1 166 ? 35.606  7.558   28.658  1.00 20.66  ? 166 TYR A CG  1 
ATOM   1344  C  CD1 . TYR A 1 166 ? 36.227  6.656   29.512  1.00 23.01  ? 166 TYR A CD1 1 
ATOM   1345  C  CD2 . TYR A 1 166 ? 34.360  7.231   28.139  1.00 20.89  ? 166 TYR A CD2 1 
ATOM   1346  C  CE1 . TYR A 1 166 ? 35.635  5.429   29.783  1.00 20.48  ? 166 TYR A CE1 1 
ATOM   1347  C  CE2 . TYR A 1 166 ? 33.753  6.002   28.405  1.00 20.46  ? 166 TYR A CE2 1 
ATOM   1348  C  CZ  . TYR A 1 166 ? 34.394  5.128   29.231  1.00 21.02  ? 166 TYR A CZ  1 
ATOM   1349  O  OH  . TYR A 1 166 ? 33.847  3.884   29.472  1.00 21.57  ? 166 TYR A OH  1 
ATOM   1350  N  N   . VAL A 1 167 ? 37.522  8.355   25.650  1.00 19.70  ? 167 VAL A N   1 
ATOM   1351  C  CA  . VAL A 1 167 ? 37.687  7.503   24.472  1.00 18.73  ? 167 VAL A CA  1 
ATOM   1352  C  C   . VAL A 1 167 ? 39.172  7.349   24.091  1.00 20.93  ? 167 VAL A C   1 
ATOM   1353  O  O   . VAL A 1 167 ? 39.623  6.242   23.724  1.00 21.97  ? 167 VAL A O   1 
ATOM   1354  C  CB  . VAL A 1 167 ? 36.837  8.045   23.316  1.00 21.21  ? 167 VAL A CB  1 
ATOM   1355  C  CG1 . VAL A 1 167 ? 36.997  7.139   22.053  1.00 21.69  ? 167 VAL A CG1 1 
ATOM   1356  C  CG2 . VAL A 1 167 ? 35.363  8.030   23.735  1.00 21.39  ? 167 VAL A CG2 1 
ATOM   1357  N  N   . ALA A 1 168 ? 39.932  8.470   24.031  1.00 19.46  ? 168 ALA A N   1 
ATOM   1358  C  CA  . ALA A 1 168 ? 41.369  8.384   23.727  1.00 20.06  ? 168 ALA A CA  1 
ATOM   1359  C  C   . ALA A 1 168 ? 42.119  7.482   24.719  1.00 21.83  ? 168 ALA A C   1 
ATOM   1360  O  O   . ALA A 1 168 ? 42.956  6.652   24.304  1.00 20.73  ? 168 ALA A O   1 
ATOM   1361  C  CB  . ALA A 1 168 ? 41.969  9.801   23.683  1.00 21.78  ? 168 ALA A CB  1 
ATOM   1362  N  N   . ASN A 1 169 ? 41.821  7.599   26.031  1.00 20.91  ? 169 ASN A N   1 
ATOM   1363  C  CA  . ASN A 1 169 ? 42.552  6.781   26.987  1.00 21.18  ? 169 ASN A CA  1 
ATOM   1364  C  C   . ASN A 1 169 ? 42.182  5.334   26.837  1.00 21.75  ? 169 ASN A C   1 
ATOM   1365  O  O   . ASN A 1 169 ? 43.048  4.466   27.000  1.00 22.91  ? 169 ASN A O   1 
ATOM   1366  C  CB  . ASN A 1 169 ? 42.295  7.249   28.411  1.00 24.05  ? 169 ASN A CB  1 
ATOM   1367  C  CG  . ASN A 1 169 ? 42.946  8.623   28.653  1.00 25.27  ? 169 ASN A CG  1 
ATOM   1368  O  OD1 . ASN A 1 169 ? 43.814  9.053   27.862  1.00 27.60  ? 169 ASN A OD1 1 
ATOM   1369  N  ND2 . ASN A 1 169 ? 42.540  9.311   29.710  1.00 29.11  ? 169 ASN A ND2 1 
ATOM   1370  N  N   . GLN A 1 170 ? 40.926  5.054   26.501  1.00 20.60  ? 170 GLN A N   1 
ATOM   1371  C  CA  . GLN A 1 170 ? 40.567  3.652   26.215  1.00 20.98  ? 170 GLN A CA  1 
ATOM   1372  C  C   . GLN A 1 170 ? 41.338  3.130   25.011  1.00 21.94  ? 170 GLN A C   1 
ATOM   1373  O  O   . GLN A 1 170 ? 41.773  1.972   24.999  1.00 23.57  ? 170 GLN A O   1 
ATOM   1374  C  CB  . GLN A 1 170 ? 39.089  3.522   25.918  1.00 20.57  ? 170 GLN A CB  1 
ATOM   1375  C  CG  . GLN A 1 170 ? 38.149  3.700   27.131  1.00 19.15  ? 170 GLN A CG  1 
ATOM   1376  C  CD  . GLN A 1 170 ? 36.772  3.527   26.663  1.00 22.40  ? 170 GLN A CD  1 
ATOM   1377  O  OE1 . GLN A 1 170 ? 36.347  2.402   26.373  1.00 21.67  ? 170 GLN A OE1 1 
ATOM   1378  N  NE2 . GLN A 1 170 ? 36.043  4.602   26.553  1.00 20.88  ? 170 GLN A NE2 1 
ATOM   1379  N  N   . LEU A 1 171 ? 41.511  3.956   23.967  1.00 19.53  ? 171 LEU A N   1 
ATOM   1380  C  CA  . LEU A 1 171 ? 42.252  3.477   22.790  1.00 22.47  ? 171 LEU A CA  1 
ATOM   1381  C  C   . LEU A 1 171 ? 43.687  3.100   23.147  1.00 22.38  ? 171 LEU A C   1 
ATOM   1382  O  O   . LEU A 1 171 ? 44.229  2.119   22.627  1.00 23.46  ? 171 LEU A O   1 
ATOM   1383  C  CB  . LEU A 1 171 ? 42.261  4.545   21.686  1.00 19.25  ? 171 LEU A CB  1 
ATOM   1384  C  CG  . LEU A 1 171 ? 40.887  4.593   20.979  1.00 20.13  ? 171 LEU A CG  1 
ATOM   1385  C  CD1 . LEU A 1 171 ? 40.807  5.877   20.148  1.00 20.00  ? 171 LEU A CD1 1 
ATOM   1386  C  CD2 . LEU A 1 171 ? 40.780  3.364   20.036  1.00 20.34  ? 171 LEU A CD2 1 
ATOM   1387  N  N   . HIS A 1 172 ? 44.299  3.836   24.080  1.00 21.71  ? 172 HIS A N   1 
ATOM   1388  C  CA  . HIS A 1 172 ? 45.642  3.460   24.493  1.00 22.51  ? 172 HIS A CA  1 
ATOM   1389  C  C   . HIS A 1 172 ? 45.620  2.108   25.207  1.00 23.19  ? 172 HIS A C   1 
ATOM   1390  O  O   . HIS A 1 172 ? 46.568  1.324   25.054  1.00 25.45  ? 172 HIS A O   1 
ATOM   1391  C  CB  . HIS A 1 172 ? 46.274  4.518   25.400  1.00 23.46  ? 172 HIS A CB  1 
ATOM   1392  C  CG  . HIS A 1 172 ? 46.740  5.747   24.687  1.00 25.44  ? 172 HIS A CG  1 
ATOM   1393  N  ND1 . HIS A 1 172 ? 47.896  5.808   23.930  1.00 24.13  ? 172 HIS A ND1 1 
ATOM   1394  C  CD2 . HIS A 1 172 ? 46.174  6.972   24.614  1.00 25.08  ? 172 HIS A CD2 1 
ATOM   1395  C  CE1 . HIS A 1 172 ? 48.019  7.028   23.422  1.00 26.46  ? 172 HIS A CE1 1 
ATOM   1396  N  NE2 . HIS A 1 172 ? 46.992  7.756   23.826  1.00 26.46  ? 172 HIS A NE2 1 
ATOM   1397  N  N   . ASP A 1 173 ? 44.564  1.839   26.012  1.00 21.94  ? 173 ASP A N   1 
ATOM   1398  C  CA  . ASP A 1 173 ? 44.376  0.485   26.570  1.00 22.85  ? 173 ASP A CA  1 
ATOM   1399  C  C   . ASP A 1 173 ? 44.225  -0.530  25.445  1.00 24.09  ? 173 ASP A C   1 
ATOM   1400  O  O   . ASP A 1 173 ? 44.712  -1.666  25.536  1.00 24.05  ? 173 ASP A O   1 
ATOM   1401  C  CB  . ASP A 1 173 ? 43.129  0.377   27.439  1.00 24.98  ? 173 ASP A CB  1 
ATOM   1402  C  CG  . ASP A 1 173 ? 43.231  1.127   28.762  1.00 29.02  ? 173 ASP A CG  1 
ATOM   1403  O  OD1 . ASP A 1 173 ? 44.301  1.678   29.079  1.00 29.72  ? 173 ASP A OD1 1 
ATOM   1404  O  OD2 . ASP A 1 173 ? 42.212  1.137   29.492  1.00 31.58  ? 173 ASP A OD2 1 
ATOM   1405  N  N   . GLY A 1 174 ? 43.564  -0.121  24.376  1.00 22.35  ? 174 GLY A N   1 
ATOM   1406  C  CA  . GLY A 1 174 ? 43.360  -1.015  23.227  1.00 24.03  ? 174 GLY A CA  1 
ATOM   1407  C  C   . GLY A 1 174 ? 44.657  -1.397  22.550  1.00 22.35  ? 174 GLY A C   1 
ATOM   1408  O  O   . GLY A 1 174 ? 44.818  -2.530  22.089  1.00 23.64  ? 174 GLY A O   1 
ATOM   1409  N  N   . ILE A 1 175 ? 45.572  -0.431  22.394  1.00 22.03  ? 175 ILE A N   1 
ATOM   1410  C  CA  . ILE A 1 175 ? 46.923  -0.714  21.877  1.00 22.86  ? 175 ILE A CA  1 
ATOM   1411  C  C   . ILE A 1 175 ? 47.611  -1.770  22.746  1.00 24.79  ? 175 ILE A C   1 
ATOM   1412  O  O   . ILE A 1 175 ? 48.088  -2.805  22.262  1.00 23.85  ? 175 ILE A O   1 
ATOM   1413  C  CB  . ILE A 1 175 ? 47.742  0.589   21.820  1.00 24.70  ? 175 ILE A CB  1 
ATOM   1414  C  CG1 . ILE A 1 175 ? 47.188  1.483   20.698  1.00 23.33  ? 175 ILE A CG1 1 
ATOM   1415  C  CG2 . ILE A 1 175 ? 49.197  0.294   21.672  1.00 24.17  ? 175 ILE A CG2 1 
ATOM   1416  C  CD1 . ILE A 1 175 ? 47.769  2.908   20.638  1.00 24.87  ? 175 ILE A CD1 1 
ATOM   1417  N  N   . ALA A 1 176 ? 47.598  -1.567  24.054  1.00 22.86  ? 176 ALA A N   1 
ATOM   1418  C  CA  . ALA A 1 176 ? 48.236  -2.532  24.925  1.00 24.75  ? 176 ALA A CA  1 
ATOM   1419  C  C   . ALA A 1 176 ? 47.551  -3.878  24.800  1.00 25.93  ? 176 ALA A C   1 
ATOM   1420  O  O   . ALA A 1 176 ? 48.216  -4.931  24.826  1.00 27.54  ? 176 ALA A O   1 
ATOM   1421  C  CB  . ALA A 1 176 ? 48.209  -2.024  26.365  1.00 27.92  ? 176 ALA A CB  1 
ATOM   1422  N  N   . PHE A 1 177 ? 46.226  -3.861  24.598  1.00 23.23  ? 177 PHE A N   1 
ATOM   1423  C  CA  . PHE A 1 177 ? 45.465  -5.106  24.493  1.00 24.65  ? 177 PHE A CA  1 
ATOM   1424  C  C   . PHE A 1 177 ? 45.876  -5.867  23.250  1.00 24.53  ? 177 PHE A C   1 
ATOM   1425  O  O   . PHE A 1 177 ? 46.075  -7.098  23.292  1.00 24.22  ? 177 PHE A O   1 
ATOM   1426  C  CB  . PHE A 1 177 ? 43.959  -4.807  24.458  1.00 24.63  ? 177 PHE A CB  1 
ATOM   1427  C  CG  . PHE A 1 177 ? 43.107  -5.991  24.045  1.00 22.76  ? 177 PHE A CG  1 
ATOM   1428  C  CD1 . PHE A 1 177 ? 42.859  -6.220  22.696  1.00 25.38  ? 177 PHE A CD1 1 
ATOM   1429  C  CD2 . PHE A 1 177 ? 42.623  -6.881  24.997  1.00 25.41  ? 177 PHE A CD2 1 
ATOM   1430  C  CE1 . PHE A 1 177 ? 42.108  -7.338  22.302  1.00 23.55  ? 177 PHE A CE1 1 
ATOM   1431  C  CE2 . PHE A 1 177 ? 41.839  -8.001  24.629  1.00 22.82  ? 177 PHE A CE2 1 
ATOM   1432  C  CZ  . PHE A 1 177 ? 41.605  -8.217  23.266  1.00 21.58  ? 177 PHE A CZ  1 
ATOM   1433  N  N   . VAL A 1 178 ? 45.931  -5.180  22.112  1.00 21.50  ? 178 VAL A N   1 
ATOM   1434  C  CA  . VAL A 1 178 ? 46.187  -5.951  20.888  1.00 20.46  ? 178 VAL A CA  1 
ATOM   1435  C  C   . VAL A 1 178 ? 47.616  -6.448  20.870  1.00 25.25  ? 178 VAL A C   1 
ATOM   1436  O  O   . VAL A 1 178 ? 47.894  -7.495  20.262  1.00 25.92  ? 178 VAL A O   1 
ATOM   1437  C  CB  . VAL A 1 178 ? 45.836  -5.145  19.624  1.00 22.27  ? 178 VAL A CB  1 
ATOM   1438  C  CG1 . VAL A 1 178 ? 44.326  -4.783  19.617  1.00 21.75  ? 178 VAL A CG1 1 
ATOM   1439  C  CG2 . VAL A 1 178 ? 46.753  -3.950  19.417  1.00 23.66  ? 178 VAL A CG2 1 
ATOM   1440  N  N   . GLU A 1 179 ? 48.554  -5.731  21.516  1.00 21.55  ? 179 GLU A N   1 
ATOM   1441  C  CA  . GLU A 1 179 ? 49.922  -6.228  21.594  1.00 22.65  ? 179 GLU A CA  1 
ATOM   1442  C  C   . GLU A 1 179 ? 49.947  -7.540  22.370  1.00 25.33  ? 179 GLU A C   1 
ATOM   1443  O  O   . GLU A 1 179 ? 50.609  -8.519  21.958  1.00 27.70  ? 179 GLU A O   1 
ATOM   1444  C  CB  . GLU A 1 179 ? 50.819  -5.204  22.286  1.00 26.90  ? 179 GLU A CB  1 
ATOM   1445  C  CG  . GLU A 1 179 ? 51.136  -3.975  21.401  1.00 25.80  ? 179 GLU A CG  1 
ATOM   1446  C  CD  . GLU A 1 179 ? 52.096  -3.027  22.036  1.00 31.22  ? 179 GLU A CD  1 
ATOM   1447  O  OE1 . GLU A 1 179 ? 51.741  -2.502  23.148  1.00 33.05  ? 179 GLU A OE1 1 
ATOM   1448  O  OE2 . GLU A 1 179 ? 53.191  -2.819  21.463  1.00 30.84  ? 179 GLU A OE2 1 
ATOM   1449  N  N   . LYS A 1 180 ? 49.315  -7.514  23.546  1.00 24.28  ? 180 LYS A N   1 
ATOM   1450  C  CA  . LYS A 1 180 ? 49.272  -8.679  24.422  1.00 25.84  ? 180 LYS A CA  1 
ATOM   1451  C  C   . LYS A 1 180 ? 48.650  -9.854  23.694  1.00 28.98  ? 180 LYS A C   1 
ATOM   1452  O  O   . LYS A 1 180 ? 49.202  -10.963 23.694  1.00 26.53  ? 180 LYS A O   1 
ATOM   1453  C  CB  . LYS A 1 180 ? 48.482  -8.346  25.682  1.00 24.49  ? 180 LYS A CB  1 
ATOM   1454  C  CG  . LYS A 1 180 ? 48.564  -9.405  26.790  1.00 33.86  ? 180 LYS A CG  1 
ATOM   1455  C  CD  . LYS A 1 180 ? 48.403  -8.784  28.188  1.00 37.79  ? 180 LYS A CD  1 
ATOM   1456  C  CE  . LYS A 1 180 ? 49.686  -8.945  29.011  1.00 47.24  ? 180 LYS A CE  1 
ATOM   1457  N  NZ  . LYS A 1 180 ? 49.828  -7.855  30.056  1.00 56.53  ? 180 LYS A NZ  1 
ATOM   1458  N  N   . ALA A 1 181 ? 47.491  -9.617  23.067  1.00 22.06  ? 181 ALA A N   1 
ATOM   1459  C  CA  . ALA A 1 181 ? 46.713  -10.710 22.487  1.00 24.74  ? 181 ALA A CA  1 
ATOM   1460  C  C   . ALA A 1 181 ? 47.421  -11.307 21.291  1.00 28.74  ? 181 ALA A C   1 
ATOM   1461  O  O   . ALA A 1 181 ? 47.346  -12.524 21.090  1.00 28.41  ? 181 ALA A O   1 
ATOM   1462  C  CB  . ALA A 1 181 ? 45.305  -10.218 22.100  1.00 26.89  ? 181 ALA A CB  1 
ATOM   1463  N  N   . SER A 1 182 ? 48.154  -10.493 20.514  1.00 23.88  ? 182 SER A N   1 
ATOM   1464  C  CA  . SER A 1 182 ? 48.805  -10.973 19.307  1.00 21.04  ? 182 SER A CA  1 
ATOM   1465  C  C   . SER A 1 182 ? 50.256  -11.402 19.524  1.00 21.14  ? 182 SER A C   1 
ATOM   1466  O  O   . SER A 1 182 ? 50.796  -12.167 18.704  1.00 25.83  ? 182 SER A O   1 
ATOM   1467  C  CB  . SER A 1 182 ? 48.767  -9.889  18.239  1.00 25.32  ? 182 SER A CB  1 
ATOM   1468  O  OG  . SER A 1 182 ? 49.694  -8.854  18.615  1.00 27.09  ? 182 SER A OG  1 
ATOM   1469  N  N   . GLY A 1 183 ? 50.912  -10.948 20.575  1.00 25.36  ? 183 GLY A N   1 
ATOM   1470  C  CA  . GLY A 1 183 ? 52.325  -11.226 20.711  1.00 25.87  ? 183 GLY A CA  1 
ATOM   1471  C  C   . GLY A 1 183 ? 53.211  -10.342 19.876  1.00 29.26  ? 183 GLY A C   1 
ATOM   1472  O  O   . GLY A 1 183 ? 54.428  -10.587 19.821  1.00 29.18  ? 183 GLY A O   1 
ATOM   1473  N  N   . ARG A 1 184 ? 52.650  -9.325  19.219  1.00 26.50  ? 184 ARG A N   1 
ATOM   1474  C  CA  . ARG A 1 184 ? 53.428  -8.459  18.343  1.00 26.47  ? 184 ARG A CA  1 
ATOM   1475  C  C   . ARG A 1 184 ? 53.634  -7.101  19.011  1.00 28.24  ? 184 ARG A C   1 
ATOM   1476  O  O   . ARG A 1 184 ? 52.906  -6.733  19.933  1.00 27.30  ? 184 ARG A O   1 
ATOM   1477  C  CB  . ARG A 1 184 ? 52.750  -8.262  16.991  1.00 23.13  ? 184 ARG A CB  1 
ATOM   1478  C  CG  . ARG A 1 184 ? 52.644  -9.578  16.148  1.00 29.11  ? 184 ARG A CG  1 
ATOM   1479  C  CD  . ARG A 1 184 ? 52.238  -9.290  14.723  1.00 30.12  ? 184 ARG A CD  1 
ATOM   1480  N  NE  . ARG A 1 184 ? 51.966  -10.488 13.904  1.00 29.28  ? 184 ARG A NE  1 
ATOM   1481  C  CZ  . ARG A 1 184 ? 51.625  -10.386 12.622  1.00 27.14  ? 184 ARG A CZ  1 
ATOM   1482  N  NH1 . ARG A 1 184 ? 51.564  -9.203  12.017  1.00 26.02  ? 184 ARG A NH1 1 
ATOM   1483  N  NH2 . ARG A 1 184 ? 51.372  -11.494 11.911  1.00 25.66  ? 184 ARG A NH2 1 
ATOM   1484  N  N   . LYS A 1 185 ? 54.668  -6.396  18.547  1.00 30.13  ? 185 LYS A N   1 
ATOM   1485  C  CA  . LYS A 1 185 ? 54.930  -5.024  18.960  1.00 29.40  ? 185 LYS A CA  1 
ATOM   1486  C  C   . LYS A 1 185 ? 54.190  -4.080  18.026  1.00 31.02  ? 185 LYS A C   1 
ATOM   1487  O  O   . LYS A 1 185 ? 54.357  -4.150  16.812  1.00 32.20  ? 185 LYS A O   1 
ATOM   1488  C  CB  . LYS A 1 185 ? 56.423  -4.710  18.898  1.00 30.92  ? 185 LYS A CB  1 
ATOM   1489  C  CG  . LYS A 1 185 ? 56.717  -3.343  19.590  1.00 36.16  ? 185 LYS A CG  1 
ATOM   1490  C  CD  . LYS A 1 185 ? 58.217  -3.096  19.652  1.00 41.13  ? 185 LYS A CD  1 
ATOM   1491  C  CE  . LYS A 1 185 ? 58.599  -2.220  20.850  1.00 46.70  ? 185 LYS A CE  1 
ATOM   1492  N  NZ  . LYS A 1 185 ? 57.714  -1.013  20.981  1.00 45.68  ? 185 LYS A NZ  1 
ATOM   1493  N  N   . PHE A 1 186 ? 53.414  -3.180  18.600  1.00 28.23  ? 186 PHE A N   1 
ATOM   1494  C  CA  . PHE A 1 186 ? 52.639  -2.205  17.842  1.00 27.80  ? 186 PHE A CA  1 
ATOM   1495  C  C   . PHE A 1 186 ? 53.563  -1.179  17.234  1.00 29.54  ? 186 PHE A C   1 
ATOM   1496  O  O   . PHE A 1 186 ? 54.483  -0.701  17.907  1.00 32.50  ? 186 PHE A O   1 
ATOM   1497  C  CB  . PHE A 1 186 ? 51.668  -1.562  18.816  1.00 27.13  ? 186 PHE A CB  1 
ATOM   1498  C  CG  . PHE A 1 186 ? 50.765  -0.524  18.248  1.00 26.12  ? 186 PHE A CG  1 
ATOM   1499  C  CD1 . PHE A 1 186 ? 51.148  0.812   18.294  1.00 26.99  ? 186 PHE A CD1 1 
ATOM   1500  C  CD2 . PHE A 1 186 ? 49.481  -0.856  17.832  1.00 24.12  ? 186 PHE A CD2 1 
ATOM   1501  C  CE1 . PHE A 1 186 ? 50.237  1.815   17.886  1.00 24.62  ? 186 PHE A CE1 1 
ATOM   1502  C  CE2 . PHE A 1 186 ? 48.591  0.080   17.400  1.00 25.03  ? 186 PHE A CE2 1 
ATOM   1503  C  CZ  . PHE A 1 186 ? 48.947  1.430   17.434  1.00 25.41  ? 186 PHE A CZ  1 
ATOM   1504  N  N   . ASP A 1 187 ? 53.337  -0.823  15.966  1.00 24.47  ? 187 ASP A N   1 
ATOM   1505  C  CA  . ASP A 1 187 ? 54.223  0.067   15.224  1.00 24.04  ? 187 ASP A CA  1 
ATOM   1506  C  C   . ASP A 1 187 ? 53.559  1.413   14.970  1.00 26.03  ? 187 ASP A C   1 
ATOM   1507  O  O   . ASP A 1 187 ? 52.513  1.474   14.313  1.00 23.61  ? 187 ASP A O   1 
ATOM   1508  C  CB  . ASP A 1 187 ? 54.652  -0.531  13.886  1.00 26.91  ? 187 ASP A CB  1 
ATOM   1509  C  CG  . ASP A 1 187 ? 55.704  0.296   13.220  1.00 33.26  ? 187 ASP A CG  1 
ATOM   1510  O  OD1 . ASP A 1 187 ? 56.887  0.319   13.618  1.00 33.61  ? 187 ASP A OD1 1 
ATOM   1511  O  OD2 . ASP A 1 187 ? 55.304  1.053   12.324  1.00 33.56  ? 187 ASP A OD2 1 
ATOM   1512  N  N   . ASP A 1 188 ? 54.103  2.480   15.555  1.00 28.57  ? 188 ASP A N   1 
ATOM   1513  C  CA  . ASP A 1 188 ? 53.444  3.776   15.394  1.00 24.04  ? 188 ASP A CA  1 
ATOM   1514  C  C   . ASP A 1 188 ? 53.282  4.167   13.934  1.00 26.38  ? 188 ASP A C   1 
ATOM   1515  O  O   . ASP A 1 188 ? 52.245  4.752   13.561  1.00 25.80  ? 188 ASP A O   1 
ATOM   1516  C  CB  . ASP A 1 188 ? 54.204  4.886   16.123  1.00 25.68  ? 188 ASP A CB  1 
ATOM   1517  C  CG  . ASP A 1 188 ? 54.080  4.776   17.620  1.00 30.21  ? 188 ASP A CG  1 
ATOM   1518  O  OD1 . ASP A 1 188 ? 53.168  4.100   18.054  1.00 31.30  ? 188 ASP A OD1 1 
ATOM   1519  O  OD2 . ASP A 1 188 ? 54.879  5.399   18.352  1.00 35.44  ? 188 ASP A OD2 1 
ATOM   1520  N  N   . GLU A 1 189 ? 54.289  3.888   13.100  1.00 25.53  ? 189 GLU A N   1 
ATOM   1521  C  CA  . GLU A 1 189 ? 54.190  4.285   11.688  1.00 28.19  ? 189 GLU A CA  1 
ATOM   1522  C  C   . GLU A 1 189 ? 53.023  3.582   10.979  1.00 29.61  ? 189 GLU A C   1 
ATOM   1523  O  O   . GLU A 1 189 ? 52.255  4.233   10.258  1.00 26.18  ? 189 GLU A O   1 
ATOM   1524  C  CB  . GLU A 1 189 ? 55.512  4.055   10.941  1.00 32.06  ? 189 GLU A CB  1 
ATOM   1525  C  CG  . GLU A 1 189 ? 55.445  4.596   9.482   1.00 36.20  ? 189 GLU A CG  1 
ATOM   1526  C  CD  . GLU A 1 189 ? 56.647  4.231   8.596   1.00 46.12  ? 189 GLU A CD  1 
ATOM   1527  O  OE1 . GLU A 1 189 ? 56.846  4.889   7.524   1.00 52.38  ? 189 GLU A OE1 1 
ATOM   1528  O  OE2 . GLU A 1 189 ? 57.417  3.333   8.994   1.00 44.50  ? 189 GLU A OE2 1 
ATOM   1529  N  N   . LEU A 1 190 ? 52.897  2.248   11.108  1.00 23.57  ? 190 LEU A N   1 
ATOM   1530  C  CA  . LEU A 1 190 ? 51.738  1.581   10.496  1.00 26.35  ? 190 LEU A CA  1 
ATOM   1531  C  C   . LEU A 1 190 ? 50.435  2.121   11.050  1.00 23.10  ? 190 LEU A C   1 
ATOM   1532  O  O   . LEU A 1 190 ? 49.434  2.235   10.321  1.00 23.80  ? 190 LEU A O   1 
ATOM   1533  C  CB  . LEU A 1 190 ? 51.777  0.058   10.746  1.00 24.39  ? 190 LEU A CB  1 
ATOM   1534  C  CG  . LEU A 1 190 ? 52.903  -0.708  10.051  1.00 30.00  ? 190 LEU A CG  1 
ATOM   1535  C  CD1 . LEU A 1 190 ? 52.853  -2.202  10.417  1.00 27.73  ? 190 LEU A CD1 1 
ATOM   1536  C  CD2 . LEU A 1 190 ? 52.815  -0.552  8.517   1.00 30.76  ? 190 LEU A CD2 1 
ATOM   1537  N  N   . PHE A 1 191 ? 50.392  2.390   12.363  1.00 20.40  ? 191 PHE A N   1 
ATOM   1538  C  CA  . PHE A 1 191 ? 49.171  2.898   12.970  1.00 22.53  ? 191 PHE A CA  1 
ATOM   1539  C  C   . PHE A 1 191 ? 48.795  4.259   12.390  1.00 22.02  ? 191 PHE A C   1 
ATOM   1540  O  O   . PHE A 1 191 ? 47.649  4.519   12.045  1.00 24.07  ? 191 PHE A O   1 
ATOM   1541  C  CB  . PHE A 1 191 ? 49.344  3.008   14.486  1.00 21.09  ? 191 PHE A CB  1 
ATOM   1542  C  CG  . PHE A 1 191 ? 48.226  3.742   15.136  1.00 22.85  ? 191 PHE A CG  1 
ATOM   1543  C  CD1 . PHE A 1 191 ? 46.904  3.273   15.012  1.00 24.05  ? 191 PHE A CD1 1 
ATOM   1544  C  CD2 . PHE A 1 191 ? 48.476  4.883   15.902  1.00 24.20  ? 191 PHE A CD2 1 
ATOM   1545  C  CE1 . PHE A 1 191 ? 45.824  4.006   15.647  1.00 22.58  ? 191 PHE A CE1 1 
ATOM   1546  C  CE2 . PHE A 1 191 ? 47.425  5.607   16.560  1.00 24.69  ? 191 PHE A CE2 1 
ATOM   1547  C  CZ  . PHE A 1 191 ? 46.086  5.172   16.416  1.00 24.32  ? 191 PHE A CZ  1 
ATOM   1548  N  N   . ILE A 1 192 ? 49.745  5.150   12.313  1.00 26.63  ? 192 ILE A N   1 
ATOM   1549  C  CA  . ILE A 1 192 ? 49.441  6.480   11.777  1.00 25.53  ? 192 ILE A CA  1 
ATOM   1550  C  C   . ILE A 1 192 ? 49.011  6.381   10.311  1.00 25.30  ? 192 ILE A C   1 
ATOM   1551  O  O   . ILE A 1 192 ? 48.050  7.035   9.884   1.00 25.64  ? 192 ILE A O   1 
ATOM   1552  C  CB  . ILE A 1 192 ? 50.664  7.380   11.990  1.00 24.16  ? 192 ILE A CB  1 
ATOM   1553  C  CG1 . ILE A 1 192 ? 50.853  7.630   13.490  1.00 24.90  ? 192 ILE A CG1 1 
ATOM   1554  C  CG2 . ILE A 1 192 ? 50.475  8.697   11.300  1.00 26.08  ? 192 ILE A CG2 1 
ATOM   1555  C  CD1 . ILE A 1 192 ? 52.123  8.356   13.760  1.00 26.93  ? 192 ILE A CD1 1 
ATOM   1556  N  N   A LYS A 1 193 ? 49.688  5.539   9.530   0.59 23.14  ? 193 LYS A N   1 
ATOM   1557  N  N   B LYS A 1 193 ? 49.689  5.542   9.526   0.41 23.17  ? 193 LYS A N   1 
ATOM   1558  C  CA  A LYS A 1 193 ? 49.253  5.323   8.158   0.59 24.87  ? 193 LYS A CA  1 
ATOM   1559  C  CA  B LYS A 1 193 ? 49.247  5.328   8.153   0.41 24.88  ? 193 LYS A CA  1 
ATOM   1560  C  C   A LYS A 1 193 ? 47.815  4.819   8.127   0.59 24.27  ? 193 LYS A C   1 
ATOM   1561  C  C   B LYS A 1 193 ? 47.815  4.810   8.119   0.41 24.28  ? 193 LYS A C   1 
ATOM   1562  O  O   A LYS A 1 193 ? 47.016  5.238   7.272   0.59 23.59  ? 193 LYS A O   1 
ATOM   1563  O  O   B LYS A 1 193 ? 47.016  5.221   7.264   0.41 23.58  ? 193 LYS A O   1 
ATOM   1564  C  CB  A LYS A 1 193 ? 50.191  4.327   7.477   0.59 26.90  ? 193 LYS A CB  1 
ATOM   1565  C  CB  B LYS A 1 193 ? 50.192  4.354   7.450   0.41 26.90  ? 193 LYS A CB  1 
ATOM   1566  C  CG  A LYS A 1 193 ? 49.847  4.046   6.033   0.59 29.35  ? 193 LYS A CG  1 
ATOM   1567  C  CG  B LYS A 1 193 ? 51.594  4.900   7.259   0.41 28.19  ? 193 LYS A CG  1 
ATOM   1568  C  CD  A LYS A 1 193 ? 51.060  3.508   5.285   0.59 27.56  ? 193 LYS A CD  1 
ATOM   1569  C  CD  B LYS A 1 193 ? 52.186  4.428   5.950   0.41 29.57  ? 193 LYS A CD  1 
ATOM   1570  C  CE  A LYS A 1 193 ? 51.434  2.112   5.763   0.59 32.27  ? 193 LYS A CE  1 
ATOM   1571  C  CE  B LYS A 1 193 ? 53.685  4.208   6.054   0.41 35.51  ? 193 LYS A CE  1 
ATOM   1572  N  NZ  A LYS A 1 193 ? 50.370  1.105   5.562   0.59 30.45  ? 193 LYS A NZ  1 
ATOM   1573  N  NZ  B LYS A 1 193 ? 54.399  5.408   6.581   0.41 36.77  ? 193 LYS A NZ  1 
ATOM   1574  N  N   . ALA A 1 194 ? 47.474  3.889   9.030   1.00 23.43  ? 194 ALA A N   1 
ATOM   1575  C  CA  . ALA A 1 194 ? 46.114  3.339   9.036   1.00 24.22  ? 194 ALA A CA  1 
ATOM   1576  C  C   . ALA A 1 194 ? 45.084  4.406   9.447   1.00 21.80  ? 194 ALA A C   1 
ATOM   1577  O  O   . ALA A 1 194 ? 43.979  4.459   8.887   1.00 23.76  ? 194 ALA A O   1 
ATOM   1578  C  CB  . ALA A 1 194 ? 46.043  2.105   9.959   1.00 23.63  ? 194 ALA A CB  1 
ATOM   1579  N  N   . VAL A 1 195 ? 45.418  5.261   10.422  1.00 21.59  ? 195 VAL A N   1 
ATOM   1580  C  CA  . VAL A 1 195 ? 44.540  6.377   10.763  1.00 22.13  ? 195 VAL A CA  1 
ATOM   1581  C  C   . VAL A 1 195 ? 44.330  7.278   9.560   1.00 21.20  ? 195 VAL A C   1 
ATOM   1582  O  O   . VAL A 1 195 ? 43.186  7.631   9.210   1.00 21.56  ? 195 VAL A O   1 
ATOM   1583  C  CB  . VAL A 1 195 ? 45.092  7.158   11.978  1.00 21.20  ? 195 VAL A CB  1 
ATOM   1584  C  CG1 . VAL A 1 195 ? 44.330  8.494   12.183  1.00 21.24  ? 195 VAL A CG1 1 
ATOM   1585  C  CG2 . VAL A 1 195 ? 44.953  6.286   13.226  1.00 18.55  ? 195 VAL A CG2 1 
ATOM   1586  N  N   . LYS A 1 196 ? 45.405  7.651   8.909   1.00 21.91  ? 196 LYS A N   1 
ATOM   1587  C  CA  . LYS A 1 196 ? 45.267  8.540   7.738   1.00 23.12  ? 196 LYS A CA  1 
ATOM   1588  C  C   . LYS A 1 196 ? 44.452  7.880   6.628   1.00 22.76  ? 196 LYS A C   1 
ATOM   1589  O  O   . LYS A 1 196 ? 43.600  8.516   5.982   1.00 24.69  ? 196 LYS A O   1 
ATOM   1590  C  CB  . LYS A 1 196 ? 46.667  8.920   7.237   1.00 21.99  ? 196 LYS A CB  1 
ATOM   1591  C  CG  . LYS A 1 196 ? 47.501  9.691   8.308   1.00 26.43  ? 196 LYS A CG  1 
ATOM   1592  C  CD  . LYS A 1 196 ? 48.623  10.457  7.599   1.00 30.52  ? 196 LYS A CD  1 
ATOM   1593  C  CE  . LYS A 1 196 ? 49.591  9.498   6.992   1.00 34.02  ? 196 LYS A CE  1 
ATOM   1594  N  NZ  . LYS A 1 196 ? 50.687  10.326  6.351   1.00 37.37  ? 196 LYS A NZ  1 
ATOM   1595  N  N   . ASN A 1 197 ? 44.677  6.586   6.389   1.00 23.86  ? 197 ASN A N   1 
ATOM   1596  C  CA  . ASN A 1 197 ? 43.892  5.925   5.360   1.00 21.56  ? 197 ASN A CA  1 
ATOM   1597  C  C   . ASN A 1 197 ? 42.422  5.829   5.739   1.00 22.20  ? 197 ASN A C   1 
ATOM   1598  O  O   . ASN A 1 197 ? 41.539  5.910   4.869   1.00 22.26  ? 197 ASN A O   1 
ATOM   1599  C  CB  . ASN A 1 197 ? 44.489  4.528   5.088   1.00 23.58  ? 197 ASN A CB  1 
ATOM   1600  C  CG  . ASN A 1 197 ? 45.779  4.619   4.223   1.00 24.89  ? 197 ASN A CG  1 
ATOM   1601  O  OD1 . ASN A 1 197 ? 45.915  5.557   3.442   1.00 28.27  ? 197 ASN A OD1 1 
ATOM   1602  N  ND2 . ASN A 1 197 ? 46.689  3.650   4.334   1.00 27.69  ? 197 ASN A ND2 1 
ATOM   1603  N  N   . GLU A 1 198 ? 42.121  5.679   7.026   1.00 21.30  ? 198 GLU A N   1 
ATOM   1604  C  CA  . GLU A 1 198 ? 40.713  5.630   7.415   1.00 19.08  ? 198 GLU A CA  1 
ATOM   1605  C  C   . GLU A 1 198 ? 40.087  7.006   7.256   1.00 22.26  ? 198 GLU A C   1 
ATOM   1606  O  O   . GLU A 1 198 ? 38.947  7.135   6.806   1.00 21.65  ? 198 GLU A O   1 
ATOM   1607  C  CB  . GLU A 1 198 ? 40.575  5.152   8.878   1.00 21.22  ? 198 GLU A CB  1 
ATOM   1608  C  CG  . GLU A 1 198 ? 39.129  5.168   9.329   1.00 21.45  ? 198 GLU A CG  1 
ATOM   1609  C  CD  . GLU A 1 198 ? 38.914  4.416   10.612  1.00 23.76  ? 198 GLU A CD  1 
ATOM   1610  O  OE1 . GLU A 1 198 ? 39.648  3.417   10.823  1.00 23.54  ? 198 GLU A OE1 1 
ATOM   1611  O  OE2 . GLU A 1 198 ? 38.019  4.813   11.397  1.00 29.36  ? 198 GLU A OE2 1 
ATOM   1612  N  N   . MET A 1 199 ? 40.838  8.054   7.588   1.00 21.43  ? 199 MET A N   1 
ATOM   1613  C  CA  . MET A 1 199 ? 40.324  9.399   7.376   1.00 23.49  ? 199 MET A CA  1 
ATOM   1614  C  C   . MET A 1 199 ? 40.073  9.639   5.884   1.00 22.83  ? 199 MET A C   1 
ATOM   1615  O  O   . MET A 1 199 ? 38.981  10.101  5.479   1.00 24.01  ? 199 MET A O   1 
ATOM   1616  C  CB  . MET A 1 199 ? 41.328  10.437  7.892   1.00 23.23  ? 199 MET A CB  1 
ATOM   1617  C  CG  . MET A 1 199 ? 41.192  10.592  9.435   1.00 26.86  ? 199 MET A CG  1 
ATOM   1618  S  SD  . MET A 1 199 ? 42.667  11.418  10.076  1.00 25.09  ? 199 MET A SD  1 
ATOM   1619  C  CE  . MET A 1 199 ? 42.185  11.542  11.834  1.00 23.57  ? 199 MET A CE  1 
ATOM   1620  N  N   . ARG A 1 200 ? 41.034  9.231   5.046   1.00 22.72  ? 200 ARG A N   1 
ATOM   1621  C  CA  . ARG A 1 200 ? 40.865  9.321   3.569   1.00 23.63  ? 200 ARG A CA  1 
ATOM   1622  C  C   . ARG A 1 200 ? 39.629  8.579   3.098   1.00 24.26  ? 200 ARG A C   1 
ATOM   1623  O  O   . ARG A 1 200 ? 38.781  9.158   2.398   1.00 23.73  ? 200 ARG A O   1 
ATOM   1624  C  CB  . ARG A 1 200 ? 42.059  8.736   2.832   1.00 24.81  ? 200 ARG A CB  1 
ATOM   1625  C  CG  . ARG A 1 200 ? 43.328  9.558   2.898   1.00 25.85  ? 200 ARG A CG  1 
ATOM   1626  C  CD  . ARG A 1 200 ? 44.466  8.781   2.159   1.00 30.64  ? 200 ARG A CD  1 
ATOM   1627  N  NE  . ARG A 1 200 ? 44.124  8.431   0.775   1.00 27.66  ? 200 ARG A NE  1 
ATOM   1628  C  CZ  . ARG A 1 200 ? 44.611  7.396   0.103   1.00 30.82  ? 200 ARG A CZ  1 
ATOM   1629  N  NH1 . ARG A 1 200 ? 45.439  6.530   0.672   1.00 30.31  ? 200 ARG A NH1 1 
ATOM   1630  N  NH2 . ARG A 1 200 ? 44.298  7.247   -1.197  1.00 29.11  ? 200 ARG A NH2 1 
ATOM   1631  N  N   . SER A 1 201 ? 39.486  7.289   3.485   1.00 24.60  ? 201 SER A N   1 
ATOM   1632  C  CA  . SER A 1 201 ? 38.426  6.490   2.870   1.00 22.97  ? 201 SER A CA  1 
ATOM   1633  C  C   . SER A 1 201 ? 37.047  6.957   3.301   1.00 24.77  ? 201 SER A C   1 
ATOM   1634  O  O   . SER A 1 201 ? 36.144  7.017   2.475   1.00 23.32  ? 201 SER A O   1 
ATOM   1635  C  CB  . SER A 1 201 ? 38.598  4.991   3.177   1.00 21.58  ? 201 SER A CB  1 
ATOM   1636  O  OG  . SER A 1 201 ? 38.292  4.742   4.538   1.00 24.41  ? 201 SER A OG  1 
ATOM   1637  N  N   . THR A 1 202 ? 36.869  7.321   4.584   1.00 21.01  ? 202 THR A N   1 
ATOM   1638  C  CA  . THR A 1 202 ? 35.556  7.697   5.086   1.00 19.93  ? 202 THR A CA  1 
ATOM   1639  C  C   . THR A 1 202 ? 35.148  9.075   4.604   1.00 20.37  ? 202 THR A C   1 
ATOM   1640  O  O   . THR A 1 202 ? 33.970  9.296   4.290   1.00 21.04  ? 202 THR A O   1 
ATOM   1641  C  CB  . THR A 1 202 ? 35.530  7.649   6.611   1.00 23.70  ? 202 THR A CB  1 
ATOM   1642  O  OG1 . THR A 1 202 ? 36.550  8.495   7.185   1.00 21.96  ? 202 THR A OG1 1 
ATOM   1643  C  CG2 . THR A 1 202 ? 35.727  6.175   7.083   1.00 20.11  ? 202 THR A CG2 1 
ATOM   1644  N  N   . SER A 1 203 ? 36.106  9.986   4.521   1.00 21.55  ? 203 SER A N   1 
ATOM   1645  C  CA  . SER A 1 203 ? 35.813  11.284  3.922   1.00 21.05  ? 203 SER A CA  1 
ATOM   1646  C  C   . SER A 1 203 ? 35.519  11.162  2.429   1.00 20.27  ? 203 SER A C   1 
ATOM   1647  O  O   . SER A 1 203 ? 34.645  11.870  1.902   1.00 22.90  ? 203 SER A O   1 
ATOM   1648  C  CB  . SER A 1 203 ? 36.990  12.217  4.134   1.00 22.54  ? 203 SER A CB  1 
ATOM   1649  O  OG  . SER A 1 203 ? 36.715  13.468  3.527   1.00 22.66  ? 203 SER A OG  1 
ATOM   1650  N  N   . ARG A 1 204 ? 36.277  10.332  1.720   1.00 20.27  ? 204 ARG A N   1 
ATOM   1651  C  CA  . ARG A 1 204 ? 36.093  10.203  0.277   1.00 20.76  ? 204 ARG A CA  1 
ATOM   1652  C  C   . ARG A 1 204 ? 34.763  9.535   -0.024  1.00 23.47  ? 204 ARG A C   1 
ATOM   1653  O  O   . ARG A 1 204 ? 34.098  9.925   -1.001  1.00 22.77  ? 204 ARG A O   1 
ATOM   1654  C  CB  . ARG A 1 204 ? 37.239  9.456   -0.372  1.00 22.59  ? 204 ARG A CB  1 
ATOM   1655  C  CG  . ARG A 1 204 ? 37.242  9.573   -1.895  1.00 24.60  ? 204 ARG A CG  1 
ATOM   1656  C  CD  . ARG A 1 204 ? 37.275  11.017  -2.274  1.00 27.97  ? 204 ARG A CD  1 
ATOM   1657  N  NE  . ARG A 1 204 ? 38.634  11.380  -2.633  1.00 33.92  ? 204 ARG A NE  1 
ATOM   1658  C  CZ  . ARG A 1 204 ? 39.023  12.639  -2.814  1.00 36.90  ? 204 ARG A CZ  1 
ATOM   1659  N  NH1 . ARG A 1 204 ? 38.155  13.650  -2.742  1.00 32.95  ? 204 ARG A NH1 1 
ATOM   1660  N  NH2 . ARG A 1 204 ? 40.307  12.891  -3.054  1.00 42.54  ? 204 ARG A NH2 1 
ATOM   1661  N  N   . TRP A 1 205 ? 34.377  8.487   0.770   1.00 20.16  ? 205 TRP A N   1 
ATOM   1662  C  CA  . TRP A 1 205 ? 33.021  7.933   0.604   1.00 19.60  ? 205 TRP A CA  1 
ATOM   1663  C  C   . TRP A 1 205 ? 31.966  9.037   0.732   1.00 23.31  ? 205 TRP A C   1 
ATOM   1664  O  O   . TRP A 1 205 ? 31.037  9.133   -0.096  1.00 21.11  ? 205 TRP A O   1 
ATOM   1665  C  CB  . TRP A 1 205 ? 32.729  6.767   1.579   1.00 20.51  ? 205 TRP A CB  1 
ATOM   1666  C  CG  . TRP A 1 205 ? 31.311  6.273   1.371   1.00 23.27  ? 205 TRP A CG  1 
ATOM   1667  C  CD1 . TRP A 1 205 ? 30.293  6.353   2.230   1.00 21.38  ? 205 TRP A CD1 1 
ATOM   1668  C  CD2 . TRP A 1 205 ? 30.768  5.763   0.138   1.00 22.26  ? 205 TRP A CD2 1 
ATOM   1669  N  NE1 . TRP A 1 205 ? 29.116  5.931   1.638   1.00 22.02  ? 205 TRP A NE1 1 
ATOM   1670  C  CE2 . TRP A 1 205 ? 29.402  5.501   0.369   1.00 22.94  ? 205 TRP A CE2 1 
ATOM   1671  C  CE3 . TRP A 1 205 ? 31.319  5.456   -1.117  1.00 22.30  ? 205 TRP A CE3 1 
ATOM   1672  C  CZ2 . TRP A 1 205 ? 28.558  4.978   -0.617  1.00 24.39  ? 205 TRP A CZ2 1 
ATOM   1673  C  CZ3 . TRP A 1 205 ? 30.500  4.947   -2.092  1.00 22.44  ? 205 TRP A CZ3 1 
ATOM   1674  C  CH2 . TRP A 1 205 ? 29.116  4.694   -1.840  1.00 21.20  ? 205 TRP A CH2 1 
ATOM   1675  N  N   . ALA A 1 206 ? 32.117  9.918   1.714   1.00 20.69  ? 206 ALA A N   1 
ATOM   1676  C  CA  . ALA A 1 206 ? 31.166  11.032  1.816   1.00 22.44  ? 206 ALA A CA  1 
ATOM   1677  C  C   . ALA A 1 206 ? 31.202  11.923  0.568   1.00 22.44  ? 206 ALA A C   1 
ATOM   1678  O  O   . ALA A 1 206 ? 30.153  12.364  0.076   1.00 22.67  ? 206 ALA A O   1 
ATOM   1679  C  CB  . ALA A 1 206 ? 31.457  11.849  3.071   1.00 19.73  ? 206 ALA A CB  1 
ATOM   1680  N  N   . ASP A 1 207 ? 32.384  12.240  0.081   1.00 21.84  ? 207 ASP A N   1 
ATOM   1681  C  CA  . ASP A 1 207 ? 32.508  13.054  -1.151  1.00 23.90  ? 207 ASP A CA  1 
ATOM   1682  C  C   . ASP A 1 207 ? 31.758  12.405  -2.317  1.00 22.48  ? 207 ASP A C   1 
ATOM   1683  O  O   . ASP A 1 207 ? 31.056  13.089  -3.070  1.00 25.03  ? 207 ASP A O   1 
ATOM   1684  C  CB  . ASP A 1 207 ? 33.971  13.205  -1.577  1.00 25.95  ? 207 ASP A CB  1 
ATOM   1685  C  CG  . ASP A 1 207 ? 34.782  14.077  -0.693  1.00 28.11  ? 207 ASP A CG  1 
ATOM   1686  O  OD1 . ASP A 1 207 ? 34.244  14.921  0.100   1.00 28.33  ? 207 ASP A OD1 1 
ATOM   1687  O  OD2 . ASP A 1 207 ? 36.032  13.911  -0.816  1.00 27.24  ? 207 ASP A OD2 1 
ATOM   1688  N  N   . ILE A 1 208 ? 31.929  11.088  -2.480  1.00 22.26  ? 208 ILE A N   1 
ATOM   1689  C  CA  . ILE A 1 208 ? 31.245  10.352  -3.529  1.00 22.05  ? 208 ILE A CA  1 
ATOM   1690  C  C   . ILE A 1 208 ? 29.736  10.487  -3.364  1.00 22.48  ? 208 ILE A C   1 
ATOM   1691  O  O   . ILE A 1 208 ? 29.027  10.783  -4.338  1.00 22.77  ? 208 ILE A O   1 
ATOM   1692  C  CB  . ILE A 1 208 ? 31.680  8.868   -3.515  1.00 24.28  ? 208 ILE A CB  1 
ATOM   1693  C  CG1 . ILE A 1 208 ? 33.153  8.724   -3.950  1.00 24.45  ? 208 ILE A CG1 1 
ATOM   1694  C  CG2 . ILE A 1 208 ? 30.746  8.024   -4.318  1.00 24.01  ? 208 ILE A CG2 1 
ATOM   1695  C  CD1 . ILE A 1 208 ? 33.742  7.317   -3.566  1.00 23.90  ? 208 ILE A CD1 1 
ATOM   1696  N  N   . CYS A 1 209 ? 29.226  10.276  -2.131  1.00 23.70  ? 209 CYS A N   1 
ATOM   1697  C  CA  . CYS A 1 209 ? 27.789  10.407  -1.867  1.00 21.03  ? 209 CYS A CA  1 
ATOM   1698  C  C   . CYS A 1 209 ? 27.294  11.795  -2.241  1.00 22.66  ? 209 CYS A C   1 
ATOM   1699  O  O   . CYS A 1 209 ? 26.173  11.934  -2.749  1.00 21.94  ? 209 CYS A O   1 
ATOM   1700  C  CB  . CYS A 1 209 ? 27.466  10.129  -0.392  1.00 20.38  ? 209 CYS A CB  1 
ATOM   1701  S  SG  . CYS A 1 209 ? 27.695  8.334   -0.028  1.00 23.68  ? 209 CYS A SG  1 
ATOM   1702  N  N   . ALA A 1 210 ? 28.106  12.813  -1.974  1.00 24.09  ? 210 ALA A N   1 
ATOM   1703  C  CA  . ALA A 1 210 ? 27.693  14.192  -2.205  1.00 24.78  ? 210 ALA A CA  1 
ATOM   1704  C  C   . ALA A 1 210 ? 27.567  14.477  -3.699  1.00 24.57  ? 210 ALA A C   1 
ATOM   1705  O  O   . ALA A 1 210 ? 26.851  15.420  -4.081  1.00 26.05  ? 210 ALA A O   1 
ATOM   1706  C  CB  . ALA A 1 210 ? 28.680  15.166  -1.503  1.00 25.14  ? 210 ALA A CB  1 
ATOM   1707  N  N   . LEU A 1 211 ? 28.223  13.674  -4.574  1.00 25.11  ? 211 LEU A N   1 
ATOM   1708  C  CA  . LEU A 1 211 ? 28.037  13.812  -6.022  1.00 21.68  ? 211 LEU A CA  1 
ATOM   1709  C  C   . LEU A 1 211 ? 26.633  13.409  -6.426  1.00 24.90  ? 211 LEU A C   1 
ATOM   1710  O  O   . LEU A 1 211 ? 26.180  13.766  -7.520  1.00 25.64  ? 211 LEU A O   1 
ATOM   1711  C  CB  . LEU A 1 211 ? 29.072  12.982  -6.773  1.00 24.75  ? 211 LEU A CB  1 
ATOM   1712  C  CG  . LEU A 1 211 ? 30.526  13.455  -6.499  1.00 26.68  ? 211 LEU A CG  1 
ATOM   1713  C  CD1 . LEU A 1 211 ? 31.574  12.535  -7.212  1.00 28.98  ? 211 LEU A CD1 1 
ATOM   1714  C  CD2 . LEU A 1 211 ? 30.719  14.919  -6.982  1.00 30.52  ? 211 LEU A CD2 1 
ATOM   1715  N  N   . ASN A 1 212 ? 25.933  12.674  -5.550  1.00 23.66  ? 212 ASN A N   1 
ATOM   1716  C  CA  . ASN A 1 212 ? 24.594  12.194  -5.895  1.00 24.03  ? 212 ASN A CA  1 
ATOM   1717  C  C   . ASN A 1 212 ? 23.542  13.268  -5.779  1.00 23.31  ? 212 ASN A C   1 
ATOM   1718  O  O   . ASN A 1 212 ? 22.364  13.002  -6.029  1.00 25.78  ? 212 ASN A O   1 
ATOM   1719  C  CB  . ASN A 1 212 ? 24.217  10.966  -5.069  1.00 20.79  ? 212 ASN A CB  1 
ATOM   1720  C  CG  . ASN A 1 212 ? 23.771  9.843   -5.959  1.00 22.68  ? 212 ASN A CG  1 
ATOM   1721  O  OD1 . ASN A 1 212 ? 24.094  9.853   -7.159  1.00 26.60  ? 212 ASN A OD1 1 
ATOM   1722  N  ND2 . ASN A 1 212 ? 22.979  8.937   -5.433  1.00 22.05  ? 212 ASN A ND2 1 
ATOM   1723  N  N   . LYS A 1 213 ? 23.937  14.490  -5.408  1.00 23.79  ? 213 LYS A N   1 
ATOM   1724  C  CA  . LYS A 1 213 ? 22.969  15.544  -5.242  1.00 25.25  ? 213 LYS A CA  1 
ATOM   1725  C  C   . LYS A 1 213 ? 22.450  16.062  -6.572  1.00 27.86  ? 213 LYS A C   1 
ATOM   1726  O  O   . LYS A 1 213 ? 21.396  16.720  -6.609  1.00 25.80  ? 213 LYS A O   1 
ATOM   1727  C  CB  . LYS A 1 213 ? 23.597  16.681  -4.422  1.00 24.29  ? 213 LYS A CB  1 
ATOM   1728  C  CG  . LYS A 1 213 ? 24.006  16.317  -3.018  1.00 25.14  ? 213 LYS A CG  1 
ATOM   1729  C  CD  . LYS A 1 213 ? 24.605  17.589  -2.375  1.00 23.70  ? 213 LYS A CD  1 
ATOM   1730  C  CE  . LYS A 1 213 ? 25.283  17.276  -1.034  1.00 29.25  ? 213 LYS A CE  1 
ATOM   1731  N  NZ  . LYS A 1 213 ? 25.813  18.468  -0.312  1.00 28.34  ? 213 LYS A NZ  1 
ATOM   1732  N  N   . VAL A 1 214 ? 23.163  15.785  -7.668  1.00 28.17  ? 214 VAL A N   1 
ATOM   1733  C  CA  . VAL A 1 214 ? 22.774  16.350  -8.948  1.00 30.13  ? 214 VAL A CA  1 
ATOM   1734  C  C   . VAL A 1 214 ? 21.666  15.514  -9.585  1.00 28.55  ? 214 VAL A C   1 
ATOM   1735  O  O   . VAL A 1 214 ? 21.433  14.337  -9.229  1.00 27.28  ? 214 VAL A O   1 
ATOM   1736  C  CB  . VAL A 1 214 ? 24.000  16.492  -9.861  1.00 34.62  ? 214 VAL A CB  1 
ATOM   1737  C  CG1 . VAL A 1 214 ? 25.170  17.063  -9.049  1.00 36.33  ? 214 VAL A CG1 1 
ATOM   1738  C  CG2 . VAL A 1 214 ? 24.408  15.112  -10.359 1.00 28.79  ? 214 VAL A CG2 1 
ATOM   1739  N  N   . LYS A 1 215 ? 20.881  16.188  -10.453 1.00 28.76  ? 215 LYS A N   1 
ATOM   1740  C  CA  . LYS A 1 215 ? 19.945  15.552  -11.372 1.00 30.28  ? 215 LYS A CA  1 
ATOM   1741  C  C   . LYS A 1 215 ? 20.590  15.412  -12.745 1.00 32.12  ? 215 LYS A C   1 
ATOM   1742  O  O   . LYS A 1 215 ? 21.025  16.419  -13.331 1.00 28.56  ? 215 LYS A O   1 
ATOM   1743  C  CB  . LYS A 1 215 ? 18.647  16.347  -11.490 1.00 29.62  ? 215 LYS A CB  1 
ATOM   1744  C  CG  . LYS A 1 215 ? 17.794  16.375  -10.239 1.00 31.54  ? 215 LYS A CG  1 
ATOM   1745  C  CD  . LYS A 1 215 ? 16.446  17.119  -10.472 1.00 31.22  ? 215 LYS A CD  1 
ATOM   1746  C  CE  . LYS A 1 215 ? 15.764  17.475  -9.159  1.00 39.63  ? 215 LYS A CE  1 
ATOM   1747  N  NZ  . LYS A 1 215 ? 14.326  17.855  -9.350  1.00 46.11  ? 215 LYS A NZ  1 
ATOM   1748  N  N   . PRO A 1 216 ? 20.668  14.200  -13.326 1.00 29.02  ? 216 PRO A N   1 
ATOM   1749  C  CA  . PRO A 1 216 ? 20.228  12.905  -12.793 1.00 31.26  ? 216 PRO A CA  1 
ATOM   1750  C  C   . PRO A 1 216 ? 21.208  12.387  -11.780 1.00 25.48  ? 216 PRO A C   1 
ATOM   1751  O  O   . PRO A 1 216 ? 22.397  12.770  -11.837 1.00 26.29  ? 216 PRO A O   1 
ATOM   1752  C  CB  . PRO A 1 216 ? 20.189  12.025  -14.045 1.00 30.39  ? 216 PRO A CB  1 
ATOM   1753  C  CG  . PRO A 1 216 ? 21.372  12.536  -14.848 1.00 25.34  ? 216 PRO A CG  1 
ATOM   1754  C  CD  . PRO A 1 216 ? 21.411  14.040  -14.593 1.00 28.68  ? 216 PRO A CD  1 
ATOM   1755  N  N   . ALA A 1 217 ? 20.768  11.576  -10.839 1.00 27.69  ? 217 ALA A N   1 
ATOM   1756  C  CA  . ALA A 1 217 ? 21.718  10.977  -9.900  1.00 27.93  ? 217 ALA A CA  1 
ATOM   1757  C  C   . ALA A 1 217 ? 22.664  10.013  -10.617 1.00 26.51  ? 217 ALA A C   1 
ATOM   1758  O  O   . ALA A 1 217 ? 22.216  9.088   -11.279 1.00 26.32  ? 217 ALA A O   1 
ATOM   1759  C  CB  . ALA A 1 217 ? 20.988  10.264  -8.749  1.00 24.69  ? 217 ALA A CB  1 
ATOM   1760  N  N   . PRO A 1 218 ? 23.975  10.184  -10.489 1.00 23.42  ? 218 PRO A N   1 
ATOM   1761  C  CA  . PRO A 1 218 ? 24.901  9.242   -11.135 1.00 24.35  ? 218 PRO A CA  1 
ATOM   1762  C  C   . PRO A 1 218 ? 24.900  7.848   -10.535 1.00 25.11  ? 218 PRO A C   1 
ATOM   1763  O  O   . PRO A 1 218 ? 25.305  6.906   -11.228 1.00 26.77  ? 218 PRO A O   1 
ATOM   1764  C  CB  . PRO A 1 218 ? 26.265  9.889   -10.936 1.00 26.44  ? 218 PRO A CB  1 
ATOM   1765  C  CG  . PRO A 1 218 ? 26.054  10.818  -9.702  1.00 23.90  ? 218 PRO A CG  1 
ATOM   1766  C  CD  . PRO A 1 218 ? 24.659  11.344  -9.881  1.00 23.70  ? 218 PRO A CD  1 
ATOM   1767  N  N   . LEU A 1 219 ? 24.498  7.703   -9.285  1.00 22.21  ? 219 LEU A N   1 
ATOM   1768  C  CA  . LEU A 1 219 ? 24.420  6.410   -8.602  1.00 23.87  ? 219 LEU A CA  1 
ATOM   1769  C  C   . LEU A 1 219 ? 23.011  6.198   -8.068  1.00 26.19  ? 219 LEU A C   1 
ATOM   1770  O  O   . LEU A 1 219 ? 22.338  7.144   -7.651  1.00 26.89  ? 219 LEU A O   1 
ATOM   1771  C  CB  . LEU A 1 219 ? 25.419  6.344   -7.427  1.00 29.05  ? 219 LEU A CB  1 
ATOM   1772  C  CG  . LEU A 1 219 ? 26.901  6.404   -7.835  1.00 30.45  ? 219 LEU A CG  1 
ATOM   1773  C  CD1 . LEU A 1 219 ? 27.807  6.508   -6.587  1.00 30.32  ? 219 LEU A CD1 1 
ATOM   1774  C  CD2 . LEU A 1 219 ? 27.303  5.230   -8.679  1.00 28.23  ? 219 LEU A CD2 1 
ATOM   1775  N  N   . ASP A 1 220 ? 22.602  4.926   -8.029  1.00 24.50  ? 220 ASP A N   1 
ATOM   1776  C  CA  . ASP A 1 220 ? 21.415  4.450   -7.358  1.00 26.75  ? 220 ASP A CA  1 
ATOM   1777  C  C   . ASP A 1 220 ? 21.837  3.671   -6.123  1.00 25.77  ? 220 ASP A C   1 
ATOM   1778  O  O   . ASP A 1 220 ? 22.962  3.141   -6.035  1.00 26.45  ? 220 ASP A O   1 
ATOM   1779  C  CB  . ASP A 1 220 ? 20.611  3.576   -8.327  1.00 28.60  ? 220 ASP A CB  1 
ATOM   1780  C  CG  . ASP A 1 220 ? 21.329  2.298   -8.607  1.00 27.85  ? 220 ASP A CG  1 
ATOM   1781  O  OD1 . ASP A 1 220 ? 22.213  2.349   -9.468  1.00 38.99  ? 220 ASP A OD1 1 
ATOM   1782  O  OD2 . ASP A 1 220 ? 21.130  1.285   -7.906  1.00 39.39  ? 220 ASP A OD2 1 
ATOM   1783  N  N   . GLU A 1 221 ? 20.953  3.640   -5.136  1.00 26.06  ? 221 GLU A N   1 
ATOM   1784  C  CA  . GLU A 1 221 ? 21.373  3.098   -3.866  1.00 28.15  ? 221 GLU A CA  1 
ATOM   1785  C  C   . GLU A 1 221 ? 21.643  1.600   -3.950  1.00 28.16  ? 221 GLU A C   1 
ATOM   1786  O  O   . GLU A 1 221 ? 22.574  1.106   -3.299  1.00 28.41  ? 221 GLU A O   1 
ATOM   1787  C  CB  . GLU A 1 221 ? 20.350  3.499   -2.801  1.00 26.65  ? 221 GLU A CB  1 
ATOM   1788  C  CG  . GLU A 1 221 ? 20.801  3.078   -1.431  1.00 28.86  ? 221 GLU A CG  1 
ATOM   1789  C  CD  . GLU A 1 221 ? 19.888  3.533   -0.320  1.00 30.97  ? 221 GLU A CD  1 
ATOM   1790  O  OE1 . GLU A 1 221 ? 20.480  3.864   0.745   1.00 31.79  ? 221 GLU A OE1 1 
ATOM   1791  O  OE2 . GLU A 1 221 ? 18.651  3.726   -0.567  1.00 33.14  ? 221 GLU A OE2 1 
ATOM   1792  N  N   . LYS A 1 222 ? 20.910  0.870   -4.798  1.00 27.19  ? 222 LYS A N   1 
ATOM   1793  C  CA  . LYS A 1 222 ? 21.234  -0.554  -4.968  1.00 29.95  ? 222 LYS A CA  1 
ATOM   1794  C  C   . LYS A 1 222 ? 22.666  -0.740  -5.438  1.00 30.31  ? 222 LYS A C   1 
ATOM   1795  O  O   . LYS A 1 222 ? 23.387  -1.595  -4.910  1.00 31.70  ? 222 LYS A O   1 
ATOM   1796  C  CB  . LYS A 1 222 ? 20.267  -1.217  -5.945  1.00 35.87  ? 222 LYS A CB  1 
ATOM   1797  C  CG  . LYS A 1 222 ? 20.171  -2.718  -5.726  1.00 43.59  ? 222 LYS A CG  1 
ATOM   1798  C  CD  . LYS A 1 222 ? 19.578  -3.440  -6.964  1.00 49.91  ? 222 LYS A CD  1 
ATOM   1799  C  CE  . LYS A 1 222 ? 19.455  -4.957  -6.742  1.00 53.89  ? 222 LYS A CE  1 
ATOM   1800  N  NZ  . LYS A 1 222 ? 20.608  -5.731  -7.317  1.00 51.35  ? 222 LYS A NZ  1 
ATOM   1801  N  N   . THR A 1 223 ? 23.110  0.076   -6.410  1.00 28.15  ? 223 THR A N   1 
ATOM   1802  C  CA  . THR A 1 223 ? 24.511  0.039   -6.826  1.00 32.44  ? 223 THR A CA  1 
ATOM   1803  C  C   . THR A 1 223 ? 25.426  0.459   -5.687  1.00 28.08  ? 223 THR A C   1 
ATOM   1804  O  O   . THR A 1 223 ? 26.468  -0.170  -5.454  1.00 28.89  ? 223 THR A O   1 
ATOM   1805  C  CB  . THR A 1 223 ? 24.733  0.935   -8.060  1.00 32.41  ? 223 THR A CB  1 
ATOM   1806  O  OG1 . THR A 1 223 ? 23.930  0.442   -9.138  1.00 32.28  ? 223 THR A OG1 1 
ATOM   1807  C  CG2 . THR A 1 223 ? 26.201  0.897   -8.520  1.00 29.38  ? 223 THR A CG2 1 
ATOM   1808  N  N   . MET A 1 224 ? 25.059  1.533   -4.960  1.00 24.86  ? 224 MET A N   1 
ATOM   1809  C  CA  . MET A 1 224 ? 25.888  1.932   -3.833  1.00 27.62  ? 224 MET A CA  1 
ATOM   1810  C  C   . MET A 1 224 ? 26.041  0.867   -2.729  1.00 26.39  ? 224 MET A C   1 
ATOM   1811  O  O   . MET A 1 224 ? 27.053  0.910   -2.000  1.00 27.18  ? 224 MET A O   1 
ATOM   1812  C  CB  . MET A 1 224 ? 25.401  3.241   -3.192  1.00 26.93  ? 224 MET A CB  1 
ATOM   1813  C  CG  . MET A 1 224 ? 25.232  4.344   -4.188  1.00 23.99  ? 224 MET A CG  1 
ATOM   1814  S  SD  . MET A 1 224 ? 24.372  5.797   -3.557  1.00 36.55  ? 224 MET A SD  1 
ATOM   1815  C  CE  . MET A 1 224 ? 25.772  6.427   -2.679  1.00 34.74  ? 224 MET A CE  1 
ATOM   1816  N  N   . TYR A 1 225 ? 25.119  -0.088  -2.587  1.00 26.95  ? 225 TYR A N   1 
ATOM   1817  C  CA  . TYR A 1 225 ? 25.340  -1.102  -1.549  1.00 30.51  ? 225 TYR A CA  1 
ATOM   1818  C  C   . TYR A 1 225 ? 26.617  -1.899  -1.816  1.00 27.64  ? 225 TYR A C   1 
ATOM   1819  O  O   . TYR A 1 225 ? 27.221  -2.395  -0.862  1.00 25.51  ? 225 TYR A O   1 
ATOM   1820  C  CB  . TYR A 1 225 ? 24.135  -2.071  -1.386  1.00 30.05  ? 225 TYR A CB  1 
ATOM   1821  C  CG  . TYR A 1 225 ? 22.877  -1.446  -0.771  1.00 30.06  ? 225 TYR A CG  1 
ATOM   1822  C  CD1 . TYR A 1 225 ? 22.972  -0.462  0.228   1.00 34.23  ? 225 TYR A CD1 1 
ATOM   1823  C  CD2 . TYR A 1 225 ? 21.593  -1.786  -1.240  1.00 33.17  ? 225 TYR A CD2 1 
ATOM   1824  C  CE1 . TYR A 1 225 ? 21.810  0.129   0.775   1.00 31.70  ? 225 TYR A CE1 1 
ATOM   1825  C  CE2 . TYR A 1 225 ? 20.459  -1.206  -0.734  1.00 35.74  ? 225 TYR A CE2 1 
ATOM   1826  C  CZ  . TYR A 1 225 ? 20.573  -0.223  0.282   1.00 35.30  ? 225 TYR A CZ  1 
ATOM   1827  O  OH  . TYR A 1 225 ? 19.448  0.353   0.826   1.00 38.37  ? 225 TYR A OH  1 
ATOM   1828  N  N   . SER A 1 226 ? 27.050  -2.045  -3.091  1.00 24.23  ? 226 SER A N   1 
ATOM   1829  C  CA  . SER A 1 226 ? 28.311  -2.734  -3.372  1.00 22.52  ? 226 SER A CA  1 
ATOM   1830  C  C   . SER A 1 226 ? 29.538  -1.852  -3.218  1.00 25.03  ? 226 SER A C   1 
ATOM   1831  O  O   . SER A 1 226 ? 30.669  -2.324  -3.359  1.00 26.24  ? 226 SER A O   1 
ATOM   1832  C  CB  . SER A 1 226 ? 28.282  -3.271  -4.797  1.00 28.43  ? 226 SER A CB  1 
ATOM   1833  O  OG  . SER A 1 226 ? 27.524  -4.460  -4.804  1.00 33.43  ? 226 SER A OG  1 
ATOM   1834  N  N   . LEU A 1 227 ? 29.346  -0.562  -2.961  1.00 24.30  ? 227 LEU A N   1 
ATOM   1835  C  CA  . LEU A 1 227 ? 30.416  0.404   -2.888  1.00 22.75  ? 227 LEU A CA  1 
ATOM   1836  C  C   . LEU A 1 227 ? 30.622  0.921   -1.474  1.00 21.48  ? 227 LEU A C   1 
ATOM   1837  O  O   . LEU A 1 227 ? 31.775  0.974   -0.998  1.00 25.89  ? 227 LEU A O   1 
ATOM   1838  C  CB  . LEU A 1 227 ? 30.093  1.590   -3.834  1.00 24.37  ? 227 LEU A CB  1 
ATOM   1839  C  CG  . LEU A 1 227 ? 29.695  1.183   -5.273  1.00 25.40  ? 227 LEU A CG  1 
ATOM   1840  C  CD1 . LEU A 1 227 ? 29.388  2.442   -6.091  1.00 25.65  ? 227 LEU A CD1 1 
ATOM   1841  C  CD2 . LEU A 1 227 ? 30.891  0.507   -5.853  1.00 27.21  ? 227 LEU A CD2 1 
ATOM   1842  N  N   . TYR A 1 228 ? 29.545  1.255   -0.772  1.00 24.19  ? 228 TYR A N   1 
ATOM   1843  C  CA  . TYR A 1 228 ? 29.680  1.709   0.605   1.00 24.16  ? 228 TYR A CA  1 
ATOM   1844  C  C   . TYR A 1 228 ? 30.179  0.559   1.462   1.00 23.43  ? 228 TYR A C   1 
ATOM   1845  O  O   . TYR A 1 228 ? 30.708  0.799   2.540   1.00 23.18  ? 228 TYR A O   1 
ATOM   1846  C  CB  . TYR A 1 228 ? 28.321  2.211   1.186   1.00 24.71  ? 228 TYR A CB  1 
ATOM   1847  C  CG  . TYR A 1 228 ? 27.584  1.145   1.970   1.00 25.06  ? 228 TYR A CG  1 
ATOM   1848  C  CD1 . TYR A 1 228 ? 27.199  -0.035  1.355   1.00 25.03  ? 228 TYR A CD1 1 
ATOM   1849  C  CD2 . TYR A 1 228 ? 27.277  1.312   3.343   1.00 23.72  ? 228 TYR A CD2 1 
ATOM   1850  C  CE1 . TYR A 1 228 ? 26.562  -1.034  2.073   1.00 27.46  ? 228 TYR A CE1 1 
ATOM   1851  C  CE2 . TYR A 1 228 ? 26.613  0.312   4.093   1.00 26.03  ? 228 TYR A CE2 1 
ATOM   1852  C  CZ  . TYR A 1 228 ? 26.268  -0.867  3.424   1.00 30.58  ? 228 TYR A CZ  1 
ATOM   1853  O  OH  . TYR A 1 228 ? 25.610  -1.905  4.055   1.00 31.74  ? 228 TYR A OH  1 
ATOM   1854  N  N   . VAL A 1 229 ? 30.055  -0.692  0.986   1.00 22.61  ? 229 VAL A N   1 
ATOM   1855  C  CA  . VAL A 1 229 ? 30.387  -1.802  1.865   1.00 23.11  ? 229 VAL A CA  1 
ATOM   1856  C  C   . VAL A 1 229 ? 31.884  -1.868  2.104   1.00 21.49  ? 229 VAL A C   1 
ATOM   1857  O  O   . VAL A 1 229 ? 32.311  -2.407  3.115   1.00 22.87  ? 229 VAL A O   1 
ATOM   1858  C  CB  . VAL A 1 229 ? 29.868  -3.113  1.276   1.00 22.87  ? 229 VAL A CB  1 
ATOM   1859  C  CG1 . VAL A 1 229 ? 30.559  -3.434  0.000   1.00 23.28  ? 229 VAL A CG1 1 
ATOM   1860  C  CG2 . VAL A 1 229 ? 30.079  -4.237  2.290   1.00 23.65  ? 229 VAL A CG2 1 
ATOM   1861  N  N   . LEU A 1 230 ? 32.707  -1.362  1.191   1.00 19.94  ? 230 LEU A N   1 
ATOM   1862  C  CA  . LEU A 1 230 ? 34.164  -1.515  1.354   1.00 23.19  ? 230 LEU A CA  1 
ATOM   1863  C  C   . LEU A 1 230 ? 34.665  -0.884  2.667   1.00 23.92  ? 230 LEU A C   1 
ATOM   1864  O  O   . LEU A 1 230 ? 35.486  -1.484  3.377   1.00 23.25  ? 230 LEU A O   1 
ATOM   1865  C  CB  . LEU A 1 230 ? 34.908  -0.954  0.132   1.00 22.58  ? 230 LEU A CB  1 
ATOM   1866  C  CG  . LEU A 1 230 ? 34.497  -1.771  -1.141  1.00 23.46  ? 230 LEU A CG  1 
ATOM   1867  C  CD1 . LEU A 1 230 ? 35.072  -1.303  -2.438  1.00 31.29  ? 230 LEU A CD1 1 
ATOM   1868  C  CD2 . LEU A 1 230 ? 34.764  -3.316  -0.960  1.00 24.05  ? 230 LEU A CD2 1 
ATOM   1869  N  N   . CYS A 1 231 ? 34.198  0.321   3.012   1.00 21.70  ? 231 CYS A N   1 
ATOM   1870  C  CA  . CYS A 1 231 ? 34.596  0.922   4.280   1.00 21.38  ? 231 CYS A CA  1 
ATOM   1871  C  C   . CYS A 1 231 ? 34.105  0.114   5.508   1.00 21.39  ? 231 CYS A C   1 
ATOM   1872  O  O   . CYS A 1 231 ? 34.624  0.295   6.613   1.00 22.47  ? 231 CYS A O   1 
ATOM   1873  C  CB  . CYS A 1 231 ? 34.027  2.342   4.409   1.00 21.00  ? 231 CYS A CB  1 
ATOM   1874  S  SG  . CYS A 1 231 ? 34.876  3.573   3.394   1.00 24.95  ? 231 CYS A SG  1 
ATOM   1875  N  N   . THR A 1 232 ? 33.050  -0.688  5.372   1.00 21.52  ? 232 THR A N   1 
ATOM   1876  C  CA  . THR A 1 232 ? 32.618  -1.554  6.474   1.00 21.14  ? 232 THR A CA  1 
ATOM   1877  C  C   . THR A 1 232 ? 33.480  -2.803  6.592   1.00 20.43  ? 232 THR A C   1 
ATOM   1878  O  O   . THR A 1 232 ? 33.356  -3.511  7.618   1.00 21.39  ? 232 THR A O   1 
ATOM   1879  C  CB  . THR A 1 232 ? 31.143  -1.969  6.326   1.00 21.83  ? 232 THR A CB  1 
ATOM   1880  O  OG1 . THR A 1 232 ? 31.034  -3.034  5.351   1.00 22.50  ? 232 THR A OG1 1 
ATOM   1881  C  CG2 . THR A 1 232 ? 30.262  -0.771  5.877   1.00 21.80  ? 232 THR A CG2 1 
ATOM   1882  N  N   . LEU A 1 233 ? 34.310  -3.087  5.583   1.00 21.68  ? 233 LEU A N   1 
ATOM   1883  C  CA  . LEU A 1 233 ? 35.261  -4.200  5.625   1.00 22.10  ? 233 LEU A CA  1 
ATOM   1884  C  C   . LEU A 1 233 ? 36.598  -3.773  6.237   1.00 22.74  ? 233 LEU A C   1 
ATOM   1885  O  O   . LEU A 1 233 ? 37.012  -4.312  7.268   1.00 23.44  ? 233 LEU A O   1 
ATOM   1886  C  CB  . LEU A 1 233 ? 35.470  -4.814  4.224   1.00 21.41  ? 233 LEU A CB  1 
ATOM   1887  C  CG  . LEU A 1 233 ? 34.131  -5.148  3.549   1.00 20.99  ? 233 LEU A CG  1 
ATOM   1888  C  CD1 . LEU A 1 233 ? 34.440  -5.819  2.202   1.00 22.19  ? 233 LEU A CD1 1 
ATOM   1889  C  CD2 . LEU A 1 233 ? 33.303  -6.163  4.387   1.00 21.61  ? 233 LEU A CD2 1 
ATOM   1890  N  N   . SER A 1 234 ? 37.255  -2.754  5.668   1.00 22.27  ? 234 SER A N   1 
ATOM   1891  C  CA  . SER A 1 234 ? 38.508  -2.297  6.257   1.00 24.18  ? 234 SER A CA  1 
ATOM   1892  C  C   . SER A 1 234 ? 38.752  -0.848  5.851   1.00 20.37  ? 234 SER A C   1 
ATOM   1893  O  O   . SER A 1 234 ? 39.505  -0.539  4.908   1.00 22.19  ? 234 SER A O   1 
ATOM   1894  C  CB  . SER A 1 234 ? 39.672  -3.208  5.886   1.00 23.13  ? 234 SER A CB  1 
ATOM   1895  O  OG  . SER A 1 234 ? 40.844  -2.911  6.631   1.00 26.16  ? 234 SER A OG  1 
ATOM   1896  N  N   . LYS A 1 235 ? 38.060  0.038   6.561   1.00 21.28  ? 235 LYS A N   1 
ATOM   1897  C  CA  . LYS A 1 235 ? 38.191  1.451   6.186   1.00 20.72  ? 235 LYS A CA  1 
ATOM   1898  C  C   . LYS A 1 235 ? 39.611  1.976   6.405   1.00 22.04  ? 235 LYS A C   1 
ATOM   1899  O  O   . LYS A 1 235 ? 40.008  2.942   5.725   1.00 21.43  ? 235 LYS A O   1 
ATOM   1900  C  CB  . LYS A 1 235 ? 37.171  2.297   6.933   1.00 22.48  ? 235 LYS A CB  1 
ATOM   1901  C  CG  . LYS A 1 235 ? 37.046  2.060   8.422   1.00 24.19  ? 235 LYS A CG  1 
ATOM   1902  C  CD  . LYS A 1 235 ? 35.843  2.845   9.003   1.00 22.85  ? 235 LYS A CD  1 
ATOM   1903  C  CE  . LYS A 1 235 ? 35.464  2.431   10.422  1.00 25.74  ? 235 LYS A CE  1 
ATOM   1904  N  NZ  . LYS A 1 235 ? 36.615  2.201   11.317  1.00 28.50  ? 235 LYS A NZ  1 
ATOM   1905  N  N   . SER A 1 236 ? 40.392  1.363   7.292   1.00 22.16  ? 236 SER A N   1 
ATOM   1906  C  CA  . SER A 1 236 ? 41.776  1.844   7.527   1.00 24.50  ? 236 SER A CA  1 
ATOM   1907  C  C   . SER A 1 236 ? 42.805  1.255   6.561   1.00 23.03  ? 236 SER A C   1 
ATOM   1908  O  O   . SER A 1 236 ? 43.999  1.545   6.711   1.00 24.35  ? 236 SER A O   1 
ATOM   1909  C  CB  . SER A 1 236 ? 42.234  1.557   8.972   1.00 24.47  ? 236 SER A CB  1 
ATOM   1910  O  OG  . SER A 1 236 ? 42.436  0.143   9.227   1.00 25.07  ? 236 SER A OG  1 
ATOM   1911  N  N   . SER A 1 237 ? 42.402  0.383   5.626   1.00 22.41  ? 237 SER A N   1 
ATOM   1912  C  CA  . SER A 1 237 ? 43.386  -0.162  4.709   1.00 25.39  ? 237 SER A CA  1 
ATOM   1913  C  C   . SER A 1 237 ? 43.737  0.787   3.548   1.00 27.88  ? 237 SER A C   1 
ATOM   1914  O  O   . SER A 1 237 ? 42.943  1.629   3.085   1.00 27.85  ? 237 SER A O   1 
ATOM   1915  C  CB  . SER A 1 237 ? 42.889  -1.494  4.137   1.00 26.23  ? 237 SER A CB  1 
ATOM   1916  O  OG  . SER A 1 237 ? 41.768  -1.217  3.287   1.00 28.86  ? 237 SER A OG  1 
ATOM   1917  N  N   . GLN A 1 238 ? 44.962  0.635   3.059   1.00 28.04  ? 238 GLN A N   1 
ATOM   1918  C  CA  . GLN A 1 238 ? 45.350  1.353   1.844   1.00 29.29  ? 238 GLN A CA  1 
ATOM   1919  C  C   . GLN A 1 238 ? 44.448  1.010   0.667   1.00 28.46  ? 238 GLN A C   1 
ATOM   1920  O  O   . GLN A 1 238 ? 44.057  1.902   -0.111  1.00 27.18  ? 238 GLN A O   1 
ATOM   1921  C  CB  . GLN A 1 238 ? 46.811  1.047   1.545   1.00 29.12  ? 238 GLN A CB  1 
ATOM   1922  C  CG  . GLN A 1 238 ? 47.391  1.803   0.413   1.00 35.56  ? 238 GLN A CG  1 
ATOM   1923  C  CD  . GLN A 1 238 ? 47.907  3.128   0.869   1.00 39.13  ? 238 GLN A CD  1 
ATOM   1924  O  OE1 . GLN A 1 238 ? 48.481  3.264   1.976   1.00 37.83  ? 238 GLN A OE1 1 
ATOM   1925  N  NE2 . GLN A 1 238 ? 47.818  4.116   -0.024  1.00 38.61  ? 238 GLN A NE2 1 
ATOM   1926  N  N   . TRP A 1 239 ? 44.085  -0.272  0.532   1.00 24.18  ? 239 TRP A N   1 
ATOM   1927  C  CA  . TRP A 1 239 ? 43.302  -0.670  -0.628  1.00 27.88  ? 239 TRP A CA  1 
ATOM   1928  C  C   . TRP A 1 239 ? 41.950  0.035   -0.642  1.00 23.57  ? 239 TRP A C   1 
ATOM   1929  O  O   . TRP A 1 239 ? 41.467  0.416   -1.722  1.00 26.30  ? 239 TRP A O   1 
ATOM   1930  C  CB  . TRP A 1 239 ? 43.157  -2.207  -0.704  1.00 25.85  ? 239 TRP A CB  1 
ATOM   1931  C  CG  . TRP A 1 239 ? 42.387  -2.877  0.380   1.00 26.04  ? 239 TRP A CG  1 
ATOM   1932  C  CD1 . TRP A 1 239 ? 42.907  -3.601  1.428   1.00 28.08  ? 239 TRP A CD1 1 
ATOM   1933  C  CD2 . TRP A 1 239 ? 40.952  -2.999  0.497   1.00 25.49  ? 239 TRP A CD2 1 
ATOM   1934  N  NE1 . TRP A 1 239 ? 41.891  -4.125  2.208   1.00 29.78  ? 239 TRP A NE1 1 
ATOM   1935  C  CE2 . TRP A 1 239 ? 40.685  -3.767  1.667   1.00 26.78  ? 239 TRP A CE2 1 
ATOM   1936  C  CE3 . TRP A 1 239 ? 39.881  -2.521  -0.254  1.00 26.58  ? 239 TRP A CE3 1 
ATOM   1937  C  CZ2 . TRP A 1 239 ? 39.387  -4.032  2.114   1.00 28.50  ? 239 TRP A CZ2 1 
ATOM   1938  C  CZ3 . TRP A 1 239 ? 38.588  -2.767  0.202   1.00 27.58  ? 239 TRP A CZ3 1 
ATOM   1939  C  CH2 . TRP A 1 239 ? 38.354  -3.541  1.358   1.00 30.03  ? 239 TRP A CH2 1 
ATOM   1940  N  N   . CYS A 1 240 ? 41.354  0.242   0.538   1.00 24.85  ? 240 CYS A N   1 
ATOM   1941  C  CA  . CYS A 1 240 ? 40.032  0.843   0.609   1.00 25.06  ? 240 CYS A CA  1 
ATOM   1942  C  C   . CYS A 1 240 ? 40.117  2.319   0.296   1.00 26.30  ? 240 CYS A C   1 
ATOM   1943  O  O   . CYS A 1 240 ? 39.355  2.827   -0.535  1.00 25.39  ? 240 CYS A O   1 
ATOM   1944  C  CB  . CYS A 1 240 ? 39.426  0.667   2.008   1.00 25.70  ? 240 CYS A CB  1 
ATOM   1945  S  SG  . CYS A 1 240 ? 37.663  1.166   2.046   1.00 27.42  ? 240 CYS A SG  1 
ATOM   1946  N  N   . ALA A 1 241 ? 41.080  3.006   0.923   1.00 26.09  ? 241 ALA A N   1 
ATOM   1947  C  CA  . ALA A 1 241 ? 41.282  4.435   0.649   1.00 24.51  ? 241 ALA A CA  1 
ATOM   1948  C  C   . ALA A 1 241 ? 41.647  4.691   -0.827  1.00 28.13  ? 241 ALA A C   1 
ATOM   1949  O  O   . ALA A 1 241 ? 41.102  5.599   -1.474  1.00 25.63  ? 241 ALA A O   1 
ATOM   1950  C  CB  . ALA A 1 241 ? 42.356  4.992   1.610   1.00 25.62  ? 241 ALA A CB  1 
ATOM   1951  N  N   . ASP A 1 242 ? 42.524  3.877   -1.397  1.00 25.87  ? 242 ASP A N   1 
ATOM   1952  C  CA  . ASP A 1 242 ? 42.883  4.042   -2.807  1.00 27.71  ? 242 ASP A CA  1 
ATOM   1953  C  C   . ASP A 1 242 ? 41.689  3.756   -3.717  1.00 26.59  ? 242 ASP A C   1 
ATOM   1954  O  O   . ASP A 1 242 ? 41.498  4.443   -4.708  1.00 27.61  ? 242 ASP A O   1 
ATOM   1955  C  CB  . ASP A 1 242 ? 44.061  3.126   -3.146  1.00 29.39  ? 242 ASP A CB  1 
ATOM   1956  C  CG  . ASP A 1 242 ? 45.354  3.632   -2.577  1.00 32.84  ? 242 ASP A CG  1 
ATOM   1957  O  OD1 . ASP A 1 242 ? 45.401  4.805   -2.122  1.00 31.41  ? 242 ASP A OD1 1 
ATOM   1958  O  OD2 . ASP A 1 242 ? 46.338  2.868   -2.618  1.00 30.79  ? 242 ASP A OD2 1 
ATOM   1959  N  N   . PHE A 1 243 ? 40.879  2.737   -3.413  1.00 25.63  ? 243 PHE A N   1 
ATOM   1960  C  CA  . PHE A 1 243 ? 39.705  2.474   -4.261  1.00 24.63  ? 243 PHE A CA  1 
ATOM   1961  C  C   . PHE A 1 243 ? 38.685  3.617   -4.200  1.00 26.47  ? 243 PHE A C   1 
ATOM   1962  O  O   . PHE A 1 243 ? 38.110  3.998   -5.235  1.00 25.87  ? 243 PHE A O   1 
ATOM   1963  C  CB  . PHE A 1 243 ? 39.023  1.165   -3.875  1.00 31.12  ? 243 PHE A CB  1 
ATOM   1964  C  CG  . PHE A 1 243 ? 37.930  0.808   -4.790  1.00 29.67  ? 243 PHE A CG  1 
ATOM   1965  C  CD1 . PHE A 1 243 ? 38.243  0.459   -6.093  1.00 30.46  ? 243 PHE A CD1 1 
ATOM   1966  C  CD2 . PHE A 1 243 ? 36.597  0.920   -4.418  1.00 32.33  ? 243 PHE A CD2 1 
ATOM   1967  C  CE1 . PHE A 1 243 ? 37.261  0.145   -6.997  1.00 34.23  ? 243 PHE A CE1 1 
ATOM   1968  C  CE2 . PHE A 1 243 ? 35.590  0.593   -5.321  1.00 30.58  ? 243 PHE A CE2 1 
ATOM   1969  C  CZ  . PHE A 1 243 ? 35.933  0.216   -6.628  1.00 31.81  ? 243 PHE A CZ  1 
ATOM   1970  N  N   . MET A 1 244 ? 38.455  4.187   -3.009  1.00 25.43  ? 244 MET A N   1 
ATOM   1971  C  CA  . MET A 1 244 ? 37.522  5.303   -2.885  1.00 24.14  ? 244 MET A CA  1 
ATOM   1972  C  C   . MET A 1 244 ? 37.984  6.461   -3.793  1.00 27.28  ? 244 MET A C   1 
ATOM   1973  O  O   . MET A 1 244 ? 37.172  7.092   -4.487  1.00 25.55  ? 244 MET A O   1 
ATOM   1974  C  CB  . MET A 1 244 ? 37.463  5.710   -1.394  1.00 22.93  ? 244 MET A CB  1 
ATOM   1975  C  CG  . MET A 1 244 ? 36.698  4.596   -0.602  1.00 22.83  ? 244 MET A CG  1 
ATOM   1976  S  SD  . MET A 1 244 ? 35.008  4.382   -1.073  1.00 28.59  ? 244 MET A SD  1 
ATOM   1977  C  CE  . MET A 1 244 ? 35.050  2.669   -1.568  1.00 31.49  ? 244 MET A CE  1 
ATOM   1978  N  N   . ASP A 1 245 ? 39.296  6.756   -3.832  1.00 24.87  ? 245 ASP A N   1 
ATOM   1979  C  CA  . ASP A 1 245 ? 39.779  7.803   -4.747  1.00 25.33  ? 245 ASP A CA  1 
ATOM   1980  C  C   . ASP A 1 245 ? 39.478  7.467   -6.204  1.00 27.68  ? 245 ASP A C   1 
ATOM   1981  O  O   . ASP A 1 245 ? 39.040  8.327   -6.975  1.00 30.94  ? 245 ASP A O   1 
ATOM   1982  C  CB  . ASP A 1 245 ? 41.281  7.998   -4.604  1.00 26.33  ? 245 ASP A CB  1 
ATOM   1983  C  CG  . ASP A 1 245 ? 41.658  8.834   -3.391  1.00 28.65  ? 245 ASP A CG  1 
ATOM   1984  O  OD1 . ASP A 1 245 ? 40.756  9.423   -2.747  1.00 30.17  ? 245 ASP A OD1 1 
ATOM   1985  O  OD2 . ASP A 1 245 ? 42.880  8.823   -3.064  1.00 30.74  ? 245 ASP A OD2 1 
ATOM   1986  N  N   . GLU A 1 246 ? 39.779  6.228   -6.609  1.00 26.67  ? 246 GLU A N   1 
ATOM   1987  C  CA  . GLU A 1 246 ? 39.500  5.780   -7.978  1.00 30.98  ? 246 GLU A CA  1 
ATOM   1988  C  C   . GLU A 1 246 ? 38.020  5.937   -8.297  1.00 27.61  ? 246 GLU A C   1 
ATOM   1989  O  O   . GLU A 1 246 ? 37.636  6.408   -9.386  1.00 29.15  ? 246 GLU A O   1 
ATOM   1990  C  CB  . GLU A 1 246 ? 39.836  4.303   -8.122  1.00 30.01  ? 246 GLU A CB  1 
ATOM   1991  C  CG  . GLU A 1 246 ? 41.171  3.877   -8.457  1.00 35.64  ? 246 GLU A CG  1 
ATOM   1992  C  CD  . GLU A 1 246 ? 41.089  2.433   -9.032  1.00 38.00  ? 246 GLU A CD  1 
ATOM   1993  O  OE1 . GLU A 1 246 ? 41.118  1.465   -8.233  1.00 36.50  ? 246 GLU A OE1 1 
ATOM   1994  O  OE2 . GLU A 1 246 ? 40.995  2.283   -10.286 1.00 44.06  ? 246 GLU A OE2 1 
ATOM   1995  N  N   . LEU A 1 247 ? 37.188  5.487   -7.360  1.00 27.70  ? 247 LEU A N   1 
ATOM   1996  C  CA  . LEU A 1 247 ? 35.743  5.517   -7.506  1.00 28.57  ? 247 LEU A CA  1 
ATOM   1997  C  C   . LEU A 1 247 ? 35.262  6.936   -7.633  1.00 26.42  ? 247 LEU A C   1 
ATOM   1998  O  O   . LEU A 1 247 ? 34.426  7.231   -8.489  1.00 28.23  ? 247 LEU A O   1 
ATOM   1999  C  CB  . LEU A 1 247 ? 35.062  4.827   -6.282  1.00 25.31  ? 247 LEU A CB  1 
ATOM   2000  C  CG  . LEU A 1 247 ? 33.535  4.705   -6.346  1.00 27.13  ? 247 LEU A CG  1 
ATOM   2001  C  CD1 . LEU A 1 247 ? 33.092  4.031   -7.660  1.00 27.13  ? 247 LEU A CD1 1 
ATOM   2002  C  CD2 . LEU A 1 247 ? 32.943  3.861   -5.165  1.00 27.39  ? 247 LEU A CD2 1 
ATOM   2003  N  N   . TYR A 1 248 ? 35.792  7.839   -6.802  1.00 26.54  ? 248 TYR A N   1 
ATOM   2004  C  CA  . TYR A 1 248 ? 35.412  9.246   -6.919  1.00 26.41  ? 248 TYR A CA  1 
ATOM   2005  C  C   . TYR A 1 248 ? 35.715  9.790   -8.323  1.00 29.62  ? 248 TYR A C   1 
ATOM   2006  O  O   . TYR A 1 248 ? 34.878  10.478  -8.914  1.00 30.75  ? 248 TYR A O   1 
ATOM   2007  C  CB  . TYR A 1 248 ? 36.116  10.043  -5.815  1.00 26.70  ? 248 TYR A CB  1 
ATOM   2008  C  CG  . TYR A 1 248 ? 35.923  11.560  -5.826  1.00 30.50  ? 248 TYR A CG  1 
ATOM   2009  C  CD1 . TYR A 1 248 ? 34.757  12.153  -5.345  1.00 31.54  ? 248 TYR A CD1 1 
ATOM   2010  C  CD2 . TYR A 1 248 ? 36.906  12.388  -6.337  1.00 34.72  ? 248 TYR A CD2 1 
ATOM   2011  C  CE1 . TYR A 1 248 ? 34.596  13.581  -5.350  1.00 26.68  ? 248 TYR A CE1 1 
ATOM   2012  C  CE2 . TYR A 1 248 ? 36.753  13.793  -6.372  1.00 38.17  ? 248 TYR A CE2 1 
ATOM   2013  C  CZ  . TYR A 1 248 ? 35.592  14.368  -5.864  1.00 38.49  ? 248 TYR A CZ  1 
ATOM   2014  O  OH  . TYR A 1 248 ? 35.418  15.740  -5.880  1.00 42.90  ? 248 TYR A OH  1 
ATOM   2015  N  N   . GLU A 1 249 ? 36.860  9.421   -8.914  1.00 30.54  ? 249 GLU A N   1 
ATOM   2016  C  CA  . GLU A 1 249 ? 37.164  9.915   -10.264 1.00 29.37  ? 249 GLU A CA  1 
ATOM   2017  C  C   . GLU A 1 249 ? 36.092  9.452   -11.252 1.00 29.33  ? 249 GLU A C   1 
ATOM   2018  O  O   . GLU A 1 249 ? 35.630  10.232  -12.091 1.00 31.14  ? 249 GLU A O   1 
ATOM   2019  C  CB  . GLU A 1 249 ? 38.534  9.407   -10.715 1.00 32.55  ? 249 GLU A CB  1 
ATOM   2020  C  CG  . GLU A 1 249 ? 39.707  10.103  -9.999  1.00 32.08  ? 249 GLU A CG  1 
ATOM   2021  C  CD  . GLU A 1 249 ? 39.629  11.633  -9.990  1.00 41.47  ? 249 GLU A CD  1 
ATOM   2022  O  OE1 . GLU A 1 249 ? 39.302  12.254  -11.034 1.00 40.17  ? 249 GLU A OE1 1 
ATOM   2023  O  OE2 . GLU A 1 249 ? 39.802  12.200  -8.879  1.00 41.85  ? 249 GLU A OE2 1 
ATOM   2024  N  N   . GLU A 1 250 ? 35.661  8.182   -11.147 1.00 27.96  ? 250 GLU A N   1 
ATOM   2025  C  CA  . GLU A 1 250 ? 34.648  7.675   -12.066 1.00 28.09  ? 250 GLU A CA  1 
ATOM   2026  C  C   . GLU A 1 250 ? 33.319  8.385   -11.859 1.00 29.25  ? 250 GLU A C   1 
ATOM   2027  O  O   . GLU A 1 250 ? 32.679  8.784   -12.846 1.00 30.19  ? 250 GLU A O   1 
ATOM   2028  C  CB  . GLU A 1 250 ? 34.453  6.147   -11.969 1.00 29.25  ? 250 GLU A CB  1 
ATOM   2029  C  CG  . GLU A 1 250 ? 33.331  5.722   -12.897 1.00 29.90  ? 250 GLU A CG  1 
ATOM   2030  C  CD  . GLU A 1 250 ? 33.190  4.221   -13.233 1.00 35.93  ? 250 GLU A CD  1 
ATOM   2031  O  OE1 . GLU A 1 250 ? 33.853  3.355   -12.614 1.00 36.39  ? 250 GLU A OE1 1 
ATOM   2032  O  OE2 . GLU A 1 250 ? 32.426  3.908   -14.209 1.00 36.78  ? 250 GLU A OE2 1 
ATOM   2033  N  N   . VAL A 1 251 ? 32.903  8.592   -10.608 1.00 28.18  ? 251 VAL A N   1 
ATOM   2034  C  CA  . VAL A 1 251 ? 31.600  9.215   -10.377 1.00 25.61  ? 251 VAL A CA  1 
ATOM   2035  C  C   . VAL A 1 251 ? 31.620  10.670  -10.810 1.00 29.61  ? 251 VAL A C   1 
ATOM   2036  O  O   . VAL A 1 251 ? 30.647  11.153  -11.421 1.00 28.26  ? 251 VAL A O   1 
ATOM   2037  C  CB  . VAL A 1 251 ? 31.154  9.026   -8.905  1.00 25.61  ? 251 VAL A CB  1 
ATOM   2038  C  CG1 . VAL A 1 251 ? 29.809  9.680   -8.685  1.00 24.99  ? 251 VAL A CG1 1 
ATOM   2039  C  CG2 . VAL A 1 251 ? 30.973  7.551   -8.673  1.00 25.68  ? 251 VAL A CG2 1 
ATOM   2040  N  N   . LYS A 1 252 ? 32.751  11.368  -10.588 1.00 29.40  ? 252 LYS A N   1 
ATOM   2041  C  CA  . LYS A 1 252 ? 32.911  12.728  -11.107 1.00 32.62  ? 252 LYS A CA  1 
ATOM   2042  C  C   . LYS A 1 252 ? 32.758  12.751  -12.633 1.00 32.93  ? 252 LYS A C   1 
ATOM   2043  O  O   . LYS A 1 252 ? 32.175  13.682  -13.207 1.00 33.31  ? 252 LYS A O   1 
ATOM   2044  C  CB  . LYS A 1 252 ? 34.300  13.264  -10.705 1.00 37.59  ? 252 LYS A CB  1 
ATOM   2045  C  CG  . LYS A 1 252 ? 34.514  14.760  -10.784 1.00 46.71  ? 252 LYS A CG  1 
ATOM   2046  C  CD  . LYS A 1 252 ? 34.243  15.353  -9.394  1.00 46.89  ? 252 LYS A CD  1 
ATOM   2047  C  CE  . LYS A 1 252 ? 33.750  16.810  -9.444  1.00 52.80  ? 252 LYS A CE  1 
ATOM   2048  N  NZ  . LYS A 1 252 ? 34.185  17.651  -8.292  1.00 53.83  ? 252 LYS A NZ  1 
ATOM   2049  N  N   . ASP A 1 253 ? 33.302  11.737  -13.315 1.00 31.41  ? 253 ASP A N   1 
ATOM   2050  C  CA  . ASP A 1 253 ? 33.180  11.665  -14.770 1.00 33.28  ? 253 ASP A CA  1 
ATOM   2051  C  C   . ASP A 1 253 ? 31.736  11.412  -15.181 1.00 33.76  ? 253 ASP A C   1 
ATOM   2052  O  O   . ASP A 1 253 ? 31.251  12.013  -16.142 1.00 33.12  ? 253 ASP A O   1 
ATOM   2053  C  CB  . ASP A 1 253 ? 34.106  10.575  -15.302 1.00 35.25  ? 253 ASP A CB  1 
ATOM   2054  C  CG  . ASP A 1 253 ? 34.039  10.461  -16.810 1.00 39.64  ? 253 ASP A CG  1 
ATOM   2055  O  OD1 . ASP A 1 253 ? 34.296  11.489  -17.496 1.00 38.79  ? 253 ASP A OD1 1 
ATOM   2056  O  OD2 . ASP A 1 253 ? 33.726  9.342   -17.308 1.00 46.44  ? 253 ASP A OD2 1 
ATOM   2057  N  N   . ARG A 1 254 ? 31.015  10.568  -14.423 1.00 29.84  ? 254 ARG A N   1 
ATOM   2058  C  CA  . ARG A 1 254 ? 29.586  10.401  -14.666 1.00 29.30  ? 254 ARG A CA  1 
ATOM   2059  C  C   . ARG A 1 254 ? 28.833  11.735  -14.574 1.00 31.80  ? 254 ARG A C   1 
ATOM   2060  O  O   . ARG A 1 254 ? 27.988  12.039  -15.430 1.00 30.22  ? 254 ARG A O   1 
ATOM   2061  C  CB  . ARG A 1 254 ? 28.992  9.370   -13.689 1.00 29.60  ? 254 ARG A CB  1 
ATOM   2062  C  CG  . ARG A 1 254 ? 29.546  7.951   -13.890 1.00 31.26  ? 254 ARG A CG  1 
ATOM   2063  C  CD  . ARG A 1 254 ? 29.027  6.962   -12.818 1.00 28.47  ? 254 ARG A CD  1 
ATOM   2064  N  NE  . ARG A 1 254 ? 27.594  6.682   -12.897 1.00 28.66  ? 254 ARG A NE  1 
ATOM   2065  C  CZ  . ARG A 1 254 ? 27.068  5.712   -13.652 1.00 34.03  ? 254 ARG A CZ  1 
ATOM   2066  N  NH1 . ARG A 1 254 ? 27.816  4.996   -14.475 1.00 33.66  ? 254 ARG A NH1 1 
ATOM   2067  N  NH2 . ARG A 1 254 ? 25.754  5.456   -13.586 1.00 32.34  ? 254 ARG A NH2 1 
ATOM   2068  N  N   . VAL A 1 255 ? 29.099  12.525  -13.523 1.00 28.02  ? 255 VAL A N   1 
ATOM   2069  C  CA  . VAL A 1 255 ? 28.429  13.821  -13.368 1.00 28.80  ? 255 VAL A CA  1 
ATOM   2070  C  C   . VAL A 1 255 ? 28.755  14.731  -14.550 1.00 30.77  ? 255 VAL A C   1 
ATOM   2071  O  O   . VAL A 1 255 ? 27.866  15.368  -15.133 1.00 32.34  ? 255 VAL A O   1 
ATOM   2072  C  CB  . VAL A 1 255 ? 28.799  14.471  -12.020 1.00 25.71  ? 255 VAL A CB  1 
ATOM   2073  C  CG1 . VAL A 1 255 ? 28.248  15.929  -11.947 1.00 31.05  ? 255 VAL A CG1 1 
ATOM   2074  C  CG2 . VAL A 1 255 ? 28.240  13.583  -10.867 1.00 27.39  ? 255 VAL A CG2 1 
ATOM   2075  N  N   . ALA A 1 256 ? 30.027  14.798  -14.931 1.00 31.44  ? 256 ALA A N   1 
ATOM   2076  C  CA  . ALA A 1 256 ? 30.449  15.642  -16.063 1.00 31.06  ? 256 ALA A CA  1 
ATOM   2077  C  C   . ALA A 1 256 ? 29.711  15.312  -17.355 1.00 33.42  ? 256 ALA A C   1 
ATOM   2078  O  O   . ALA A 1 256 ? 29.495  16.193  -18.210 1.00 34.11  ? 256 ALA A O   1 
ATOM   2079  C  CB  . ALA A 1 256 ? 31.949  15.465  -16.307 1.00 31.22  ? 256 ALA A CB  1 
ATOM   2080  N  N   . ARG A 1 257 ? 29.362  14.048  -17.542 1.00 31.12  ? 257 ARG A N   1 
ATOM   2081  C  CA  . ARG A 1 257 ? 28.802  13.573  -18.790 1.00 35.99  ? 257 ARG A CA  1 
ATOM   2082  C  C   . ARG A 1 257 ? 27.286  13.481  -18.745 1.00 33.09  ? 257 ARG A C   1 
ATOM   2083  O  O   . ARG A 1 257 ? 26.677  13.075  -19.754 1.00 35.40  ? 257 ARG A O   1 
ATOM   2084  C  CB  . ARG A 1 257 ? 29.413  12.218  -19.132 1.00 34.47  ? 257 ARG A CB  1 
ATOM   2085  C  CG  . ARG A 1 257 ? 30.797  12.422  -19.704 1.00 40.33  ? 257 ARG A CG  1 
ATOM   2086  C  CD  . ARG A 1 257 ? 31.276  11.166  -20.334 1.00 45.56  ? 257 ARG A CD  1 
ATOM   2087  N  NE  . ARG A 1 257 ? 31.568  10.191  -19.294 1.00 42.08  ? 257 ARG A NE  1 
ATOM   2088  C  CZ  . ARG A 1 257 ? 31.141  8.936   -19.346 1.00 48.15  ? 257 ARG A CZ  1 
ATOM   2089  N  NH1 . ARG A 1 257 ? 30.339  8.519   -20.314 1.00 47.96  ? 257 ARG A NH1 1 
ATOM   2090  N  NH2 . ARG A 1 257 ? 31.503  8.085   -18.388 1.00 45.05  ? 257 ARG A NH2 1 
ATOM   2091  N  N   . GLY A 1 258 ? 26.679  13.875  -17.623 1.00 33.33  ? 258 GLY A N   1 
ATOM   2092  C  CA  . GLY A 1 258 ? 25.242  13.849  -17.430 1.00 30.92  ? 258 GLY A CA  1 
ATOM   2093  C  C   . GLY A 1 258 ? 24.703  12.445  -17.336 1.00 34.57  ? 258 GLY A C   1 
ATOM   2094  O  O   . GLY A 1 258 ? 23.520  12.217  -17.647 1.00 31.56  ? 258 GLY A O   1 
ATOM   2095  N  N   . ILE A 1 259 ? 25.553  11.507  -16.920 1.00 29.37  ? 259 ILE A N   1 
ATOM   2096  C  CA  . ILE A 1 259 ? 25.180  10.097  -16.789 1.00 30.33  ? 259 ILE A CA  1 
ATOM   2097  C  C   . ILE A 1 259 ? 24.247  9.878   -15.599 1.00 30.28  ? 259 ILE A C   1 
ATOM   2098  O  O   . ILE A 1 259 ? 24.529  10.297  -14.459 1.00 29.75  ? 259 ILE A O   1 
ATOM   2099  C  CB  . ILE A 1 259 ? 26.448  9.236   -16.663 1.00 32.37  ? 259 ILE A CB  1 
ATOM   2100  C  CG1 . ILE A 1 259 ? 27.333  9.367   -17.893 1.00 36.22  ? 259 ILE A CG1 1 
ATOM   2101  C  CG2 . ILE A 1 259 ? 26.079  7.772   -16.381 1.00 35.09  ? 259 ILE A CG2 1 
ATOM   2102  C  CD1 . ILE A 1 259 ? 26.734  8.742   -19.109 1.00 38.01  ? 259 ILE A CD1 1 
ATOM   2103  N  N   . ALA A 1 260 ? 23.151  9.158   -15.849 1.00 31.13  ? 260 ALA A N   1 
ATOM   2104  C  CA  . ALA A 1 260 ? 22.162  8.783   -14.856 1.00 30.24  ? 260 ALA A CA  1 
ATOM   2105  C  C   . ALA A 1 260 ? 22.243  7.292   -14.553 1.00 29.92  ? 260 ALA A C   1 
ATOM   2106  O  O   . ALA A 1 260 ? 22.333  6.479   -15.479 1.00 30.65  ? 260 ALA A O   1 
ATOM   2107  C  CB  . ALA A 1 260 ? 20.767  9.084   -15.381 1.00 30.76  ? 260 ALA A CB  1 
ATOM   2108  N  N   . ALA A 1 261 ? 22.162  6.954   -13.257 1.00 27.42  ? 261 ALA A N   1 
ATOM   2109  C  CA  . ALA A 1 261 ? 21.989  5.555   -12.845 1.00 27.84  ? 261 ALA A CA  1 
ATOM   2110  C  C   . ALA A 1 261 ? 20.698  4.994   -13.414 1.00 30.83  ? 261 ALA A C   1 
ATOM   2111  O  O   . ALA A 1 261 ? 20.636  3.826   -13.818 1.00 32.44  ? 261 ALA A O   1 
ATOM   2112  C  CB  . ALA A 1 261 ? 21.981  5.461   -11.309 1.00 29.43  ? 261 ALA A CB  1 
ATOM   2113  N  N   . VAL A 1 262 ? 19.665  5.828   -13.498 1.00 30.02  ? 262 VAL A N   1 
ATOM   2114  C  CA  . VAL A 1 262 ? 18.324  5.399   -13.912 1.00 30.09  ? 262 VAL A CA  1 
ATOM   2115  C  C   . VAL A 1 262 ? 17.874  6.318   -15.037 1.00 33.43  ? 262 VAL A C   1 
ATOM   2116  O  O   . VAL A 1 262 ? 17.572  7.494   -14.793 1.00 31.04  ? 262 VAL A O   1 
ATOM   2117  C  CB  . VAL A 1 262 ? 17.354  5.436   -12.720 1.00 32.21  ? 262 VAL A CB  1 
ATOM   2118  C  CG1 . VAL A 1 262 ? 15.945  5.167   -13.166 1.00 31.38  ? 262 VAL A CG1 1 
ATOM   2119  C  CG2 . VAL A 1 262 ? 17.799  4.412   -11.681 1.00 30.81  ? 262 VAL A CG2 1 
ATOM   2120  N  N   . PRO A 1 263 ? 17.838  5.829   -16.281 1.00 32.01  ? 263 PRO A N   1 
ATOM   2121  C  CA  . PRO A 1 263 ? 17.786  6.742   -17.439 1.00 34.90  ? 263 PRO A CA  1 
ATOM   2122  C  C   . PRO A 1 263 ? 16.445  7.466   -17.571 1.00 39.14  ? 263 PRO A C   1 
ATOM   2123  O  O   . PRO A 1 263 ? 16.391  8.532   -18.195 1.00 41.07  ? 263 PRO A O   1 
ATOM   2124  C  CB  . PRO A 1 263 ? 18.058  5.804   -18.629 1.00 39.40  ? 263 PRO A CB  1 
ATOM   2125  C  CG  . PRO A 1 263 ? 17.686  4.461   -18.153 1.00 36.17  ? 263 PRO A CG  1 
ATOM   2126  C  CD  . PRO A 1 263 ? 18.015  4.428   -16.677 1.00 33.62  ? 263 PRO A CD  1 
ATOM   2127  N  N   . ASN A 1 264 ? 15.365  6.926   -16.996 1.00 34.28  ? 264 ASN A N   1 
ATOM   2128  C  CA  . ASN A 1 264 ? 14.086  7.611   -16.981 1.00 37.38  ? 264 ASN A CA  1 
ATOM   2129  C  C   . ASN A 1 264 ? 13.831  8.279   -15.636 1.00 34.03  ? 264 ASN A C   1 
ATOM   2130  O  O   . ASN A 1 264 ? 12.681  8.455   -15.249 1.00 34.04  ? 264 ASN A O   1 
ATOM   2131  C  CB  . ASN A 1 264 ? 12.954  6.639   -17.314 1.00 38.06  ? 264 ASN A CB  1 
ATOM   2132  C  CG  . ASN A 1 264 ? 12.855  5.479   -16.330 1.00 39.62  ? 264 ASN A CG  1 
ATOM   2133  O  OD1 . ASN A 1 264 ? 13.827  5.103   -15.675 1.00 39.57  ? 264 ASN A OD1 1 
ATOM   2134  N  ND2 . ASN A 1 264 ? 11.667  4.890   -16.238 1.00 38.68  ? 264 ASN A ND2 1 
ATOM   2135  N  N   . GLU A 1 265 ? 14.884  8.661   -14.925 1.00 32.73  ? 265 GLU A N   1 
ATOM   2136  C  CA  . GLU A 1 265 ? 14.716  9.294   -13.617 1.00 33.55  ? 265 GLU A CA  1 
ATOM   2137  C  C   . GLU A 1 265 ? 13.649  10.405  -13.641 1.00 35.14  ? 265 GLU A C   1 
ATOM   2138  O  O   . GLU A 1 265 ? 13.707  11.357  -14.428 1.00 33.54  ? 265 GLU A O   1 
ATOM   2139  C  CB  . GLU A 1 265 ? 16.061  9.853   -13.105 1.00 33.68  ? 265 GLU A CB  1 
ATOM   2140  C  CG  . GLU A 1 265 ? 15.909  10.605  -11.756 1.00 29.49  ? 265 GLU A CG  1 
ATOM   2141  C  CD  . GLU A 1 265 ? 17.199  11.254  -11.233 1.00 32.15  ? 265 GLU A CD  1 
ATOM   2142  O  OE1 . GLU A 1 265 ? 18.291  10.656  -11.363 1.00 30.20  ? 265 GLU A OE1 1 
ATOM   2143  O  OE2 . GLU A 1 265 ? 17.115  12.381  -10.694 1.00 30.75  ? 265 GLU A OE2 1 
ATOM   2144  N  N   . ALA A 1 266 ? 12.643  10.276  -12.790 1.00 30.74  ? 266 ALA A N   1 
ATOM   2145  C  CA  . ALA A 1 266 ? 11.689  11.367  -12.624 1.00 32.57  ? 266 ALA A CA  1 
ATOM   2146  C  C   . ALA A 1 266 ? 11.369  11.621  -11.171 1.00 32.11  ? 266 ALA A C   1 
ATOM   2147  O  O   . ALA A 1 266 ? 10.853  12.697  -10.835 1.00 33.16  ? 266 ALA A O   1 
ATOM   2148  C  CB  . ALA A 1 266 ? 10.391  11.058  -13.376 1.00 31.46  ? 266 ALA A CB  1 
ATOM   2149  N  N   . ILE A 1 267 ? 11.634  10.652  -10.306 1.00 31.19  ? 267 ILE A N   1 
ATOM   2150  C  CA  . ILE A 1 267 ? 11.312  10.701  -8.886  1.00 29.37  ? 267 ILE A CA  1 
ATOM   2151  C  C   . ILE A 1 267 ? 12.560  10.308  -8.091  1.00 29.23  ? 267 ILE A C   1 
ATOM   2152  O  O   . ILE A 1 267 ? 13.185  9.288   -8.376  1.00 30.46  ? 267 ILE A O   1 
ATOM   2153  C  CB  . ILE A 1 267 ? 10.159  9.743   -8.567  1.00 29.49  ? 267 ILE A CB  1 
ATOM   2154  C  CG1 . ILE A 1 267 ? 8.887   10.167  -9.320  1.00 34.57  ? 267 ILE A CG1 1 
ATOM   2155  C  CG2 . ILE A 1 267 ? 10.006  9.581   -7.035  1.00 28.53  ? 267 ILE A CG2 1 
ATOM   2156  C  CD1 . ILE A 1 267 ? 7.843   9.063   -9.300  1.00 37.03  ? 267 ILE A CD1 1 
ATOM   2157  N  N   . ARG A 1 268 ? 12.906  11.102  -7.100  1.00 27.60  ? 268 ARG A N   1 
ATOM   2158  C  CA  . ARG A 1 268 ? 14.077  10.834  -6.276  1.00 27.32  ? 268 ARG A CA  1 
ATOM   2159  C  C   . ARG A 1 268 ? 13.615  10.454  -4.885  1.00 26.13  ? 268 ARG A C   1 
ATOM   2160  O  O   . ARG A 1 268 ? 12.885  11.211  -4.227  1.00 26.25  ? 268 ARG A O   1 
ATOM   2161  C  CB  . ARG A 1 268 ? 15.012  12.036  -6.255  1.00 25.67  ? 268 ARG A CB  1 
ATOM   2162  C  CG  . ARG A 1 268 ? 15.660  12.335  -7.666  1.00 25.30  ? 268 ARG A CG  1 
ATOM   2163  C  CD  . ARG A 1 268 ? 16.260  13.784  -7.726  1.00 28.42  ? 268 ARG A CD  1 
ATOM   2164  N  NE  . ARG A 1 268 ? 17.464  13.919  -6.895  1.00 24.79  ? 268 ARG A NE  1 
ATOM   2165  C  CZ  . ARG A 1 268 ? 18.704  13.698  -7.319  1.00 24.94  ? 268 ARG A CZ  1 
ATOM   2166  N  NH1 . ARG A 1 268 ? 18.957  13.307  -8.557  1.00 25.75  ? 268 ARG A NH1 1 
ATOM   2167  N  NH2 . ARG A 1 268 ? 19.722  13.870  -6.477  1.00 25.51  ? 268 ARG A NH2 1 
ATOM   2168  N  N   . LEU A 1 269 ? 14.058  9.298   -4.428  1.00 25.91  ? 269 LEU A N   1 
ATOM   2169  C  CA  . LEU A 1 269 ? 13.674  8.751   -3.148  1.00 22.47  ? 269 LEU A CA  1 
ATOM   2170  C  C   . LEU A 1 269 ? 14.870  8.714   -2.205  1.00 27.16  ? 269 LEU A C   1 
ATOM   2171  O  O   . LEU A 1 269 ? 16.018  8.560   -2.639  1.00 27.48  ? 269 LEU A O   1 
ATOM   2172  C  CB  . LEU A 1 269 ? 13.125  7.316   -3.265  1.00 23.05  ? 269 LEU A CB  1 
ATOM   2173  C  CG  . LEU A 1 269 ? 11.907  7.175   -4.220  1.00 24.07  ? 269 LEU A CG  1 
ATOM   2174  C  CD1 . LEU A 1 269 ? 11.455  5.697   -4.407  1.00 28.01  ? 269 LEU A CD1 1 
ATOM   2175  C  CD2 . LEU A 1 269 ? 10.753  8.034   -3.782  1.00 26.13  ? 269 LEU A CD2 1 
ATOM   2176  N  N   . MET A 1 270 ? 14.576  8.800   -0.911  1.00 25.74  ? 270 MET A N   1 
ATOM   2177  C  CA  . MET A 1 270 ? 15.524  8.557   0.154   1.00 26.10  ? 270 MET A CA  1 
ATOM   2178  C  C   . MET A 1 270 ? 14.981  7.442   1.018   1.00 25.30  ? 270 MET A C   1 
ATOM   2179  O  O   . MET A 1 270 ? 13.771  7.370   1.255   1.00 27.19  ? 270 MET A O   1 
ATOM   2180  C  CB  . MET A 1 270 ? 15.761  9.808   0.972   1.00 23.67  ? 270 MET A CB  1 
ATOM   2181  C  CG  . MET A 1 270 ? 17.000  9.834   1.873   1.00 27.14  ? 270 MET A CG  1 
ATOM   2182  S  SD  . MET A 1 270 ? 16.865  11.107  3.200   1.00 28.81  ? 270 MET A SD  1 
ATOM   2183  C  CE  . MET A 1 270 ? 15.287  10.802  3.965   1.00 28.07  ? 270 MET A CE  1 
ATOM   2184  N  N   . THR A 1 271 ? 15.867  6.516   1.393   1.00 25.76  ? 271 THR A N   1 
ATOM   2185  C  CA  . THR A 1 271 ? 15.525  5.474   2.352   1.00 24.37  ? 271 THR A CA  1 
ATOM   2186  C  C   . THR A 1 271 ? 16.218  5.736   3.683   1.00 26.42  ? 271 THR A C   1 
ATOM   2187  O  O   . THR A 1 271 ? 16.775  6.802   3.939   1.00 25.96  ? 271 THR A O   1 
ATOM   2188  C  CB  . THR A 1 271 ? 15.893  4.080   1.798   1.00 25.30  ? 271 THR A CB  1 
ATOM   2189  O  OG1 . THR A 1 271 ? 17.324  4.005   1.683   1.00 27.87  ? 271 THR A OG1 1 
ATOM   2190  C  CG2 . THR A 1 271 ? 15.305  3.857   0.474   1.00 28.84  ? 271 THR A CG2 1 
ATOM   2191  N  N   . ASP A 1 272 ? 16.108  4.779   4.588   1.00 25.35  ? 272 ASP A N   1 
ATOM   2192  C  CA  . ASP A 1 272 ? 16.761  4.958   5.905   1.00 27.77  ? 272 ASP A CA  1 
ATOM   2193  C  C   . ASP A 1 272 ? 17.642  3.739   6.165   1.00 29.14  ? 272 ASP A C   1 
ATOM   2194  O  O   . ASP A 1 272 ? 18.481  3.460   5.336   1.00 32.38  ? 272 ASP A O   1 
ATOM   2195  C  CB  . ASP A 1 272 ? 15.774  5.339   7.008   1.00 29.94  ? 272 ASP A CB  1 
ATOM   2196  C  CG  . ASP A 1 272 ? 16.474  5.860   8.248   1.00 30.51  ? 272 ASP A CG  1 
ATOM   2197  O  OD1 . ASP A 1 272 ? 17.462  6.573   8.097   1.00 35.05  ? 272 ASP A OD1 1 
ATOM   2198  O  OD2 . ASP A 1 272 ? 16.079  5.467   9.328   1.00 32.14  ? 272 ASP A OD2 1 
ATOM   2199  N  N   . THR A 1 273 ? 17.322  2.943   7.168   1.00 27.67  ? 273 THR A N   1 
ATOM   2200  C  CA  . THR A 1 273 ? 18.171  1.803   7.562   1.00 32.09  ? 273 THR A CA  1 
ATOM   2201  C  C   . THR A 1 273 ? 18.327  0.747   6.463   1.00 38.39  ? 273 THR A C   1 
ATOM   2202  O  O   . THR A 1 273 ? 17.470  0.617   5.573   1.00 40.19  ? 273 THR A O   1 
ATOM   2203  C  CB  . THR A 1 273 ? 17.594  1.110   8.798   1.00 37.13  ? 273 THR A CB  1 
ATOM   2204  O  OG1 . THR A 1 273 ? 16.415  0.454   8.358   1.00 38.07  ? 273 THR A OG1 1 
ATOM   2205  C  CG2 . THR A 1 273 ? 17.190  2.072   9.884   1.00 38.74  ? 273 THR A CG2 1 
ATOM   2206  N  N   . GLN A 1 274 ? 19.351  -0.065  6.668   1.00 40.13  ? 274 GLN A N   1 
ATOM   2207  C  CA  . GLN A 1 274 ? 19.742  -1.225  5.847   1.00 40.50  ? 274 GLN A CA  1 
ATOM   2208  C  C   . GLN A 1 274 ? 18.476  -2.001  5.530   1.00 30.81  ? 274 GLN A C   1 
ATOM   2209  O  O   . GLN A 1 274 ? 17.790  -2.421  6.433   1.00 31.96  ? 274 GLN A O   1 
ATOM   2210  C  CB  . GLN A 1 274 ? 20.645  -2.096  6.736   1.00 39.11  ? 274 GLN A CB  1 
ATOM   2211  C  CG  . GLN A 1 274 ? 19.987  -2.779  7.944   1.00 35.58  ? 274 GLN A CG  1 
ATOM   2212  C  CD  . GLN A 1 274 ? 20.178  -2.241  9.349   1.00 39.04  ? 274 GLN A CD  1 
ATOM   2213  O  OE1 . GLN A 1 274 ? 19.429  -1.378  9.794   1.00 43.69  ? 274 GLN A OE1 1 
ATOM   2214  N  NE2 . GLN A 1 274 ? 21.127  -2.791  10.101  1.00 31.77  ? 274 GLN A NE2 1 
ATOM   2215  N  N   . PRO A 1 275 ? 17.884  -2.282  4.198   1.00 34.75  ? 275 PRO A N   1 
ATOM   2216  C  CA  . PRO A 1 275 ? 16.663  -3.038  3.863   1.00 30.64  ? 275 PRO A CA  1 
ATOM   2217  C  C   . PRO A 1 275 ? 16.945  -4.531  3.833   1.00 28.81  ? 275 PRO A C   1 
ATOM   2218  O  O   . PRO A 1 275 ? 18.112  -4.931  3.852   1.00 31.87  ? 275 PRO A O   1 
ATOM   2219  C  CB  . PRO A 1 275 ? 16.328  -2.513  2.468   1.00 40.99  ? 275 PRO A CB  1 
ATOM   2220  C  CG  . PRO A 1 275 ? 17.685  -2.431  1.880   1.00 36.86  ? 275 PRO A CG  1 
ATOM   2221  C  CD  . PRO A 1 275 ? 18.605  -1.914  2.977   1.00 41.62  ? 275 PRO A CD  1 
ATOM   2222  N  N   . PRO A 1 276 ? 15.935  -5.383  3.853   1.00 32.57  ? 276 PRO A N   1 
ATOM   2223  C  CA  . PRO A 1 276 ? 16.181  -6.801  3.592   1.00 28.99  ? 276 PRO A CA  1 
ATOM   2224  C  C   . PRO A 1 276 ? 16.549  -7.035  2.118   1.00 29.34  ? 276 PRO A C   1 
ATOM   2225  O  O   . PRO A 1 276 ? 16.244  -6.238  1.238   1.00 32.28  ? 276 PRO A O   1 
ATOM   2226  C  CB  . PRO A 1 276 ? 14.861  -7.503  3.935   1.00 33.09  ? 276 PRO A CB  1 
ATOM   2227  C  CG  . PRO A 1 276 ? 13.924  -6.459  4.412   1.00 36.59  ? 276 PRO A CG  1 
ATOM   2228  C  CD  . PRO A 1 276 ? 14.525  -5.086  4.175   1.00 33.41  ? 276 PRO A CD  1 
ATOM   2229  N  N   . TRP A 1 277 ? 17.160  -8.169  1.847   1.00 35.59  ? 277 TRP A N   1 
ATOM   2230  C  CA  . TRP A 1 277 ? 17.636  -8.391  0.473   1.00 32.61  ? 277 TRP A CA  1 
ATOM   2231  C  C   . TRP A 1 277 ? 16.491  -8.419  -0.528  1.00 33.34  ? 277 TRP A C   1 
ATOM   2232  O  O   . TRP A 1 277 ? 16.621  -7.908  -1.661  1.00 37.97  ? 277 TRP A O   1 
ATOM   2233  C  CB  . TRP A 1 277 ? 18.418  -9.678  0.333   1.00 34.84  ? 277 TRP A CB  1 
ATOM   2234  C  CG  . TRP A 1 277 ? 19.739  -9.566  0.845   1.00 36.32  ? 277 TRP A CG  1 
ATOM   2235  C  CD1 . TRP A 1 277 ? 20.147  -9.723  2.152   1.00 36.24  ? 277 TRP A CD1 1 
ATOM   2236  C  CD2 . TRP A 1 277 ? 20.766  -8.860  0.211   1.00 35.66  ? 277 TRP A CD2 1 
ATOM   2237  N  NE1 . TRP A 1 277 ? 21.470  -9.384  2.281   1.00 37.84  ? 277 TRP A NE1 1 
ATOM   2238  C  CE2 . TRP A 1 277 ? 21.856  -8.789  1.108   1.00 42.77  ? 277 TRP A CE2 1 
ATOM   2239  C  CE3 . TRP A 1 277 ? 20.896  -8.299  -1.061  1.00 47.32  ? 277 TRP A CE3 1 
ATOM   2240  C  CZ2 . TRP A 1 277 ? 23.062  -8.191  0.763   1.00 44.58  ? 277 TRP A CZ2 1 
ATOM   2241  C  CZ3 . TRP A 1 277 ? 22.090  -7.718  -1.411  1.00 46.21  ? 277 TRP A CZ3 1 
ATOM   2242  C  CH2 . TRP A 1 277 ? 23.156  -7.658  -0.505  1.00 47.31  ? 277 TRP A CH2 1 
ATOM   2243  N  N   . SER A 1 278 ? 15.359  -8.979  -0.118  1.00 29.32  ? 278 SER A N   1 
ATOM   2244  C  CA  . SER A 1 278 ? 14.165  -9.076  -0.938  1.00 36.63  ? 278 SER A CA  1 
ATOM   2245  C  C   . SER A 1 278 ? 13.634  -7.734  -1.392  1.00 39.60  ? 278 SER A C   1 
ATOM   2246  O  O   . SER A 1 278 ? 12.845  -7.698  -2.349  1.00 44.26  ? 278 SER A O   1 
ATOM   2247  C  CB  . SER A 1 278 ? 13.067  -9.830  -0.164  1.00 40.50  ? 278 SER A CB  1 
ATOM   2248  O  OG  . SER A 1 278 ? 13.204  -11.226 -0.330  1.00 46.39  ? 278 SER A OG  1 
ATOM   2249  N  N   . PHE A 1 279 ? 14.028  -6.639  -0.732  1.00 35.56  ? 279 PHE A N   1 
ATOM   2250  C  CA  . PHE A 1 279 ? 13.575  -5.335  -1.173  1.00 40.48  ? 279 PHE A CA  1 
ATOM   2251  C  C   . PHE A 1 279 ? 14.256  -4.922  -2.470  1.00 40.47  ? 279 PHE A C   1 
ATOM   2252  O  O   . PHE A 1 279 ? 13.695  -4.125  -3.233  1.00 41.32  ? 279 PHE A O   1 
ATOM   2253  C  CB  . PHE A 1 279 ? 13.839  -4.300  -0.082  1.00 34.55  ? 279 PHE A CB  1 
ATOM   2254  C  CG  . PHE A 1 279 ? 13.106  -3.001  -0.281  1.00 36.58  ? 279 PHE A CG  1 
ATOM   2255  C  CD1 . PHE A 1 279 ? 13.666  -1.989  -1.035  1.00 37.99  ? 279 PHE A CD1 1 
ATOM   2256  C  CD2 . PHE A 1 279 ? 11.867  -2.790  0.287   1.00 35.00  ? 279 PHE A CD2 1 
ATOM   2257  C  CE1 . PHE A 1 279 ? 13.007  -0.786  -1.218  1.00 36.37  ? 279 PHE A CE1 1 
ATOM   2258  C  CE2 . PHE A 1 279 ? 11.193  -1.579  0.083   1.00 33.67  ? 279 PHE A CE2 1 
ATOM   2259  C  CZ  . PHE A 1 279 ? 11.759  -0.602  -0.668  1.00 35.06  ? 279 PHE A CZ  1 
ATOM   2260  N  N   . LEU A 1 280 ? 15.449  -5.460  -2.743  1.00 42.10  ? 280 LEU A N   1 
ATOM   2261  C  CA  . LEU A 1 280 ? 16.216  -4.988  -3.894  1.00 44.23  ? 280 LEU A CA  1 
ATOM   2262  C  C   . LEU A 1 280 ? 15.419  -5.092  -5.182  1.00 45.41  ? 280 LEU A C   1 
ATOM   2263  O  O   . LEU A 1 280 ? 15.504  -4.212  -6.051  1.00 42.71  ? 280 LEU A O   1 
ATOM   2264  C  CB  . LEU A 1 280 ? 17.521  -5.767  -4.007  1.00 48.19  ? 280 LEU A CB  1 
ATOM   2265  C  CG  . LEU A 1 280 ? 18.680  -5.291  -3.143  1.00 41.27  ? 280 LEU A CG  1 
ATOM   2266  C  CD1 . LEU A 1 280 ? 18.392  -4.874  -1.652  1.00 42.01  ? 280 LEU A CD1 1 
ATOM   2267  C  CD2 . LEU A 1 280 ? 19.732  -6.301  -3.271  1.00 48.46  ? 280 LEU A CD2 1 
ATOM   2268  N  N   . LYS A 1 281 ? 14.636  -6.158  -5.324  1.00 40.83  ? 281 LYS A N   1 
ATOM   2269  C  CA  . LYS A 1 281 ? 13.757  -6.303  -6.470  1.00 44.80  ? 281 LYS A CA  1 
ATOM   2270  C  C   . LYS A 1 281 ? 12.680  -5.206  -6.530  1.00 41.94  ? 281 LYS A C   1 
ATOM   2271  O  O   . LYS A 1 281 ? 12.148  -4.930  -7.613  1.00 41.17  ? 281 LYS A O   1 
ATOM   2272  C  CB  . LYS A 1 281 ? 13.130  -7.702  -6.433  1.00 44.68  ? 281 LYS A CB  1 
ATOM   2273  C  CG  . LYS A 1 281 ? 11.678  -7.676  -6.022  1.00 48.03  ? 281 LYS A CG  1 
ATOM   2274  C  CD  . LYS A 1 281 ? 10.949  -8.989  -6.292  1.00 51.25  ? 281 LYS A CD  1 
ATOM   2275  C  CE  . LYS A 1 281 ? 11.513  -10.128 -5.465  1.00 53.92  ? 281 LYS A CE  1 
ATOM   2276  N  NZ  . LYS A 1 281 ? 10.643  -11.340 -5.647  1.00 62.37  ? 281 LYS A NZ  1 
ATOM   2277  N  N   . ILE A 1 282 ? 12.294  -4.620  -5.380  1.00 38.92  ? 282 ILE A N   1 
ATOM   2278  C  CA  . ILE A 1 282 ? 11.370  -3.476  -5.388  1.00 38.48  ? 282 ILE A CA  1 
ATOM   2279  C  C   . ILE A 1 282 ? 12.033  -2.237  -5.986  1.00 36.90  ? 282 ILE A C   1 
ATOM   2280  O  O   . ILE A 1 282 ? 11.390  -1.482  -6.729  1.00 38.70  ? 282 ILE A O   1 
ATOM   2281  C  CB  . ILE A 1 282 ? 10.849  -3.184  -3.966  1.00 37.66  ? 282 ILE A CB  1 
ATOM   2282  C  CG1 . ILE A 1 282 ? 10.087  -4.401  -3.427  1.00 40.41  ? 282 ILE A CG1 1 
ATOM   2283  C  CG2 . ILE A 1 282 ? 10.003  -1.898  -3.960  1.00 37.49  ? 282 ILE A CG2 1 
ATOM   2284  C  CD1 . ILE A 1 282 ? 9.294   -4.133  -2.144  1.00 38.44  ? 282 ILE A CD1 1 
ATOM   2285  N  N   . PHE A 1 283 ? 13.313  -1.994  -5.666  1.00 38.33  ? 283 PHE A N   1 
ATOM   2286  C  CA  . PHE A 1 283 ? 14.050  -0.920  -6.350  1.00 38.13  ? 283 PHE A CA  1 
ATOM   2287  C  C   . PHE A 1 283 ? 13.971  -1.069  -7.857  1.00 39.72  ? 283 PHE A C   1 
ATOM   2288  O  O   . PHE A 1 283 ? 13.784  -0.086  -8.583  1.00 37.64  ? 283 PHE A O   1 
ATOM   2289  C  CB  . PHE A 1 283 ? 15.537  -0.867  -5.948  1.00 35.53  ? 283 PHE A CB  1 
ATOM   2290  C  CG  . PHE A 1 283 ? 15.826  -0.378  -4.547  1.00 40.47  ? 283 PHE A CG  1 
ATOM   2291  C  CD1 . PHE A 1 283 ? 15.403  0.882   -4.120  1.00 44.02  ? 283 PHE A CD1 1 
ATOM   2292  C  CD2 . PHE A 1 283 ? 16.579  -1.146  -3.677  1.00 35.71  ? 283 PHE A CD2 1 
ATOM   2293  C  CE1 . PHE A 1 283 ? 15.710  1.336   -2.845  1.00 40.29  ? 283 PHE A CE1 1 
ATOM   2294  C  CE2 . PHE A 1 283 ? 16.870  -0.724  -2.407  1.00 37.44  ? 283 PHE A CE2 1 
ATOM   2295  C  CZ  . PHE A 1 283 ? 16.455  0.526   -1.972  1.00 36.41  ? 283 PHE A CZ  1 
ATOM   2296  N  N   . ARG A 1 284 ? 14.122  -2.295  -8.350  1.00 37.09  ? 284 ARG A N   1 
ATOM   2297  C  CA  . ARG A 1 284 ? 14.044  -2.511  -9.784  1.00 36.75  ? 284 ARG A CA  1 
ATOM   2298  C  C   . ARG A 1 284 ? 12.646  -2.202  -10.314 1.00 40.82  ? 284 ARG A C   1 
ATOM   2299  O  O   . ARG A 1 284 ? 12.497  -1.556  -11.356 1.00 39.64  ? 284 ARG A O   1 
ATOM   2300  C  CB  . ARG A 1 284 ? 14.434  -3.952  -10.094 1.00 42.99  ? 284 ARG A CB  1 
ATOM   2301  C  CG  . ARG A 1 284 ? 15.929  -4.082  -10.326 1.00 50.84  ? 284 ARG A CG  1 
ATOM   2302  C  CD  . ARG A 1 284 ? 16.331  -5.496  -10.758 1.00 58.04  ? 284 ARG A CD  1 
ATOM   2303  N  NE  . ARG A 1 284 ? 16.998  -6.188  -9.661  1.00 61.97  ? 284 ARG A NE  1 
ATOM   2304  C  CZ  . ARG A 1 284 ? 16.579  -7.324  -9.119  1.00 59.74  ? 284 ARG A CZ  1 
ATOM   2305  N  NH1 . ARG A 1 284 ? 15.542  -7.991  -9.615  1.00 57.49  ? 284 ARG A NH1 1 
ATOM   2306  N  NH2 . ARG A 1 284 ? 17.225  -7.809  -8.065  1.00 57.40  ? 284 ARG A NH2 1 
ATOM   2307  N  N   . TYR A 1 285 ? 11.604  -2.632  -9.594  1.00 38.98  ? 285 TYR A N   1 
ATOM   2308  C  CA  . TYR A 1 285 ? 10.236  -2.292  -9.985  1.00 39.52  ? 285 TYR A CA  1 
ATOM   2309  C  C   . TYR A 1 285 ? 10.010  -0.784  -9.939  1.00 36.38  ? 285 TYR A C   1 
ATOM   2310  O  O   . TYR A 1 285 ? 9.299   -0.217  -10.781 1.00 37.95  ? 285 TYR A O   1 
ATOM   2311  C  CB  . TYR A 1 285 ? 9.258   -2.990  -9.044  1.00 44.17  ? 285 TYR A CB  1 
ATOM   2312  C  CG  . TYR A 1 285 ? 7.817   -2.620  -9.240  1.00 44.49  ? 285 TYR A CG  1 
ATOM   2313  C  CD1 . TYR A 1 285 ? 7.081   -3.162  -10.283 1.00 47.14  ? 285 TYR A CD1 1 
ATOM   2314  C  CD2 . TYR A 1 285 ? 7.182   -1.726  -8.370  1.00 45.12  ? 285 TYR A CD2 1 
ATOM   2315  C  CE1 . TYR A 1 285 ? 5.749   -2.838  -10.482 1.00 50.83  ? 285 TYR A CE1 1 
ATOM   2316  C  CE2 . TYR A 1 285 ? 5.831   -1.385  -8.556  1.00 44.86  ? 285 TYR A CE2 1 
ATOM   2317  C  CZ  . TYR A 1 285 ? 5.124   -1.944  -9.617  1.00 50.68  ? 285 TYR A CZ  1 
ATOM   2318  O  OH  . TYR A 1 285 ? 3.782   -1.650  -9.848  1.00 47.65  ? 285 TYR A OH  1 
ATOM   2319  N  N   . LEU A 1 286 ? 10.591  -0.129  -8.949  1.00 36.30  ? 286 LEU A N   1 
ATOM   2320  C  CA  . LEU A 1 286 ? 10.418  1.313   -8.802  1.00 37.85  ? 286 LEU A CA  1 
ATOM   2321  C  C   . LEU A 1 286 ? 10.973  2.046   -10.015 1.00 38.08  ? 286 LEU A C   1 
ATOM   2322  O  O   . LEU A 1 286 ? 10.477  3.118   -10.393 1.00 40.32  ? 286 LEU A O   1 
ATOM   2323  C  CB  . LEU A 1 286 ? 11.098  1.764   -7.500  1.00 35.05  ? 286 LEU A CB  1 
ATOM   2324  C  CG  . LEU A 1 286 ? 10.265  1.607   -6.222  1.00 38.78  ? 286 LEU A CG  1 
ATOM   2325  C  CD1 . LEU A 1 286 ? 11.099  1.849   -4.963  1.00 36.32  ? 286 LEU A CD1 1 
ATOM   2326  C  CD2 . LEU A 1 286 ? 9.116   2.561   -6.269  1.00 40.21  ? 286 LEU A CD2 1 
ATOM   2327  N  N   . GLU A 1 287 ? 11.961  1.453   -10.682 1.00 42.58  ? 287 GLU A N   1 
ATOM   2328  C  CA  . GLU A 1 287 ? 12.557  2.108   -11.836 1.00 39.61  ? 287 GLU A CA  1 
ATOM   2329  C  C   . GLU A 1 287 ? 11.575  2.219   -12.980 1.00 40.17  ? 287 GLU A C   1 
ATOM   2330  O  O   . GLU A 1 287 ? 11.704  3.128   -13.803 1.00 42.18  ? 287 GLU A O   1 
ATOM   2331  C  CB  . GLU A 1 287 ? 13.798  1.346   -12.263 1.00 41.64  ? 287 GLU A CB  1 
ATOM   2332  C  CG  . GLU A 1 287 ? 14.893  1.512   -11.266 1.00 35.54  ? 287 GLU A CG  1 
ATOM   2333  C  CD  . GLU A 1 287 ? 16.118  0.723   -11.664 1.00 51.76  ? 287 GLU A CD  1 
ATOM   2334  O  OE1 . GLU A 1 287 ? 17.117  0.727   -10.914 1.00 51.39  ? 287 GLU A OE1 1 
ATOM   2335  O  OE2 . GLU A 1 287 ? 16.060  0.077   -12.741 1.00 54.57  ? 287 GLU A OE2 1 
ATOM   2336  N  N   . THR A 1 288 ? 10.567  1.323   -13.053 1.00 40.49  ? 288 THR A N   1 
ATOM   2337  C  CA  . THR A 1 288 ? 9.547   1.457   -14.098 1.00 42.78  ? 288 THR A CA  1 
ATOM   2338  C  C   . THR A 1 288 ? 8.665   2.684   -13.900 1.00 42.16  ? 288 THR A C   1 
ATOM   2339  O  O   . THR A 1 288 ? 8.034   3.142   -14.861 1.00 46.01  ? 288 THR A O   1 
ATOM   2340  C  CB  . THR A 1 288 ? 8.680   0.175   -14.214 1.00 45.04  ? 288 THR A CB  1 
ATOM   2341  O  OG1 . THR A 1 288 ? 7.571   0.238   -13.289 1.00 46.40  ? 288 THR A OG1 1 
ATOM   2342  C  CG2 . THR A 1 288 ? 9.516   -1.070  -14.019 1.00 46.20  ? 288 THR A CG2 1 
ATOM   2343  N  N   . TYR A 1 289 ? 8.621   3.245   -12.688 1.00 42.14  ? 289 TYR A N   1 
ATOM   2344  C  CA  . TYR A 1 289 ? 8.061   4.561   -12.461 1.00 36.56  ? 289 TYR A CA  1 
ATOM   2345  C  C   . TYR A 1 289 ? 9.073   5.672   -12.673 1.00 39.27  ? 289 TYR A C   1 
ATOM   2346  O  O   . TYR A 1 289 ? 8.716   6.834   -12.469 1.00 40.30  ? 289 TYR A O   1 
ATOM   2347  C  CB  . TYR A 1 289 ? 7.552   4.708   -11.001 1.00 38.97  ? 289 TYR A CB  1 
ATOM   2348  C  CG  . TYR A 1 289 ? 6.281   3.956   -10.759 1.00 42.81  ? 289 TYR A CG  1 
ATOM   2349  C  CD1 . TYR A 1 289 ? 5.050   4.540   -11.045 1.00 42.28  ? 289 TYR A CD1 1 
ATOM   2350  C  CD2 . TYR A 1 289 ? 6.304   2.664   -10.225 1.00 40.04  ? 289 TYR A CD2 1 
ATOM   2351  C  CE1 . TYR A 1 289 ? 3.863   3.855   -10.842 1.00 46.95  ? 289 TYR A CE1 1 
ATOM   2352  C  CE2 . TYR A 1 289 ? 5.113   1.963   -10.013 1.00 43.64  ? 289 TYR A CE2 1 
ATOM   2353  C  CZ  . TYR A 1 289 ? 3.897   2.576   -10.313 1.00 45.29  ? 289 TYR A CZ  1 
ATOM   2354  O  OH  . TYR A 1 289 ? 2.703   1.932   -10.118 1.00 47.11  ? 289 TYR A OH  1 
ATOM   2355  N  N   . GLY A 1 290 ? 10.332  5.355   -12.999 1.00 34.52  ? 290 GLY A N   1 
ATOM   2356  C  CA  . GLY A 1 290 ? 11.348  6.396   -13.005 1.00 35.98  ? 290 GLY A CA  1 
ATOM   2357  C  C   . GLY A 1 290 ? 11.806  6.837   -11.638 1.00 34.74  ? 290 GLY A C   1 
ATOM   2358  O  O   . GLY A 1 290 ? 12.340  7.951   -11.491 1.00 34.21  ? 290 GLY A O   1 
ATOM   2359  N  N   . ALA A 1 291 ? 11.612  6.008   -10.611 1.00 31.05  ? 291 ALA A N   1 
ATOM   2360  C  CA  . ALA A 1 291 ? 12.030  6.344   -9.267  1.00 32.84  ? 291 ALA A CA  1 
ATOM   2361  C  C   . ALA A 1 291 ? 13.418  5.770   -9.044  1.00 34.00  ? 291 ALA A C   1 
ATOM   2362  O  O   . ALA A 1 291 ? 13.689  4.624   -9.415  1.00 32.33  ? 291 ALA A O   1 
ATOM   2363  C  CB  . ALA A 1 291 ? 11.059  5.807   -8.211  1.00 29.70  ? 291 ALA A CB  1 
ATOM   2364  N  N   . VAL A 1 292 ? 14.301  6.592   -8.511  1.00 27.41  ? 292 VAL A N   1 
ATOM   2365  C  CA  . VAL A 1 292 ? 15.639  6.207   -8.093  1.00 28.85  ? 292 VAL A CA  1 
ATOM   2366  C  C   . VAL A 1 292 ? 15.809  6.554   -6.610  1.00 29.59  ? 292 VAL A C   1 
ATOM   2367  O  O   . VAL A 1 292 ? 15.470  7.665   -6.168  1.00 27.16  ? 292 VAL A O   1 
ATOM   2368  C  CB  . VAL A 1 292 ? 16.710  6.901   -8.950  1.00 30.05  ? 292 VAL A CB  1 
ATOM   2369  C  CG1 . VAL A 1 292 ? 16.533  8.445   -8.906  1.00 29.70  ? 292 VAL A CG1 1 
ATOM   2370  C  CG2 . VAL A 1 292 ? 18.098  6.534   -8.426  1.00 29.25  ? 292 VAL A CG2 1 
ATOM   2371  N  N   . SER A 1 293 ? 16.360  5.618   -5.832  1.00 27.83  ? 293 SER A N   1 
ATOM   2372  C  CA  . SER A 1 293 ? 16.853  5.981   -4.514  1.00 25.20  ? 293 SER A CA  1 
ATOM   2373  C  C   . SER A 1 293 ? 18.226  6.624   -4.608  1.00 25.27  ? 293 SER A C   1 
ATOM   2374  O  O   . SER A 1 293 ? 19.168  5.998   -5.095  1.00 25.45  ? 293 SER A O   1 
ATOM   2375  C  CB  . SER A 1 293 ? 16.920  4.780   -3.568  1.00 27.34  ? 293 SER A CB  1 
ATOM   2376  O  OG  . SER A 1 293 ? 17.200  5.347   -2.332  1.00 29.27  ? 293 SER A OG  1 
ATOM   2377  N  N   . ILE A 1 294 ? 18.356  7.865   -4.104  1.00 23.90  ? 294 ILE A N   1 
ATOM   2378  C  CA  . ILE A 1 294 ? 19.654  8.516   -4.131  1.00 23.21  ? 294 ILE A CA  1 
ATOM   2379  C  C   . ILE A 1 294 ? 20.509  8.166   -2.934  1.00 23.84  ? 294 ILE A C   1 
ATOM   2380  O  O   . ILE A 1 294 ? 21.666  8.619   -2.856  1.00 23.35  ? 294 ILE A O   1 
ATOM   2381  C  CB  . ILE A 1 294 ? 19.505  10.049  -4.298  1.00 25.96  ? 294 ILE A CB  1 
ATOM   2382  C  CG1 . ILE A 1 294 ? 18.601  10.664  -3.235  1.00 26.26  ? 294 ILE A CG1 1 
ATOM   2383  C  CG2 . ILE A 1 294 ? 18.906  10.282  -5.692  1.00 29.52  ? 294 ILE A CG2 1 
ATOM   2384  C  CD1 . ILE A 1 294 ? 19.184  10.673  -1.818  1.00 23.39  ? 294 ILE A CD1 1 
ATOM   2385  N  N   . GLY A 1 295 ? 19.980  7.383   -1.972  1.00 24.39  ? 295 GLY A N   1 
ATOM   2386  C  CA  . GLY A 1 295 ? 20.756  7.140   -0.777  1.00 22.84  ? 295 GLY A CA  1 
ATOM   2387  C  C   . GLY A 1 295 ? 19.907  7.228   0.481   1.00 22.77  ? 295 GLY A C   1 
ATOM   2388  O  O   . GLY A 1 295 ? 18.663  7.210   0.431   1.00 25.61  ? 295 GLY A O   1 
ATOM   2389  N  N   . SER A 1 296 ? 20.619  7.309   1.606   1.00 21.04  ? 296 SER A N   1 
ATOM   2390  C  CA  . SER A 1 296 ? 20.080  7.290   2.970   1.00 20.16  ? 296 SER A CA  1 
ATOM   2391  C  C   . SER A 1 296 ? 21.175  7.741   3.923   1.00 19.73  ? 296 SER A C   1 
ATOM   2392  O  O   . SER A 1 296 ? 22.370  7.640   3.606   1.00 23.62  ? 296 SER A O   1 
ATOM   2393  C  CB  . SER A 1 296 ? 19.604  5.871   3.324   1.00 22.17  ? 296 SER A CB  1 
ATOM   2394  O  OG  . SER A 1 296 ? 20.688  4.911   3.239   1.00 23.73  ? 296 SER A OG  1 
ATOM   2395  N  N   . LEU A 1 297 ? 20.769  8.133   5.145   1.00 22.10  ? 297 LEU A N   1 
ATOM   2396  C  CA  . LEU A 1 297 ? 21.769  8.382   6.153   1.00 21.94  ? 297 LEU A CA  1 
ATOM   2397  C  C   . LEU A 1 297 ? 22.603  7.136   6.405   1.00 22.09  ? 297 LEU A C   1 
ATOM   2398  O  O   . LEU A 1 297 ? 23.817  7.224   6.680   1.00 23.58  ? 297 LEU A O   1 
ATOM   2399  C  CB  . LEU A 1 297 ? 21.093  8.850   7.458   1.00 21.52  ? 297 LEU A CB  1 
ATOM   2400  C  CG  . LEU A 1 297 ? 22.067  9.280   8.516   1.00 24.37  ? 297 LEU A CG  1 
ATOM   2401  C  CD1 . LEU A 1 297 ? 22.757  10.555  8.078   1.00 23.39  ? 297 LEU A CD1 1 
ATOM   2402  C  CD2 . LEU A 1 297 ? 21.353  9.480   9.897   1.00 27.15  ? 297 LEU A CD2 1 
ATOM   2403  N  N   . TYR A 1 298 ? 21.978  5.959   6.275   1.00 21.88  ? 298 TYR A N   1 
ATOM   2404  C  CA  . TYR A 1 298 ? 22.728  4.721   6.489   1.00 24.26  ? 298 TYR A CA  1 
ATOM   2405  C  C   . TYR A 1 298 ? 23.822  4.519   5.446   1.00 21.36  ? 298 TYR A C   1 
ATOM   2406  O  O   . TYR A 1 298 ? 25.007  4.322   5.781   1.00 23.00  ? 298 TYR A O   1 
ATOM   2407  C  CB  . TYR A 1 298 ? 21.731  3.596   6.516   1.00 22.69  ? 298 TYR A CB  1 
ATOM   2408  C  CG  . TYR A 1 298 ? 22.360  2.234   6.512   1.00 23.54  ? 298 TYR A CG  1 
ATOM   2409  C  CD1 . TYR A 1 298 ? 22.680  1.633   5.306   1.00 27.57  ? 298 TYR A CD1 1 
ATOM   2410  C  CD2 . TYR A 1 298 ? 22.546  1.524   7.693   1.00 28.26  ? 298 TYR A CD2 1 
ATOM   2411  C  CE1 . TYR A 1 298 ? 23.247  0.388   5.267   1.00 25.20  ? 298 TYR A CE1 1 
ATOM   2412  C  CE2 . TYR A 1 298 ? 23.097  0.250   7.676   1.00 26.70  ? 298 TYR A CE2 1 
ATOM   2413  C  CZ  . TYR A 1 298 ? 23.458  -0.294  6.464   1.00 28.39  ? 298 TYR A CZ  1 
ATOM   2414  O  OH  . TYR A 1 298 ? 24.001  -1.584  6.448   1.00 29.81  ? 298 TYR A OH  1 
ATOM   2415  N  N   . THR A 1 299 ? 23.471  4.588   4.143   1.00 22.34  ? 299 THR A N   1 
ATOM   2416  C  CA  . THR A 1 299 ? 24.481  4.424   3.115   1.00 22.65  ? 299 THR A CA  1 
ATOM   2417  C  C   . THR A 1 299 ? 25.514  5.543   3.181   1.00 21.72  ? 299 THR A C   1 
ATOM   2418  O  O   . THR A 1 299 ? 26.722  5.294   3.106   1.00 21.67  ? 299 THR A O   1 
ATOM   2419  C  CB  . THR A 1 299 ? 23.777  4.388   1.756   1.00 24.79  ? 299 THR A CB  1 
ATOM   2420  O  OG1 . THR A 1 299 ? 22.972  3.183   1.701   1.00 26.42  ? 299 THR A OG1 1 
ATOM   2421  C  CG2 . THR A 1 299 ? 24.764  4.402   0.636   1.00 26.43  ? 299 THR A CG2 1 
ATOM   2422  N  N   . PHE A 1 300 ? 25.067  6.762   3.429   1.00 21.14  ? 300 PHE A N   1 
ATOM   2423  C  CA  . PHE A 1 300 ? 26.013  7.899   3.449   1.00 22.78  ? 300 PHE A CA  1 
ATOM   2424  C  C   . PHE A 1 300 ? 26.908  7.953   4.690   1.00 19.59  ? 300 PHE A C   1 
ATOM   2425  O  O   . PHE A 1 300 ? 28.014  8.416   4.557   1.00 21.60  ? 300 PHE A O   1 
ATOM   2426  C  CB  . PHE A 1 300 ? 25.208  9.191   3.534   1.00 22.47  ? 300 PHE A CB  1 
ATOM   2427  C  CG  . PHE A 1 300 ? 24.395  9.522   2.315   1.00 23.55  ? 300 PHE A CG  1 
ATOM   2428  C  CD1 . PHE A 1 300 ? 24.447  8.728   1.191   1.00 20.83  ? 300 PHE A CD1 1 
ATOM   2429  C  CD2 . PHE A 1 300 ? 23.624  10.666  2.275   1.00 22.95  ? 300 PHE A CD2 1 
ATOM   2430  C  CE1 . PHE A 1 300 ? 23.724  9.066   0.069   1.00 22.71  ? 300 PHE A CE1 1 
ATOM   2431  C  CE2 . PHE A 1 300 ? 22.907  11.002  1.150   1.00 21.82  ? 300 PHE A CE2 1 
ATOM   2432  C  CZ  . PHE A 1 300 ? 22.960  10.196  0.050   1.00 22.73  ? 300 PHE A CZ  1 
ATOM   2433  N  N   . ALA A 1 301 ? 26.443  7.464   5.842   1.00 20.90  ? 301 ALA A N   1 
ATOM   2434  C  CA  . ALA A 1 301 ? 27.149  7.768   7.074   1.00 22.56  ? 301 ALA A CA  1 
ATOM   2435  C  C   . ALA A 1 301 ? 27.290  6.581   8.027   1.00 20.86  ? 301 ALA A C   1 
ATOM   2436  O  O   . ALA A 1 301 ? 27.619  6.806   9.212   1.00 21.71  ? 301 ALA A O   1 
ATOM   2437  C  CB  . ALA A 1 301 ? 26.428  8.911   7.819   1.00 23.15  ? 301 ALA A CB  1 
ATOM   2438  N  N   . LEU A 1 302 ? 27.029  5.351   7.577   1.00 20.44  ? 302 LEU A N   1 
ATOM   2439  C  CA  . LEU A 1 302 ? 27.405  4.223   8.439   1.00 21.81  ? 302 LEU A CA  1 
ATOM   2440  C  C   . LEU A 1 302 ? 28.920  4.248   8.651   1.00 21.66  ? 302 LEU A C   1 
ATOM   2441  O  O   . LEU A 1 302 ? 29.417  3.931   9.753   1.00 23.70  ? 302 LEU A O   1 
ATOM   2442  C  CB  . LEU A 1 302 ? 27.004  2.910   7.786   1.00 22.45  ? 302 LEU A CB  1 
ATOM   2443  C  CG  . LEU A 1 302 ? 27.177  1.663   8.668   1.00 24.93  ? 302 LEU A CG  1 
ATOM   2444  C  CD1 . LEU A 1 302 ? 26.192  1.710   9.782   1.00 24.03  ? 302 LEU A CD1 1 
ATOM   2445  C  CD2 . LEU A 1 302 ? 26.968  0.431   7.722   1.00 26.73  ? 302 LEU A CD2 1 
ATOM   2446  N  N   . GLU A 1 303 ? 29.657  4.654   7.607   1.00 23.40  ? 303 GLU A N   1 
ATOM   2447  C  CA  . GLU A 1 303 ? 31.106  4.851   7.676   1.00 20.03  ? 303 GLU A CA  1 
ATOM   2448  C  C   . GLU A 1 303 ? 31.493  6.231   7.152   1.00 21.05  ? 303 GLU A C   1 
ATOM   2449  O  O   . GLU A 1 303 ? 32.559  6.718   7.509   1.00 22.30  ? 303 GLU A O   1 
ATOM   2450  C  CB  . GLU A 1 303 ? 31.904  3.814   6.911   1.00 20.64  ? 303 GLU A CB  1 
ATOM   2451  C  CG  . GLU A 1 303 ? 31.558  2.387   7.325   1.00 20.55  ? 303 GLU A CG  1 
ATOM   2452  C  CD  . GLU A 1 303 ? 32.119  1.942   8.671   1.00 24.23  ? 303 GLU A CD  1 
ATOM   2453  O  OE1 . GLU A 1 303 ? 32.487  2.767   9.516   1.00 25.75  ? 303 GLU A OE1 1 
ATOM   2454  O  OE2 . GLU A 1 303 ? 32.168  0.688   8.877   1.00 21.99  ? 303 GLU A OE2 1 
ATOM   2455  N  N   . GLY A 1 304 ? 30.730  6.813   6.226   1.00 20.04  ? 304 GLY A N   1 
ATOM   2456  C  CA  . GLY A 1 304 ? 31.107  8.135   5.720   1.00 17.87  ? 304 GLY A CA  1 
ATOM   2457  C  C   . GLY A 1 304 ? 31.197  9.143   6.861   1.00 19.28  ? 304 GLY A C   1 
ATOM   2458  O  O   . GLY A 1 304 ? 30.342  9.177   7.747   1.00 22.18  ? 304 GLY A O   1 
ATOM   2459  N  N   . ILE A 1 305 ? 32.220  10.015  6.793   1.00 21.10  ? 305 ILE A N   1 
ATOM   2460  C  CA  . ILE A 1 305 ? 32.444  11.066  7.813   1.00 17.46  ? 305 ILE A CA  1 
ATOM   2461  C  C   . ILE A 1 305 ? 32.353  12.443  7.142   1.00 19.98  ? 305 ILE A C   1 
ATOM   2462  O  O   . ILE A 1 305 ? 33.032  12.683  6.154   1.00 20.70  ? 305 ILE A O   1 
ATOM   2463  C  CB  . ILE A 1 305 ? 33.813  10.833  8.501   1.00 19.80  ? 305 ILE A CB  1 
ATOM   2464  C  CG1 . ILE A 1 305 ? 33.746  9.490   9.280   1.00 23.15  ? 305 ILE A CG1 1 
ATOM   2465  C  CG2 . ILE A 1 305 ? 34.153  11.953  9.467   1.00 23.26  ? 305 ILE A CG2 1 
ATOM   2466  C  CD1 . ILE A 1 305 ? 32.846  9.576   10.462  1.00 21.35  ? 305 ILE A CD1 1 
ATOM   2467  N  N   . TRP A 1 306 ? 31.536  13.327  7.708   1.00 21.21  ? 306 TRP A N   1 
ATOM   2468  C  CA  . TRP A 1 306 ? 31.024  14.526  7.034   1.00 19.27  ? 306 TRP A CA  1 
ATOM   2469  C  C   . TRP A 1 306 ? 31.380  15.792  7.808   1.00 20.16  ? 306 TRP A C   1 
ATOM   2470  O  O   . TRP A 1 306 ? 31.701  15.781  9.018   1.00 23.21  ? 306 TRP A O   1 
ATOM   2471  C  CB  . TRP A 1 306 ? 29.490  14.410  6.915   1.00 22.20  ? 306 TRP A CB  1 
ATOM   2472  C  CG  . TRP A 1 306 ? 29.035  13.226  6.034   1.00 23.28  ? 306 TRP A CG  1 
ATOM   2473  C  CD1 . TRP A 1 306 ? 28.990  11.876  6.381   1.00 21.31  ? 306 TRP A CD1 1 
ATOM   2474  C  CD2 . TRP A 1 306 ? 28.597  13.319  4.686   1.00 21.51  ? 306 TRP A CD2 1 
ATOM   2475  N  NE1 . TRP A 1 306 ? 28.534  11.144  5.287   1.00 21.47  ? 306 TRP A NE1 1 
ATOM   2476  C  CE2 . TRP A 1 306 ? 28.297  12.001  4.232   1.00 24.03  ? 306 TRP A CE2 1 
ATOM   2477  C  CE3 . TRP A 1 306 ? 28.414  14.406  3.803   1.00 22.66  ? 306 TRP A CE3 1 
ATOM   2478  C  CZ2 . TRP A 1 306 ? 27.815  11.744  2.921   1.00 22.82  ? 306 TRP A CZ2 1 
ATOM   2479  C  CZ3 . TRP A 1 306 ? 27.925  14.155  2.506   1.00 20.74  ? 306 TRP A CZ3 1 
ATOM   2480  C  CH2 . TRP A 1 306 ? 27.674  12.820  2.066   1.00 22.83  ? 306 TRP A CH2 1 
ATOM   2481  N  N   . GLU A 1 307 ? 31.273  16.910  7.096   1.00 19.82  ? 307 GLU A N   1 
ATOM   2482  C  CA  . GLU A 1 307 ? 31.395  18.210  7.750   1.00 24.74  ? 307 GLU A CA  1 
ATOM   2483  C  C   . GLU A 1 307 ? 30.529  19.205  6.993   1.00 23.60  ? 307 GLU A C   1 
ATOM   2484  O  O   . GLU A 1 307 ? 30.125  18.966  5.852   1.00 22.37  ? 307 GLU A O   1 
ATOM   2485  C  CB  . GLU A 1 307 ? 32.852  18.683  7.796   1.00 23.66  ? 307 GLU A CB  1 
ATOM   2486  C  CG  . GLU A 1 307 ? 33.299  19.335  6.460   1.00 24.30  ? 307 GLU A CG  1 
ATOM   2487  C  CD  . GLU A 1 307 ? 34.778  19.632  6.390   1.00 29.10  ? 307 GLU A CD  1 
ATOM   2488  O  OE1 . GLU A 1 307 ? 35.504  19.353  7.385   1.00 28.05  ? 307 GLU A OE1 1 
ATOM   2489  O  OE2 . GLU A 1 307 ? 35.205  20.154  5.325   1.00 29.84  ? 307 GLU A OE2 1 
ATOM   2490  N  N   . ASP A 1 308 ? 30.249  20.343  7.639   1.00 22.65  ? 308 ASP A N   1 
ATOM   2491  C  CA  . ASP A 1 308 ? 29.671  21.491  6.948   1.00 24.98  ? 308 ASP A CA  1 
ATOM   2492  C  C   . ASP A 1 308 ? 30.712  22.188  6.077   1.00 28.94  ? 308 ASP A C   1 
ATOM   2493  O  O   . ASP A 1 308 ? 31.763  22.595  6.562   1.00 24.44  ? 308 ASP A O   1 
ATOM   2494  C  CB  . ASP A 1 308 ? 29.129  22.499  7.981   1.00 25.05  ? 308 ASP A CB  1 
ATOM   2495  C  CG  . ASP A 1 308 ? 28.029  21.887  8.863   1.00 33.60  ? 308 ASP A CG  1 
ATOM   2496  O  OD1 . ASP A 1 308 ? 27.348  20.946  8.381   1.00 30.70  ? 308 ASP A OD1 1 
ATOM   2497  O  OD2 . ASP A 1 308 ? 27.860  22.319  10.020  1.00 34.84  ? 308 ASP A OD2 1 
ATOM   2498  N  N   . LYS A 1 309 ? 30.414  22.351  4.803   1.00 25.54  ? 309 LYS A N   1 
ATOM   2499  C  CA  . LYS A 1 309 ? 31.312  22.990  3.853   1.00 24.86  ? 309 LYS A CA  1 
ATOM   2500  C  C   . LYS A 1 309 ? 31.111  24.495  3.878   1.00 27.64  ? 309 LYS A C   1 
ATOM   2501  O  O   . LYS A 1 309 ? 30.185  25.024  4.502   1.00 29.20  ? 309 LYS A O   1 
ATOM   2502  C  CB  . LYS A 1 309 ? 31.037  22.436  2.454   1.00 27.82  ? 309 LYS A CB  1 
ATOM   2503  C  CG  . LYS A 1 309 ? 31.395  20.950  2.333   1.00 26.76  ? 309 LYS A CG  1 
ATOM   2504  C  CD  . LYS A 1 309 ? 32.944  20.784  2.485   1.00 30.54  ? 309 LYS A CD  1 
ATOM   2505  C  CE  . LYS A 1 309 ? 33.414  19.327  2.327   1.00 30.02  ? 309 LYS A CE  1 
ATOM   2506  N  NZ  . LYS A 1 309 ? 34.902  19.229  2.502   1.00 27.85  ? 309 LYS A NZ  1 
ATOM   2507  N  N   . PRO A 1 310 ? 31.927  25.238  3.119   1.00 30.25  ? 310 PRO A N   1 
ATOM   2508  C  CA  . PRO A 1 310 ? 31.819  26.705  3.139   1.00 29.95  ? 310 PRO A CA  1 
ATOM   2509  C  C   . PRO A 1 310 ? 30.488  27.281  2.643   1.00 30.42  ? 310 PRO A C   1 
ATOM   2510  O  O   . PRO A 1 310 ? 30.142  28.435  3.002   1.00 30.29  ? 310 PRO A O   1 
ATOM   2511  C  CB  . PRO A 1 310 ? 32.979  27.142  2.235   1.00 31.88  ? 310 PRO A CB  1 
ATOM   2512  C  CG  . PRO A 1 310 ? 33.996  26.080  2.482   1.00 31.66  ? 310 PRO A CG  1 
ATOM   2513  C  CD  . PRO A 1 310 ? 33.219  24.790  2.552   1.00 29.33  ? 310 PRO A CD  1 
ATOM   2514  N  N   . ASP A 1 311 ? 29.750  26.555  1.786   1.00 26.72  ? 311 ASP A N   1 
ATOM   2515  C  CA  . ASP A 1 311 ? 28.433  27.001  1.340   1.00 27.61  ? 311 ASP A CA  1 
ATOM   2516  C  C   . ASP A 1 311 ? 27.289  26.467  2.212   1.00 25.45  ? 311 ASP A C   1 
ATOM   2517  O  O   . ASP A 1 311 ? 26.117  26.612  1.836   1.00 28.25  ? 311 ASP A O   1 
ATOM   2518  C  CB  . ASP A 1 311 ? 28.198  26.612  -0.102  1.00 28.39  ? 311 ASP A CB  1 
ATOM   2519  C  CG  . ASP A 1 311 ? 28.025  25.101  -0.280  1.00 26.77  ? 311 ASP A CG  1 
ATOM   2520  O  OD1 . ASP A 1 311 ? 28.404  24.388  0.640   1.00 27.84  ? 311 ASP A OD1 1 
ATOM   2521  O  OD2 . ASP A 1 311 ? 27.601  24.674  -1.388  1.00 34.20  ? 311 ASP A OD2 1 
ATOM   2522  N  N   . GLY A 1 312 ? 27.590  25.902  3.354   1.00 27.57  ? 312 GLY A N   1 
ATOM   2523  C  CA  . GLY A 1 312 ? 26.567  25.340  4.230   1.00 24.49  ? 312 GLY A CA  1 
ATOM   2524  C  C   . GLY A 1 312 ? 26.146  23.936  3.886   1.00 27.99  ? 312 GLY A C   1 
ATOM   2525  O  O   . GLY A 1 312 ? 25.377  23.350  4.653   1.00 27.80  ? 312 GLY A O   1 
ATOM   2526  N  N   . SER A 1 313 ? 26.644  23.383  2.795   1.00 23.55  ? 313 SER A N   1 
ATOM   2527  C  CA  . SER A 1 313 ? 26.239  22.031  2.369   1.00 26.38  ? 313 SER A CA  1 
ATOM   2528  C  C   . SER A 1 313 ? 27.009  20.978  3.121   1.00 27.20  ? 313 SER A C   1 
ATOM   2529  O  O   . SER A 1 313 ? 28.058  21.238  3.734   1.00 22.13  ? 313 SER A O   1 
ATOM   2530  C  CB  . SER A 1 313 ? 26.442  21.841  0.865   1.00 26.28  ? 313 SER A CB  1 
ATOM   2531  O  OG  . SER A 1 313 ? 27.830  21.848  0.547   1.00 26.96  ? 313 SER A OG  1 
ATOM   2532  N  N   . TRP A 1 314 ? 26.547  19.722  2.977   1.00 23.06  ? 314 TRP A N   1 
ATOM   2533  C  CA  . TRP A 1 314 ? 27.170  18.608  3.676   1.00 25.04  ? 314 TRP A CA  1 
ATOM   2534  C  C   . TRP A 1 314 ? 28.163  17.950  2.713   1.00 22.02  ? 314 TRP A C   1 
ATOM   2535  O  O   . TRP A 1 314 ? 27.842  17.741  1.513   1.00 26.12  ? 314 TRP A O   1 
ATOM   2536  C  CB  . TRP A 1 314 ? 26.129  17.569  4.045   1.00 26.19  ? 314 TRP A CB  1 
ATOM   2537  C  CG  . TRP A 1 314 ? 26.393  16.950  5.374   1.00 22.15  ? 314 TRP A CG  1 
ATOM   2538  C  CD1 . TRP A 1 314 ? 27.162  17.458  6.406   1.00 23.98  ? 314 TRP A CD1 1 
ATOM   2539  C  CD2 . TRP A 1 314 ? 25.841  15.706  5.853   1.00 25.15  ? 314 TRP A CD2 1 
ATOM   2540  N  NE1 . TRP A 1 314 ? 27.052  16.639  7.524   1.00 23.06  ? 314 TRP A NE1 1 
ATOM   2541  C  CE2 . TRP A 1 314 ? 26.292  15.533  7.180   1.00 26.45  ? 314 TRP A CE2 1 
ATOM   2542  C  CE3 . TRP A 1 314 ? 25.045  14.713  5.254   1.00 27.74  ? 314 TRP A CE3 1 
ATOM   2543  C  CZ2 . TRP A 1 314 ? 25.968  14.414  7.918   1.00 26.83  ? 314 TRP A CZ2 1 
ATOM   2544  C  CZ3 . TRP A 1 314 ? 24.721  13.573  6.010   1.00 26.11  ? 314 TRP A CZ3 1 
ATOM   2545  C  CH2 . TRP A 1 314 ? 25.184  13.443  7.300   1.00 27.74  ? 314 TRP A CH2 1 
ATOM   2546  N  N   . GLY A 1 315 ? 29.418  17.769  3.158   1.00 23.71  ? 315 GLY A N   1 
ATOM   2547  C  CA  . GLY A 1 315 ? 30.425  17.101  2.351   1.00 25.40  ? 315 GLY A CA  1 
ATOM   2548  C  C   . GLY A 1 315 ? 31.414  16.305  3.195   1.00 21.75  ? 315 GLY A C   1 
ATOM   2549  O  O   . GLY A 1 315 ? 31.300  16.241  4.418   1.00 21.86  ? 315 GLY A O   1 
ATOM   2550  N  N   . GLY A 1 316 ? 32.340  15.630  2.520   1.00 23.41  ? 316 GLY A N   1 
ATOM   2551  C  CA  . GLY A 1 316 ? 33.389  14.895  3.235   1.00 25.42  ? 316 GLY A CA  1 
ATOM   2552  C  C   . GLY A 1 316 ? 34.200  15.759  4.203   1.00 24.24  ? 316 GLY A C   1 
ATOM   2553  O  O   . GLY A 1 316 ? 34.561  16.907  3.915   1.00 22.76  ? 316 GLY A O   1 
ATOM   2554  N  N   . ARG A 1 317 ? 34.494  15.195  5.369   1.00 23.22  ? 317 ARG A N   1 
ATOM   2555  C  CA  . ARG A 1 317 ? 35.205  15.944  6.413   1.00 22.93  ? 317 ARG A CA  1 
ATOM   2556  C  C   . ARG A 1 317 ? 36.607  16.225  5.933   1.00 24.76  ? 317 ARG A C   1 
ATOM   2557  O  O   . ARG A 1 317 ? 37.193  15.405  5.240   1.00 24.97  ? 317 ARG A O   1 
ATOM   2558  C  CB  . ARG A 1 317 ? 35.249  15.152  7.714   1.00 24.64  ? 317 ARG A CB  1 
ATOM   2559  C  CG  . ARG A 1 317 ? 35.927  15.960  8.817   1.00 21.63  ? 317 ARG A CG  1 
ATOM   2560  C  CD  . ARG A 1 317 ? 35.748  15.284  10.178  1.00 24.61  ? 317 ARG A CD  1 
ATOM   2561  N  NE  . ARG A 1 317 ? 36.566  16.014  11.134  1.00 25.84  ? 317 ARG A NE  1 
ATOM   2562  C  CZ  . ARG A 1 317 ? 36.471  15.879  12.443  1.00 26.34  ? 317 ARG A CZ  1 
ATOM   2563  N  NH1 . ARG A 1 317 ? 35.602  15.025  12.972  1.00 24.92  ? 317 ARG A NH1 1 
ATOM   2564  N  NH2 . ARG A 1 317 ? 37.264  16.630  13.241  1.00 26.33  ? 317 ARG A NH2 1 
ATOM   2565  N  N   . THR A 1 318 ? 37.117  17.426  6.213   1.00 24.28  ? 318 THR A N   1 
ATOM   2566  C  CA  . THR A 1 318 ? 38.441  17.803  5.724   1.00 24.20  ? 318 THR A CA  1 
ATOM   2567  C  C   . THR A 1 318 ? 39.517  16.981  6.449   1.00 25.16  ? 318 THR A C   1 
ATOM   2568  O  O   . THR A 1 318 ? 39.506  16.859  7.686   1.00 24.97  ? 318 THR A O   1 
ATOM   2569  C  CB  . THR A 1 318 ? 38.677  19.324  5.892   1.00 27.89  ? 318 THR A CB  1 
ATOM   2570  O  OG1 . THR A 1 318 ? 37.812  20.066  5.007   1.00 27.68  ? 318 THR A OG1 1 
ATOM   2571  C  CG2 . THR A 1 318 ? 40.074  19.719  5.435   1.00 27.27  ? 318 THR A CG2 1 
ATOM   2572  N  N   . LEU A 1 319 ? 40.471  16.463  5.681   1.00 25.97  ? 319 LEU A N   1 
ATOM   2573  C  CA  . LEU A 1 319 ? 41.586  15.719  6.259   1.00 28.73  ? 319 LEU A CA  1 
ATOM   2574  C  C   . LEU A 1 319 ? 42.485  16.669  7.065   1.00 29.70  ? 319 LEU A C   1 
ATOM   2575  O  O   . LEU A 1 319 ? 42.712  17.820  6.665   1.00 29.11  ? 319 LEU A O   1 
ATOM   2576  C  CB  . LEU A 1 319 ? 42.359  15.018  5.143   1.00 27.71  ? 319 LEU A CB  1 
ATOM   2577  C  CG  . LEU A 1 319 ? 41.472  14.207  4.173   1.00 24.15  ? 319 LEU A CG  1 
ATOM   2578  C  CD1 . LEU A 1 319 ? 42.297  13.858  2.987   1.00 27.43  ? 319 LEU A CD1 1 
ATOM   2579  C  CD2 . LEU A 1 319 ? 41.062  12.930  4.888   1.00 27.49  ? 319 LEU A CD2 1 
ATOM   2580  N  N   . PRO A 1 320 ? 42.944  16.249  8.239   1.00 27.91  ? 320 PRO A N   1 
ATOM   2581  C  CA  . PRO A 1 320 ? 43.647  17.207  9.126   1.00 32.10  ? 320 PRO A CA  1 
ATOM   2582  C  C   . PRO A 1 320 ? 44.895  17.781  8.498   1.00 33.84  ? 320 PRO A C   1 
ATOM   2583  O  O   . PRO A 1 320 ? 45.188  18.968  8.681   1.00 31.86  ? 320 PRO A O   1 
ATOM   2584  C  CB  . PRO A 1 320 ? 43.980  16.371  10.380  1.00 34.34  ? 320 PRO A CB  1 
ATOM   2585  C  CG  . PRO A 1 320 ? 43.021  15.164  10.363  1.00 29.20  ? 320 PRO A CG  1 
ATOM   2586  C  CD  . PRO A 1 320 ? 42.646  14.939  8.888   1.00 26.01  ? 320 PRO A CD  1 
ATOM   2587  N  N   . TRP A 1 321 ? 45.620  16.991  7.701   1.00 30.65  ? 321 TRP A N   1 
ATOM   2588  C  CA  . TRP A 1 321 ? 46.803  17.525  7.053   1.00 31.07  ? 321 TRP A CA  1 
ATOM   2589  C  C   . TRP A 1 321 ? 46.465  18.526  5.948   1.00 32.23  ? 321 TRP A C   1 
ATOM   2590  O  O   . TRP A 1 321 ? 47.370  19.244  5.517   1.00 38.34  ? 321 TRP A O   1 
ATOM   2591  C  CB  . TRP A 1 321 ? 47.695  16.407  6.491   1.00 33.32  ? 321 TRP A CB  1 
ATOM   2592  C  CG  . TRP A 1 321 ? 46.997  15.420  5.548   1.00 31.19  ? 321 TRP A CG  1 
ATOM   2593  C  CD1 . TRP A 1 321 ? 46.896  15.492  4.182   1.00 33.74  ? 321 TRP A CD1 1 
ATOM   2594  C  CD2 . TRP A 1 321 ? 46.324  14.230  5.933   1.00 27.94  ? 321 TRP A CD2 1 
ATOM   2595  N  NE1 . TRP A 1 321 ? 46.192  14.391  3.697   1.00 31.32  ? 321 TRP A NE1 1 
ATOM   2596  C  CE2 . TRP A 1 321 ? 45.841  13.609  4.755   1.00 25.57  ? 321 TRP A CE2 1 
ATOM   2597  C  CE3 . TRP A 1 321 ? 46.093  13.619  7.167   1.00 29.17  ? 321 TRP A CE3 1 
ATOM   2598  C  CZ2 . TRP A 1 321 ? 45.124  12.411  4.783   1.00 25.88  ? 321 TRP A CZ2 1 
ATOM   2599  C  CZ3 . TRP A 1 321 ? 45.383  12.445  7.200   1.00 27.26  ? 321 TRP A CZ3 1 
ATOM   2600  C  CH2 . TRP A 1 321 ? 44.904  11.853  6.025   1.00 28.17  ? 321 TRP A CH2 1 
ATOM   2601  N  N   . ASP A 1 322 ? 45.199  18.641  5.522   1.00 30.41  ? 322 ASP A N   1 
ATOM   2602  C  CA  . ASP A 1 322 ? 44.769  19.703  4.580   1.00 35.26  ? 322 ASP A CA  1 
ATOM   2603  C  C   . ASP A 1 322 ? 44.337  20.980  5.283   1.00 36.50  ? 322 ASP A C   1 
ATOM   2604  O  O   . ASP A 1 322 ? 43.965  21.945  4.607   1.00 37.65  ? 322 ASP A O   1 
ATOM   2605  C  CB  . ASP A 1 322 ? 43.594  19.245  3.701   1.00 33.22  ? 322 ASP A CB  1 
ATOM   2606  C  CG  . ASP A 1 322 ? 44.012  18.224  2.667   1.00 35.57  ? 322 ASP A CG  1 
ATOM   2607  O  OD1 . ASP A 1 322 ? 45.198  18.216  2.308   1.00 42.49  ? 322 ASP A OD1 1 
ATOM   2608  O  OD2 . ASP A 1 322 ? 43.161  17.449  2.210   1.00 34.62  ? 322 ASP A OD2 1 
ATOM   2609  N  N   . LYS A 1 323 ? 44.361  20.958  6.608   1.00 32.72  ? 323 LYS A N   1 
ATOM   2610  C  CA  . LYS A 1 323 ? 43.959  21.988  7.546   1.00 35.52  ? 323 LYS A CA  1 
ATOM   2611  C  C   . LYS A 1 323 ? 45.145  22.447  8.359   1.00 36.14  ? 323 LYS A C   1 
ATOM   2612  O  O   . LYS A 1 323 ? 44.946  23.049  9.414   1.00 38.68  ? 323 LYS A O   1 
ATOM   2613  C  CB  . LYS A 1 323 ? 42.954  21.421  8.563   1.00 40.71  ? 323 LYS A CB  1 
ATOM   2614  C  CG  . LYS A 1 323 ? 41.574  21.152  8.159   1.00 42.18  ? 323 LYS A CG  1 
ATOM   2615  C  CD  . LYS A 1 323 ? 40.684  21.535  9.309   1.00 41.14  ? 323 LYS A CD  1 
ATOM   2616  C  CE  . LYS A 1 323 ? 40.171  20.351  10.076  1.00 41.56  ? 323 LYS A CE  1 
ATOM   2617  N  NZ  . LYS A 1 323 ? 38.712  20.461  10.414  1.00 39.25  ? 323 LYS A NZ  1 
ATOM   2618  N  N   . GLY A 1 324 ? 46.354  22.010  8.001   1.00 32.59  ? 324 GLY A N   1 
ATOM   2619  C  CA  . GLY A 1 324 ? 47.543  22.338  8.762   1.00 35.49  ? 324 GLY A CA  1 
ATOM   2620  C  C   . GLY A 1 324 ? 47.755  21.585  10.064  1.00 36.52  ? 324 GLY A C   1 
ATOM   2621  O  O   . GLY A 1 324 ? 48.575  22.030  10.877  1.00 39.72  ? 324 GLY A O   1 
ATOM   2622  N  N   . ILE A 1 325 ? 47.069  20.455  10.296  1.00 34.34  ? 325 ILE A N   1 
ATOM   2623  C  CA  . ILE A 1 325 ? 47.183  19.699  11.553  1.00 35.74  ? 325 ILE A CA  1 
ATOM   2624  C  C   . ILE A 1 325 ? 48.099  18.505  11.309  1.00 39.49  ? 325 ILE A C   1 
ATOM   2625  O  O   . ILE A 1 325 ? 47.755  17.619  10.518  1.00 37.94  ? 325 ILE A O   1 
ATOM   2626  C  CB  . ILE A 1 325 ? 45.802  19.231  12.053  1.00 34.65  ? 325 ILE A CB  1 
ATOM   2627  C  CG1 . ILE A 1 325 ? 44.892  20.434  12.328  1.00 37.19  ? 325 ILE A CG1 1 
ATOM   2628  C  CG2 . ILE A 1 325 ? 45.907  18.370  13.321  1.00 32.55  ? 325 ILE A CG2 1 
ATOM   2629  C  CD1 . ILE A 1 325 ? 43.406  20.053  12.453  1.00 39.66  ? 325 ILE A CD1 1 
ATOM   2630  N  N   . GLU A 1 326 ? 49.253  18.453  11.985  1.00 39.19  ? 326 GLU A N   1 
ATOM   2631  C  CA  . GLU A 1 326 ? 50.202  17.371  11.726  1.00 41.40  ? 326 GLU A CA  1 
ATOM   2632  C  C   . GLU A 1 326 ? 49.841  16.144  12.572  1.00 39.34  ? 326 GLU A C   1 
ATOM   2633  O  O   . GLU A 1 326 ? 49.189  16.260  13.615  1.00 36.22  ? 326 GLU A O   1 
ATOM   2634  C  CB  . GLU A 1 326 ? 51.633  17.818  12.015  1.00 47.45  ? 326 GLU A CB  1 
ATOM   2635  C  CG  . GLU A 1 326 ? 52.276  18.599  10.853  1.00 51.73  ? 326 GLU A CG  1 
ATOM   2636  C  CD  . GLU A 1 326 ? 53.786  18.758  11.004  1.00 60.34  ? 326 GLU A CD  1 
ATOM   2637  O  OE1 . GLU A 1 326 ? 54.272  18.603  12.140  1.00 63.69  ? 326 GLU A OE1 1 
ATOM   2638  O  OE2 . GLU A 1 326 ? 54.481  19.061  9.998   1.00 64.14  ? 326 GLU A OE2 1 
ATOM   2639  N  N   . ILE A 1 327 ? 50.201  14.956  12.084  1.00 38.16  ? 327 ILE A N   1 
ATOM   2640  C  CA  . ILE A 1 327 ? 49.943  13.700  12.812  1.00 31.35  ? 327 ILE A CA  1 
ATOM   2641  C  C   . ILE A 1 327 ? 51.253  12.922  12.823  1.00 34.15  ? 327 ILE A C   1 
ATOM   2642  O  O   . ILE A 1 327 ? 51.500  12.068  11.970  1.00 38.18  ? 327 ILE A O   1 
ATOM   2643  C  CB  . ILE A 1 327 ? 48.817  12.859  12.203  1.00 35.19  ? 327 ILE A CB  1 
ATOM   2644  C  CG1 . ILE A 1 327 ? 47.621  13.702  11.809  1.00 37.16  ? 327 ILE A CG1 1 
ATOM   2645  C  CG2 . ILE A 1 327 ? 48.393  11.776  13.165  1.00 31.13  ? 327 ILE A CG2 1 
ATOM   2646  C  CD1 . ILE A 1 327 ? 46.386  12.848  11.346  1.00 39.32  ? 327 ILE A CD1 1 
ATOM   2647  N  N   . ASN A 1 328 ? 52.081  13.191  13.792  1.00 34.45  ? 328 ASN A N   1 
ATOM   2648  C  CA  . ASN A 1 328 ? 53.438  12.701  13.750  1.00 36.37  ? 328 ASN A CA  1 
ATOM   2649  C  C   . ASN A 1 328 ? 53.771  11.802  14.903  1.00 36.37  ? 328 ASN A C   1 
ATOM   2650  O  O   . ASN A 1 328 ? 54.941  11.425  15.046  1.00 39.32  ? 328 ASN A O   1 
ATOM   2651  C  CB  . ASN A 1 328 ? 54.428  13.872  13.720  1.00 38.39  ? 328 ASN A CB  1 
ATOM   2652  C  CG  . ASN A 1 328 ? 54.351  14.651  12.434  1.00 47.73  ? 328 ASN A CG  1 
ATOM   2653  O  OD1 . ASN A 1 328 ? 54.564  15.863  12.414  1.00 50.36  ? 328 ASN A OD1 1 
ATOM   2654  N  ND2 . ASN A 1 328 ? 54.140  13.935  11.326  1.00 51.02  ? 328 ASN A ND2 1 
ATOM   2655  N  N   . ASP A 1 329 ? 52.800  11.501  15.761  1.00 31.98  ? 329 ASP A N   1 
ATOM   2656  C  CA  . ASP A 1 329 ? 53.074  10.709  16.942  1.00 29.15  ? 329 ASP A CA  1 
ATOM   2657  C  C   . ASP A 1 329 ? 51.805  10.011  17.389  1.00 28.15  ? 329 ASP A C   1 
ATOM   2658  O  O   . ASP A 1 329 ? 50.674  10.389  17.015  1.00 28.15  ? 329 ASP A O   1 
ATOM   2659  C  CB  . ASP A 1 329 ? 53.652  11.548  18.091  1.00 34.66  ? 329 ASP A CB  1 
ATOM   2660  C  CG  . ASP A 1 329 ? 52.640  12.587  18.623  1.00 37.43  ? 329 ASP A CG  1 
ATOM   2661  O  OD1 . ASP A 1 329 ? 52.561  13.724  18.061  1.00 44.21  ? 329 ASP A OD1 1 
ATOM   2662  O  OD2 . ASP A 1 329 ? 51.867  12.265  19.543  1.00 36.93  ? 329 ASP A OD2 1 
ATOM   2663  N  N   . ARG A 1 330 ? 52.031  8.956   18.176  1.00 27.57  ? 330 ARG A N   1 
ATOM   2664  C  CA  . ARG A 1 330 ? 50.949  8.093   18.635  1.00 27.08  ? 330 ARG A CA  1 
ATOM   2665  C  C   . ARG A 1 330 ? 49.871  8.869   19.382  1.00 26.66  ? 330 ARG A C   1 
ATOM   2666  O  O   . ARG A 1 330 ? 48.673  8.706   19.099  1.00 24.02  ? 330 ARG A O   1 
ATOM   2667  C  CB  . ARG A 1 330 ? 51.516  6.974   19.519  1.00 25.67  ? 330 ARG A CB  1 
ATOM   2668  C  CG  . ARG A 1 330 ? 50.453  6.000   19.964  1.00 27.70  ? 330 ARG A CG  1 
ATOM   2669  C  CD  . ARG A 1 330 ? 50.979  5.067   21.066  1.00 27.84  ? 330 ARG A CD  1 
ATOM   2670  N  NE  . ARG A 1 330 ? 52.003  4.154   20.578  1.00 28.65  ? 330 ARG A NE  1 
ATOM   2671  C  CZ  . ARG A 1 330 ? 52.420  3.065   21.220  1.00 31.10  ? 330 ARG A CZ  1 
ATOM   2672  N  NH1 . ARG A 1 330 ? 51.869  2.676   22.373  1.00 25.73  ? 330 ARG A NH1 1 
ATOM   2673  N  NH2 . ARG A 1 330 ? 53.450  2.377   20.723  1.00 30.86  ? 330 ARG A NH2 1 
ATOM   2674  N  N   . ASP A 1 331 ? 50.261  9.681   20.387  1.00 28.31  ? 331 ASP A N   1 
ATOM   2675  C  CA  . ASP A 1 331 ? 49.231  10.320  21.227  1.00 25.86  ? 331 ASP A CA  1 
ATOM   2676  C  C   . ASP A 1 331 ? 48.353  11.275  20.421  1.00 26.70  ? 331 ASP A C   1 
ATOM   2677  O  O   . ASP A 1 331 ? 47.119  11.279  20.563  1.00 26.42  ? 331 ASP A O   1 
ATOM   2678  C  CB  . ASP A 1 331 ? 49.879  11.062  22.380  1.00 32.82  ? 331 ASP A CB  1 
ATOM   2679  C  CG  . ASP A 1 331 ? 50.536  10.120  23.364  1.00 36.13  ? 331 ASP A CG  1 
ATOM   2680  O  OD1 . ASP A 1 331 ? 50.451  8.890   23.170  1.00 32.23  ? 331 ASP A OD1 1 
ATOM   2681  O  OD2 . ASP A 1 331 ? 51.224  10.616  24.276  1.00 40.90  ? 331 ASP A OD2 1 
ATOM   2682  N  N   . THR A 1 332 ? 48.971  12.053  19.534  1.00 26.00  ? 332 THR A N   1 
ATOM   2683  C  CA  . THR A 1 332 ? 48.210  12.948  18.649  1.00 26.16  ? 332 THR A CA  1 
ATOM   2684  C  C   . THR A 1 332 ? 47.297  12.147  17.723  1.00 23.80  ? 332 THR A C   1 
ATOM   2685  O  O   . THR A 1 332 ? 46.109  12.473  17.550  1.00 23.54  ? 332 THR A O   1 
ATOM   2686  C  CB  . THR A 1 332 ? 49.178  13.833  17.825  1.00 28.44  ? 332 THR A CB  1 
ATOM   2687  O  OG1 . THR A 1 332 ? 50.095  14.547  18.682  1.00 29.57  ? 332 THR A OG1 1 
ATOM   2688  C  CG2 . THR A 1 332 ? 48.418  14.886  17.072  1.00 28.74  ? 332 THR A CG2 1 
ATOM   2689  N  N   . ALA A 1 333 ? 47.839  11.075  17.111  1.00 23.93  ? 333 ALA A N   1 
ATOM   2690  C  CA  . ALA A 1 333 ? 47.042  10.203  16.238  1.00 24.80  ? 333 ALA A CA  1 
ATOM   2691  C  C   . ALA A 1 333 ? 45.857  9.594   16.992  1.00 21.54  ? 333 ALA A C   1 
ATOM   2692  O  O   . ALA A 1 333 ? 44.726  9.600   16.489  1.00 22.73  ? 333 ALA A O   1 
ATOM   2693  C  CB  . ALA A 1 333 ? 47.929  9.086   15.661  1.00 23.95  ? 333 ALA A CB  1 
ATOM   2694  N  N   . VAL A 1 334 ? 46.078  9.148   18.241  1.00 22.92  ? 334 VAL A N   1 
ATOM   2695  C  CA  . VAL A 1 334 ? 44.987  8.511   18.985  1.00 21.24  ? 334 VAL A CA  1 
ATOM   2696  C  C   . VAL A 1 334 ? 43.870  9.493   19.215  1.00 23.16  ? 334 VAL A C   1 
ATOM   2697  O  O   . VAL A 1 334 ? 42.697  9.203   18.930  1.00 23.57  ? 334 VAL A O   1 
ATOM   2698  C  CB  . VAL A 1 334 ? 45.507  7.872   20.288  1.00 21.76  ? 334 VAL A CB  1 
ATOM   2699  C  CG1 . VAL A 1 334 ? 44.358  7.578   21.339  1.00 22.19  ? 334 VAL A CG1 1 
ATOM   2700  C  CG2 . VAL A 1 334 ? 46.367  6.616   19.934  1.00 19.35  ? 334 VAL A CG2 1 
ATOM   2701  N  N   . ARG A 1 335 ? 44.215  10.714  19.676  1.00 23.97  ? 335 ARG A N   1 
ATOM   2702  C  CA  . ARG A 1 335 ? 43.169  11.673  19.983  1.00 23.99  ? 335 ARG A CA  1 
ATOM   2703  C  C   . ARG A 1 335 ? 42.427  12.099  18.729  1.00 24.13  ? 335 ARG A C   1 
ATOM   2704  O  O   . ARG A 1 335 ? 41.183  12.136  18.729  1.00 22.83  ? 335 ARG A O   1 
ATOM   2705  C  CB  . ARG A 1 335 ? 43.750  12.867  20.713  1.00 26.63  ? 335 ARG A CB  1 
ATOM   2706  C  CG  . ARG A 1 335 ? 42.678  13.609  21.508  1.00 23.65  ? 335 ARG A CG  1 
ATOM   2707  C  CD  . ARG A 1 335 ? 43.278  14.823  22.245  1.00 27.98  ? 335 ARG A CD  1 
ATOM   2708  N  NE  . ARG A 1 335 ? 42.299  15.439  23.133  1.00 25.95  ? 335 ARG A NE  1 
ATOM   2709  C  CZ  . ARG A 1 335 ? 41.842  14.938  24.287  1.00 25.87  ? 335 ARG A CZ  1 
ATOM   2710  N  NH1 . ARG A 1 335 ? 42.290  13.794  24.792  1.00 25.28  ? 335 ARG A NH1 1 
ATOM   2711  N  NH2 . ARG A 1 335 ? 40.989  15.686  25.002  1.00 28.79  ? 335 ARG A NH2 1 
ATOM   2712  N  N   . LEU A 1 336 ? 43.168  12.381  17.630  1.00 23.20  ? 336 LEU A N   1 
ATOM   2713  C  CA  . LEU A 1 336 ? 42.503  12.746  16.377  1.00 23.51  ? 336 LEU A CA  1 
ATOM   2714  C  C   . LEU A 1 336 ? 41.637  11.612  15.854  1.00 23.00  ? 336 LEU A C   1 
ATOM   2715  O  O   . LEU A 1 336 ? 40.536  11.865  15.347  1.00 22.52  ? 336 LEU A O   1 
ATOM   2716  C  CB  . LEU A 1 336 ? 43.488  13.145  15.265  1.00 25.85  ? 336 LEU A CB  1 
ATOM   2717  C  CG  . LEU A 1 336 ? 44.150  14.484  15.485  1.00 31.55  ? 336 LEU A CG  1 
ATOM   2718  C  CD1 . LEU A 1 336 ? 45.483  14.576  14.670  1.00 33.54  ? 336 LEU A CD1 1 
ATOM   2719  C  CD2 . LEU A 1 336 ? 43.172  15.574  15.078  1.00 30.59  ? 336 LEU A CD2 1 
ATOM   2720  N  N   . TYR A 1 337 ? 42.102  10.372  16.002  1.00 20.52  ? 337 TYR A N   1 
ATOM   2721  C  CA  . TYR A 1 337 ? 41.333  9.200   15.546  1.00 22.12  ? 337 TYR A CA  1 
ATOM   2722  C  C   . TYR A 1 337 ? 40.039  9.037   16.348  1.00 24.49  ? 337 TYR A C   1 
ATOM   2723  O  O   . TYR A 1 337 ? 38.962  8.840   15.763  1.00 21.77  ? 337 TYR A O   1 
ATOM   2724  C  CB  . TYR A 1 337 ? 42.221  7.974   15.665  1.00 21.39  ? 337 TYR A CB  1 
ATOM   2725  C  CG  . TYR A 1 337 ? 41.644  6.691   15.042  1.00 22.26  ? 337 TYR A CG  1 
ATOM   2726  C  CD1 . TYR A 1 337 ? 41.091  6.688   13.775  1.00 23.49  ? 337 TYR A CD1 1 
ATOM   2727  C  CD2 . TYR A 1 337 ? 41.745  5.519   15.714  1.00 21.62  ? 337 TYR A CD2 1 
ATOM   2728  C  CE1 . TYR A 1 337 ? 40.636  5.520   13.187  1.00 25.72  ? 337 TYR A CE1 1 
ATOM   2729  C  CE2 . TYR A 1 337 ? 41.259  4.330   15.176  1.00 21.83  ? 337 TYR A CE2 1 
ATOM   2730  C  CZ  . TYR A 1 337 ? 40.706  4.342   13.904  1.00 23.24  ? 337 TYR A CZ  1 
ATOM   2731  O  OH  . TYR A 1 337 ? 40.271  3.130   13.366  1.00 23.20  ? 337 TYR A OH  1 
ATOM   2732  N  N   . ALA A 1 338 ? 40.120  9.177   17.686  1.00 22.34  ? 338 ALA A N   1 
ATOM   2733  C  CA  . ALA A 1 338 ? 38.906  9.187   18.515  1.00 22.83  ? 338 ALA A CA  1 
ATOM   2734  C  C   . ALA A 1 338 ? 37.940  10.271  18.083  1.00 25.27  ? 338 ALA A C   1 
ATOM   2735  O  O   . ALA A 1 338 ? 36.733  10.021  17.878  1.00 20.89  ? 338 ALA A O   1 
ATOM   2736  C  CB  . ALA A 1 338 ? 39.282  9.357   19.986  1.00 23.84  ? 338 ALA A CB  1 
ATOM   2737  N  N   . ASP A 1 339 ? 38.458  11.496  17.921  1.00 23.00  ? 339 ASP A N   1 
ATOM   2738  C  CA  . ASP A 1 339 ? 37.596  12.608  17.518  1.00 26.47  ? 339 ASP A CA  1 
ATOM   2739  C  C   . ASP A 1 339 ? 36.925  12.343  16.165  1.00 24.02  ? 339 ASP A C   1 
ATOM   2740  O  O   . ASP A 1 339 ? 35.719  12.615  15.999  1.00 23.84  ? 339 ASP A O   1 
ATOM   2741  C  CB  . ASP A 1 339 ? 38.402  13.906  17.471  1.00 21.90  ? 339 ASP A CB  1 
ATOM   2742  C  CG  . ASP A 1 339 ? 37.637  15.009  16.822  1.00 30.52  ? 339 ASP A CG  1 
ATOM   2743  O  OD1 . ASP A 1 339 ? 36.783  15.615  17.475  1.00 25.92  ? 339 ASP A OD1 1 
ATOM   2744  O  OD2 . ASP A 1 339 ? 37.843  15.282  15.631  1.00 28.12  ? 339 ASP A OD2 1 
ATOM   2745  N  N   . TRP A 1 340 ? 37.694  11.812  15.195  1.00 20.50  ? 340 TRP A N   1 
ATOM   2746  C  CA  . TRP A 1 340 ? 37.148  11.540  13.867  1.00 22.80  ? 340 TRP A CA  1 
ATOM   2747  C  C   . TRP A 1 340 ? 35.971  10.592  13.962  1.00 20.07  ? 340 TRP A C   1 
ATOM   2748  O  O   . TRP A 1 340 ? 34.859  10.888  13.493  1.00 20.34  ? 340 TRP A O   1 
ATOM   2749  C  CB  . TRP A 1 340 ? 38.241  10.942  12.999  1.00 22.07  ? 340 TRP A CB  1 
ATOM   2750  C  CG  . TRP A 1 340 ? 37.939  10.879  11.523  1.00 20.54  ? 340 TRP A CG  1 
ATOM   2751  C  CD1 . TRP A 1 340 ? 37.416  9.819   10.838  1.00 22.34  ? 340 TRP A CD1 1 
ATOM   2752  C  CD2 . TRP A 1 340 ? 38.185  11.908  10.533  1.00 20.50  ? 340 TRP A CD2 1 
ATOM   2753  N  NE1 . TRP A 1 340 ? 37.342  10.089  9.505   1.00 22.47  ? 340 TRP A NE1 1 
ATOM   2754  C  CE2 . TRP A 1 340 ? 37.788  11.367  9.274   1.00 21.63  ? 340 TRP A CE2 1 
ATOM   2755  C  CE3 . TRP A 1 340 ? 38.721  13.186  10.578  1.00 21.14  ? 340 TRP A CE3 1 
ATOM   2756  C  CZ2 . TRP A 1 340 ? 37.894  12.081  8.076   1.00 25.02  ? 340 TRP A CZ2 1 
ATOM   2757  C  CZ3 . TRP A 1 340 ? 38.811  13.910  9.385   1.00 24.83  ? 340 TRP A CZ3 1 
ATOM   2758  C  CH2 . TRP A 1 340 ? 38.410  13.341  8.137   1.00 24.93  ? 340 TRP A CH2 1 
ATOM   2759  N  N   . ASN A 1 341 ? 36.163  9.474   14.687  1.00 20.96  ? 341 ASN A N   1 
ATOM   2760  C  CA  . ASN A 1 341 ? 35.104  8.483   14.807  1.00 21.43  ? 341 ASN A CA  1 
ATOM   2761  C  C   . ASN A 1 341 ? 33.910  9.010   15.593  1.00 22.12  ? 341 ASN A C   1 
ATOM   2762  O  O   . ASN A 1 341 ? 32.749  8.700   15.254  1.00 21.33  ? 341 ASN A O   1 
ATOM   2763  C  CB  . ASN A 1 341 ? 35.683  7.214   15.435  1.00 22.89  ? 341 ASN A CB  1 
ATOM   2764  C  CG  . ASN A 1 341 ? 36.314  6.362   14.397  1.00 22.88  ? 341 ASN A CG  1 
ATOM   2765  O  OD1 . ASN A 1 341 ? 35.604  5.644   13.683  1.00 23.25  ? 341 ASN A OD1 1 
ATOM   2766  N  ND2 . ASN A 1 341 ? 37.643  6.462   14.240  1.00 23.56  ? 341 ASN A ND2 1 
ATOM   2767  N  N   . LEU A 1 342 ? 34.159  9.835   16.634  1.00 19.68  ? 342 LEU A N   1 
ATOM   2768  C  CA  . LEU A 1 342 ? 33.039  10.361  17.418  1.00 24.25  ? 342 LEU A CA  1 
ATOM   2769  C  C   . LEU A 1 342 ? 32.124  11.269  16.593  1.00 23.30  ? 342 LEU A C   1 
ATOM   2770  O  O   . LEU A 1 342 ? 30.973  11.498  16.970  1.00 24.78  ? 342 LEU A O   1 
ATOM   2771  C  CB  . LEU A 1 342 ? 33.588  11.119  18.638  1.00 22.91  ? 342 LEU A CB  1 
ATOM   2772  C  CG  . LEU A 1 342 ? 34.087  10.100  19.687  1.00 21.78  ? 342 LEU A CG  1 
ATOM   2773  C  CD1 . LEU A 1 342 ? 34.953  10.757  20.756  1.00 25.22  ? 342 LEU A CD1 1 
ATOM   2774  C  CD2 . LEU A 1 342 ? 32.906  9.254   20.359  1.00 20.67  ? 342 LEU A CD2 1 
ATOM   2775  N  N   . SER A 1 343 ? 32.606  11.798  15.481  1.00 21.00  ? 343 SER A N   1 
ATOM   2776  C  CA  . SER A 1 343 ? 31.761  12.653  14.663  1.00 23.35  ? 343 SER A CA  1 
ATOM   2777  C  C   . SER A 1 343 ? 30.834  11.857  13.744  1.00 24.12  ? 343 SER A C   1 
ATOM   2778  O  O   . SER A 1 343 ? 30.055  12.462  12.993  1.00 24.32  ? 343 SER A O   1 
ATOM   2779  C  CB  . SER A 1 343 ? 32.647  13.611  13.865  1.00 23.61  ? 343 SER A CB  1 
ATOM   2780  O  OG  . SER A 1 343 ? 33.301  12.993  12.758  1.00 22.13  ? 343 SER A OG  1 
ATOM   2781  N  N   . LYS A 1 344 ? 30.920  10.514  13.760  1.00 18.95  ? 344 LYS A N   1 
ATOM   2782  C  CA  . LYS A 1 344 ? 30.120  9.700   12.842  1.00 20.93  ? 344 LYS A CA  1 
ATOM   2783  C  C   . LYS A 1 344 ? 28.634  10.079  12.890  1.00 19.77  ? 344 LYS A C   1 
ATOM   2784  O  O   . LYS A 1 344 ? 28.011  10.036  13.977  1.00 19.06  ? 344 LYS A O   1 
ATOM   2785  C  CB  . LYS A 1 344 ? 30.292  8.240   13.256  1.00 23.27  ? 344 LYS A CB  1 
ATOM   2786  C  CG  . LYS A 1 344 ? 29.738  7.278   12.268  1.00 26.19  ? 344 LYS A CG  1 
ATOM   2787  C  CD  . LYS A 1 344 ? 29.884  5.805   12.776  1.00 31.77  ? 344 LYS A CD  1 
ATOM   2788  C  CE  . LYS A 1 344 ? 31.310  5.250   12.807  1.00 26.09  ? 344 LYS A CE  1 
ATOM   2789  N  NZ  . LYS A 1 344 ? 31.894  4.832   11.509  1.00 26.28  ? 344 LYS A NZ  1 
ATOM   2790  N  N   . PRO A 1 345 ? 28.027  10.462  11.771  1.00 19.14  ? 345 PRO A N   1 
ATOM   2791  C  CA  . PRO A 1 345 ? 26.616  10.867  11.857  1.00 21.11  ? 345 PRO A CA  1 
ATOM   2792  C  C   . PRO A 1 345 ? 25.719  9.756   12.365  1.00 22.38  ? 345 PRO A C   1 
ATOM   2793  O  O   . PRO A 1 345 ? 24.792  10.037  13.094  1.00 21.65  ? 345 PRO A O   1 
ATOM   2794  C  CB  . PRO A 1 345 ? 26.268  11.270  10.427  1.00 21.01  ? 345 PRO A CB  1 
ATOM   2795  C  CG  . PRO A 1 345 ? 27.668  11.746  9.843   1.00 23.72  ? 345 PRO A CG  1 
ATOM   2796  C  CD  . PRO A 1 345 ? 28.643  10.765  10.457  1.00 22.77  ? 345 PRO A CD  1 
ATOM   2797  N  N   . GLN A 1 346 ? 26.000  8.501   12.016  1.00 19.66  ? 346 GLN A N   1 
ATOM   2798  C  CA  . GLN A 1 346 ? 25.137  7.393   12.432  1.00 23.94  ? 346 GLN A CA  1 
ATOM   2799  C  C   . GLN A 1 346 ? 25.298  6.992   13.870  1.00 24.47  ? 346 GLN A C   1 
ATOM   2800  O  O   . GLN A 1 346 ? 24.651  6.000   14.257  1.00 23.69  ? 346 GLN A O   1 
ATOM   2801  C  CB  . GLN A 1 346 ? 25.376  6.190   11.524  1.00 21.34  ? 346 GLN A CB  1 
ATOM   2802  C  CG  . GLN A 1 346 ? 24.483  6.257   10.315  1.00 23.28  ? 346 GLN A CG  1 
ATOM   2803  C  CD  . GLN A 1 346 ? 22.999  5.947   10.599  1.00 27.32  ? 346 GLN A CD  1 
ATOM   2804  O  OE1 . GLN A 1 346 ? 22.503  5.911   11.755  1.00 32.44  ? 346 GLN A OE1 1 
ATOM   2805  N  NE2 . GLN A 1 346 ? 22.272  5.810   9.561   1.00 25.36  ? 346 GLN A NE2 1 
ATOM   2806  N  N   . TRP A 1 347 ? 26.089  7.715   14.690  1.00 22.36  ? 347 TRP A N   1 
ATOM   2807  C  CA  . TRP A 1 347 ? 26.093  7.460   16.137  1.00 21.18  ? 347 TRP A CA  1 
ATOM   2808  C  C   . TRP A 1 347 ? 25.230  8.452   16.910  1.00 21.72  ? 347 TRP A C   1 
ATOM   2809  O  O   . TRP A 1 347 ? 24.969  8.251   18.103  1.00 21.84  ? 347 TRP A O   1 
ATOM   2810  C  CB  . TRP A 1 347 ? 27.544  7.528   16.735  1.00 21.13  ? 347 TRP A CB  1 
ATOM   2811  C  CG  . TRP A 1 347 ? 28.458  6.336   16.394  1.00 20.99  ? 347 TRP A CG  1 
ATOM   2812  C  CD1 . TRP A 1 347 ? 28.094  5.187   15.712  1.00 23.16  ? 347 TRP A CD1 1 
ATOM   2813  C  CD2 . TRP A 1 347 ? 29.865  6.177   16.738  1.00 19.50  ? 347 TRP A CD2 1 
ATOM   2814  N  NE1 . TRP A 1 347 ? 29.174  4.337   15.600  1.00 24.96  ? 347 TRP A NE1 1 
ATOM   2815  C  CE2 . TRP A 1 347 ? 30.273  4.887   16.227  1.00 19.48  ? 347 TRP A CE2 1 
ATOM   2816  C  CE3 . TRP A 1 347 ? 30.800  6.966   17.393  1.00 21.51  ? 347 TRP A CE3 1 
ATOM   2817  C  CZ2 . TRP A 1 347 ? 31.589  4.419   16.313  1.00 21.12  ? 347 TRP A CZ2 1 
ATOM   2818  C  CZ3 . TRP A 1 347 ? 32.121  6.469   17.516  1.00 20.46  ? 347 TRP A CZ3 1 
ATOM   2819  C  CH2 . TRP A 1 347 ? 32.489  5.181   16.994  1.00 21.10  ? 347 TRP A CH2 1 
ATOM   2820  N  N   . GLN A 1 348 ? 24.818  9.554   16.279  1.00 21.97  ? 348 GLN A N   1 
ATOM   2821  C  CA  . GLN A 1 348 ? 24.225  10.630  17.065  1.00 19.27  ? 348 GLN A CA  1 
ATOM   2822  C  C   . GLN A 1 348 ? 22.822  10.274  17.574  1.00 20.67  ? 348 GLN A C   1 
ATOM   2823  O  O   . GLN A 1 348 ? 22.436  10.732  18.657  1.00 21.04  ? 348 GLN A O   1 
ATOM   2824  C  CB  . GLN A 1 348 ? 24.210  11.912  16.214  1.00 20.18  ? 348 GLN A CB  1 
ATOM   2825  C  CG  . GLN A 1 348 ? 25.595  12.185  15.638  1.00 20.74  ? 348 GLN A CG  1 
ATOM   2826  C  CD  . GLN A 1 348 ? 26.691  12.283  16.700  1.00 23.05  ? 348 GLN A CD  1 
ATOM   2827  O  OE1 . GLN A 1 348 ? 26.567  13.057  17.686  1.00 22.73  ? 348 GLN A OE1 1 
ATOM   2828  N  NE2 . GLN A 1 348 ? 27.779  11.542  16.500  1.00 22.13  ? 348 GLN A NE2 1 
ATOM   2829  N  N   . HIS A 1 349 ? 22.052  9.466   16.821  1.00 19.98  ? 349 HIS A N   1 
ATOM   2830  C  CA  . HIS A 1 349 ? 20.687  9.229   17.220  1.00 20.05  ? 349 HIS A CA  1 
ATOM   2831  C  C   . HIS A 1 349 ? 20.643  8.269   18.418  1.00 21.06  ? 349 HIS A C   1 
ATOM   2832  O  O   . HIS A 1 349 ? 19.582  8.093   19.001  1.00 20.94  ? 349 HIS A O   1 
ATOM   2833  C  CB  . HIS A 1 349 ? 19.932  8.635   16.054  1.00 23.46  ? 349 HIS A CB  1 
ATOM   2834  C  CG  . HIS A 1 349 ? 20.321  7.215   15.797  1.00 21.67  ? 349 HIS A CG  1 
ATOM   2835  N  ND1 . HIS A 1 349 ? 21.509  6.885   15.185  1.00 23.05  ? 349 HIS A ND1 1 
ATOM   2836  C  CD2 . HIS A 1 349 ? 19.732  6.044   16.161  1.00 24.02  ? 349 HIS A CD2 1 
ATOM   2837  C  CE1 . HIS A 1 349 ? 21.614  5.560   15.135  1.00 25.41  ? 349 HIS A CE1 1 
ATOM   2838  N  NE2 . HIS A 1 349 ? 20.551  5.024   15.722  1.00 23.01  ? 349 HIS A NE2 1 
ATOM   2839  N  N   . PHE A 1 350 ? 21.792  7.677   18.788  1.00 20.89  ? 350 PHE A N   1 
ATOM   2840  C  CA  . PHE A 1 350 ? 21.808  6.846   20.003  1.00 18.21  ? 350 PHE A CA  1 
ATOM   2841  C  C   . PHE A 1 350 ? 21.558  7.672   21.246  1.00 20.95  ? 350 PHE A C   1 
ATOM   2842  O  O   . PHE A 1 350 ? 21.147  7.128   22.300  1.00 23.39  ? 350 PHE A O   1 
ATOM   2843  C  CB  . PHE A 1 350 ? 23.143  6.091   20.129  1.00 18.81  ? 350 PHE A CB  1 
ATOM   2844  C  CG  . PHE A 1 350 ? 23.269  4.863   19.233  1.00 19.36  ? 350 PHE A CG  1 
ATOM   2845  C  CD1 . PHE A 1 350 ? 22.737  3.615   19.651  1.00 19.02  ? 350 PHE A CD1 1 
ATOM   2846  C  CD2 . PHE A 1 350 ? 23.905  4.926   17.992  1.00 20.27  ? 350 PHE A CD2 1 
ATOM   2847  C  CE1 . PHE A 1 350 ? 22.835  2.502   18.837  1.00 22.56  ? 350 PHE A CE1 1 
ATOM   2848  C  CE2 . PHE A 1 350 ? 24.014  3.801   17.166  1.00 21.00  ? 350 PHE A CE2 1 
ATOM   2849  C  CZ  . PHE A 1 350 ? 23.476  2.545   17.596  1.00 21.78  ? 350 PHE A CZ  1 
ATOM   2850  N  N   . TYR A 1 351 ? 21.751  8.973   21.142  1.00 20.49  ? 351 TYR A N   1 
ATOM   2851  C  CA  . TYR A 1 351 ? 21.528  9.938   22.220  1.00 22.47  ? 351 TYR A CA  1 
ATOM   2852  C  C   . TYR A 1 351 ? 20.323  10.833  21.996  1.00 27.22  ? 351 TYR A C   1 
ATOM   2853  O  O   . TYR A 1 351 ? 19.602  11.114  22.930  1.00 25.75  ? 351 TYR A O   1 
ATOM   2854  C  CB  . TYR A 1 351 ? 22.745  10.827  22.373  1.00 24.89  ? 351 TYR A CB  1 
ATOM   2855  C  CG  . TYR A 1 351 ? 24.033  10.053  22.345  1.00 23.14  ? 351 TYR A CG  1 
ATOM   2856  C  CD1 . TYR A 1 351 ? 24.367  9.193   23.394  1.00 22.25  ? 351 TYR A CD1 1 
ATOM   2857  C  CD2 . TYR A 1 351 ? 24.915  10.168  21.276  1.00 21.93  ? 351 TYR A CD2 1 
ATOM   2858  C  CE1 . TYR A 1 351 ? 25.532  8.436   23.351  1.00 20.44  ? 351 TYR A CE1 1 
ATOM   2859  C  CE2 . TYR A 1 351 ? 26.091  9.457   21.228  1.00 23.82  ? 351 TYR A CE2 1 
ATOM   2860  C  CZ  . TYR A 1 351 ? 26.390  8.562   22.267  1.00 24.56  ? 351 TYR A CZ  1 
ATOM   2861  O  OH  . TYR A 1 351 ? 27.550  7.864   22.309  1.00 26.47  ? 351 TYR A OH  1 
ATOM   2862  N  N   . ASP A 1 352 ? 20.106  11.323  20.780  1.00 22.76  ? 352 ASP A N   1 
ATOM   2863  C  CA  . ASP A 1 352 ? 19.124  12.383  20.513  1.00 23.88  ? 352 ASP A CA  1 
ATOM   2864  C  C   . ASP A 1 352 ? 18.539  12.162  19.119  1.00 23.23  ? 352 ASP A C   1 
ATOM   2865  O  O   . ASP A 1 352 ? 19.188  12.489  18.113  1.00 22.60  ? 352 ASP A O   1 
ATOM   2866  C  CB  . ASP A 1 352 ? 19.811  13.746  20.596  1.00 24.67  ? 352 ASP A CB  1 
ATOM   2867  C  CG  . ASP A 1 352 ? 18.870  14.878  20.360  1.00 27.44  ? 352 ASP A CG  1 
ATOM   2868  O  OD1 . ASP A 1 352 ? 17.700  14.639  19.976  1.00 25.99  ? 352 ASP A OD1 1 
ATOM   2869  O  OD2 . ASP A 1 352 ? 19.287  16.051  20.623  1.00 30.04  ? 352 ASP A OD2 1 
ATOM   2870  N  N   . PRO A 1 353 ? 17.303  11.649  19.014  1.00 25.24  ? 353 PRO A N   1 
ATOM   2871  C  CA  . PRO A 1 353 ? 16.747  11.344  17.679  1.00 26.56  ? 353 PRO A CA  1 
ATOM   2872  C  C   . PRO A 1 353 ? 16.591  12.592  16.821  1.00 22.33  ? 353 PRO A C   1 
ATOM   2873  O  O   . PRO A 1 353 ? 16.586  12.481  15.590  1.00 22.67  ? 353 PRO A O   1 
ATOM   2874  C  CB  . PRO A 1 353 ? 15.366  10.766  17.962  1.00 25.65  ? 353 PRO A CB  1 
ATOM   2875  C  CG  . PRO A 1 353 ? 15.000  11.357  19.409  1.00 30.45  ? 353 PRO A CG  1 
ATOM   2876  C  CD  . PRO A 1 353 ? 16.285  11.654  20.096  1.00 30.32  ? 353 PRO A CD  1 
ATOM   2877  N  N   . THR A 1 354 ? 16.425  13.761  17.437  1.00 23.15  ? 354 THR A N   1 
ATOM   2878  C  CA  . THR A 1 354 ? 16.233  14.964  16.641  1.00 23.96  ? 354 THR A CA  1 
ATOM   2879  C  C   . THR A 1 354 ? 17.482  15.319  15.846  1.00 25.19  ? 354 THR A C   1 
ATOM   2880  O  O   . THR A 1 354 ? 17.366  15.970  14.794  1.00 22.84  ? 354 THR A O   1 
ATOM   2881  C  CB  . THR A 1 354 ? 15.818  16.157  17.518  1.00 24.91  ? 354 THR A CB  1 
ATOM   2882  O  OG1 . THR A 1 354 ? 16.947  16.620  18.278  1.00 25.35  ? 354 THR A OG1 1 
ATOM   2883  C  CG2 . THR A 1 354 ? 14.639  15.806  18.424  1.00 26.42  ? 354 THR A CG2 1 
ATOM   2884  N  N   . ILE A 1 355 ? 18.669  14.856  16.286  1.00 22.71  ? 355 ILE A N   1 
ATOM   2885  C  CA  . ILE A 1 355 ? 19.864  15.079  15.488  1.00 25.50  ? 355 ILE A CA  1 
ATOM   2886  C  C   . ILE A 1 355 ? 19.758  14.310  14.171  1.00 22.80  ? 355 ILE A C   1 
ATOM   2887  O  O   . ILE A 1 355 ? 20.089  14.828  13.079  1.00 23.17  ? 355 ILE A O   1 
ATOM   2888  C  CB  . ILE A 1 355 ? 21.119  14.672  16.271  1.00 23.73  ? 355 ILE A CB  1 
ATOM   2889  C  CG1 . ILE A 1 355 ? 21.215  15.469  17.592  1.00 23.73  ? 355 ILE A CG1 1 
ATOM   2890  C  CG2 . ILE A 1 355 ? 22.381  14.930  15.401  1.00 21.68  ? 355 ILE A CG2 1 
ATOM   2891  C  CD1 . ILE A 1 355 ? 22.472  15.062  18.405  1.00 25.10  ? 355 ILE A CD1 1 
ATOM   2892  N  N   . LYS A 1 356 ? 19.276  13.066  14.254  1.00 22.57  ? 356 LYS A N   1 
ATOM   2893  C  CA  . LYS A 1 356 ? 19.045  12.320  13.033  1.00 22.24  ? 356 LYS A CA  1 
ATOM   2894  C  C   . LYS A 1 356 ? 17.895  12.907  12.229  1.00 24.80  ? 356 LYS A C   1 
ATOM   2895  O  O   . LYS A 1 356 ? 17.955  12.945  10.991  1.00 24.32  ? 356 LYS A O   1 
ATOM   2896  C  CB  . LYS A 1 356 ? 18.761  10.858  13.390  1.00 21.81  ? 356 LYS A CB  1 
ATOM   2897  C  CG  . LYS A 1 356 ? 18.258  10.087  12.164  1.00 20.45  ? 356 LYS A CG  1 
ATOM   2898  C  CD  . LYS A 1 356 ? 18.382  8.552   12.390  1.00 22.85  ? 356 LYS A CD  1 
ATOM   2899  C  CE  . LYS A 1 356 ? 17.864  7.770   11.223  1.00 31.80  ? 356 LYS A CE  1 
ATOM   2900  N  NZ  . LYS A 1 356 ? 16.965  6.676   11.591  1.00 31.48  ? 356 LYS A NZ  1 
ATOM   2901  N  N   . SER A 1 357 ? 16.864  13.414  12.891  1.00 22.32  ? 357 SER A N   1 
ATOM   2902  C  CA  . SER A 1 357 ? 15.756  14.026  12.146  1.00 23.53  ? 357 SER A CA  1 
ATOM   2903  C  C   . SER A 1 357 ? 16.281  15.209  11.331  1.00 20.73  ? 357 SER A C   1 
ATOM   2904  O  O   . SER A 1 357 ? 15.966  15.364  10.138  1.00 21.72  ? 357 SER A O   1 
ATOM   2905  C  CB  . SER A 1 357 ? 14.642  14.539  13.083  1.00 24.84  ? 357 SER A CB  1 
ATOM   2906  O  OG  . SER A 1 357 ? 13.942  13.482  13.731  1.00 25.45  ? 357 SER A OG  1 
ATOM   2907  N  N   . ASP A 1 358 ? 17.121  16.039  11.960  1.00 22.64  ? 358 ASP A N   1 
ATOM   2908  C  CA  . ASP A 1 358 ? 17.647  17.187  11.218  1.00 22.83  ? 358 ASP A CA  1 
ATOM   2909  C  C   . ASP A 1 358 ? 18.541  16.728  10.071  1.00 22.38  ? 358 ASP A C   1 
ATOM   2910  O  O   . ASP A 1 358 ? 18.530  17.306  8.980   1.00 22.68  ? 358 ASP A O   1 
ATOM   2911  C  CB  . ASP A 1 358 ? 18.400  18.102  12.164  1.00 25.02  ? 358 ASP A CB  1 
ATOM   2912  C  CG  . ASP A 1 358 ? 17.493  18.820  13.150  1.00 31.00  ? 358 ASP A CG  1 
ATOM   2913  O  OD1 . ASP A 1 358 ? 16.268  18.968  12.892  1.00 31.35  ? 358 ASP A OD1 1 
ATOM   2914  O  OD2 . ASP A 1 358 ? 18.014  19.263  14.189  1.00 30.40  ? 358 ASP A OD2 1 
ATOM   2915  N  N   . MET A 1 359 ? 19.309  15.663  10.299  1.00 22.00  ? 359 MET A N   1 
ATOM   2916  C  CA  . MET A 1 359 ? 20.188  15.116  9.284   1.00 21.93  ? 359 MET A CA  1 
ATOM   2917  C  C   . MET A 1 359 ? 19.369  14.621  8.081   1.00 21.56  ? 359 MET A C   1 
ATOM   2918  O  O   . MET A 1 359 ? 19.683  14.944  6.920   1.00 21.99  ? 359 MET A O   1 
ATOM   2919  C  CB  . MET A 1 359 ? 20.966  14.003  10.020  1.00 24.98  ? 359 MET A CB  1 
ATOM   2920  C  CG  . MET A 1 359 ? 22.290  14.510  10.573  1.00 22.53  ? 359 MET A CG  1 
ATOM   2921  S  SD  . MET A 1 359 ? 23.044  13.092  11.383  1.00 25.48  ? 359 MET A SD  1 
ATOM   2922  C  CE  . MET A 1 359 ? 24.436  13.846  12.155  1.00 25.92  ? 359 MET A CE  1 
ATOM   2923  N  N   . MET A 1 360 ? 18.264  13.886  8.356   1.00 23.08  ? 360 MET A N   1 
ATOM   2924  C  CA  . MET A 1 360 ? 17.366  13.440  7.290   1.00 22.89  ? 360 MET A CA  1 
ATOM   2925  C  C   . MET A 1 360 ? 16.707  14.597  6.564   1.00 21.84  ? 360 MET A C   1 
ATOM   2926  O  O   . MET A 1 360 ? 16.707  14.612  5.328   1.00 22.60  ? 360 MET A O   1 
ATOM   2927  C  CB  . MET A 1 360 ? 16.365  12.384  7.771   1.00 25.00  ? 360 MET A CB  1 
ATOM   2928  C  CG  . MET A 1 360 ? 17.019  11.351  8.645   1.00 25.75  ? 360 MET A CG  1 
ATOM   2929  S  SD  . MET A 1 360 ? 15.782  10.240  9.311   1.00 27.15  ? 360 MET A SD  1 
ATOM   2930  C  CE  . MET A 1 360 ? 15.381  9.150   7.974   1.00 29.13  ? 360 MET A CE  1 
ATOM   2931  N  N   . LEU A 1 361 ? 16.331  15.645  7.271   1.00 20.44  ? 361 LEU A N   1 
ATOM   2932  C  CA  . LEU A 1 361 ? 15.721  16.786  6.566   1.00 26.01  ? 361 LEU A CA  1 
ATOM   2933  C  C   . LEU A 1 361 ? 16.740  17.485  5.688   1.00 22.64  ? 361 LEU A C   1 
ATOM   2934  O  O   . LEU A 1 361 ? 16.414  17.937  4.579   1.00 22.83  ? 361 LEU A O   1 
ATOM   2935  C  CB  . LEU A 1 361 ? 15.139  17.775  7.562   1.00 25.68  ? 361 LEU A CB  1 
ATOM   2936  C  CG  . LEU A 1 361 ? 13.953  17.202  8.333   1.00 22.70  ? 361 LEU A CG  1 
ATOM   2937  C  CD1 . LEU A 1 361 ? 13.685  18.164  9.460   1.00 26.77  ? 361 LEU A CD1 1 
ATOM   2938  C  CD2 . LEU A 1 361 ? 12.703  17.080  7.436   1.00 23.85  ? 361 LEU A CD2 1 
ATOM   2939  N  N   . ARG A 1 362 ? 17.989  17.512  6.126   1.00 21.81  ? 362 ARG A N   1 
ATOM   2940  C  CA  . ARG A 1 362 ? 19.035  18.128  5.320   1.00 22.28  ? 362 ARG A CA  1 
ATOM   2941  C  C   . ARG A 1 362 ? 19.356  17.291  4.087   1.00 21.16  ? 362 ARG A C   1 
ATOM   2942  O  O   . ARG A 1 362 ? 19.599  17.836  3.009   1.00 24.10  ? 362 ARG A O   1 
ATOM   2943  C  CB  . ARG A 1 362 ? 20.284  18.286  6.166   1.00 21.14  ? 362 ARG A CB  1 
ATOM   2944  C  CG  . ARG A 1 362 ? 21.374  19.055  5.461   1.00 23.94  ? 362 ARG A CG  1 
ATOM   2945  C  CD  . ARG A 1 362 ? 22.597  18.979  6.303   1.00 24.58  ? 362 ARG A CD  1 
ATOM   2946  N  NE  . ARG A 1 362 ? 23.658  19.850  5.848   1.00 25.38  ? 362 ARG A NE  1 
ATOM   2947  C  CZ  . ARG A 1 362 ? 24.762  20.103  6.541   1.00 27.97  ? 362 ARG A CZ  1 
ATOM   2948  N  NH1 . ARG A 1 362 ? 24.948  19.598  7.754   1.00 24.10  ? 362 ARG A NH1 1 
ATOM   2949  N  NH2 . ARG A 1 362 ? 25.686  20.919  6.020   1.00 24.83  ? 362 ARG A NH2 1 
ATOM   2950  N  N   . ILE A 1 363 ? 19.377  15.962  4.224   1.00 20.42  ? 363 ILE A N   1 
ATOM   2951  C  CA  . ILE A 1 363 ? 19.578  15.136  3.025   1.00 20.62  ? 363 ILE A CA  1 
ATOM   2952  C  C   . ILE A 1 363 ? 18.441  15.338  2.032   1.00 20.30  ? 363 ILE A C   1 
ATOM   2953  O  O   . ILE A 1 363 ? 18.681  15.486  0.819   1.00 22.43  ? 363 ILE A O   1 
ATOM   2954  C  CB  . ILE A 1 363 ? 19.716  13.651  3.408   1.00 19.17  ? 363 ILE A CB  1 
ATOM   2955  C  CG1 . ILE A 1 363 ? 21.050  13.409  4.136   1.00 18.62  ? 363 ILE A CG1 1 
ATOM   2956  C  CG2 . ILE A 1 363 ? 19.644  12.832  2.138   1.00 20.58  ? 363 ILE A CG2 1 
ATOM   2957  C  CD1 . ILE A 1 363 ? 21.080  11.971  4.947   1.00 21.39  ? 363 ILE A CD1 1 
ATOM   2958  N  N   . ILE A 1 364 ? 17.190  15.370  2.520   1.00 21.49  ? 364 ILE A N   1 
ATOM   2959  C  CA  . ILE A 1 364 ? 16.040  15.636  1.651   1.00 21.43  ? 364 ILE A CA  1 
ATOM   2960  C  C   . ILE A 1 364 ? 16.231  16.924  0.857   1.00 26.48  ? 364 ILE A C   1 
ATOM   2961  O  O   . ILE A 1 364 ? 16.007  16.944  -0.357  1.00 24.40  ? 364 ILE A O   1 
ATOM   2962  C  CB  . ILE A 1 364 ? 14.730  15.674  2.439   1.00 22.33  ? 364 ILE A CB  1 
ATOM   2963  C  CG1 . ILE A 1 364 ? 14.377  14.262  2.916   1.00 21.90  ? 364 ILE A CG1 1 
ATOM   2964  C  CG2 . ILE A 1 364 ? 13.564  16.215  1.526   1.00 24.24  ? 364 ILE A CG2 1 
ATOM   2965  C  CD1 . ILE A 1 364 ? 13.363  14.300  4.042   1.00 22.07  ? 364 ILE A CD1 1 
ATOM   2966  N  N   . LYS A 1 365 ? 16.673  17.998  1.520   1.00 22.33  ? 365 LYS A N   1 
ATOM   2967  C  CA  . LYS A 1 365 ? 16.900  19.272  0.837   1.00 24.14  ? 365 LYS A CA  1 
ATOM   2968  C  C   . LYS A 1 365 ? 18.063  19.186  -0.158  1.00 23.77  ? 365 LYS A C   1 
ATOM   2969  O  O   . LYS A 1 365 ? 17.894  19.481  -1.354  1.00 27.60  ? 365 LYS A O   1 
ATOM   2970  C  CB  . LYS A 1 365 ? 17.136  20.348  1.897   1.00 23.70  ? 365 LYS A CB  1 
ATOM   2971  C  CG  . LYS A 1 365 ? 17.909  21.599  1.429   1.00 29.06  ? 365 LYS A CG  1 
ATOM   2972  C  CD  . LYS A 1 365 ? 17.716  22.665  2.494   1.00 31.78  ? 365 LYS A CD  1 
ATOM   2973  C  CE  . LYS A 1 365 ? 18.962  23.511  2.670   1.00 39.34  ? 365 LYS A CE  1 
ATOM   2974  N  NZ  . LYS A 1 365 ? 19.230  24.351  1.464   1.00 45.52  ? 365 LYS A NZ  1 
ATOM   2975  N  N   . GLU A 1 366 ? 19.248  18.765  0.307   1.00 22.90  ? 366 GLU A N   1 
ATOM   2976  C  CA  . GLU A 1 366 ? 20.465  18.914  -0.488  1.00 21.66  ? 366 GLU A CA  1 
ATOM   2977  C  C   . GLU A 1 366 ? 20.499  17.928  -1.650  1.00 25.82  ? 366 GLU A C   1 
ATOM   2978  O  O   . GLU A 1 366 ? 21.034  18.265  -2.709  1.00 22.96  ? 366 GLU A O   1 
ATOM   2979  C  CB  . GLU A 1 366 ? 21.689  18.769  0.409   1.00 23.79  ? 366 GLU A CB  1 
ATOM   2980  C  CG  . GLU A 1 366 ? 21.849  19.974  1.335   1.00 25.86  ? 366 GLU A CG  1 
ATOM   2981  C  CD  . GLU A 1 366 ? 23.163  19.975  2.117   1.00 25.24  ? 366 GLU A CD  1 
ATOM   2982  O  OE1 . GLU A 1 366 ? 24.150  19.301  1.712   1.00 25.42  ? 366 GLU A OE1 1 
ATOM   2983  O  OE2 . GLU A 1 366 ? 23.220  20.689  3.148   1.00 25.28  ? 366 GLU A OE2 1 
ATOM   2984  N  N   . TRP A 1 367 ? 19.902  16.742  -1.494  1.00 22.01  ? 367 TRP A N   1 
ATOM   2985  C  CA  . TRP A 1 367 ? 19.869  15.735  -2.567  1.00 21.96  ? 367 TRP A CA  1 
ATOM   2986  C  C   . TRP A 1 367 ? 18.569  15.802  -3.383  1.00 24.49  ? 367 TRP A C   1 
ATOM   2987  O  O   . TRP A 1 367 ? 18.330  14.945  -4.247  1.00 24.25  ? 367 TRP A O   1 
ATOM   2988  C  CB  . TRP A 1 367 ? 20.077  14.308  -1.969  1.00 21.81  ? 367 TRP A CB  1 
ATOM   2989  C  CG  . TRP A 1 367 ? 21.540  13.923  -1.724  1.00 23.06  ? 367 TRP A CG  1 
ATOM   2990  C  CD1 . TRP A 1 367 ? 22.338  13.122  -2.538  1.00 22.08  ? 367 TRP A CD1 1 
ATOM   2991  C  CD2 . TRP A 1 367 ? 22.367  14.295  -0.615  1.00 21.22  ? 367 TRP A CD2 1 
ATOM   2992  N  NE1 . TRP A 1 367 ? 23.575  12.978  -1.980  1.00 21.92  ? 367 TRP A NE1 1 
ATOM   2993  C  CE2 . TRP A 1 367 ? 23.624  13.674  -0.803  1.00 21.92  ? 367 TRP A CE2 1 
ATOM   2994  C  CE3 . TRP A 1 367 ? 22.156  15.056  0.553   1.00 23.59  ? 367 TRP A CE3 1 
ATOM   2995  C  CZ2 . TRP A 1 367 ? 24.684  13.821  0.107   1.00 23.01  ? 367 TRP A CZ2 1 
ATOM   2996  C  CZ3 . TRP A 1 367 ? 23.217  15.196  1.475   1.00 23.15  ? 367 TRP A CZ3 1 
ATOM   2997  C  CH2 . TRP A 1 367 ? 24.462  14.590  1.250   1.00 21.44  ? 367 TRP A CH2 1 
ATOM   2998  N  N   . GLN A 1 368 ? 17.745  16.827  -3.151  1.00 22.67  ? 368 GLN A N   1 
ATOM   2999  C  CA  . GLN A 1 368 ? 16.549  17.121  -3.929  1.00 22.56  ? 368 GLN A CA  1 
ATOM   3000  C  C   . GLN A 1 368 ? 15.593  15.928  -3.965  1.00 24.97  ? 368 GLN A C   1 
ATOM   3001  O  O   . GLN A 1 368 ? 15.206  15.429  -5.032  1.00 24.18  ? 368 GLN A O   1 
ATOM   3002  C  CB  . GLN A 1 368 ? 16.933  17.572  -5.341  1.00 25.18  ? 368 GLN A CB  1 
ATOM   3003  C  CG  . GLN A 1 368 ? 18.062  18.604  -5.385  1.00 30.66  ? 368 GLN A CG  1 
ATOM   3004  C  CD  . GLN A 1 368 ? 18.266  19.123  -6.841  1.00 35.37  ? 368 GLN A CD  1 
ATOM   3005  O  OE1 . GLN A 1 368 ? 17.432  19.855  -7.376  1.00 33.41  ? 368 GLN A OE1 1 
ATOM   3006  N  NE2 . GLN A 1 368 ? 19.351  18.673  -7.488  1.00 33.94  ? 368 GLN A NE2 1 
ATOM   3007  N  N   . VAL A 1 369 ? 15.217  15.487  -2.771  1.00 22.86  ? 369 VAL A N   1 
ATOM   3008  C  CA  . VAL A 1 369 ? 14.423  14.283  -2.606  1.00 22.91  ? 369 VAL A CA  1 
ATOM   3009  C  C   . VAL A 1 369 ? 12.937  14.602  -2.683  1.00 26.39  ? 369 VAL A C   1 
ATOM   3010  O  O   . VAL A 1 369 ? 12.454  15.551  -2.038  1.00 24.37  ? 369 VAL A O   1 
ATOM   3011  C  CB  . VAL A 1 369 ? 14.763  13.606  -1.282  1.00 21.22  ? 369 VAL A CB  1 
ATOM   3012  C  CG1 . VAL A 1 369 ? 13.776  12.476  -0.984  1.00 20.90  ? 369 VAL A CG1 1 
ATOM   3013  C  CG2 . VAL A 1 369 ? 16.200  13.053  -1.359  1.00 22.15  ? 369 VAL A CG2 1 
ATOM   3014  N  N   . ASP A 1 370 ? 12.201  13.762  -3.442  1.00 21.56  ? 370 ASP A N   1 
ATOM   3015  C  CA  . ASP A 1 370 ? 10.762  13.885  -3.615  1.00 22.36  ? 370 ASP A CA  1 
ATOM   3016  C  C   . ASP A 1 370 ? 9.947   13.063  -2.619  1.00 26.34  ? 370 ASP A C   1 
ATOM   3017  O  O   . ASP A 1 370 ? 8.756   13.359  -2.425  1.00 25.00  ? 370 ASP A O   1 
ATOM   3018  C  CB  . ASP A 1 370 ? 10.382  13.430  -5.036  1.00 24.68  ? 370 ASP A CB  1 
ATOM   3019  C  CG  . ASP A 1 370 ? 11.118  14.192  -6.102  1.00 28.69  ? 370 ASP A CG  1 
ATOM   3020  O  OD1 . ASP A 1 370 ? 11.097  15.425  -5.973  1.00 30.90  ? 370 ASP A OD1 1 
ATOM   3021  O  OD2 . ASP A 1 370 ? 11.662  13.610  -7.085  1.00 29.21  ? 370 ASP A OD2 1 
ATOM   3022  N  N   . GLY A 1 371 ? 10.506  11.993  -2.054  1.00 23.10  ? 371 GLY A N   1 
ATOM   3023  C  CA  . GLY A 1 371 ? 9.710   11.115  -1.214  1.00 24.36  ? 371 GLY A CA  1 
ATOM   3024  C  C   . GLY A 1 371 ? 10.624  10.232  -0.407  1.00 24.41  ? 371 GLY A C   1 
ATOM   3025  O  O   . GLY A 1 371 ? 11.738  9.954   -0.831  1.00 24.13  ? 371 GLY A O   1 
ATOM   3026  N  N   . VAL A 1 372 ? 10.169  9.813   0.788   1.00 22.08  ? 372 VAL A N   1 
ATOM   3027  C  CA  . VAL A 1 372 ? 10.995  9.070   1.740   1.00 20.24  ? 372 VAL A CA  1 
ATOM   3028  C  C   . VAL A 1 372 ? 10.303  7.760   2.070   1.00 24.33  ? 372 VAL A C   1 
ATOM   3029  O  O   . VAL A 1 372 ? 9.092   7.741   2.325   1.00 23.10  ? 372 VAL A O   1 
ATOM   3030  C  CB  . VAL A 1 372 ? 11.258  9.844   3.056   1.00 20.93  ? 372 VAL A CB  1 
ATOM   3031  C  CG1 . VAL A 1 372 ? 12.159  8.988   3.933   1.00 23.10  ? 372 VAL A CG1 1 
ATOM   3032  C  CG2 . VAL A 1 372 ? 11.879  11.251  2.741   1.00 22.65  ? 372 VAL A CG2 1 
ATOM   3033  N  N   . MET A 1 373 ? 11.067  6.656   2.054   1.00 22.21  ? 373 MET A N   1 
ATOM   3034  C  CA  . MET A 1 373 ? 10.493  5.332   2.344   1.00 22.00  ? 373 MET A CA  1 
ATOM   3035  C  C   . MET A 1 373 ? 11.261  4.823   3.541   1.00 23.51  ? 373 MET A C   1 
ATOM   3036  O  O   . MET A 1 373 ? 12.480  4.622   3.420   1.00 24.75  ? 373 MET A O   1 
ATOM   3037  C  CB  . MET A 1 373 ? 10.737  4.410   1.155   1.00 24.69  ? 373 MET A CB  1 
ATOM   3038  C  CG  . MET A 1 373 ? 10.075  4.834   -0.147  1.00 26.05  ? 373 MET A CG  1 
ATOM   3039  S  SD  . MET A 1 373 ? 10.148  3.434   -1.335  1.00 27.25  ? 373 MET A SD  1 
ATOM   3040  C  CE  . MET A 1 373 ? 11.887  3.406   -1.675  1.00 28.14  ? 373 MET A CE  1 
ATOM   3041  N  N   . LEU A 1 374 ? 10.625  4.745   4.718   1.00 21.64  ? 374 LEU A N   1 
ATOM   3042  C  CA  . LEU A 1 374 ? 11.313  4.371   5.954   1.00 22.45  ? 374 LEU A CA  1 
ATOM   3043  C  C   . LEU A 1 374 ? 11.084  2.896   6.297   1.00 22.73  ? 374 LEU A C   1 
ATOM   3044  O  O   . LEU A 1 374 ? 9.958   2.497   6.545   1.00 22.63  ? 374 LEU A O   1 
ATOM   3045  C  CB  . LEU A 1 374 ? 10.808  5.206   7.128   1.00 23.70  ? 374 LEU A CB  1 
ATOM   3046  C  CG  . LEU A 1 374 ? 11.063  6.716   7.062   1.00 26.47  ? 374 LEU A CG  1 
ATOM   3047  C  CD1 . LEU A 1 374 ? 10.458  7.357   8.330   1.00 27.81  ? 374 LEU A CD1 1 
ATOM   3048  C  CD2 . LEU A 1 374 ? 12.544  7.069   6.966   1.00 31.32  ? 374 LEU A CD2 1 
ATOM   3049  N  N   . HIS A 1 375 ? 12.175  2.146   6.450   1.00 22.40  ? 375 HIS A N   1 
ATOM   3050  C  CA  . HIS A 1 375 ? 12.165  0.756   6.913   1.00 21.73  ? 375 HIS A CA  1 
ATOM   3051  C  C   . HIS A 1 375 ? 12.024  0.759   8.433   1.00 22.34  ? 375 HIS A C   1 
ATOM   3052  O  O   . HIS A 1 375 ? 12.885  1.287   9.132   1.00 27.07  ? 375 HIS A O   1 
ATOM   3053  C  CB  . HIS A 1 375 ? 13.481  0.097   6.478   1.00 22.04  ? 375 HIS A CB  1 
ATOM   3054  C  CG  . HIS A 1 375 ? 13.612  -1.358  6.856   1.00 25.09  ? 375 HIS A CG  1 
ATOM   3055  N  ND1 . HIS A 1 375 ? 14.845  -1.971  6.979   1.00 25.56  ? 375 HIS A ND1 1 
ATOM   3056  C  CD2 . HIS A 1 375 ? 12.683  -2.308  7.128   1.00 26.61  ? 375 HIS A CD2 1 
ATOM   3057  C  CE1 . HIS A 1 375 ? 14.664  -3.249  7.306   1.00 25.13  ? 375 HIS A CE1 1 
ATOM   3058  N  NE2 . HIS A 1 375 ? 13.366  -3.476  7.434   1.00 24.83  ? 375 HIS A NE2 1 
ATOM   3059  N  N   . LEU A 1 376 ? 10.932  0.226   8.956   1.00 22.46  ? 376 LEU A N   1 
ATOM   3060  C  CA  . LEU A 1 376 ? 10.804  0.028   10.391  1.00 21.20  ? 376 LEU A CA  1 
ATOM   3061  C  C   . LEU A 1 376 ? 11.428  -1.352  10.602  1.00 23.71  ? 376 LEU A C   1 
ATOM   3062  O  O   . LEU A 1 376 ? 10.776  -2.379  10.357  1.00 27.22  ? 376 LEU A O   1 
ATOM   3063  C  CB  . LEU A 1 376 ? 9.339   0.069   10.843  1.00 22.59  ? 376 LEU A CB  1 
ATOM   3064  C  CG  . LEU A 1 376 ? 8.674   1.410   10.457  1.00 24.77  ? 376 LEU A CG  1 
ATOM   3065  C  CD1 . LEU A 1 376 ? 7.240   1.388   10.886  1.00 25.10  ? 376 LEU A CD1 1 
ATOM   3066  C  CD2 . LEU A 1 376 ? 9.416   2.581   11.195  1.00 28.57  ? 376 LEU A CD2 1 
ATOM   3067  N  N   . ASN A 1 377 ? 12.711  -1.377  10.984  1.00 22.07  ? 377 ASN A N   1 
ATOM   3068  C  CA  . ASN A 1 377 ? 13.542  -2.592  10.879  1.00 21.38  ? 377 ASN A CA  1 
ATOM   3069  C  C   . ASN A 1 377 ? 13.549  -3.318  12.229  1.00 22.08  ? 377 ASN A C   1 
ATOM   3070  O  O   . ASN A 1 377 ? 14.282  -2.953  13.164  1.00 23.13  ? 377 ASN A O   1 
ATOM   3071  C  CB  . ASN A 1 377 ? 14.925  -2.200  10.408  1.00 23.51  ? 377 ASN A CB  1 
ATOM   3072  C  CG  . ASN A 1 377 ? 15.877  -3.351  10.379  1.00 22.71  ? 377 ASN A CG  1 
ATOM   3073  O  OD1 . ASN A 1 377 ? 15.475  -4.528  10.457  1.00 23.05  ? 377 ASN A OD1 1 
ATOM   3074  N  ND2 . ASN A 1 377 ? 17.137  -3.031  10.165  1.00 25.12  ? 377 ASN A ND2 1 
ATOM   3075  N  N   . ARG A 1 378 ? 12.699  -4.328  12.337  1.00 20.50  ? 378 ARG A N   1 
ATOM   3076  C  CA  . ARG A 1 378 ? 12.592  -5.099  13.566  1.00 22.69  ? 378 ARG A CA  1 
ATOM   3077  C  C   . ARG A 1 378 ? 13.856  -5.895  13.884  1.00 23.41  ? 378 ARG A C   1 
ATOM   3078  O  O   . ARG A 1 378 ? 13.944  -6.487  14.958  1.00 23.10  ? 378 ARG A O   1 
ATOM   3079  C  CB  . ARG A 1 378 ? 11.445  -6.070  13.456  1.00 24.10  ? 378 ARG A CB  1 
ATOM   3080  C  CG  . ARG A 1 378 ? 10.108  -5.428  13.240  1.00 26.71  ? 378 ARG A CG  1 
ATOM   3081  C  CD  . ARG A 1 378 ? 9.037   -6.483  13.127  1.00 30.94  ? 378 ARG A CD  1 
ATOM   3082  N  NE  . ARG A 1 378 ? 7.708   -5.907  13.189  1.00 32.46  ? 378 ARG A NE  1 
ATOM   3083  C  CZ  . ARG A 1 378 ? 7.052   -5.571  14.289  1.00 33.61  ? 378 ARG A CZ  1 
ATOM   3084  N  NH1 . ARG A 1 378 ? 7.531   -5.833  15.500  1.00 34.71  ? 378 ARG A NH1 1 
ATOM   3085  N  NH2 . ARG A 1 378 ? 5.870   -4.972  14.170  1.00 37.01  ? 378 ARG A NH2 1 
ATOM   3086  N  N   . GLY A 1 379 ? 14.789  -5.953  12.977  1.00 21.48  ? 379 GLY A N   1 
ATOM   3087  C  CA  . GLY A 1 379 ? 15.995  -6.758  13.098  1.00 22.86  ? 379 GLY A CA  1 
ATOM   3088  C  C   . GLY A 1 379 ? 17.155  -6.046  13.743  1.00 22.63  ? 379 GLY A C   1 
ATOM   3089  O  O   . GLY A 1 379 ? 18.192  -6.665  14.007  1.00 23.13  ? 379 GLY A O   1 
ATOM   3090  N  N   . CYS A 1 380 ? 17.015  -4.732  14.079  1.00 23.77  ? 380 CYS A N   1 
ATOM   3091  C  CA  . CYS A 1 380 ? 18.169  -3.937  14.488  1.00 20.72  ? 380 CYS A CA  1 
ATOM   3092  C  C   . CYS A 1 380 ? 17.691  -2.878  15.473  1.00 21.17  ? 380 CYS A C   1 
ATOM   3093  O  O   . CYS A 1 380 ? 17.241  -1.800  15.036  1.00 23.18  ? 380 CYS A O   1 
ATOM   3094  C  CB  . CYS A 1 380 ? 18.774  -3.264  13.264  1.00 23.29  ? 380 CYS A CB  1 
ATOM   3095  S  SG  . CYS A 1 380 ? 20.140  -2.159  13.638  1.00 21.39  ? 380 CYS A SG  1 
ATOM   3096  N  N   . GLU A 1 381 ? 17.796  -3.147  16.782  1.00 20.16  ? 381 GLU A N   1 
ATOM   3097  C  CA  . GLU A 1 381 ? 17.453  -2.088  17.744  1.00 21.40  ? 381 GLU A CA  1 
ATOM   3098  C  C   . GLU A 1 381 ? 18.320  -0.833  17.556  1.00 21.16  ? 381 GLU A C   1 
ATOM   3099  O  O   . GLU A 1 381 ? 17.819  0.296   17.674  1.00 21.74  ? 381 GLU A O   1 
ATOM   3100  C  CB  . GLU A 1 381 ? 17.541  -2.593  19.212  1.00 22.08  ? 381 GLU A CB  1 
ATOM   3101  C  CG  . GLU A 1 381 ? 18.984  -3.091  19.703  1.00 24.10  ? 381 GLU A CG  1 
ATOM   3102  C  CD  . GLU A 1 381 ? 19.178  -3.157  21.195  1.00 26.05  ? 381 GLU A CD  1 
ATOM   3103  O  OE1 . GLU A 1 381 ? 20.108  -3.942  21.624  1.00 24.95  ? 381 GLU A OE1 1 
ATOM   3104  O  OE2 . GLU A 1 381 ? 18.425  -2.458  21.931  1.00 26.01  ? 381 GLU A OE2 1 
ATOM   3105  N  N   . GLY A 1 382 ? 19.604  -0.999  17.295  1.00 23.70  ? 382 GLY A N   1 
ATOM   3106  C  CA  . GLY A 1 382 ? 20.526  0.144   17.349  1.00 22.38  ? 382 GLY A CA  1 
ATOM   3107  C  C   . GLY A 1 382 ? 20.211  1.242   16.346  1.00 24.04  ? 382 GLY A C   1 
ATOM   3108  O  O   . GLY A 1 382 ? 20.231  2.438   16.697  1.00 21.06  ? 382 GLY A O   1 
ATOM   3109  N  N   . LEU A 1 383 ? 19.884  0.860   15.103  1.00 23.29  ? 383 LEU A N   1 
ATOM   3110  C  CA  . LEU A 1 383 ? 19.621  1.857   14.066  1.00 21.26  ? 383 LEU A CA  1 
ATOM   3111  C  C   . LEU A 1 383 ? 18.142  2.214   13.989  1.00 23.52  ? 383 LEU A C   1 
ATOM   3112  O  O   . LEU A 1 383 ? 17.799  3.198   13.305  1.00 23.61  ? 383 LEU A O   1 
ATOM   3113  C  CB  . LEU A 1 383 ? 20.140  1.358   12.697  1.00 21.73  ? 383 LEU A CB  1 
ATOM   3114  C  CG  . LEU A 1 383 ? 21.668  1.147   12.720  1.00 22.52  ? 383 LEU A CG  1 
ATOM   3115  C  CD1 . LEU A 1 383 ? 22.164  0.822   11.289  1.00 24.51  ? 383 LEU A CD1 1 
ATOM   3116  C  CD2 . LEU A 1 383 ? 22.426  2.394   13.208  1.00 24.41  ? 383 LEU A CD2 1 
ATOM   3117  N  N   . SER A 1 384 ? 17.262  1.471   14.696  1.00 21.14  ? 384 SER A N   1 
ATOM   3118  C  CA  . SER A 1 384 ? 15.832  1.762   14.701  1.00 21.11  ? 384 SER A CA  1 
ATOM   3119  C  C   . SER A 1 384 ? 15.405  2.648   15.877  1.00 24.65  ? 384 SER A C   1 
ATOM   3120  O  O   . SER A 1 384 ? 14.295  3.187   15.840  1.00 24.32  ? 384 SER A O   1 
ATOM   3121  C  CB  . SER A 1 384 ? 15.016  0.438   14.699  1.00 23.45  ? 384 SER A CB  1 
ATOM   3122  O  OG  . SER A 1 384 ? 15.194  -0.223  13.443  1.00 23.51  ? 384 SER A OG  1 
ATOM   3123  N  N   . VAL A 1 385 ? 16.218  2.808   16.929  1.00 22.52  ? 385 VAL A N   1 
ATOM   3124  C  CA  . VAL A 1 385 ? 15.754  3.665   18.038  1.00 22.88  ? 385 VAL A CA  1 
ATOM   3125  C  C   . VAL A 1 385 ? 15.482  5.054   17.476  1.00 24.27  ? 385 VAL A C   1 
ATOM   3126  O  O   . VAL A 1 385 ? 16.250  5.559   16.638  1.00 23.71  ? 385 VAL A O   1 
ATOM   3127  C  CB  . VAL A 1 385 ? 16.745  3.747   19.219  1.00 25.01  ? 385 VAL A CB  1 
ATOM   3128  C  CG1 . VAL A 1 385 ? 16.706  2.436   20.091  1.00 26.09  ? 385 VAL A CG1 1 
ATOM   3129  C  CG2 . VAL A 1 385 ? 18.164  4.052   18.785  1.00 24.71  ? 385 VAL A CG2 1 
ATOM   3130  N  N   . GLY A 1 386 ? 14.341  5.642   17.892  1.00 24.66  ? 386 GLY A N   1 
ATOM   3131  C  CA  . GLY A 1 386 ? 13.970  6.998   17.440  1.00 22.30  ? 386 GLY A CA  1 
ATOM   3132  C  C   . GLY A 1 386 ? 13.281  7.070   16.094  1.00 25.12  ? 386 GLY A C   1 
ATOM   3133  O  O   . GLY A 1 386 ? 12.862  8.158   15.679  1.00 22.92  ? 386 GLY A O   1 
ATOM   3134  N  N   . ILE A 1 387 ? 13.115  5.940   15.397  1.00 23.23  ? 387 ILE A N   1 
ATOM   3135  C  CA  . ILE A 1 387 ? 12.667  6.009   14.013  1.00 25.32  ? 387 ILE A CA  1 
ATOM   3136  C  C   . ILE A 1 387 ? 11.303  6.684   13.902  1.00 23.94  ? 387 ILE A C   1 
ATOM   3137  O  O   . ILE A 1 387 ? 11.050  7.412   12.933  1.00 25.06  ? 387 ILE A O   1 
ATOM   3138  C  CB  . ILE A 1 387 ? 12.636  4.588   13.401  1.00 19.25  ? 387 ILE A CB  1 
ATOM   3139  C  CG1 . ILE A 1 387 ? 12.398  4.666   11.895  1.00 27.43  ? 387 ILE A CG1 1 
ATOM   3140  C  CG2 . ILE A 1 387 ? 11.574  3.690   14.052  1.00 25.48  ? 387 ILE A CG2 1 
ATOM   3141  C  CD1 . ILE A 1 387 ? 13.347  5.558   11.160  1.00 31.28  ? 387 ILE A CD1 1 
ATOM   3142  N  N   . MET A 1 388 ? 10.394  6.479   14.886  1.00 23.28  ? 388 MET A N   1 
ATOM   3143  C  CA  . MET A 1 388 ? 9.075   7.103   14.738  1.00 24.46  ? 388 MET A CA  1 
ATOM   3144  C  C   . MET A 1 388 ? 9.134   8.616   14.969  1.00 22.98  ? 388 MET A C   1 
ATOM   3145  O  O   . MET A 1 388 ? 8.378   9.360   14.340  1.00 26.79  ? 388 MET A O   1 
ATOM   3146  C  CB  . MET A 1 388 ? 8.014   6.477   15.659  1.00 28.65  ? 388 MET A CB  1 
ATOM   3147  C  CG  . MET A 1 388 ? 7.867   4.961   15.503  1.00 28.00  ? 388 MET A CG  1 
ATOM   3148  S  SD  . MET A 1 388 ? 7.313   4.574   13.795  1.00 34.13  ? 388 MET A SD  1 
ATOM   3149  C  CE  . MET A 1 388 ? 5.842   5.567   13.657  1.00 32.79  ? 388 MET A CE  1 
ATOM   3150  N  N   . GLU A 1 389 ? 10.084  9.103   15.773  1.00 25.04  ? 389 GLU A N   1 
ATOM   3151  C  CA  . GLU A 1 389 ? 10.248  10.549  15.885  1.00 24.39  ? 389 GLU A CA  1 
ATOM   3152  C  C   . GLU A 1 389 ? 10.825  11.120  14.590  1.00 22.62  ? 389 GLU A C   1 
ATOM   3153  O  O   . GLU A 1 389 ? 10.480  12.225  14.191  1.00 23.57  ? 389 GLU A O   1 
ATOM   3154  C  CB  . GLU A 1 389 ? 11.131  10.899  17.106  1.00 24.82  ? 389 GLU A CB  1 
ATOM   3155  C  CG  . GLU A 1 389 ? 10.508  10.511  18.501  1.00 26.52  ? 389 GLU A CG  1 
ATOM   3156  C  CD  . GLU A 1 389 ? 9.285   11.387  18.899  1.00 27.39  ? 389 GLU A CD  1 
ATOM   3157  O  OE1 . GLU A 1 389 ? 9.021   12.495  18.309  1.00 26.58  ? 389 GLU A OE1 1 
ATOM   3158  O  OE2 . GLU A 1 389 ? 8.580   10.985  19.839  1.00 26.90  ? 389 GLU A OE2 1 
ATOM   3159  N  N   . ASN A 1 390 ? 11.706  10.364  13.923  1.00 23.73  ? 390 ASN A N   1 
ATOM   3160  C  CA  . ASN A 1 390 ? 12.204  10.779  12.607  1.00 23.85  ? 390 ASN A CA  1 
ATOM   3161  C  C   . ASN A 1 390 ? 11.064  10.882  11.592  1.00 23.86  ? 390 ASN A C   1 
ATOM   3162  O  O   . ASN A 1 390 ? 10.967  11.871  10.846  1.00 23.49  ? 390 ASN A O   1 
ATOM   3163  C  CB  . ASN A 1 390 ? 13.261  9.784   12.117  1.00 24.16  ? 390 ASN A CB  1 
ATOM   3164  C  CG  . ASN A 1 390 ? 14.483  9.637   13.047  1.00 25.26  ? 390 ASN A CG  1 
ATOM   3165  O  OD1 . ASN A 1 390 ? 15.048  8.550   13.112  1.00 25.07  ? 390 ASN A OD1 1 
ATOM   3166  N  ND2 . ASN A 1 390 ? 14.888  10.719  13.769  1.00 21.94  ? 390 ASN A ND2 1 
ATOM   3167  N  N   A ARG A 1 391 ? 10.179  9.874   11.565  0.49 24.21  ? 391 ARG A N   1 
ATOM   3168  N  N   B ARG A 1 391 ? 10.171  9.874   11.561  0.51 24.22  ? 391 ARG A N   1 
ATOM   3169  C  CA  A ARG A 1 391 ? 9.016   9.927   10.679  0.49 24.97  ? 391 ARG A CA  1 
ATOM   3170  C  CA  B ARG A 1 391 ? 9.016   9.946   10.662  0.51 24.96  ? 391 ARG A CA  1 
ATOM   3171  C  C   A ARG A 1 391 ? 8.171   11.168  10.940  0.49 26.14  ? 391 ARG A C   1 
ATOM   3172  C  C   B ARG A 1 391 ? 8.158   11.171  10.940  0.51 26.14  ? 391 ARG A C   1 
ATOM   3173  O  O   A ARG A 1 391 ? 7.733   11.853  10.001  0.49 24.04  ? 391 ARG A O   1 
ATOM   3174  O  O   B ARG A 1 391 ? 7.714   11.860  10.006  0.51 24.04  ? 391 ARG A O   1 
ATOM   3175  C  CB  A ARG A 1 391 ? 8.165   8.672   10.872  0.49 27.60  ? 391 ARG A CB  1 
ATOM   3176  C  CB  B ARG A 1 391 ? 8.169   8.669   10.770  0.51 27.61  ? 391 ARG A CB  1 
ATOM   3177  C  CG  A ARG A 1 391 ? 7.126   8.475   9.801   0.49 28.67  ? 391 ARG A CG  1 
ATOM   3178  C  CG  B ARG A 1 391 ? 6.989   8.675   9.809   0.51 28.68  ? 391 ARG A CG  1 
ATOM   3179  C  CD  A ARG A 1 391 ? 6.022   7.630   10.347  0.49 30.19  ? 391 ARG A CD  1 
ATOM   3180  C  CD  B ARG A 1 391 ? 5.976   7.587   10.101  0.51 30.25  ? 391 ARG A CD  1 
ATOM   3181  N  NE  A ARG A 1 391 ? 5.307   8.415   11.344  0.49 30.95  ? 391 ARG A NE  1 
ATOM   3182  N  NE  B ARG A 1 391 ? 5.026   7.920   11.148  0.51 30.74  ? 391 ARG A NE  1 
ATOM   3183  C  CZ  A ARG A 1 391 ? 4.444   9.375   11.042  0.49 31.11  ? 391 ARG A CZ  1 
ATOM   3184  C  CZ  B ARG A 1 391 ? 3.909   7.249   11.395  0.51 30.33  ? 391 ARG A CZ  1 
ATOM   3185  N  NH1 A ARG A 1 391 ? 4.064   9.595   9.790   0.49 28.63  ? 391 ARG A NH1 1 
ATOM   3186  N  NH1 B ARG A 1 391 ? 3.544   6.200   10.657  0.51 30.68  ? 391 ARG A NH1 1 
ATOM   3187  N  NH2 A ARG A 1 391 ? 3.954   10.134  12.015  0.49 29.88  ? 391 ARG A NH2 1 
ATOM   3188  N  NH2 B ARG A 1 391 ? 3.142   7.633   12.404  0.51 34.37  ? 391 ARG A NH2 1 
ATOM   3189  N  N   . LEU A 1 392 ? 7.888   11.445  12.220  1.00 25.15  ? 392 LEU A N   1 
ATOM   3190  C  CA  . LEU A 1 392 ? 7.102   12.616  12.571  1.00 24.57  ? 392 LEU A CA  1 
ATOM   3191  C  C   . LEU A 1 392 ? 7.762   13.896  12.067  1.00 23.89  ? 392 LEU A C   1 
ATOM   3192  O  O   . LEU A 1 392 ? 7.084   14.781  11.536  1.00 25.68  ? 392 LEU A O   1 
ATOM   3193  C  CB  . LEU A 1 392 ? 6.908   12.650  14.088  1.00 24.36  ? 392 LEU A CB  1 
ATOM   3194  C  CG  . LEU A 1 392 ? 5.977   13.749  14.589  1.00 28.00  ? 392 LEU A CG  1 
ATOM   3195  C  CD1 . LEU A 1 392 ? 4.520   13.614  14.018  1.00 30.24  ? 392 LEU A CD1 1 
ATOM   3196  C  CD2 . LEU A 1 392 ? 5.978   13.819  16.139  1.00 29.60  ? 392 LEU A CD2 1 
ATOM   3197  N  N   . ALA A 1 393 ? 9.081   14.019  12.223  1.00 22.03  ? 393 ALA A N   1 
ATOM   3198  C  CA  . ALA A 1 393 ? 9.732   15.252  11.825  1.00 21.60  ? 393 ALA A CA  1 
ATOM   3199  C  C   . ALA A 1 393 ? 9.662   15.440  10.304  1.00 26.11  ? 393 ALA A C   1 
ATOM   3200  O  O   . ALA A 1 393 ? 9.449   16.558  9.796   1.00 25.43  ? 393 ALA A O   1 
ATOM   3201  C  CB  . ALA A 1 393 ? 11.199  15.251  12.337  1.00 24.08  ? 393 ALA A CB  1 
ATOM   3202  N  N   . ILE A 1 394 ? 9.808   14.343  9.558   1.00 22.25  ? 394 ILE A N   1 
ATOM   3203  C  CA  . ILE A 1 394 ? 9.691   14.442  8.102   1.00 20.69  ? 394 ILE A CA  1 
ATOM   3204  C  C   . ILE A 1 394 ? 8.243   14.718  7.729   1.00 20.93  ? 394 ILE A C   1 
ATOM   3205  O  O   . ILE A 1 394 ? 7.963   15.546  6.858   1.00 24.43  ? 394 ILE A O   1 
ATOM   3206  C  CB  . ILE A 1 394 ? 10.228  13.153  7.438   1.00 23.28  ? 394 ILE A CB  1 
ATOM   3207  C  CG1 . ILE A 1 394 ? 11.719  12.954  7.734   1.00 23.92  ? 394 ILE A CG1 1 
ATOM   3208  C  CG2 . ILE A 1 394 ? 9.901   13.200  5.837   1.00 23.57  ? 394 ILE A CG2 1 
ATOM   3209  C  CD1 . ILE A 1 394 ? 12.208  11.540  7.271   1.00 24.05  ? 394 ILE A CD1 1 
ATOM   3210  N  N   . ALA A 1 395 ? 7.298   14.096  8.432   1.00 24.53  ? 395 ALA A N   1 
ATOM   3211  C  CA  . ALA A 1 395 ? 5.895   14.341  8.124   1.00 24.39  ? 395 ALA A CA  1 
ATOM   3212  C  C   . ALA A 1 395 ? 5.551   15.816  8.302   1.00 28.99  ? 395 ALA A C   1 
ATOM   3213  O  O   . ALA A 1 395 ? 4.844   16.406  7.481   1.00 29.06  ? 395 ALA A O   1 
ATOM   3214  C  CB  . ALA A 1 395 ? 5.006   13.454  9.005   1.00 25.34  ? 395 ALA A CB  1 
ATOM   3215  N  N   . LYS A 1 396 ? 6.067   16.433  9.355   1.00 26.27  ? 396 LYS A N   1 
ATOM   3216  C  CA  . LYS A 1 396 ? 5.725   17.818  9.587   1.00 27.35  ? 396 LYS A CA  1 
ATOM   3217  C  C   . LYS A 1 396 ? 6.330   18.735  8.538   1.00 27.92  ? 396 LYS A C   1 
ATOM   3218  O  O   . LYS A 1 396 ? 5.806   19.829  8.303   1.00 27.39  ? 396 LYS A O   1 
ATOM   3219  C  CB  . LYS A 1 396 ? 6.213   18.273  10.958  1.00 28.67  ? 396 LYS A CB  1 
ATOM   3220  C  CG  . LYS A 1 396 ? 5.519   17.602  12.130  1.00 32.41  ? 396 LYS A CG  1 
ATOM   3221  C  CD  . LYS A 1 396 ? 6.051   18.190  13.439  1.00 32.74  ? 396 LYS A CD  1 
ATOM   3222  C  CE  . LYS A 1 396 ? 5.357   17.565  14.635  1.00 38.34  ? 396 LYS A CE  1 
ATOM   3223  N  NZ  . LYS A 1 396 ? 5.902   18.042  15.945  1.00 38.21  ? 396 LYS A NZ  1 
ATOM   3224  N  N   . SER A 1 397 ? 7.474   18.345  7.975   1.00 29.63  ? 397 SER A N   1 
ATOM   3225  C  CA  . SER A 1 397 ? 8.203   19.199  7.048   1.00 29.29  ? 397 SER A CA  1 
ATOM   3226  C  C   . SER A 1 397 ? 7.480   19.352  5.716   1.00 29.98  ? 397 SER A C   1 
ATOM   3227  O  O   . SER A 1 397 ? 7.803   20.291  4.958   1.00 29.01  ? 397 SER A O   1 
ATOM   3228  C  CB  . SER A 1 397 ? 9.596   18.623  6.812   1.00 26.18  ? 397 SER A CB  1 
ATOM   3229  O  OG  . SER A 1 397 ? 9.532   17.507  5.904   1.00 28.78  ? 397 SER A OG  1 
ATOM   3230  N  N   . GLY A 1 398 ? 6.517   18.453  5.411   1.00 29.81  ? 398 GLY A N   1 
ATOM   3231  C  CA  . GLY A 1 398 ? 5.770   18.468  4.161   1.00 29.07  ? 398 GLY A CA  1 
ATOM   3232  C  C   . GLY A 1 398 ? 6.315   17.582  3.057   1.00 27.75  ? 398 GLY A C   1 
ATOM   3233  O  O   . GLY A 1 398 ? 5.674   17.469  1.995   1.00 29.34  ? 398 GLY A O   1 
ATOM   3234  N  N   . THR A 1 399 ? 7.435   16.923  3.277   1.00 26.92  ? 399 THR A N   1 
ATOM   3235  C  CA  . THR A 1 399 ? 7.912   15.912  2.349   1.00 26.65  ? 399 THR A CA  1 
ATOM   3236  C  C   . THR A 1 399 ? 7.104   14.622  2.501   1.00 26.23  ? 399 THR A C   1 
ATOM   3237  O  O   . THR A 1 399 ? 6.883   14.171  3.632   1.00 24.85  ? 399 THR A O   1 
ATOM   3238  C  CB  . THR A 1 399 ? 9.399   15.661  2.619   1.00 25.85  ? 399 THR A CB  1 
ATOM   3239  O  OG1 . THR A 1 399 ? 10.121  16.842  2.246   1.00 27.94  ? 399 THR A OG1 1 
ATOM   3240  C  CG2 . THR A 1 399 ? 9.910   14.452  1.829   1.00 24.10  ? 399 THR A CG2 1 
ATOM   3241  N  N   . PRO A 1 400 ? 6.641   14.022  1.401   1.00 23.58  ? 400 PRO A N   1 
ATOM   3242  C  CA  . PRO A 1 400 ? 5.922   12.740  1.490   1.00 23.92  ? 400 PRO A CA  1 
ATOM   3243  C  C   . PRO A 1 400 ? 6.804   11.681  2.136   1.00 25.37  ? 400 PRO A C   1 
ATOM   3244  O  O   . PRO A 1 400 ? 8.002   11.561  1.829   1.00 22.99  ? 400 PRO A O   1 
ATOM   3245  C  CB  . PRO A 1 400 ? 5.603   12.395  0.024   1.00 28.14  ? 400 PRO A CB  1 
ATOM   3246  C  CG  . PRO A 1 400 ? 5.672   13.792  -0.694  1.00 28.03  ? 400 PRO A CG  1 
ATOM   3247  C  CD  . PRO A 1 400 ? 6.716   14.534  0.019   1.00 26.40  ? 400 PRO A CD  1 
ATOM   3248  N  N   . VAL A 1 401 ? 6.181   10.887  2.996   1.00 24.43  ? 401 VAL A N   1 
ATOM   3249  C  CA  . VAL A 1 401 ? 6.926   9.844   3.696   1.00 24.75  ? 401 VAL A CA  1 
ATOM   3250  C  C   . VAL A 1 401 ? 6.010   8.679   3.998   1.00 22.77  ? 401 VAL A C   1 
ATOM   3251  O  O   . VAL A 1 401 ? 4.831   8.851   4.345   1.00 25.67  ? 401 VAL A O   1 
ATOM   3252  C  CB  . VAL A 1 401 ? 7.603   10.398  4.961   1.00 23.83  ? 401 VAL A CB  1 
ATOM   3253  C  CG1 . VAL A 1 401 ? 6.627   11.080  5.874   1.00 25.84  ? 401 VAL A CG1 1 
ATOM   3254  C  CG2 . VAL A 1 401 ? 8.356   9.241   5.758   1.00 24.09  ? 401 VAL A CG2 1 
ATOM   3255  N  N   A MET A 1 402 ? 6.542   7.471   3.803   0.35 22.74  ? 402 MET A N   1 
ATOM   3256  N  N   B MET A 1 402 ? 6.551   7.479   3.823   0.65 22.69  ? 402 MET A N   1 
ATOM   3257  C  CA  A MET A 1 402 ? 5.834   6.234   4.115   0.35 24.18  ? 402 MET A CA  1 
ATOM   3258  C  CA  B MET A 1 402 ? 5.839   6.253   4.151   0.65 24.16  ? 402 MET A CA  1 
ATOM   3259  C  C   A MET A 1 402 ? 6.765   5.295   4.871   0.35 24.06  ? 402 MET A C   1 
ATOM   3260  C  C   B MET A 1 402 ? 6.767   5.347   4.952   0.65 24.06  ? 402 MET A C   1 
ATOM   3261  O  O   A MET A 1 402 ? 7.998   5.424   4.820   0.35 23.88  ? 402 MET A O   1 
ATOM   3262  O  O   B MET A 1 402 ? 7.995   5.541   4.998   0.65 23.77  ? 402 MET A O   1 
ATOM   3263  C  CB  A MET A 1 402 ? 5.286   5.538   2.843   0.35 25.04  ? 402 MET A CB  1 
ATOM   3264  C  CB  B MET A 1 402 ? 5.338   5.533   2.873   0.65 25.07  ? 402 MET A CB  1 
ATOM   3265  C  CG  A MET A 1 402 ? 6.312   5.262   1.713   0.35 24.77  ? 402 MET A CG  1 
ATOM   3266  C  CG  B MET A 1 402 ? 6.472   5.132   1.891   0.65 24.78  ? 402 MET A CG  1 
ATOM   3267  S  SD  A MET A 1 402 ? 6.389   3.557   1.129   0.35 31.42  ? 402 MET A SD  1 
ATOM   3268  S  SD  B MET A 1 402 ? 7.213   3.556   2.351   0.65 22.67  ? 402 MET A SD  1 
ATOM   3269  C  CE  A MET A 1 402 ? 7.717   2.967   2.143   0.35 25.13  ? 402 MET A CE  1 
ATOM   3270  C  CE  B MET A 1 402 ? 5.911   2.373   1.890   0.65 22.64  ? 402 MET A CE  1 
ATOM   3271  N  N   . THR A 1 403 ? 6.156   4.368   5.614   1.00 24.12  ? 403 THR A N   1 
ATOM   3272  C  CA  . THR A 1 403 ? 6.907   3.334   6.323   1.00 22.35  ? 403 THR A CA  1 
ATOM   3273  C  C   . THR A 1 403 ? 6.527   1.975   5.768   1.00 23.14  ? 403 THR A C   1 
ATOM   3274  O  O   . THR A 1 403 ? 5.441   1.783   5.234   1.00 24.32  ? 403 THR A O   1 
ATOM   3275  C  CB  . THR A 1 403 ? 6.628   3.337   7.828   1.00 23.84  ? 403 THR A CB  1 
ATOM   3276  O  OG1 . THR A 1 403 ? 5.223   3.108   8.042   1.00 25.08  ? 403 THR A OG1 1 
ATOM   3277  C  CG2 . THR A 1 403 ? 7.080   4.657   8.412   1.00 24.67  ? 403 THR A CG2 1 
ATOM   3278  N  N   . PHE A 1 404 ? 7.420   1.020   5.971   1.00 22.19  ? 404 PHE A N   1 
ATOM   3279  C  CA  . PHE A 1 404 ? 7.126   -0.389  5.771   1.00 24.62  ? 404 PHE A CA  1 
ATOM   3280  C  C   . PHE A 1 404 ? 7.900   -1.146  6.839   1.00 26.70  ? 404 PHE A C   1 
ATOM   3281  O  O   . PHE A 1 404 ? 9.003   -0.747  7.223   1.00 24.64  ? 404 PHE A O   1 
ATOM   3282  C  CB  . PHE A 1 404 ? 7.523   -0.880  4.371   1.00 26.58  ? 404 PHE A CB  1 
ATOM   3283  C  CG  . PHE A 1 404 ? 9.004   -0.793  4.074   1.00 27.82  ? 404 PHE A CG  1 
ATOM   3284  C  CD1 . PHE A 1 404 ? 9.575   0.395   3.605   1.00 27.77  ? 404 PHE A CD1 1 
ATOM   3285  C  CD2 . PHE A 1 404 ? 9.828   -1.909  4.266   1.00 27.59  ? 404 PHE A CD2 1 
ATOM   3286  C  CE1 . PHE A 1 404 ? 10.951  0.503   3.333   1.00 30.09  ? 404 PHE A CE1 1 
ATOM   3287  C  CE2 . PHE A 1 404 ? 11.209  -1.835  4.007   1.00 27.10  ? 404 PHE A CE2 1 
ATOM   3288  C  CZ  . PHE A 1 404 ? 11.787  -0.649  3.515   1.00 28.98  ? 404 PHE A CZ  1 
ATOM   3289  N  N   . GLU A 1 405 ? 7.311   -2.222  7.335   1.00 25.50  ? 405 GLU A N   1 
ATOM   3290  C  CA  . GLU A 1 405 ? 7.999   -3.023  8.338   1.00 26.95  ? 405 GLU A CA  1 
ATOM   3291  C  C   . GLU A 1 405 ? 8.878   -4.084  7.686   1.00 25.07  ? 405 GLU A C   1 
ATOM   3292  O  O   . GLU A 1 405 ? 8.560   -4.616  6.628   1.00 26.92  ? 405 GLU A O   1 
ATOM   3293  C  CB  . GLU A 1 405 ? 6.989   -3.697  9.273   1.00 28.97  ? 405 GLU A CB  1 
ATOM   3294  C  CG  . GLU A 1 405 ? 6.278   -2.679  10.154  1.00 32.41  ? 405 GLU A CG  1 
ATOM   3295  C  CD  . GLU A 1 405 ? 5.390   -3.290  11.210  1.00 39.92  ? 405 GLU A CD  1 
ATOM   3296  O  OE1 . GLU A 1 405 ? 5.649   -4.429  11.647  1.00 37.45  ? 405 GLU A OE1 1 
ATOM   3297  O  OE2 . GLU A 1 405 ? 4.453   -2.587  11.636  1.00 35.77  ? 405 GLU A OE2 1 
ATOM   3298  N  N   . GLY A 1 406 ? 10.026  -4.348  8.299   1.00 25.39  ? 406 GLY A N   1 
ATOM   3299  C  CA  . GLY A 1 406 ? 10.798  -5.466  7.834   1.00 24.90  ? 406 GLY A CA  1 
ATOM   3300  C  C   . GLY A 1 406 ? 11.791  -5.912  8.881   1.00 22.04  ? 406 GLY A C   1 
ATOM   3301  O  O   . GLY A 1 406 ? 11.638  -5.639  10.077  1.00 23.61  ? 406 GLY A O   1 
ATOM   3302  N  N   . ASN A 1 407 ? 12.740  -6.729  8.409   1.00 23.75  ? 407 ASN A N   1 
ATOM   3303  C  CA  . ASN A 1 407 ? 13.876  -7.178  9.210   1.00 21.94  ? 407 ASN A CA  1 
ATOM   3304  C  C   . ASN A 1 407 ? 15.009  -7.435  8.236   1.00 24.14  ? 407 ASN A C   1 
ATOM   3305  O  O   . ASN A 1 407 ? 14.876  -8.299  7.363   1.00 22.34  ? 407 ASN A O   1 
ATOM   3306  C  CB  . ASN A 1 407 ? 13.468  -8.485  9.984   1.00 20.95  ? 407 ASN A CB  1 
ATOM   3307  C  CG  . ASN A 1 407 ? 14.513  -8.918  10.940  1.00 21.64  ? 407 ASN A CG  1 
ATOM   3308  O  OD1 . ASN A 1 407 ? 15.679  -8.956  10.592  1.00 21.82  ? 407 ASN A OD1 1 
ATOM   3309  N  ND2 . ASN A 1 407 ? 14.086  -9.322  12.167  1.00 20.55  ? 407 ASN A ND2 1 
ATOM   3310  N  N   . MET A 1 408 ? 16.141  -6.742  8.371   1.00 23.18  ? 408 MET A N   1 
ATOM   3311  C  CA  . MET A 1 408 ? 17.185  -6.785  7.357   1.00 22.28  ? 408 MET A CA  1 
ATOM   3312  C  C   . MET A 1 408 ? 17.798  -8.170  7.291   1.00 23.07  ? 408 MET A C   1 
ATOM   3313  O  O   . MET A 1 408 ? 18.245  -8.596  6.232   1.00 25.23  ? 408 MET A O   1 
ATOM   3314  C  CB  . MET A 1 408 ? 18.290  -5.777  7.671   1.00 24.27  ? 408 MET A CB  1 
ATOM   3315  C  CG  . MET A 1 408 ? 19.272  -6.095  8.799   1.00 25.95  ? 408 MET A CG  1 
ATOM   3316  S  SD  . MET A 1 408 ? 18.607  -6.162  10.464  1.00 22.95  ? 408 MET A SD  1 
ATOM   3317  C  CE  . MET A 1 408 ? 20.144  -6.479  11.241  1.00 22.30  ? 408 MET A CE  1 
ATOM   3318  N  N   . GLY A 1 409 ? 17.830  -8.873  8.418   1.00 22.78  ? 409 GLY A N   1 
ATOM   3319  C  CA  . GLY A 1 409 ? 18.492  -10.162 8.378   1.00 24.63  ? 409 GLY A CA  1 
ATOM   3320  C  C   . GLY A 1 409 ? 17.581  -11.375 8.400   1.00 26.16  ? 409 GLY A C   1 
ATOM   3321  O  O   . GLY A 1 409 ? 18.021  -12.453 7.962   1.00 27.37  ? 409 GLY A O   1 
ATOM   3322  N  N   . ASP A 1 410 ? 16.328  -11.236 8.832   1.00 22.96  ? 410 ASP A N   1 
ATOM   3323  C  CA  . ASP A 1 410 ? 15.432  -12.385 9.056   1.00 22.72  ? 410 ASP A CA  1 
ATOM   3324  C  C   . ASP A 1 410 ? 14.178  -12.161 8.241   1.00 24.16  ? 410 ASP A C   1 
ATOM   3325  O  O   . ASP A 1 410 ? 13.262  -11.463 8.682   1.00 24.41  ? 410 ASP A O   1 
ATOM   3326  C  CB  . ASP A 1 410 ? 15.098  -12.540 10.541  1.00 23.50  ? 410 ASP A CB  1 
ATOM   3327  C  CG  . ASP A 1 410 ? 14.405  -13.827 10.859  1.00 26.58  ? 410 ASP A CG  1 
ATOM   3328  O  OD1 . ASP A 1 410 ? 13.914  -14.468 9.891   1.00 26.34  ? 410 ASP A OD1 1 
ATOM   3329  O  OD2 . ASP A 1 410 ? 14.338  -14.143 12.091  1.00 25.37  ? 410 ASP A OD2 1 
ATOM   3330  N  N   A GLU A 1 411 ? 14.102  -12.782 7.059   0.53 26.02  ? 411 GLU A N   1 
ATOM   3331  N  N   B GLU A 1 411 ? 14.136  -12.788 7.056   0.47 26.02  ? 411 GLU A N   1 
ATOM   3332  C  CA  A GLU A 1 411 ? 12.958  -12.451 6.220   0.53 28.39  ? 411 GLU A CA  1 
ATOM   3333  C  CA  B GLU A 1 411 ? 13.008  -12.618 6.147   0.47 28.44  ? 411 GLU A CA  1 
ATOM   3334  C  C   A GLU A 1 411 ? 11.651  -13.080 6.722   0.53 26.78  ? 411 GLU A C   1 
ATOM   3335  C  C   B GLU A 1 411 ? 11.672  -13.054 6.747   0.47 26.79  ? 411 GLU A C   1 
ATOM   3336  O  O   A GLU A 1 411 ? 10.587  -12.884 6.104   0.53 26.44  ? 411 GLU A O   1 
ATOM   3337  O  O   B GLU A 1 411 ? 10.610  -12.695 6.214   0.47 26.56  ? 411 GLU A O   1 
ATOM   3338  C  CB  A GLU A 1 411 ? 13.279  -12.855 4.773   0.53 30.86  ? 411 GLU A CB  1 
ATOM   3339  C  CB  B GLU A 1 411 ? 13.289  -13.371 4.834   0.47 29.61  ? 411 GLU A CB  1 
ATOM   3340  C  CG  A GLU A 1 411 ? 14.372  -11.936 4.234   0.53 31.27  ? 411 GLU A CG  1 
ATOM   3341  C  CG  B GLU A 1 411 ? 13.090  -14.864 4.870   0.47 32.22  ? 411 GLU A CG  1 
ATOM   3342  C  CD  A GLU A 1 411 ? 14.047  -11.194 2.940   0.53 32.80  ? 411 GLU A CD  1 
ATOM   3343  C  CD  B GLU A 1 411 ? 12.929  -15.475 3.461   0.47 35.47  ? 411 GLU A CD  1 
ATOM   3344  O  OE1 A GLU A 1 411 ? 12.945  -11.377 2.420   0.53 34.33  ? 411 GLU A OE1 1 
ATOM   3345  O  OE1 B GLU A 1 411 ? 13.392  -14.901 2.442   0.47 37.65  ? 411 GLU A OE1 1 
ATOM   3346  O  OE2 A GLU A 1 411 ? 14.902  -10.408 2.473   0.53 30.43  ? 411 GLU A OE2 1 
ATOM   3347  O  OE2 B GLU A 1 411 ? 12.325  -16.533 3.374   0.47 34.07  ? 411 GLU A OE2 1 
ATOM   3348  N  N   . ARG A 1 412 ? 11.681  -13.824 7.838   1.00 27.25  ? 412 ARG A N   1 
ATOM   3349  C  CA  . ARG A 1 412 ? 10.414  -14.232 8.442   1.00 27.38  ? 412 ARG A CA  1 
ATOM   3350  C  C   . ARG A 1 412 ? 9.607   -13.031 8.861   1.00 27.90  ? 412 ARG A C   1 
ATOM   3351  O  O   . ARG A 1 412 ? 8.379   -13.129 8.978   1.00 26.90  ? 412 ARG A O   1 
ATOM   3352  C  CB  . ARG A 1 412 ? 10.640  -15.112 9.687   1.00 28.02  ? 412 ARG A CB  1 
ATOM   3353  C  CG  . ARG A 1 412 ? 11.064  -16.509 9.289   1.00 30.23  ? 412 ARG A CG  1 
ATOM   3354  C  CD  . ARG A 1 412 ? 11.417  -17.346 10.529  1.00 29.24  ? 412 ARG A CD  1 
ATOM   3355  N  NE  . ARG A 1 412 ? 12.666  -16.879 11.135  1.00 27.37  ? 412 ARG A NE  1 
ATOM   3356  C  CZ  . ARG A 1 412 ? 13.379  -17.575 12.018  1.00 28.47  ? 412 ARG A CZ  1 
ATOM   3357  N  NH1 . ARG A 1 412 ? 13.005  -18.782 12.405  1.00 27.96  ? 412 ARG A NH1 1 
ATOM   3358  N  NH2 . ARG A 1 412 ? 14.500  -17.045 12.517  1.00 28.26  ? 412 ARG A NH2 1 
ATOM   3359  N  N   . GLU A 1 413 ? 10.285  -11.908 9.120   1.00 25.52  ? 413 GLU A N   1 
ATOM   3360  C  CA  . GLU A 1 413 ? 9.643   -10.666 9.546   1.00 26.56  ? 413 GLU A CA  1 
ATOM   3361  C  C   . GLU A 1 413 ? 9.604   -9.643  8.429   1.00 27.98  ? 413 GLU A C   1 
ATOM   3362  O  O   . GLU A 1 413 ? 9.452   -8.449  8.680   1.00 26.63  ? 413 GLU A O   1 
ATOM   3363  C  CB  . GLU A 1 413 ? 10.335  -10.092 10.786  1.00 24.87  ? 413 GLU A CB  1 
ATOM   3364  C  CG  . GLU A 1 413 ? 10.052  -10.975 12.022  1.00 26.88  ? 413 GLU A CG  1 
ATOM   3365  C  CD  . GLU A 1 413 ? 10.538  -10.336 13.328  1.00 32.62  ? 413 GLU A CD  1 
ATOM   3366  O  OE1 . GLU A 1 413 ? 11.530  -9.585  13.294  1.00 28.92  ? 413 GLU A OE1 1 
ATOM   3367  O  OE2 . GLU A 1 413 ? 9.969   -10.663 14.409  1.00 36.20  ? 413 GLU A OE2 1 
ATOM   3368  N  N   . PHE A 1 414 ? 9.654   -10.087 7.189   1.00 23.46  ? 414 PHE A N   1 
ATOM   3369  C  CA  . PHE A 1 414 ? 9.455   -9.172  6.054   1.00 25.55  ? 414 PHE A CA  1 
ATOM   3370  C  C   . PHE A 1 414 ? 8.399   -9.732  5.098   1.00 32.04  ? 414 PHE A C   1 
ATOM   3371  O  O   . PHE A 1 414 ? 8.518   -10.869 4.613   1.00 29.88  ? 414 PHE A O   1 
ATOM   3372  C  CB  . PHE A 1 414 ? 10.781  -8.930  5.321   1.00 26.39  ? 414 PHE A CB  1 
ATOM   3373  C  CG  . PHE A 1 414 ? 10.644  -8.043  4.082   1.00 28.27  ? 414 PHE A CG  1 
ATOM   3374  C  CD1 . PHE A 1 414 ? 10.251  -6.694  4.213   1.00 28.12  ? 414 PHE A CD1 1 
ATOM   3375  C  CD2 . PHE A 1 414 ? 10.900  -8.550  2.811   1.00 30.72  ? 414 PHE A CD2 1 
ATOM   3376  C  CE1 . PHE A 1 414 ? 10.123  -5.887  3.088   1.00 29.18  ? 414 PHE A CE1 1 
ATOM   3377  C  CE2 . PHE A 1 414 ? 10.769  -7.746  1.681   1.00 31.86  ? 414 PHE A CE2 1 
ATOM   3378  C  CZ  . PHE A 1 414 ? 10.391  -6.394  1.829   1.00 30.26  ? 414 PHE A CZ  1 
ATOM   3379  N  N   . ASP A 1 415 ? 7.367   -8.942  4.817   1.00 27.38  ? 415 ASP A N   1 
ATOM   3380  C  CA  . ASP A 1 415 ? 6.262   -9.346  3.970   1.00 32.94  ? 415 ASP A CA  1 
ATOM   3381  C  C   . ASP A 1 415 ? 6.504   -8.665  2.627   1.00 33.16  ? 415 ASP A C   1 
ATOM   3382  O  O   . ASP A 1 415 ? 6.242   -7.467  2.470   1.00 30.09  ? 415 ASP A O   1 
ATOM   3383  C  CB  . ASP A 1 415 ? 4.928   -8.936  4.593   1.00 35.06  ? 415 ASP A CB  1 
ATOM   3384  C  CG  . ASP A 1 415 ? 3.723   -9.530  3.885   1.00 32.55  ? 415 ASP A CG  1 
ATOM   3385  O  OD1 . ASP A 1 415 ? 3.728   -9.700  2.638   1.00 31.11  ? 415 ASP A OD1 1 
ATOM   3386  O  OD2 . ASP A 1 415 ? 2.738   -9.854  4.570   1.00 38.50  ? 415 ASP A OD2 1 
ATOM   3387  N  N   . GLU A 1 416 ? 7.010   -9.431  1.666   1.00 33.70  ? 416 GLU A N   1 
ATOM   3388  C  CA  . GLU A 1 416 ? 7.295   -8.868  0.347   1.00 30.57  ? 416 GLU A CA  1 
ATOM   3389  C  C   . GLU A 1 416 ? 6.037   -8.342  -0.325  1.00 31.09  ? 416 GLU A C   1 
ATOM   3390  O  O   . GLU A 1 416 ? 6.071   -7.281  -0.973  1.00 30.98  ? 416 GLU A O   1 
ATOM   3391  C  CB  . GLU A 1 416 ? 7.929   -9.939  -0.539  1.00 38.27  ? 416 GLU A CB  1 
ATOM   3392  C  CG  . GLU A 1 416 ? 9.264   -10.369 -0.024  1.00 42.32  ? 416 GLU A CG  1 
ATOM   3393  C  CD  . GLU A 1 416 ? 9.952   -11.292 -0.997  1.00 49.89  ? 416 GLU A CD  1 
ATOM   3394  O  OE1 . GLU A 1 416 ? 10.312  -12.408 -0.549  1.00 51.96  ? 416 GLU A OE1 1 
ATOM   3395  O  OE2 . GLU A 1 416 ? 10.086  -10.906 -2.188  1.00 46.00  ? 416 GLU A OE2 1 
ATOM   3396  N  N   . VAL A 1 417 ? 4.941   -9.091  -0.225  1.00 28.85  ? 417 VAL A N   1 
ATOM   3397  C  CA  . VAL A 1 417 ? 3.712   -8.738  -0.940  1.00 32.35  ? 417 VAL A CA  1 
ATOM   3398  C  C   . VAL A 1 417 ? 3.133   -7.434  -0.407  1.00 29.99  ? 417 VAL A C   1 
ATOM   3399  O  O   . VAL A 1 417 ? 2.804   -6.520  -1.176  1.00 29.64  ? 417 VAL A O   1 
ATOM   3400  C  CB  . VAL A 1 417 ? 2.699   -9.879  -0.846  1.00 34.53  ? 417 VAL A CB  1 
ATOM   3401  C  CG1 . VAL A 1 417 ? 1.363   -9.438  -1.434  1.00 33.03  ? 417 VAL A CG1 1 
ATOM   3402  C  CG2 . VAL A 1 417 ? 3.250   -11.062 -1.617  1.00 36.61  ? 417 VAL A CG2 1 
ATOM   3403  N  N   . ARG A 1 418 ? 2.986   -7.341  0.916   1.00 25.74  ? 418 ARG A N   1 
ATOM   3404  C  CA  . ARG A 1 418 ? 2.424   -6.139  1.521   1.00 28.58  ? 418 ARG A CA  1 
ATOM   3405  C  C   . ARG A 1 418 ? 3.337   -4.946  1.292   1.00 27.64  ? 418 ARG A C   1 
ATOM   3406  O  O   . ARG A 1 418 ? 2.859   -3.840  0.993   1.00 25.98  ? 418 ARG A O   1 
ATOM   3407  C  CB  . ARG A 1 418 ? 2.206   -6.370  3.023   1.00 29.29  ? 418 ARG A CB  1 
ATOM   3408  C  CG  . ARG A 1 418 ? 0.972   -7.265  3.318   1.00 33.59  ? 418 ARG A CG  1 
ATOM   3409  C  CD  . ARG A 1 418 ? 0.693   -7.390  4.832   1.00 35.76  ? 418 ARG A CD  1 
ATOM   3410  N  NE  . ARG A 1 418 ? -0.566  -8.097  5.086   1.00 42.33  ? 418 ARG A NE  1 
ATOM   3411  C  CZ  . ARG A 1 418 ? -0.696  -9.425  5.058   1.00 44.82  ? 418 ARG A CZ  1 
ATOM   3412  N  NH1 . ARG A 1 418 ? 0.345   -10.217 4.843   1.00 43.88  ? 418 ARG A NH1 1 
ATOM   3413  N  NH2 . ARG A 1 418 ? -1.898  -9.973  5.248   1.00 39.14  ? 418 ARG A NH2 1 
ATOM   3414  N  N   . THR A 1 419 ? 4.655   -5.135  1.451   1.00 25.70  ? 419 THR A N   1 
ATOM   3415  C  CA  . THR A 1 419 ? 5.587   -4.030  1.260   1.00 28.50  ? 419 THR A CA  1 
ATOM   3416  C  C   . THR A 1 419 ? 5.547   -3.515  -0.172  1.00 25.41  ? 419 THR A C   1 
ATOM   3417  O  O   . THR A 1 419 ? 5.521   -2.293  -0.393  1.00 25.13  ? 419 THR A O   1 
ATOM   3418  C  CB  . THR A 1 419 ? 7.003   -4.465  1.623   1.00 28.56  ? 419 THR A CB  1 
ATOM   3419  O  OG1 . THR A 1 419 ? 7.053   -4.778  3.027   1.00 30.67  ? 419 THR A OG1 1 
ATOM   3420  C  CG2 . THR A 1 419 ? 8.053   -3.324  1.367   1.00 25.55  ? 419 THR A CG2 1 
ATOM   3421  N  N   . GLN A 1 420 ? 5.535   -4.416  -1.172  1.00 25.06  ? 420 GLN A N   1 
ATOM   3422  C  CA  . GLN A 1 420 ? 5.469   -3.910  -2.544  1.00 27.82  ? 420 GLN A CA  1 
ATOM   3423  C  C   . GLN A 1 420 ? 4.160   -3.164  -2.791  1.00 29.72  ? 420 GLN A C   1 
ATOM   3424  O  O   . GLN A 1 420 ? 4.155   -2.141  -3.497  1.00 28.07  ? 420 GLN A O   1 
ATOM   3425  C  CB  . GLN A 1 420 ? 5.685   -5.042  -3.563  1.00 33.82  ? 420 GLN A CB  1 
ATOM   3426  C  CG  . GLN A 1 420 ? 5.345   -4.630  -4.969  1.00 39.01  ? 420 GLN A CG  1 
ATOM   3427  C  CD  . GLN A 1 420 ? 6.139   -5.410  -6.030  1.00 46.71  ? 420 GLN A CD  1 
ATOM   3428  O  OE1 . GLN A 1 420 ? 7.085   -6.147  -5.714  1.00 49.17  ? 420 GLN A OE1 1 
ATOM   3429  N  NE2 . GLN A 1 420 ? 5.709   -5.300  -7.274  1.00 49.75  ? 420 GLN A NE2 1 
ATOM   3430  N  N   . ALA A 1 421 ? 3.048   -3.635  -2.204  1.00 28.03  ? 421 ALA A N   1 
ATOM   3431  C  CA  . ALA A 1 421 ? 1.784   -2.911  -2.362  1.00 26.09  ? 421 ALA A CA  1 
ATOM   3432  C  C   . ALA A 1 421 ? 1.879   -1.536  -1.711  1.00 30.11  ? 421 ALA A C   1 
ATOM   3433  O  O   . ALA A 1 421 ? 1.386   -0.544  -2.276  1.00 28.55  ? 421 ALA A O   1 
ATOM   3434  C  CB  . ALA A 1 421 ? 0.612   -3.686  -1.773  1.00 28.10  ? 421 ALA A CB  1 
ATOM   3435  N  N   . ARG A 1 422 ? 2.525   -1.445  -0.528  1.00 23.79  ? 422 ARG A N   1 
ATOM   3436  C  CA  . ARG A 1 422 ? 2.666   -0.117  0.095   1.00 25.13  ? 422 ARG A CA  1 
ATOM   3437  C  C   . ARG A 1 422 ? 3.530   0.820   -0.757  1.00 28.31  ? 422 ARG A C   1 
ATOM   3438  O  O   . ARG A 1 422 ? 3.278   2.037   -0.800  1.00 25.44  ? 422 ARG A O   1 
ATOM   3439  C  CB  . ARG A 1 422 ? 3.280   -0.224  1.488   1.00 26.71  ? 422 ARG A CB  1 
ATOM   3440  C  CG  . ARG A 1 422 ? 2.405   -0.998  2.513   1.00 23.90  ? 422 ARG A CG  1 
ATOM   3441  C  CD  . ARG A 1 422 ? 3.126   -1.103  3.907   1.00 26.38  ? 422 ARG A CD  1 
ATOM   3442  N  NE  . ARG A 1 422 ? 3.219   0.194   4.575   1.00 26.20  ? 422 ARG A NE  1 
ATOM   3443  C  CZ  . ARG A 1 422 ? 2.256   0.693   5.333   1.00 25.85  ? 422 ARG A CZ  1 
ATOM   3444  N  NH1 . ARG A 1 422 ? 1.104   0.037   5.523   1.00 25.95  ? 422 ARG A NH1 1 
ATOM   3445  N  NH2 . ARG A 1 422 ? 2.423   1.891   5.890   1.00 27.68  ? 422 ARG A NH2 1 
ATOM   3446  N  N   . VAL A 1 423 ? 4.608   0.294   -1.360  1.00 25.64  ? 423 VAL A N   1 
ATOM   3447  C  CA  . VAL A 1 423 ? 5.515   1.128   -2.126  1.00 28.02  ? 423 VAL A CA  1 
ATOM   3448  C  C   . VAL A 1 423 ? 4.849   1.534   -3.430  1.00 25.85  ? 423 VAL A C   1 
ATOM   3449  O  O   . VAL A 1 423 ? 5.016   2.676   -3.905  1.00 26.99  ? 423 VAL A O   1 
ATOM   3450  C  CB  . VAL A 1 423 ? 6.865   0.401   -2.359  1.00 30.70  ? 423 VAL A CB  1 
ATOM   3451  C  CG1 . VAL A 1 423 ? 7.682   1.105   -3.428  1.00 31.65  ? 423 VAL A CG1 1 
ATOM   3452  C  CG2 . VAL A 1 423 ? 7.629   0.284   -1.061  1.00 29.51  ? 423 VAL A CG2 1 
ATOM   3453  N  N   . ASP A 1 424 ? 4.031   0.651   -4.002  1.00 25.89  ? 424 ASP A N   1 
ATOM   3454  C  CA  . ASP A 1 424 ? 3.265   1.059   -5.175  1.00 29.56  ? 424 ASP A CA  1 
ATOM   3455  C  C   . ASP A 1 424 ? 2.228   2.116   -4.844  1.00 27.60  ? 424 ASP A C   1 
ATOM   3456  O  O   . ASP A 1 424 ? 1.997   3.040   -5.646  1.00 27.84  ? 424 ASP A O   1 
ATOM   3457  C  CB  . ASP A 1 424 ? 2.577   -0.108  -5.857  1.00 30.76  ? 424 ASP A CB  1 
ATOM   3458  C  CG  . ASP A 1 424 ? 2.136   0.275   -7.255  1.00 36.53  ? 424 ASP A CG  1 
ATOM   3459  O  OD1 . ASP A 1 424 ? 2.984   0.285   -8.168  1.00 36.94  ? 424 ASP A OD1 1 
ATOM   3460  O  OD2 . ASP A 1 424 ? 0.919   0.565   -7.453  1.00 37.02  ? 424 ASP A OD2 1 
ATOM   3461  N  N   . ALA A 1 425 ? 1.589   1.993   -3.683  1.00 27.29  ? 425 ALA A N   1 
ATOM   3462  C  CA  . ALA A 1 425 ? 0.656   3.023   -3.280  1.00 27.53  ? 425 ALA A CA  1 
ATOM   3463  C  C   . ALA A 1 425 ? 1.389   4.343   -3.127  1.00 25.01  ? 425 ALA A C   1 
ATOM   3464  O  O   . ALA A 1 425 ? 0.840   5.392   -3.429  1.00 25.93  ? 425 ALA A O   1 
ATOM   3465  C  CB  . ALA A 1 425 ? -0.067  2.630   -1.986  1.00 27.31  ? 425 ALA A CB  1 
ATOM   3466  N  N   . PHE A 1 426 ? 2.629   4.302   -2.635  1.00 24.78  ? 426 PHE A N   1 
ATOM   3467  C  CA  . PHE A 1 426 ? 3.414   5.522   -2.490  1.00 25.11  ? 426 PHE A CA  1 
ATOM   3468  C  C   . PHE A 1 426 ? 3.706   6.162   -3.847  1.00 24.03  ? 426 PHE A C   1 
ATOM   3469  O  O   . PHE A 1 426 ? 3.674   7.383   -3.981  1.00 27.74  ? 426 PHE A O   1 
ATOM   3470  C  CB  . PHE A 1 426 ? 4.712   5.200   -1.762  1.00 23.74  ? 426 PHE A CB  1 
ATOM   3471  C  CG  . PHE A 1 426 ? 5.415   6.433   -1.238  1.00 23.87  ? 426 PHE A CG  1 
ATOM   3472  C  CD1 . PHE A 1 426 ? 4.741   7.314   -0.473  1.00 25.35  ? 426 PHE A CD1 1 
ATOM   3473  C  CD2 . PHE A 1 426 ? 6.771   6.641   -1.462  1.00 26.40  ? 426 PHE A CD2 1 
ATOM   3474  C  CE1 . PHE A 1 426 ? 5.376   8.448   0.065   1.00 25.46  ? 426 PHE A CE1 1 
ATOM   3475  C  CE2 . PHE A 1 426 ? 7.427   7.738   -0.929  1.00 26.00  ? 426 PHE A CE2 1 
ATOM   3476  C  CZ  . PHE A 1 426 ? 6.734   8.668   -0.188  1.00 24.82  ? 426 PHE A CZ  1 
ATOM   3477  N  N   . MET A 1 427 ? 3.957   5.364   -4.871  1.00 23.15  ? 427 MET A N   1 
ATOM   3478  C  CA  . MET A 1 427 ? 4.267   5.934   -6.179  1.00 24.31  ? 427 MET A CA  1 
ATOM   3479  C  C   . MET A 1 427 ? 3.029   6.632   -6.718  1.00 25.86  ? 427 MET A C   1 
ATOM   3480  O  O   . MET A 1 427 ? 3.110   7.732   -7.277  1.00 25.30  ? 427 MET A O   1 
ATOM   3481  C  CB  . MET A 1 427 ? 4.665   4.800   -7.112  1.00 26.95  ? 427 MET A CB  1 
ATOM   3482  C  CG  . MET A 1 427 ? 6.132   4.405   -7.075  1.00 30.39  ? 427 MET A CG  1 
ATOM   3483  S  SD  . MET A 1 427 ? 7.455   5.567   -6.756  1.00 37.41  ? 427 MET A SD  1 
ATOM   3484  C  CE  . MET A 1 427 ? 7.541   5.606   -4.986  1.00 28.38  ? 427 MET A CE  1 
ATOM   3485  N  N   . GLU A 1 428 ? 1.860   6.022   -6.501  1.00 23.99  ? 428 GLU A N   1 
ATOM   3486  C  CA  . GLU A 1 428 ? 0.607   6.647   -6.875  1.00 25.57  ? 428 GLU A CA  1 
ATOM   3487  C  C   . GLU A 1 428 ? 0.456   7.953   -6.134  1.00 24.97  ? 428 GLU A C   1 
ATOM   3488  O  O   . GLU A 1 428 ? 0.104   8.963   -6.734  1.00 25.39  ? 428 GLU A O   1 
ATOM   3489  C  CB  . GLU A 1 428 ? -0.577  5.740   -6.578  1.00 25.73  ? 428 GLU A CB  1 
ATOM   3490  C  CG  . GLU A 1 428 ? -1.899  6.382   -6.875  1.00 25.11  ? 428 GLU A CG  1 
ATOM   3491  C  CD  . GLU A 1 428 ? -3.075  5.417   -6.763  1.00 25.72  ? 428 GLU A CD  1 
ATOM   3492  O  OE1 . GLU A 1 428 ? -3.280  4.824   -5.671  1.00 25.30  ? 428 GLU A OE1 1 
ATOM   3493  O  OE2 . GLU A 1 428 ? -3.763  5.242   -7.777  1.00 28.06  ? 428 GLU A OE2 1 
ATOM   3494  N  N   . GLN A 1 429 ? 0.704   7.930   -4.827  1.00 25.12  ? 429 GLN A N   1 
ATOM   3495  C  CA  . GLN A 1 429 ? 0.627   9.143   -4.007  1.00 26.75  ? 429 GLN A CA  1 
ATOM   3496  C  C   . GLN A 1 429 ? 1.529   10.243  -4.558  1.00 25.74  ? 429 GLN A C   1 
ATOM   3497  O  O   . GLN A 1 429 ? 1.118   11.421  -4.637  1.00 25.70  ? 429 GLN A O   1 
ATOM   3498  C  CB  . GLN A 1 429 ? 1.025   8.821   -2.567  1.00 24.63  ? 429 GLN A CB  1 
ATOM   3499  C  CG  . GLN A 1 429 ? 1.141   10.117  -1.753  1.00 23.76  ? 429 GLN A CG  1 
ATOM   3500  C  CD  . GLN A 1 429 ? 1.747   9.921   -0.376  1.00 29.29  ? 429 GLN A CD  1 
ATOM   3501  O  OE1 . GLN A 1 429 ? 2.240   10.887  0.219   1.00 29.36  ? 429 GLN A OE1 1 
ATOM   3502  N  NE2 . GLN A 1 429 ? 1.691   8.681   0.157   1.00 27.21  ? 429 GLN A NE2 1 
ATOM   3503  N  N   . LEU A 1 430 ? 2.758   9.887   -4.945  1.00 24.40  ? 430 LEU A N   1 
ATOM   3504  C  CA  . LEU A 1 430 ? 3.674   10.898  -5.484  1.00 25.02  ? 430 LEU A CA  1 
ATOM   3505  C  C   . LEU A 1 430 ? 3.163   11.471  -6.797  1.00 29.87  ? 430 LEU A C   1 
ATOM   3506  O  O   . LEU A 1 430 ? 3.267   12.689  -7.033  1.00 29.33  ? 430 LEU A O   1 
ATOM   3507  C  CB  . LEU A 1 430 ? 5.057   10.326  -5.680  1.00 26.39  ? 430 LEU A CB  1 
ATOM   3508  C  CG  . LEU A 1 430 ? 5.684   9.951   -4.348  1.00 24.06  ? 430 LEU A CG  1 
ATOM   3509  C  CD1 . LEU A 1 430 ? 7.036   9.475   -4.650  1.00 26.23  ? 430 LEU A CD1 1 
ATOM   3510  C  CD2 . LEU A 1 430 ? 5.715   11.108  -3.258  1.00 26.50  ? 430 LEU A CD2 1 
ATOM   3511  N  N   . GLY A 1 431 ? 2.603   10.622  -7.662  1.00 27.98  ? 431 GLY A N   1 
ATOM   3512  C  CA  . GLY A 1 431 ? 1.928   11.141  -8.855  1.00 30.75  ? 431 GLY A CA  1 
ATOM   3513  C  C   . GLY A 1 431 ? 0.775   12.092  -8.548  1.00 31.06  ? 431 GLY A C   1 
ATOM   3514  O  O   . GLY A 1 431 ? 0.626   13.143  -9.194  1.00 29.63  ? 431 GLY A O   1 
ATOM   3515  N  N   . VAL A 1 432 ? -0.101  11.716  -7.605  1.00 24.51  ? 432 VAL A N   1 
ATOM   3516  C  CA  . VAL A 1 432 ? -1.257  12.567  -7.286  1.00 28.48  ? 432 VAL A CA  1 
ATOM   3517  C  C   . VAL A 1 432 ? -0.780  13.935  -6.814  1.00 27.98  ? 432 VAL A C   1 
ATOM   3518  O  O   . VAL A 1 432 ? -1.334  14.981  -7.210  1.00 27.03  ? 432 VAL A O   1 
ATOM   3519  C  CB  . VAL A 1 432 ? -2.140  11.888  -6.213  1.00 29.75  ? 432 VAL A CB  1 
ATOM   3520  C  CG1 . VAL A 1 432 ? -3.120  12.876  -5.657  1.00 26.71  ? 432 VAL A CG1 1 
ATOM   3521  C  CG2 . VAL A 1 432 ? -2.873  10.669  -6.813  1.00 23.98  ? 432 VAL A CG2 1 
ATOM   3522  N  N   . ARG A 1 433 ? 0.233   13.933  -5.936  1.00 26.05  ? 433 ARG A N   1 
ATOM   3523  C  CA  . ARG A 1 433 ? 0.798   15.179  -5.401  1.00 27.26  ? 433 ARG A CA  1 
ATOM   3524  C  C   . ARG A 1 433 ? 1.347   16.046  -6.517  1.00 29.10  ? 433 ARG A C   1 
ATOM   3525  O  O   . ARG A 1 433 ? 1.180   17.278  -6.501  1.00 28.57  ? 433 ARG A O   1 
ATOM   3526  C  CB  . ARG A 1 433 ? 1.891   14.833  -4.383  1.00 28.54  ? 433 ARG A CB  1 
ATOM   3527  C  CG  . ARG A 1 433 ? 1.310   14.474  -2.990  1.00 29.97  ? 433 ARG A CG  1 
ATOM   3528  C  CD  . ARG A 1 433 ? 2.420   14.063  -2.095  1.00 32.03  ? 433 ARG A CD  1 
ATOM   3529  N  NE  . ARG A 1 433 ? 1.983   13.583  -0.787  1.00 36.13  ? 433 ARG A NE  1 
ATOM   3530  C  CZ  . ARG A 1 433 ? 2.020   14.355  0.287   1.00 36.90  ? 433 ARG A CZ  1 
ATOM   3531  N  NH1 . ARG A 1 433 ? 2.323   15.639  0.182   1.00 31.84  ? 433 ARG A NH1 1 
ATOM   3532  N  NH2 . ARG A 1 433 ? 1.807   13.814  1.492   1.00 34.42  ? 433 ARG A NH2 1 
ATOM   3533  N  N   . ARG A 1 434 ? 1.961   15.421  -7.522  1.00 26.51  ? 434 ARG A N   1 
ATOM   3534  C  CA  . ARG A 1 434 ? 2.477   16.203  -8.660  1.00 28.75  ? 434 ARG A CA  1 
ATOM   3535  C  C   . ARG A 1 434 ? 1.351   16.850  -9.452  1.00 33.27  ? 434 ARG A C   1 
ATOM   3536  O  O   . ARG A 1 434 ? 1.462   18.018  -9.872  1.00 30.65  ? 434 ARG A O   1 
ATOM   3537  C  CB  . ARG A 1 434 ? 3.354   15.298  -9.549  1.00 33.24  ? 434 ARG A CB  1 
ATOM   3538  C  CG  . ARG A 1 434 ? 3.972   15.966  -10.821 1.00 40.96  ? 434 ARG A CG  1 
ATOM   3539  C  CD  . ARG A 1 434 ? 4.201   14.947  -11.964 1.00 51.28  ? 434 ARG A CD  1 
ATOM   3540  N  NE  . ARG A 1 434 ? 2.976   14.230  -12.328 1.00 54.23  ? 434 ARG A NE  1 
ATOM   3541  C  CZ  . ARG A 1 434 ? 2.797   12.913  -12.253 1.00 53.79  ? 434 ARG A CZ  1 
ATOM   3542  N  NH1 . ARG A 1 434 ? 3.777   12.092  -11.878 1.00 52.06  ? 434 ARG A NH1 1 
ATOM   3543  N  NH2 . ARG A 1 434 ? 1.596   12.408  -12.542 1.00 50.07  ? 434 ARG A NH2 1 
ATOM   3544  N  N   . GLN A 1 435 ? 0.250   16.110  -9.681  1.00 31.39  ? 435 GLN A N   1 
ATOM   3545  C  CA  . GLN A 1 435 ? -0.890  16.671  -10.405 1.00 32.99  ? 435 GLN A CA  1 
ATOM   3546  C  C   . GLN A 1 435 ? -1.507  17.834  -9.636  1.00 34.08  ? 435 GLN A C   1 
ATOM   3547  O  O   . GLN A 1 435 ? -1.833  18.874  -10.223 1.00 31.86  ? 435 GLN A O   1 
ATOM   3548  C  CB  . GLN A 1 435 ? -1.935  15.581  -10.639 1.00 31.13  ? 435 GLN A CB  1 
ATOM   3549  C  CG  . GLN A 1 435 ? -1.383  14.494  -11.504 1.00 37.13  ? 435 GLN A CG  1 
ATOM   3550  C  CD  . GLN A 1 435 ? -1.388  14.835  -12.967 1.00 40.34  ? 435 GLN A CD  1 
ATOM   3551  O  OE1 . GLN A 1 435 ? -1.771  15.939  -13.381 1.00 42.82  ? 435 GLN A OE1 1 
ATOM   3552  N  NE2 . GLN A 1 435 ? -0.921  13.892  -13.771 1.00 47.47  ? 435 GLN A NE2 1 
ATOM   3553  N  N   . ALA A 1 436 ? -1.723  17.651  -8.322  1.00 29.49  ? 436 ALA A N   1 
ATOM   3554  C  CA  . ALA A 1 436 ? -2.274  18.739  -7.516  1.00 29.27  ? 436 ALA A CA  1 
ATOM   3555  C  C   . ALA A 1 436 ? -1.352  19.955  -7.556  1.00 34.88  ? 436 ALA A C   1 
ATOM   3556  O  O   . ALA A 1 436 ? -1.818  21.083  -7.756  1.00 39.55  ? 436 ALA A O   1 
ATOM   3557  C  CB  . ALA A 1 436 ? -2.496  18.277  -6.068  1.00 28.87  ? 436 ALA A CB  1 
ATOM   3558  N  N   . ALA A 1 437 ? -0.041  19.749  -7.396  1.00 28.88  ? 437 ALA A N   1 
ATOM   3559  C  CA  . ALA A 1 437 ? 0.863   20.906  -7.363  1.00 36.90  ? 437 ALA A CA  1 
ATOM   3560  C  C   . ALA A 1 437 ? 0.855   21.641  -8.692  1.00 40.05  ? 437 ALA A C   1 
ATOM   3561  O  O   . ALA A 1 437 ? 0.814   22.881  -8.739  1.00 44.17  ? 437 ALA A O   1 
ATOM   3562  C  CB  . ALA A 1 437 ? 2.284   20.468  -7.024  1.00 32.69  ? 437 ALA A CB  1 
ATOM   3563  N  N   . SER A 1 438 ? 0.907   20.891  -9.790  1.00 39.53  ? 438 SER A N   1 
ATOM   3564  C  CA  . SER A 1 438 ? 0.840   21.519  -11.094 1.00 39.46  ? 438 SER A CA  1 
ATOM   3565  C  C   . SER A 1 438 ? -0.474  22.286  -11.269 1.00 47.81  ? 438 SER A C   1 
ATOM   3566  O  O   . SER A 1 438 ? -0.475  23.397  -11.811 1.00 51.12  ? 438 SER A O   1 
ATOM   3567  C  CB  . SER A 1 438 ? 1.026   20.461  -12.180 1.00 39.57  ? 438 SER A CB  1 
ATOM   3568  O  OG  . SER A 1 438 ? 0.802   21.074  -13.441 1.00 47.63  ? 438 SER A OG  1 
ATOM   3569  N  N   . ALA A 1 439 ? -1.600  21.731  -10.788 1.00 41.60  ? 439 ALA A N   1 
ATOM   3570  C  CA  . ALA A 1 439 ? -2.894  22.401  -10.938 1.00 46.01  ? 439 ALA A CA  1 
ATOM   3571  C  C   . ALA A 1 439 ? -2.949  23.701  -10.157 1.00 49.60  ? 439 ALA A C   1 
ATOM   3572  O  O   . ALA A 1 439 ? -3.571  24.671  -10.609 1.00 55.79  ? 439 ALA A O   1 
ATOM   3573  C  CB  . ALA A 1 439 ? -4.039  21.489  -10.485 1.00 42.02  ? 439 ALA A CB  1 
ATOM   3574  N  N   . TRP A 1 440 ? -2.313  23.736  -8.980  1.00 51.12  ? 440 TRP A N   1 
ATOM   3575  C  CA  . TRP A 1 440 ? -2.307  24.946  -8.153  1.00 60.53  ? 440 TRP A CA  1 
ATOM   3576  C  C   . TRP A 1 440 ? -1.421  26.032  -8.753  1.00 62.04  ? 440 TRP A C   1 
ATOM   3577  O  O   . TRP A 1 440 ? -1.812  27.202  -8.808  1.00 68.61  ? 440 TRP A O   1 
ATOM   3578  C  CB  . TRP A 1 440 ? -1.842  24.627  -6.725  1.00 62.72  ? 440 TRP A CB  1 
ATOM   3579  C  CG  . TRP A 1 440 ? -1.846  25.860  -5.815  1.00 74.40  ? 440 TRP A CG  1 
ATOM   3580  C  CD1 . TRP A 1 440 ? -0.787  26.693  -5.547  1.00 73.48  ? 440 TRP A CD1 1 
ATOM   3581  C  CD2 . TRP A 1 440 ? -2.965  26.395  -5.087  1.00 77.52  ? 440 TRP A CD2 1 
ATOM   3582  N  NE1 . TRP A 1 440 ? -1.179  27.703  -4.694  1.00 77.89  ? 440 TRP A NE1 1 
ATOM   3583  C  CE2 . TRP A 1 440 ? -2.508  27.545  -4.398  1.00 80.28  ? 440 TRP A CE2 1 
ATOM   3584  C  CE3 . TRP A 1 440 ? -4.308  26.015  -4.952  1.00 80.42  ? 440 TRP A CE3 1 
ATOM   3585  C  CZ2 . TRP A 1 440 ? -3.349  28.314  -3.581  1.00 81.48  ? 440 TRP A CZ2 1 
ATOM   3586  C  CZ3 . TRP A 1 440 ? -5.143  26.778  -4.138  1.00 81.40  ? 440 TRP A CZ3 1 
ATOM   3587  C  CH2 . TRP A 1 440 ? -4.657  27.915  -3.464  1.00 82.68  ? 440 TRP A CH2 1 
ATOM   3588  N  N   . SER A 1 441 ? -0.210  25.670  -9.167  1.00 59.65  ? 441 SER A N   1 
ATOM   3589  C  CA  . SER A 1 441 ? 0.724   26.595  -9.794  1.00 64.61  ? 441 SER A CA  1 
ATOM   3590  C  C   . SER A 1 441 ? 0.517   26.714  -11.302 1.00 69.53  ? 441 SER A C   1 
ATOM   3591  O  O   . SER A 1 441 ? 1.269   27.444  -11.960 1.00 74.03  ? 441 SER A O   1 
ATOM   3592  C  CB  . SER A 1 441 ? 2.156   26.152  -9.499  1.00 60.33  ? 441 SER A CB  1 
ATOM   3593  O  OG  . SER A 1 441 ? 2.583   25.194  -10.450 1.00 61.98  ? 441 SER A OG  1 
ATOM   3594  N  N   . HIS A 1 442 ? -0.491  26.028  -11.849 1.00 67.94  ? 442 HIS A N   1 
ATOM   3595  C  CA  . HIS A 1 442 ? -0.763  25.944  -13.292 1.00 70.46  ? 442 HIS A CA  1 
ATOM   3596  C  C   . HIS A 1 442 ? 0.488   25.579  -14.103 1.00 75.12  ? 442 HIS A C   1 
ATOM   3597  O  O   . HIS A 1 442 ? 0.882   24.405  -14.160 1.00 71.23  ? 442 HIS A O   1 
ATOM   3598  C  CB  . HIS A 1 442 ? -1.373  27.245  -13.798 1.00 76.12  ? 442 HIS A CB  1 
ATOM   3599  C  CG  . HIS A 1 442 ? -2.583  27.684  -13.030 1.00 77.67  ? 442 HIS A CG  1 
ATOM   3600  N  ND1 . HIS A 1 442 ? -3.665  26.858  -12.806 1.00 77.26  ? 442 HIS A ND1 1 
ATOM   3601  C  CD2 . HIS A 1 442 ? -2.889  28.870  -12.454 1.00 76.99  ? 442 HIS A CD2 1 
ATOM   3602  C  CE1 . HIS A 1 442 ? -4.580  27.513  -12.114 1.00 78.44  ? 442 HIS A CE1 1 
ATOM   3603  N  NE2 . HIS A 1 442 ? -4.135  28.736  -11.889 1.00 79.63  ? 442 HIS A NE2 1 
ATOM   3604  N  N   . SER B 2 2   ? -2.374  -7.915  57.021  0.50 67.32  ? 2   SER B N   1 
ATOM   3605  C  CA  . SER B 2 2   ? -2.702  -8.407  58.384  1.00 66.68  ? 2   SER B CA  1 
ATOM   3606  C  C   . SER B 2 2   ? -2.278  -7.370  59.430  1.00 67.88  ? 2   SER B C   1 
ATOM   3607  O  O   . SER B 2 2   ? -3.120  -6.534  59.778  1.00 71.87  ? 2   SER B O   1 
ATOM   3608  C  CB  . SER B 2 2   ? -2.089  -9.747  58.638  1.00 78.23  ? 2   SER B CB  1 
ATOM   3609  O  OG  . SER B 2 2   ? -3.084  -10.759 58.622  1.00 88.05  ? 2   SER B OG  1 
ATOM   3610  N  N   . ASP B 2 3   ? -1.033  -7.411  59.918  1.00 61.31  ? 3   ASP B N   1 
ATOM   3611  C  CA  . ASP B 2 3   ? -0.664  -6.397  60.900  1.00 54.89  ? 3   ASP B CA  1 
ATOM   3612  C  C   . ASP B 2 3   ? -0.509  -5.007  60.279  1.00 53.79  ? 3   ASP B C   1 
ATOM   3613  O  O   . ASP B 2 3   ? -0.484  -4.010  61.013  1.00 50.65  ? 3   ASP B O   1 
ATOM   3614  C  CB  . ASP B 2 3   ? 0.573   -6.873  61.692  1.00 49.06  ? 3   ASP B CB  1 
ATOM   3615  C  CG  . ASP B 2 3   ? 1.884   -6.772  60.909  1.00 46.16  ? 3   ASP B CG  1 
ATOM   3616  O  OD1 . ASP B 2 3   ? 1.917   -6.155  59.849  1.00 42.27  ? 3   ASP B OD1 1 
ATOM   3617  O  OD2 . ASP B 2 3   ? 2.898   -7.338  61.351  1.00 45.98  ? 3   ASP B OD2 1 
ATOM   3618  N  N   . GLY B 2 4   ? -0.452  -4.910  58.953  1.00 49.45  ? 4   GLY B N   1 
ATOM   3619  C  CA  . GLY B 2 4   ? -0.441  -3.608  58.321  1.00 43.73  ? 4   GLY B CA  1 
ATOM   3620  C  C   . GLY B 2 4   ? 0.855   -2.836  58.439  1.00 42.70  ? 4   GLY B C   1 
ATOM   3621  O  O   . GLY B 2 4   ? 0.860   -1.633  58.128  1.00 37.13  ? 4   GLY B O   1 
ATOM   3622  N  N   . LEU B 2 5   ? 1.958   -3.495  58.859  1.00 37.31  ? 5   LEU B N   1 
ATOM   3623  C  CA  . LEU B 2 5   ? 3.233   -2.804  59.075  1.00 35.64  ? 5   LEU B CA  1 
ATOM   3624  C  C   . LEU B 2 5   ? 3.711   -2.070  57.825  1.00 35.59  ? 5   LEU B C   1 
ATOM   3625  O  O   . LEU B 2 5   ? 4.298   -0.987  57.934  1.00 33.95  ? 5   LEU B O   1 
ATOM   3626  C  CB  . LEU B 2 5   ? 4.313   -3.783  59.509  1.00 32.56  ? 5   LEU B CB  1 
ATOM   3627  C  CG  . LEU B 2 5   ? 5.738   -3.271  59.789  1.00 35.16  ? 5   LEU B CG  1 
ATOM   3628  C  CD1 . LEU B 2 5   ? 5.707   -2.101  60.831  1.00 36.90  ? 5   LEU B CD1 1 
ATOM   3629  C  CD2 . LEU B 2 5   ? 6.659   -4.399  60.320  1.00 34.07  ? 5   LEU B CD2 1 
ATOM   3630  N  N   . PHE B 2 6   ? 3.520   -2.657  56.628  1.00 31.26  ? 6   PHE B N   1 
ATOM   3631  C  CA  . PHE B 2 6   ? 3.985   -2.044  55.393  1.00 32.51  ? 6   PHE B CA  1 
ATOM   3632  C  C   . PHE B 2 6   ? 2.925   -1.171  54.697  1.00 34.78  ? 6   PHE B C   1 
ATOM   3633  O  O   . PHE B 2 6   ? 3.138   -0.767  53.545  1.00 35.82  ? 6   PHE B O   1 
ATOM   3634  C  CB  . PHE B 2 6   ? 4.508   -3.134  54.446  1.00 29.92  ? 6   PHE B CB  1 
ATOM   3635  C  CG  . PHE B 2 6   ? 5.857   -3.651  54.836  1.00 30.24  ? 6   PHE B CG  1 
ATOM   3636  C  CD1 . PHE B 2 6   ? 5.964   -4.606  55.854  1.00 30.89  ? 6   PHE B CD1 1 
ATOM   3637  C  CD2 . PHE B 2 6   ? 7.014   -3.182  54.218  1.00 31.04  ? 6   PHE B CD2 1 
ATOM   3638  C  CE1 . PHE B 2 6   ? 7.198   -5.062  56.251  1.00 30.90  ? 6   PHE B CE1 1 
ATOM   3639  C  CE2 . PHE B 2 6   ? 8.261   -3.633  54.608  1.00 32.76  ? 6   PHE B CE2 1 
ATOM   3640  C  CZ  . PHE B 2 6   ? 8.353   -4.586  55.622  1.00 33.09  ? 6   PHE B CZ  1 
ATOM   3641  N  N   . ASP B 2 7   ? 1.829   -0.828  55.387  1.00 34.67  ? 7   ASP B N   1 
ATOM   3642  C  CA  . ASP B 2 7   ? 0.739   -0.086  54.756  1.00 35.80  ? 7   ASP B CA  1 
ATOM   3643  C  C   . ASP B 2 7   ? 1.180   1.302   54.289  1.00 34.74  ? 7   ASP B C   1 
ATOM   3644  O  O   . ASP B 2 7   ? 0.660   1.798   53.282  1.00 35.72  ? 7   ASP B O   1 
ATOM   3645  C  CB  . ASP B 2 7   ? -0.448  -0.011  55.735  1.00 36.84  ? 7   ASP B CB  1 
ATOM   3646  C  CG  . ASP B 2 7   ? -1.293  -1.278  55.705  1.00 44.91  ? 7   ASP B CG  1 
ATOM   3647  O  OD1 . ASP B 2 7   ? -0.829  -2.249  55.053  1.00 43.84  ? 7   ASP B OD1 1 
ATOM   3648  O  OD2 . ASP B 2 7   ? -2.421  -1.292  56.259  1.00 47.85  ? 7   ASP B OD2 1 
ATOM   3649  N  N   . GLN B 2 8   ? 2.136   1.950   54.975  1.00 34.41  ? 8   GLN B N   1 
ATOM   3650  C  CA  . GLN B 2 8   ? 2.570   3.268   54.498  1.00 33.26  ? 8   GLN B CA  1 
ATOM   3651  C  C   . GLN B 2 8   ? 3.267   3.171   53.147  1.00 32.56  ? 8   GLN B C   1 
ATOM   3652  O  O   . GLN B 2 8   ? 3.087   4.038   52.273  1.00 33.58  ? 8   GLN B O   1 
ATOM   3653  C  CB  . GLN B 2 8   ? 3.485   3.964   55.507  1.00 36.38  ? 8   GLN B CB  1 
ATOM   3654  C  CG  . GLN B 2 8   ? 3.966   5.356   54.982  1.00 31.04  ? 8   GLN B CG  1 
ATOM   3655  C  CD  . GLN B 2 8   ? 2.800   6.385   54.796  1.00 35.22  ? 8   GLN B CD  1 
ATOM   3656  O  OE1 . GLN B 2 8   ? 2.444   6.747   53.661  1.00 36.36  ? 8   GLN B OE1 1 
ATOM   3657  N  NE2 . GLN B 2 8   ? 2.231   6.848   55.887  1.00 37.96  ? 8   GLN B NE2 1 
ATOM   3658  N  N   . PHE B 2 9   ? 4.066   2.128   52.943  1.00 29.83  ? 9   PHE B N   1 
ATOM   3659  C  CA  . PHE B 2 9   ? 4.692   1.949   51.632  1.00 31.85  ? 9   PHE B CA  1 
ATOM   3660  C  C   . PHE B 2 9   ? 3.653   1.664   50.543  1.00 31.41  ? 9   PHE B C   1 
ATOM   3661  O  O   . PHE B 2 9   ? 3.784   2.136   49.400  1.00 31.12  ? 9   PHE B O   1 
ATOM   3662  C  CB  . PHE B 2 9   ? 5.710   0.820   51.695  1.00 30.54  ? 9   PHE B CB  1 
ATOM   3663  C  CG  . PHE B 2 9   ? 6.804   1.033   52.666  1.00 31.13  ? 9   PHE B CG  1 
ATOM   3664  C  CD1 . PHE B 2 9   ? 7.836   1.908   52.378  1.00 30.22  ? 9   PHE B CD1 1 
ATOM   3665  C  CD2 . PHE B 2 9   ? 6.834   0.328   53.884  1.00 30.88  ? 9   PHE B CD2 1 
ATOM   3666  C  CE1 . PHE B 2 9   ? 8.889   2.089   53.252  1.00 30.23  ? 9   PHE B CE1 1 
ATOM   3667  C  CE2 . PHE B 2 9   ? 7.885   0.560   54.813  1.00 37.37  ? 9   PHE B CE2 1 
ATOM   3668  C  CZ  . PHE B 2 9   ? 8.916   1.439   54.500  1.00 31.87  ? 9   PHE B CZ  1 
ATOM   3669  N  N   . LYS B 2 10  ? 2.599   0.911   50.889  1.00 32.79  ? 10  LYS B N   1 
ATOM   3670  C  CA  . LYS B 2 10  ? 1.571   0.565   49.920  1.00 30.67  ? 10  LYS B CA  1 
ATOM   3671  C  C   . LYS B 2 10  ? 0.751   1.800   49.531  1.00 34.59  ? 10  LYS B C   1 
ATOM   3672  O  O   . LYS B 2 10  ? 0.457   2.022   48.352  1.00 32.71  ? 10  LYS B O   1 
ATOM   3673  C  CB  . LYS B 2 10  ? 0.707   -0.561  50.508  1.00 33.10  ? 10  LYS B CB  1 
ATOM   3674  C  CG  . LYS B 2 10  ? -0.544  -0.901  49.753  1.00 43.36  ? 10  LYS B CG  1 
ATOM   3675  C  CD  . LYS B 2 10  ? -1.028  -2.317  50.156  1.00 49.10  ? 10  LYS B CD  1 
ATOM   3676  C  CE  . LYS B 2 10  ? -1.991  -2.881  49.118  1.00 50.65  ? 10  LYS B CE  1 
ATOM   3677  N  NZ  . LYS B 2 10  ? -3.278  -2.138  49.061  1.00 53.76  ? 10  LYS B NZ  1 
ATOM   3678  N  N   . THR B 2 11  ? 0.425   2.643   50.506  1.00 30.96  ? 11  THR B N   1 
ATOM   3679  C  CA  . THR B 2 11  ? -0.208  3.928   50.217  1.00 32.42  ? 11  THR B CA  1 
ATOM   3680  C  C   . THR B 2 11  ? 0.667   4.802   49.318  1.00 32.60  ? 11  THR B C   1 
ATOM   3681  O  O   . THR B 2 11  ? 0.179   5.398   48.351  1.00 33.05  ? 11  THR B O   1 
ATOM   3682  C  CB  . THR B 2 11  ? -0.479  4.668   51.519  1.00 29.37  ? 11  THR B CB  1 
ATOM   3683  O  OG1 . THR B 2 11  ? -1.308  3.869   52.340  1.00 36.74  ? 11  THR B OG1 1 
ATOM   3684  C  CG2 . THR B 2 11  ? -1.234  5.942   51.226  1.00 36.55  ? 11  THR B CG2 1 
ATOM   3685  N  N   . TRP B 2 12  ? 1.950   4.955   49.670  1.00 29.15  ? 12  TRP B N   1 
ATOM   3686  C  CA  . TRP B 2 12  ? 2.846   5.757   48.843  1.00 33.04  ? 12  TRP B CA  1 
ATOM   3687  C  C   . TRP B 2 12  ? 2.884   5.249   47.401  1.00 32.44  ? 12  TRP B C   1 
ATOM   3688  O  O   . TRP B 2 12  ? 2.930   6.034   46.445  1.00 33.80  ? 12  TRP B O   1 
ATOM   3689  C  CB  . TRP B 2 12  ? 4.247   5.726   49.436  1.00 29.57  ? 12  TRP B CB  1 
ATOM   3690  C  CG  . TRP B 2 12  ? 4.471   6.679   50.583  1.00 31.48  ? 12  TRP B CG  1 
ATOM   3691  C  CD1 . TRP B 2 12  ? 3.730   7.796   50.896  1.00 29.83  ? 12  TRP B CD1 1 
ATOM   3692  C  CD2 . TRP B 2 12  ? 5.533   6.604   51.555  1.00 32.43  ? 12  TRP B CD2 1 
ATOM   3693  N  NE1 . TRP B 2 12  ? 4.285   8.423   52.013  1.00 33.46  ? 12  TRP B NE1 1 
ATOM   3694  C  CE2 . TRP B 2 12  ? 5.386   7.706   52.430  1.00 33.92  ? 12  TRP B CE2 1 
ATOM   3695  C  CE3 . TRP B 2 12  ? 6.606   5.715   51.756  1.00 29.48  ? 12  TRP B CE3 1 
ATOM   3696  C  CZ2 . TRP B 2 12  ? 6.263   7.926   53.501  1.00 30.12  ? 12  TRP B CZ2 1 
ATOM   3697  C  CZ3 . TRP B 2 12  ? 7.468   5.936   52.802  1.00 30.39  ? 12  TRP B CZ3 1 
ATOM   3698  C  CH2 . TRP B 2 12  ? 7.299   7.034   53.665  1.00 28.77  ? 12  TRP B CH2 1 
ATOM   3699  N  N   . TYR B 2 13  ? 2.879   3.936   47.221  1.00 31.68  ? 13  TYR B N   1 
ATOM   3700  C  CA  . TYR B 2 13  ? 2.946   3.390   45.874  1.00 32.94  ? 13  TYR B CA  1 
ATOM   3701  C  C   . TYR B 2 13  ? 1.642   3.673   45.138  1.00 34.50  ? 13  TYR B C   1 
ATOM   3702  O  O   . TYR B 2 13  ? 1.654   4.246   44.046  1.00 34.62  ? 13  TYR B O   1 
ATOM   3703  C  CB  . TYR B 2 13  ? 3.244   1.888   45.937  1.00 31.13  ? 13  TYR B CB  1 
ATOM   3704  C  CG  . TYR B 2 13  ? 3.045   1.118   44.642  1.00 34.47  ? 13  TYR B CG  1 
ATOM   3705  C  CD1 . TYR B 2 13  ? 4.032   1.102   43.662  1.00 38.54  ? 13  TYR B CD1 1 
ATOM   3706  C  CD2 . TYR B 2 13  ? 1.884   0.387   44.412  1.00 35.76  ? 13  TYR B CD2 1 
ATOM   3707  C  CE1 . TYR B 2 13  ? 3.869   0.378   42.484  1.00 39.64  ? 13  TYR B CE1 1 
ATOM   3708  C  CE2 . TYR B 2 13  ? 1.706   -0.342  43.242  1.00 43.74  ? 13  TYR B CE2 1 
ATOM   3709  C  CZ  . TYR B 2 13  ? 2.694   -0.333  42.274  1.00 43.48  ? 13  TYR B CZ  1 
ATOM   3710  O  OH  . TYR B 2 13  ? 2.490   -1.079  41.131  1.00 45.92  ? 13  TYR B OH  1 
ATOM   3711  N  N   . GLU B 2 14  ? 0.505   3.342   45.768  1.00 29.88  ? 14  GLU B N   1 
ATOM   3712  C  CA  . GLU B 2 14  ? -0.810  3.533   45.154  1.00 33.02  ? 14  GLU B CA  1 
ATOM   3713  C  C   . GLU B 2 14  ? -1.101  5.004   44.875  1.00 32.54  ? 14  GLU B C   1 
ATOM   3714  O  O   . GLU B 2 14  ? -1.732  5.341   43.863  1.00 40.35  ? 14  GLU B O   1 
ATOM   3715  C  CB  . GLU B 2 14  ? -1.860  2.971   46.093  1.00 38.14  ? 14  GLU B CB  1 
ATOM   3716  C  CG  . GLU B 2 14  ? -1.780  1.474   46.130  1.00 44.06  ? 14  GLU B CG  1 
ATOM   3717  C  CD  . GLU B 2 14  ? -2.943  0.867   46.849  1.00 52.50  ? 14  GLU B CD  1 
ATOM   3718  O  OE1 . GLU B 2 14  ? -4.040  1.463   46.788  1.00 56.82  ? 14  GLU B OE1 1 
ATOM   3719  O  OE2 . GLU B 2 14  ? -2.749  -0.198  47.480  1.00 60.29  ? 14  GLU B OE2 1 
ATOM   3720  N  N   . LYS B 2 15  ? -0.654  5.884   45.761  1.00 32.66  ? 15  LYS B N   1 
ATOM   3721  C  CA  . LYS B 2 15  ? -0.927  7.315   45.721  1.00 33.11  ? 15  LYS B CA  1 
ATOM   3722  C  C   . LYS B 2 15  ? 0.331   8.114   45.420  1.00 33.20  ? 15  LYS B C   1 
ATOM   3723  O  O   . LYS B 2 15  ? 0.530   9.198   45.956  1.00 32.26  ? 15  LYS B O   1 
ATOM   3724  C  CB  . LYS B 2 15  ? -1.531  7.789   47.047  1.00 34.97  ? 15  LYS B CB  1 
ATOM   3725  C  CG  . LYS B 2 15  ? -2.805  7.049   47.446  1.00 36.82  ? 15  LYS B CG  1 
ATOM   3726  C  CD  . LYS B 2 15  ? -4.052  7.761   47.045  1.00 49.22  ? 15  LYS B CD  1 
ATOM   3727  C  CE  . LYS B 2 15  ? -4.400  7.480   45.567  1.00 48.87  ? 15  LYS B CE  1 
ATOM   3728  N  NZ  . LYS B 2 15  ? -5.873  7.588   45.295  1.00 53.00  ? 15  LYS B NZ  1 
ATOM   3729  N  N   . ARG B 2 16  ? 1.193   7.597   44.541  1.00 32.63  ? 16  ARG B N   1 
ATOM   3730  C  CA  . ARG B 2 16  ? 2.482   8.252   44.347  1.00 32.62  ? 16  ARG B CA  1 
ATOM   3731  C  C   . ARG B 2 16  ? 2.308   9.680   43.819  1.00 29.96  ? 16  ARG B C   1 
ATOM   3732  O  O   . ARG B 2 16  ? 3.057   10.582  44.218  1.00 31.22  ? 16  ARG B O   1 
ATOM   3733  C  CB  . ARG B 2 16  ? 3.358   7.416   43.408  1.00 31.46  ? 16  ARG B CB  1 
ATOM   3734  C  CG  . ARG B 2 16  ? 2.710   7.165   42.050  1.00 31.08  ? 16  ARG B CG  1 
ATOM   3735  C  CD  . ARG B 2 16  ? 3.757   6.573   41.068  1.00 30.55  ? 16  ARG B CD  1 
ATOM   3736  N  NE  . ARG B 2 16  ? 4.907   7.460   40.921  1.00 28.38  ? 16  ARG B NE  1 
ATOM   3737  C  CZ  . ARG B 2 16  ? 6.037   7.133   40.309  1.00 32.03  ? 16  ARG B CZ  1 
ATOM   3738  N  NH1 . ARG B 2 16  ? 6.178   5.964   39.695  1.00 30.24  ? 16  ARG B NH1 1 
ATOM   3739  N  NH2 . ARG B 2 16  ? 7.071   7.979   40.357  1.00 28.39  ? 16  ARG B NH2 1 
ATOM   3740  N  N   . HIS B 2 17  ? 1.309   9.912   42.964  1.00 31.54  ? 17  HIS B N   1 
ATOM   3741  C  CA  . HIS B 2 17  ? 1.189   11.232  42.329  1.00 31.23  ? 17  HIS B CA  1 
ATOM   3742  C  C   . HIS B 2 17  ? 0.604   12.245  43.283  1.00 31.60  ? 17  HIS B C   1 
ATOM   3743  O  O   . HIS B 2 17  ? 1.033   13.415  43.301  1.00 32.71  ? 17  HIS B O   1 
ATOM   3744  C  CB  . HIS B 2 17  ? 0.332   11.187  41.078  1.00 30.01  ? 17  HIS B CB  1 
ATOM   3745  C  CG  . HIS B 2 17  ? 0.885   10.292  40.007  1.00 32.95  ? 17  HIS B CG  1 
ATOM   3746  N  ND1 . HIS B 2 17  ? 2.191   10.376  39.583  1.00 30.66  ? 17  HIS B ND1 1 
ATOM   3747  C  CD2 . HIS B 2 17  ? 0.297   9.326   39.256  1.00 32.69  ? 17  HIS B CD2 1 
ATOM   3748  C  CE1 . HIS B 2 17  ? 2.389   9.490   38.621  1.00 31.60  ? 17  HIS B CE1 1 
ATOM   3749  N  NE2 . HIS B 2 17  ? 1.247   8.863   38.380  1.00 33.10  ? 17  HIS B NE2 1 
ATOM   3750  N  N   . ASP B 2 18  ? -0.355  11.801  44.094  1.00 32.36  ? 18  ASP B N   1 
ATOM   3751  C  CA  . ASP B 2 18  ? -0.860  12.636  45.180  1.00 34.99  ? 18  ASP B CA  1 
ATOM   3752  C  C   . ASP B 2 18  ? 0.268   13.047  46.097  1.00 34.29  ? 18  ASP B C   1 
ATOM   3753  O  O   . ASP B 2 18  ? 0.352   14.217  46.512  1.00 34.18  ? 18  ASP B O   1 
ATOM   3754  C  CB  . ASP B 2 18  ? -1.941  11.890  45.966  1.00 35.25  ? 18  ASP B CB  1 
ATOM   3755  C  CG  . ASP B 2 18  ? -3.270  11.887  45.273  1.00 40.77  ? 18  ASP B CG  1 
ATOM   3756  O  OD1 . ASP B 2 18  ? -3.474  12.697  44.337  1.00 40.77  ? 18  ASP B OD1 1 
ATOM   3757  O  OD2 . ASP B 2 18  ? -4.133  11.086  45.690  1.00 47.22  ? 18  ASP B OD2 1 
ATOM   3758  N  N   . TYR B 2 19  ? 1.147   12.097  46.417  1.00 31.15  ? 19  TYR B N   1 
ATOM   3759  C  CA  . TYR B 2 19  ? 2.284   12.384  47.286  1.00 34.15  ? 19  TYR B CA  1 
ATOM   3760  C  C   . TYR B 2 19  ? 3.174   13.475  46.708  1.00 30.17  ? 19  TYR B C   1 
ATOM   3761  O  O   . TYR B 2 19  ? 3.589   14.396  47.419  1.00 31.17  ? 19  TYR B O   1 
ATOM   3762  C  CB  . TYR B 2 19  ? 3.109   11.126  47.516  1.00 30.01  ? 19  TYR B CB  1 
ATOM   3763  C  CG  . TYR B 2 19  ? 4.396   11.453  48.272  1.00 31.52  ? 19  TYR B CG  1 
ATOM   3764  C  CD1 . TYR B 2 19  ? 5.551   11.810  47.593  1.00 30.48  ? 19  TYR B CD1 1 
ATOM   3765  C  CD2 . TYR B 2 19  ? 4.439   11.429  49.680  1.00 30.54  ? 19  TYR B CD2 1 
ATOM   3766  C  CE1 . TYR B 2 19  ? 6.720   12.159  48.290  1.00 31.56  ? 19  TYR B CE1 1 
ATOM   3767  C  CE2 . TYR B 2 19  ? 5.618   11.754  50.372  1.00 27.94  ? 19  TYR B CE2 1 
ATOM   3768  C  CZ  . TYR B 2 19  ? 6.724   12.111  49.670  1.00 30.88  ? 19  TYR B CZ  1 
ATOM   3769  O  OH  . TYR B 2 19  ? 7.855   12.436  50.345  1.00 33.18  ? 19  TYR B OH  1 
ATOM   3770  N  N   . ALA B 2 20  ? 3.488   13.373  45.421  1.00 30.05  ? 20  ALA B N   1 
ATOM   3771  C  CA  . ALA B 2 20  ? 4.343   14.352  44.765  1.00 29.41  ? 20  ALA B CA  1 
ATOM   3772  C  C   . ALA B 2 20  ? 3.720   15.743  44.801  1.00 28.69  ? 20  ALA B C   1 
ATOM   3773  O  O   . ALA B 2 20  ? 4.380   16.725  45.150  1.00 29.37  ? 20  ALA B O   1 
ATOM   3774  C  CB  . ALA B 2 20  ? 4.605   13.900  43.320  1.00 26.43  ? 20  ALA B CB  1 
ATOM   3775  N  N   A ARG B 2 21  ? 2.439   15.848  44.442  0.37 29.35  ? 21  ARG B N   1 
ATOM   3776  N  N   B ARG B 2 21  ? 2.450   15.845  44.420  0.63 29.29  ? 21  ARG B N   1 
ATOM   3777  C  CA  A ARG B 2 21  ? 1.807   17.166  44.409  0.37 32.02  ? 21  ARG B CA  1 
ATOM   3778  C  CA  B ARG B 2 21  ? 1.795   17.150  44.420  0.63 32.04  ? 21  ARG B CA  1 
ATOM   3779  C  C   A ARG B 2 21  ? 1.720   17.784  45.806  0.37 32.65  ? 21  ARG B C   1 
ATOM   3780  C  C   B ARG B 2 21  ? 1.811   17.769  45.818  0.63 32.65  ? 21  ARG B C   1 
ATOM   3781  O  O   A ARG B 2 21  ? 1.807   19.007  45.949  0.37 33.99  ? 21  ARG B O   1 
ATOM   3782  O  O   B ARG B 2 21  ? 2.083   18.962  45.978  0.63 33.87  ? 21  ARG B O   1 
ATOM   3783  C  CB  A ARG B 2 21  ? 0.414   17.074  43.779  0.37 32.68  ? 21  ARG B CB  1 
ATOM   3784  C  CB  B ARG B 2 21  ? 0.364   16.995  43.912  0.63 32.76  ? 21  ARG B CB  1 
ATOM   3785  C  CG  A ARG B 2 21  ? 0.356   16.495  42.357  0.37 31.35  ? 21  ARG B CG  1 
ATOM   3786  C  CG  B ARG B 2 21  ? 0.246   16.741  42.412  0.63 31.29  ? 21  ARG B CG  1 
ATOM   3787  C  CD  A ARG B 2 21  ? -1.030  16.738  41.727  0.37 31.86  ? 21  ARG B CD  1 
ATOM   3788  C  CD  B ARG B 2 21  ? -1.229  16.685  42.019  0.63 31.83  ? 21  ARG B CD  1 
ATOM   3789  N  NE  A ARG B 2 21  ? -1.307  15.857  40.593  0.37 32.13  ? 21  ARG B NE  1 
ATOM   3790  N  NE  B ARG B 2 21  ? -1.842  15.388  42.297  0.63 34.73  ? 21  ARG B NE  1 
ATOM   3791  C  CZ  A ARG B 2 21  ? -1.154  16.177  39.314  0.37 32.73  ? 21  ARG B CZ  1 
ATOM   3792  C  CZ  B ARG B 2 21  ? -1.904  14.387  41.422  0.63 33.33  ? 21  ARG B CZ  1 
ATOM   3793  N  NH1 A ARG B 2 21  ? -0.762  17.381  38.939  0.37 29.41  ? 21  ARG B NH1 1 
ATOM   3794  N  NH1 B ARG B 2 21  ? -1.421  14.508  40.196  0.63 32.92  ? 21  ARG B NH1 1 
ATOM   3795  N  NH2 A ARG B 2 21  ? -1.392  15.256  38.384  0.37 35.45  ? 21  ARG B NH2 1 
ATOM   3796  N  NH2 B ARG B 2 21  ? -2.496  13.249  41.776  0.63 34.53  ? 21  ARG B NH2 1 
ATOM   3797  N  N   . ASP B 2 22  ? 1.560   16.961  46.849  1.00 32.49  ? 22  ASP B N   1 
ATOM   3798  C  CA  . ASP B 2 22  ? 1.532   17.495  48.211  1.00 34.54  ? 22  ASP B CA  1 
ATOM   3799  C  C   . ASP B 2 22  ? 2.931   17.851  48.700  1.00 35.81  ? 22  ASP B C   1 
ATOM   3800  O  O   . ASP B 2 22  ? 3.103   18.825  49.442  1.00 33.78  ? 22  ASP B O   1 
ATOM   3801  C  CB  . ASP B 2 22  ? 0.888   16.488  49.150  1.00 36.38  ? 22  ASP B CB  1 
ATOM   3802  C  CG  . ASP B 2 22  ? 0.959   16.924  50.603  1.00 42.21  ? 22  ASP B CG  1 
ATOM   3803  O  OD1 . ASP B 2 22  ? 0.267   17.909  50.970  1.00 43.93  ? 22  ASP B OD1 1 
ATOM   3804  O  OD2 . ASP B 2 22  ? 1.740   16.311  51.366  1.00 44.61  ? 22  ASP B OD2 1 
ATOM   3805  N  N   . TRP B 2 23  ? 3.943   17.118  48.242  1.00 31.73  ? 23  TRP B N   1 
ATOM   3806  C  CA  . TRP B 2 23  ? 5.323   17.463  48.564  1.00 29.73  ? 23  TRP B CA  1 
ATOM   3807  C  C   . TRP B 2 23  ? 5.663   18.842  48.045  1.00 35.02  ? 23  TRP B C   1 
ATOM   3808  O  O   . TRP B 2 23  ? 6.353   19.617  48.712  1.00 35.79  ? 23  TRP B O   1 
ATOM   3809  C  CB  . TRP B 2 23  ? 6.261   16.425  47.964  1.00 32.09  ? 23  TRP B CB  1 
ATOM   3810  C  CG  . TRP B 2 23  ? 7.695   16.637  48.272  1.00 32.55  ? 23  TRP B CG  1 
ATOM   3811  C  CD1 . TRP B 2 23  ? 8.365   16.105  49.284  1.00 30.68  ? 23  TRP B CD1 1 
ATOM   3812  C  CD2 . TRP B 2 23  ? 8.636   17.443  47.540  1.00 28.90  ? 23  TRP B CD2 1 
ATOM   3813  N  NE1 . TRP B 2 23  ? 9.665   16.532  49.272  1.00 31.26  ? 23  TRP B NE1 1 
ATOM   3814  C  CE2 . TRP B 2 23  ? 9.857   17.326  48.181  1.00 26.34  ? 23  TRP B CE2 1 
ATOM   3815  C  CE3 . TRP B 2 23  ? 8.557   18.223  46.384  1.00 29.96  ? 23  TRP B CE3 1 
ATOM   3816  C  CZ2 . TRP B 2 23  ? 11.020  17.975  47.724  1.00 29.03  ? 23  TRP B CZ2 1 
ATOM   3817  C  CZ3 . TRP B 2 23  ? 9.699   18.877  45.948  1.00 32.11  ? 23  TRP B CZ3 1 
ATOM   3818  C  CH2 . TRP B 2 23  ? 10.920  18.740  46.625  1.00 28.59  ? 23  TRP B CH2 1 
ATOM   3819  N  N   . LYS B 2 24  ? 5.187   19.167  46.846  1.00 30.99  ? 24  LYS B N   1 
ATOM   3820  C  CA  . LYS B 2 24  ? 5.458   20.488  46.285  1.00 33.56  ? 24  LYS B CA  1 
ATOM   3821  C  C   . LYS B 2 24  ? 4.812   21.574  47.137  1.00 36.94  ? 24  LYS B C   1 
ATOM   3822  O  O   . LYS B 2 24  ? 5.410   22.633  47.380  1.00 37.40  ? 24  LYS B O   1 
ATOM   3823  C  CB  . LYS B 2 24  ? 4.909   20.529  44.873  1.00 33.47  ? 24  LYS B CB  1 
ATOM   3824  C  CG  . LYS B 2 24  ? 5.695   19.693  43.910  1.00 33.71  ? 24  LYS B CG  1 
ATOM   3825  C  CD  . LYS B 2 24  ? 5.118   19.880  42.514  1.00 32.95  ? 24  LYS B CD  1 
ATOM   3826  C  CE  . LYS B 2 24  ? 5.532   21.192  41.886  1.00 37.07  ? 24  LYS B CE  1 
ATOM   3827  N  NZ  . LYS B 2 24  ? 4.859   21.245  40.564  1.00 39.39  ? 24  LYS B NZ  1 
ATOM   3828  N  N   . VAL B 2 25  ? 3.581   21.328  47.591  1.00 35.93  ? 25  VAL B N   1 
ATOM   3829  C  CA  . VAL B 2 25  ? 2.912   22.274  48.483  1.00 40.15  ? 25  VAL B CA  1 
ATOM   3830  C  C   . VAL B 2 25  ? 3.713   22.466  49.770  1.00 41.34  ? 25  VAL B C   1 
ATOM   3831  O  O   . VAL B 2 25  ? 3.922   23.599  50.227  1.00 40.69  ? 25  VAL B O   1 
ATOM   3832  C  CB  . VAL B 2 25  ? 1.467   21.812  48.755  1.00 37.12  ? 25  VAL B CB  1 
ATOM   3833  C  CG1 . VAL B 2 25  ? 0.788   22.781  49.718  1.00 42.68  ? 25  VAL B CG1 1 
ATOM   3834  C  CG2 . VAL B 2 25  ? 0.681   21.840  47.461  1.00 41.07  ? 25  VAL B CG2 1 
ATOM   3835  N  N   . ARG B 2 26  ? 4.204   21.371  50.347  1.00 37.74  ? 26  ARG B N   1 
ATOM   3836  C  CA  . ARG B 2 26  ? 4.855   21.419  51.658  1.00 42.97  ? 26  ARG B CA  1 
ATOM   3837  C  C   . ARG B 2 26  ? 6.226   22.083  51.598  1.00 41.62  ? 26  ARG B C   1 
ATOM   3838  O  O   . ARG B 2 26  ? 6.627   22.757  52.551  1.00 40.56  ? 26  ARG B O   1 
ATOM   3839  C  CB  . ARG B 2 26  ? 5.009   20.001  52.227  1.00 43.50  ? 26  ARG B CB  1 
ATOM   3840  C  CG  . ARG B 2 26  ? 3.699   19.332  52.630  1.00 42.65  ? 26  ARG B CG  1 
ATOM   3841  C  CD  . ARG B 2 26  ? 3.904   18.021  53.418  1.00 43.20  ? 26  ARG B CD  1 
ATOM   3842  N  NE  . ARG B 2 26  ? 4.358   16.890  52.597  1.00 39.49  ? 26  ARG B NE  1 
ATOM   3843  C  CZ  . ARG B 2 26  ? 5.544   16.298  52.757  1.00 43.22  ? 26  ARG B CZ  1 
ATOM   3844  N  NH1 . ARG B 2 26  ? 6.423   16.747  53.634  1.00 43.42  ? 26  ARG B NH1 1 
ATOM   3845  N  NH2 . ARG B 2 26  ? 5.850   15.214  52.035  1.00 35.88  ? 26  ARG B NH2 1 
ATOM   3846  N  N   . THR B 2 27  ? 6.971   21.872  50.517  1.00 38.24  ? 27  THR B N   1 
ATOM   3847  C  CA  . THR B 2 27  ? 8.363   22.299  50.420  1.00 37.34  ? 27  THR B CA  1 
ATOM   3848  C  C   . THR B 2 27  ? 8.585   23.482  49.501  1.00 37.56  ? 27  THR B C   1 
ATOM   3849  O  O   . THR B 2 27  ? 9.616   24.144  49.610  1.00 40.52  ? 27  THR B O   1 
ATOM   3850  C  CB  . THR B 2 27  ? 9.243   21.150  49.894  1.00 37.83  ? 27  THR B CB  1 
ATOM   3851  O  OG1 . THR B 2 27  ? 8.922   20.893  48.520  1.00 37.98  ? 27  THR B OG1 1 
ATOM   3852  C  CG2 . THR B 2 27  ? 9.056   19.886  50.703  1.00 35.77  ? 27  THR B CG2 1 
ATOM   3853  N  N   . GLY B 2 28  ? 7.683   23.747  48.572  1.00 40.44  ? 28  GLY B N   1 
ATOM   3854  C  CA  . GLY B 2 28  ? 8.014   24.716  47.545  1.00 41.36  ? 28  GLY B CA  1 
ATOM   3855  C  C   . GLY B 2 28  ? 8.998   24.254  46.496  1.00 39.81  ? 28  GLY B C   1 
ATOM   3856  O  O   . GLY B 2 28  ? 9.389   25.066  45.649  1.00 40.31  ? 28  GLY B O   1 
ATOM   3857  N  N   . GLY B 2 29  ? 9.414   22.945  46.505  1.00 34.18  ? 29  GLY B N   1 
ATOM   3858  C  CA  . GLY B 2 29  ? 10.470  22.468  45.624  1.00 37.99  ? 29  GLY B CA  1 
ATOM   3859  C  C   . GLY B 2 29  ? 9.962   21.986  44.262  1.00 32.97  ? 29  GLY B C   1 
ATOM   3860  O  O   . GLY B 2 29  ? 8.745   21.882  44.056  1.00 35.50  ? 29  GLY B O   1 
ATOM   3861  N  N   . GLN B 2 30  ? 10.910  21.727  43.351  1.00 29.26  ? 30  GLN B N   1 
ATOM   3862  C  CA  . GLN B 2 30  ? 10.574  21.182  42.039  1.00 31.44  ? 30  GLN B CA  1 
ATOM   3863  C  C   . GLN B 2 30  ? 10.604  19.656  42.098  1.00 29.41  ? 30  GLN B C   1 
ATOM   3864  O  O   . GLN B 2 30  ? 11.256  19.076  42.954  1.00 28.47  ? 30  GLN B O   1 
ATOM   3865  C  CB  . GLN B 2 30  ? 11.508  21.651  40.916  1.00 34.50  ? 30  GLN B CB  1 
ATOM   3866  C  CG  . GLN B 2 30  ? 11.764  23.167  40.752  1.00 41.59  ? 30  GLN B CG  1 
ATOM   3867  C  CD  . GLN B 2 30  ? 12.729  23.446  39.566  1.00 46.05  ? 30  GLN B CD  1 
ATOM   3868  O  OE1 . GLN B 2 30  ? 12.682  22.743  38.543  1.00 43.66  ? 30  GLN B OE1 1 
ATOM   3869  N  NE2 . GLN B 2 30  ? 13.563  24.497  39.682  1.00 50.61  ? 30  GLN B NE2 1 
ATOM   3870  N  N   . VAL B 2 31  ? 9.850   19.030  41.196  1.00 26.90  ? 31  VAL B N   1 
ATOM   3871  C  CA  . VAL B 2 31  ? 9.813   17.575  41.032  1.00 24.73  ? 31  VAL B CA  1 
ATOM   3872  C  C   . VAL B 2 31  ? 10.462  17.244  39.689  1.00 27.17  ? 31  VAL B C   1 
ATOM   3873  O  O   . VAL B 2 31  ? 10.289  17.978  38.695  1.00 26.40  ? 31  VAL B O   1 
ATOM   3874  C  CB  . VAL B 2 31  ? 8.354   17.029  41.110  1.00 23.92  ? 31  VAL B CB  1 
ATOM   3875  C  CG1 . VAL B 2 31  ? 8.324   15.522  40.820  1.00 23.96  ? 31  VAL B CG1 1 
ATOM   3876  C  CG2 . VAL B 2 31  ? 7.778   17.317  42.559  1.00 27.22  ? 31  VAL B CG2 1 
ATOM   3877  N  N   . VAL B 2 32  ? 11.232  16.151  39.655  1.00 24.19  ? 32  VAL B N   1 
ATOM   3878  C  CA  . VAL B 2 32  ? 11.994  15.786  38.464  1.00 22.25  ? 32  VAL B CA  1 
ATOM   3879  C  C   . VAL B 2 32  ? 11.657  14.341  38.170  1.00 22.02  ? 32  VAL B C   1 
ATOM   3880  O  O   . VAL B 2 32  ? 11.839  13.487  39.038  1.00 24.30  ? 32  VAL B O   1 
ATOM   3881  C  CB  . VAL B 2 32  ? 13.507  15.965  38.707  1.00 23.50  ? 32  VAL B CB  1 
ATOM   3882  C  CG1 . VAL B 2 32  ? 14.318  15.685  37.367  1.00 23.96  ? 32  VAL B CG1 1 
ATOM   3883  C  CG2 . VAL B 2 32  ? 13.765  17.337  39.222  1.00 32.57  ? 32  VAL B CG2 1 
ATOM   3884  N  N   . ALA B 2 33  ? 11.126  14.073  36.979  1.00 20.91  ? 33  ALA B N   1 
ATOM   3885  C  CA  . ALA B 2 33  ? 10.860  12.690  36.558  1.00 23.26  ? 33  ALA B CA  1 
ATOM   3886  C  C   . ALA B 2 33  ? 12.185  12.068  36.169  1.00 24.21  ? 33  ALA B C   1 
ATOM   3887  O  O   . ALA B 2 33  ? 12.902  12.644  35.355  1.00 23.58  ? 33  ALA B O   1 
ATOM   3888  C  CB  . ALA B 2 33  ? 9.893   12.697  35.385  1.00 23.02  ? 33  ALA B CB  1 
ATOM   3889  N  N   . THR B 2 34  ? 12.538  10.938  36.770  1.00 21.83  ? 34  THR B N   1 
ATOM   3890  C  CA  . THR B 2 34  ? 13.833  10.300  36.549  1.00 22.92  ? 34  THR B CA  1 
ATOM   3891  C  C   . THR B 2 34  ? 13.625  8.997   35.801  1.00 23.27  ? 34  THR B C   1 
ATOM   3892  O  O   . THR B 2 34  ? 12.561  8.381   35.885  1.00 23.37  ? 34  THR B O   1 
ATOM   3893  C  CB  . THR B 2 34  ? 14.581  10.030  37.851  1.00 22.47  ? 34  THR B CB  1 
ATOM   3894  O  OG1 . THR B 2 34  ? 13.868  9.068   38.636  1.00 22.71  ? 34  THR B OG1 1 
ATOM   3895  C  CG2 . THR B 2 34  ? 14.783  11.378  38.695  1.00 22.32  ? 34  THR B CG2 1 
ATOM   3896  N  N   . MET B 2 35  ? 14.640  8.602   35.060  1.00 23.97  ? 35  MET B N   1 
ATOM   3897  C  CA  . MET B 2 35  ? 14.551  7.457   34.175  1.00 22.58  ? 35  MET B CA  1 
ATOM   3898  C  C   . MET B 2 35  ? 15.836  6.694   34.423  1.00 27.25  ? 35  MET B C   1 
ATOM   3899  O  O   . MET B 2 35  ? 16.923  7.292   34.371  1.00 27.10  ? 35  MET B O   1 
ATOM   3900  C  CB  . MET B 2 35  ? 14.487  7.917   32.731  1.00 21.73  ? 35  MET B CB  1 
ATOM   3901  C  CG  . MET B 2 35  ? 13.172  8.752   32.481  1.00 23.68  ? 35  MET B CG  1 
ATOM   3902  S  SD  . MET B 2 35  ? 12.870  9.014   30.748  1.00 25.67  ? 35  MET B SD  1 
ATOM   3903  C  CE  . MET B 2 35  ? 11.163  9.609   30.764  1.00 25.94  ? 35  MET B CE  1 
ATOM   3904  N  N   . CYS B 2 36  ? 15.706  5.387   34.599  1.00 25.53  ? 36  CYS B N   1 
ATOM   3905  C  CA  . CYS B 2 36  ? 16.795  4.457   34.911  1.00 27.49  ? 36  CYS B CA  1 
ATOM   3906  C  C   . CYS B 2 36  ? 17.432  4.703   36.280  1.00 27.17  ? 36  CYS B C   1 
ATOM   3907  O  O   . CYS B 2 36  ? 17.577  5.850   36.769  1.00 30.07  ? 36  CYS B O   1 
ATOM   3908  C  CB  . CYS B 2 36  ? 17.882  4.470   33.813  1.00 26.19  ? 36  CYS B CB  1 
ATOM   3909  S  SG  . CYS B 2 36  ? 19.217  3.261   34.154  1.00 24.12  ? 36  CYS B SG  1 
ATOM   3910  N  N   . THR B 2 37  ? 17.811  3.618   36.925  1.00 24.64  ? 37  THR B N   1 
ATOM   3911  C  CA  . THR B 2 37  ? 18.234  3.683   38.321  1.00 23.71  ? 37  THR B CA  1 
ATOM   3912  C  C   . THR B 2 37  ? 19.654  4.237   38.442  1.00 22.54  ? 37  THR B C   1 
ATOM   3913  O  O   . THR B 2 37  ? 20.091  4.478   39.556  1.00 21.58  ? 37  THR B O   1 
ATOM   3914  C  CB  . THR B 2 37  ? 18.183  2.286   38.934  1.00 27.59  ? 37  THR B CB  1 
ATOM   3915  O  OG1 . THR B 2 37  ? 18.961  1.450   38.068  1.00 23.34  ? 37  THR B OG1 1 
ATOM   3916  C  CG2 . THR B 2 37  ? 16.745  1.800   38.970  1.00 26.59  ? 37  THR B CG2 1 
ATOM   3917  N  N   . TYR B 2 38  ? 20.284  4.614   37.320  1.00 23.64  ? 38  TYR B N   1 
ATOM   3918  C  CA  . TYR B 2 38  ? 21.606  5.232   37.367  1.00 21.16  ? 38  TYR B CA  1 
ATOM   3919  C  C   . TYR B 2 38  ? 21.529  6.743   37.535  1.00 23.31  ? 38  TYR B C   1 
ATOM   3920  O  O   . TYR B 2 38  ? 22.566  7.375   37.684  1.00 24.38  ? 38  TYR B O   1 
ATOM   3921  C  CB  . TYR B 2 38  ? 22.415  4.875   36.103  1.00 20.59  ? 38  TYR B CB  1 
ATOM   3922  C  CG  . TYR B 2 38  ? 23.066  3.493   36.206  1.00 18.74  ? 38  TYR B CG  1 
ATOM   3923  C  CD1 . TYR B 2 38  ? 24.063  3.222   37.171  1.00 20.98  ? 38  TYR B CD1 1 
ATOM   3924  C  CD2 . TYR B 2 38  ? 22.746  2.487   35.284  1.00 24.95  ? 38  TYR B CD2 1 
ATOM   3925  C  CE1 . TYR B 2 38  ? 24.688  1.960   37.233  1.00 23.18  ? 38  TYR B CE1 1 
ATOM   3926  C  CE2 . TYR B 2 38  ? 23.332  1.244   35.357  1.00 24.04  ? 38  TYR B CE2 1 
ATOM   3927  C  CZ  . TYR B 2 38  ? 24.303  1.002   36.274  1.00 23.71  ? 38  TYR B CZ  1 
ATOM   3928  O  OH  . TYR B 2 38  ? 24.926  -0.200  36.281  1.00 25.42  ? 38  TYR B OH  1 
ATOM   3929  N  N   . THR B 2 39  ? 20.339  7.325   37.563  1.00 23.84  ? 39  THR B N   1 
ATOM   3930  C  CA  . THR B 2 39  ? 20.218  8.755   37.801  1.00 25.91  ? 39  THR B CA  1 
ATOM   3931  C  C   . THR B 2 39  ? 20.956  9.136   39.089  1.00 23.82  ? 39  THR B C   1 
ATOM   3932  O  O   . THR B 2 39  ? 20.761  8.478   40.116  1.00 22.43  ? 39  THR B O   1 
ATOM   3933  C  CB  . THR B 2 39  ? 18.752  9.156   37.943  1.00 26.03  ? 39  THR B CB  1 
ATOM   3934  O  OG1 . THR B 2 39  ? 18.116  9.089   36.663  1.00 25.60  ? 39  THR B OG1 1 
ATOM   3935  C  CG2 . THR B 2 39  ? 18.663  10.546  38.556  1.00 25.01  ? 39  THR B CG2 1 
ATOM   3936  N  N   . PRO B 2 40  ? 21.858  10.117  39.059  1.00 25.98  ? 40  PRO B N   1 
ATOM   3937  C  CA  . PRO B 2 40  ? 22.539  10.492  40.316  1.00 27.15  ? 40  PRO B CA  1 
ATOM   3938  C  C   . PRO B 2 40  ? 21.683  11.384  41.212  1.00 23.28  ? 40  PRO B C   1 
ATOM   3939  O  O   . PRO B 2 40  ? 21.765  12.611  41.286  1.00 23.47  ? 40  PRO B O   1 
ATOM   3940  C  CB  . PRO B 2 40  ? 23.830  11.130  39.811  1.00 25.66  ? 40  PRO B CB  1 
ATOM   3941  C  CG  . PRO B 2 40  ? 23.369  11.810  38.505  1.00 27.88  ? 40  PRO B CG  1 
ATOM   3942  C  CD  . PRO B 2 40  ? 22.418  10.817  37.890  1.00 27.60  ? 40  PRO B CD  1 
ATOM   3943  N  N   . GLU B 2 41  ? 20.807  10.700  41.925  1.00 22.84  ? 41  GLU B N   1 
ATOM   3944  C  CA  . GLU B 2 41  ? 19.761  11.320  42.725  1.00 25.80  ? 41  GLU B CA  1 
ATOM   3945  C  C   . GLU B 2 41  ? 20.322  12.297  43.734  1.00 22.64  ? 41  GLU B C   1 
ATOM   3946  O  O   . GLU B 2 41  ? 19.653  13.299  44.079  1.00 26.01  ? 41  GLU B O   1 
ATOM   3947  C  CB  . GLU B 2 41  ? 19.008  10.258  43.495  1.00 30.29  ? 41  GLU B CB  1 
ATOM   3948  C  CG  . GLU B 2 41  ? 17.981  9.539   42.792  1.00 38.08  ? 41  GLU B CG  1 
ATOM   3949  C  CD  . GLU B 2 41  ? 17.300  8.634   43.803  1.00 33.57  ? 41  GLU B CD  1 
ATOM   3950  O  OE1 . GLU B 2 41  ? 17.940  7.703   44.357  1.00 36.34  ? 41  GLU B OE1 1 
ATOM   3951  O  OE2 . GLU B 2 41  ? 16.137  8.941   44.114  1.00 42.69  ? 41  GLU B OE2 1 
ATOM   3952  N  N   . GLU B 2 42  ? 21.561  12.049  44.212  1.00 21.55  ? 42  GLU B N   1 
ATOM   3953  C  CA  . GLU B 2 42  ? 22.129  12.944  45.232  1.00 23.32  ? 42  GLU B CA  1 
ATOM   3954  C  C   . GLU B 2 42  ? 22.154  14.391  44.753  1.00 23.84  ? 42  GLU B C   1 
ATOM   3955  O  O   . GLU B 2 42  ? 21.953  15.327  45.548  1.00 23.73  ? 42  GLU B O   1 
ATOM   3956  C  CB  . GLU B 2 42  ? 23.559  12.513  45.579  1.00 24.37  ? 42  GLU B CB  1 
ATOM   3957  C  CG  . GLU B 2 42  ? 23.613  11.220  46.314  1.00 23.60  ? 42  GLU B CG  1 
ATOM   3958  C  CD  . GLU B 2 42  ? 23.592  9.992   45.353  1.00 24.19  ? 42  GLU B CD  1 
ATOM   3959  O  OE1 . GLU B 2 42  ? 23.391  10.118  44.099  1.00 24.99  ? 42  GLU B OE1 1 
ATOM   3960  O  OE2 . GLU B 2 42  ? 23.899  8.920   45.882  1.00 27.86  ? 42  GLU B OE2 1 
ATOM   3961  N  N   . LEU B 2 43  ? 22.421  14.590  43.465  1.00 22.47  ? 43  LEU B N   1 
ATOM   3962  C  CA  . LEU B 2 43  ? 22.490  15.934  42.895  1.00 22.06  ? 43  LEU B CA  1 
ATOM   3963  C  C   . LEU B 2 43  ? 21.124  16.594  42.892  1.00 23.53  ? 43  LEU B C   1 
ATOM   3964  O  O   . LEU B 2 43  ? 21.019  17.800  43.167  1.00 26.58  ? 43  LEU B O   1 
ATOM   3965  C  CB  . LEU B 2 43  ? 23.058  15.887  41.443  1.00 26.17  ? 43  LEU B CB  1 
ATOM   3966  C  CG  . LEU B 2 43  ? 24.614  15.915  41.347  1.00 25.29  ? 43  LEU B CG  1 
ATOM   3967  C  CD1 . LEU B 2 43  ? 25.313  14.784  42.086  1.00 29.95  ? 43  LEU B CD1 1 
ATOM   3968  C  CD2 . LEU B 2 43  ? 24.981  15.895  39.839  1.00 23.09  ? 43  LEU B CD2 1 
ATOM   3969  N  N   . LEU B 2 44  ? 20.085  15.863  42.474  1.00 22.06  ? 44  LEU B N   1 
ATOM   3970  C  CA  . LEU B 2 44  ? 18.734  16.413  42.476  1.00 24.04  ? 44  LEU B CA  1 
ATOM   3971  C  C   . LEU B 2 44  ? 18.284  16.782  43.884  1.00 24.94  ? 44  LEU B C   1 
ATOM   3972  O  O   . LEU B 2 44  ? 17.701  17.851  44.107  1.00 25.55  ? 44  LEU B O   1 
ATOM   3973  C  CB  . LEU B 2 44  ? 17.772  15.412  41.856  1.00 22.58  ? 44  LEU B CB  1 
ATOM   3974  C  CG  . LEU B 2 44  ? 18.181  15.040  40.404  1.00 26.29  ? 44  LEU B CG  1 
ATOM   3975  C  CD1 . LEU B 2 44  ? 17.292  13.931  39.854  1.00 26.33  ? 44  LEU B CD1 1 
ATOM   3976  C  CD2 . LEU B 2 44  ? 18.048  16.277  39.532  1.00 25.04  ? 44  LEU B CD2 1 
ATOM   3977  N  N   . ILE B 2 45  ? 18.557  15.916  44.867  1.00 21.26  ? 45  ILE B N   1 
ATOM   3978  C  CA  . ILE B 2 45  ? 18.194  16.200  46.242  1.00 25.39  ? 45  ILE B CA  1 
ATOM   3979  C  C   . ILE B 2 45  ? 18.933  17.438  46.733  1.00 24.49  ? 45  ILE B C   1 
ATOM   3980  O  O   . ILE B 2 45  ? 18.337  18.303  47.355  1.00 24.92  ? 45  ILE B O   1 
ATOM   3981  C  CB  . ILE B 2 45  ? 18.475  14.959  47.096  1.00 26.05  ? 45  ILE B CB  1 
ATOM   3982  C  CG1 . ILE B 2 45  ? 17.528  13.853  46.615  1.00 24.23  ? 45  ILE B CG1 1 
ATOM   3983  C  CG2 . ILE B 2 45  ? 18.446  15.266  48.642  1.00 26.48  ? 45  ILE B CG2 1 
ATOM   3984  C  CD1 . ILE B 2 45  ? 17.940  12.380  47.139  1.00 26.67  ? 45  ILE B CD1 1 
ATOM   3985  N  N   . ALA B 2 46  ? 20.231  17.545  46.417  1.00 26.01  ? 46  ALA B N   1 
ATOM   3986  C  CA  . ALA B 2 46  ? 21.025  18.681  46.872  1.00 27.62  ? 46  ALA B CA  1 
ATOM   3987  C  C   . ALA B 2 46  ? 20.512  19.963  46.231  1.00 29.37  ? 46  ALA B C   1 
ATOM   3988  O  O   . ALA B 2 46  ? 20.571  21.042  46.847  1.00 32.50  ? 46  ALA B O   1 
ATOM   3989  C  CB  . ALA B 2 46  ? 22.496  18.440  46.544  1.00 25.31  ? 46  ALA B CB  1 
ATOM   3990  N  N   . ALA B 2 47  ? 19.910  19.843  45.067  1.00 26.35  ? 47  ALA B N   1 
ATOM   3991  C  CA  . ALA B 2 47  ? 19.354  21.018  44.383  1.00 27.76  ? 47  ALA B CA  1 
ATOM   3992  C  C   . ALA B 2 47  ? 17.958  21.371  44.866  1.00 31.78  ? 47  ALA B C   1 
ATOM   3993  O  O   . ALA B 2 47  ? 17.339  22.248  44.249  1.00 30.56  ? 47  ALA B O   1 
ATOM   3994  C  CB  . ALA B 2 47  ? 19.335  20.800  42.865  1.00 29.36  ? 47  ALA B CB  1 
ATOM   3995  N  N   . GLY B 2 48  ? 17.451  20.684  45.909  1.00 30.50  ? 48  GLY B N   1 
ATOM   3996  C  CA  . GLY B 2 48  ? 16.149  20.974  46.493  1.00 28.36  ? 48  GLY B CA  1 
ATOM   3997  C  C   . GLY B 2 48  ? 14.973  20.312  45.798  1.00 24.97  ? 48  GLY B C   1 
ATOM   3998  O  O   . GLY B 2 48  ? 13.845  20.766  45.974  1.00 27.60  ? 48  GLY B O   1 
ATOM   3999  N  N   . MET B 2 49  ? 15.192  19.214  45.075  1.00 23.94  ? 49  MET B N   1 
ATOM   4000  C  CA  . MET B 2 49  ? 14.224  18.673  44.140  1.00 23.92  ? 49  MET B CA  1 
ATOM   4001  C  C   . MET B 2 49  ? 13.813  17.292  44.631  1.00 25.51  ? 49  MET B C   1 
ATOM   4002  O  O   . MET B 2 49  ? 14.549  16.674  45.402  1.00 28.02  ? 49  MET B O   1 
ATOM   4003  C  CB  . MET B 2 49  ? 14.874  18.545  42.733  1.00 24.31  ? 49  MET B CB  1 
ATOM   4004  C  CG  . MET B 2 49  ? 15.000  19.905  42.066  1.00 28.22  ? 49  MET B CG  1 
ATOM   4005  S  SD  . MET B 2 49  ? 15.735  19.591  40.451  1.00 31.85  ? 49  MET B SD  1 
ATOM   4006  C  CE  . MET B 2 49  ? 16.268  21.237  39.916  1.00 26.59  ? 49  MET B CE  1 
ATOM   4007  N  N   . LEU B 2 50  ? 12.595  16.873  44.256  1.00 23.73  ? 50  LEU B N   1 
ATOM   4008  C  CA  . LEU B 2 50  ? 12.091  15.523  44.541  1.00 22.02  ? 50  LEU B CA  1 
ATOM   4009  C  C   . LEU B 2 50  ? 12.308  14.641  43.287  1.00 23.18  ? 50  LEU B C   1 
ATOM   4010  O  O   . LEU B 2 50  ? 11.560  14.790  42.297  1.00 23.76  ? 50  LEU B O   1 
ATOM   4011  C  CB  . LEU B 2 50  ? 10.601  15.562  44.912  1.00 22.82  ? 50  LEU B CB  1 
ATOM   4012  C  CG  . LEU B 2 50  ? 9.965   14.172  45.165  1.00 27.34  ? 50  LEU B CG  1 
ATOM   4013  C  CD1 . LEU B 2 50  ? 10.548  13.583  46.439  1.00 29.21  ? 50  LEU B CD1 1 
ATOM   4014  C  CD2 . LEU B 2 50  ? 8.419   14.216  45.290  1.00 26.79  ? 50  LEU B CD2 1 
ATOM   4015  N  N   . PRO B 2 51  ? 13.236  13.694  43.293  1.00 23.09  ? 51  PRO B N   1 
ATOM   4016  C  CA  . PRO B 2 51  ? 13.322  12.742  42.161  1.00 23.22  ? 51  PRO B CA  1 
ATOM   4017  C  C   . PRO B 2 51  ? 12.172  11.743  42.241  1.00 25.18  ? 51  PRO B C   1 
ATOM   4018  O  O   . PRO B 2 51  ? 11.922  11.145  43.298  1.00 25.50  ? 51  PRO B O   1 
ATOM   4019  C  CB  . PRO B 2 51  ? 14.682  12.037  42.361  1.00 27.02  ? 51  PRO B CB  1 
ATOM   4020  C  CG  . PRO B 2 51  ? 15.223  12.497  43.691  1.00 27.21  ? 51  PRO B CG  1 
ATOM   4021  C  CD  . PRO B 2 51  ? 14.147  13.327  44.386  1.00 27.05  ? 51  PRO B CD  1 
ATOM   4022  N  N   . VAL B 2 52  ? 11.468  11.541  41.122  1.00 24.29  ? 52  VAL B N   1 
ATOM   4023  C  CA  . VAL B 2 52  ? 10.432  10.494  41.082  1.00 22.28  ? 52  VAL B CA  1 
ATOM   4024  C  C   . VAL B 2 52  ? 10.659  9.646   39.846  1.00 23.83  ? 52  VAL B C   1 
ATOM   4025  O  O   . VAL B 2 52  ? 10.593  10.151  38.725  1.00 22.79  ? 52  VAL B O   1 
ATOM   4026  C  CB  . VAL B 2 52  ? 9.012   11.079  41.110  1.00 24.47  ? 52  VAL B CB  1 
ATOM   4027  C  CG1 . VAL B 2 52  ? 8.794   11.882  42.428  1.00 22.36  ? 52  VAL B CG1 1 
ATOM   4028  C  CG2 . VAL B 2 52  ? 8.765   12.064  39.961  1.00 26.98  ? 52  VAL B CG2 1 
ATOM   4029  N  N   . ARG B 2 53  ? 10.940  8.351   40.061  1.00 24.02  ? 53  ARG B N   1 
ATOM   4030  C  CA  . ARG B 2 53  ? 11.206  7.433   38.975  1.00 24.26  ? 53  ARG B CA  1 
ATOM   4031  C  C   . ARG B 2 53  ? 9.949   7.160   38.180  1.00 23.61  ? 53  ARG B C   1 
ATOM   4032  O  O   . ARG B 2 53  ? 8.945   6.717   38.737  1.00 25.34  ? 53  ARG B O   1 
ATOM   4033  C  CB  . ARG B 2 53  ? 11.742  6.126   39.558  1.00 23.65  ? 53  ARG B CB  1 
ATOM   4034  C  CG  . ARG B 2 53  ? 11.874  5.048   38.498  1.00 31.89  ? 53  ARG B CG  1 
ATOM   4035  C  CD  . ARG B 2 53  ? 13.261  4.948   38.032  1.00 30.57  ? 53  ARG B CD  1 
ATOM   4036  N  NE  . ARG B 2 53  ? 13.400  3.871   37.042  1.00 39.48  ? 53  ARG B NE  1 
ATOM   4037  C  CZ  . ARG B 2 53  ? 13.331  2.555   37.225  1.00 32.47  ? 53  ARG B CZ  1 
ATOM   4038  N  NH1 . ARG B 2 53  ? 13.241  2.003   38.432  1.00 37.95  ? 53  ARG B NH1 1 
ATOM   4039  N  NH2 . ARG B 2 53  ? 13.391  1.763   36.158  1.00 36.77  ? 53  ARG B NH2 1 
ATOM   4040  N  N   . VAL B 2 54  ? 10.031  7.369   36.858  1.00 23.72  ? 54  VAL B N   1 
ATOM   4041  C  CA  . VAL B 2 54  ? 8.901   7.047   35.995  1.00 24.73  ? 54  VAL B CA  1 
ATOM   4042  C  C   . VAL B 2 54  ? 8.738   5.537   35.955  1.00 27.67  ? 54  VAL B C   1 
ATOM   4043  O  O   . VAL B 2 54  ? 9.706   4.809   35.720  1.00 26.64  ? 54  VAL B O   1 
ATOM   4044  C  CB  . VAL B 2 54  ? 9.147   7.579   34.575  1.00 25.69  ? 54  VAL B CB  1 
ATOM   4045  C  CG1 . VAL B 2 54  ? 8.033   7.047   33.659  1.00 26.03  ? 54  VAL B CG1 1 
ATOM   4046  C  CG2 . VAL B 2 54  ? 9.256   9.145   34.603  1.00 26.94  ? 54  VAL B CG2 1 
ATOM   4047  N  N   . LEU B 2 55  ? 7.541   5.061   36.230  1.00 26.74  ? 55  LEU B N   1 
ATOM   4048  C  CA  . LEU B 2 55  ? 7.267   3.632   36.065  1.00 29.82  ? 55  LEU B CA  1 
ATOM   4049  C  C   . LEU B 2 55  ? 6.017   3.490   35.205  1.00 34.18  ? 55  LEU B C   1 
ATOM   4050  O  O   . LEU B 2 55  ? 5.255   4.449   35.024  1.00 29.92  ? 55  LEU B O   1 
ATOM   4051  C  CB  . LEU B 2 55  ? 7.059   2.952   37.423  1.00 31.54  ? 55  LEU B CB  1 
ATOM   4052  C  CG  . LEU B 2 55  ? 8.334   3.063   38.279  1.00 34.69  ? 55  LEU B CG  1 
ATOM   4053  C  CD1 . LEU B 2 55  ? 8.067   2.650   39.733  1.00 33.52  ? 55  LEU B CD1 1 
ATOM   4054  C  CD2 . LEU B 2 55  ? 9.473   2.275   37.616  1.00 33.25  ? 55  LEU B CD2 1 
ATOM   4055  N  N   . GLY B 2 56  ? 5.799   2.289   34.693  1.00 33.15  ? 56  GLY B N   1 
ATOM   4056  C  CA  . GLY B 2 56  ? 4.602   2.058   33.912  1.00 33.91  ? 56  GLY B CA  1 
ATOM   4057  C  C   . GLY B 2 56  ? 3.386   1.810   34.775  1.00 35.21  ? 56  GLY B C   1 
ATOM   4058  O  O   . GLY B 2 56  ? 3.475   1.606   35.987  1.00 38.53  ? 56  GLY B O   1 
ATOM   4059  N  N   . ALA B 2 57  ? 2.225   1.845   34.131  1.00 32.60  ? 57  ALA B N   1 
ATOM   4060  C  CA  . ALA B 2 57  ? 0.969   1.602   34.824  1.00 31.37  ? 57  ALA B CA  1 
ATOM   4061  C  C   . ALA B 2 57  ? 0.448   0.179   34.644  1.00 34.63  ? 57  ALA B C   1 
ATOM   4062  O  O   . ALA B 2 57  ? -0.524  -0.194  35.307  1.00 34.37  ? 57  ALA B O   1 
ATOM   4063  C  CB  . ALA B 2 57  ? -0.093  2.596   34.339  1.00 34.60  ? 57  ALA B CB  1 
ATOM   4064  N  N   . HIS B 2 58  ? 1.032   -0.604  33.740  1.00 34.56  ? 58  HIS B N   1 
ATOM   4065  C  CA  . HIS B 2 58  ? 0.588   -1.966  33.475  1.00 32.88  ? 58  HIS B CA  1 
ATOM   4066  C  C   . HIS B 2 58  ? -0.900  -1.998  33.140  1.00 36.70  ? 58  HIS B C   1 
ATOM   4067  O  O   . HIS B 2 58  ? -1.661  -2.800  33.672  1.00 36.69  ? 58  HIS B O   1 
ATOM   4068  C  CB  . HIS B 2 58  ? 0.880   -2.866  34.673  1.00 33.99  ? 58  HIS B CB  1 
ATOM   4069  C  CG  . HIS B 2 58  ? 2.321   -2.912  35.025  1.00 37.70  ? 58  HIS B CG  1 
ATOM   4070  N  ND1 . HIS B 2 58  ? 3.232   -3.686  34.338  1.00 37.71  ? 58  HIS B ND1 1 
ATOM   4071  C  CD2 . HIS B 2 58  ? 3.018   -2.272  35.992  1.00 38.02  ? 58  HIS B CD2 1 
ATOM   4072  C  CE1 . HIS B 2 58  ? 4.432   -3.513  34.862  1.00 32.66  ? 58  HIS B CE1 1 
ATOM   4073  N  NE2 . HIS B 2 58  ? 4.331   -2.652  35.861  1.00 36.22  ? 58  HIS B NE2 1 
ATOM   4074  N  N   . GLU B 2 59  ? -1.324  -1.087  32.276  1.00 37.60  ? 59  GLU B N   1 
ATOM   4075  C  CA  . GLU B 2 59  ? -2.688  -1.048  31.774  1.00 37.87  ? 59  GLU B CA  1 
ATOM   4076  C  C   . GLU B 2 59  ? -2.658  -0.804  30.269  1.00 38.41  ? 59  GLU B C   1 
ATOM   4077  O  O   . GLU B 2 59  ? -1.659  -0.306  29.728  1.00 33.61  ? 59  GLU B O   1 
ATOM   4078  C  CB  . GLU B 2 59  ? -3.522  0.042   32.472  1.00 41.85  ? 59  GLU B CB  1 
ATOM   4079  C  CG  . GLU B 2 59  ? -2.951  1.414   32.329  1.00 42.55  ? 59  GLU B CG  1 
ATOM   4080  C  CD  . GLU B 2 59  ? -3.588  2.423   33.275  1.00 50.36  ? 59  GLU B CD  1 
ATOM   4081  O  OE1 . GLU B 2 59  ? -3.840  2.056   34.447  1.00 51.32  ? 59  GLU B OE1 1 
ATOM   4082  O  OE2 . GLU B 2 59  ? -3.762  3.600   32.854  1.00 51.37  ? 59  GLU B OE2 1 
ATOM   4083  N  N   . PRO B 2 60  ? -3.735  -1.146  29.564  1.00 37.75  ? 60  PRO B N   1 
ATOM   4084  C  CA  . PRO B 2 60  ? -3.725  -0.949  28.107  1.00 35.92  ? 60  PRO B CA  1 
ATOM   4085  C  C   . PRO B 2 60  ? -3.547  0.527   27.762  1.00 38.60  ? 60  PRO B C   1 
ATOM   4086  O  O   . PRO B 2 60  ? -3.988  1.420   28.499  1.00 36.83  ? 60  PRO B O   1 
ATOM   4087  C  CB  . PRO B 2 60  ? -5.083  -1.495  27.656  1.00 42.28  ? 60  PRO B CB  1 
ATOM   4088  C  CG  . PRO B 2 60  ? -5.648  -2.225  28.828  1.00 41.01  ? 60  PRO B CG  1 
ATOM   4089  C  CD  . PRO B 2 60  ? -5.034  -1.640  30.051  1.00 37.54  ? 60  PRO B CD  1 
ATOM   4090  N  N   . GLN B 2 61  ? -2.812  0.780   26.679  1.00 36.89  ? 61  GLN B N   1 
ATOM   4091  C  CA  . GLN B 2 61  ? -2.505  2.151   26.291  1.00 37.04  ? 61  GLN B CA  1 
ATOM   4092  C  C   . GLN B 2 61  ? -2.256  2.160   24.795  1.00 41.12  ? 61  GLN B C   1 
ATOM   4093  O  O   . GLN B 2 61  ? -1.675  1.214   24.244  1.00 36.32  ? 61  GLN B O   1 
ATOM   4094  C  CB  . GLN B 2 61  ? -1.284  2.744   27.019  1.00 37.03  ? 61  GLN B CB  1 
ATOM   4095  C  CG  . GLN B 2 61  ? 0.038   2.069   26.664  1.00 34.62  ? 61  GLN B CG  1 
ATOM   4096  C  CD  . GLN B 2 61  ? 0.745   2.716   25.450  1.00 35.99  ? 61  GLN B CD  1 
ATOM   4097  O  OE1 . GLN B 2 61  ? 0.330   3.775   24.946  1.00 35.06  ? 61  GLN B OE1 1 
ATOM   4098  N  NE2 . GLN B 2 61  ? 1.759   2.033   24.928  1.00 35.39  ? 61  GLN B NE2 1 
ATOM   4099  N  N   . ASN B 2 62  ? -2.691  3.238   24.149  1.00 39.81  ? 62  ASN B N   1 
ATOM   4100  C  CA  . ASN B 2 62  ? -2.530  3.383   22.709  1.00 40.73  ? 62  ASN B CA  1 
ATOM   4101  C  C   . ASN B 2 62  ? -2.104  4.797   22.374  1.00 37.91  ? 62  ASN B C   1 
ATOM   4102  O  O   . ASN B 2 62  ? -2.525  5.363   21.367  1.00 47.06  ? 62  ASN B O   1 
ATOM   4103  C  CB  . ASN B 2 62  ? -3.817  3.035   21.949  1.00 48.76  ? 62  ASN B CB  1 
ATOM   4104  C  CG  . ASN B 2 62  ? -3.547  2.229   20.671  1.00 58.42  ? 62  ASN B CG  1 
ATOM   4105  O  OD1 . ASN B 2 62  ? -2.671  2.586   19.872  1.00 57.35  ? 62  ASN B OD1 1 
ATOM   4106  N  ND2 . ASN B 2 62  ? -4.322  1.153   20.460  1.00 61.76  ? 62  ASN B ND2 1 
ATOM   4107  N  N   . VAL B 2 63  ? -1.269  5.402   23.212  1.00 36.45  ? 63  VAL B N   1 
ATOM   4108  C  CA  . VAL B 2 63  ? -0.758  6.734   22.917  1.00 35.19  ? 63  VAL B CA  1 
ATOM   4109  C  C   . VAL B 2 63  ? 0.677   6.729   22.415  1.00 32.92  ? 63  VAL B C   1 
ATOM   4110  O  O   . VAL B 2 63  ? 1.150   7.774   21.930  1.00 32.09  ? 63  VAL B O   1 
ATOM   4111  C  CB  . VAL B 2 63  ? -0.860  7.654   24.151  1.00 32.44  ? 63  VAL B CB  1 
ATOM   4112  C  CG1 . VAL B 2 63  ? -2.310  7.791   24.543  1.00 40.47  ? 63  VAL B CG1 1 
ATOM   4113  C  CG2 . VAL B 2 63  ? -0.040  7.085   25.300  1.00 33.11  ? 63  VAL B CG2 1 
ATOM   4114  N  N   . THR B 2 64  ? 1.397   5.614   22.533  1.00 29.67  ? 64  THR B N   1 
ATOM   4115  C  CA  . THR B 2 64  ? 2.815   5.657   22.188  1.00 28.71  ? 64  THR B CA  1 
ATOM   4116  C  C   . THR B 2 64  ? 3.109   5.239   20.751  1.00 28.05  ? 64  THR B C   1 
ATOM   4117  O  O   . THR B 2 64  ? 4.245   5.405   20.315  1.00 27.74  ? 64  THR B O   1 
ATOM   4118  C  CB  . THR B 2 64  ? 3.666   4.800   23.131  1.00 29.96  ? 64  THR B CB  1 
ATOM   4119  O  OG1 . THR B 2 64  ? 3.283   3.426   23.013  1.00 32.37  ? 64  THR B OG1 1 
ATOM   4120  C  CG2 . THR B 2 64  ? 3.496   5.276   24.576  1.00 28.29  ? 64  THR B CG2 1 
ATOM   4121  N  N   . GLU B 2 65  ? 2.135   4.698   20.013  1.00 30.85  ? 65  GLU B N   1 
ATOM   4122  C  CA  . GLU B 2 65  ? 2.458   4.167   18.686  1.00 34.98  ? 65  GLU B CA  1 
ATOM   4123  C  C   . GLU B 2 65  ? 3.058   5.229   17.767  1.00 33.51  ? 65  GLU B C   1 
ATOM   4124  O  O   . GLU B 2 65  ? 4.003   4.900   17.030  1.00 33.54  ? 65  GLU B O   1 
ATOM   4125  C  CB  . GLU B 2 65  ? 1.214   3.513   18.063  1.00 37.69  ? 65  GLU B CB  1 
ATOM   4126  C  CG  . GLU B 2 65  ? 1.451   2.798   16.694  1.00 42.71  ? 65  GLU B CG  1 
ATOM   4127  C  CD  . GLU B 2 65  ? 1.571   3.751   15.470  1.00 46.50  ? 65  GLU B CD  1 
ATOM   4128  O  OE1 . GLU B 2 65  ? 1.020   4.888   15.536  1.00 45.70  ? 65  GLU B OE1 1 
ATOM   4129  O  OE2 . GLU B 2 65  ? 2.139   3.342   14.416  1.00 43.68  ? 65  GLU B OE2 1 
ATOM   4130  N  N   . PRO B 2 66  ? 2.629   6.499   17.800  1.00 30.50  ? 66  PRO B N   1 
ATOM   4131  C  CA  . PRO B 2 66  ? 3.294   7.527   16.974  1.00 32.70  ? 66  PRO B CA  1 
ATOM   4132  C  C   . PRO B 2 66  ? 4.718   7.900   17.424  1.00 30.84  ? 66  PRO B C   1 
ATOM   4133  O  O   . PRO B 2 66  ? 5.403   8.642   16.705  1.00 29.27  ? 66  PRO B O   1 
ATOM   4134  C  CB  . PRO B 2 66  ? 2.346   8.739   17.093  1.00 33.15  ? 66  PRO B CB  1 
ATOM   4135  C  CG  . PRO B 2 66  ? 1.125   8.245   17.631  1.00 36.02  ? 66  PRO B CG  1 
ATOM   4136  C  CD  . PRO B 2 66  ? 1.418   7.029   18.447  1.00 34.09  ? 66  PRO B CD  1 
ATOM   4137  N  N   . HIS B 2 67  ? 5.187   7.419   18.573  1.00 28.53  ? 67  HIS B N   1 
ATOM   4138  C  CA  . HIS B 2 67  ? 6.472   7.837   19.127  1.00 25.35  ? 67  HIS B CA  1 
ATOM   4139  C  C   . HIS B 2 67  ? 7.514   6.743   19.230  1.00 28.07  ? 67  HIS B C   1 
ATOM   4140  O  O   . HIS B 2 67  ? 8.704   7.058   19.176  1.00 26.98  ? 67  HIS B O   1 
ATOM   4141  C  CB  . HIS B 2 67  ? 6.300   8.464   20.531  1.00 26.70  ? 67  HIS B CB  1 
ATOM   4142  C  CG  . HIS B 2 67  ? 5.386   9.643   20.525  1.00 28.34  ? 67  HIS B CG  1 
ATOM   4143  N  ND1 . HIS B 2 67  ? 5.829   10.899  20.165  1.00 28.26  ? 67  HIS B ND1 1 
ATOM   4144  C  CD2 . HIS B 2 67  ? 4.045   9.744   20.682  1.00 29.37  ? 67  HIS B CD2 1 
ATOM   4145  C  CE1 . HIS B 2 67  ? 4.807   11.737  20.157  1.00 30.73  ? 67  HIS B CE1 1 
ATOM   4146  N  NE2 . HIS B 2 67  ? 3.712   11.067  20.469  1.00 28.69  ? 67  HIS B NE2 1 
ATOM   4147  N  N   . ILE B 2 68  ? 7.115   5.496   19.492  1.00 28.05  ? 68  ILE B N   1 
ATOM   4148  C  CA  . ILE B 2 68  ? 8.044   4.387   19.718  1.00 26.29  ? 68  ILE B CA  1 
ATOM   4149  C  C   . ILE B 2 68  ? 7.512   3.181   18.963  1.00 29.62  ? 68  ILE B C   1 
ATOM   4150  O  O   . ILE B 2 68  ? 6.361   2.776   19.160  1.00 29.49  ? 68  ILE B O   1 
ATOM   4151  C  CB  . ILE B 2 68  ? 8.217   4.037   21.213  1.00 25.78  ? 68  ILE B CB  1 
ATOM   4152  C  CG1 . ILE B 2 68  ? 8.809   5.237   21.951  1.00 27.56  ? 68  ILE B CG1 1 
ATOM   4153  C  CG2 . ILE B 2 68  ? 9.072   2.754   21.370  1.00 28.03  ? 68  ILE B CG2 1 
ATOM   4154  C  CD1 . ILE B 2 68  ? 9.019   5.067   23.417  1.00 26.82  ? 68  ILE B CD1 1 
ATOM   4155  N  N   . PHE B 2 69  ? 8.334   2.628   18.079  1.00 26.56  ? 69  PHE B N   1 
ATOM   4156  C  CA  . PHE B 2 69  ? 7.941   1.496   17.265  1.00 26.57  ? 69  PHE B CA  1 
ATOM   4157  C  C   . PHE B 2 69  ? 7.747   0.266   18.147  1.00 27.44  ? 69  PHE B C   1 
ATOM   4158  O  O   . PHE B 2 69  ? 8.439   0.099   19.160  1.00 26.38  ? 69  PHE B O   1 
ATOM   4159  C  CB  . PHE B 2 69  ? 9.010   1.279   16.210  1.00 26.20  ? 69  PHE B CB  1 
ATOM   4160  C  CG  . PHE B 2 69  ? 8.752   0.130   15.274  1.00 25.98  ? 69  PHE B CG  1 
ATOM   4161  C  CD1 . PHE B 2 69  ? 7.467   -0.136  14.804  1.00 28.12  ? 69  PHE B CD1 1 
ATOM   4162  C  CD2 . PHE B 2 69  ? 9.806   -0.667  14.841  1.00 26.83  ? 69  PHE B CD2 1 
ATOM   4163  C  CE1 . PHE B 2 69  ? 7.228   -1.173  13.901  1.00 30.35  ? 69  PHE B CE1 1 
ATOM   4164  C  CE2 . PHE B 2 69  ? 9.571   -1.713  13.956  1.00 28.22  ? 69  PHE B CE2 1 
ATOM   4165  C  CZ  . PHE B 2 69  ? 8.269   -1.962  13.490  1.00 29.30  ? 69  PHE B CZ  1 
ATOM   4166  N  N   . GLY B 2 70  ? 6.734   -0.537  17.814  1.00 28.26  ? 70  GLY B N   1 
ATOM   4167  C  CA  . GLY B 2 70  ? 6.324   -1.672  18.649  1.00 27.67  ? 70  GLY B CA  1 
ATOM   4168  C  C   . GLY B 2 70  ? 7.316   -2.808  18.763  1.00 31.07  ? 70  GLY B C   1 
ATOM   4169  O  O   . GLY B 2 70  ? 7.053   -3.790  19.481  1.00 30.27  ? 70  GLY B O   1 
ATOM   4170  N  N   . MET B 2 71  ? 8.465   -2.716  18.089  1.00 27.63  ? 71  MET B N   1 
ATOM   4171  C  CA  . MET B 2 71  ? 9.500   -3.698  18.326  1.00 29.40  ? 71  MET B CA  1 
ATOM   4172  C  C   . MET B 2 71  ? 10.200  -3.479  19.645  1.00 28.84  ? 71  MET B C   1 
ATOM   4173  O  O   . MET B 2 71  ? 11.037  -4.297  20.004  1.00 24.64  ? 71  MET B O   1 
ATOM   4174  C  CB  . MET B 2 71  ? 10.613  -3.695  17.273  1.00 26.75  ? 71  MET B CB  1 
ATOM   4175  C  CG  . MET B 2 71  ? 11.475  -2.427  17.333  1.00 27.19  ? 71  MET B CG  1 
ATOM   4176  S  SD  . MET B 2 71  ? 12.628  -2.313  15.920  1.00 26.55  ? 71  MET B SD  1 
ATOM   4177  C  CE  . MET B 2 71  ? 14.042  -3.177  16.634  1.00 23.13  ? 71  MET B CE  1 
ATOM   4178  N  N   . PHE B 2 72  ? 9.939   -2.384  20.352  1.00 23.36  ? 72  PHE B N   1 
ATOM   4179  C  CA  . PHE B 2 72  ? 10.673  -2.084  21.572  1.00 25.64  ? 72  PHE B CA  1 
ATOM   4180  C  C   . PHE B 2 72  ? 9.842   -2.490  22.782  1.00 24.71  ? 72  PHE B C   1 
ATOM   4181  O  O   . PHE B 2 72  ? 8.641   -2.772  22.686  1.00 22.41  ? 72  PHE B O   1 
ATOM   4182  C  CB  . PHE B 2 72  ? 11.053  -0.602  21.627  1.00 23.87  ? 72  PHE B CB  1 
ATOM   4183  C  CG  . PHE B 2 72  ? 12.040  -0.221  20.540  1.00 25.84  ? 72  PHE B CG  1 
ATOM   4184  C  CD1 . PHE B 2 72  ? 13.354  -0.736  20.590  1.00 26.23  ? 72  PHE B CD1 1 
ATOM   4185  C  CD2 . PHE B 2 72  ? 11.659  0.542   19.461  1.00 28.34  ? 72  PHE B CD2 1 
ATOM   4186  C  CE1 . PHE B 2 72  ? 14.294  -0.422  19.607  1.00 26.18  ? 72  PHE B CE1 1 
ATOM   4187  C  CE2 . PHE B 2 72  ? 12.583  0.826   18.448  1.00 26.15  ? 72  PHE B CE2 1 
ATOM   4188  C  CZ  . PHE B 2 72  ? 13.908  0.335   18.547  1.00 25.95  ? 72  PHE B CZ  1 
ATOM   4189  N  N   . CYS B 2 73  ? 10.504  -2.506  23.924  1.00 23.93  ? 73  CYS B N   1 
ATOM   4190  C  CA  . CYS B 2 73  ? 9.969   -3.223  25.078  1.00 24.23  ? 73  CYS B CA  1 
ATOM   4191  C  C   . CYS B 2 73  ? 8.687   -2.574  25.633  1.00 25.87  ? 73  CYS B C   1 
ATOM   4192  O  O   . CYS B 2 73  ? 8.435   -1.360  25.471  1.00 23.81  ? 73  CYS B O   1 
ATOM   4193  C  CB  . CYS B 2 73  ? 11.042  -3.321  26.167  1.00 23.35  ? 73  CYS B CB  1 
ATOM   4194  S  SG  . CYS B 2 73  ? 11.411  -1.751  27.047  1.00 22.32  ? 73  CYS B SG  1 
ATOM   4195  N  N   . PRO B 2 74  ? 7.843   -3.370  26.276  1.00 24.05  ? 74  PRO B N   1 
ATOM   4196  C  CA  . PRO B 2 74  ? 6.641   -2.814  26.928  1.00 28.36  ? 74  PRO B CA  1 
ATOM   4197  C  C   . PRO B 2 74  ? 6.953   -1.757  27.960  1.00 27.06  ? 74  PRO B C   1 
ATOM   4198  O  O   . PRO B 2 74  ? 6.185   -0.799  28.085  1.00 28.84  ? 74  PRO B O   1 
ATOM   4199  C  CB  . PRO B 2 74  ? 5.966   -4.052  27.556  1.00 30.41  ? 74  PRO B CB  1 
ATOM   4200  C  CG  . PRO B 2 74  ? 6.445   -5.196  26.715  1.00 32.14  ? 74  PRO B CG  1 
ATOM   4201  C  CD  . PRO B 2 74  ? 7.872   -4.850  26.285  1.00 23.59  ? 74  PRO B CD  1 
ATOM   4202  N  N   . PHE B 2 75  ? 8.071   -1.873  28.673  1.00 25.30  ? 75  PHE B N   1 
ATOM   4203  C  CA  . PHE B 2 75  ? 8.354   -0.924  29.738  1.00 28.67  ? 75  PHE B CA  1 
ATOM   4204  C  C   . PHE B 2 75  ? 8.642   0.463   29.167  1.00 25.10  ? 75  PHE B C   1 
ATOM   4205  O  O   . PHE B 2 75  ? 8.160   1.458   29.726  1.00 27.08  ? 75  PHE B O   1 
ATOM   4206  C  CB  . PHE B 2 75  ? 9.537   -1.401  30.567  1.00 26.54  ? 75  PHE B CB  1 
ATOM   4207  C  CG  . PHE B 2 75  ? 9.901   -0.470  31.687  1.00 28.37  ? 75  PHE B CG  1 
ATOM   4208  C  CD1 . PHE B 2 75  ? 8.954   -0.136  32.645  1.00 28.78  ? 75  PHE B CD1 1 
ATOM   4209  C  CD2 . PHE B 2 75  ? 11.180  -0.004  31.838  1.00 27.43  ? 75  PHE B CD2 1 
ATOM   4210  C  CE1 . PHE B 2 75  ? 9.269   0.707   33.744  1.00 30.00  ? 75  PHE B CE1 1 
ATOM   4211  C  CE2 . PHE B 2 75  ? 11.512  0.852   32.906  1.00 31.34  ? 75  PHE B CE2 1 
ATOM   4212  C  CZ  . PHE B 2 75  ? 10.574  1.185   33.878  1.00 28.44  ? 75  PHE B CZ  1 
ATOM   4213  N  N   . CYS B 2 76  ? 9.410   0.564   28.063  1.00 25.55  ? 76  CYS B N   1 
ATOM   4214  C  CA  . CYS B 2 76  ? 9.802   1.914   27.634  1.00 21.35  ? 76  CYS B CA  1 
ATOM   4215  C  C   . CYS B 2 76  ? 8.583   2.608   27.068  1.00 23.52  ? 76  CYS B C   1 
ATOM   4216  O  O   . CYS B 2 76  ? 8.467   3.857   27.124  1.00 25.09  ? 76  CYS B O   1 
ATOM   4217  C  CB  . CYS B 2 76  ? 10.882  1.990   26.558  1.00 26.85  ? 76  CYS B CB  1 
ATOM   4218  S  SG  . CYS B 2 76  ? 10.626  1.310   24.944  1.00 25.38  ? 76  CYS B SG  1 
ATOM   4219  N  N   . ARG B 2 77  ? 7.621   1.816   26.591  1.00 21.75  ? 77  ARG B N   1 
ATOM   4220  C  CA  . ARG B 2 77  ? 6.400   2.350   25.992  1.00 25.03  ? 77  ARG B CA  1 
ATOM   4221  C  C   . ARG B 2 77  ? 5.401   2.713   27.095  1.00 29.05  ? 77  ARG B C   1 
ATOM   4222  O  O   . ARG B 2 77  ? 4.899   3.838   27.122  1.00 25.93  ? 77  ARG B O   1 
ATOM   4223  C  CB  . ARG B 2 77  ? 5.814   1.344   24.966  1.00 28.92  ? 77  ARG B CB  1 
ATOM   4224  C  CG  . ARG B 2 77  ? 6.654   1.364   23.610  1.00 25.31  ? 77  ARG B CG  1 
ATOM   4225  C  CD  . ARG B 2 77  ? 6.726   -0.024  22.918  1.00 28.91  ? 77  ARG B CD  1 
ATOM   4226  N  NE  . ARG B 2 77  ? 5.372   -0.509  22.717  1.00 35.47  ? 77  ARG B NE  1 
ATOM   4227  C  CZ  . ARG B 2 77  ? 4.993   -1.777  22.855  1.00 37.48  ? 77  ARG B CZ  1 
ATOM   4228  N  NH1 . ARG B 2 77  ? 5.872   -2.759  23.052  1.00 37.84  ? 77  ARG B NH1 1 
ATOM   4229  N  NH2 . ARG B 2 77  ? 3.704   -2.068  22.763  1.00 39.39  ? 77  ARG B NH2 1 
ATOM   4230  N  N   . ASP B 2 78  ? 5.170   1.793   28.061  1.00 22.99  ? 78  ASP B N   1 
ATOM   4231  C  CA  . ASP B 2 78  ? 4.333   2.062   29.229  1.00 27.52  ? 78  ASP B CA  1 
ATOM   4232  C  C   . ASP B 2 78  ? 4.789   3.328   29.951  1.00 25.40  ? 78  ASP B C   1 
ATOM   4233  O  O   . ASP B 2 78  ? 3.980   4.192   30.289  1.00 26.67  ? 78  ASP B O   1 
ATOM   4234  C  CB  . ASP B 2 78  ? 4.408   0.858   30.175  1.00 26.76  ? 78  ASP B CB  1 
ATOM   4235  C  CG  . ASP B 2 78  ? 3.291   0.808   31.206  1.00 30.78  ? 78  ASP B CG  1 
ATOM   4236  O  OD1 . ASP B 2 78  ? 2.420   1.705   31.215  1.00 32.20  ? 78  ASP B OD1 1 
ATOM   4237  O  OD2 . ASP B 2 78  ? 3.267   -0.190  32.002  1.00 31.53  ? 78  ASP B OD2 1 
ATOM   4238  N  N   . SER B 2 79  ? 6.097   3.458   30.177  1.00 23.03  ? 79  SER B N   1 
ATOM   4239  C  CA  . SER B 2 79  ? 6.632   4.638   30.849  1.00 23.64  ? 79  SER B CA  1 
ATOM   4240  C  C   . SER B 2 79  ? 6.317   5.901   30.062  1.00 21.83  ? 79  SER B C   1 
ATOM   4241  O  O   . SER B 2 79  ? 5.884   6.896   30.636  1.00 23.52  ? 79  SER B O   1 
ATOM   4242  C  CB  . SER B 2 79  ? 8.147   4.476   31.000  1.00 25.53  ? 79  SER B CB  1 
ATOM   4243  O  OG  . SER B 2 79  ? 8.468   3.406   31.898  1.00 25.86  ? 79  SER B OG  1 
ATOM   4244  N  N   . LEU B 2 80  ? 6.591   5.902   28.749  1.00 23.14  ? 80  LEU B N   1 
ATOM   4245  C  CA  . LEU B 2 80  ? 6.326   7.087   27.942  1.00 24.65  ? 80  LEU B CA  1 
ATOM   4246  C  C   . LEU B 2 80  ? 4.842   7.447   27.982  1.00 26.61  ? 80  LEU B C   1 
ATOM   4247  O  O   . LEU B 2 80  ? 4.487   8.634   28.099  1.00 25.33  ? 80  LEU B O   1 
ATOM   4248  C  CB  . LEU B 2 80  ? 6.783   6.869   26.473  1.00 23.03  ? 80  LEU B CB  1 
ATOM   4249  C  CG  . LEU B 2 80  ? 6.426   8.037   25.536  1.00 22.61  ? 80  LEU B CG  1 
ATOM   4250  C  CD1 . LEU B 2 80  ? 7.066   9.345   26.058  1.00 24.18  ? 80  LEU B CD1 1 
ATOM   4251  C  CD2 . LEU B 2 80  ? 6.828   7.764   24.059  1.00 21.53  ? 80  LEU B CD2 1 
ATOM   4252  N  N   . ALA B 2 81  ? 3.966   6.446   27.941  1.00 24.62  ? 81  ALA B N   1 
ATOM   4253  C  CA  . ALA B 2 81  ? 2.532   6.741   27.969  1.00 24.93  ? 81  ALA B CA  1 
ATOM   4254  C  C   . ALA B 2 81  ? 2.170   7.553   29.208  1.00 25.18  ? 81  ALA B C   1 
ATOM   4255  O  O   . ALA B 2 81  ? 1.332   8.451   29.129  1.00 29.33  ? 81  ALA B O   1 
ATOM   4256  C  CB  . ALA B 2 81  ? 1.691   5.450   27.937  1.00 22.92  ? 81  ALA B CB  1 
ATOM   4257  N  N   . GLN B 2 82  ? 2.789   7.245   30.359  1.00 25.06  ? 82  GLN B N   1 
ATOM   4258  C  CA  . GLN B 2 82  ? 2.465   7.974   31.602  1.00 25.25  ? 82  GLN B CA  1 
ATOM   4259  C  C   . GLN B 2 82  ? 2.752   9.461   31.440  1.00 23.26  ? 82  GLN B C   1 
ATOM   4260  O  O   . GLN B 2 82  ? 1.985   10.306  31.941  1.00 28.48  ? 82  GLN B O   1 
ATOM   4261  C  CB  . GLN B 2 82  ? 3.258   7.445   32.802  1.00 26.25  ? 82  GLN B CB  1 
ATOM   4262  C  CG  . GLN B 2 82  ? 3.105   5.906   33.105  1.00 23.70  ? 82  GLN B CG  1 
ATOM   4263  C  CD  . GLN B 2 82  ? 1.712   5.489   32.960  1.00 30.31  ? 82  GLN B CD  1 
ATOM   4264  O  OE1 . GLN B 2 82  ? 0.870   5.940   33.712  1.00 29.41  ? 82  GLN B OE1 1 
ATOM   4265  N  NE2 . GLN B 2 82  ? 1.433   4.568   32.015  1.00 32.32  ? 82  GLN B NE2 1 
ATOM   4266  N  N   . GLY B 2 83  ? 3.839   9.804   30.748  1.00 26.81  ? 83  GLY B N   1 
ATOM   4267  C  CA  . GLY B 2 83  ? 4.094   11.206  30.434  1.00 24.31  ? 83  GLY B CA  1 
ATOM   4268  C  C   . GLY B 2 83  ? 3.069   11.784  29.482  1.00 26.43  ? 83  GLY B C   1 
ATOM   4269  O  O   . GLY B 2 83  ? 2.528   12.865  29.722  1.00 26.55  ? 83  GLY B O   1 
ATOM   4270  N  N   . LEU B 2 84  ? 2.809   11.082  28.372  1.00 24.79  ? 84  LEU B N   1 
ATOM   4271  C  CA  . LEU B 2 84  ? 1.900   11.609  27.361  1.00 27.63  ? 84  LEU B CA  1 
ATOM   4272  C  C   . LEU B 2 84  ? 0.496   11.798  27.905  1.00 29.33  ? 84  LEU B C   1 
ATOM   4273  O  O   . LEU B 2 84  ? -0.206  12.726  27.487  1.00 29.08  ? 84  LEU B O   1 
ATOM   4274  C  CB  . LEU B 2 84  ? 1.872   10.658  26.154  1.00 26.66  ? 84  LEU B CB  1 
ATOM   4275  C  CG  . LEU B 2 84  ? 3.241   10.553  25.510  1.00 29.29  ? 84  LEU B CG  1 
ATOM   4276  C  CD1 . LEU B 2 84  ? 3.172   9.501   24.401  1.00 26.32  ? 84  LEU B CD1 1 
ATOM   4277  C  CD2 . LEU B 2 84  ? 3.648   11.897  24.922  1.00 27.03  ? 84  LEU B CD2 1 
ATOM   4278  N  N   . LEU B 2 85  ? 0.076   10.962  28.865  1.00 27.56  ? 85  LEU B N   1 
ATOM   4279  C  CA  . LEU B 2 85  ? -1.280  11.007  29.371  1.00 28.45  ? 85  LEU B CA  1 
ATOM   4280  C  C   . LEU B 2 85  ? -1.452  12.073  30.436  1.00 27.92  ? 85  LEU B C   1 
ATOM   4281  O  O   . LEU B 2 85  ? -2.570  12.242  30.926  1.00 31.67  ? 85  LEU B O   1 
ATOM   4282  C  CB  . LEU B 2 85  ? -1.696  9.667   29.969  1.00 28.73  ? 85  LEU B CB  1 
ATOM   4283  C  CG  . LEU B 2 85  ? -1.862  8.527   28.958  1.00 30.63  ? 85  LEU B CG  1 
ATOM   4284  C  CD1 . LEU B 2 85  ? -2.080  7.245   29.723  1.00 33.33  ? 85  LEU B CD1 1 
ATOM   4285  C  CD2 . LEU B 2 85  ? -3.038  8.807   28.050  1.00 34.62  ? 85  LEU B CD2 1 
ATOM   4286  N  N   . GLY B 2 86  ? -0.367  12.784  30.789  1.00 26.82  ? 86  GLY B N   1 
ATOM   4287  C  CA  . GLY B 2 86  ? -0.428  13.878  31.754  1.00 28.86  ? 86  GLY B CA  1 
ATOM   4288  C  C   . GLY B 2 86  ? -0.232  13.466  33.202  1.00 28.95  ? 86  GLY B C   1 
ATOM   4289  O  O   . GLY B 2 86  ? -0.412  14.298  34.102  1.00 29.28  ? 86  GLY B O   1 
ATOM   4290  N  N   . ARG B 2 87  ? 0.153   12.216  33.465  1.00 26.94  ? 87  ARG B N   1 
ATOM   4291  C  CA  . ARG B 2 87  ? 0.184   11.765  34.852  1.00 28.69  ? 87  ARG B CA  1 
ATOM   4292  C  C   . ARG B 2 87  ? 1.422   12.252  35.617  1.00 29.85  ? 87  ARG B C   1 
ATOM   4293  O  O   . ARG B 2 87  ? 1.451   12.161  36.851  1.00 32.84  ? 87  ARG B O   1 
ATOM   4294  C  CB  . ARG B 2 87  ? 0.086   10.249  34.855  1.00 29.10  ? 87  ARG B CB  1 
ATOM   4295  C  CG  . ARG B 2 87  ? -1.307  9.792   34.409  1.00 28.92  ? 87  ARG B CG  1 
ATOM   4296  C  CD  . ARG B 2 87  ? -1.300  8.317   34.213  1.00 32.78  ? 87  ARG B CD  1 
ATOM   4297  N  NE  . ARG B 2 87  ? -2.604  7.878   33.744  1.00 35.34  ? 87  ARG B NE  1 
ATOM   4298  C  CZ  . ARG B 2 87  ? -2.893  6.619   33.433  1.00 39.51  ? 87  ARG B CZ  1 
ATOM   4299  N  NH1 . ARG B 2 87  ? -1.984  5.654   33.537  1.00 39.10  ? 87  ARG B NH1 1 
ATOM   4300  N  NH2 . ARG B 2 87  ? -4.135  6.319   33.039  1.00 42.10  ? 87  ARG B NH2 1 
ATOM   4301  N  N   . PHE B 2 88  ? 2.403   12.836  34.934  1.00 28.69  ? 88  PHE B N   1 
ATOM   4302  C  CA  . PHE B 2 88  ? 3.534   13.462  35.596  1.00 29.05  ? 88  PHE B CA  1 
ATOM   4303  C  C   . PHE B 2 88  ? 3.540   14.961  35.292  1.00 29.96  ? 88  PHE B C   1 
ATOM   4304  O  O   . PHE B 2 88  ? 4.601   15.589  35.247  1.00 29.40  ? 88  PHE B O   1 
ATOM   4305  C  CB  . PHE B 2 88  ? 4.854   12.805  35.182  1.00 29.11  ? 88  PHE B CB  1 
ATOM   4306  C  CG  . PHE B 2 88  ? 5.105   11.447  35.815  1.00 27.56  ? 88  PHE B CG  1 
ATOM   4307  C  CD1 . PHE B 2 88  ? 4.638   10.280  35.227  1.00 25.34  ? 88  PHE B CD1 1 
ATOM   4308  C  CD2 . PHE B 2 88  ? 5.867   11.340  36.966  1.00 28.81  ? 88  PHE B CD2 1 
ATOM   4309  C  CE1 . PHE B 2 88  ? 4.877   9.011   35.804  1.00 26.12  ? 88  PHE B CE1 1 
ATOM   4310  C  CE2 . PHE B 2 88  ? 6.116   10.089  37.549  1.00 29.67  ? 88  PHE B CE2 1 
ATOM   4311  C  CZ  . PHE B 2 88  ? 5.626   8.916   36.965  1.00 31.87  ? 88  PHE B CZ  1 
ATOM   4312  N  N   . ASP B 2 89  ? 2.352   15.552  35.111  1.00 27.96  ? 89  ASP B N   1 
ATOM   4313  C  CA  . ASP B 2 89  ? 2.283   16.972  34.778  1.00 28.25  ? 89  ASP B CA  1 
ATOM   4314  C  C   . ASP B 2 89  ? 2.825   17.880  35.894  1.00 32.22  ? 89  ASP B C   1 
ATOM   4315  O  O   . ASP B 2 89  ? 3.220   19.013  35.609  1.00 34.14  ? 89  ASP B O   1 
ATOM   4316  C  CB  . ASP B 2 89  ? 0.829   17.321  34.363  1.00 31.20  ? 89  ASP B CB  1 
ATOM   4317  C  CG  . ASP B 2 89  ? -0.214  17.175  35.491  1.00 36.77  ? 89  ASP B CG  1 
ATOM   4318  O  OD1 . ASP B 2 89  ? 0.089   16.699  36.607  1.00 35.13  ? 89  ASP B OD1 1 
ATOM   4319  O  OD2 . ASP B 2 89  ? -1.388  17.538  35.241  1.00 44.14  ? 89  ASP B OD2 1 
ATOM   4320  N  N   . TYR B 2 90  ? 2.950   17.385  37.127  1.00 27.04  ? 90  TYR B N   1 
ATOM   4321  C  CA  . TYR B 2 90  ? 3.536   18.195  38.194  1.00 29.92  ? 90  TYR B CA  1 
ATOM   4322  C  C   . TYR B 2 90  ? 5.066   18.230  38.139  1.00 28.82  ? 90  TYR B C   1 
ATOM   4323  O  O   . TYR B 2 90  ? 5.671   18.991  38.915  1.00 28.12  ? 90  TYR B O   1 
ATOM   4324  C  CB  . TYR B 2 90  ? 3.110   17.667  39.566  1.00 29.33  ? 90  TYR B CB  1 
ATOM   4325  C  CG  . TYR B 2 90  ? 3.407   16.181  39.672  1.00 29.22  ? 90  TYR B CG  1 
ATOM   4326  C  CD1 . TYR B 2 90  ? 4.707   15.696  39.955  1.00 26.85  ? 90  TYR B CD1 1 
ATOM   4327  C  CD2 . TYR B 2 90  ? 2.395   15.258  39.485  1.00 33.37  ? 90  TYR B CD2 1 
ATOM   4328  C  CE1 . TYR B 2 90  ? 4.977   14.318  40.023  1.00 28.93  ? 90  TYR B CE1 1 
ATOM   4329  C  CE2 . TYR B 2 90  ? 2.652   13.899  39.547  1.00 29.50  ? 90  TYR B CE2 1 
ATOM   4330  C  CZ  . TYR B 2 90  ? 3.927   13.431  39.853  1.00 29.61  ? 90  TYR B CZ  1 
ATOM   4331  O  OH  . TYR B 2 90  ? 4.134   12.076  39.906  1.00 27.16  ? 90  TYR B OH  1 
ATOM   4332  N  N   . ALA B 2 91  ? 5.711   17.478  37.231  1.00 27.16  ? 91  ALA B N   1 
ATOM   4333  C  CA  . ALA B 2 91  ? 7.175   17.400  37.190  1.00 25.23  ? 91  ALA B CA  1 
ATOM   4334  C  C   . ALA B 2 91  ? 7.713   18.469  36.236  1.00 29.92  ? 91  ALA B C   1 
ATOM   4335  O  O   . ALA B 2 91  ? 7.431   18.431  35.030  1.00 34.81  ? 91  ALA B O   1 
ATOM   4336  C  CB  . ALA B 2 91  ? 7.655   16.023  36.735  1.00 27.32  ? 91  ALA B CB  1 
ATOM   4337  N  N   . GLU B 2 92  ? 8.562   19.359  36.753  1.00 29.16  ? 92  GLU B N   1 
ATOM   4338  C  CA  . GLU B 2 92  ? 9.176   20.366  35.901  1.00 26.91  ? 92  GLU B CA  1 
ATOM   4339  C  C   . GLU B 2 92  ? 10.323  19.797  35.091  1.00 26.21  ? 92  GLU B C   1 
ATOM   4340  O  O   . GLU B 2 92  ? 10.534  20.249  33.978  1.00 27.49  ? 92  GLU B O   1 
ATOM   4341  C  CB  . GLU B 2 92  ? 9.695   21.524  36.739  1.00 28.83  ? 92  GLU B CB  1 
ATOM   4342  C  CG  . GLU B 2 92  ? 8.594   22.442  37.356  1.00 34.66  ? 92  GLU B CG  1 
ATOM   4343  C  CD  . GLU B 2 92  ? 8.134   22.022  38.777  1.00 39.54  ? 92  GLU B CD  1 
ATOM   4344  O  OE1 . GLU B 2 92  ? 8.384   20.858  39.241  1.00 33.17  ? 92  GLU B OE1 1 
ATOM   4345  O  OE2 . GLU B 2 92  ? 7.564   22.901  39.477  1.00 35.78  ? 92  GLU B OE2 1 
ATOM   4346  N  N   . GLY B 2 93  ? 11.077  18.826  35.618  1.00 26.64  ? 93  GLY B N   1 
ATOM   4347  C  CA  . GLY B 2 93  ? 12.262  18.335  34.947  1.00 24.42  ? 93  GLY B CA  1 
ATOM   4348  C  C   . GLY B 2 93  ? 12.073  16.898  34.501  1.00 22.01  ? 93  GLY B C   1 
ATOM   4349  O  O   . GLY B 2 93  ? 11.175  16.182  34.968  1.00 23.64  ? 93  GLY B O   1 
ATOM   4350  N  N   . VAL B 2 94  ? 12.952  16.485  33.602  1.00 21.11  ? 94  VAL B N   1 
ATOM   4351  C  CA  . VAL B 2 94  ? 13.076  15.061  33.263  1.00 23.86  ? 94  VAL B CA  1 
ATOM   4352  C  C   . VAL B 2 94  ? 14.539  14.771  33.046  1.00 22.91  ? 94  VAL B C   1 
ATOM   4353  O  O   . VAL B 2 94  ? 15.253  15.581  32.446  1.00 22.66  ? 94  VAL B O   1 
ATOM   4354  C  CB  . VAL B 2 94  ? 12.207  14.670  32.051  1.00 19.36  ? 94  VAL B CB  1 
ATOM   4355  C  CG1 . VAL B 2 94  ? 12.628  15.397  30.794  1.00 22.33  ? 94  VAL B CG1 1 
ATOM   4356  C  CG2 . VAL B 2 94  ? 12.268  13.101  31.833  1.00 21.55  ? 94  VAL B CG2 1 
ATOM   4357  N  N   . THR B 2 95  ? 14.999  13.596  33.503  1.00 19.54  ? 95  THR B N   1 
ATOM   4358  C  CA  . THR B 2 95  ? 16.411  13.299  33.359  1.00 18.29  ? 95  THR B CA  1 
ATOM   4359  C  C   . THR B 2 95  ? 16.593  11.787  33.236  1.00 20.37  ? 95  THR B C   1 
ATOM   4360  O  O   . THR B 2 95  ? 15.909  11.023  33.917  1.00 22.45  ? 95  THR B O   1 
ATOM   4361  C  CB  . THR B 2 95  ? 17.247  13.876  34.527  1.00 21.63  ? 95  THR B CB  1 
ATOM   4362  O  OG1 . THR B 2 95  ? 18.633  13.618  34.303  1.00 22.72  ? 95  THR B OG1 1 
ATOM   4363  C  CG2 . THR B 2 95  ? 16.819  13.292  35.943  1.00 22.16  ? 95  THR B CG2 1 
ATOM   4364  N  N   . LEU B 2 96  ? 17.498  11.387  32.366  1.00 22.26  ? 96  LEU B N   1 
ATOM   4365  C  CA  . LEU B 2 96  ? 17.872  10.003  32.154  1.00 19.60  ? 96  LEU B CA  1 
ATOM   4366  C  C   . LEU B 2 96  ? 19.381  9.906   32.299  1.00 23.03  ? 96  LEU B C   1 
ATOM   4367  O  O   . LEU B 2 96  ? 20.107  10.763  31.783  1.00 21.59  ? 96  LEU B O   1 
ATOM   4368  C  CB  . LEU B 2 96  ? 17.488  9.573   30.742  1.00 18.36  ? 96  LEU B CB  1 
ATOM   4369  C  CG  . LEU B 2 96  ? 18.160  8.285   30.301  1.00 20.12  ? 96  LEU B CG  1 
ATOM   4370  C  CD1 . LEU B 2 96  ? 17.616  7.153   31.093  1.00 23.64  ? 96  LEU B CD1 1 
ATOM   4371  C  CD2 . LEU B 2 96  ? 17.865  8.073   28.804  1.00 23.69  ? 96  LEU B CD2 1 
ATOM   4372  N  N   . THR B 2 97  ? 19.856  8.847   32.922  1.00 22.31  ? 97  THR B N   1 
ATOM   4373  C  CA  . THR B 2 97  ? 21.288  8.526   32.906  1.00 18.00  ? 97  THR B CA  1 
ATOM   4374  C  C   . THR B 2 97  ? 21.450  7.302   32.025  1.00 21.88  ? 97  THR B C   1 
ATOM   4375  O  O   . THR B 2 97  ? 20.698  6.324   32.180  1.00 23.33  ? 97  THR B O   1 
ATOM   4376  C  CB  . THR B 2 97  ? 21.854  8.336   34.318  1.00 20.71  ? 97  THR B CB  1 
ATOM   4377  O  OG1 . THR B 2 97  ? 21.850  9.601   34.984  1.00 23.13  ? 97  THR B OG1 1 
ATOM   4378  C  CG2 . THR B 2 97  ? 23.295  7.846   34.284  1.00 21.93  ? 97  THR B CG2 1 
ATOM   4379  N  N   . GLN B 2 98  ? 22.378  7.415   31.070  1.00 21.54  ? 98  GLN B N   1 
ATOM   4380  C  CA  . GLN B 2 98  ? 22.565  6.478   29.970  1.00 19.33  ? 98  GLN B CA  1 
ATOM   4381  C  C   . GLN B 2 98  ? 22.717  5.032   30.410  1.00 19.94  ? 98  GLN B C   1 
ATOM   4382  O  O   . GLN B 2 98  ? 23.569  4.698   31.245  1.00 21.78  ? 98  GLN B O   1 
ATOM   4383  C  CB  . GLN B 2 98  ? 23.836  6.901   29.237  1.00 23.66  ? 98  GLN B CB  1 
ATOM   4384  C  CG  . GLN B 2 98  ? 24.391  6.051   28.242  1.00 21.81  ? 98  GLN B CG  1 
ATOM   4385  C  CD  . GLN B 2 98  ? 25.469  6.810   27.487  1.00 21.82  ? 98  GLN B CD  1 
ATOM   4386  O  OE1 . GLN B 2 98  ? 25.131  7.610   26.602  1.00 24.92  ? 98  GLN B OE1 1 
ATOM   4387  N  NE2 . GLN B 2 98  ? 26.745  6.591   27.839  1.00 21.69  ? 98  GLN B NE2 1 
ATOM   4388  N  N   A SER B 2 99  ? 21.972  4.166   29.735  0.50 21.30  ? 99  SER B N   1 
ATOM   4389  N  N   B SER B 2 99  ? 21.878  4.168   29.853  0.50 21.31  ? 99  SER B N   1 
ATOM   4390  C  CA  A SER B 2 99  ? 22.073  2.735   29.951  0.50 20.47  ? 99  SER B CA  1 
ATOM   4391  C  CA  B SER B 2 99  ? 22.162  2.740   29.841  0.50 20.45  ? 99  SER B CA  1 
ATOM   4392  C  C   A SER B 2 99  ? 21.582  2.033   28.681  0.50 22.25  ? 99  SER B C   1 
ATOM   4393  C  C   B SER B 2 99  ? 21.447  2.179   28.613  0.50 22.29  ? 99  SER B C   1 
ATOM   4394  O  O   A SER B 2 99  ? 22.109  2.267   27.579  0.50 23.46  ? 99  SER B O   1 
ATOM   4395  O  O   B SER B 2 99  ? 21.687  2.647   27.483  0.50 21.47  ? 99  SER B O   1 
ATOM   4396  C  CB  A SER B 2 99  ? 21.249  2.334   31.184  0.50 21.90  ? 99  SER B CB  1 
ATOM   4397  C  CB  B SER B 2 99  ? 21.726  2.054   31.154  0.50 21.46  ? 99  SER B CB  1 
ATOM   4398  O  OG  A SER B 2 99  ? 19.905  2.809   31.055  0.50 25.15  ? 99  SER B OG  1 
ATOM   4399  O  OG  B SER B 2 99  ? 22.411  0.807   31.367  0.50 23.08  ? 99  SER B OG  1 
ATOM   4400  N  N   . CYS B 2 100 ? 20.515  1.251   28.821  1.00 21.43  ? 100 CYS B N   1 
ATOM   4401  C  CA  . CYS B 2 100 ? 19.848  0.613   27.688  1.00 21.79  ? 100 CYS B CA  1 
ATOM   4402  C  C   . CYS B 2 100 ? 19.401  1.617   26.610  1.00 19.92  ? 100 CYS B C   1 
ATOM   4403  O  O   . CYS B 2 100 ? 18.747  2.641   26.931  1.00 21.13  ? 100 CYS B O   1 
ATOM   4404  C  CB  . CYS B 2 100 ? 18.628  -0.157  28.194  1.00 26.08  ? 100 CYS B CB  1 
ATOM   4405  S  SG  . CYS B 2 100 ? 17.590  -0.843  26.882  1.00 24.44  ? 100 CYS B SG  1 
ATOM   4406  N  N   . ILE B 2 101 ? 19.661  1.299   25.328  1.00 20.87  ? 101 ILE B N   1 
ATOM   4407  C  CA  . ILE B 2 101 ? 19.321  2.302   24.294  1.00 18.73  ? 101 ILE B CA  1 
ATOM   4408  C  C   . ILE B 2 101 ? 17.801  2.430   24.081  1.00 19.24  ? 101 ILE B C   1 
ATOM   4409  O  O   . ILE B 2 101 ? 17.325  3.483   23.615  1.00 21.69  ? 101 ILE B O   1 
ATOM   4410  C  CB  . ILE B 2 101 ? 20.049  2.070   22.939  1.00 18.54  ? 101 ILE B CB  1 
ATOM   4411  C  CG1 . ILE B 2 101 ? 19.625  0.743   22.304  1.00 21.49  ? 101 ILE B CG1 1 
ATOM   4412  C  CG2 . ILE B 2 101 ? 21.581  2.158   23.119  1.00 19.14  ? 101 ILE B CG2 1 
ATOM   4413  C  CD1 . ILE B 2 101 ? 20.112  0.539   20.873  1.00 24.34  ? 101 ILE B CD1 1 
ATOM   4414  N  N   . GLN B 2 102 ? 17.028  1.386   24.357  1.00 18.98  ? 102 GLN B N   1 
ATOM   4415  C  CA  . GLN B 2 102 ? 15.573  1.489   24.209  1.00 19.85  ? 102 GLN B CA  1 
ATOM   4416  C  C   . GLN B 2 102 ? 15.005  2.547   25.125  1.00 23.91  ? 102 GLN B C   1 
ATOM   4417  O  O   . GLN B 2 102 ? 14.126  3.302   24.715  1.00 24.65  ? 102 GLN B O   1 
ATOM   4418  C  CB  . GLN B 2 102 ? 14.892  0.140   24.508  1.00 20.51  ? 102 GLN B CB  1 
ATOM   4419  C  CG  . GLN B 2 102 ? 15.406  -0.968  23.559  1.00 20.52  ? 102 GLN B CG  1 
ATOM   4420  C  CD  . GLN B 2 102 ? 14.478  -2.144  23.492  1.00 23.22  ? 102 GLN B CD  1 
ATOM   4421  O  OE1 . GLN B 2 102 ? 13.274  -2.043  23.776  1.00 23.92  ? 102 GLN B OE1 1 
ATOM   4422  N  NE2 . GLN B 2 102 ? 15.030  -3.278  23.099  1.00 23.75  ? 102 GLN B NE2 1 
ATOM   4423  N  N   . TYR B 2 103 ? 15.496  2.590   26.359  1.00 22.83  ? 103 TYR B N   1 
ATOM   4424  C  CA  . TYR B 2 103 ? 15.023  3.543   27.395  1.00 21.12  ? 103 TYR B CA  1 
ATOM   4425  C  C   . TYR B 2 103 ? 15.297  4.978   26.935  1.00 25.33  ? 103 TYR B C   1 
ATOM   4426  O  O   . TYR B 2 103 ? 14.558  5.861   27.296  1.00 24.78  ? 103 TYR B O   1 
ATOM   4427  C  CB  . TYR B 2 103 ? 15.753  3.260   28.702  1.00 28.38  ? 103 TYR B CB  1 
ATOM   4428  C  CG  . TYR B 2 103 ? 15.026  3.482   30.001  1.00 25.15  ? 103 TYR B CG  1 
ATOM   4429  C  CD1 . TYR B 2 103 ? 14.139  4.523   30.195  1.00 28.79  ? 103 TYR B CD1 1 
ATOM   4430  C  CD2 . TYR B 2 103 ? 15.289  2.645   31.071  1.00 33.06  ? 103 TYR B CD2 1 
ATOM   4431  C  CE1 . TYR B 2 103 ? 13.515  4.699   31.420  1.00 28.28  ? 103 TYR B CE1 1 
ATOM   4432  C  CE2 . TYR B 2 103 ? 14.670  2.796   32.293  1.00 29.90  ? 103 TYR B CE2 1 
ATOM   4433  C  CZ  . TYR B 2 103 ? 13.795  3.846   32.480  1.00 34.54  ? 103 TYR B CZ  1 
ATOM   4434  O  OH  . TYR B 2 103 ? 13.219  3.978   33.713  1.00 37.22  ? 103 TYR B OH  1 
ATOM   4435  N  N   . ARG B 2 104 ? 16.363  5.173   26.165  1.00 24.38  ? 104 ARG B N   1 
ATOM   4436  C  CA  . ARG B 2 104 ? 16.665  6.532   25.672  1.00 24.59  ? 104 ARG B CA  1 
ATOM   4437  C  C   . ARG B 2 104 ? 15.558  7.094   24.782  1.00 24.68  ? 104 ARG B C   1 
ATOM   4438  O  O   . ARG B 2 104 ? 15.386  8.331   24.694  1.00 22.48  ? 104 ARG B O   1 
ATOM   4439  C  CB  . ARG B 2 104 ? 17.987  6.519   24.930  1.00 24.40  ? 104 ARG B CB  1 
ATOM   4440  C  CG  . ARG B 2 104 ? 19.130  5.971   25.804  1.00 24.04  ? 104 ARG B CG  1 
ATOM   4441  C  CD  . ARG B 2 104 ? 20.460  5.915   25.050  1.00 24.44  ? 104 ARG B CD  1 
ATOM   4442  N  NE  . ARG B 2 104 ? 21.409  4.999   25.681  1.00 21.08  ? 104 ARG B NE  1 
ATOM   4443  C  CZ  . ARG B 2 104 ? 22.653  4.890   25.252  1.00 20.90  ? 104 ARG B CZ  1 
ATOM   4444  N  NH1 . ARG B 2 104 ? 23.104  5.655   24.252  1.00 20.15  ? 104 ARG B NH1 1 
ATOM   4445  N  NH2 . ARG B 2 104 ? 23.454  3.987   25.810  1.00 21.72  ? 104 ARG B NH2 1 
ATOM   4446  N  N   . GLN B 2 105 ? 14.771  6.233   24.143  1.00 23.80  ? 105 GLN B N   1 
ATOM   4447  C  CA  . GLN B 2 105 ? 13.589  6.703   23.427  1.00 26.39  ? 105 GLN B CA  1 
ATOM   4448  C  C   . GLN B 2 105 ? 12.520  7.270   24.350  1.00 26.83  ? 105 GLN B C   1 
ATOM   4449  O  O   . GLN B 2 105 ? 11.866  8.280   24.009  1.00 24.26  ? 105 GLN B O   1 
ATOM   4450  C  CB  . GLN B 2 105 ? 13.003  5.563   22.621  1.00 26.97  ? 105 GLN B CB  1 
ATOM   4451  C  CG  . GLN B 2 105 ? 13.985  5.008   21.663  1.00 23.36  ? 105 GLN B CG  1 
ATOM   4452  C  CD  . GLN B 2 105 ? 13.348  3.864   20.944  1.00 23.47  ? 105 GLN B CD  1 
ATOM   4453  O  OE1 . GLN B 2 105 ? 13.035  3.970   19.774  1.00 24.70  ? 105 GLN B OE1 1 
ATOM   4454  N  NE2 . GLN B 2 105 ? 13.065  2.773   21.684  1.00 22.85  ? 105 GLN B NE2 1 
ATOM   4455  N  N   . THR B 2 106 ? 12.272  6.627   25.501  1.00 21.20  ? 106 THR B N   1 
ATOM   4456  C  CA  . THR B 2 106 ? 11.324  7.191   26.444  1.00 21.58  ? 106 THR B CA  1 
ATOM   4457  C  C   . THR B 2 106 ? 11.700  8.623   26.738  1.00 23.27  ? 106 THR B C   1 
ATOM   4458  O  O   . THR B 2 106 ? 10.859  9.500   26.639  1.00 24.17  ? 106 THR B O   1 
ATOM   4459  C  CB  . THR B 2 106 ? 11.306  6.369   27.720  1.00 23.58  ? 106 THR B CB  1 
ATOM   4460  O  OG1 . THR B 2 106 ? 11.063  5.007   27.374  1.00 25.02  ? 106 THR B OG1 1 
ATOM   4461  C  CG2 . THR B 2 106 ? 10.215  6.796   28.698  1.00 22.69  ? 106 THR B CG2 1 
ATOM   4462  N  N   . PHE B 2 107 ? 12.967  8.846   27.098  1.00 21.90  ? 107 PHE B N   1 
ATOM   4463  C  CA  . PHE B 2 107 ? 13.471  10.187  27.416  1.00 20.53  ? 107 PHE B CA  1 
ATOM   4464  C  C   . PHE B 2 107 ? 13.305  11.148  26.238  1.00 21.19  ? 107 PHE B C   1 
ATOM   4465  O  O   . PHE B 2 107 ? 12.831  12.281  26.417  1.00 22.27  ? 107 PHE B O   1 
ATOM   4466  C  CB  . PHE B 2 107 ? 14.942  10.063  27.820  1.00 18.52  ? 107 PHE B CB  1 
ATOM   4467  C  CG  . PHE B 2 107 ? 15.602  11.408  28.033  1.00 20.63  ? 107 PHE B CG  1 
ATOM   4468  C  CD1 . PHE B 2 107 ? 15.401  12.074  29.235  1.00 20.24  ? 107 PHE B CD1 1 
ATOM   4469  C  CD2 . PHE B 2 107 ? 16.422  11.968  27.046  1.00 21.48  ? 107 PHE B CD2 1 
ATOM   4470  C  CE1 . PHE B 2 107 ? 15.983  13.367  29.450  1.00 20.65  ? 107 PHE B CE1 1 
ATOM   4471  C  CE2 . PHE B 2 107 ? 17.038  13.157  27.249  1.00 22.44  ? 107 PHE B CE2 1 
ATOM   4472  C  CZ  . PHE B 2 107 ? 16.819  13.881  28.476  1.00 23.83  ? 107 PHE B CZ  1 
ATOM   4473  N  N   . GLY B 2 108 ? 13.668  10.700  25.018  1.00 23.01  ? 108 GLY B N   1 
ATOM   4474  C  CA  . GLY B 2 108 ? 13.659  11.606  23.875  1.00 20.34  ? 108 GLY B CA  1 
ATOM   4475  C  C   . GLY B 2 108 ? 12.243  12.018  23.487  1.00 24.01  ? 108 GLY B C   1 
ATOM   4476  O  O   . GLY B 2 108 ? 11.971  13.200  23.241  1.00 26.47  ? 108 GLY B O   1 
ATOM   4477  N  N   . SER B 2 109 ? 11.319  11.059  23.444  1.00 20.83  ? 109 SER B N   1 
ATOM   4478  C  CA  . SER B 2 109 ? 9.936   11.411  23.151  1.00 21.41  ? 109 SER B CA  1 
ATOM   4479  C  C   . SER B 2 109 ? 9.322   12.235  24.290  1.00 23.93  ? 109 SER B C   1 
ATOM   4480  O  O   . SER B 2 109 ? 8.522   13.156  24.047  1.00 22.73  ? 109 SER B O   1 
ATOM   4481  C  CB  . SER B 2 109 ? 9.131   10.137  22.913  1.00 28.66  ? 109 SER B CB  1 
ATOM   4482  O  OG  . SER B 2 109 ? 9.550   9.466   21.716  1.00 25.10  ? 109 SER B OG  1 
ATOM   4483  N  N   . TRP B 2 110 ? 9.652   11.905  25.549  1.00 21.60  ? 110 TRP B N   1 
ATOM   4484  C  CA  . TRP B 2 110 ? 9.089   12.668  26.683  1.00 21.56  ? 110 TRP B CA  1 
ATOM   4485  C  C   . TRP B 2 110 ? 9.507   14.150  26.656  1.00 21.22  ? 110 TRP B C   1 
ATOM   4486  O  O   . TRP B 2 110 ? 8.680   15.055  26.845  1.00 23.74  ? 110 TRP B O   1 
ATOM   4487  C  CB  . TRP B 2 110 ? 9.556   12.003  27.966  1.00 22.36  ? 110 TRP B CB  1 
ATOM   4488  C  CG  . TRP B 2 110 ? 9.033   12.491  29.228  1.00 20.48  ? 110 TRP B CG  1 
ATOM   4489  C  CD1 . TRP B 2 110 ? 9.197   13.749  29.773  1.00 23.54  ? 110 TRP B CD1 1 
ATOM   4490  C  CD2 . TRP B 2 110 ? 8.300   11.722  30.192  1.00 22.03  ? 110 TRP B CD2 1 
ATOM   4491  N  NE1 . TRP B 2 110 ? 8.613   13.788  31.034  1.00 25.77  ? 110 TRP B NE1 1 
ATOM   4492  C  CE2 . TRP B 2 110 ? 8.053   12.564  31.306  1.00 24.85  ? 110 TRP B CE2 1 
ATOM   4493  C  CE3 . TRP B 2 110 ? 7.846   10.391  30.231  1.00 22.13  ? 110 TRP B CE3 1 
ATOM   4494  C  CZ2 . TRP B 2 110 ? 7.365   12.120  32.445  1.00 24.11  ? 110 TRP B CZ2 1 
ATOM   4495  C  CZ3 . TRP B 2 110 ? 7.176   9.941   31.367  1.00 23.15  ? 110 TRP B CZ3 1 
ATOM   4496  C  CH2 . TRP B 2 110 ? 6.931   10.809  32.453  1.00 25.17  ? 110 TRP B CH2 1 
ATOM   4497  N  N   . ARG B 2 111 ? 10.815  14.416  26.535  1.00 22.91  ? 111 ARG B N   1 
ATOM   4498  C  CA  . ARG B 2 111 ? 11.231  15.814  26.523  1.00 24.85  ? 111 ARG B CA  1 
ATOM   4499  C  C   . ARG B 2 111 ? 10.666  16.570  25.320  1.00 25.85  ? 111 ARG B C   1 
ATOM   4500  O  O   . ARG B 2 111 ? 10.448  17.788  25.402  1.00 25.27  ? 111 ARG B O   1 
ATOM   4501  C  CB  . ARG B 2 111 ? 12.759  15.933  26.584  1.00 26.49  ? 111 ARG B CB  1 
ATOM   4502  C  CG  . ARG B 2 111 ? 13.509  15.669  25.302  1.00 27.83  ? 111 ARG B CG  1 
ATOM   4503  C  CD  . ARG B 2 111 ? 15.048  15.718  25.535  1.00 29.21  ? 111 ARG B CD  1 
ATOM   4504  N  NE  . ARG B 2 111 ? 15.772  15.496  24.284  1.00 36.91  ? 111 ARG B NE  1 
ATOM   4505  C  CZ  . ARG B 2 111 ? 15.822  16.361  23.269  1.00 41.39  ? 111 ARG B CZ  1 
ATOM   4506  N  NH1 . ARG B 2 111 ? 15.168  17.514  23.293  1.00 45.19  ? 111 ARG B NH1 1 
ATOM   4507  N  NH2 . ARG B 2 111 ? 16.515  16.044  22.182  1.00 46.63  ? 111 ARG B NH2 1 
ATOM   4508  N  N   . LEU B 2 112 ? 10.390  15.881  24.206  1.00 23.43  ? 112 LEU B N   1 
ATOM   4509  C  CA  . LEU B 2 112 ? 9.881   16.582  23.032  1.00 24.07  ? 112 LEU B CA  1 
ATOM   4510  C  C   . LEU B 2 112 ? 8.377   16.820  23.104  1.00 28.29  ? 112 LEU B C   1 
ATOM   4511  O  O   . LEU B 2 112 ? 7.876   17.820  22.553  1.00 29.07  ? 112 LEU B O   1 
ATOM   4512  C  CB  . LEU B 2 112 ? 10.132  15.775  21.746  1.00 25.32  ? 112 LEU B CB  1 
ATOM   4513  C  CG  . LEU B 2 112 ? 11.489  15.807  21.048  1.00 31.96  ? 112 LEU B CG  1 
ATOM   4514  C  CD1 . LEU B 2 112 ? 11.558  14.647  20.007  1.00 29.15  ? 112 LEU B CD1 1 
ATOM   4515  C  CD2 . LEU B 2 112 ? 11.799  17.211  20.452  1.00 31.11  ? 112 LEU B CD2 1 
ATOM   4516  N  N   . HIS B 2 113 ? 7.631   15.922  23.759  1.00 23.04  ? 113 HIS B N   1 
ATOM   4517  C  CA  . HIS B 2 113 ? 6.161   15.904  23.641  1.00 23.30  ? 113 HIS B CA  1 
ATOM   4518  C  C   . HIS B 2 113 ? 5.363   16.083  24.927  1.00 26.80  ? 113 HIS B C   1 
ATOM   4519  O  O   . HIS B 2 113 ? 4.144   16.265  24.849  1.00 26.87  ? 113 HIS B O   1 
ATOM   4520  C  CB  . HIS B 2 113 ? 5.722   14.603  22.976  1.00 23.83  ? 113 HIS B CB  1 
ATOM   4521  C  CG  . HIS B 2 113 ? 6.233   14.483  21.589  1.00 25.97  ? 113 HIS B CG  1 
ATOM   4522  N  ND1 . HIS B 2 113 ? 5.750   15.248  20.548  1.00 29.67  ? 113 HIS B ND1 1 
ATOM   4523  C  CD2 . HIS B 2 113 ? 7.197   13.701  21.072  1.00 26.67  ? 113 HIS B CD2 1 
ATOM   4524  C  CE1 . HIS B 2 113 ? 6.386   14.914  19.433  1.00 29.22  ? 113 HIS B CE1 1 
ATOM   4525  N  NE2 . HIS B 2 113 ? 7.276   13.989  19.731  1.00 24.65  ? 113 HIS B NE2 1 
ATOM   4526  N  N   . VAL B 2 114 ? 5.976   16.055  26.102  1.00 26.38  ? 114 VAL B N   1 
ATOM   4527  C  CA  . VAL B 2 114 ? 5.263   16.310  27.350  1.00 24.51  ? 114 VAL B CA  1 
ATOM   4528  C  C   . VAL B 2 114 ? 5.331   17.819  27.599  1.00 25.65  ? 114 VAL B C   1 
ATOM   4529  O  O   . VAL B 2 114 ? 6.424   18.336  27.864  1.00 26.01  ? 114 VAL B O   1 
ATOM   4530  C  CB  . VAL B 2 114 ? 5.848   15.505  28.515  1.00 25.38  ? 114 VAL B CB  1 
ATOM   4531  C  CG1 . VAL B 2 114 ? 5.142   15.889  29.818  1.00 26.33  ? 114 VAL B CG1 1 
ATOM   4532  C  CG2 . VAL B 2 114 ? 5.689   14.004  28.224  1.00 23.42  ? 114 VAL B CG2 1 
ATOM   4533  N  N   . PRO B 2 115 ? 4.232   18.542  27.493  1.00 26.89  ? 115 PRO B N   1 
ATOM   4534  C  CA  . PRO B 2 115 ? 4.339   20.004  27.381  1.00 28.25  ? 115 PRO B CA  1 
ATOM   4535  C  C   . PRO B 2 115 ? 4.608   20.694  28.710  1.00 30.57  ? 115 PRO B C   1 
ATOM   4536  O  O   . PRO B 2 115 ? 4.967   21.875  28.702  1.00 29.43  ? 115 PRO B O   1 
ATOM   4537  C  CB  . PRO B 2 115 ? 2.986   20.411  26.798  1.00 30.07  ? 115 PRO B CB  1 
ATOM   4538  C  CG  . PRO B 2 115 ? 2.034   19.392  27.329  1.00 32.85  ? 115 PRO B CG  1 
ATOM   4539  C  CD  . PRO B 2 115 ? 2.844   18.067  27.336  1.00 26.27  ? 115 PRO B CD  1 
ATOM   4540  N  N   . THR B 2 116 ? 4.495   19.985  29.830  1.00 27.56  ? 116 THR B N   1 
ATOM   4541  C  CA  . THR B 2 116 ? 4.849   20.500  31.147  1.00 25.60  ? 116 THR B CA  1 
ATOM   4542  C  C   . THR B 2 116 ? 6.345   20.384  31.466  1.00 26.45  ? 116 THR B C   1 
ATOM   4543  O  O   . THR B 2 116 ? 6.761   20.863  32.514  1.00 26.62  ? 116 THR B O   1 
ATOM   4544  C  CB  . THR B 2 116 ? 4.014   19.794  32.216  1.00 27.65  ? 116 THR B CB  1 
ATOM   4545  O  OG1 . THR B 2 116 ? 4.099   18.378  31.969  1.00 28.81  ? 116 THR B OG1 1 
ATOM   4546  C  CG2 . THR B 2 116 ? 2.564   20.222  32.098  1.00 28.65  ? 116 THR B CG2 1 
ATOM   4547  N  N   . VAL B 2 117 ? 7.169   19.799  30.586  1.00 28.09  ? 117 VAL B N   1 
ATOM   4548  C  CA  . VAL B 2 117 ? 8.616   19.746  30.824  1.00 25.29  ? 117 VAL B CA  1 
ATOM   4549  C  C   . VAL B 2 117 ? 9.194   21.150  30.662  1.00 26.51  ? 117 VAL B C   1 
ATOM   4550  O  O   . VAL B 2 117 ? 9.039   21.765  29.600  1.00 28.58  ? 117 VAL B O   1 
ATOM   4551  C  CB  . VAL B 2 117 ? 9.297   18.769  29.854  1.00 26.34  ? 117 VAL B CB  1 
ATOM   4552  C  CG1 . VAL B 2 117 ? 10.846  18.796  30.029  1.00 25.87  ? 117 VAL B CG1 1 
ATOM   4553  C  CG2 . VAL B 2 117 ? 8.732   17.334  30.034  1.00 26.24  ? 117 VAL B CG2 1 
ATOM   4554  N  N   . LYS B 2 118 ? 9.870   21.653  31.720  1.00 26.36  ? 118 LYS B N   1 
ATOM   4555  C  CA  . LYS B 2 118 ? 10.628  22.912  31.697  1.00 25.77  ? 118 LYS B CA  1 
ATOM   4556  C  C   . LYS B 2 118 ? 12.136  22.708  31.523  1.00 29.46  ? 118 LYS B C   1 
ATOM   4557  O  O   . LYS B 2 118 ? 12.815  23.596  30.984  1.00 27.19  ? 118 LYS B O   1 
ATOM   4558  C  CB  . LYS B 2 118 ? 10.352  23.714  32.984  1.00 24.96  ? 118 LYS B CB  1 
ATOM   4559  C  CG  . LYS B 2 118 ? 8.898   24.014  33.290  1.00 31.50  ? 118 LYS B CG  1 
ATOM   4560  C  CD  . LYS B 2 118 ? 8.113   24.461  32.042  1.00 39.69  ? 118 LYS B CD  1 
ATOM   4561  C  CE  . LYS B 2 118 ? 6.574   24.194  32.145  1.00 46.62  ? 118 LYS B CE  1 
ATOM   4562  N  NZ  . LYS B 2 118 ? 5.795   24.571  30.898  1.00 43.00  ? 118 LYS B NZ  1 
ATOM   4563  N  N   . TRP B 2 119 ? 12.677  21.541  31.861  1.00 23.13  ? 119 TRP B N   1 
ATOM   4564  C  CA  . TRP B 2 119 ? 14.080  21.330  31.543  1.00 23.86  ? 119 TRP B CA  1 
ATOM   4565  C  C   . TRP B 2 119 ? 14.332  19.845  31.441  1.00 26.80  ? 119 TRP B C   1 
ATOM   4566  O  O   . TRP B 2 119 ? 13.555  19.045  31.982  1.00 26.86  ? 119 TRP B O   1 
ATOM   4567  C  CB  . TRP B 2 119 ? 14.987  21.962  32.595  1.00 24.08  ? 119 TRP B CB  1 
ATOM   4568  C  CG  . TRP B 2 119 ? 14.781  21.432  34.010  1.00 24.76  ? 119 TRP B CG  1 
ATOM   4569  C  CD1 . TRP B 2 119 ? 13.953  21.948  34.985  1.00 29.02  ? 119 TRP B CD1 1 
ATOM   4570  C  CD2 . TRP B 2 119 ? 15.443  20.321  34.591  1.00 29.51  ? 119 TRP B CD2 1 
ATOM   4571  N  NE1 . TRP B 2 119 ? 14.093  21.201  36.158  1.00 31.29  ? 119 TRP B NE1 1 
ATOM   4572  C  CE2 . TRP B 2 119 ? 14.996  20.205  35.929  1.00 28.62  ? 119 TRP B CE2 1 
ATOM   4573  C  CE3 . TRP B 2 119 ? 16.390  19.421  34.120  1.00 24.48  ? 119 TRP B CE3 1 
ATOM   4574  C  CZ2 . TRP B 2 119 ? 15.456  19.206  36.783  1.00 28.41  ? 119 TRP B CZ2 1 
ATOM   4575  C  CZ3 . TRP B 2 119 ? 16.854  18.408  35.006  1.00 30.72  ? 119 TRP B CZ3 1 
ATOM   4576  C  CH2 . TRP B 2 119 ? 16.368  18.328  36.308  1.00 29.45  ? 119 TRP B CH2 1 
ATOM   4577  N  N   . ASP B 2 120 ? 15.414  19.489  30.751  1.00 24.68  ? 120 ASP B N   1 
ATOM   4578  C  CA  . ASP B 2 120 ? 15.776  18.083  30.633  1.00 21.55  ? 120 ASP B CA  1 
ATOM   4579  C  C   . ASP B 2 120 ? 17.284  17.950  30.698  1.00 24.18  ? 120 ASP B C   1 
ATOM   4580  O  O   . ASP B 2 120 ? 18.013  18.887  30.395  1.00 25.25  ? 120 ASP B O   1 
ATOM   4581  C  CB  . ASP B 2 120 ? 15.265  17.449  29.359  1.00 23.77  ? 120 ASP B CB  1 
ATOM   4582  C  CG  . ASP B 2 120 ? 15.940  18.005  28.108  1.00 27.20  ? 120 ASP B CG  1 
ATOM   4583  O  OD1 . ASP B 2 120 ? 17.038  17.523  27.743  1.00 28.38  ? 120 ASP B OD1 1 
ATOM   4584  O  OD2 . ASP B 2 120 ? 15.345  18.908  27.544  1.00 32.31  ? 120 ASP B OD2 1 
ATOM   4585  N  N   . TYR B 2 121 ? 17.759  16.773  31.082  1.00 22.63  ? 121 TYR B N   1 
ATOM   4586  C  CA  . TYR B 2 121 ? 19.208  16.519  31.084  1.00 19.87  ? 121 TYR B CA  1 
ATOM   4587  C  C   . TYR B 2 121 ? 19.504  15.036  30.884  1.00 23.70  ? 121 TYR B C   1 
ATOM   4588  O  O   . TYR B 2 121 ? 18.965  14.184  31.603  1.00 23.31  ? 121 TYR B O   1 
ATOM   4589  C  CB  . TYR B 2 121 ? 19.851  16.977  32.381  1.00 21.98  ? 121 TYR B CB  1 
ATOM   4590  C  CG  . TYR B 2 121 ? 21.362  17.105  32.307  1.00 22.92  ? 121 TYR B CG  1 
ATOM   4591  C  CD1 . TYR B 2 121 ? 22.183  16.010  32.558  1.00 22.89  ? 121 TYR B CD1 1 
ATOM   4592  C  CD2 . TYR B 2 121 ? 21.967  18.332  31.948  1.00 25.06  ? 121 TYR B CD2 1 
ATOM   4593  C  CE1 . TYR B 2 121 ? 23.607  16.096  32.470  1.00 22.08  ? 121 TYR B CE1 1 
ATOM   4594  C  CE2 . TYR B 2 121 ? 23.396  18.440  31.856  1.00 22.23  ? 121 TYR B CE2 1 
ATOM   4595  C  CZ  . TYR B 2 121 ? 24.189  17.332  32.139  1.00 21.91  ? 121 TYR B CZ  1 
ATOM   4596  O  OH  . TYR B 2 121 ? 25.559  17.434  32.075  1.00 22.41  ? 121 TYR B OH  1 
ATOM   4597  N  N   . TYR B 2 122 ? 20.375  14.747  29.919  1.00 21.04  ? 122 TYR B N   1 
ATOM   4598  C  CA  . TYR B 2 122 ? 20.830  13.385  29.647  1.00 20.29  ? 122 TYR B CA  1 
ATOM   4599  C  C   . TYR B 2 122 ? 22.252  13.258  30.184  1.00 22.33  ? 122 TYR B C   1 
ATOM   4600  O  O   . TYR B 2 122 ? 23.148  13.964  29.733  1.00 22.18  ? 122 TYR B O   1 
ATOM   4601  C  CB  . TYR B 2 122 ? 20.791  13.145  28.155  1.00 20.30  ? 122 TYR B CB  1 
ATOM   4602  C  CG  . TYR B 2 122 ? 21.287  11.813  27.679  1.00 19.73  ? 122 TYR B CG  1 
ATOM   4603  C  CD1 . TYR B 2 122 ? 22.668  11.547  27.499  1.00 19.47  ? 122 TYR B CD1 1 
ATOM   4604  C  CD2 . TYR B 2 122 ? 20.391  10.826  27.372  1.00 28.52  ? 122 TYR B CD2 1 
ATOM   4605  C  CE1 . TYR B 2 122 ? 23.118  10.294  26.974  1.00 19.77  ? 122 TYR B CE1 1 
ATOM   4606  C  CE2 . TYR B 2 122 ? 20.813  9.584   26.905  1.00 27.58  ? 122 TYR B CE2 1 
ATOM   4607  C  CZ  . TYR B 2 122 ? 22.170  9.316   26.736  1.00 24.96  ? 122 TYR B CZ  1 
ATOM   4608  O  OH  . TYR B 2 122 ? 22.593  8.088   26.223  1.00 25.74  ? 122 TYR B OH  1 
ATOM   4609  N  N   . VAL B 2 123 ? 22.484  12.298  31.063  1.00 20.90  ? 123 VAL B N   1 
ATOM   4610  C  CA  . VAL B 2 123 ? 23.803  12.083  31.652  1.00 21.36  ? 123 VAL B CA  1 
ATOM   4611  C  C   . VAL B 2 123 ? 24.437  10.900  30.917  1.00 21.27  ? 123 VAL B C   1 
ATOM   4612  O  O   . VAL B 2 123 ? 24.020  9.748   31.161  1.00 21.38  ? 123 VAL B O   1 
ATOM   4613  C  CB  . VAL B 2 123 ? 23.705  11.733  33.146  1.00 21.26  ? 123 VAL B CB  1 
ATOM   4614  C  CG1 . VAL B 2 123 ? 25.122  11.587  33.781  1.00 22.62  ? 123 VAL B CG1 1 
ATOM   4615  C  CG2 . VAL B 2 123 ? 22.857  12.697  33.904  1.00 24.77  ? 123 VAL B CG2 1 
ATOM   4616  N  N   . PRO B 2 124 ? 25.531  11.104  30.145  1.00 22.53  ? 124 PRO B N   1 
ATOM   4617  C  CA  . PRO B 2 124 ? 26.171  9.954   29.454  1.00 21.39  ? 124 PRO B CA  1 
ATOM   4618  C  C   . PRO B 2 124 ? 27.157  9.261   30.381  1.00 20.65  ? 124 PRO B C   1 
ATOM   4619  O  O   . PRO B 2 124 ? 28.403  9.283   30.227  1.00 23.74  ? 124 PRO B O   1 
ATOM   4620  C  CB  . PRO B 2 124 ? 26.813  10.604  28.201  1.00 25.39  ? 124 PRO B CB  1 
ATOM   4621  C  CG  . PRO B 2 124 ? 26.949  12.041  28.513  1.00 28.42  ? 124 PRO B CG  1 
ATOM   4622  C  CD  . PRO B 2 124 ? 26.070  12.400  29.713  1.00 21.95  ? 124 PRO B CD  1 
ATOM   4623  N  N   . MET B 2 125 ? 26.583  8.597   31.393  1.00 22.45  ? 125 MET B N   1 
ATOM   4624  C  CA  . MET B 2 125 ? 27.371  7.742   32.259  1.00 20.56  ? 125 MET B CA  1 
ATOM   4625  C  C   . MET B 2 125 ? 28.051  6.707   31.372  1.00 21.20  ? 125 MET B C   1 
ATOM   4626  O  O   . MET B 2 125 ? 27.347  6.008   30.621  1.00 22.62  ? 125 MET B O   1 
ATOM   4627  C  CB  . MET B 2 125 ? 26.482  6.913   33.179  1.00 22.87  ? 125 MET B CB  1 
ATOM   4628  C  CG  . MET B 2 125 ? 27.269  6.111   34.115  1.00 24.36  ? 125 MET B CG  1 
ATOM   4629  S  SD  . MET B 2 125 ? 26.301  5.259   35.348  1.00 22.30  ? 125 MET B SD  1 
ATOM   4630  C  CE  . MET B 2 125 ? 27.561  4.053   35.943  1.00 23.00  ? 125 MET B CE  1 
ATOM   4631  N  N   . PRO B 2 126 ? 29.346  6.475   31.532  1.00 19.55  ? 126 PRO B N   1 
ATOM   4632  C  CA  . PRO B 2 126 ? 30.011  5.366   30.851  1.00 19.16  ? 126 PRO B CA  1 
ATOM   4633  C  C   . PRO B 2 126 ? 29.255  4.054   31.007  1.00 18.69  ? 126 PRO B C   1 
ATOM   4634  O  O   . PRO B 2 126 ? 28.710  3.736   32.080  1.00 20.61  ? 126 PRO B O   1 
ATOM   4635  C  CB  . PRO B 2 126 ? 31.388  5.290   31.540  1.00 22.29  ? 126 PRO B CB  1 
ATOM   4636  C  CG  . PRO B 2 126 ? 31.631  6.698   32.054  1.00 23.60  ? 126 PRO B CG  1 
ATOM   4637  C  CD  . PRO B 2 126 ? 30.269  7.301   32.327  1.00 24.49  ? 126 PRO B CD  1 
ATOM   4638  N  N   . ASN B 2 127 ? 29.202  3.304   29.898  1.00 19.85  ? 127 ASN B N   1 
ATOM   4639  C  CA  . ASN B 2 127 ? 28.713  1.925   30.012  1.00 19.35  ? 127 ASN B CA  1 
ATOM   4640  C  C   . ASN B 2 127 ? 29.826  0.988   30.509  1.00 17.60  ? 127 ASN B C   1 
ATOM   4641  O  O   . ASN B 2 127 ? 29.547  0.073   31.273  1.00 20.21  ? 127 ASN B O   1 
ATOM   4642  C  CB  . ASN B 2 127 ? 28.219  1.378   28.670  1.00 18.44  ? 127 ASN B CB  1 
ATOM   4643  C  CG  . ASN B 2 127 ? 26.764  1.802   28.339  1.00 21.37  ? 127 ASN B CG  1 
ATOM   4644  O  OD1 . ASN B 2 127 ? 25.994  2.240   29.207  1.00 22.31  ? 127 ASN B OD1 1 
ATOM   4645  N  ND2 . ASN B 2 127 ? 26.438  1.754   27.047  1.00 24.24  ? 127 ASN B ND2 1 
ATOM   4646  N  N   . GLU B 2 128 ? 31.074  1.198   30.117  1.00 19.62  ? 128 GLU B N   1 
ATOM   4647  C  CA  . GLU B 2 128 ? 32.127  0.237   30.479  1.00 21.16  ? 128 GLU B CA  1 
ATOM   4648  C  C   . GLU B 2 128 ? 32.724  0.593   31.851  1.00 20.51  ? 128 GLU B C   1 
ATOM   4649  O  O   . GLU B 2 128 ? 33.875  1.039   31.993  1.00 21.68  ? 128 GLU B O   1 
ATOM   4650  C  CB  . GLU B 2 128 ? 33.200  0.172   29.400  1.00 21.30  ? 128 GLU B CB  1 
ATOM   4651  C  CG  . GLU B 2 128 ? 34.110  -1.032  29.611  1.00 23.26  ? 128 GLU B CG  1 
ATOM   4652  C  CD  . GLU B 2 128 ? 35.010  -1.319  28.440  1.00 24.38  ? 128 GLU B CD  1 
ATOM   4653  O  OE1 . GLU B 2 128 ? 34.893  -0.629  27.376  1.00 22.80  ? 128 GLU B OE1 1 
ATOM   4654  O  OE2 . GLU B 2 128 ? 35.884  -2.208  28.619  1.00 25.43  ? 128 GLU B OE2 1 
ATOM   4655  N  N   . VAL B 2 129 ? 31.894  0.406   32.889  1.00 18.48  ? 129 VAL B N   1 
ATOM   4656  C  CA  . VAL B 2 129 ? 32.347  0.593   34.278  1.00 19.98  ? 129 VAL B CA  1 
ATOM   4657  C  C   . VAL B 2 129 ? 33.532  -0.290  34.613  1.00 23.77  ? 129 VAL B C   1 
ATOM   4658  O  O   . VAL B 2 129 ? 34.302  0.030   35.513  1.00 21.75  ? 129 VAL B O   1 
ATOM   4659  C  CB  . VAL B 2 129 ? 31.188  0.401   35.262  1.00 22.25  ? 129 VAL B CB  1 
ATOM   4660  C  CG1 . VAL B 2 129 ? 30.098  1.514   34.965  1.00 22.22  ? 129 VAL B CG1 1 
ATOM   4661  C  CG2 . VAL B 2 129 ? 30.655  -1.082  35.318  1.00 23.41  ? 129 VAL B CG2 1 
ATOM   4662  N  N   . GLN B 2 130 ? 33.776  -1.356  33.828  1.00 19.82  ? 130 GLN B N   1 
ATOM   4663  C  CA  . GLN B 2 130 ? 34.984  -2.130  34.075  1.00 19.66  ? 130 GLN B CA  1 
ATOM   4664  C  C   . GLN B 2 130 ? 36.250  -1.468  33.582  1.00 22.14  ? 130 GLN B C   1 
ATOM   4665  O  O   . GLN B 2 130 ? 37.344  -1.938  33.947  1.00 23.56  ? 130 GLN B O   1 
ATOM   4666  C  CB  . GLN B 2 130 ? 34.859  -3.533  33.420  1.00 20.61  ? 130 GLN B CB  1 
ATOM   4667  C  CG  . GLN B 2 130 ? 33.885  -4.405  34.220  1.00 21.81  ? 130 GLN B CG  1 
ATOM   4668  C  CD  . GLN B 2 130 ? 33.536  -5.684  33.444  1.00 22.47  ? 130 GLN B CD  1 
ATOM   4669  O  OE1 . GLN B 2 130 ? 34.392  -6.297  32.806  1.00 20.83  ? 130 GLN B OE1 1 
ATOM   4670  N  NE2 . GLN B 2 130 ? 32.252  -6.070  33.464  1.00 24.03  ? 130 GLN B NE2 1 
ATOM   4671  N  N   . SER B 2 131 ? 36.154  -0.373  32.801  1.00 20.83  ? 131 SER B N   1 
ATOM   4672  C  CA  . SER B 2 131 ? 37.349  0.281   32.279  1.00 20.82  ? 131 SER B CA  1 
ATOM   4673  C  C   . SER B 2 131 ? 38.034  1.081   33.385  1.00 22.45  ? 131 SER B C   1 
ATOM   4674  O  O   . SER B 2 131 ? 37.358  1.770   34.145  1.00 21.46  ? 131 SER B O   1 
ATOM   4675  C  CB  . SER B 2 131 ? 36.995  1.288   31.179  1.00 22.46  ? 131 SER B CB  1 
ATOM   4676  O  OG  . SER B 2 131 ? 38.085  2.167   30.908  1.00 23.54  ? 131 SER B OG  1 
ATOM   4677  N  N   . PRO B 2 132 ? 39.376  1.081   33.419  1.00 24.07  ? 132 PRO B N   1 
ATOM   4678  C  CA  . PRO B 2 132 ? 40.100  1.942   34.355  1.00 21.58  ? 132 PRO B CA  1 
ATOM   4679  C  C   . PRO B 2 132 ? 39.883  3.432   34.137  1.00 25.12  ? 132 PRO B C   1 
ATOM   4680  O  O   . PRO B 2 132 ? 40.271  4.216   35.016  1.00 25.38  ? 132 PRO B O   1 
ATOM   4681  C  CB  . PRO B 2 132 ? 41.563  1.558   34.139  1.00 26.05  ? 132 PRO B CB  1 
ATOM   4682  C  CG  . PRO B 2 132 ? 41.612  0.672   32.910  1.00 31.34  ? 132 PRO B CG  1 
ATOM   4683  C  CD  . PRO B 2 132 ? 40.239  0.119   32.709  1.00 24.27  ? 132 PRO B CD  1 
ATOM   4684  N  N   . HIS B 2 133 ? 39.283  3.836   33.018  1.00 23.92  ? 133 HIS B N   1 
ATOM   4685  C  CA  . HIS B 2 133 ? 39.027  5.269   32.752  1.00 20.91  ? 133 HIS B CA  1 
ATOM   4686  C  C   . HIS B 2 133 ? 37.595  5.705   33.021  1.00 23.40  ? 133 HIS B C   1 
ATOM   4687  O  O   . HIS B 2 133 ? 37.290  6.929   32.903  1.00 22.12  ? 133 HIS B O   1 
ATOM   4688  C  CB  . HIS B 2 133 ? 39.417  5.518   31.297  1.00 19.96  ? 133 HIS B CB  1 
ATOM   4689  C  CG  . HIS B 2 133 ? 40.827  5.080   31.015  1.00 23.70  ? 133 HIS B CG  1 
ATOM   4690  N  ND1 . HIS B 2 133 ? 41.921  5.655   31.638  1.00 24.66  ? 133 HIS B ND1 1 
ATOM   4691  C  CD2 . HIS B 2 133 ? 41.310  4.067   30.266  1.00 25.26  ? 133 HIS B CD2 1 
ATOM   4692  C  CE1 . HIS B 2 133 ? 43.026  5.051   31.228  1.00 25.16  ? 133 HIS B CE1 1 
ATOM   4693  N  NE2 . HIS B 2 133 ? 42.678  4.040   30.443  1.00 25.03  ? 133 HIS B NE2 1 
ATOM   4694  N  N   . ALA B 2 134 ? 36.699  4.757   33.396  1.00 20.90  ? 134 ALA B N   1 
ATOM   4695  C  CA  . ALA B 2 134 ? 35.293  5.103   33.486  1.00 19.91  ? 134 ALA B CA  1 
ATOM   4696  C  C   . ALA B 2 134 ? 35.027  5.977   34.698  1.00 19.15  ? 134 ALA B C   1 
ATOM   4697  O  O   . ALA B 2 134 ? 34.187  6.867   34.606  1.00 22.29  ? 134 ALA B O   1 
ATOM   4698  C  CB  . ALA B 2 134 ? 34.408  3.858   33.538  1.00 20.19  ? 134 ALA B CB  1 
ATOM   4699  N  N   . ARG B 2 135 ? 35.722  5.756   35.819  1.00 19.17  ? 135 ARG B N   1 
ATOM   4700  C  CA  . ARG B 2 135 ? 35.393  6.547   37.034  1.00 19.07  ? 135 ARG B CA  1 
ATOM   4701  C  C   . ARG B 2 135 ? 35.836  8.019   36.902  1.00 20.69  ? 135 ARG B C   1 
ATOM   4702  O  O   . ARG B 2 135 ? 35.137  8.918   37.423  1.00 22.27  ? 135 ARG B O   1 
ATOM   4703  C  CB  . ARG B 2 135 ? 35.950  5.903   38.292  1.00 21.66  ? 135 ARG B CB  1 
ATOM   4704  C  CG  . ARG B 2 135 ? 35.154  4.642   38.599  1.00 21.75  ? 135 ARG B CG  1 
ATOM   4705  C  CD  . ARG B 2 135 ? 35.943  3.665   39.427  1.00 24.20  ? 135 ARG B CD  1 
ATOM   4706  N  NE  . ARG B 2 135 ? 35.113  2.474   39.621  1.00 24.26  ? 135 ARG B NE  1 
ATOM   4707  C  CZ  . ARG B 2 135 ? 34.817  1.592   38.674  1.00 23.84  ? 135 ARG B CZ  1 
ATOM   4708  N  NH1 . ARG B 2 135 ? 35.283  1.720   37.436  1.00 21.93  ? 135 ARG B NH1 1 
ATOM   4709  N  NH2 . ARG B 2 135 ? 33.991  0.586   38.964  1.00 25.57  ? 135 ARG B NH2 1 
ATOM   4710  N  N   . LYS B 2 136 ? 36.943  8.285   36.211  1.00 21.26  ? 136 LYS B N   1 
ATOM   4711  C  CA  . LYS B 2 136 ? 37.304  9.680   35.903  1.00 21.05  ? 136 LYS B CA  1 
ATOM   4712  C  C   . LYS B 2 136 ? 36.285  10.326  34.964  1.00 25.29  ? 136 LYS B C   1 
ATOM   4713  O  O   . LYS B 2 136 ? 35.851  11.480  35.192  1.00 22.28  ? 136 LYS B O   1 
ATOM   4714  C  CB  . LYS B 2 136 ? 38.721  9.723   35.304  1.00 21.25  ? 136 LYS B CB  1 
ATOM   4715  C  CG  . LYS B 2 136 ? 39.250  11.178  34.928  1.00 25.19  ? 136 LYS B CG  1 
ATOM   4716  C  CD  . LYS B 2 136 ? 38.996  12.173  36.048  1.00 28.80  ? 136 LYS B CD  1 
ATOM   4717  C  CE  . LYS B 2 136 ? 39.169  13.581  35.536  1.00 36.43  ? 136 LYS B CE  1 
ATOM   4718  N  NZ  . LYS B 2 136 ? 39.639  14.501  36.646  1.00 39.51  ? 136 LYS B NZ  1 
ATOM   4719  N  N   . ALA B 2 137 ? 35.881  9.602   33.906  1.00 23.40  ? 137 ALA B N   1 
ATOM   4720  C  CA  . ALA B 2 137 ? 34.886  10.134  32.982  1.00 19.25  ? 137 ALA B CA  1 
ATOM   4721  C  C   . ALA B 2 137 ? 33.576  10.414  33.709  1.00 23.68  ? 137 ALA B C   1 
ATOM   4722  O  O   . ALA B 2 137 ? 32.997  11.485  33.550  1.00 22.61  ? 137 ALA B O   1 
ATOM   4723  C  CB  . ALA B 2 137 ? 34.661  9.175   31.799  1.00 23.33  ? 137 ALA B CB  1 
ATOM   4724  N  N   . HIS B 2 138 ? 33.148  9.518   34.620  1.00 20.15  ? 138 HIS B N   1 
ATOM   4725  C  CA  . HIS B 2 138 ? 31.869  9.752   35.289  1.00 19.69  ? 138 HIS B CA  1 
ATOM   4726  C  C   . HIS B 2 138 ? 31.964  10.831  36.363  1.00 21.15  ? 138 HIS B C   1 
ATOM   4727  O  O   . HIS B 2 138 ? 31.018  11.612  36.547  1.00 20.86  ? 138 HIS B O   1 
ATOM   4728  C  CB  . HIS B 2 138 ? 31.283  8.494   35.956  1.00 18.95  ? 138 HIS B CB  1 
ATOM   4729  C  CG  . HIS B 2 138 ? 29.802  8.634   36.182  1.00 18.57  ? 138 HIS B CG  1 
ATOM   4730  N  ND1 . HIS B 2 138 ? 28.988  9.288   35.285  1.00 20.88  ? 138 HIS B ND1 1 
ATOM   4731  C  CD2 . HIS B 2 138 ? 28.997  8.202   37.167  1.00 19.23  ? 138 HIS B CD2 1 
ATOM   4732  C  CE1 . HIS B 2 138 ? 27.734  9.211   35.682  1.00 19.82  ? 138 HIS B CE1 1 
ATOM   4733  N  NE2 . HIS B 2 138 ? 27.711  8.542   36.819  1.00 19.97  ? 138 HIS B NE2 1 
ATOM   4734  N  N   . TYR B 2 139 ? 33.121  10.964  36.997  1.00 19.78  ? 139 TYR B N   1 
ATOM   4735  C  CA  . TYR B 2 139 ? 33.361  12.130  37.858  1.00 20.73  ? 139 TYR B CA  1 
ATOM   4736  C  C   . TYR B 2 139 ? 33.012  13.419  37.107  1.00 21.77  ? 139 TYR B C   1 
ATOM   4737  O  O   . TYR B 2 139 ? 32.289  14.285  37.623  1.00 22.22  ? 139 TYR B O   1 
ATOM   4738  C  CB  . TYR B 2 139 ? 34.831  12.118  38.282  1.00 20.22  ? 139 TYR B CB  1 
ATOM   4739  C  CG  . TYR B 2 139 ? 35.266  13.218  39.192  1.00 22.05  ? 139 TYR B CG  1 
ATOM   4740  C  CD1 . TYR B 2 139 ? 35.543  14.505  38.675  1.00 26.48  ? 139 TYR B CD1 1 
ATOM   4741  C  CD2 . TYR B 2 139 ? 35.411  13.000  40.584  1.00 23.26  ? 139 TYR B CD2 1 
ATOM   4742  C  CE1 . TYR B 2 139 ? 35.945  15.525  39.531  1.00 28.52  ? 139 TYR B CE1 1 
ATOM   4743  C  CE2 . TYR B 2 139 ? 35.787  14.025  41.440  1.00 25.97  ? 139 TYR B CE2 1 
ATOM   4744  C  CZ  . TYR B 2 139 ? 36.058  15.271  40.900  1.00 28.06  ? 139 TYR B CZ  1 
ATOM   4745  O  OH  . TYR B 2 139 ? 36.458  16.252  41.787  1.00 28.97  ? 139 TYR B OH  1 
ATOM   4746  N  N   . GLU B 2 140 ? 33.556  13.575  35.894  1.00 20.52  ? 140 GLU B N   1 
ATOM   4747  C  CA  . GLU B 2 140 ? 33.332  14.826  35.158  1.00 18.60  ? 140 GLU B CA  1 
ATOM   4748  C  C   . GLU B 2 140 ? 31.875  14.959  34.709  1.00 22.46  ? 140 GLU B C   1 
ATOM   4749  O  O   . GLU B 2 140 ? 31.324  16.074  34.734  1.00 24.31  ? 140 GLU B O   1 
ATOM   4750  C  CB  . GLU B 2 140 ? 34.310  14.907  33.991  1.00 19.83  ? 140 GLU B CB  1 
ATOM   4751  C  CG  . GLU B 2 140 ? 35.775  14.926  34.400  1.00 20.81  ? 140 GLU B CG  1 
ATOM   4752  C  CD  . GLU B 2 140 ? 36.208  16.177  35.231  1.00 29.91  ? 140 GLU B CD  1 
ATOM   4753  O  OE1 . GLU B 2 140 ? 35.401  17.120  35.391  1.00 29.74  ? 140 GLU B OE1 1 
ATOM   4754  O  OE2 . GLU B 2 140 ? 37.377  16.214  35.704  1.00 30.62  ? 140 GLU B OE2 1 
ATOM   4755  N  N   . GLU B 2 141 ? 31.196  13.851  34.377  1.00 19.36  ? 141 GLU B N   1 
ATOM   4756  C  CA  . GLU B 2 141 ? 29.761  13.924  34.045  1.00 20.95  ? 141 GLU B CA  1 
ATOM   4757  C  C   . GLU B 2 141 ? 28.953  14.392  35.247  1.00 21.06  ? 141 GLU B C   1 
ATOM   4758  O  O   . GLU B 2 141 ? 28.079  15.280  35.128  1.00 22.74  ? 141 GLU B O   1 
ATOM   4759  C  CB  . GLU B 2 141 ? 29.245  12.552  33.547  1.00 19.35  ? 141 GLU B CB  1 
ATOM   4760  C  CG  . GLU B 2 141 ? 29.871  12.123  32.264  1.00 19.98  ? 141 GLU B CG  1 
ATOM   4761  C  CD  . GLU B 2 141 ? 29.585  13.026  31.065  1.00 26.82  ? 141 GLU B CD  1 
ATOM   4762  O  OE1 . GLU B 2 141 ? 28.805  14.019  31.156  1.00 26.97  ? 141 GLU B OE1 1 
ATOM   4763  O  OE2 . GLU B 2 141 ? 30.148  12.714  29.998  1.00 25.06  ? 141 GLU B OE2 1 
ATOM   4764  N  N   . VAL B 2 142 ? 29.243  13.828  36.421  1.00 20.81  ? 142 VAL B N   1 
ATOM   4765  C  CA  . VAL B 2 142 ? 28.493  14.196  37.612  1.00 19.79  ? 142 VAL B CA  1 
ATOM   4766  C  C   . VAL B 2 142 ? 28.766  15.658  37.958  1.00 22.41  ? 142 VAL B C   1 
ATOM   4767  O  O   . VAL B 2 142 ? 27.834  16.416  38.263  1.00 23.66  ? 142 VAL B O   1 
ATOM   4768  C  CB  . VAL B 2 142 ? 28.831  13.237  38.760  1.00 22.57  ? 142 VAL B CB  1 
ATOM   4769  C  CG1 . VAL B 2 142 ? 28.223  13.695  40.048  1.00 23.13  ? 142 VAL B CG1 1 
ATOM   4770  C  CG2 . VAL B 2 142 ? 28.301  11.809  38.440  1.00 19.44  ? 142 VAL B CG2 1 
ATOM   4771  N  N   . GLN B 2 143 ? 30.041  16.095  37.895  1.00 19.69  ? 143 GLN B N   1 
ATOM   4772  C  CA  . GLN B 2 143 ? 30.323  17.507  38.142  1.00 21.29  ? 143 GLN B CA  1 
ATOM   4773  C  C   . GLN B 2 143 ? 29.632  18.395  37.119  1.00 25.70  ? 143 GLN B C   1 
ATOM   4774  O  O   . GLN B 2 143 ? 29.157  19.495  37.458  1.00 23.55  ? 143 GLN B O   1 
ATOM   4775  C  CB  . GLN B 2 143 ? 31.823  17.768  38.137  1.00 22.43  ? 143 GLN B CB  1 
ATOM   4776  C  CG  . GLN B 2 143 ? 32.183  19.282  38.175  1.00 23.34  ? 143 GLN B CG  1 
ATOM   4777  C  CD  . GLN B 2 143 ? 31.834  19.988  39.485  1.00 24.73  ? 143 GLN B CD  1 
ATOM   4778  O  OE1 . GLN B 2 143 ? 31.507  19.355  40.470  1.00 26.16  ? 143 GLN B OE1 1 
ATOM   4779  N  NE2 . GLN B 2 143 ? 31.894  21.328  39.489  1.00 24.37  ? 143 GLN B NE2 1 
ATOM   4780  N  N   . ALA B 2 144 ? 29.582  17.967  35.842  1.00 21.84  ? 144 ALA B N   1 
ATOM   4781  C  CA  . ALA B 2 144 ? 28.919  18.793  34.835  1.00 22.54  ? 144 ALA B CA  1 
ATOM   4782  C  C   . ALA B 2 144 ? 27.413  18.862  35.100  1.00 22.03  ? 144 ALA B C   1 
ATOM   4783  O  O   . ALA B 2 144 ? 26.796  19.917  34.911  1.00 21.86  ? 144 ALA B O   1 
ATOM   4784  C  CB  . ALA B 2 144 ? 29.197  18.265  33.411  1.00 23.46  ? 144 ALA B CB  1 
ATOM   4785  N  N   . PHE B 2 145 ? 26.806  17.779  35.589  1.00 20.09  ? 145 PHE B N   1 
ATOM   4786  C  CA  . PHE B 2 145 ? 25.380  17.847  35.922  1.00 20.56  ? 145 PHE B CA  1 
ATOM   4787  C  C   . PHE B 2 145 ? 25.162  18.778  37.115  1.00 23.05  ? 145 PHE B C   1 
ATOM   4788  O  O   . PHE B 2 145 ? 24.192  19.537  37.156  1.00 23.96  ? 145 PHE B O   1 
ATOM   4789  C  CB  . PHE B 2 145 ? 24.859  16.443  36.218  1.00 19.78  ? 145 PHE B CB  1 
ATOM   4790  C  CG  . PHE B 2 145 ? 23.341  16.276  36.199  1.00 23.04  ? 145 PHE B CG  1 
ATOM   4791  C  CD1 . PHE B 2 145 ? 22.463  17.222  35.676  1.00 24.68  ? 145 PHE B CD1 1 
ATOM   4792  C  CD2 . PHE B 2 145 ? 22.810  15.112  36.778  1.00 21.16  ? 145 PHE B CD2 1 
ATOM   4793  C  CE1 . PHE B 2 145 ? 21.081  17.014  35.720  1.00 24.84  ? 145 PHE B CE1 1 
ATOM   4794  C  CE2 . PHE B 2 145 ? 21.446  14.900  36.773  1.00 26.56  ? 145 PHE B CE2 1 
ATOM   4795  C  CZ  . PHE B 2 145 ? 20.586  15.824  36.254  1.00 24.62  ? 145 PHE B CZ  1 
ATOM   4796  N  N   . ARG B 2 146 ? 26.087  18.745  38.073  1.00 22.50  ? 146 ARG B N   1 
ATOM   4797  C  CA  . ARG B 2 146 ? 26.011  19.655  39.223  1.00 21.83  ? 146 ARG B CA  1 
ATOM   4798  C  C   . ARG B 2 146 ? 26.037  21.103  38.742  1.00 25.52  ? 146 ARG B C   1 
ATOM   4799  O  O   . ARG B 2 146 ? 25.260  21.933  39.221  1.00 25.07  ? 146 ARG B O   1 
ATOM   4800  C  CB  . ARG B 2 146 ? 27.180  19.356  40.152  1.00 24.59  ? 146 ARG B CB  1 
ATOM   4801  C  CG  . ARG B 2 146 ? 27.184  20.275  41.407  1.00 26.56  ? 146 ARG B CG  1 
ATOM   4802  C  CD  . ARG B 2 146 ? 28.558  20.789  41.572  1.00 32.67  ? 146 ARG B CD  1 
ATOM   4803  N  NE  . ARG B 2 146 ? 28.798  21.300  42.903  1.00 30.93  ? 146 ARG B NE  1 
ATOM   4804  C  CZ  . ARG B 2 146 ? 29.889  21.015  43.587  1.00 31.20  ? 146 ARG B CZ  1 
ATOM   4805  N  NH1 . ARG B 2 146 ? 30.815  20.200  43.087  1.00 30.63  ? 146 ARG B NH1 1 
ATOM   4806  N  NH2 . ARG B 2 146 ? 30.032  21.513  44.814  1.00 32.06  ? 146 ARG B NH2 1 
ATOM   4807  N  N   . VAL B 2 147 ? 26.921  21.417  37.787  1.00 24.71  ? 147 VAL B N   1 
ATOM   4808  C  CA  . VAL B 2 147 ? 27.015  22.795  37.271  1.00 22.01  ? 147 VAL B CA  1 
ATOM   4809  C  C   . VAL B 2 147 ? 25.731  23.177  36.548  1.00 25.07  ? 147 VAL B C   1 
ATOM   4810  O  O   . VAL B 2 147 ? 25.213  24.288  36.715  1.00 24.53  ? 147 VAL B O   1 
ATOM   4811  C  CB  . VAL B 2 147 ? 28.259  22.941  36.379  1.00 26.52  ? 147 VAL B CB  1 
ATOM   4812  C  CG1 . VAL B 2 147 ? 28.223  24.218  35.555  1.00 29.47  ? 147 VAL B CG1 1 
ATOM   4813  C  CG2 . VAL B 2 147 ? 29.533  22.886  37.269  1.00 25.14  ? 147 VAL B CG2 1 
ATOM   4814  N  N   . PHE B 2 148 ? 25.188  22.245  35.748  1.00 22.50  ? 148 PHE B N   1 
ATOM   4815  C  CA  . PHE B 2 148 ? 23.907  22.475  35.101  1.00 23.05  ? 148 PHE B CA  1 
ATOM   4816  C  C   . PHE B 2 148 ? 22.815  22.813  36.111  1.00 22.51  ? 148 PHE B C   1 
ATOM   4817  O  O   . PHE B 2 148 ? 22.057  23.774  35.918  1.00 24.26  ? 148 PHE B O   1 
ATOM   4818  C  CB  . PHE B 2 148 ? 23.519  21.246  34.288  1.00 20.58  ? 148 PHE B CB  1 
ATOM   4819  C  CG  . PHE B 2 148 ? 22.101  21.302  33.752  1.00 20.87  ? 148 PHE B CG  1 
ATOM   4820  C  CD1 . PHE B 2 148 ? 21.044  20.810  34.486  1.00 22.82  ? 148 PHE B CD1 1 
ATOM   4821  C  CD2 . PHE B 2 148 ? 21.873  21.752  32.460  1.00 19.22  ? 148 PHE B CD2 1 
ATOM   4822  C  CE1 . PHE B 2 148 ? 19.712  20.844  34.007  1.00 22.98  ? 148 PHE B CE1 1 
ATOM   4823  C  CE2 . PHE B 2 148 ? 20.546  21.784  31.965  1.00 24.71  ? 148 PHE B CE2 1 
ATOM   4824  C  CZ  . PHE B 2 148 ? 19.483  21.304  32.742  1.00 25.85  ? 148 PHE B CZ  1 
ATOM   4825  N  N   . LEU B 2 149 ? 22.728  22.047  37.201  1.00 22.39  ? 149 LEU B N   1 
ATOM   4826  C  CA  . LEU B 2 149 ? 21.667  22.225  38.178  1.00 22.62  ? 149 LEU B CA  1 
ATOM   4827  C  C   . LEU B 2 149 ? 21.831  23.539  38.943  1.00 23.90  ? 149 LEU B C   1 
ATOM   4828  O  O   . LEU B 2 149 ? 20.846  24.236  39.209  1.00 26.26  ? 149 LEU B O   1 
ATOM   4829  C  CB  . LEU B 2 149 ? 21.659  21.034  39.133  1.00 26.32  ? 149 LEU B CB  1 
ATOM   4830  C  CG  . LEU B 2 149 ? 21.127  19.752  38.464  1.00 23.61  ? 149 LEU B CG  1 
ATOM   4831  C  CD1 . LEU B 2 149 ? 21.481  18.618  39.391  1.00 26.74  ? 149 LEU B CD1 1 
ATOM   4832  C  CD2 . LEU B 2 149 ? 19.606  19.790  38.303  1.00 22.42  ? 149 LEU B CD2 1 
ATOM   4833  N  N   . GLN B 2 150 ? 23.080  23.915  39.264  1.00 23.90  ? 150 GLN B N   1 
ATOM   4834  C  CA  . GLN B 2 150 ? 23.345  25.187  39.952  1.00 25.63  ? 150 GLN B CA  1 
ATOM   4835  C  C   . GLN B 2 150 ? 22.942  26.345  39.075  1.00 26.04  ? 150 GLN B C   1 
ATOM   4836  O  O   . GLN B 2 150 ? 22.499  27.399  39.564  1.00 28.12  ? 150 GLN B O   1 
ATOM   4837  C  CB  . GLN B 2 150 ? 24.857  25.335  40.192  1.00 28.33  ? 150 GLN B CB  1 
ATOM   4838  C  CG  . GLN B 2 150 ? 25.496  24.445  41.077  1.00 35.78  ? 150 GLN B CG  1 
ATOM   4839  C  CD  . GLN B 2 150 ? 26.896  24.883  41.381  1.00 33.89  ? 150 GLN B CD  1 
ATOM   4840  O  OE1 . GLN B 2 150 ? 27.326  24.846  42.507  1.00 36.78  ? 150 GLN B OE1 1 
ATOM   4841  N  NE2 . GLN B 2 150 ? 27.626  25.349  40.327  1.00 31.62  ? 150 GLN B NE2 1 
ATOM   4842  N  N   . THR B 2 151 ? 23.184  26.204  37.763  1.00 23.86  ? 151 THR B N   1 
ATOM   4843  C  CA  . THR B 2 151 ? 22.859  27.257  36.820  1.00 26.85  ? 151 THR B CA  1 
ATOM   4844  C  C   . THR B 2 151 ? 21.350  27.351  36.669  1.00 25.82  ? 151 THR B C   1 
ATOM   4845  O  O   . THR B 2 151 ? 20.772  28.441  36.770  1.00 29.58  ? 151 THR B O   1 
ATOM   4846  C  CB  . THR B 2 151 ? 23.535  26.978  35.475  1.00 27.94  ? 151 THR B CB  1 
ATOM   4847  O  OG1 . THR B 2 151 ? 24.971  26.886  35.653  1.00 28.15  ? 151 THR B OG1 1 
ATOM   4848  C  CG2 . THR B 2 151 ? 23.200  28.081  34.526  1.00 28.12  ? 151 THR B CG2 1 
ATOM   4849  N  N   . LEU B 2 152 ? 20.706  26.181  36.593  1.00 25.25  ? 152 LEU B N   1 
ATOM   4850  C  CA  . LEU B 2 152 ? 19.262  26.100  36.434  1.00 25.83  ? 152 LEU B CA  1 
ATOM   4851  C  C   . LEU B 2 152 ? 18.523  26.755  37.588  1.00 29.09  ? 152 LEU B C   1 
ATOM   4852  O  O   . LEU B 2 152 ? 17.611  27.572  37.378  1.00 30.78  ? 152 LEU B O   1 
ATOM   4853  C  CB  . LEU B 2 152 ? 18.857  24.619  36.331  1.00 24.92  ? 152 LEU B CB  1 
ATOM   4854  C  CG  . LEU B 2 152 ? 17.372  24.391  36.100  1.00 27.18  ? 152 LEU B CG  1 
ATOM   4855  C  CD1 . LEU B 2 152 ? 16.949  24.811  34.756  1.00 31.70  ? 152 LEU B CD1 1 
ATOM   4856  C  CD2 . LEU B 2 152 ? 17.117  22.877  36.266  1.00 29.26  ? 152 LEU B CD2 1 
ATOM   4857  N  N   . THR B 2 153 ? 18.889  26.392  38.823  1.00 27.35  ? 153 THR B N   1 
ATOM   4858  C  CA  . THR B 2 153 ? 18.205  26.917  40.002  1.00 28.19  ? 153 THR B CA  1 
ATOM   4859  C  C   . THR B 2 153 ? 18.729  28.277  40.441  1.00 30.02  ? 153 THR B C   1 
ATOM   4860  O  O   . THR B 2 153 ? 18.043  28.974  41.191  1.00 32.56  ? 153 THR B O   1 
ATOM   4861  C  CB  . THR B 2 153 ? 18.356  25.931  41.152  1.00 29.54  ? 153 THR B CB  1 
ATOM   4862  O  OG1 . THR B 2 153 ? 19.741  25.840  41.486  1.00 33.86  ? 153 THR B OG1 1 
ATOM   4863  C  CG2 . THR B 2 153 ? 17.840  24.556  40.778  1.00 29.17  ? 153 THR B CG2 1 
ATOM   4864  N  N   . GLY B 2 154 ? 19.928  28.666  39.987  1.00 32.31  ? 154 GLY B N   1 
ATOM   4865  C  CA  . GLY B 2 154 ? 20.584  29.888  40.427  1.00 33.76  ? 154 GLY B CA  1 
ATOM   4866  C  C   . GLY B 2 154 ? 21.177  29.825  41.818  1.00 40.57  ? 154 GLY B C   1 
ATOM   4867  O  O   . GLY B 2 154 ? 21.637  30.852  42.327  1.00 37.66  ? 154 GLY B O   1 
ATOM   4868  N  N   . LYS B 2 155 ? 21.157  28.668  42.459  1.00 32.49  ? 155 LYS B N   1 
ATOM   4869  C  CA  . LYS B 2 155 ? 21.633  28.499  43.832  1.00 35.31  ? 155 LYS B CA  1 
ATOM   4870  C  C   . LYS B 2 155 ? 22.889  27.633  43.815  1.00 34.93  ? 155 LYS B C   1 
ATOM   4871  O  O   . LYS B 2 155 ? 22.895  26.566  43.189  1.00 34.59  ? 155 LYS B O   1 
ATOM   4872  C  CB  . LYS B 2 155 ? 20.568  27.841  44.729  1.00 40.13  ? 155 LYS B CB  1 
ATOM   4873  C  CG  . LYS B 2 155 ? 19.164  28.475  44.699  1.00 39.96  ? 155 LYS B CG  1 
ATOM   4874  C  CD  . LYS B 2 155 ? 19.217  29.873  45.276  1.00 49.89  ? 155 LYS B CD  1 
ATOM   4875  C  CE  . LYS B 2 155 ? 19.447  29.830  46.790  1.00 51.41  ? 155 LYS B CE  1 
ATOM   4876  N  NZ  . LYS B 2 155 ? 19.207  31.136  47.436  1.00 58.25  ? 155 LYS B NZ  1 
ATOM   4877  N  N   . GLU B 2 156 ? 23.951  28.081  44.484  1.00 32.22  ? 156 GLU B N   1 
ATOM   4878  C  CA  . GLU B 2 156 ? 25.152  27.251  44.505  1.00 31.92  ? 156 GLU B CA  1 
ATOM   4879  C  C   . GLU B 2 156 ? 24.860  25.923  45.203  1.00 31.96  ? 156 GLU B C   1 
ATOM   4880  O  O   . GLU B 2 156 ? 24.247  25.880  46.274  1.00 30.05  ? 156 GLU B O   1 
ATOM   4881  C  CB  . GLU B 2 156 ? 26.282  27.986  45.217  1.00 35.17  ? 156 GLU B CB  1 
ATOM   4882  C  CG  . GLU B 2 156 ? 27.569  27.197  45.331  1.00 34.90  ? 156 GLU B CG  1 
ATOM   4883  C  CD  . GLU B 2 156 ? 28.651  27.940  46.151  1.00 43.47  ? 156 GLU B CD  1 
ATOM   4884  O  OE1 . GLU B 2 156 ? 28.360  29.022  46.701  1.00 49.37  ? 156 GLU B OE1 1 
ATOM   4885  O  OE2 . GLU B 2 156 ? 29.766  27.380  46.342  1.00 44.70  ? 156 GLU B OE2 1 
ATOM   4886  N  N   . ILE B 2 157 ? 25.304  24.845  44.602  1.00 28.30  ? 157 ILE B N   1 
ATOM   4887  C  CA  . ILE B 2 157 ? 25.156  23.518  45.195  1.00 27.41  ? 157 ILE B CA  1 
ATOM   4888  C  C   . ILE B 2 157 ? 26.526  23.192  45.781  1.00 27.83  ? 157 ILE B C   1 
ATOM   4889  O  O   . ILE B 2 157 ? 27.454  22.819  45.048  1.00 31.73  ? 157 ILE B O   1 
ATOM   4890  C  CB  . ILE B 2 157 ? 24.713  22.477  44.167  1.00 27.58  ? 157 ILE B CB  1 
ATOM   4891  C  CG1 . ILE B 2 157 ? 23.311  22.796  43.602  1.00 26.40  ? 157 ILE B CG1 1 
ATOM   4892  C  CG2 . ILE B 2 157 ? 24.720  21.079  44.807  1.00 30.50  ? 157 ILE B CG2 1 
ATOM   4893  C  CD1 . ILE B 2 157 ? 22.942  21.933  42.423  1.00 27.61  ? 157 ILE B CD1 1 
ATOM   4894  N  N   . THR B 2 158 ? 26.648  23.310  47.092  1.00 26.94  ? 158 THR B N   1 
ATOM   4895  C  CA  . THR B 2 158 ? 27.943  23.258  47.767  1.00 27.74  ? 158 THR B CA  1 
ATOM   4896  C  C   . THR B 2 158 ? 28.349  21.804  48.046  1.00 29.64  ? 158 THR B C   1 
ATOM   4897  O  O   . THR B 2 158 ? 27.525  20.903  47.994  1.00 28.95  ? 158 THR B O   1 
ATOM   4898  C  CB  . THR B 2 158 ? 27.874  24.012  49.074  1.00 30.75  ? 158 THR B CB  1 
ATOM   4899  O  OG1 . THR B 2 158 ? 26.967  23.318  49.950  1.00 29.89  ? 158 THR B OG1 1 
ATOM   4900  C  CG2 . THR B 2 158 ? 27.367  25.451  48.857  1.00 27.90  ? 158 THR B CG2 1 
ATOM   4901  N  N   . ASP B 2 159 ? 29.633  21.583  48.353  1.00 26.39  ? 159 ASP B N   1 
ATOM   4902  C  CA  . ASP B 2 159 ? 30.018  20.219  48.721  1.00 28.14  ? 159 ASP B CA  1 
ATOM   4903  C  C   . ASP B 2 159 ? 29.238  19.750  49.954  1.00 31.18  ? 159 ASP B C   1 
ATOM   4904  O  O   . ASP B 2 159 ? 28.849  18.573  50.048  1.00 26.07  ? 159 ASP B O   1 
ATOM   4905  C  CB  . ASP B 2 159 ? 31.529  20.165  48.987  1.00 32.87  ? 159 ASP B CB  1 
ATOM   4906  C  CG  . ASP B 2 159 ? 32.354  20.249  47.694  1.00 35.01  ? 159 ASP B CG  1 
ATOM   4907  O  OD1 . ASP B 2 159 ? 31.761  20.352  46.601  1.00 35.89  ? 159 ASP B OD1 1 
ATOM   4908  O  OD2 . ASP B 2 159 ? 33.594  20.245  47.765  1.00 43.33  ? 159 ASP B OD2 1 
ATOM   4909  N  N   . ALA B 2 160 ? 28.987  20.672  50.904  1.00 31.14  ? 160 ALA B N   1 
ATOM   4910  C  CA  . ALA B 2 160 ? 28.194  20.308  52.074  1.00 30.75  ? 160 ALA B CA  1 
ATOM   4911  C  C   . ALA B 2 160 ? 26.790  19.877  51.688  1.00 30.65  ? 160 ALA B C   1 
ATOM   4912  O  O   . ALA B 2 160 ? 26.255  18.917  52.272  1.00 30.49  ? 160 ALA B O   1 
ATOM   4913  C  CB  . ALA B 2 160 ? 28.154  21.459  53.068  1.00 29.41  ? 160 ALA B CB  1 
ATOM   4914  N  N   . MET B 2 161 ? 26.184  20.536  50.696  1.00 26.17  ? 161 MET B N   1 
ATOM   4915  C  CA  . MET B 2 161 ? 24.826  20.145  50.323  1.00 26.55  ? 161 MET B CA  1 
ATOM   4916  C  C   . MET B 2 161 ? 24.867  18.764  49.659  1.00 29.06  ? 161 MET B C   1 
ATOM   4917  O  O   . MET B 2 161 ? 23.960  17.934  49.854  1.00 27.99  ? 161 MET B O   1 
ATOM   4918  C  CB  . MET B 2 161 ? 24.192  21.128  49.324  1.00 30.18  ? 161 MET B CB  1 
ATOM   4919  C  CG  . MET B 2 161 ? 23.564  22.359  50.006  1.00 26.98  ? 161 MET B CG  1 
ATOM   4920  S  SD  . MET B 2 161 ? 23.762  23.842  48.919  1.00 30.32  ? 161 MET B SD  1 
ATOM   4921  C  CE  . MET B 2 161 ? 22.300  23.451  47.969  1.00 29.86  ? 161 MET B CE  1 
ATOM   4922  N  N   . LEU B 2 162 ? 25.936  18.515  48.900  1.00 24.72  ? 162 LEU B N   1 
ATOM   4923  C  CA  . LEU B 2 162 ? 26.088  17.238  48.211  1.00 23.96  ? 162 LEU B CA  1 
ATOM   4924  C  C   . LEU B 2 162 ? 26.378  16.138  49.223  1.00 26.89  ? 162 LEU B C   1 
ATOM   4925  O  O   . LEU B 2 162 ? 25.865  15.029  49.104  1.00 27.16  ? 162 LEU B O   1 
ATOM   4926  C  CB  . LEU B 2 162 ? 27.205  17.322  47.184  1.00 27.16  ? 162 LEU B CB  1 
ATOM   4927  C  CG  . LEU B 2 162 ? 26.917  18.105  45.901  1.00 27.14  ? 162 LEU B CG  1 
ATOM   4928  C  CD1 . LEU B 2 162 ? 28.195  18.370  45.153  1.00 27.90  ? 162 LEU B CD1 1 
ATOM   4929  C  CD2 . LEU B 2 162 ? 25.917  17.361  45.051  1.00 28.36  ? 162 LEU B CD2 1 
ATOM   4930  N  N   . SER B 2 163 ? 27.188  16.437  50.223  1.00 26.10  ? 163 SER B N   1 
ATOM   4931  C  CA  . SER B 2 163 ? 27.439  15.411  51.246  1.00 27.83  ? 163 SER B CA  1 
ATOM   4932  C  C   . SER B 2 163 ? 26.199  15.080  52.047  1.00 28.68  ? 163 SER B C   1 
ATOM   4933  O  O   . SER B 2 163 ? 25.962  13.907  52.377  1.00 29.37  ? 163 SER B O   1 
ATOM   4934  C  CB  . SER B 2 163 ? 28.583  15.813  52.171  1.00 29.90  ? 163 SER B CB  1 
ATOM   4935  O  OG  . SER B 2 163 ? 29.795  15.789  51.399  1.00 35.18  ? 163 SER B OG  1 
ATOM   4936  N  N   . ASP B 2 164 ? 25.419  16.085  52.415  1.00 28.64  ? 164 ASP B N   1 
ATOM   4937  C  CA  . ASP B 2 164 ? 24.199  15.803  53.168  1.00 28.34  ? 164 ASP B CA  1 
ATOM   4938  C  C   . ASP B 2 164 ? 23.238  14.969  52.314  1.00 31.21  ? 164 ASP B C   1 
ATOM   4939  O  O   . ASP B 2 164 ? 22.619  14.018  52.797  1.00 28.69  ? 164 ASP B O   1 
ATOM   4940  C  CB  . ASP B 2 164 ? 23.530  17.109  53.583  1.00 33.10  ? 164 ASP B CB  1 
ATOM   4941  C  CG  . ASP B 2 164 ? 22.051  16.912  53.889  1.00 42.64  ? 164 ASP B CG  1 
ATOM   4942  O  OD1 . ASP B 2 164 ? 21.753  16.538  55.042  1.00 48.39  ? 164 ASP B OD1 1 
ATOM   4943  O  OD2 . ASP B 2 164 ? 21.196  16.996  52.975  1.00 47.54  ? 164 ASP B OD2 1 
ATOM   4944  N  N   . ALA B 2 165 ? 23.176  15.244  51.006  1.00 27.49  ? 165 ALA B N   1 
ATOM   4945  C  CA  . ALA B 2 165 ? 22.300  14.465  50.143  1.00 27.60  ? 165 ALA B CA  1 
ATOM   4946  C  C   . ALA B 2 165 ? 22.820  13.036  49.992  1.00 22.72  ? 165 ALA B C   1 
ATOM   4947  O  O   . ALA B 2 165 ? 22.040  12.080  49.991  1.00 28.24  ? 165 ALA B O   1 
ATOM   4948  C  CB  . ALA B 2 165 ? 22.171  15.106  48.756  1.00 25.64  ? 165 ALA B CB  1 
ATOM   4949  N  N   . LEU B 2 166 ? 24.126  12.885  49.843  1.00 22.54  ? 166 LEU B N   1 
ATOM   4950  C  CA  . LEU B 2 166 ? 24.653  11.519  49.739  1.00 25.34  ? 166 LEU B CA  1 
ATOM   4951  C  C   . LEU B 2 166 ? 24.416  10.774  51.041  1.00 24.02  ? 166 LEU B C   1 
ATOM   4952  O  O   . LEU B 2 166 ? 24.161  9.552   51.025  1.00 24.76  ? 166 LEU B O   1 
ATOM   4953  C  CB  . LEU B 2 166 ? 26.146  11.592  49.414  1.00 28.24  ? 166 LEU B CB  1 
ATOM   4954  C  CG  . LEU B 2 166 ? 26.964  10.296  49.333  1.00 25.36  ? 166 LEU B CG  1 
ATOM   4955  C  CD1 . LEU B 2 166 ? 26.432  9.355   48.282  1.00 24.30  ? 166 LEU B CD1 1 
ATOM   4956  C  CD2 . LEU B 2 166 ? 28.447  10.631  49.153  1.00 24.92  ? 166 LEU B CD2 1 
ATOM   4957  N  N   . ALA B 2 167 ? 24.474  11.474  52.179  1.00 26.97  ? 167 ALA B N   1 
ATOM   4958  C  CA  . ALA B 2 167 ? 24.271  10.794  53.458  1.00 24.45  ? 167 ALA B CA  1 
ATOM   4959  C  C   . ALA B 2 167 ? 22.847  10.269  53.546  1.00 27.13  ? 167 ALA B C   1 
ATOM   4960  O  O   . ALA B 2 167 ? 22.623  9.136   53.986  1.00 30.31  ? 167 ALA B O   1 
ATOM   4961  C  CB  . ALA B 2 167 ? 24.585  11.732  54.635  1.00 24.24  ? 167 ALA B CB  1 
ATOM   4962  N  N   . VAL B 2 168 ? 21.875  11.044  53.051  1.00 24.62  ? 168 VAL B N   1 
ATOM   4963  C  CA  . VAL B 2 168 ? 20.487  10.581  53.043  1.00 27.29  ? 168 VAL B CA  1 
ATOM   4964  C  C   . VAL B 2 168 ? 20.338  9.376   52.115  1.00 26.42  ? 168 VAL B C   1 
ATOM   4965  O  O   . VAL B 2 168 ? 19.655  8.400   52.449  1.00 28.81  ? 168 VAL B O   1 
ATOM   4966  C  CB  . VAL B 2 168 ? 19.560  11.752  52.640  1.00 34.57  ? 168 VAL B CB  1 
ATOM   4967  C  CG1 . VAL B 2 168 ? 18.141  11.292  52.453  1.00 35.74  ? 168 VAL B CG1 1 
ATOM   4968  C  CG2 . VAL B 2 168 ? 19.564  12.827  53.777  1.00 34.55  ? 168 VAL B CG2 1 
ATOM   4969  N  N   . CYS B 2 169 ? 20.929  9.443   50.936  1.00 22.29  ? 169 CYS B N   1 
ATOM   4970  C  CA  . CYS B 2 169 ? 20.849  8.320   49.986  1.00 22.88  ? 169 CYS B CA  1 
ATOM   4971  C  C   . CYS B 2 169 ? 21.552  7.091   50.557  1.00 25.85  ? 169 CYS B C   1 
ATOM   4972  O  O   . CYS B 2 169 ? 21.010  5.979   50.513  1.00 25.82  ? 169 CYS B O   1 
ATOM   4973  C  CB  . CYS B 2 169 ? 21.445  8.729   48.636  1.00 23.33  ? 169 CYS B CB  1 
ATOM   4974  S  SG  . CYS B 2 169 ? 20.294  9.929   47.835  1.00 28.09  ? 169 CYS B SG  1 
ATOM   4975  N  N   . ASP B 2 170 ? 22.761  7.258   51.116  1.00 22.03  ? 170 ASP B N   1 
ATOM   4976  C  CA  . ASP B 2 170 ? 23.440  6.082   51.662  1.00 23.92  ? 170 ASP B CA  1 
ATOM   4977  C  C   . ASP B 2 170 ? 22.661  5.491   52.843  1.00 25.57  ? 170 ASP B C   1 
ATOM   4978  O  O   . ASP B 2 170 ? 22.661  4.271   53.046  1.00 26.71  ? 170 ASP B O   1 
ATOM   4979  C  CB  . ASP B 2 170 ? 24.851  6.459   52.103  1.00 25.60  ? 170 ASP B CB  1 
ATOM   4980  C  CG  . ASP B 2 170 ? 25.833  6.536   50.937  1.00 26.08  ? 170 ASP B CG  1 
ATOM   4981  O  OD1 . ASP B 2 170 ? 25.521  5.970   49.883  1.00 24.21  ? 170 ASP B OD1 1 
ATOM   4982  O  OD2 . ASP B 2 170 ? 26.923  7.167   51.123  1.00 30.61  ? 170 ASP B OD2 1 
ATOM   4983  N  N   . GLU B 2 171 ? 22.014  6.339   53.649  1.00 24.63  ? 171 GLU B N   1 
ATOM   4984  C  CA  . GLU B 2 171 ? 21.218  5.813   54.763  1.00 27.94  ? 171 GLU B CA  1 
ATOM   4985  C  C   . GLU B 2 171 ? 20.052  5.000   54.210  1.00 29.06  ? 171 GLU B C   1 
ATOM   4986  O  O   . GLU B 2 171 ? 19.748  3.904   54.696  1.00 28.06  ? 171 GLU B O   1 
ATOM   4987  C  CB  . GLU B 2 171 ? 20.710  6.968   55.634  1.00 28.77  ? 171 GLU B CB  1 
ATOM   4988  C  CG  . GLU B 2 171 ? 19.559  6.497   56.553  1.00 30.35  ? 171 GLU B CG  1 
ATOM   4989  C  CD  . GLU B 2 171 ? 19.402  7.333   57.812  1.00 43.35  ? 171 GLU B CD  1 
ATOM   4990  O  OE1 . GLU B 2 171 ? 19.305  8.581   57.646  1.00 47.32  ? 171 GLU B OE1 1 
ATOM   4991  O  OE2 . GLU B 2 171 ? 19.301  6.758   58.934  1.00 51.10  ? 171 GLU B OE2 1 
ATOM   4992  N  N   . ASN B 2 172 ? 19.403  5.505   53.163  1.00 27.42  ? 172 ASN B N   1 
ATOM   4993  C  CA  . ASN B 2 172 ? 18.354  4.728   52.503  1.00 26.47  ? 172 ASN B CA  1 
ATOM   4994  C  C   . ASN B 2 172 ? 18.880  3.397   52.015  1.00 26.22  ? 172 ASN B C   1 
ATOM   4995  O  O   . ASN B 2 172 ? 18.211  2.358   52.208  1.00 26.76  ? 172 ASN B O   1 
ATOM   4996  C  CB  . ASN B 2 172 ? 17.753  5.529   51.347  1.00 26.63  ? 172 ASN B CB  1 
ATOM   4997  C  CG  . ASN B 2 172 ? 16.423  4.934   50.842  1.00 24.43  ? 172 ASN B CG  1 
ATOM   4998  O  OD1 . ASN B 2 172 ? 16.346  4.379   49.729  1.00 27.43  ? 172 ASN B OD1 1 
ATOM   4999  N  ND2 . ASN B 2 172 ? 15.386  5.059   51.640  1.00 28.34  ? 172 ASN B ND2 1 
ATOM   5000  N  N   . ARG B 2 173 ? 20.074  3.400   51.385  1.00 23.42  ? 173 ARG B N   1 
ATOM   5001  C  CA  . ARG B 2 173 ? 20.646  2.155   50.883  1.00 25.58  ? 173 ARG B CA  1 
ATOM   5002  C  C   . ARG B 2 173 ? 20.973  1.184   52.014  1.00 27.00  ? 173 ARG B C   1 
ATOM   5003  O  O   . ARG B 2 173 ? 20.773  -0.037  51.876  1.00 24.92  ? 173 ARG B O   1 
ATOM   5004  C  CB  . ARG B 2 173 ? 21.882  2.453   50.061  1.00 24.92  ? 173 ARG B CB  1 
ATOM   5005  C  CG  . ARG B 2 173 ? 21.509  3.273   48.820  1.00 25.54  ? 173 ARG B CG  1 
ATOM   5006  C  CD  . ARG B 2 173 ? 22.756  3.944   48.181  1.00 26.03  ? 173 ARG B CD  1 
ATOM   5007  N  NE  . ARG B 2 173 ? 22.426  4.759   46.996  1.00 25.25  ? 173 ARG B NE  1 
ATOM   5008  C  CZ  . ARG B 2 173 ? 23.040  5.881   46.655  1.00 26.14  ? 173 ARG B CZ  1 
ATOM   5009  N  NH1 . ARG B 2 173 ? 24.085  6.330   47.333  1.00 25.18  ? 173 ARG B NH1 1 
ATOM   5010  N  NH2 . ARG B 2 173 ? 22.637  6.531   45.564  1.00 24.56  ? 173 ARG B NH2 1 
ATOM   5011  N  N   . ARG B 2 174 ? 21.481  1.701   53.127  1.00 26.97  ? 174 ARG B N   1 
ATOM   5012  C  CA  . ARG B 2 174 ? 21.847  0.820   54.232  1.00 25.47  ? 174 ARG B CA  1 
ATOM   5013  C  C   . ARG B 2 174 ? 20.604  0.269   54.897  1.00 25.64  ? 174 ARG B C   1 
ATOM   5014  O  O   . ARG B 2 174 ? 20.553  -0.924  55.259  1.00 27.68  ? 174 ARG B O   1 
ATOM   5015  C  CB  . ARG B 2 174 ? 22.726  1.584   55.205  1.00 29.25  ? 174 ARG B CB  1 
ATOM   5016  C  CG  . ARG B 2 174 ? 24.080  1.911   54.612  1.00 31.17  ? 174 ARG B CG  1 
ATOM   5017  C  CD  . ARG B 2 174 ? 25.099  2.345   55.647  1.00 40.39  ? 174 ARG B CD  1 
ATOM   5018  N  NE  . ARG B 2 174 ? 26.375  2.629   55.000  1.00 42.94  ? 174 ARG B NE  1 
ATOM   5019  C  CZ  . ARG B 2 174 ? 26.883  3.833   54.744  1.00 40.58  ? 174 ARG B CZ  1 
ATOM   5020  N  NH1 . ARG B 2 174 ? 26.272  4.952   55.110  1.00 34.98  ? 174 ARG B NH1 1 
ATOM   5021  N  NH2 . ARG B 2 174 ? 28.069  3.913   54.144  1.00 43.58  ? 174 ARG B NH2 1 
ATOM   5022  N  N   . LEU B 2 175 ? 19.581  1.117   55.074  1.00 26.15  ? 175 LEU B N   1 
ATOM   5023  C  CA  . LEU B 2 175 ? 18.340  0.633   55.683  1.00 26.83  ? 175 LEU B CA  1 
ATOM   5024  C  C   . LEU B 2 175 ? 17.667  -0.428  54.813  1.00 26.97  ? 175 LEU B C   1 
ATOM   5025  O  O   . LEU B 2 175 ? 17.191  -1.433  55.348  1.00 26.13  ? 175 LEU B O   1 
ATOM   5026  C  CB  . LEU B 2 175 ? 17.381  1.782   55.935  1.00 28.29  ? 175 LEU B CB  1 
ATOM   5027  C  CG  . LEU B 2 175 ? 17.919  2.670   57.046  1.00 28.39  ? 175 LEU B CG  1 
ATOM   5028  C  CD1 . LEU B 2 175 ? 17.100  4.000   57.035  1.00 29.52  ? 175 LEU B CD1 1 
ATOM   5029  C  CD2 . LEU B 2 175 ? 17.903  2.025   58.475  1.00 29.69  ? 175 LEU B CD2 1 
ATOM   5030  N  N   . LEU B 2 176 ? 17.619  -0.224  53.470  1.00 27.67  ? 176 LEU B N   1 
ATOM   5031  C  CA  . LEU B 2 176 ? 17.059  -1.246  52.568  1.00 23.89  ? 176 LEU B CA  1 
ATOM   5032  C  C   . LEU B 2 176 ? 17.839  -2.546  52.651  1.00 26.76  ? 176 LEU B C   1 
ATOM   5033  O  O   . LEU B 2 176 ? 17.237  -3.629  52.680  1.00 26.95  ? 176 LEU B O   1 
ATOM   5034  C  CB  . LEU B 2 176 ? 16.990  -0.731  51.122  1.00 25.31  ? 176 LEU B CB  1 
ATOM   5035  C  CG  . LEU B 2 176 ? 15.815  0.266   50.871  1.00 24.22  ? 176 LEU B CG  1 
ATOM   5036  C  CD1 . LEU B 2 176 ? 15.963  0.905   49.465  1.00 25.10  ? 176 LEU B CD1 1 
ATOM   5037  C  CD2 . LEU B 2 176 ? 14.423  -0.386  51.072  1.00 26.31  ? 176 LEU B CD2 1 
ATOM   5038  N  N   . ARG B 2 177 ? 19.180  -2.467  52.750  1.00 26.13  ? 177 ARG B N   1 
ATOM   5039  C  CA  . ARG B 2 177 ? 19.989  -3.679  52.941  1.00 28.05  ? 177 ARG B CA  1 
ATOM   5040  C  C   . ARG B 2 177 ? 19.657  -4.357  54.283  1.00 27.20  ? 177 ARG B C   1 
ATOM   5041  O  O   . ARG B 2 177 ? 19.605  -5.596  54.367  1.00 30.25  ? 177 ARG B O   1 
ATOM   5042  C  CB  . ARG B 2 177 ? 21.490  -3.325  52.892  1.00 29.75  ? 177 ARG B CB  1 
ATOM   5043  C  CG  . ARG B 2 177 ? 22.208  -3.359  51.481  1.00 31.87  ? 177 ARG B CG  1 
ATOM   5044  C  CD  . ARG B 2 177 ? 21.991  -4.676  50.667  1.00 30.14  ? 177 ARG B CD  1 
ATOM   5045  N  NE  . ARG B 2 177 ? 22.953  -5.727  51.020  1.00 30.94  ? 177 ARG B NE  1 
ATOM   5046  C  CZ  . ARG B 2 177 ? 24.238  -5.723  50.691  1.00 32.97  ? 177 ARG B CZ  1 
ATOM   5047  N  NH1 . ARG B 2 177 ? 24.791  -4.702  50.023  1.00 29.63  ? 177 ARG B NH1 1 
ATOM   5048  N  NH2 . ARG B 2 177 ? 24.979  -6.777  50.994  1.00 37.13  ? 177 ARG B NH2 1 
ATOM   5049  N  N   . GLU B 2 178 ? 19.441  -3.576  55.364  1.00 26.63  ? 178 GLU B N   1 
ATOM   5050  C  CA  . GLU B 2 178 ? 19.066  -4.170  56.641  1.00 26.51  ? 178 GLU B CA  1 
ATOM   5051  C  C   . GLU B 2 178 ? 17.713  -4.856  56.553  1.00 26.16  ? 178 GLU B C   1 
ATOM   5052  O  O   . GLU B 2 178 ? 17.492  -5.908  57.195  1.00 29.01  ? 178 GLU B O   1 
ATOM   5053  C  CB  . GLU B 2 178 ? 18.979  -3.063  57.713  1.00 31.03  ? 178 GLU B CB  1 
ATOM   5054  C  CG  . GLU B 2 178 ? 20.315  -2.628  58.308  1.00 37.31  ? 178 GLU B CG  1 
ATOM   5055  C  CD  . GLU B 2 178 ? 20.152  -1.567  59.418  1.00 43.24  ? 178 GLU B CD  1 
ATOM   5056  O  OE1 . GLU B 2 178 ? 19.186  -1.655  60.197  1.00 45.40  ? 178 GLU B OE1 1 
ATOM   5057  O  OE2 . GLU B 2 178 ? 21.017  -0.670  59.517  1.00 51.41  ? 178 GLU B OE2 1 
ATOM   5058  N  N   . LEU B 2 179 ? 16.769  -4.226  55.828  1.00 28.69  ? 179 LEU B N   1 
ATOM   5059  C  CA  . LEU B 2 179 ? 15.455  -4.814  55.619  1.00 28.21  ? 179 LEU B CA  1 
ATOM   5060  C  C   . LEU B 2 179 ? 15.593  -6.134  54.893  1.00 28.06  ? 179 LEU B C   1 
ATOM   5061  O  O   . LEU B 2 179 ? 14.919  -7.110  55.240  1.00 30.26  ? 179 LEU B O   1 
ATOM   5062  C  CB  . LEU B 2 179 ? 14.572  -3.898  54.778  1.00 28.38  ? 179 LEU B CB  1 
ATOM   5063  C  CG  . LEU B 2 179 ? 13.106  -4.279  54.740  1.00 31.43  ? 179 LEU B CG  1 
ATOM   5064  C  CD1 . LEU B 2 179 ? 12.377  -3.876  56.015  1.00 34.79  ? 179 LEU B CD1 1 
ATOM   5065  C  CD2 . LEU B 2 179 ? 12.470  -3.587  53.537  1.00 33.00  ? 179 LEU B CD2 1 
ATOM   5066  N  N   . TYR B 2 180 ? 16.447  -6.166  53.867  1.00 25.13  ? 180 TYR B N   1 
ATOM   5067  C  CA  . TYR B 2 180 ? 16.682  -7.400  53.084  1.00 24.66  ? 180 TYR B CA  1 
ATOM   5068  C  C   . TYR B 2 180 ? 17.258  -8.519  53.948  1.00 31.49  ? 180 TYR B C   1 
ATOM   5069  O  O   . TYR B 2 180 ? 16.990  -9.698  53.682  1.00 29.07  ? 180 TYR B O   1 
ATOM   5070  C  CB  . TYR B 2 180 ? 17.639  -7.145  51.941  1.00 25.83  ? 180 TYR B CB  1 
ATOM   5071  C  CG  . TYR B 2 180 ? 16.920  -6.821  50.647  1.00 28.24  ? 180 TYR B CG  1 
ATOM   5072  C  CD1 . TYR B 2 180 ? 15.827  -5.923  50.645  1.00 26.97  ? 180 TYR B CD1 1 
ATOM   5073  C  CD2 . TYR B 2 180 ? 17.317  -7.396  49.452  1.00 25.62  ? 180 TYR B CD2 1 
ATOM   5074  C  CE1 . TYR B 2 180 ? 15.158  -5.617  49.456  1.00 28.70  ? 180 TYR B CE1 1 
ATOM   5075  C  CE2 . TYR B 2 180 ? 16.687  -7.081  48.268  1.00 25.82  ? 180 TYR B CE2 1 
ATOM   5076  C  CZ  . TYR B 2 180 ? 15.595  -6.219  48.268  1.00 27.78  ? 180 TYR B CZ  1 
ATOM   5077  O  OH  . TYR B 2 180 ? 14.964  -5.971  47.053  1.00 31.85  ? 180 TYR B OH  1 
ATOM   5078  N  N   . GLU B 2 181 ? 18.108  -8.177  54.924  1.00 30.55  ? 181 GLU B N   1 
ATOM   5079  C  CA  . GLU B 2 181 ? 18.742  -9.180  55.789  1.00 31.44  ? 181 GLU B CA  1 
ATOM   5080  C  C   . GLU B 2 181 ? 17.718  -10.095 56.447  1.00 35.22  ? 181 GLU B C   1 
ATOM   5081  O  O   . GLU B 2 181 ? 17.996  -11.273 56.684  1.00 33.15  ? 181 GLU B O   1 
ATOM   5082  C  CB  . GLU B 2 181 ? 19.545  -8.473  56.881  1.00 35.55  ? 181 GLU B CB  1 
ATOM   5083  C  CG  . GLU B 2 181 ? 21.020  -8.295  56.605  1.00 39.82  ? 181 GLU B CG  1 
ATOM   5084  C  CD  . GLU B 2 181 ? 21.754  -9.607  56.445  1.00 39.58  ? 181 GLU B CD  1 
ATOM   5085  O  OE1 . GLU B 2 181 ? 21.775  -10.421 57.407  1.00 53.76  ? 181 GLU B OE1 1 
ATOM   5086  O  OE2 . GLU B 2 181 ? 22.336  -9.808  55.370  1.00 51.41  ? 181 GLU B OE2 1 
ATOM   5087  N  N   . TYR B 2 182 ? 16.531  -9.571  56.758  1.00 32.09  ? 182 TYR B N   1 
ATOM   5088  C  CA  . TYR B 2 182 ? 15.486  -10.389 57.388  1.00 33.71  ? 182 TYR B CA  1 
ATOM   5089  C  C   . TYR B 2 182 ? 14.954  -11.477 56.460  1.00 32.07  ? 182 TYR B C   1 
ATOM   5090  O  O   . TYR B 2 182 ? 14.466  -12.503 56.940  1.00 32.40  ? 182 TYR B O   1 
ATOM   5091  C  CB  . TYR B 2 182 ? 14.341  -9.504  57.833  1.00 30.71  ? 182 TYR B CB  1 
ATOM   5092  C  CG  . TYR B 2 182 ? 14.574  -8.794  59.120  1.00 32.59  ? 182 TYR B CG  1 
ATOM   5093  C  CD1 . TYR B 2 182 ? 14.247  -9.403  60.339  1.00 34.60  ? 182 TYR B CD1 1 
ATOM   5094  C  CD2 . TYR B 2 182 ? 15.141  -7.533  59.136  1.00 30.59  ? 182 TYR B CD2 1 
ATOM   5095  C  CE1 . TYR B 2 182 ? 14.425  -8.768  61.516  1.00 36.34  ? 182 TYR B CE1 1 
ATOM   5096  C  CE2 . TYR B 2 182 ? 15.325  -6.889  60.346  1.00 33.23  ? 182 TYR B CE2 1 
ATOM   5097  C  CZ  . TYR B 2 182 ? 14.978  -7.508  61.511  1.00 35.80  ? 182 TYR B CZ  1 
ATOM   5098  O  OH  . TYR B 2 182 ? 15.160  -6.907  62.749  1.00 38.23  ? 182 TYR B OH  1 
ATOM   5099  N  N   . ARG B 2 183 ? 15.047  -11.286 55.139  1.00 30.24  ? 183 ARG B N   1 
ATOM   5100  C  CA  . ARG B 2 183 ? 14.614  -12.303 54.184  1.00 31.59  ? 183 ARG B CA  1 
ATOM   5101  C  C   . ARG B 2 183 ? 15.492  -13.558 54.197  1.00 33.01  ? 183 ARG B C   1 
ATOM   5102  O  O   . ARG B 2 183 ? 15.062  -14.593 53.663  1.00 33.31  ? 183 ARG B O   1 
ATOM   5103  C  CB  . ARG B 2 183 ? 14.553  -11.657 52.784  1.00 31.98  ? 183 ARG B CB  1 
ATOM   5104  C  CG  . ARG B 2 183 ? 13.751  -10.317 52.794  1.00 30.19  ? 183 ARG B CG  1 
ATOM   5105  C  CD  . ARG B 2 183 ? 13.933  -9.617  51.440  1.00 32.35  ? 183 ARG B CD  1 
ATOM   5106  N  NE  . ARG B 2 183 ? 13.094  -10.215 50.412  1.00 32.53  ? 183 ARG B NE  1 
ATOM   5107  C  CZ  . ARG B 2 183 ? 13.165  -9.914  49.124  1.00 33.12  ? 183 ARG B CZ  1 
ATOM   5108  N  NH1 . ARG B 2 183 ? 14.025  -9.008  48.662  1.00 34.13  ? 183 ARG B NH1 1 
ATOM   5109  N  NH2 . ARG B 2 183 ? 12.319  -10.491 48.279  1.00 30.48  ? 183 ARG B NH2 1 
ATOM   5110  N  N   . LYS B 2 184 ? 16.688  -13.510 54.814  1.00 33.39  ? 184 LYS B N   1 
ATOM   5111  C  CA  . LYS B 2 184 ? 17.528  -14.708 54.904  1.00 33.42  ? 184 LYS B CA  1 
ATOM   5112  C  C   . LYS B 2 184 ? 17.010  -15.734 55.900  1.00 37.56  ? 184 LYS B C   1 
ATOM   5113  O  O   . LYS B 2 184 ? 17.416  -16.905 55.816  1.00 36.71  ? 184 LYS B O   1 
ATOM   5114  C  CB  . LYS B 2 184 ? 18.965  -14.379 55.309  1.00 37.03  ? 184 LYS B CB  1 
ATOM   5115  C  CG  . LYS B 2 184 ? 19.624  -13.405 54.385  1.00 31.66  ? 184 LYS B CG  1 
ATOM   5116  C  CD  . LYS B 2 184 ? 20.861  -12.795 54.981  1.00 40.23  ? 184 LYS B CD  1 
ATOM   5117  C  CE  . LYS B 2 184 ? 22.026  -12.945 54.076  1.00 39.66  ? 184 LYS B CE  1 
ATOM   5118  N  NZ  . LYS B 2 184 ? 23.006  -11.862 54.296  1.00 38.87  ? 184 LYS B NZ  1 
ATOM   5119  N  N   . ALA B 2 185 ? 16.141  -15.335 56.827  1.00 32.20  ? 185 ALA B N   1 
ATOM   5120  C  CA  . ALA B 2 185 ? 15.681  -16.259 57.869  1.00 34.78  ? 185 ALA B CA  1 
ATOM   5121  C  C   . ALA B 2 185 ? 14.824  -17.384 57.264  1.00 36.52  ? 185 ALA B C   1 
ATOM   5122  O  O   . ALA B 2 185 ? 14.303  -17.283 56.140  1.00 32.58  ? 185 ALA B O   1 
ATOM   5123  C  CB  . ALA B 2 185 ? 14.893  -15.502 58.946  1.00 35.79  ? 185 ALA B CB  1 
ATOM   5124  N  N   . ALA B 2 186 ? 14.702  -18.487 58.020  1.00 36.76  ? 186 ALA B N   1 
ATOM   5125  C  CA  . ALA B 2 186 ? 13.869  -19.607 57.572  1.00 37.57  ? 186 ALA B CA  1 
ATOM   5126  C  C   . ALA B 2 186 ? 12.416  -19.181 57.377  1.00 38.67  ? 186 ALA B C   1 
ATOM   5127  O  O   . ALA B 2 186 ? 11.747  -19.622 56.437  1.00 39.35  ? 186 ALA B O   1 
ATOM   5128  C  CB  . ALA B 2 186 ? 13.936  -20.755 58.577  1.00 36.87  ? 186 ALA B CB  1 
ATOM   5129  N  N   . ASP B 2 187 ? 11.918  -18.287 58.232  1.00 37.52  ? 187 ASP B N   1 
ATOM   5130  C  CA  . ASP B 2 187 ? 10.543  -17.801 58.132  1.00 36.06  ? 187 ASP B CA  1 
ATOM   5131  C  C   . ASP B 2 187 ? 10.619  -16.283 58.077  1.00 37.53  ? 187 ASP B C   1 
ATOM   5132  O  O   . ASP B 2 187 ? 10.544  -15.610 59.120  1.00 37.80  ? 187 ASP B O   1 
ATOM   5133  C  CB  . ASP B 2 187 ? 9.702   -18.276 59.311  1.00 41.31  ? 187 ASP B CB  1 
ATOM   5134  C  CG  . ASP B 2 187 ? 9.200   -19.678 59.091  1.00 44.69  ? 187 ASP B CG  1 
ATOM   5135  O  OD1 . ASP B 2 187 ? 9.996   -20.594 59.339  1.00 52.12  ? 187 ASP B OD1 1 
ATOM   5136  O  OD2 . ASP B 2 187 ? 8.066   -19.866 58.606  1.00 55.11  ? 187 ASP B OD2 1 
ATOM   5137  N  N   . PRO B 2 188 ? 10.741  -15.707 56.884  1.00 36.79  ? 188 PRO B N   1 
ATOM   5138  C  CA  . PRO B 2 188 ? 11.106  -14.284 56.769  1.00 30.82  ? 188 PRO B CA  1 
ATOM   5139  C  C   . PRO B 2 188 ? 10.032  -13.382 57.375  1.00 36.61  ? 188 PRO B C   1 
ATOM   5140  O  O   . PRO B 2 188 ? 8.842   -13.559 57.126  1.00 37.04  ? 188 PRO B O   1 
ATOM   5141  C  CB  . PRO B 2 188 ? 11.224  -14.075 55.245  1.00 35.95  ? 188 PRO B CB  1 
ATOM   5142  C  CG  . PRO B 2 188 ? 11.435  -15.398 54.672  1.00 33.24  ? 188 PRO B CG  1 
ATOM   5143  C  CD  . PRO B 2 188 ? 10.703  -16.380 55.578  1.00 33.27  ? 188 PRO B CD  1 
ATOM   5144  N  N   . LYS B 2 189 ? 10.461  -12.408 58.182  1.00 33.34  ? 189 LYS B N   1 
ATOM   5145  C  CA  . LYS B 2 189 ? 9.547   -11.418 58.746  1.00 34.17  ? 189 LYS B CA  1 
ATOM   5146  C  C   . LYS B 2 189 ? 9.164   -10.345 57.735  1.00 33.40  ? 189 LYS B C   1 
ATOM   5147  O  O   . LYS B 2 189 ? 8.375   -9.454  58.060  1.00 38.09  ? 189 LYS B O   1 
ATOM   5148  C  CB  . LYS B 2 189 ? 10.174  -10.772 59.986  1.00 37.35  ? 189 LYS B CB  1 
ATOM   5149  C  CG  . LYS B 2 189 ? 10.199  -11.759 61.124  1.00 35.32  ? 189 LYS B CG  1 
ATOM   5150  C  CD  . LYS B 2 189 ? 10.374  -11.073 62.466  1.00 45.16  ? 189 LYS B CD  1 
ATOM   5151  C  CE  . LYS B 2 189 ? 10.652  -12.028 63.594  1.00 44.08  ? 189 LYS B CE  1 
ATOM   5152  N  NZ  . LYS B 2 189 ? 9.569   -13.029 63.675  1.00 51.91  ? 189 LYS B NZ  1 
ATOM   5153  N  N   . VAL B 2 190 ? 9.703   -10.429 56.524  1.00 32.97  ? 190 VAL B N   1 
ATOM   5154  C  CA  . VAL B 2 190 ? 9.449   -9.498  55.421  1.00 32.79  ? 190 VAL B CA  1 
ATOM   5155  C  C   . VAL B 2 190 ? 9.213   -10.357 54.197  1.00 32.37  ? 190 VAL B C   1 
ATOM   5156  O  O   . VAL B 2 190 ? 10.079  -11.157 53.845  1.00 32.00  ? 190 VAL B O   1 
ATOM   5157  C  CB  . VAL B 2 190 ? 10.648  -8.571  55.176  1.00 30.60  ? 190 VAL B CB  1 
ATOM   5158  C  CG1 . VAL B 2 190 ? 10.373  -7.629  54.019  1.00 33.46  ? 190 VAL B CG1 1 
ATOM   5159  C  CG2 . VAL B 2 190 ? 10.992  -7.782  56.489  1.00 34.43  ? 190 VAL B CG2 1 
ATOM   5160  N  N   . THR B 2 191 ? 8.041   -10.221 53.568  1.00 32.94  ? 191 THR B N   1 
ATOM   5161  C  CA  . THR B 2 191 ? 7.795   -10.965 52.331  1.00 26.79  ? 191 THR B CA  1 
ATOM   5162  C  C   . THR B 2 191 ? 8.408   -10.239 51.126  1.00 30.30  ? 191 THR B C   1 
ATOM   5163  O  O   . THR B 2 191 ? 8.809   -9.068  51.201  1.00 32.73  ? 191 THR B O   1 
ATOM   5164  C  CB  . THR B 2 191 ? 6.292   -11.138 52.095  1.00 33.36  ? 191 THR B CB  1 
ATOM   5165  O  OG1 . THR B 2 191 ? 5.674   -9.864  51.813  1.00 32.05  ? 191 THR B OG1 1 
ATOM   5166  C  CG2 . THR B 2 191 ? 5.565   -11.845 53.254  1.00 32.61  ? 191 THR B CG2 1 
ATOM   5167  N  N   . GLY B 2 192 ? 8.424   -10.943 49.983  1.00 30.17  ? 192 GLY B N   1 
ATOM   5168  C  CA  . GLY B 2 192 ? 8.927   -10.337 48.767  1.00 31.72  ? 192 GLY B CA  1 
ATOM   5169  C  C   . GLY B 2 192 ? 8.094   -9.137  48.357  1.00 29.68  ? 192 GLY B C   1 
ATOM   5170  O  O   . GLY B 2 192 ? 8.630   -8.154  47.866  1.00 30.65  ? 192 GLY B O   1 
ATOM   5171  N  N   . VAL B 2 193 ? 6.770   -9.227  48.515  1.00 29.83  ? 193 VAL B N   1 
ATOM   5172  C  CA  . VAL B 2 193 ? 5.890   -8.107  48.186  1.00 29.51  ? 193 VAL B CA  1 
ATOM   5173  C  C   . VAL B 2 193 ? 6.176   -6.916  49.098  1.00 31.21  ? 193 VAL B C   1 
ATOM   5174  O  O   . VAL B 2 193 ? 6.316   -5.779  48.633  1.00 30.33  ? 193 VAL B O   1 
ATOM   5175  C  CB  . VAL B 2 193 ? 4.413   -8.530  48.269  1.00 35.86  ? 193 VAL B CB  1 
ATOM   5176  C  CG1 . VAL B 2 193 ? 3.517   -7.302  48.317  1.00 33.68  ? 193 VAL B CG1 1 
ATOM   5177  C  CG2 . VAL B 2 193 ? 4.028   -9.415  47.044  1.00 33.41  ? 193 VAL B CG2 1 
ATOM   5178  N  N   . GLU B 2 194 ? 6.286   -7.160  50.411  1.00 31.03  ? 194 GLU B N   1 
ATOM   5179  C  CA  . GLU B 2 194 ? 6.578   -6.058  51.329  1.00 30.27  ? 194 GLU B CA  1 
ATOM   5180  C  C   . GLU B 2 194 ? 7.930   -5.419  51.030  1.00 32.51  ? 194 GLU B C   1 
ATOM   5181  O  O   . GLU B 2 194 ? 8.068   -4.181  51.077  1.00 31.27  ? 194 GLU B O   1 
ATOM   5182  C  CB  . GLU B 2 194 ? 6.537   -6.561  52.771  1.00 27.60  ? 194 GLU B CB  1 
ATOM   5183  C  CG  . GLU B 2 194 ? 5.141   -6.905  53.236  1.00 31.98  ? 194 GLU B CG  1 
ATOM   5184  C  CD  . GLU B 2 194 ? 5.106   -7.678  54.552  1.00 37.69  ? 194 GLU B CD  1 
ATOM   5185  O  OE1 . GLU B 2 194 ? 6.076   -8.384  54.872  1.00 35.04  ? 194 GLU B OE1 1 
ATOM   5186  O  OE2 . GLU B 2 194 ? 4.046   -7.662  55.192  1.00 37.24  ? 194 GLU B OE2 1 
ATOM   5187  N  N   . ALA B 2 195 ? 8.959   -6.242  50.768  1.00 31.76  ? 195 ALA B N   1 
ATOM   5188  C  CA  . ALA B 2 195 ? 10.260  -5.708  50.390  1.00 30.78  ? 195 ALA B CA  1 
ATOM   5189  C  C   . ALA B 2 195 ? 10.178  -4.825  49.153  1.00 31.30  ? 195 ALA B C   1 
ATOM   5190  O  O   . ALA B 2 195 ? 10.855  -3.777  49.079  1.00 28.35  ? 195 ALA B O   1 
ATOM   5191  C  CB  . ALA B 2 195 ? 11.237  -6.841  50.132  1.00 29.91  ? 195 ALA B CB  1 
ATOM   5192  N  N   . LEU B 2 196 ? 9.355   -5.240  48.178  1.00 28.28  ? 196 LEU B N   1 
ATOM   5193  C  CA  . LEU B 2 196 ? 9.195   -4.514  46.919  1.00 29.20  ? 196 LEU B CA  1 
ATOM   5194  C  C   . LEU B 2 196 ? 8.465   -3.194  47.135  1.00 30.41  ? 196 LEU B C   1 
ATOM   5195  O  O   . LEU B 2 196 ? 8.748   -2.225  46.449  1.00 27.63  ? 196 LEU B O   1 
ATOM   5196  C  CB  . LEU B 2 196 ? 8.454   -5.388  45.914  1.00 31.63  ? 196 LEU B CB  1 
ATOM   5197  C  CG  . LEU B 2 196 ? 8.285   -4.880  44.479  1.00 33.17  ? 196 LEU B CG  1 
ATOM   5198  C  CD1 . LEU B 2 196 ? 9.626   -4.539  43.861  1.00 32.14  ? 196 LEU B CD1 1 
ATOM   5199  C  CD2 . LEU B 2 196 ? 7.597   -5.966  43.585  1.00 33.35  ? 196 LEU B CD2 1 
ATOM   5200  N  N   . TYR B 2 197 ? 7.476   -3.162  48.022  1.00 28.18  ? 197 TYR B N   1 
ATOM   5201  C  CA  . TYR B 2 197 ? 6.815   -1.891  48.311  1.00 31.05  ? 197 TYR B CA  1 
ATOM   5202  C  C   . TYR B 2 197 ? 7.828   -0.899  48.853  1.00 30.92  ? 197 TYR B C   1 
ATOM   5203  O  O   . TYR B 2 197 ? 7.916   0.249   48.383  1.00 29.40  ? 197 TYR B O   1 
ATOM   5204  C  CB  . TYR B 2 197 ? 5.674   -2.092  49.299  1.00 30.62  ? 197 TYR B CB  1 
ATOM   5205  C  CG  . TYR B 2 197 ? 4.351   -2.525  48.686  1.00 30.21  ? 197 TYR B CG  1 
ATOM   5206  C  CD1 . TYR B 2 197 ? 3.641   -1.682  47.835  1.00 36.17  ? 197 TYR B CD1 1 
ATOM   5207  C  CD2 . TYR B 2 197 ? 3.769   -3.747  49.029  1.00 34.28  ? 197 TYR B CD2 1 
ATOM   5208  C  CE1 . TYR B 2 197 ? 2.403   -2.058  47.321  1.00 38.40  ? 197 TYR B CE1 1 
ATOM   5209  C  CE2 . TYR B 2 197 ? 2.521   -4.124  48.519  1.00 36.98  ? 197 TYR B CE2 1 
ATOM   5210  C  CZ  . TYR B 2 197 ? 1.852   -3.288  47.672  1.00 38.91  ? 197 TYR B CZ  1 
ATOM   5211  O  OH  . TYR B 2 197 ? 0.625   -3.665  47.159  1.00 45.80  ? 197 TYR B OH  1 
ATOM   5212  N  N   . ALA B 2 198 ? 8.684   -1.370  49.757  1.00 31.16  ? 198 ALA B N   1 
ATOM   5213  C  CA  . ALA B 2 198 ? 9.737   -0.539  50.349  1.00 28.16  ? 198 ALA B CA  1 
ATOM   5214  C  C   . ALA B 2 198 ? 10.761  -0.081  49.316  1.00 30.69  ? 198 ALA B C   1 
ATOM   5215  O  O   . ALA B 2 198 ? 11.083  1.119   49.228  1.00 30.89  ? 198 ALA B O   1 
ATOM   5216  C  CB  . ALA B 2 198 ? 10.441  -1.323  51.459  1.00 28.27  ? 198 ALA B CB  1 
ATOM   5217  N  N   . SER B 2 199 ? 11.320  -1.025  48.538  1.00 26.69  ? 199 SER B N   1 
ATOM   5218  C  CA  . SER B 2 199 ? 12.403  -0.690  47.596  1.00 26.76  ? 199 SER B CA  1 
ATOM   5219  C  C   . SER B 2 199 ? 11.911  0.148   46.407  1.00 25.57  ? 199 SER B C   1 
ATOM   5220  O  O   . SER B 2 199 ? 12.661  1.003   45.890  1.00 26.76  ? 199 SER B O   1 
ATOM   5221  C  CB  . SER B 2 199 ? 13.084  -1.989  47.088  1.00 29.17  ? 199 SER B CB  1 
ATOM   5222  O  OG  . SER B 2 199 ? 12.161  -2.756  46.313  1.00 30.30  ? 199 SER B OG  1 
ATOM   5223  N  N   . LEU B 2 200 ? 10.678  -0.078  45.944  1.00 26.44  ? 200 LEU B N   1 
ATOM   5224  C  CA  . LEU B 2 200 ? 10.132  0.706   44.834  1.00 27.32  ? 200 LEU B CA  1 
ATOM   5225  C  C   . LEU B 2 200 ? 9.790   2.131   45.253  1.00 27.33  ? 200 LEU B C   1 
ATOM   5226  O  O   . LEU B 2 200 ? 10.065  3.094   44.512  1.00 27.70  ? 200 LEU B O   1 
ATOM   5227  C  CB  . LEU B 2 200 ? 8.866   0.040   44.290  1.00 32.47  ? 200 LEU B CB  1 
ATOM   5228  C  CG  . LEU B 2 200 ? 8.832   -0.525  42.884  1.00 35.23  ? 200 LEU B CG  1 
ATOM   5229  C  CD1 . LEU B 2 200 ? 7.367   -0.655  42.481  1.00 36.61  ? 200 LEU B CD1 1 
ATOM   5230  C  CD2 . LEU B 2 200 ? 9.659   0.214   41.817  1.00 29.72  ? 200 LEU B CD2 1 
ATOM   5231  N  N   . THR B 2 201 ? 9.143   2.290   46.421  1.00 26.03  ? 201 THR B N   1 
ATOM   5232  C  CA  . THR B 2 201 ? 8.784   3.649   46.854  1.00 27.90  ? 201 THR B CA  1 
ATOM   5233  C  C   . THR B 2 201 ? 10.017  4.473   47.224  1.00 26.33  ? 201 THR B C   1 
ATOM   5234  O  O   . THR B 2 201 ? 9.976   5.711   47.160  1.00 25.89  ? 201 THR B O   1 
ATOM   5235  C  CB  . THR B 2 201 ? 7.791   3.629   48.032  1.00 29.57  ? 201 THR B CB  1 
ATOM   5236  O  OG1 . THR B 2 201 ? 8.284   2.855   49.151  1.00 25.29  ? 201 THR B OG1 1 
ATOM   5237  C  CG2 . THR B 2 201 ? 6.417   3.040   47.590  1.00 28.74  ? 201 THR B CG2 1 
ATOM   5238  N  N   . ALA B 2 202 ? 11.119  3.827   47.614  1.00 25.97  ? 202 ALA B N   1 
ATOM   5239  C  CA  . ALA B 2 202 ? 12.362  4.555   47.792  1.00 24.97  ? 202 ALA B CA  1 
ATOM   5240  C  C   . ALA B 2 202 ? 12.679  5.435   46.583  1.00 27.94  ? 202 ALA B C   1 
ATOM   5241  O  O   . ALA B 2 202 ? 13.401  6.429   46.738  1.00 27.73  ? 202 ALA B O   1 
ATOM   5242  C  CB  . ALA B 2 202 ? 13.526  3.597   48.011  1.00 28.68  ? 202 ALA B CB  1 
ATOM   5243  N  N   . GLN B 2 203 ? 12.142  5.102   45.397  1.00 23.52  ? 203 GLN B N   1 
ATOM   5244  C  CA  . GLN B 2 203 ? 12.508  5.732   44.133  1.00 25.39  ? 203 GLN B CA  1 
ATOM   5245  C  C   . GLN B 2 203 ? 11.562  6.870   43.751  1.00 23.92  ? 203 GLN B C   1 
ATOM   5246  O  O   . GLN B 2 203 ? 11.774  7.521   42.716  1.00 26.00  ? 203 GLN B O   1 
ATOM   5247  C  CB  . GLN B 2 203 ? 12.545  4.666   43.033  1.00 23.73  ? 203 GLN B CB  1 
ATOM   5248  C  CG  . GLN B 2 203 ? 13.453  3.473   43.454  1.00 21.90  ? 203 GLN B CG  1 
ATOM   5249  C  CD  . GLN B 2 203 ? 13.626  2.463   42.355  1.00 24.58  ? 203 GLN B CD  1 
ATOM   5250  O  OE1 . GLN B 2 203 ? 13.865  2.814   41.195  1.00 26.64  ? 203 GLN B OE1 1 
ATOM   5251  N  NE2 . GLN B 2 203 ? 13.619  1.181   42.738  1.00 26.55  ? 203 GLN B NE2 1 
ATOM   5252  N  N   . PHE B 2 204 ? 10.567  7.163   44.589  1.00 24.31  ? 204 PHE B N   1 
ATOM   5253  C  CA  . PHE B 2 204 ? 9.775   8.357   44.310  1.00 25.96  ? 204 PHE B CA  1 
ATOM   5254  C  C   . PHE B 2 204 ? 9.174   8.985   45.561  1.00 24.80  ? 204 PHE B C   1 
ATOM   5255  O  O   . PHE B 2 204 ? 8.202   9.738   45.450  1.00 27.65  ? 204 PHE B O   1 
ATOM   5256  C  CB  . PHE B 2 204 ? 8.633   8.034   43.290  1.00 27.11  ? 204 PHE B CB  1 
ATOM   5257  C  CG  . PHE B 2 204 ? 7.816   6.801   43.643  1.00 29.19  ? 204 PHE B CG  1 
ATOM   5258  C  CD1 . PHE B 2 204 ? 6.871   6.837   44.659  1.00 26.60  ? 204 PHE B CD1 1 
ATOM   5259  C  CD2 . PHE B 2 204 ? 7.980   5.615   42.910  1.00 29.21  ? 204 PHE B CD2 1 
ATOM   5260  C  CE1 . PHE B 2 204 ? 6.093   5.693   44.962  1.00 31.16  ? 204 PHE B CE1 1 
ATOM   5261  C  CE2 . PHE B 2 204 ? 7.226   4.451   43.226  1.00 33.08  ? 204 PHE B CE2 1 
ATOM   5262  C  CZ  . PHE B 2 204 ? 6.291   4.509   44.242  1.00 30.79  ? 204 PHE B CZ  1 
ATOM   5263  N  N   . ILE B 2 205 ? 9.718   8.706   46.749  1.00 23.91  ? 205 ILE B N   1 
ATOM   5264  C  CA  . ILE B 2 205 ? 9.337   9.365   48.006  1.00 22.62  ? 205 ILE B CA  1 
ATOM   5265  C  C   . ILE B 2 205 ? 10.560  10.114  48.517  1.00 26.30  ? 205 ILE B C   1 
ATOM   5266  O  O   . ILE B 2 205 ? 11.701  9.728   48.244  1.00 28.32  ? 205 ILE B O   1 
ATOM   5267  C  CB  . ILE B 2 205 ? 8.822   8.291   49.010  1.00 24.81  ? 205 ILE B CB  1 
ATOM   5268  C  CG1 . ILE B 2 205 ? 7.602   7.539   48.420  1.00 27.58  ? 205 ILE B CG1 1 
ATOM   5269  C  CG2 . ILE B 2 205 ? 8.596   8.833   50.420  1.00 27.24  ? 205 ILE B CG2 1 
ATOM   5270  C  CD1 . ILE B 2 205 ? 6.362   8.432   48.056  1.00 29.23  ? 205 ILE B CD1 1 
ATOM   5271  N  N   . ASP B 2 206 ? 10.334  11.258  49.179  1.00 29.36  ? 206 ASP B N   1 
ATOM   5272  C  CA  . ASP B 2 206 ? 11.441  11.985  49.791  1.00 30.34  ? 206 ASP B CA  1 
ATOM   5273  C  C   . ASP B 2 206 ? 12.297  11.065  50.661  1.00 31.56  ? 206 ASP B C   1 
ATOM   5274  O  O   . ASP B 2 206 ? 11.793  10.436  51.590  1.00 30.98  ? 206 ASP B O   1 
ATOM   5275  C  CB  . ASP B 2 206 ? 10.884  13.147  50.636  1.00 31.12  ? 206 ASP B CB  1 
ATOM   5276  C  CG  . ASP B 2 206 ? 11.976  14.147  51.044  1.00 39.73  ? 206 ASP B CG  1 
ATOM   5277  O  OD1 . ASP B 2 206 ? 12.852  13.696  51.831  1.00 38.84  ? 206 ASP B OD1 1 
ATOM   5278  O  OD2 . ASP B 2 206 ? 11.953  15.349  50.643  1.00 38.04  ? 206 ASP B OD2 1 
ATOM   5279  N  N   . LYS B 2 207 ? 13.597  10.957  50.353  1.00 31.28  ? 207 LYS B N   1 
ATOM   5280  C  CA  . LYS B 2 207 ? 14.408  9.948   51.036  1.00 31.74  ? 207 LYS B CA  1 
ATOM   5281  C  C   . LYS B 2 207 ? 14.414  10.145  52.557  1.00 30.50  ? 207 LYS B C   1 
ATOM   5282  O  O   . LYS B 2 207 ? 14.507  9.167   53.294  1.00 30.30  ? 207 LYS B O   1 
ATOM   5283  C  CB  . LYS B 2 207 ? 15.835  9.959   50.483  1.00 38.97  ? 207 LYS B CB  1 
ATOM   5284  C  CG  . LYS B 2 207 ? 15.981  9.447   49.073  1.00 43.87  ? 207 LYS B CG  1 
ATOM   5285  C  CD  . LYS B 2 207 ? 16.233  7.983   49.031  1.00 37.08  ? 207 LYS B CD  1 
ATOM   5286  C  CE  . LYS B 2 207 ? 16.455  7.491   47.575  1.00 40.36  ? 207 LYS B CE  1 
ATOM   5287  N  NZ  . LYS B 2 207 ? 15.790  8.333   46.520  1.00 41.47  ? 207 LYS B NZ  1 
ATOM   5288  N  N   A ARG B 2 208 ? 14.352  11.396  53.037  0.52 30.59  ? 208 ARG B N   1 
ATOM   5289  N  N   B ARG B 2 208 ? 14.349  11.393  53.033  0.48 30.60  ? 208 ARG B N   1 
ATOM   5290  C  CA  A ARG B 2 208 ? 14.295  11.631  54.480  0.52 33.20  ? 208 ARG B CA  1 
ATOM   5291  C  CA  B ARG B 2 208 ? 14.282  11.639  54.473  0.48 33.20  ? 208 ARG B CA  1 
ATOM   5292  C  C   A ARG B 2 208 ? 13.037  11.013  55.078  0.52 32.96  ? 208 ARG B C   1 
ATOM   5293  C  C   B ARG B 2 208 ? 13.039  10.997  55.066  0.48 32.96  ? 208 ARG B C   1 
ATOM   5294  O  O   A ARG B 2 208 ? 13.087  10.387  56.148  0.52 33.34  ? 208 ARG B O   1 
ATOM   5295  O  O   B ARG B 2 208 ? 13.093  10.352  56.125  0.48 33.35  ? 208 ARG B O   1 
ATOM   5296  C  CB  A ARG B 2 208 ? 14.336  13.136  54.766  0.52 35.49  ? 208 ARG B CB  1 
ATOM   5297  C  CB  B ARG B 2 208 ? 14.258  13.143  54.725  0.48 35.48  ? 208 ARG B CB  1 
ATOM   5298  C  CG  A ARG B 2 208 ? 15.675  13.775  54.372  0.52 37.89  ? 208 ARG B CG  1 
ATOM   5299  C  CG  B ARG B 2 208 ? 15.579  13.812  54.426  0.48 37.90  ? 208 ARG B CG  1 
ATOM   5300  C  CD  A ARG B 2 208 ? 15.656  15.305  54.550  0.52 39.14  ? 208 ARG B CD  1 
ATOM   5301  C  CD  B ARG B 2 208 ? 15.503  15.306  54.718  0.48 39.00  ? 208 ARG B CD  1 
ATOM   5302  N  NE  A ARG B 2 208 ? 16.956  15.913  54.274  0.52 41.05  ? 208 ARG B NE  1 
ATOM   5303  N  NE  B ARG B 2 208 ? 15.023  16.038  53.546  0.48 40.35  ? 208 ARG B NE  1 
ATOM   5304  C  CZ  A ARG B 2 208 ? 18.036  15.818  55.040  0.52 39.07  ? 208 ARG B CZ  1 
ATOM   5305  C  CZ  B ARG B 2 208 ? 13.745  16.267  53.264  0.48 39.24  ? 208 ARG B CZ  1 
ATOM   5306  N  NH1 A ARG B 2 208 ? 18.012  15.186  56.197  0.52 42.72  ? 208 ARG B NH1 1 
ATOM   5307  N  NH1 B ARG B 2 208 ? 12.770  15.743  53.989  0.48 39.38  ? 208 ARG B NH1 1 
ATOM   5308  N  NH2 A ARG B 2 208 ? 19.165  16.406  54.645  0.52 41.51  ? 208 ARG B NH2 1 
ATOM   5309  N  NH2 B ARG B 2 208 ? 13.436  17.093  52.267  0.48 39.50  ? 208 ARG B NH2 1 
ATOM   5310  N  N   . GLU B 2 209 ? 11.897  11.193  54.405  1.00 29.22  ? 209 GLU B N   1 
ATOM   5311  C  CA  . GLU B 2 209 ? 10.653  10.607  54.887  1.00 31.22  ? 209 GLU B CA  1 
ATOM   5312  C  C   . GLU B 2 209 ? 10.675  9.097   54.756  1.00 29.99  ? 209 GLU B C   1 
ATOM   5313  O  O   . GLU B 2 209 ? 10.253  8.387   55.680  1.00 30.69  ? 209 GLU B O   1 
ATOM   5314  C  CB  . GLU B 2 209 ? 9.475   11.186  54.125  1.00 32.29  ? 209 GLU B CB  1 
ATOM   5315  C  CG  . GLU B 2 209 ? 9.051   12.617  54.538  1.00 37.36  ? 209 GLU B CG  1 
ATOM   5316  C  CD  . GLU B 2 209 ? 8.399   13.430  53.407  1.00 43.58  ? 209 GLU B CD  1 
ATOM   5317  O  OE1 . GLU B 2 209 ? 7.408   12.959  52.806  1.00 38.10  ? 209 GLU B OE1 1 
ATOM   5318  O  OE2 . GLU B 2 209 ? 8.764   14.632  53.258  1.00 49.04  ? 209 GLU B OE2 1 
ATOM   5319  N  N   . HIS B 2 210 ? 11.186  8.599   53.633  1.00 26.51  ? 210 HIS B N   1 
ATOM   5320  C  CA  . HIS B 2 210 ? 11.290  7.143   53.426  1.00 25.52  ? 210 HIS B CA  1 
ATOM   5321  C  C   . HIS B 2 210 ? 12.226  6.492   54.468  1.00 30.80  ? 210 HIS B C   1 
ATOM   5322  O  O   . HIS B 2 210 ? 11.912  5.434   55.042  1.00 28.96  ? 210 HIS B O   1 
ATOM   5323  C  CB  . HIS B 2 210 ? 11.771  6.884   51.980  1.00 25.14  ? 210 HIS B CB  1 
ATOM   5324  C  CG  . HIS B 2 210 ? 11.507  5.493   51.484  1.00 28.47  ? 210 HIS B CG  1 
ATOM   5325  N  ND1 . HIS B 2 210 ? 12.405  4.460   51.664  1.00 29.12  ? 210 HIS B ND1 1 
ATOM   5326  C  CD2 . HIS B 2 210 ? 10.453  4.972   50.799  1.00 26.37  ? 210 HIS B CD2 1 
ATOM   5327  C  CE1 . HIS B 2 210 ? 11.909  3.360   51.130  1.00 30.59  ? 210 HIS B CE1 1 
ATOM   5328  N  NE2 . HIS B 2 210 ? 10.733  3.645   50.593  1.00 28.36  ? 210 HIS B NE2 1 
ATOM   5329  N  N   . ASN B 2 211 ? 13.367  7.132   54.766  1.00 28.20  ? 211 ASN B N   1 
ATOM   5330  C  CA  . ASN B 2 211 ? 14.271  6.591   55.782  1.00 29.84  ? 211 ASN B CA  1 
ATOM   5331  C  C   . ASN B 2 211 ? 13.581  6.492   57.136  1.00 32.98  ? 211 ASN B C   1 
ATOM   5332  O  O   . ASN B 2 211 ? 13.854  5.577   57.931  1.00 30.16  ? 211 ASN B O   1 
ATOM   5333  C  CB  . ASN B 2 211 ? 15.491  7.497   55.925  1.00 30.18  ? 211 ASN B CB  1 
ATOM   5334  C  CG  . ASN B 2 211 ? 16.469  7.351   54.763  1.00 31.45  ? 211 ASN B CG  1 
ATOM   5335  O  OD1 . ASN B 2 211 ? 16.352  6.442   53.948  1.00 30.02  ? 211 ASN B OD1 1 
ATOM   5336  N  ND2 . ASN B 2 211 ? 17.358  8.335   54.622  1.00 30.87  ? 211 ASN B ND2 1 
ATOM   5337  N  N   . GLU B 2 212 ? 12.764  7.490   57.461  1.00 32.09  ? 212 GLU B N   1 
ATOM   5338  C  CA  . GLU B 2 212 ? 12.085  7.464   58.744  1.00 28.87  ? 212 GLU B CA  1 
ATOM   5339  C  C   . GLU B 2 212 ? 11.125  6.287   58.800  1.00 30.79  ? 212 GLU B C   1 
ATOM   5340  O  O   . GLU B 2 212 ? 10.996  5.606   59.850  1.00 30.82  ? 212 GLU B O   1 
ATOM   5341  C  CB  . GLU B 2 212 ? 11.417  8.825   58.937  1.00 35.42  ? 212 GLU B CB  1 
ATOM   5342  C  CG  . GLU B 2 212 ? 10.635  8.952   60.163  1.00 37.01  ? 212 GLU B CG  1 
ATOM   5343  C  CD  . GLU B 2 212 ? 11.514  9.223   61.347  1.00 43.10  ? 212 GLU B CD  1 
ATOM   5344  O  OE1 . GLU B 2 212 ? 12.712  9.524   61.133  1.00 48.54  ? 212 GLU B OE1 1 
ATOM   5345  O  OE2 . GLU B 2 212 ? 11.004  9.111   62.467  1.00 47.19  ? 212 GLU B OE2 1 
ATOM   5346  N  N   A MET B 2 213 ? 10.465  5.996   57.672  0.47 32.30  ? 213 MET B N   1 
ATOM   5347  N  N   B MET B 2 213 ? 10.451  6.009   57.677  0.53 32.30  ? 213 MET B N   1 
ATOM   5348  C  CA  A MET B 2 213 ? 9.541   4.872   57.625  0.47 33.63  ? 213 MET B CA  1 
ATOM   5349  C  CA  B MET B 2 213 ? 9.551   4.865   57.629  0.53 33.64  ? 213 MET B CA  1 
ATOM   5350  C  C   A MET B 2 213 ? 10.270  3.528   57.631  0.47 32.39  ? 213 MET B C   1 
ATOM   5351  C  C   B MET B 2 213 ? 10.302  3.539   57.681  0.53 32.40  ? 213 MET B C   1 
ATOM   5352  O  O   A MET B 2 213 ? 9.762   2.552   58.214  0.47 32.98  ? 213 MET B O   1 
ATOM   5353  O  O   B MET B 2 213 ? 9.833   2.580   58.320  0.53 32.96  ? 213 MET B O   1 
ATOM   5354  C  CB  A MET B 2 213 ? 8.635   5.002   56.407  0.47 34.60  ? 213 MET B CB  1 
ATOM   5355  C  CB  B MET B 2 213 ? 8.668   4.927   56.389  0.53 34.62  ? 213 MET B CB  1 
ATOM   5356  C  CG  A MET B 2 213 ? 7.516   3.990   56.383  0.47 33.71  ? 213 MET B CG  1 
ATOM   5357  C  CG  B MET B 2 213 ? 7.678   3.776   56.350  0.53 33.56  ? 213 MET B CG  1 
ATOM   5358  S  SD  A MET B 2 213 ? 6.486   4.128   57.854  0.47 40.29  ? 213 MET B SD  1 
ATOM   5359  S  SD  B MET B 2 213 ? 6.536   3.732   57.720  0.53 41.24  ? 213 MET B SD  1 
ATOM   5360  C  CE  A MET B 2 213 ? 6.192   2.358   58.115  0.47 37.64  ? 213 MET B CE  1 
ATOM   5361  C  CE  B MET B 2 213 ? 6.282   5.489   57.970  0.53 31.37  ? 213 MET B CE  1 
ATOM   5362  N  N   . LEU B 2 214 ? 11.454  3.449   57.007  1.00 29.94  ? 214 LEU B N   1 
ATOM   5363  C  CA  . LEU B 2 214 ? 12.270  2.237   57.125  1.00 28.25  ? 214 LEU B CA  1 
ATOM   5364  C  C   . LEU B 2 214 ? 12.744  2.025   58.559  1.00 29.34  ? 214 LEU B C   1 
ATOM   5365  O  O   . LEU B 2 214 ? 12.765  0.892   59.064  1.00 28.04  ? 214 LEU B O   1 
ATOM   5366  C  CB  . LEU B 2 214 ? 13.474  2.285   56.199  1.00 29.45  ? 214 LEU B CB  1 
ATOM   5367  C  CG  . LEU B 2 214 ? 13.141  2.177   54.684  1.00 30.02  ? 214 LEU B CG  1 
ATOM   5368  C  CD1 . LEU B 2 214 ? 14.345  2.541   53.817  1.00 27.00  ? 214 LEU B CD1 1 
ATOM   5369  C  CD2 . LEU B 2 214 ? 12.705  0.744   54.347  1.00 30.36  ? 214 LEU B CD2 1 
ATOM   5370  N  N   . LYS B 2 215 ? 13.095  3.109   59.255  1.00 31.23  ? 215 LYS B N   1 
ATOM   5371  C  CA  . LYS B 2 215 ? 13.551  2.966   60.626  1.00 30.71  ? 215 LYS B CA  1 
ATOM   5372  C  C   . LYS B 2 215 ? 12.420  2.481   61.518  1.00 30.19  ? 215 LYS B C   1 
ATOM   5373  O  O   . LYS B 2 215 ? 12.624  1.608   62.368  1.00 31.47  ? 215 LYS B O   1 
ATOM   5374  C  CB  . LYS B 2 215 ? 14.132  4.307   61.127  1.00 29.04  ? 215 LYS B CB  1 
ATOM   5375  C  CG  . LYS B 2 215 ? 15.550  4.531   60.545  1.00 36.38  ? 215 LYS B CG  1 
ATOM   5376  C  CD  . LYS B 2 215 ? 16.275  5.699   61.201  1.00 34.99  ? 215 LYS B CD  1 
ATOM   5377  C  CE  . LYS B 2 215 ? 16.285  6.937   60.340  1.00 40.51  ? 215 LYS B CE  1 
ATOM   5378  N  NZ  . LYS B 2 215 ? 17.376  7.895   60.752  1.00 48.45  ? 215 LYS B NZ  1 
ATOM   5379  N  N   . LYS B 2 216 ? 11.208  3.006   61.316  1.00 30.00  ? 216 LYS B N   1 
ATOM   5380  C  CA  . LYS B 2 216 ? 10.067  2.517   62.075  1.00 30.67  ? 216 LYS B CA  1 
ATOM   5381  C  C   . LYS B 2 216 ? 9.848   1.024   61.816  1.00 33.63  ? 216 LYS B C   1 
ATOM   5382  O  O   . LYS B 2 216 ? 9.642   0.241   62.753  1.00 32.74  ? 216 LYS B O   1 
ATOM   5383  C  CB  . LYS B 2 216 ? 8.814   3.306   61.690  1.00 34.63  ? 216 LYS B CB  1 
ATOM   5384  C  CG  . LYS B 2 216 ? 7.523   2.506   61.906  1.00 37.93  ? 216 LYS B CG  1 
ATOM   5385  C  CD  . LYS B 2 216 ? 6.267   3.343   61.786  1.00 41.33  ? 216 LYS B CD  1 
ATOM   5386  C  CE  . LYS B 2 216 ? 5.047   2.437   61.877  1.00 42.32  ? 216 LYS B CE  1 
ATOM   5387  N  NZ  . LYS B 2 216 ? 3.803   3.188   62.205  1.00 43.97  ? 216 LYS B NZ  1 
ATOM   5388  N  N   . THR B 2 217 ? 9.835   0.641   60.536  1.00 31.11  ? 217 THR B N   1 
ATOM   5389  C  CA  . THR B 2 217 ? 9.659   -0.744  60.099  1.00 31.34  ? 217 THR B CA  1 
ATOM   5390  C  C   . THR B 2 217 ? 10.672  -1.681  60.734  1.00 31.13  ? 217 THR B C   1 
ATOM   5391  O  O   . THR B 2 217 ? 10.300  -2.700  61.332  1.00 34.01  ? 217 THR B O   1 
ATOM   5392  C  CB  . THR B 2 217 ? 9.776   -0.821  58.584  1.00 34.50  ? 217 THR B CB  1 
ATOM   5393  O  OG1 . THR B 2 217 ? 8.816   0.059   57.983  1.00 33.92  ? 217 THR B OG1 1 
ATOM   5394  C  CG2 . THR B 2 217 ? 9.647   -2.297  58.113  1.00 32.53  ? 217 THR B CG2 1 
ATOM   5395  N  N   . LEU B 2 218 ? 11.956  -1.320  60.687  1.00 31.49  ? 218 LEU B N   1 
ATOM   5396  C  CA  . LEU B 2 218 ? 12.982  -2.186  61.277  1.00 29.30  ? 218 LEU B CA  1 
ATOM   5397  C  C   . LEU B 2 218 ? 12.886  -2.269  62.796  1.00 36.13  ? 218 LEU B C   1 
ATOM   5398  O  O   . LEU B 2 218 ? 13.239  -3.290  63.378  1.00 38.11  ? 218 LEU B O   1 
ATOM   5399  C  CB  . LEU B 2 218 ? 14.345  -1.664  60.877  1.00 33.60  ? 218 LEU B CB  1 
ATOM   5400  C  CG  . LEU B 2 218 ? 14.591  -1.755  59.381  1.00 31.37  ? 218 LEU B CG  1 
ATOM   5401  C  CD1 . LEU B 2 218 ? 15.912  -1.009  59.084  1.00 32.87  ? 218 LEU B CD1 1 
ATOM   5402  C  CD2 . LEU B 2 218 ? 14.686  -3.226  58.899  1.00 23.99  ? 218 LEU B CD2 1 
ATOM   5403  N  N   . ALA B 2 219 ? 12.460  -1.193  63.454  1.00 33.14  ? 219 ALA B N   1 
ATOM   5404  C  CA  . ALA B 2 219 ? 12.202  -1.230  64.882  1.00 37.32  ? 219 ALA B CA  1 
ATOM   5405  C  C   . ALA B 2 219 ? 11.104  -2.235  65.243  1.00 36.00  ? 219 ALA B C   1 
ATOM   5406  O  O   . ALA B 2 219 ? 11.117  -2.791  66.348  1.00 36.03  ? 219 ALA B O   1 
ATOM   5407  C  CB  . ALA B 2 219 ? 11.843  0.178   65.368  1.00 33.05  ? 219 ALA B CB  1 
ATOM   5408  N  N   . ALA B 2 220 ? 10.172  -2.499  64.322  1.00 34.73  ? 220 ALA B N   1 
ATOM   5409  C  CA  . ALA B 2 220 ? 9.077   -3.429  64.602  1.00 41.81  ? 220 ALA B CA  1 
ATOM   5410  C  C   . ALA B 2 220 ? 9.448   -4.886  64.320  1.00 39.24  ? 220 ALA B C   1 
ATOM   5411  O  O   . ALA B 2 220 ? 8.906   -5.807  64.964  1.00 39.27  ? 220 ALA B O   1 
ATOM   5412  C  CB  . ALA B 2 220 ? 7.848   -3.066  63.752  1.00 36.59  ? 220 ALA B CB  1 
ATOM   5413  N  N   . LEU B 2 221 ? 10.354  -5.096  63.367  1.00 35.72  ? 221 LEU B N   1 
ATOM   5414  C  CA  . LEU B 2 221 ? 10.588  -6.439  62.832  1.00 33.72  ? 221 LEU B CA  1 
ATOM   5415  C  C   . LEU B 2 221 ? 11.007  -7.435  63.894  1.00 41.84  ? 221 LEU B C   1 
ATOM   5416  O  O   . LEU B 2 221 ? 10.525  -8.579  63.836  1.00 42.19  ? 221 LEU B O   1 
ATOM   5417  C  CB  . LEU B 2 221 ? 11.669  -6.387  61.742  1.00 32.89  ? 221 LEU B CB  1 
ATOM   5418  C  CG  . LEU B 2 221 ? 11.145  -5.740  60.473  1.00 37.14  ? 221 LEU B CG  1 
ATOM   5419  C  CD1 . LEU B 2 221 ? 12.237  -5.600  59.375  1.00 28.27  ? 221 LEU B CD1 1 
ATOM   5420  C  CD2 . LEU B 2 221 ? 9.839   -6.434  60.050  1.00 36.12  ? 221 LEU B CD2 1 
ATOM   5421  N  N   . PRO B 2 222 ? 11.894  -7.106  64.844  1.00 41.23  ? 222 PRO B N   1 
ATOM   5422  C  CA  . PRO B 2 222 ? 12.294  -8.110  65.844  1.00 43.69  ? 222 PRO B CA  1 
ATOM   5423  C  C   . PRO B 2 222 ? 11.117  -8.772  66.542  1.00 47.07  ? 222 PRO B C   1 
ATOM   5424  O  O   . PRO B 2 222 ? 11.200  -9.956  66.905  1.00 48.50  ? 222 PRO B O   1 
ATOM   5425  C  CB  . PRO B 2 222 ? 13.129  -7.287  66.834  1.00 44.82  ? 222 PRO B CB  1 
ATOM   5426  C  CG  . PRO B 2 222 ? 13.768  -6.265  65.939  1.00 42.76  ? 222 PRO B CG  1 
ATOM   5427  C  CD  . PRO B 2 222 ? 12.658  -5.854  65.016  1.00 40.21  ? 222 PRO B CD  1 
ATOM   5428  N  N   . ASN B 2 223 ? 10.003  -8.066  66.718  1.00 39.70  ? 223 ASN B N   1 
ATOM   5429  C  CA  . ASN B 2 223 ? 8.894   -8.618  67.486  1.00 46.84  ? 223 ASN B CA  1 
ATOM   5430  C  C   . ASN B 2 223 ? 7.660   -8.936  66.654  1.00 45.73  ? 223 ASN B C   1 
ATOM   5431  O  O   . ASN B 2 223 ? 6.606   -9.261  67.215  1.00 41.72  ? 223 ASN B O   1 
ATOM   5432  C  CB  . ASN B 2 223 ? 8.592   -7.658  68.624  1.00 52.52  ? 223 ASN B CB  1 
ATOM   5433  C  CG  . ASN B 2 223 ? 9.757   -7.606  69.559  1.00 51.68  ? 223 ASN B CG  1 
ATOM   5434  O  OD1 . ASN B 2 223 ? 10.281  -8.666  69.919  1.00 52.32  ? 223 ASN B OD1 1 
ATOM   5435  N  ND2 . ASN B 2 223 ? 10.255  -6.403  69.860  1.00 52.00  ? 223 ASN B ND2 1 
ATOM   5436  N  N   . ARG B 2 224 ? 7.810   -8.947  65.333  1.00 44.29  ? 224 ARG B N   1 
ATOM   5437  C  CA  . ARG B 2 224 ? 6.713   -9.148  64.406  1.00 41.03  ? 224 ARG B CA  1 
ATOM   5438  C  C   . ARG B 2 224 ? 6.383   -10.634 64.345  1.00 42.84  ? 224 ARG B C   1 
ATOM   5439  O  O   . ARG B 2 224 ? 7.267   -11.455 64.108  1.00 45.36  ? 224 ARG B O   1 
ATOM   5440  C  CB  . ARG B 2 224 ? 7.120   -8.643  63.016  1.00 39.80  ? 224 ARG B CB  1 
ATOM   5441  C  CG  . ARG B 2 224 ? 5.963   -8.324  62.165  1.00 40.17  ? 224 ARG B CG  1 
ATOM   5442  C  CD  . ARG B 2 224 ? 6.336   -8.226  60.685  1.00 38.15  ? 224 ARG B CD  1 
ATOM   5443  N  NE  . ARG B 2 224 ? 5.112   -7.960  59.942  1.00 36.71  ? 224 ARG B NE  1 
ATOM   5444  C  CZ  . ARG B 2 224 ? 5.050   -7.684  58.653  1.00 40.66  ? 224 ARG B CZ  1 
ATOM   5445  N  NH1 . ARG B 2 224 ? 6.089   -7.887  57.857  1.00 37.17  ? 224 ARG B NH1 1 
ATOM   5446  N  NH2 . ARG B 2 224 ? 3.884   -7.296  58.127  1.00 39.79  ? 224 ARG B NH2 1 
ATOM   5447  N  N   . LYS B 2 225 ? 5.122   -10.986 64.555  1.00 47.77  ? 225 LYS B N   1 
ATOM   5448  C  CA  . LYS B 2 225 ? 4.727   -12.386 64.439  1.00 50.92  ? 225 LYS B CA  1 
ATOM   5449  C  C   . LYS B 2 225 ? 4.582   -12.757 62.967  1.00 50.41  ? 225 LYS B C   1 
ATOM   5450  O  O   . LYS B 2 225 ? 4.099   -11.958 62.166  1.00 57.31  ? 225 LYS B O   1 
ATOM   5451  C  CB  . LYS B 2 225 ? 3.419   -12.635 65.194  1.00 55.11  ? 225 LYS B CB  1 
ATOM   5452  C  CG  . LYS B 2 225 ? 2.171   -12.167 64.448  1.00 65.53  ? 225 LYS B CG  1 
ATOM   5453  C  CD  . LYS B 2 225 ? 1.069   -13.227 64.484  1.00 69.06  ? 225 LYS B CD  1 
ATOM   5454  C  CE  . LYS B 2 225 ? 0.285   -13.171 65.783  1.00 70.91  ? 225 LYS B CE  1 
ATOM   5455  N  NZ  . LYS B 2 225 ? -0.585  -14.373 65.988  1.00 74.51  ? 225 LYS B NZ  1 
ATOM   5456  N  N   . VAL B 2 226 ? 5.072   -13.938 62.586  1.00 48.24  ? 226 VAL B N   1 
ATOM   5457  C  CA  . VAL B 2 226 ? 4.883   -14.454 61.229  1.00 44.88  ? 226 VAL B CA  1 
ATOM   5458  C  C   . VAL B 2 226 ? 3.781   -15.500 61.273  1.00 47.40  ? 226 VAL B C   1 
ATOM   5459  O  O   . VAL B 2 226 ? 3.848   -16.438 62.073  1.00 50.07  ? 226 VAL B O   1 
ATOM   5460  C  CB  . VAL B 2 226 ? 6.183   -15.038 60.648  1.00 47.76  ? 226 VAL B CB  1 
ATOM   5461  C  CG1 . VAL B 2 226 ? 5.955   -15.613 59.207  1.00 44.43  ? 226 VAL B CG1 1 
ATOM   5462  C  CG2 . VAL B 2 226 ? 7.270   -13.974 60.612  1.00 44.91  ? 226 VAL B CG2 1 
ATOM   5463  N  N   . GLU B 2 227 ? 2.742   -15.325 60.455  1.00 45.69  ? 227 GLU B N   1 
ATOM   5464  C  CA  . GLU B 2 227 ? 1.674   -16.324 60.410  1.00 52.51  ? 227 GLU B CA  1 
ATOM   5465  C  C   . GLU B 2 227 ? 1.786   -17.264 59.212  1.00 49.72  ? 227 GLU B C   1 
ATOM   5466  O  O   . GLU B 2 227 ? 1.482   -18.463 59.319  1.00 47.82  ? 227 GLU B O   1 
ATOM   5467  C  CB  . GLU B 2 227 ? 0.302   -15.641 60.382  1.00 57.98  ? 227 GLU B CB  1 
ATOM   5468  C  CG  . GLU B 2 227 ? -0.214  -15.137 61.728  1.00 63.48  ? 227 GLU B CG  1 
ATOM   5469  C  CD  . GLU B 2 227 ? -0.714  -16.245 62.672  1.00 69.70  ? 227 GLU B CD  1 
ATOM   5470  O  OE1 . GLU B 2 227 ? -1.049  -17.368 62.211  1.00 70.73  ? 227 GLU B OE1 1 
ATOM   5471  O  OE2 . GLU B 2 227 ? -0.795  -15.975 63.894  1.00 73.39  ? 227 GLU B OE2 1 
ATOM   5472  N  N   . ARG B 2 228 ? 2.208   -16.732 58.082  1.00 44.71  ? 228 ARG B N   1 
ATOM   5473  C  CA  . ARG B 2 228 ? 2.224   -17.450 56.806  1.00 44.84  ? 228 ARG B CA  1 
ATOM   5474  C  C   . ARG B 2 228 ? 3.319   -18.504 56.754  1.00 46.27  ? 228 ARG B C   1 
ATOM   5475  O  O   . ARG B 2 228 ? 4.380   -18.373 57.384  1.00 45.46  ? 228 ARG B O   1 
ATOM   5476  C  CB  . ARG B 2 228 ? 2.407   -16.449 55.662  1.00 42.56  ? 228 ARG B CB  1 
ATOM   5477  C  CG  . ARG B 2 228 ? 3.739   -15.752 55.691  1.00 41.31  ? 228 ARG B CG  1 
ATOM   5478  C  CD  . ARG B 2 228 ? 3.784   -14.585 54.708  1.00 42.70  ? 228 ARG B CD  1 
ATOM   5479  N  NE  . ARG B 2 228 ? 3.699   -15.067 53.339  1.00 38.44  ? 228 ARG B NE  1 
ATOM   5480  C  CZ  . ARG B 2 228 ? 4.713   -15.632 52.702  1.00 39.86  ? 228 ARG B CZ  1 
ATOM   5481  N  NH1 . ARG B 2 228 ? 5.912   -15.745 53.268  1.00 36.30  ? 228 ARG B NH1 1 
ATOM   5482  N  NH2 . ARG B 2 228 ? 4.526   -16.087 51.467  1.00 37.79  ? 228 ARG B NH2 1 
ATOM   5483  N  N   . LYS B 2 229 ? 3.064   -19.555 55.972  1.00 40.25  ? 229 LYS B N   1 
ATOM   5484  C  CA  . LYS B 2 229 ? 4.105   -20.543 55.725  1.00 45.52  ? 229 LYS B CA  1 
ATOM   5485  C  C   . LYS B 2 229 ? 5.025   -20.039 54.614  1.00 42.83  ? 229 LYS B C   1 
ATOM   5486  O  O   . LYS B 2 229 ? 4.574   -19.385 53.666  1.00 40.24  ? 229 LYS B O   1 
ATOM   5487  C  CB  . LYS B 2 229 ? 3.474   -21.878 55.341  1.00 46.78  ? 229 LYS B CB  1 
ATOM   5488  C  CG  . LYS B 2 229 ? 2.604   -22.471 56.453  1.00 49.95  ? 229 LYS B CG  1 
ATOM   5489  C  CD  . LYS B 2 229 ? 3.348   -22.895 57.739  1.00 56.28  ? 229 LYS B CD  1 
ATOM   5490  C  CE  . LYS B 2 229 ? 3.045   -24.376 58.077  1.00 65.92  ? 229 LYS B CE  1 
ATOM   5491  N  NZ  . LYS B 2 229 ? 4.169   -25.194 58.658  1.00 63.66  ? 229 LYS B NZ  1 
ATOM   5492  N  N   . THR B 2 230 ? 6.330   -20.307 54.754  1.00 39.80  ? 230 THR B N   1 
ATOM   5493  C  CA  . THR B 2 230 ? 7.303   -19.797 53.785  1.00 40.10  ? 230 THR B CA  1 
ATOM   5494  C  C   . THR B 2 230 ? 7.107   -20.467 52.416  1.00 37.33  ? 230 THR B C   1 
ATOM   5495  O  O   . THR B 2 230 ? 7.113   -19.793 51.375  1.00 37.93  ? 230 THR B O   1 
ATOM   5496  C  CB  . THR B 2 230 ? 8.724   -20.024 54.330  1.00 38.28  ? 230 THR B CB  1 
ATOM   5497  O  OG1 . THR B 2 230 ? 8.850   -19.365 55.609  1.00 44.22  ? 230 THR B OG1 1 
ATOM   5498  C  CG2 . THR B 2 230 ? 9.796   -19.461 53.404  1.00 38.96  ? 230 THR B CG2 1 
ATOM   5499  N  N   . GLY B 2 231 ? 6.885   -21.789 52.397  1.00 37.47  ? 231 GLY B N   1 
ATOM   5500  C  CA  . GLY B 2 231 ? 6.848   -22.423 51.086  1.00 36.98  ? 231 GLY B CA  1 
ATOM   5501  C  C   . GLY B 2 231 ? 8.211   -22.348 50.404  1.00 36.72  ? 231 GLY B C   1 
ATOM   5502  O  O   . GLY B 2 231 ? 9.256   -22.120 51.040  1.00 40.55  ? 231 GLY B O   1 
ATOM   5503  N  N   . ALA B 2 232 ? 8.210   -22.511 49.074  1.00 36.27  ? 232 ALA B N   1 
ATOM   5504  C  CA  . ALA B 2 232 ? 9.478   -22.502 48.350  1.00 35.63  ? 232 ALA B CA  1 
ATOM   5505  C  C   . ALA B 2 232 ? 10.123  -21.117 48.351  1.00 32.89  ? 232 ALA B C   1 
ATOM   5506  O  O   . ALA B 2 232 ? 9.442   -20.096 48.269  1.00 35.43  ? 232 ALA B O   1 
ATOM   5507  C  CB  . ALA B 2 232 ? 9.298   -22.969 46.906  1.00 32.80  ? 232 ALA B CB  1 
ATOM   5508  N  N   . ARG B 2 233 ? 11.452  -21.101 48.441  1.00 32.21  ? 233 ARG B N   1 
ATOM   5509  C  CA  . ARG B 2 233 ? 12.247  -19.871 48.452  1.00 31.93  ? 233 ARG B CA  1 
ATOM   5510  C  C   . ARG B 2 233 ? 12.633  -19.497 47.009  1.00 30.61  ? 233 ARG B C   1 
ATOM   5511  O  O   . ARG B 2 233 ? 13.449  -20.175 46.361  1.00 30.53  ? 233 ARG B O   1 
ATOM   5512  C  CB  . ARG B 2 233 ? 13.483  -20.047 49.320  1.00 30.62  ? 233 ARG B CB  1 
ATOM   5513  C  CG  . ARG B 2 233 ? 13.150  -20.332 50.827  1.00 31.99  ? 233 ARG B CG  1 
ATOM   5514  C  CD  . ARG B 2 233 ? 14.452  -20.507 51.591  1.00 30.98  ? 233 ARG B CD  1 
ATOM   5515  N  NE  . ARG B 2 233 ? 15.206  -19.259 51.719  1.00 30.09  ? 233 ARG B NE  1 
ATOM   5516  C  CZ  . ARG B 2 233 ? 15.028  -18.396 52.711  1.00 34.00  ? 233 ARG B CZ  1 
ATOM   5517  N  NH1 . ARG B 2 233 ? 14.114  -18.612 53.643  1.00 31.48  ? 233 ARG B NH1 1 
ATOM   5518  N  NH2 . ARG B 2 233 ? 15.756  -17.265 52.744  1.00 31.99  ? 233 ARG B NH2 1 
ATOM   5519  N  N   . PHE B 2 234 ? 12.013  -18.436 46.492  1.00 30.72  ? 234 PHE B N   1 
ATOM   5520  C  CA  . PHE B 2 234 ? 12.166  -18.015 45.096  1.00 25.18  ? 234 PHE B CA  1 
ATOM   5521  C  C   . PHE B 2 234 ? 13.060  -16.794 45.014  1.00 28.49  ? 234 PHE B C   1 
ATOM   5522  O  O   . PHE B 2 234 ? 13.148  -15.993 45.962  1.00 27.84  ? 234 PHE B O   1 
ATOM   5523  C  CB  . PHE B 2 234 ? 10.796  -17.654 44.494  1.00 29.29  ? 234 PHE B CB  1 
ATOM   5524  C  CG  . PHE B 2 234 ? 9.971   -18.824 44.030  1.00 28.66  ? 234 PHE B CG  1 
ATOM   5525  C  CD1 . PHE B 2 234 ? 10.549  -20.054 43.773  1.00 31.78  ? 234 PHE B CD1 1 
ATOM   5526  C  CD2 . PHE B 2 234 ? 8.622   -18.657 43.757  1.00 34.12  ? 234 PHE B CD2 1 
ATOM   5527  C  CE1 . PHE B 2 234 ? 9.776   -21.144 43.323  1.00 37.25  ? 234 PHE B CE1 1 
ATOM   5528  C  CE2 . PHE B 2 234 ? 7.840   -19.726 43.286  1.00 38.67  ? 234 PHE B CE2 1 
ATOM   5529  C  CZ  . PHE B 2 234 ? 8.426   -20.965 43.049  1.00 35.36  ? 234 PHE B CZ  1 
ATOM   5530  N  N   . MET B 2 235 ? 13.718  -16.635 43.876  1.00 24.72  ? 235 MET B N   1 
ATOM   5531  C  CA  . MET B 2 235 ? 14.328  -15.370 43.551  1.00 24.94  ? 235 MET B CA  1 
ATOM   5532  C  C   . MET B 2 235 ? 13.679  -14.873 42.269  1.00 27.63  ? 235 MET B C   1 
ATOM   5533  O  O   . MET B 2 235 ? 13.330  -15.668 41.403  1.00 28.93  ? 235 MET B O   1 
ATOM   5534  C  CB  . MET B 2 235 ? 15.852  -15.548 43.411  1.00 28.72  ? 235 MET B CB  1 
ATOM   5535  C  CG  . MET B 2 235 ? 16.609  -14.487 42.639  1.00 27.15  ? 235 MET B CG  1 
ATOM   5536  S  SD  . MET B 2 235 ? 18.371  -14.872 42.663  1.00 29.51  ? 235 MET B SD  1 
ATOM   5537  C  CE  . MET B 2 235 ? 19.030  -13.188 42.698  1.00 26.30  ? 235 MET B CE  1 
ATOM   5538  N  N   . THR B 2 236 ? 13.489  -13.556 42.135  1.00 25.22  ? 236 THR B N   1 
ATOM   5539  C  CA  . THR B 2 236 ? 13.011  -13.022 40.865  1.00 25.06  ? 236 THR B CA  1 
ATOM   5540  C  C   . THR B 2 236 ? 14.144  -12.268 40.197  1.00 25.27  ? 236 THR B C   1 
ATOM   5541  O  O   . THR B 2 236 ? 14.973  -11.644 40.868  1.00 25.03  ? 236 THR B O   1 
ATOM   5542  C  CB  . THR B 2 236 ? 11.798  -12.099 41.018  1.00 28.07  ? 236 THR B CB  1 
ATOM   5543  O  OG1 . THR B 2 236 ? 12.085  -11.118 42.006  1.00 26.79  ? 236 THR B OG1 1 
ATOM   5544  C  CG2 . THR B 2 236 ? 10.564  -12.894 41.446  1.00 26.69  ? 236 THR B CG2 1 
ATOM   5545  N  N   . ILE B 2 237 ? 14.227  -12.376 38.879  1.00 22.77  ? 237 ILE B N   1 
ATOM   5546  C  CA  . ILE B 2 237 ? 15.343  -11.825 38.098  1.00 22.11  ? 237 ILE B CA  1 
ATOM   5547  C  C   . ILE B 2 237 ? 14.782  -11.093 36.875  1.00 25.39  ? 237 ILE B C   1 
ATOM   5548  O  O   . ILE B 2 237 ? 13.854  -11.575 36.215  1.00 24.47  ? 237 ILE B O   1 
ATOM   5549  C  CB  . ILE B 2 237 ? 16.324  -12.932 37.636  1.00 24.16  ? 237 ILE B CB  1 
ATOM   5550  C  CG1 . ILE B 2 237 ? 16.874  -13.742 38.850  1.00 23.16  ? 237 ILE B CG1 1 
ATOM   5551  C  CG2 . ILE B 2 237 ? 17.437  -12.312 36.824  1.00 27.48  ? 237 ILE B CG2 1 
ATOM   5552  C  CD1 . ILE B 2 237 ? 17.889  -14.942 38.438  1.00 25.83  ? 237 ILE B CD1 1 
ATOM   5553  N  N   . GLY B 2 238 ? 15.272  -9.890  36.610  1.00 23.81  ? 238 GLY B N   1 
ATOM   5554  C  CA  . GLY B 2 238 ? 14.763  -9.202  35.436  1.00 25.48  ? 238 GLY B CA  1 
ATOM   5555  C  C   . GLY B 2 238 ? 15.316  -7.803  35.390  1.00 23.66  ? 238 GLY B C   1 
ATOM   5556  O  O   . GLY B 2 238 ? 16.302  -7.469  36.065  1.00 24.95  ? 238 GLY B O   1 
ATOM   5557  N  N   . SER B 2 239 ? 14.700  -7.000  34.537  1.00 26.45  ? 239 SER B N   1 
ATOM   5558  C  CA  . SER B 2 239 ? 15.173  -5.645  34.405  1.00 25.69  ? 239 SER B CA  1 
ATOM   5559  C  C   . SER B 2 239 ? 14.521  -4.770  35.458  1.00 23.38  ? 239 SER B C   1 
ATOM   5560  O  O   . SER B 2 239 ? 15.133  -4.556  36.486  1.00 28.49  ? 239 SER B O   1 
ATOM   5561  C  CB  . SER B 2 239 ? 14.895  -5.155  33.004  1.00 24.18  ? 239 SER B CB  1 
ATOM   5562  O  OG  . SER B 2 239 ? 13.508  -5.301  32.710  1.00 23.14  ? 239 SER B OG  1 
ATOM   5563  N  N   . GLU B 2 240 ? 13.256  -4.361  35.273  1.00 25.62  ? 240 GLU B N   1 
ATOM   5564  C  CA  . GLU B 2 240 ? 12.603  -3.482  36.242  1.00 28.18  ? 240 GLU B CA  1 
ATOM   5565  C  C   . GLU B 2 240 ? 11.833  -4.327  37.280  1.00 29.53  ? 240 GLU B C   1 
ATOM   5566  O  O   . GLU B 2 240 ? 12.051  -4.183  38.487  1.00 29.16  ? 240 GLU B O   1 
ATOM   5567  C  CB  . GLU B 2 240 ? 11.650  -2.492  35.568  1.00 32.01  ? 240 GLU B CB  1 
ATOM   5568  C  CG  . GLU B 2 240 ? 10.701  -1.879  36.600  1.00 34.34  ? 240 GLU B CG  1 
ATOM   5569  C  CD  . GLU B 2 240 ? 11.378  -0.897  37.560  1.00 36.68  ? 240 GLU B CD  1 
ATOM   5570  O  OE1 . GLU B 2 240 ? 12.623  -0.699  37.505  1.00 37.36  ? 240 GLU B OE1 1 
ATOM   5571  O  OE2 . GLU B 2 240 ? 10.690  -0.452  38.519  1.00 42.23  ? 240 GLU B OE2 1 
ATOM   5572  N  N   . ASN B 2 241 ? 10.928  -5.213  36.814  1.00 27.60  ? 241 ASN B N   1 
ATOM   5573  C  CA  . ASN B 2 241 ? 10.105  -6.085  37.656  1.00 29.77  ? 241 ASN B CA  1 
ATOM   5574  C  C   . ASN B 2 241 ? 9.308   -5.260  38.677  1.00 31.60  ? 241 ASN B C   1 
ATOM   5575  O  O   . ASN B 2 241 ? 9.464   -5.425  39.885  1.00 28.40  ? 241 ASN B O   1 
ATOM   5576  C  CB  . ASN B 2 241 ? 10.954  -7.160  38.385  1.00 28.95  ? 241 ASN B CB  1 
ATOM   5577  C  CG  . ASN B 2 241 ? 11.420  -8.278  37.447  1.00 29.30  ? 241 ASN B CG  1 
ATOM   5578  O  OD1 . ASN B 2 241 ? 11.082  -8.260  36.287  1.00 29.91  ? 241 ASN B OD1 1 
ATOM   5579  N  ND2 . ASN B 2 241 ? 12.195  -9.232  37.958  1.00 30.42  ? 241 ASN B ND2 1 
ATOM   5580  N  N   . ASP B 2 242 ? 8.440   -4.368  38.191  1.00 28.52  ? 242 ASP B N   1 
ATOM   5581  C  CA  . ASP B 2 242 ? 7.709   -3.538  39.153  1.00 33.49  ? 242 ASP B CA  1 
ATOM   5582  C  C   . ASP B 2 242 ? 6.227   -3.889  39.264  1.00 36.53  ? 242 ASP B C   1 
ATOM   5583  O  O   . ASP B 2 242 ? 5.473   -3.119  39.858  1.00 39.21  ? 242 ASP B O   1 
ATOM   5584  C  CB  . ASP B 2 242 ? 7.826   -2.054  38.814  1.00 33.35  ? 242 ASP B CB  1 
ATOM   5585  C  CG  . ASP B 2 242 ? 7.374   -1.726  37.407  1.00 36.81  ? 242 ASP B CG  1 
ATOM   5586  O  OD1 . ASP B 2 242 ? 7.092   -2.638  36.617  1.00 41.51  ? 242 ASP B OD1 1 
ATOM   5587  O  OD2 . ASP B 2 242 ? 7.279   -0.530  37.057  1.00 44.60  ? 242 ASP B OD2 1 
ATOM   5588  N  N   . ASP B 2 243 ? 5.786   -5.024  38.726  1.00 33.98  ? 243 ASP B N   1 
ATOM   5589  C  CA  . ASP B 2 243 ? 4.371   -5.389  38.831  1.00 34.94  ? 243 ASP B CA  1 
ATOM   5590  C  C   . ASP B 2 243 ? 4.156   -6.099  40.167  1.00 36.95  ? 243 ASP B C   1 
ATOM   5591  O  O   . ASP B 2 243 ? 4.196   -7.329  40.257  1.00 36.11  ? 243 ASP B O   1 
ATOM   5592  C  CB  . ASP B 2 243 ? 3.953   -6.268  37.658  1.00 36.45  ? 243 ASP B CB  1 
ATOM   5593  C  CG  . ASP B 2 243 ? 2.420   -6.403  37.545  1.00 41.99  ? 243 ASP B CG  1 
ATOM   5594  O  OD1 . ASP B 2 243 ? 1.731   -6.088  38.542  1.00 41.16  ? 243 ASP B OD1 1 
ATOM   5595  O  OD2 . ASP B 2 243 ? 1.908   -6.817  36.474  1.00 45.14  ? 243 ASP B OD2 1 
ATOM   5596  N  N   . ILE B 2 244 ? 3.891   -5.310  41.222  1.00 37.73  ? 244 ILE B N   1 
ATOM   5597  C  CA  . ILE B 2 244 ? 3.730   -5.874  42.568  1.00 36.00  ? 244 ILE B CA  1 
ATOM   5598  C  C   . ILE B 2 244 ? 2.560   -6.854  42.616  1.00 38.05  ? 244 ILE B C   1 
ATOM   5599  O  O   . ILE B 2 244 ? 2.630   -7.887  43.292  1.00 38.34  ? 244 ILE B O   1 
ATOM   5600  C  CB  . ILE B 2 244 ? 3.577   -4.745  43.616  1.00 39.15  ? 244 ILE B CB  1 
ATOM   5601  C  CG1 . ILE B 2 244 ? 4.646   -3.669  43.403  1.00 37.57  ? 244 ILE B CG1 1 
ATOM   5602  C  CG2 . ILE B 2 244 ? 3.652   -5.296  45.069  1.00 36.68  ? 244 ILE B CG2 1 
ATOM   5603  C  CD1 . ILE B 2 244 ? 4.946   -2.777  44.648  1.00 38.29  ? 244 ILE B CD1 1 
ATOM   5604  N  N   . ALA B 2 245 ? 1.471   -6.563  41.901  1.00 38.92  ? 245 ALA B N   1 
ATOM   5605  C  CA  . ALA B 2 245 ? 0.357   -7.519  41.854  1.00 42.73  ? 245 ALA B CA  1 
ATOM   5606  C  C   . ALA B 2 245 ? 0.804   -8.883  41.330  1.00 43.02  ? 245 ALA B C   1 
ATOM   5607  O  O   . ALA B 2 245 ? 0.335   -9.939  41.793  1.00 39.59  ? 245 ALA B O   1 
ATOM   5608  C  CB  . ALA B 2 245 ? -0.787  -6.981  40.988  1.00 44.66  ? 245 ALA B CB  1 
ATOM   5609  N  N   . PHE B 2 246 ? 1.682   -8.884  40.336  1.00 42.77  ? 246 PHE B N   1 
ATOM   5610  C  CA  . PHE B 2 246 ? 2.169   -10.156 39.843  1.00 37.11  ? 246 PHE B CA  1 
ATOM   5611  C  C   . PHE B 2 246 ? 2.992   -10.853 40.929  1.00 38.24  ? 246 PHE B C   1 
ATOM   5612  O  O   . PHE B 2 246 ? 2.858   -12.067 41.137  1.00 37.26  ? 246 PHE B O   1 
ATOM   5613  C  CB  . PHE B 2 246 ? 3.006   -9.957  38.572  1.00 37.75  ? 246 PHE B CB  1 
ATOM   5614  C  CG  . PHE B 2 246 ? 3.611   -11.255 38.078  1.00 37.62  ? 246 PHE B CG  1 
ATOM   5615  C  CD1 . PHE B 2 246 ? 4.811   -11.732 38.587  1.00 35.07  ? 246 PHE B CD1 1 
ATOM   5616  C  CD2 . PHE B 2 246 ? 2.905   -12.036 37.170  1.00 43.31  ? 246 PHE B CD2 1 
ATOM   5617  C  CE1 . PHE B 2 246 ? 5.298   -12.936 38.169  1.00 36.80  ? 246 PHE B CE1 1 
ATOM   5618  C  CE2 . PHE B 2 246 ? 3.399   -13.238 36.744  1.00 39.25  ? 246 PHE B CE2 1 
ATOM   5619  C  CZ  . PHE B 2 246 ? 4.593   -13.690 37.250  1.00 42.56  ? 246 PHE B CZ  1 
ATOM   5620  N  N   . MET B 2 247 ? 3.846   -10.098 41.636  1.00 33.94  ? 247 MET B N   1 
ATOM   5621  C  CA  . MET B 2 247 ? 4.635   -10.693 42.722  1.00 36.67  ? 247 MET B CA  1 
ATOM   5622  C  C   . MET B 2 247 ? 3.730   -11.290 43.804  1.00 32.99  ? 247 MET B C   1 
ATOM   5623  O  O   . MET B 2 247 ? 4.069   -12.313 44.401  1.00 37.21  ? 247 MET B O   1 
ATOM   5624  C  CB  . MET B 2 247 ? 5.569   -9.644  43.347  1.00 33.32  ? 247 MET B CB  1 
ATOM   5625  C  CG  . MET B 2 247 ? 6.692   -9.128  42.397  1.00 39.24  ? 247 MET B CG  1 
ATOM   5626  S  SD  . MET B 2 247 ? 7.437   -10.307 41.250  1.00 35.48  ? 247 MET B SD  1 
ATOM   5627  C  CE  . MET B 2 247 ? 8.795   -9.271  40.695  1.00 33.48  ? 247 MET B CE  1 
ATOM   5628  N  N   . GLY B 2 248 ? 2.581   -10.650 44.089  1.00 36.06  ? 248 GLY B N   1 
ATOM   5629  C  CA  . GLY B 2 248 ? 1.642   -11.180 45.067  1.00 37.19  ? 248 GLY B CA  1 
ATOM   5630  C  C   . GLY B 2 248 ? 1.031   -12.495 44.634  1.00 37.26  ? 248 GLY B C   1 
ATOM   5631  O  O   . GLY B 2 248 ? 0.779   -13.373 45.461  1.00 37.40  ? 248 GLY B O   1 
ATOM   5632  N  N   . MET B 2 249 ? 0.802   -12.663 43.330  1.00 40.23  ? 249 MET B N   1 
ATOM   5633  C  CA  . MET B 2 249 ? 0.350   -13.961 42.850  1.00 38.91  ? 249 MET B CA  1 
ATOM   5634  C  C   . MET B 2 249 ? 1.410   -15.017 43.104  1.00 39.04  ? 249 MET B C   1 
ATOM   5635  O  O   . MET B 2 249 ? 1.094   -16.116 43.583  1.00 44.00  ? 249 MET B O   1 
ATOM   5636  C  CB  . MET B 2 249 ? -0.006  -13.864 41.375  1.00 39.92  ? 249 MET B CB  1 
ATOM   5637  C  CG  . MET B 2 249 ? -0.416  -15.156 40.682  1.00 46.19  ? 249 MET B CG  1 
ATOM   5638  S  SD  . MET B 2 249 ? 1.007   -16.191 40.281  1.00 44.35  ? 249 MET B SD  1 
ATOM   5639  C  CE  . MET B 2 249 ? 1.466   -15.534 38.682  1.00 44.13  ? 249 MET B CE  1 
ATOM   5640  N  N   . VAL B 2 250 ? 2.678   -14.684 42.845  1.00 37.55  ? 250 VAL B N   1 
ATOM   5641  C  CA  . VAL B 2 250 ? 3.761   -15.650 43.025  1.00 40.76  ? 250 VAL B CA  1 
ATOM   5642  C  C   . VAL B 2 250 ? 3.760   -16.182 44.451  1.00 39.81  ? 250 VAL B C   1 
ATOM   5643  O  O   . VAL B 2 250 ? 3.784   -17.397 44.677  1.00 41.63  ? 250 VAL B O   1 
ATOM   5644  C  CB  . VAL B 2 250 ? 5.121   -15.027 42.656  1.00 37.27  ? 250 VAL B CB  1 
ATOM   5645  C  CG1 . VAL B 2 250 ? 6.258   -16.024 42.926  1.00 40.33  ? 250 VAL B CG1 1 
ATOM   5646  C  CG2 . VAL B 2 250 ? 5.159   -14.540 41.192  1.00 37.39  ? 250 VAL B CG2 1 
ATOM   5647  N  N   . GLU B 2 251 ? 3.645   -15.280 45.436  1.00 36.69  ? 251 GLU B N   1 
ATOM   5648  C  CA  . GLU B 2 251 ? 3.705   -15.622 46.854  1.00 37.24  ? 251 GLU B CA  1 
ATOM   5649  C  C   . GLU B 2 251 ? 2.420   -16.210 47.391  1.00 42.78  ? 251 GLU B C   1 
ATOM   5650  O  O   . GLU B 2 251 ? 2.377   -16.596 48.562  1.00 49.95  ? 251 GLU B O   1 
ATOM   5651  C  CB  . GLU B 2 251 ? 4.035   -14.375 47.669  1.00 36.00  ? 251 GLU B CB  1 
ATOM   5652  C  CG  . GLU B 2 251 ? 5.428   -13.935 47.387  1.00 32.70  ? 251 GLU B CG  1 
ATOM   5653  C  CD  . GLU B 2 251 ? 5.985   -12.968 48.420  1.00 35.78  ? 251 GLU B CD  1 
ATOM   5654  O  OE1 . GLU B 2 251 ? 5.223   -12.054 48.856  1.00 36.07  ? 251 GLU B OE1 1 
ATOM   5655  O  OE2 . GLU B 2 251 ? 7.213   -13.082 48.718  1.00 33.66  ? 251 GLU B OE2 1 
ATOM   5656  N  N   . SER B 2 252 ? 1.359   -16.239 46.606  1.00 39.36  ? 252 SER B N   1 
ATOM   5657  C  CA  . SER B 2 252 ? 0.139   -16.881 47.042  1.00 42.27  ? 252 SER B CA  1 
ATOM   5658  C  C   . SER B 2 252 ? 0.078   -18.338 46.606  1.00 43.21  ? 252 SER B C   1 
ATOM   5659  O  O   . SER B 2 252 ? -0.864  -19.033 46.982  1.00 46.32  ? 252 SER B O   1 
ATOM   5660  C  CB  . SER B 2 252 ? -1.070  -16.118 46.497  1.00 43.71  ? 252 SER B CB  1 
ATOM   5661  O  OG  . SER B 2 252 ? -1.185  -16.367 45.102  1.00 46.77  ? 252 SER B OG  1 
ATOM   5662  N  N   . VAL B 2 253 ? 1.057   -18.822 45.828  1.00 42.72  ? 253 VAL B N   1 
ATOM   5663  C  CA  . VAL B 2 253 ? 1.014   -20.209 45.366  1.00 44.24  ? 253 VAL B CA  1 
ATOM   5664  C  C   . VAL B 2 253 ? 1.724   -21.155 46.311  1.00 42.48  ? 253 VAL B C   1 
ATOM   5665  O  O   . VAL B 2 253 ? 1.601   -22.377 46.146  1.00 45.45  ? 253 VAL B O   1 
ATOM   5666  C  CB  . VAL B 2 253 ? 1.589   -20.374 43.945  1.00 44.10  ? 253 VAL B CB  1 
ATOM   5667  C  CG1 . VAL B 2 253 ? 1.092   -19.273 43.036  1.00 47.06  ? 253 VAL B CG1 1 
ATOM   5668  C  CG2 . VAL B 2 253 ? 3.088   -20.345 43.986  1.00 40.30  ? 253 VAL B CG2 1 
ATOM   5669  N  N   . GLY B 2 254 ? 2.405   -20.640 47.334  1.00 40.66  ? 254 GLY B N   1 
ATOM   5670  C  CA  . GLY B 2 254 ? 3.070   -21.498 48.301  1.00 42.79  ? 254 GLY B CA  1 
ATOM   5671  C  C   . GLY B 2 254 ? 4.560   -21.243 48.234  1.00 39.44  ? 254 GLY B C   1 
ATOM   5672  O  O   . GLY B 2 254 ? 5.388   -22.163 48.171  1.00 39.36  ? 254 GLY B O   1 
ATOM   5673  N  N   . ALA B 2 255 ? 4.910   -19.968 48.199  1.00 39.89  ? 255 ALA B N   1 
ATOM   5674  C  CA  . ALA B 2 255 ? 6.298   -19.579 48.045  1.00 36.08  ? 255 ALA B CA  1 
ATOM   5675  C  C   . ALA B 2 255 ? 6.516   -18.247 48.724  1.00 34.22  ? 255 ALA B C   1 
ATOM   5676  O  O   . ALA B 2 255 ? 5.574   -17.500 49.000  1.00 35.51  ? 255 ALA B O   1 
ATOM   5677  C  CB  . ALA B 2 255 ? 6.686   -19.460 46.572  1.00 37.50  ? 255 ALA B CB  1 
ATOM   5678  N  N   . THR B 2 256 ? 7.789   -17.911 48.888  1.00 31.46  ? 256 THR B N   1 
ATOM   5679  C  CA  . THR B 2 256 ? 8.192   -16.567 49.275  1.00 31.53  ? 256 THR B CA  1 
ATOM   5680  C  C   . THR B 2 256 ? 9.333   -16.144 48.360  1.00 32.87  ? 256 THR B C   1 
ATOM   5681  O  O   . THR B 2 256 ? 10.252  -16.926 48.110  1.00 32.13  ? 256 THR B O   1 
ATOM   5682  C  CB  . THR B 2 256 ? 8.631   -16.512 50.734  1.00 32.05  ? 256 THR B CB  1 
ATOM   5683  O  OG1 . THR B 2 256 ? 7.610   -17.075 51.574  1.00 37.06  ? 256 THR B OG1 1 
ATOM   5684  C  CG2 . THR B 2 256 ? 9.030   -15.069 51.158  1.00 33.55  ? 256 THR B CG2 1 
ATOM   5685  N  N   . ILE B 2 257 ? 9.282   -14.918 47.851  1.00 29.19  ? 257 ILE B N   1 
ATOM   5686  C  CA  . ILE B 2 257 ? 10.403  -14.353 47.116  1.00 30.33  ? 257 ILE B CA  1 
ATOM   5687  C  C   . ILE B 2 257 ? 11.388  -13.813 48.140  1.00 31.25  ? 257 ILE B C   1 
ATOM   5688  O  O   . ILE B 2 257 ? 11.106  -12.830 48.835  1.00 31.45  ? 257 ILE B O   1 
ATOM   5689  C  CB  . ILE B 2 257 ? 9.952   -13.267 46.136  1.00 33.51  ? 257 ILE B CB  1 
ATOM   5690  C  CG1 . ILE B 2 257 ? 8.968   -13.870 45.131  1.00 32.58  ? 257 ILE B CG1 1 
ATOM   5691  C  CG2 . ILE B 2 257 ? 11.144  -12.682 45.424  1.00 30.15  ? 257 ILE B CG2 1 
ATOM   5692  C  CD1 . ILE B 2 257 ? 8.093   -12.814 44.439  1.00 37.29  ? 257 ILE B CD1 1 
ATOM   5693  N  N   . VAL B 2 258 ? 12.530  -14.489 48.294  1.00 30.61  ? 258 VAL B N   1 
ATOM   5694  C  CA  . VAL B 2 258 ? 13.431  -14.095 49.379  1.00 28.98  ? 258 VAL B CA  1 
ATOM   5695  C  C   . VAL B 2 258 ? 14.534  -13.164 48.913  1.00 29.70  ? 258 VAL B C   1 
ATOM   5696  O  O   . VAL B 2 258 ? 15.222  -12.572 49.766  1.00 28.67  ? 258 VAL B O   1 
ATOM   5697  C  CB  . VAL B 2 258 ? 14.030  -15.323 50.105  1.00 29.04  ? 258 VAL B CB  1 
ATOM   5698  C  CG1 . VAL B 2 258 ? 12.882  -16.138 50.816  1.00 32.78  ? 258 VAL B CG1 1 
ATOM   5699  C  CG2 . VAL B 2 258 ? 14.770  -16.225 49.132  1.00 30.17  ? 258 VAL B CG2 1 
ATOM   5700  N  N   . ILE B 2 259 ? 14.714  -13.000 47.608  1.00 26.57  ? 259 ILE B N   1 
ATOM   5701  C  CA  . ILE B 2 259 ? 15.726  -12.102 47.061  1.00 26.47  ? 259 ILE B CA  1 
ATOM   5702  C  C   . ILE B 2 259 ? 15.426  -11.877 45.585  1.00 29.03  ? 259 ILE B C   1 
ATOM   5703  O  O   . ILE B 2 259 ? 14.577  -12.564 44.996  1.00 25.10  ? 259 ILE B O   1 
ATOM   5704  C  CB  . ILE B 2 259 ? 17.127  -12.725 47.319  1.00 31.13  ? 259 ILE B CB  1 
ATOM   5705  C  CG1 . ILE B 2 259 ? 18.271  -11.758 47.003  1.00 24.79  ? 259 ILE B CG1 1 
ATOM   5706  C  CG2 . ILE B 2 259 ? 17.316  -13.987 46.488  1.00 28.76  ? 259 ILE B CG2 1 
ATOM   5707  C  CD1 . ILE B 2 259 ? 18.148  -10.397 47.742  1.00 27.53  ? 259 ILE B CD1 1 
ATOM   5708  N  N   . ASP B 2 260 ? 16.049  -10.857 45.004  1.00 27.47  ? 260 ASP B N   1 
ATOM   5709  C  CA  . ASP B 2 260 ? 15.733  -10.450 43.640  1.00 27.65  ? 260 ASP B CA  1 
ATOM   5710  C  C   . ASP B 2 260 ? 16.981  -9.843  43.045  1.00 24.83  ? 260 ASP B C   1 
ATOM   5711  O  O   . ASP B 2 260 ? 17.896  -9.418  43.755  1.00 24.39  ? 260 ASP B O   1 
ATOM   5712  C  CB  . ASP B 2 260 ? 14.609  -9.420  43.621  1.00 23.77  ? 260 ASP B CB  1 
ATOM   5713  C  CG  . ASP B 2 260 ? 14.999  -8.128  44.356  1.00 31.22  ? 260 ASP B CG  1 
ATOM   5714  O  OD1 . ASP B 2 260 ? 15.668  -7.261  43.744  1.00 30.59  ? 260 ASP B OD1 1 
ATOM   5715  O  OD2 . ASP B 2 260 ? 14.800  -8.051  45.605  1.00 31.65  ? 260 ASP B OD2 1 
ATOM   5716  N  N   . ASP B 2 261 ? 16.998  -9.812  41.716  1.00 22.80  ? 261 ASP B N   1 
ATOM   5717  C  CA  . ASP B 2 261 ? 18.021  -9.112  40.921  1.00 24.69  ? 261 ASP B CA  1 
ATOM   5718  C  C   . ASP B 2 261 ? 17.214  -8.273  39.927  1.00 23.72  ? 261 ASP B C   1 
ATOM   5719  O  O   . ASP B 2 261 ? 16.941  -8.740  38.816  1.00 21.66  ? 261 ASP B O   1 
ATOM   5720  C  CB  . ASP B 2 261 ? 18.982  -10.109 40.176  1.00 23.07  ? 261 ASP B CB  1 
ATOM   5721  C  CG  . ASP B 2 261 ? 19.962  -9.360  39.276  1.00 22.95  ? 261 ASP B CG  1 
ATOM   5722  O  OD1 . ASP B 2 261 ? 20.632  -8.445  39.814  1.00 26.62  ? 261 ASP B OD1 1 
ATOM   5723  O  OD2 . ASP B 2 261 ? 20.036  -9.630  38.061  1.00 23.31  ? 261 ASP B OD2 1 
ATOM   5724  N  N   . GLN B 2 262 ? 16.805  -7.056  40.325  1.00 22.54  ? 262 GLN B N   1 
ATOM   5725  C  CA  . GLN B 2 262 ? 15.932  -6.253  39.481  1.00 23.85  ? 262 GLN B CA  1 
ATOM   5726  C  C   . GLN B 2 262 ? 16.042  -4.817  39.970  1.00 21.86  ? 262 GLN B C   1 
ATOM   5727  O  O   . GLN B 2 262 ? 16.402  -4.567  41.136  1.00 23.38  ? 262 GLN B O   1 
ATOM   5728  C  CB  . GLN B 2 262 ? 14.474  -6.715  39.539  1.00 25.39  ? 262 GLN B CB  1 
ATOM   5729  C  CG  . GLN B 2 262 ? 13.867  -6.552  40.914  1.00 25.85  ? 262 GLN B CG  1 
ATOM   5730  C  CD  . GLN B 2 262 ? 12.837  -7.608  41.295  1.00 26.59  ? 262 GLN B CD  1 
ATOM   5731  O  OE1 . GLN B 2 262 ? 12.845  -8.721  40.762  1.00 27.54  ? 262 GLN B OE1 1 
ATOM   5732  N  NE2 . GLN B 2 262 ? 11.982  -7.286  42.253  1.00 28.79  ? 262 GLN B NE2 1 
ATOM   5733  N  N   . CYS B 2 263 ? 15.714  -3.901  39.078  1.00 22.24  ? 263 CYS B N   1 
ATOM   5734  C  CA  . CYS B 2 263 ? 15.859  -2.468  39.394  1.00 22.26  ? 263 CYS B CA  1 
ATOM   5735  C  C   . CYS B 2 263 ? 14.723  -1.907  40.250  1.00 25.85  ? 263 CYS B C   1 
ATOM   5736  O  O   . CYS B 2 263 ? 14.851  -0.790  40.771  1.00 24.56  ? 263 CYS B O   1 
ATOM   5737  C  CB  . CYS B 2 263 ? 16.057  -1.675  38.070  1.00 20.87  ? 263 CYS B CB  1 
ATOM   5738  S  SG  . CYS B 2 263 ? 17.888  -1.632  37.717  1.00 21.23  ? 263 CYS B SG  1 
ATOM   5739  N  N   . SER B 2 264 ? 13.608  -2.624  40.378  1.00 23.10  ? 264 SER B N   1 
ATOM   5740  C  CA  . SER B 2 264 ? 12.643  -2.267  41.406  1.00 24.54  ? 264 SER B CA  1 
ATOM   5741  C  C   . SER B 2 264 ? 13.150  -2.592  42.796  1.00 26.69  ? 264 SER B C   1 
ATOM   5742  O  O   . SER B 2 264 ? 12.567  -2.097  43.764  1.00 26.17  ? 264 SER B O   1 
ATOM   5743  C  CB  . SER B 2 264 ? 11.311  -2.995  41.213  1.00 27.44  ? 264 SER B CB  1 
ATOM   5744  O  OG  . SER B 2 264 ? 11.513  -4.402  41.297  1.00 26.16  ? 264 SER B OG  1 
ATOM   5745  N  N   . GLY B 2 265 ? 14.243  -3.363  42.899  1.00 25.57  ? 265 GLY B N   1 
ATOM   5746  C  CA  . GLY B 2 265 ? 14.759  -3.939  44.118  1.00 27.24  ? 265 GLY B CA  1 
ATOM   5747  C  C   . GLY B 2 265 ? 16.267  -3.827  44.271  1.00 25.61  ? 265 GLY B C   1 
ATOM   5748  O  O   . GLY B 2 265 ? 16.803  -2.722  44.292  1.00 24.80  ? 265 GLY B O   1 
ATOM   5749  N  N   . SER B 2 266 ? 16.959  -4.965  44.396  1.00 25.45  ? 266 SER B N   1 
ATOM   5750  C  CA  . SER B 2 266 ? 18.377  -4.944  44.809  1.00 23.12  ? 266 SER B CA  1 
ATOM   5751  C  C   . SER B 2 266 ? 19.264  -4.100  43.894  1.00 25.35  ? 266 SER B C   1 
ATOM   5752  O  O   . SER B 2 266 ? 20.197  -3.417  44.378  1.00 23.18  ? 266 SER B O   1 
ATOM   5753  C  CB  . SER B 2 266 ? 18.907  -6.387  44.869  1.00 23.95  ? 266 SER B CB  1 
ATOM   5754  O  OG  . SER B 2 266 ? 18.858  -6.988  43.561  1.00 24.83  ? 266 SER B OG  1 
ATOM   5755  N  N   . ARG B 2 267 ? 19.033  -4.144  42.566  1.00 23.15  ? 267 ARG B N   1 
ATOM   5756  C  CA  . ARG B 2 267 ? 19.978  -3.471  41.673  1.00 22.55  ? 267 ARG B CA  1 
ATOM   5757  C  C   . ARG B 2 267 ? 19.920  -1.959  41.836  1.00 25.94  ? 267 ARG B C   1 
ATOM   5758  O  O   . ARG B 2 267 ? 20.884  -1.290  41.471  1.00 26.01  ? 267 ARG B O   1 
ATOM   5759  C  CB  . ARG B 2 267 ? 19.746  -3.882  40.206  1.00 22.90  ? 267 ARG B CB  1 
ATOM   5760  C  CG  . ARG B 2 267 ? 20.987  -3.716  39.287  1.00 23.09  ? 267 ARG B CG  1 
ATOM   5761  C  CD  . ARG B 2 267 ? 20.681  -3.980  37.806  1.00 22.29  ? 267 ARG B CD  1 
ATOM   5762  N  NE  . ARG B 2 267 ? 20.361  -5.393  37.551  1.00 19.85  ? 267 ARG B NE  1 
ATOM   5763  C  CZ  . ARG B 2 267 ? 19.177  -5.839  37.132  1.00 23.37  ? 267 ARG B CZ  1 
ATOM   5764  N  NH1 . ARG B 2 267 ? 18.153  -5.028  36.893  1.00 20.39  ? 267 ARG B NH1 1 
ATOM   5765  N  NH2 . ARG B 2 267 ? 18.993  -7.156  36.984  1.00 20.65  ? 267 ARG B NH2 1 
ATOM   5766  N  N   . TYR B 2 268 ? 18.813  -1.421  42.360  1.00 21.86  ? 268 TYR B N   1 
ATOM   5767  C  CA  . TYR B 2 268 ? 18.763  0.022   42.621  1.00 21.71  ? 268 TYR B CA  1 
ATOM   5768  C  C   . TYR B 2 268 ? 19.662  0.424   43.796  1.00 24.13  ? 268 TYR B C   1 
ATOM   5769  O  O   . TYR B 2 268 ? 20.432  1.393   43.709  1.00 25.04  ? 268 TYR B O   1 
ATOM   5770  C  CB  . TYR B 2 268 ? 17.322  0.407   42.877  1.00 22.73  ? 268 TYR B CB  1 
ATOM   5771  C  CG  . TYR B 2 268 ? 17.159  1.780   43.528  1.00 24.55  ? 268 TYR B CG  1 
ATOM   5772  C  CD1 . TYR B 2 268 ? 17.449  2.924   42.813  1.00 25.96  ? 268 TYR B CD1 1 
ATOM   5773  C  CD2 . TYR B 2 268 ? 16.734  1.882   44.857  1.00 22.99  ? 268 TYR B CD2 1 
ATOM   5774  C  CE1 . TYR B 2 268 ? 17.293  4.193   43.404  1.00 27.21  ? 268 TYR B CE1 1 
ATOM   5775  C  CE2 . TYR B 2 268 ? 16.583  3.149   45.468  1.00 26.66  ? 268 TYR B CE2 1 
ATOM   5776  C  CZ  . TYR B 2 268 ? 16.850  4.277   44.693  1.00 28.72  ? 268 TYR B CZ  1 
ATOM   5777  O  OH  . TYR B 2 268 ? 16.689  5.513   45.222  1.00 30.95  ? 268 TYR B OH  1 
ATOM   5778  N  N   . PHE B 2 269 ? 19.558  -0.260  44.934  1.00 22.29  ? 269 PHE B N   1 
ATOM   5779  C  CA  . PHE B 2 269 ? 20.142  0.275   46.162  1.00 23.06  ? 269 PHE B CA  1 
ATOM   5780  C  C   . PHE B 2 269 ? 21.384  -0.446  46.674  1.00 25.54  ? 269 PHE B C   1 
ATOM   5781  O  O   . PHE B 2 269 ? 21.950  0.014   47.667  1.00 26.84  ? 269 PHE B O   1 
ATOM   5782  C  CB  . PHE B 2 269 ? 19.075  0.256   47.263  1.00 21.26  ? 269 PHE B CB  1 
ATOM   5783  C  CG  . PHE B 2 269 ? 18.695  -1.137  47.736  1.00 23.31  ? 269 PHE B CG  1 
ATOM   5784  C  CD1 . PHE B 2 269 ? 19.448  -1.801  48.683  1.00 22.61  ? 269 PHE B CD1 1 
ATOM   5785  C  CD2 . PHE B 2 269 ? 17.526  -1.734  47.262  1.00 24.12  ? 269 PHE B CD2 1 
ATOM   5786  C  CE1 . PHE B 2 269 ? 19.104  -3.091  49.122  1.00 24.36  ? 269 PHE B CE1 1 
ATOM   5787  C  CE2 . PHE B 2 269 ? 17.146  -3.013  47.712  1.00 26.00  ? 269 PHE B CE2 1 
ATOM   5788  C  CZ  . PHE B 2 269 ? 17.938  -3.676  48.624  1.00 23.12  ? 269 PHE B CZ  1 
ATOM   5789  N  N   . TRP B 2 270 ? 21.790  -1.579  46.058  1.00 23.67  ? 270 TRP B N   1 
ATOM   5790  C  CA  . TRP B 2 270 ? 22.620  -2.573  46.753  1.00 24.71  ? 270 TRP B CA  1 
ATOM   5791  C  C   . TRP B 2 270 ? 23.766  -1.971  47.554  1.00 26.47  ? 270 TRP B C   1 
ATOM   5792  O  O   . TRP B 2 270 ? 23.918  -2.267  48.740  1.00 26.14  ? 270 TRP B O   1 
ATOM   5793  C  CB  . TRP B 2 270 ? 23.172  -3.579  45.738  1.00 20.34  ? 270 TRP B CB  1 
ATOM   5794  C  CG  . TRP B 2 270 ? 23.586  -4.898  46.419  1.00 24.51  ? 270 TRP B CG  1 
ATOM   5795  C  CD1 . TRP B 2 270 ? 24.854  -5.391  46.517  1.00 27.57  ? 270 TRP B CD1 1 
ATOM   5796  C  CD2 . TRP B 2 270 ? 22.735  -5.833  47.111  1.00 27.73  ? 270 TRP B CD2 1 
ATOM   5797  N  NE1 . TRP B 2 270 ? 24.837  -6.581  47.219  1.00 31.42  ? 270 TRP B NE1 1 
ATOM   5798  C  CE2 . TRP B 2 270 ? 23.549  -6.854  47.602  1.00 25.18  ? 270 TRP B CE2 1 
ATOM   5799  C  CE3 . TRP B 2 270 ? 21.368  -5.866  47.392  1.00 28.49  ? 270 TRP B CE3 1 
ATOM   5800  C  CZ2 . TRP B 2 270 ? 23.027  -7.971  48.302  1.00 29.66  ? 270 TRP B CZ2 1 
ATOM   5801  C  CZ3 . TRP B 2 270 ? 20.843  -6.945  48.085  1.00 30.01  ? 270 TRP B CZ3 1 
ATOM   5802  C  CH2 . TRP B 2 270 ? 21.676  -7.990  48.540  1.00 29.95  ? 270 TRP B CH2 1 
ATOM   5803  N  N   . ASN B 2 271 ? 24.608  -1.155  46.906  1.00 23.10  ? 271 ASN B N   1 
ATOM   5804  C  CA  . ASN B 2 271 ? 25.819  -0.623  47.557  1.00 22.61  ? 271 ASN B CA  1 
ATOM   5805  C  C   . ASN B 2 271 ? 25.642  0.838   47.978  1.00 21.54  ? 271 ASN B C   1 
ATOM   5806  O  O   . ASN B 2 271 ? 25.082  1.644   47.237  1.00 24.07  ? 271 ASN B O   1 
ATOM   5807  C  CB  . ASN B 2 271 ? 27.015  -0.747  46.627  1.00 23.27  ? 271 ASN B CB  1 
ATOM   5808  C  CG  . ASN B 2 271 ? 26.829  0.072   45.340  1.00 26.63  ? 271 ASN B CG  1 
ATOM   5809  O  OD1 . ASN B 2 271 ? 25.773  -0.013  44.639  1.00 23.15  ? 271 ASN B OD1 1 
ATOM   5810  N  ND2 . ASN B 2 271 ? 27.818  0.863   45.028  1.00 24.44  ? 271 ASN B ND2 1 
ATOM   5811  N  N   . ALA B 2 272 ? 26.112  1.159   49.182  1.00 21.97  ? 272 ALA B N   1 
ATOM   5812  C  CA  . ALA B 2 272 ? 26.308  2.562   49.566  1.00 25.98  ? 272 ALA B CA  1 
ATOM   5813  C  C   . ALA B 2 272 ? 27.673  3.057   49.067  1.00 24.50  ? 272 ALA B C   1 
ATOM   5814  O  O   . ALA B 2 272 ? 28.593  2.272   48.805  1.00 26.23  ? 272 ALA B O   1 
ATOM   5815  C  CB  . ALA B 2 272 ? 26.214  2.681   51.085  1.00 27.80  ? 272 ALA B CB  1 
ATOM   5816  N  N   . SER B 2 273 ? 27.838  4.391   48.967  1.00 24.08  ? 273 SER B N   1 
ATOM   5817  C  CA  . SER B 2 273 ? 29.125  4.909   48.521  1.00 21.55  ? 273 SER B CA  1 
ATOM   5818  C  C   . SER B 2 273 ? 30.231  4.554   49.532  1.00 23.51  ? 273 SER B C   1 
ATOM   5819  O  O   . SER B 2 273 ? 29.976  4.221   50.706  1.00 28.66  ? 273 SER B O   1 
ATOM   5820  C  CB  . SER B 2 273 ? 29.052  6.444   48.352  1.00 24.60  ? 273 SER B CB  1 
ATOM   5821  O  OG  . SER B 2 273 ? 29.041  6.986   49.676  1.00 25.06  ? 273 SER B OG  1 
ATOM   5822  N  N   . LYS B 2 274 ? 31.528  4.648   49.058  1.00 24.67  ? 274 LYS B N   1 
ATOM   5823  C  CA  . LYS B 2 274 ? 32.715  4.444   49.900  1.00 24.12  ? 274 LYS B CA  1 
ATOM   5824  C  C   . LYS B 2 274 ? 33.019  5.750   50.641  1.00 25.53  ? 274 LYS B C   1 
ATOM   5825  O  O   . LYS B 2 274 ? 32.788  6.826   50.083  1.00 27.80  ? 274 LYS B O   1 
ATOM   5826  C  CB  . LYS B 2 274 ? 33.935  4.100   49.039  1.00 27.44  ? 274 LYS B CB  1 
ATOM   5827  C  CG  . LYS B 2 274 ? 33.911  2.706   48.382  1.00 29.51  ? 274 LYS B CG  1 
ATOM   5828  C  CD  . LYS B 2 274 ? 33.559  1.601   49.373  1.00 33.36  ? 274 LYS B CD  1 
ATOM   5829  C  CE  . LYS B 2 274 ? 33.695  0.226   48.672  1.00 34.77  ? 274 LYS B CE  1 
ATOM   5830  N  NZ  . LYS B 2 274 ? 33.156  -0.828  49.528  1.00 36.86  ? 274 LYS B NZ  1 
ATOM   5831  N  N   . PRO B 2 275 ? 33.596  5.686   51.853  1.00 28.45  ? 275 PRO B N   1 
ATOM   5832  C  CA  . PRO B 2 275 ? 34.015  6.926   52.533  1.00 27.82  ? 275 PRO B CA  1 
ATOM   5833  C  C   . PRO B 2 275 ? 35.104  7.573   51.695  1.00 28.76  ? 275 PRO B C   1 
ATOM   5834  O  O   . PRO B 2 275 ? 35.955  6.886   51.131  1.00 26.63  ? 275 PRO B O   1 
ATOM   5835  C  CB  . PRO B 2 275 ? 34.538  6.447   53.888  1.00 25.25  ? 275 PRO B CB  1 
ATOM   5836  C  CG  . PRO B 2 275 ? 34.998  5.030   53.647  1.00 25.75  ? 275 PRO B CG  1 
ATOM   5837  C  CD  . PRO B 2 275 ? 34.043  4.482   52.573  1.00 22.86  ? 275 PRO B CD  1 
ATOM   5838  N  N   . GLU B 2 276 ? 35.000  8.885   51.534  1.00 25.29  ? 276 GLU B N   1 
ATOM   5839  C  CA  . GLU B 2 276 ? 35.753  9.570   50.497  1.00 26.56  ? 276 GLU B CA  1 
ATOM   5840  C  C   . GLU B 2 276 ? 35.551  11.055  50.691  1.00 28.46  ? 276 GLU B C   1 
ATOM   5841  O  O   . GLU B 2 276 ? 34.420  11.501  50.974  1.00 28.43  ? 276 GLU B O   1 
ATOM   5842  C  CB  . GLU B 2 276 ? 35.312  9.077   49.098  1.00 26.65  ? 276 GLU B CB  1 
ATOM   5843  C  CG  . GLU B 2 276 ? 35.669  9.959   47.963  1.00 28.87  ? 276 GLU B CG  1 
ATOM   5844  C  CD  . GLU B 2 276 ? 37.157  10.106  47.773  1.00 31.18  ? 276 GLU B CD  1 
ATOM   5845  O  OE1 . GLU B 2 276 ? 37.906  9.111   47.883  1.00 29.86  ? 276 GLU B OE1 1 
ATOM   5846  O  OE2 . GLU B 2 276 ? 37.586  11.265  47.533  1.00 33.05  ? 276 GLU B OE2 1 
ATOM   5847  N  N   . GLY B 2 277 ? 36.656  11.809  50.619  1.00 25.60  ? 277 GLY B N   1 
ATOM   5848  C  CA  . GLY B 2 277 ? 36.588  13.227  50.934  1.00 24.00  ? 277 GLY B CA  1 
ATOM   5849  C  C   . GLY B 2 277 ? 36.102  14.119  49.802  1.00 27.53  ? 277 GLY B C   1 
ATOM   5850  O  O   . GLY B 2 277 ? 35.587  15.221  50.061  1.00 26.89  ? 277 GLY B O   1 
ATOM   5851  N  N   . ASP B 2 278 ? 36.274  13.686  48.560  1.00 25.56  ? 278 ASP B N   1 
ATOM   5852  C  CA  . ASP B 2 278 ? 35.801  14.408  47.374  1.00 24.35  ? 278 ASP B CA  1 
ATOM   5853  C  C   . ASP B 2 278 ? 34.390  13.905  47.086  1.00 26.00  ? 278 ASP B C   1 
ATOM   5854  O  O   . ASP B 2 278 ? 34.214  12.804  46.522  1.00 22.63  ? 278 ASP B O   1 
ATOM   5855  C  CB  . ASP B 2 278 ? 36.728  14.153  46.193  1.00 25.81  ? 278 ASP B CB  1 
ATOM   5856  C  CG  . ASP B 2 278 ? 36.323  14.949  44.955  1.00 27.47  ? 278 ASP B CG  1 
ATOM   5857  O  OD1 . ASP B 2 278 ? 35.105  15.195  44.733  1.00 25.36  ? 278 ASP B OD1 1 
ATOM   5858  O  OD2 . ASP B 2 278 ? 37.212  15.272  44.159  1.00 29.32  ? 278 ASP B OD2 1 
ATOM   5859  N  N   . VAL B 2 279 ? 33.378  14.697  47.434  1.00 22.92  ? 279 VAL B N   1 
ATOM   5860  C  CA  . VAL B 2 279 ? 32.024  14.157  47.358  1.00 23.38  ? 279 VAL B CA  1 
ATOM   5861  C  C   . VAL B 2 279 ? 31.616  13.805  45.918  1.00 24.17  ? 279 VAL B C   1 
ATOM   5862  O  O   . VAL B 2 279 ? 30.855  12.856  45.718  1.00 24.47  ? 279 VAL B O   1 
ATOM   5863  C  CB  . VAL B 2 279 ? 31.020  15.085  48.021  1.00 23.79  ? 279 VAL B CB  1 
ATOM   5864  C  CG1 . VAL B 2 279 ? 30.825  16.392  47.231  1.00 22.34  ? 279 VAL B CG1 1 
ATOM   5865  C  CG2 . VAL B 2 279 ? 29.695  14.377  48.238  1.00 25.07  ? 279 VAL B CG2 1 
ATOM   5866  N  N   . ILE B 2 280 ? 32.067  14.554  44.892  1.00 19.90  ? 280 ILE B N   1 
ATOM   5867  C  CA  . ILE B 2 280 ? 31.761  14.175  43.512  1.00 21.30  ? 280 ILE B CA  1 
ATOM   5868  C  C   . ILE B 2 280 ? 32.317  12.788  43.162  1.00 21.99  ? 280 ILE B C   1 
ATOM   5869  O  O   . ILE B 2 280 ? 31.647  11.978  42.508  1.00 23.55  ? 280 ILE B O   1 
ATOM   5870  C  CB  . ILE B 2 280 ? 32.286  15.252  42.534  1.00 23.50  ? 280 ILE B CB  1 
ATOM   5871  C  CG1 . ILE B 2 280 ? 31.519  16.548  42.791  1.00 23.09  ? 280 ILE B CG1 1 
ATOM   5872  C  CG2 . ILE B 2 280 ? 32.125  14.828  41.064  1.00 23.36  ? 280 ILE B CG2 1 
ATOM   5873  C  CD1 . ILE B 2 280 ? 30.058  16.538  42.456  1.00 24.18  ? 280 ILE B CD1 1 
ATOM   5874  N  N   . LYS B 2 281 ? 33.563  12.512  43.543  1.00 21.69  ? 281 LYS B N   1 
ATOM   5875  C  CA  . LYS B 2 281 ? 34.105  11.166  43.369  1.00 24.11  ? 281 LYS B CA  1 
ATOM   5876  C  C   . LYS B 2 281 ? 33.268  10.122  44.119  1.00 24.74  ? 281 LYS B C   1 
ATOM   5877  O  O   . LYS B 2 281 ? 32.998  9.038   43.568  1.00 25.15  ? 281 LYS B O   1 
ATOM   5878  C  CB  . LYS B 2 281 ? 35.577  11.135  43.867  1.00 25.78  ? 281 LYS B CB  1 
ATOM   5879  C  CG  . LYS B 2 281 ? 36.295  9.736   43.713  1.00 26.85  ? 281 LYS B CG  1 
ATOM   5880  C  CD  . LYS B 2 281 ? 37.783  9.878   44.108  1.00 29.86  ? 281 LYS B CD  1 
ATOM   5881  C  CE  . LYS B 2 281 ? 38.602  8.602   43.941  1.00 36.44  ? 281 LYS B CE  1 
ATOM   5882  N  NZ  . LYS B 2 281 ? 38.147  7.611   44.982  1.00 38.02  ? 281 LYS B NZ  1 
ATOM   5883  N  N   . ALA B 2 282 ? 32.867  10.413  45.371  1.00 20.73  ? 282 ALA B N   1 
ATOM   5884  C  CA  . ALA B 2 282 ? 32.075  9.427   46.150  1.00 20.91  ? 282 ALA B CA  1 
ATOM   5885  C  C   . ALA B 2 282 ? 30.785  9.066   45.404  1.00 27.17  ? 282 ALA B C   1 
ATOM   5886  O  O   . ALA B 2 282 ? 30.397  7.881   45.286  1.00 25.46  ? 282 ALA B O   1 
ATOM   5887  C  CB  . ALA B 2 282 ? 31.729  10.019  47.521  1.00 22.74  ? 282 ALA B CB  1 
ATOM   5888  N  N   . ILE B 2 283 ? 30.093  10.094  44.908  1.00 23.58  ? 283 ILE B N   1 
ATOM   5889  C  CA  . ILE B 2 283 ? 28.847  9.890   44.155  1.00 23.43  ? 283 ILE B CA  1 
ATOM   5890  C  C   . ILE B 2 283 ? 29.109  9.172   42.843  1.00 24.12  ? 283 ILE B C   1 
ATOM   5891  O  O   . ILE B 2 283 ? 28.481  8.142   42.567  1.00 24.15  ? 283 ILE B O   1 
ATOM   5892  C  CB  . ILE B 2 283 ? 28.148  11.229  43.908  1.00 24.15  ? 283 ILE B CB  1 
ATOM   5893  C  CG1 . ILE B 2 283 ? 27.686  11.866  45.209  1.00 23.54  ? 283 ILE B CG1 1 
ATOM   5894  C  CG2 . ILE B 2 283 ? 26.918  11.030  43.021  1.00 22.92  ? 283 ILE B CG2 1 
ATOM   5895  C  CD1 . ILE B 2 283 ? 27.371  13.385  44.984  1.00 22.21  ? 283 ILE B CD1 1 
ATOM   5896  N  N   . ALA B 2 284 ? 30.002  9.705   41.998  1.00 21.13  ? 284 ALA B N   1 
ATOM   5897  C  CA  . ALA B 2 284 ? 30.215  9.095   40.686  1.00 20.59  ? 284 ALA B CA  1 
ATOM   5898  C  C   . ALA B 2 284 ? 30.638  7.632   40.834  1.00 23.56  ? 284 ALA B C   1 
ATOM   5899  O  O   . ALA B 2 284 ? 30.206  6.757   40.057  1.00 24.35  ? 284 ALA B O   1 
ATOM   5900  C  CB  . ALA B 2 284 ? 31.253  9.871   39.895  1.00 24.03  ? 284 ALA B CB  1 
ATOM   5901  N  N   . GLU B 2 285 ? 31.520  7.353   41.782  1.00 21.54  ? 285 GLU B N   1 
ATOM   5902  C  CA  . GLU B 2 285 ? 31.998  5.968   41.892  1.00 21.79  ? 285 GLU B CA  1 
ATOM   5903  C  C   . GLU B 2 285 ? 30.982  5.030   42.470  1.00 24.45  ? 285 GLU B C   1 
ATOM   5904  O  O   . GLU B 2 285 ? 31.078  3.822   42.189  1.00 23.18  ? 285 GLU B O   1 
ATOM   5905  C  CB  . GLU B 2 285 ? 33.281  5.888   42.706  1.00 21.90  ? 285 GLU B CB  1 
ATOM   5906  C  CG  . GLU B 2 285 ? 34.344  6.648   41.972  1.00 23.85  ? 285 GLU B CG  1 
ATOM   5907  C  CD  . GLU B 2 285 ? 35.734  6.442   42.440  1.00 30.79  ? 285 GLU B CD  1 
ATOM   5908  O  OE1 . GLU B 2 285 ? 35.967  5.956   43.560  1.00 32.83  ? 285 GLU B OE1 1 
ATOM   5909  O  OE2 . GLU B 2 285 ? 36.631  6.824   41.656  1.00 27.40  ? 285 GLU B OE2 1 
ATOM   5910  N  N   . ARG B 2 286 ? 30.098  5.516   43.361  1.00 22.96  ? 286 ARG B N   1 
ATOM   5911  C  CA  . ARG B 2 286 ? 29.017  4.665   43.862  1.00 23.05  ? 286 ARG B CA  1 
ATOM   5912  C  C   . ARG B 2 286 ? 28.249  4.040   42.691  1.00 22.43  ? 286 ARG B C   1 
ATOM   5913  O  O   . ARG B 2 286 ? 27.908  2.847   42.724  1.00 23.05  ? 286 ARG B O   1 
ATOM   5914  C  CB  . ARG B 2 286 ? 28.073  5.477   44.742  1.00 22.82  ? 286 ARG B CB  1 
ATOM   5915  C  CG  . ARG B 2 286 ? 27.006  4.607   45.411  1.00 22.71  ? 286 ARG B CG  1 
ATOM   5916  C  CD  . ARG B 2 286 ? 25.720  4.572   44.573  1.00 23.76  ? 286 ARG B CD  1 
ATOM   5917  N  NE  . ARG B 2 286 ? 24.880  3.463   45.015  1.00 22.41  ? 286 ARG B NE  1 
ATOM   5918  C  CZ  . ARG B 2 286 ? 23.759  3.098   44.409  1.00 21.50  ? 286 ARG B CZ  1 
ATOM   5919  N  NH1 . ARG B 2 286 ? 23.327  3.722   43.319  1.00 21.66  ? 286 ARG B NH1 1 
ATOM   5920  N  NH2 . ARG B 2 286 ? 23.105  2.022   44.861  1.00 22.19  ? 286 ARG B NH2 1 
ATOM   5921  N  N   . TYR B 2 287 ? 27.953  4.828   41.655  1.00 20.61  ? 287 TYR B N   1 
ATOM   5922  C  CA  . TYR B 2 287 ? 27.189  4.298   40.528  1.00 20.97  ? 287 TYR B CA  1 
ATOM   5923  C  C   . TYR B 2 287 ? 28.043  3.392   39.664  1.00 23.45  ? 287 TYR B C   1 
ATOM   5924  O  O   . TYR B 2 287 ? 27.531  2.365   39.175  1.00 22.95  ? 287 TYR B O   1 
ATOM   5925  C  CB  . TYR B 2 287 ? 26.568  5.434   39.701  1.00 24.41  ? 287 TYR B CB  1 
ATOM   5926  C  CG  . TYR B 2 287 ? 25.491  6.121   40.509  1.00 22.95  ? 287 TYR B CG  1 
ATOM   5927  C  CD1 . TYR B 2 287 ? 24.180  5.628   40.545  1.00 20.63  ? 287 TYR B CD1 1 
ATOM   5928  C  CD2 . TYR B 2 287 ? 25.790  7.241   41.290  1.00 23.46  ? 287 TYR B CD2 1 
ATOM   5929  C  CE1 . TYR B 2 287 ? 23.171  6.263   41.277  1.00 23.46  ? 287 TYR B CE1 1 
ATOM   5930  C  CE2 . TYR B 2 287 ? 24.802  7.869   42.048  1.00 25.06  ? 287 TYR B CE2 1 
ATOM   5931  C  CZ  . TYR B 2 287 ? 23.493  7.381   42.031  1.00 22.81  ? 287 TYR B CZ  1 
ATOM   5932  O  OH  . TYR B 2 287 ? 22.506  7.959   42.789  1.00 23.58  ? 287 TYR B OH  1 
ATOM   5933  N  N   . CYS B 2 288 ? 29.333  3.759   39.433  1.00 20.67  ? 288 CYS B N   1 
ATOM   5934  C  CA  . CYS B 2 288 ? 30.197  2.865   38.654  1.00 22.84  ? 288 CYS B CA  1 
ATOM   5935  C  C   . CYS B 2 288 ? 30.389  1.546   39.383  1.00 24.06  ? 288 CYS B C   1 
ATOM   5936  O  O   . CYS B 2 288 ? 30.644  0.529   38.727  1.00 23.11  ? 288 CYS B O   1 
ATOM   5937  C  CB  . CYS B 2 288 ? 31.579  3.442   38.413  1.00 21.85  ? 288 CYS B CB  1 
ATOM   5938  S  SG  . CYS B 2 288 ? 31.543  4.965   37.392  1.00 25.76  ? 288 CYS B SG  1 
ATOM   5939  N  N   . ASP B 2 289 ? 30.378  1.573   40.732  1.00 21.50  ? 289 ASP B N   1 
ATOM   5940  C  CA  . ASP B 2 289 ? 30.664  0.369   41.506  1.00 22.23  ? 289 ASP B CA  1 
ATOM   5941  C  C   . ASP B 2 289 ? 29.429  -0.484  41.757  1.00 23.21  ? 289 ASP B C   1 
ATOM   5942  O  O   . ASP B 2 289 ? 29.557  -1.603  42.306  1.00 25.64  ? 289 ASP B O   1 
ATOM   5943  C  CB  . ASP B 2 289 ? 31.305  0.755   42.828  1.00 25.96  ? 289 ASP B CB  1 
ATOM   5944  C  CG  . ASP B 2 289 ? 32.739  1.278   42.663  1.00 27.40  ? 289 ASP B CG  1 
ATOM   5945  O  OD1 . ASP B 2 289 ? 33.352  1.051   41.601  1.00 29.81  ? 289 ASP B OD1 1 
ATOM   5946  O  OD2 . ASP B 2 289 ? 33.258  1.888   43.634  1.00 26.22  ? 289 ASP B OD2 1 
ATOM   5947  N  N   . ARG B 2 290 ? 28.248  0.051   41.449  1.00 23.35  ? 290 ARG B N   1 
ATOM   5948  C  CA  . ARG B 2 290 ? 26.984  -0.632  41.702  1.00 24.20  ? 290 ARG B CA  1 
ATOM   5949  C  C   . ARG B 2 290 ? 26.906  -1.933  40.885  1.00 23.01  ? 290 ARG B C   1 
ATOM   5950  O  O   . ARG B 2 290 ? 27.481  -2.022  39.777  1.00 22.72  ? 290 ARG B O   1 
ATOM   5951  C  CB  . ARG B 2 290 ? 25.837  0.277   41.275  1.00 22.91  ? 290 ARG B CB  1 
ATOM   5952  C  CG  . ARG B 2 290 ? 24.441  -0.187  41.727  1.00 22.64  ? 290 ARG B CG  1 
ATOM   5953  C  CD  . ARG B 2 290 ? 23.376  0.428   40.845  1.00 22.62  ? 290 ARG B CD  1 
ATOM   5954  N  NE  . ARG B 2 290 ? 23.190  -0.286  39.565  1.00 21.72  ? 290 ARG B NE  1 
ATOM   5955  C  CZ  . ARG B 2 290 ? 22.217  0.015   38.714  1.00 21.84  ? 290 ARG B CZ  1 
ATOM   5956  N  NH1 . ARG B 2 290 ? 21.409  1.039   38.928  1.00 23.80  ? 290 ARG B NH1 1 
ATOM   5957  N  NH2 . ARG B 2 290 ? 22.031  -0.734  37.646  1.00 22.11  ? 290 ARG B NH2 1 
ATOM   5958  N  N   . PRO B 2 291 ? 26.170  -2.959  41.350  1.00 25.22  ? 291 PRO B N   1 
ATOM   5959  C  CA  . PRO B 2 291 ? 25.941  -4.103  40.436  1.00 21.58  ? 291 PRO B CA  1 
ATOM   5960  C  C   . PRO B 2 291 ? 25.426  -3.611  39.101  1.00 23.66  ? 291 PRO B C   1 
ATOM   5961  O  O   . PRO B 2 291 ? 24.510  -2.775  39.027  1.00 26.01  ? 291 PRO B O   1 
ATOM   5962  C  CB  . PRO B 2 291 ? 24.889  -4.962  41.147  1.00 23.38  ? 291 PRO B CB  1 
ATOM   5963  C  CG  . PRO B 2 291 ? 24.862  -4.482  42.571  1.00 28.74  ? 291 PRO B CG  1 
ATOM   5964  C  CD  . PRO B 2 291 ? 25.478  -3.119  42.656  1.00 25.34  ? 291 PRO B CD  1 
ATOM   5965  N  N   . ALA B 2 292 ? 26.006  -4.134  38.042  1.00 21.40  ? 292 ALA B N   1 
ATOM   5966  C  CA  . ALA B 2 292 ? 25.839  -3.546  36.717  1.00 21.82  ? 292 ALA B CA  1 
ATOM   5967  C  C   . ALA B 2 292 ? 24.569  -4.010  36.010  1.00 23.17  ? 292 ALA B C   1 
ATOM   5968  O  O   . ALA B 2 292 ? 24.242  -5.226  36.020  1.00 23.89  ? 292 ALA B O   1 
ATOM   5969  C  CB  . ALA B 2 292 ? 27.059  -3.856  35.838  1.00 21.86  ? 292 ALA B CB  1 
ATOM   5970  N  N   . CYS B 2 293 ? 23.888  -3.044  35.342  1.00 22.67  ? 293 CYS B N   1 
ATOM   5971  C  CA  . CYS B 2 293 ? 22.957  -3.348  34.257  1.00 21.61  ? 293 CYS B CA  1 
ATOM   5972  C  C   . CYS B 2 293 ? 23.653  -4.269  33.245  1.00 21.11  ? 293 CYS B C   1 
ATOM   5973  O  O   . CYS B 2 293 ? 24.868  -4.134  33.039  1.00 22.01  ? 293 CYS B O   1 
ATOM   5974  C  CB  . CYS B 2 293 ? 22.586  -2.037  33.455  1.00 21.50  ? 293 CYS B CB  1 
ATOM   5975  S  SG  . CYS B 2 293 ? 21.352  -2.241  32.156  1.00 26.20  ? 293 CYS B SG  1 
ATOM   5976  N  N   . PRO B 2 294 ? 22.945  -5.233  32.630  1.00 21.48  ? 294 PRO B N   1 
ATOM   5977  C  CA  . PRO B 2 294 ? 23.567  -6.042  31.537  1.00 19.65  ? 294 PRO B CA  1 
ATOM   5978  C  C   . PRO B 2 294 ? 24.280  -5.189  30.496  1.00 22.17  ? 294 PRO B C   1 
ATOM   5979  O  O   . PRO B 2 294 ? 25.351  -5.555  30.001  1.00 24.38  ? 294 PRO B O   1 
ATOM   5980  C  CB  . PRO B 2 294 ? 22.368  -6.795  30.929  1.00 21.19  ? 294 PRO B CB  1 
ATOM   5981  C  CG  . PRO B 2 294 ? 21.447  -6.991  32.113  1.00 21.96  ? 294 PRO B CG  1 
ATOM   5982  C  CD  . PRO B 2 294 ? 21.576  -5.699  32.956  1.00 20.67  ? 294 PRO B CD  1 
ATOM   5983  N  N   . THR B 2 295 ? 23.682  -4.057  30.142  1.00 18.49  ? 295 THR B N   1 
ATOM   5984  C  CA  . THR B 2 295 ? 24.282  -3.126  29.203  1.00 19.03  ? 295 THR B CA  1 
ATOM   5985  C  C   . THR B 2 295 ? 25.666  -2.678  29.632  1.00 23.83  ? 295 THR B C   1 
ATOM   5986  O  O   . THR B 2 295 ? 26.488  -2.343  28.765  1.00 21.19  ? 295 THR B O   1 
ATOM   5987  C  CB  . THR B 2 295 ? 23.380  -1.902  29.068  1.00 21.94  ? 295 THR B CB  1 
ATOM   5988  O  OG1 . THR B 2 295 ? 22.209  -2.328  28.351  1.00 27.50  ? 295 THR B OG1 1 
ATOM   5989  C  CG2 . THR B 2 295 ? 24.037  -0.740  28.256  1.00 25.72  ? 295 THR B CG2 1 
ATOM   5990  N  N   . LYS B 2 296 ? 25.905  -2.571  30.946  1.00 19.69  ? 296 LYS B N   1 
ATOM   5991  C  CA  . LYS B 2 296 ? 27.170  -2.059  31.480  1.00 19.81  ? 296 LYS B CA  1 
ATOM   5992  C  C   . LYS B 2 296 ? 28.086  -3.187  31.950  1.00 22.89  ? 296 LYS B C   1 
ATOM   5993  O  O   . LYS B 2 296 ? 29.122  -2.947  32.593  1.00 21.31  ? 296 LYS B O   1 
ATOM   5994  C  CB  . LYS B 2 296 ? 26.896  -1.024  32.592  1.00 21.23  ? 296 LYS B CB  1 
ATOM   5995  C  CG  . LYS B 2 296 ? 26.089  0.168   32.132  1.00 21.65  ? 296 LYS B CG  1 
ATOM   5996  C  CD  . LYS B 2 296 ? 26.223  1.283   33.152  1.00 18.67  ? 296 LYS B CD  1 
ATOM   5997  C  CE  . LYS B 2 296 ? 25.278  2.467   32.815  1.00 20.68  ? 296 LYS B CE  1 
ATOM   5998  N  NZ  . LYS B 2 296 ? 25.824  3.349   31.717  1.00 20.93  ? 296 LYS B NZ  1 
ATOM   5999  N  N   . ASP B 2 297 ? 27.787  -4.412  31.540  1.00 23.02  ? 297 ASP B N   1 
ATOM   6000  C  CA  . ASP B 2 297 ? 28.477  -5.567  32.109  1.00 22.09  ? 297 ASP B CA  1 
ATOM   6001  C  C   . ASP B 2 297 ? 29.282  -6.262  31.010  1.00 22.40  ? 297 ASP B C   1 
ATOM   6002  O  O   . ASP B 2 297 ? 28.847  -7.259  30.403  1.00 22.35  ? 297 ASP B O   1 
ATOM   6003  C  CB  . ASP B 2 297 ? 27.493  -6.451  32.783  1.00 21.34  ? 297 ASP B CB  1 
ATOM   6004  C  CG  . ASP B 2 297 ? 28.139  -7.307  33.842  1.00 24.33  ? 297 ASP B CG  1 
ATOM   6005  O  OD1 . ASP B 2 297 ? 29.141  -6.821  34.494  1.00 22.82  ? 297 ASP B OD1 1 
ATOM   6006  O  OD2 . ASP B 2 297 ? 27.706  -8.512  34.003  1.00 22.92  ? 297 ASP B OD2 1 
ATOM   6007  N  N   . TYR B 2 298 ? 30.443  -5.670  30.706  1.00 21.63  ? 298 TYR B N   1 
ATOM   6008  C  CA  . TYR B 2 298 ? 31.374  -6.190  29.718  1.00 20.62  ? 298 TYR B CA  1 
ATOM   6009  C  C   . TYR B 2 298 ? 32.736  -5.584  30.015  1.00 22.51  ? 298 TYR B C   1 
ATOM   6010  O  O   . TYR B 2 298 ? 32.802  -4.486  30.603  1.00 20.33  ? 298 TYR B O   1 
ATOM   6011  C  CB  . TYR B 2 298 ? 30.911  -5.907  28.267  1.00 19.65  ? 298 TYR B CB  1 
ATOM   6012  C  CG  . TYR B 2 298 ? 30.845  -4.451  27.907  1.00 19.07  ? 298 TYR B CG  1 
ATOM   6013  C  CD1 . TYR B 2 298 ? 31.974  -3.814  27.385  1.00 22.46  ? 298 TYR B CD1 1 
ATOM   6014  C  CD2 . TYR B 2 298 ? 29.657  -3.747  28.124  1.00 20.27  ? 298 TYR B CD2 1 
ATOM   6015  C  CE1 . TYR B 2 298 ? 31.929  -2.420  27.072  1.00 20.30  ? 298 TYR B CE1 1 
ATOM   6016  C  CE2 . TYR B 2 298 ? 29.575  -2.365  27.750  1.00 19.37  ? 298 TYR B CE2 1 
ATOM   6017  C  CZ  . TYR B 2 298 ? 30.728  -1.756  27.265  1.00 22.74  ? 298 TYR B CZ  1 
ATOM   6018  O  OH  . TYR B 2 298 ? 30.745  -0.410  26.865  1.00 20.96  ? 298 TYR B OH  1 
ATOM   6019  N  N   . PRO B 2 299 ? 33.828  -6.260  29.660  1.00 21.41  ? 299 PRO B N   1 
ATOM   6020  C  CA  . PRO B 2 299 ? 33.906  -7.566  28.992  1.00 19.93  ? 299 PRO B CA  1 
ATOM   6021  C  C   . PRO B 2 299 ? 33.464  -8.705  29.898  1.00 24.02  ? 299 PRO B C   1 
ATOM   6022  O  O   . PRO B 2 299 ? 33.016  -9.727  29.358  1.00 22.50  ? 299 PRO B O   1 
ATOM   6023  C  CB  . PRO B 2 299 ? 35.398  -7.723  28.663  1.00 22.68  ? 299 PRO B CB  1 
ATOM   6024  C  CG  . PRO B 2 299 ? 36.103  -6.878  29.728  1.00 22.58  ? 299 PRO B CG  1 
ATOM   6025  C  CD  . PRO B 2 299 ? 35.177  -5.683  29.867  1.00 24.33  ? 299 PRO B CD  1 
ATOM   6026  N  N   . ALA B 2 300 ? 33.644  -8.579  31.216  1.00 23.65  ? 300 ALA B N   1 
ATOM   6027  C  CA  . ALA B 2 300 ? 33.256  -9.671  32.112  1.00 22.81  ? 300 ALA B CA  1 
ATOM   6028  C  C   . ALA B 2 300 ? 31.763  -9.645  32.409  1.00 23.92  ? 300 ALA B C   1 
ATOM   6029  O  O   . ALA B 2 300 ? 31.156  -8.590  32.599  1.00 23.88  ? 300 ALA B O   1 
ATOM   6030  C  CB  . ALA B 2 300 ? 34.045  -9.598  33.395  1.00 24.30  ? 300 ALA B CB  1 
ATOM   6031  N  N   . HIS B 2 301 ? 31.167  -10.834 32.530  1.00 22.94  ? 301 HIS B N   1 
ATOM   6032  C  CA  . HIS B 2 301 ? 29.820  -10.917 33.073  1.00 22.36  ? 301 HIS B CA  1 
ATOM   6033  C  C   . HIS B 2 301 ? 29.869  -10.940 34.612  1.00 23.21  ? 301 HIS B C   1 
ATOM   6034  O  O   . HIS B 2 301 ? 29.602  -11.966 35.253  1.00 22.45  ? 301 HIS B O   1 
ATOM   6035  C  CB  . HIS B 2 301 ? 29.132  -12.198 32.581  1.00 24.08  ? 301 HIS B CB  1 
ATOM   6036  C  CG  . HIS B 2 301 ? 28.708  -12.204 31.134  1.00 26.70  ? 301 HIS B CG  1 
ATOM   6037  N  ND1 . HIS B 2 301 ? 27.698  -11.395 30.639  1.00 25.29  ? 301 HIS B ND1 1 
ATOM   6038  C  CD2 . HIS B 2 301 ? 29.090  -13.004 30.109  1.00 24.76  ? 301 HIS B CD2 1 
ATOM   6039  C  CE1 . HIS B 2 301 ? 27.509  -11.672 29.350  1.00 28.21  ? 301 HIS B CE1 1 
ATOM   6040  N  NE2 . HIS B 2 301 ? 28.343  -12.641 29.008  1.00 26.53  ? 301 HIS B NE2 1 
ATOM   6041  N  N   . THR B 2 302 ? 30.188  -9.794  35.239  1.00 22.06  ? 302 THR B N   1 
ATOM   6042  C  CA  . THR B 2 302 ? 30.214  -9.762  36.704  1.00 22.52  ? 302 THR B CA  1 
ATOM   6043  C  C   . THR B 2 302 ? 28.843  -10.001 37.312  1.00 23.56  ? 302 THR B C   1 
ATOM   6044  O  O   . THR B 2 302 ? 28.748  -10.414 38.479  1.00 26.94  ? 302 THR B O   1 
ATOM   6045  C  CB  . THR B 2 302 ? 30.719  -8.415  37.241  1.00 25.28  ? 302 THR B CB  1 
ATOM   6046  O  OG1 . THR B 2 302 ? 29.745  -7.419  36.988  1.00 26.09  ? 302 THR B OG1 1 
ATOM   6047  C  CG2 . THR B 2 302 ? 32.060  -7.977  36.647  1.00 26.21  ? 302 THR B CG2 1 
ATOM   6048  N  N   . ARG B 2 303 ? 27.794  -9.726  36.549  1.00 22.75  ? 303 ARG B N   1 
ATOM   6049  C  CA  . ARG B 2 303 ? 26.431  -9.966  36.980  1.00 23.40  ? 303 ARG B CA  1 
ATOM   6050  C  C   . ARG B 2 303 ? 26.212  -11.425 37.356  1.00 25.02  ? 303 ARG B C   1 
ATOM   6051  O  O   . ARG B 2 303 ? 25.502  -11.728 38.327  1.00 24.57  ? 303 ARG B O   1 
ATOM   6052  C  CB  . ARG B 2 303 ? 25.464  -9.564  35.874  1.00 25.06  ? 303 ARG B CB  1 
ATOM   6053  C  CG  . ARG B 2 303 ? 23.999  -9.809  36.239  1.00 27.23  ? 303 ARG B CG  1 
ATOM   6054  C  CD  . ARG B 2 303 ? 23.127  -9.137  35.179  1.00 21.24  ? 303 ARG B CD  1 
ATOM   6055  N  NE  . ARG B 2 303 ? 21.727  -9.418  35.474  1.00 25.67  ? 303 ARG B NE  1 
ATOM   6056  C  CZ  . ARG B 2 303 ? 20.905  -10.119 34.699  1.00 25.37  ? 303 ARG B CZ  1 
ATOM   6057  N  NH1 . ARG B 2 303 ? 21.223  -10.434 33.427  1.00 24.31  ? 303 ARG B NH1 1 
ATOM   6058  N  NH2 . ARG B 2 303 ? 19.729  -10.495 35.193  1.00 24.38  ? 303 ARG B NH2 1 
ATOM   6059  N  N   . PHE B 2 304 ? 26.822  -12.335 36.620  1.00 24.43  ? 304 PHE B N   1 
ATOM   6060  C  CA  . PHE B 2 304 ? 26.614  -13.751 36.924  1.00 22.85  ? 304 PHE B CA  1 
ATOM   6061  C  C   . PHE B 2 304 ? 27.068  -14.092 38.350  1.00 24.64  ? 304 PHE B C   1 
ATOM   6062  O  O   . PHE B 2 304 ? 26.440  -14.914 39.040  1.00 28.11  ? 304 PHE B O   1 
ATOM   6063  C  CB  . PHE B 2 304 ? 27.362  -14.650 35.913  1.00 25.67  ? 304 PHE B CB  1 
ATOM   6064  C  CG  . PHE B 2 304 ? 26.860  -14.542 34.471  1.00 26.54  ? 304 PHE B CG  1 
ATOM   6065  C  CD1 . PHE B 2 304 ? 25.862  -13.647 34.115  1.00 24.44  ? 304 PHE B CD1 1 
ATOM   6066  C  CD2 . PHE B 2 304 ? 27.393  -15.383 33.493  1.00 27.63  ? 304 PHE B CD2 1 
ATOM   6067  C  CE1 . PHE B 2 304 ? 25.421  -13.526 32.794  1.00 28.80  ? 304 PHE B CE1 1 
ATOM   6068  C  CE2 . PHE B 2 304 ? 26.923  -15.311 32.141  1.00 29.97  ? 304 PHE B CE2 1 
ATOM   6069  C  CZ  . PHE B 2 304 ? 25.935  -14.361 31.814  1.00 30.57  ? 304 PHE B CZ  1 
ATOM   6070  N  N   . ASP B 2 305 ? 28.224  -13.580 38.777  1.00 26.21  ? 305 ASP B N   1 
ATOM   6071  C  CA  . ASP B 2 305 ? 28.678  -13.883 40.147  1.00 26.52  ? 305 ASP B CA  1 
ATOM   6072  C  C   . ASP B 2 305 ? 27.815  -13.169 41.186  1.00 28.41  ? 305 ASP B C   1 
ATOM   6073  O  O   . ASP B 2 305 ? 27.596  -13.699 42.302  1.00 26.81  ? 305 ASP B O   1 
ATOM   6074  C  CB  . ASP B 2 305 ? 30.151  -13.483 40.354  1.00 31.83  ? 305 ASP B CB  1 
ATOM   6075  C  CG  . ASP B 2 305 ? 31.121  -14.164 39.396  1.00 39.82  ? 305 ASP B CG  1 
ATOM   6076  O  OD1 . ASP B 2 305 ? 31.010  -15.400 39.188  1.00 37.24  ? 305 ASP B OD1 1 
ATOM   6077  O  OD2 . ASP B 2 305 ? 31.981  -13.432 38.824  1.00 40.12  ? 305 ASP B OD2 1 
ATOM   6078  N  N   . HIS B 2 306 ? 27.388  -11.942 40.877  1.00 23.81  ? 306 HIS B N   1 
ATOM   6079  C  CA  . HIS B 2 306 ? 26.504  -11.194 41.772  1.00 24.81  ? 306 HIS B CA  1 
ATOM   6080  C  C   . HIS B 2 306 ? 25.176  -11.911 41.971  1.00 27.53  ? 306 HIS B C   1 
ATOM   6081  O  O   . HIS B 2 306 ? 24.720  -12.112 43.113  1.00 27.74  ? 306 HIS B O   1 
ATOM   6082  C  CB  . HIS B 2 306 ? 26.262  -9.779  41.193  1.00 22.90  ? 306 HIS B CB  1 
ATOM   6083  C  CG  . HIS B 2 306 ? 25.224  -8.992  41.924  1.00 24.62  ? 306 HIS B CG  1 
ATOM   6084  N  ND1 . HIS B 2 306 ? 25.403  -8.578  43.228  1.00 25.91  ? 306 HIS B ND1 1 
ATOM   6085  C  CD2 . HIS B 2 306 ? 24.006  -8.525  41.546  1.00 24.17  ? 306 HIS B CD2 1 
ATOM   6086  C  CE1 . HIS B 2 306 ? 24.349  -7.893  43.621  1.00 29.64  ? 306 HIS B CE1 1 
ATOM   6087  N  NE2 . HIS B 2 306 ? 23.488  -7.843  42.622  1.00 25.03  ? 306 HIS B NE2 1 
ATOM   6088  N  N   . VAL B 2 307 ? 24.576  -12.379 40.875  1.00 23.63  ? 307 VAL B N   1 
ATOM   6089  C  CA  . VAL B 2 307 ? 23.283  -13.075 40.975  1.00 25.69  ? 307 VAL B CA  1 
ATOM   6090  C  C   . VAL B 2 307 ? 23.419  -14.422 41.708  1.00 26.92  ? 307 VAL B C   1 
ATOM   6091  O  O   . VAL B 2 307 ? 22.635  -14.724 42.623  1.00 26.70  ? 307 VAL B O   1 
ATOM   6092  C  CB  . VAL B 2 307 ? 22.662  -13.240 39.584  1.00 24.55  ? 307 VAL B CB  1 
ATOM   6093  C  CG1 . VAL B 2 307 ? 21.365  -14.085 39.665  1.00 27.63  ? 307 VAL B CG1 1 
ATOM   6094  C  CG2 . VAL B 2 307 ? 22.261  -11.898 39.033  1.00 23.16  ? 307 VAL B CG2 1 
ATOM   6095  N  N   . LEU B 2 308 ? 24.422  -15.247 41.353  1.00 23.27  ? 308 LEU B N   1 
ATOM   6096  C  CA  . LEU B 2 308 ? 24.600  -16.515 42.086  1.00 26.04  ? 308 LEU B CA  1 
ATOM   6097  C  C   . LEU B 2 308 ? 24.953  -16.278 43.547  1.00 27.37  ? 308 LEU B C   1 
ATOM   6098  O  O   . LEU B 2 308 ? 24.469  -16.989 44.434  1.00 28.32  ? 308 LEU B O   1 
ATOM   6099  C  CB  . LEU B 2 308 ? 25.675  -17.340 41.413  1.00 25.99  ? 308 LEU B CB  1 
ATOM   6100  C  CG  . LEU B 2 308 ? 25.896  -18.694 42.098  1.00 29.56  ? 308 LEU B CG  1 
ATOM   6101  C  CD1 . LEU B 2 308 ? 24.573  -19.482 42.119  1.00 31.89  ? 308 LEU B CD1 1 
ATOM   6102  C  CD2 . LEU B 2 308 ? 27.030  -19.460 41.433  1.00 30.00  ? 308 LEU B CD2 1 
ATOM   6103  N  N   . GLY B 2 309 ? 25.771  -15.256 43.832  1.00 28.61  ? 309 GLY B N   1 
ATOM   6104  C  CA  . GLY B 2 309 ? 26.106  -14.954 45.212  1.00 29.04  ? 309 GLY B CA  1 
ATOM   6105  C  C   . GLY B 2 309 ? 24.887  -14.587 46.036  1.00 27.08  ? 309 GLY B C   1 
ATOM   6106  O  O   . GLY B 2 309 ? 24.724  -15.061 47.162  1.00 29.72  ? 309 GLY B O   1 
ATOM   6107  N  N   . MET B 2 310 ? 24.042  -13.710 45.499  1.00 27.36  ? 310 MET B N   1 
ATOM   6108  C  CA  . MET B 2 310 ? 22.756  -13.415 46.131  1.00 28.91  ? 310 MET B CA  1 
ATOM   6109  C  C   . MET B 2 310 ? 21.904  -14.665 46.323  1.00 29.45  ? 310 MET B C   1 
ATOM   6110  O  O   . MET B 2 310 ? 21.342  -14.879 47.403  1.00 29.32  ? 310 MET B O   1 
ATOM   6111  C  CB  . MET B 2 310 ? 22.052  -12.356 45.297  1.00 30.82  ? 310 MET B CB  1 
ATOM   6112  C  CG  . MET B 2 310 ? 22.398  -10.946 45.800  1.00 30.91  ? 310 MET B CG  1 
ATOM   6113  S  SD  . MET B 2 310 ? 21.438  -9.639  45.057  1.00 30.98  ? 310 MET B SD  1 
ATOM   6114  C  CE  . MET B 2 310 ? 21.274  -10.205 43.342  1.00 26.03  ? 310 MET B CE  1 
ATOM   6115  N  N   . ALA B 2 311 ? 21.810  -15.510 45.298  1.00 27.74  ? 311 ALA B N   1 
ATOM   6116  C  CA  . ALA B 2 311 ? 21.019  -16.727 45.415  1.00 28.77  ? 311 ALA B CA  1 
ATOM   6117  C  C   . ALA B 2 311 ? 21.526  -17.621 46.530  1.00 30.12  ? 311 ALA B C   1 
ATOM   6118  O  O   . ALA B 2 311 ? 20.735  -18.243 47.226  1.00 29.87  ? 311 ALA B O   1 
ATOM   6119  C  CB  . ALA B 2 311 ? 21.050  -17.516 44.108  1.00 30.71  ? 311 ALA B CB  1 
ATOM   6120  N  N   . LYS B 2 312 ? 22.845  -17.773 46.656  1.00 30.03  ? 312 LYS B N   1 
ATOM   6121  C  CA  . LYS B 2 312 ? 23.393  -18.635 47.700  1.00 29.19  ? 312 LYS B CA  1 
ATOM   6122  C  C   . LYS B 2 312 ? 23.208  -18.019 49.088  1.00 31.09  ? 312 LYS B C   1 
ATOM   6123  O  O   . LYS B 2 312 ? 22.841  -18.714 50.046  1.00 33.83  ? 312 LYS B O   1 
ATOM   6124  C  CB  . LYS B 2 312 ? 24.874  -18.890 47.413  1.00 31.05  ? 312 LYS B CB  1 
ATOM   6125  C  CG  . LYS B 2 312 ? 25.103  -19.817 46.203  1.00 33.03  ? 312 LYS B CG  1 
ATOM   6126  C  CD  . LYS B 2 312 ? 24.384  -21.161 46.330  1.00 36.48  ? 312 LYS B CD  1 
ATOM   6127  C  CE  . LYS B 2 312 ? 24.755  -22.063 45.106  1.00 33.89  ? 312 LYS B CE  1 
ATOM   6128  N  NZ  . LYS B 2 312 ? 24.592  -23.501 45.360  1.00 37.91  ? 312 LYS B NZ  1 
ATOM   6129  N  N   . GLU B 2 313 ? 23.423  -16.717 49.184  1.00 30.84  ? 313 GLU B N   1 
ATOM   6130  C  CA  . GLU B 2 313 ? 23.383  -16.009 50.461  1.00 32.25  ? 313 GLU B CA  1 
ATOM   6131  C  C   . GLU B 2 313 ? 21.976  -15.976 51.040  1.00 29.97  ? 313 GLU B C   1 
ATOM   6132  O  O   . GLU B 2 313 ? 21.801  -15.927 52.268  1.00 33.58  ? 313 GLU B O   1 
ATOM   6133  C  CB  . GLU B 2 313 ? 23.921  -14.598 50.222  1.00 30.66  ? 313 GLU B CB  1 
ATOM   6134  C  CG  . GLU B 2 313 ? 24.121  -13.756 51.462  1.00 34.77  ? 313 GLU B CG  1 
ATOM   6135  C  CD  . GLU B 2 313 ? 24.330  -12.274 51.108  1.00 41.40  ? 313 GLU B CD  1 
ATOM   6136  O  OE1 . GLU B 2 313 ? 24.036  -11.416 51.966  1.00 46.06  ? 313 GLU B OE1 1 
ATOM   6137  O  OE2 . GLU B 2 313 ? 24.754  -11.946 49.960  1.00 48.05  ? 313 GLU B OE2 1 
ATOM   6138  N  N   . TYR B 2 314 ? 20.967  -15.987 50.181  1.00 31.75  ? 314 TYR B N   1 
ATOM   6139  C  CA  . TYR B 2 314 ? 19.584  -15.989 50.634  1.00 32.52  ? 314 TYR B CA  1 
ATOM   6140  C  C   . TYR B 2 314 ? 18.936  -17.370 50.512  1.00 32.97  ? 314 TYR B C   1 
ATOM   6141  O  O   . TYR B 2 314 ? 17.710  -17.494 50.663  1.00 32.92  ? 314 TYR B O   1 
ATOM   6142  C  CB  . TYR B 2 314 ? 18.782  -14.920 49.858  1.00 28.44  ? 314 TYR B CB  1 
ATOM   6143  C  CG  . TYR B 2 314 ? 19.145  -13.495 50.253  1.00 28.62  ? 314 TYR B CG  1 
ATOM   6144  C  CD1 . TYR B 2 314 ? 20.309  -12.884 49.798  1.00 27.21  ? 314 TYR B CD1 1 
ATOM   6145  C  CD2 . TYR B 2 314 ? 18.368  -12.801 51.154  1.00 30.59  ? 314 TYR B CD2 1 
ATOM   6146  C  CE1 . TYR B 2 314 ? 20.629  -11.565 50.190  1.00 30.05  ? 314 TYR B CE1 1 
ATOM   6147  C  CE2 . TYR B 2 314 ? 18.701  -11.554 51.570  1.00 30.31  ? 314 TYR B CE2 1 
ATOM   6148  C  CZ  . TYR B 2 314 ? 19.826  -10.939 51.114  1.00 28.70  ? 314 TYR B CZ  1 
ATOM   6149  O  OH  . TYR B 2 314 ? 20.092  -9.657  51.533  1.00 31.30  ? 314 TYR B OH  1 
ATOM   6150  N  N   . ASN B 2 315 ? 19.735  -18.426 50.327  1.00 27.73  ? 315 ASN B N   1 
ATOM   6151  C  CA  . ASN B 2 315 ? 19.196  -19.802 50.323  1.00 33.30  ? 315 ASN B CA  1 
ATOM   6152  C  C   . ASN B 2 315 ? 18.061  -19.978 49.316  1.00 31.97  ? 315 ASN B C   1 
ATOM   6153  O  O   . ASN B 2 315 ? 16.997  -20.514 49.630  1.00 33.89  ? 315 ASN B O   1 
ATOM   6154  C  CB  . ASN B 2 315 ? 18.750  -20.219 51.729  1.00 33.67  ? 315 ASN B CB  1 
ATOM   6155  C  CG  . ASN B 2 315 ? 19.914  -20.711 52.569  1.00 45.65  ? 315 ASN B CG  1 
ATOM   6156  O  OD1 . ASN B 2 315 ? 20.686  -21.568 52.125  1.00 49.70  ? 315 ASN B OD1 1 
ATOM   6157  N  ND2 . ASN B 2 315 ? 20.057  -20.173 53.771  1.00 50.91  ? 315 ASN B ND2 1 
ATOM   6158  N  N   . VAL B 2 316 ? 18.315  -19.576 48.069  1.00 30.32  ? 316 VAL B N   1 
ATOM   6159  C  CA  . VAL B 2 316 ? 17.282  -19.660 47.049  1.00 28.60  ? 316 VAL B CA  1 
ATOM   6160  C  C   . VAL B 2 316 ? 17.099  -21.100 46.586  1.00 32.90  ? 316 VAL B C   1 
ATOM   6161  O  O   . VAL B 2 316 ? 18.075  -21.821 46.359  1.00 32.62  ? 316 VAL B O   1 
ATOM   6162  C  CB  . VAL B 2 316 ? 17.646  -18.735 45.886  1.00 29.72  ? 316 VAL B CB  1 
ATOM   6163  C  CG1 . VAL B 2 316 ? 16.816  -19.052 44.710  1.00 31.67  ? 316 VAL B CG1 1 
ATOM   6164  C  CG2 . VAL B 2 316 ? 17.423  -17.311 46.366  1.00 28.25  ? 316 VAL B CG2 1 
ATOM   6165  N  N   . GLU B 2 317 ? 15.839  -21.510 46.414  1.00 29.21  ? 317 GLU B N   1 
ATOM   6166  C  CA  . GLU B 2 317 ? 15.550  -22.857 45.885  1.00 30.06  ? 317 GLU B CA  1 
ATOM   6167  C  C   . GLU B 2 317 ? 15.208  -22.874 44.401  1.00 36.40  ? 317 GLU B C   1 
ATOM   6168  O  O   . GLU B 2 317 ? 15.490  -23.870 43.718  1.00 34.58  ? 317 GLU B O   1 
ATOM   6169  C  CB  . GLU B 2 317 ? 14.431  -23.507 46.700  1.00 33.80  ? 317 GLU B CB  1 
ATOM   6170  C  CG  . GLU B 2 317 ? 14.888  -23.678 48.181  1.00 37.94  ? 317 GLU B CG  1 
ATOM   6171  C  CD  . GLU B 2 317 ? 13.787  -24.002 49.189  1.00 41.71  ? 317 GLU B CD  1 
ATOM   6172  O  OE1 . GLU B 2 317 ? 12.576  -23.780 48.930  1.00 37.51  ? 317 GLU B OE1 1 
ATOM   6173  O  OE2 . GLU B 2 317 ? 14.150  -24.560 50.254  1.00 49.53  ? 317 GLU B OE2 1 
ATOM   6174  N  N   . GLY B 2 318 ? 14.616  -21.800 43.888  1.00 31.78  ? 318 GLY B N   1 
ATOM   6175  C  CA  . GLY B 2 318 ? 14.254  -21.712 42.486  1.00 29.83  ? 318 GLY B CA  1 
ATOM   6176  C  C   . GLY B 2 318 ? 14.277  -20.273 42.046  1.00 26.80  ? 318 GLY B C   1 
ATOM   6177  O  O   . GLY B 2 318 ? 13.834  -19.382 42.782  1.00 31.57  ? 318 GLY B O   1 
ATOM   6178  N  N   . ALA B 2 319 ? 14.768  -20.018 40.842  1.00 26.12  ? 319 ALA B N   1 
ATOM   6179  C  CA  . ALA B 2 319 ? 14.929  -18.649 40.333  1.00 25.17  ? 319 ALA B CA  1 
ATOM   6180  C  C   . ALA B 2 319 ? 13.988  -18.439 39.169  1.00 27.31  ? 319 ALA B C   1 
ATOM   6181  O  O   . ALA B 2 319 ? 13.975  -19.264 38.243  1.00 29.33  ? 319 ALA B O   1 
ATOM   6182  C  CB  . ALA B 2 319 ? 16.371  -18.398 39.869  1.00 26.82  ? 319 ALA B CB  1 
ATOM   6183  N  N   . ILE B 2 320 ? 13.227  -17.335 39.198  1.00 25.65  ? 320 ILE B N   1 
ATOM   6184  C  CA  . ILE B 2 320 ? 12.244  -17.005 38.173  1.00 26.43  ? 320 ILE B CA  1 
ATOM   6185  C  C   . ILE B 2 320 ? 12.752  -15.799 37.363  1.00 27.32  ? 320 ILE B C   1 
ATOM   6186  O  O   . ILE B 2 320 ? 12.801  -14.673 37.880  1.00 26.99  ? 320 ILE B O   1 
ATOM   6187  C  CB  . ILE B 2 320 ? 10.867  -16.703 38.794  1.00 31.19  ? 320 ILE B CB  1 
ATOM   6188  C  CG1 . ILE B 2 320 ? 10.347  -17.896 39.633  1.00 32.54  ? 320 ILE B CG1 1 
ATOM   6189  C  CG2 . ILE B 2 320 ? 9.846   -16.332 37.715  1.00 29.27  ? 320 ILE B CG2 1 
ATOM   6190  C  CD1 . ILE B 2 320 ? 9.026   -17.592 40.355  1.00 33.82  ? 320 ILE B CD1 1 
ATOM   6191  N  N   . PHE B 2 321 ? 13.031  -16.019 36.060  1.00 25.31  ? 321 PHE B N   1 
ATOM   6192  C  CA  . PHE B 2 321 ? 13.358  -14.923 35.145  1.00 25.07  ? 321 PHE B CA  1 
ATOM   6193  C  C   . PHE B 2 321 ? 12.060  -14.313 34.657  1.00 28.28  ? 321 PHE B C   1 
ATOM   6194  O  O   . PHE B 2 321 ? 11.251  -15.003 34.034  1.00 26.20  ? 321 PHE B O   1 
ATOM   6195  C  CB  . PHE B 2 321 ? 14.164  -15.407 33.935  1.00 27.18  ? 321 PHE B CB  1 
ATOM   6196  C  CG  . PHE B 2 321 ? 15.561  -15.810 34.261  1.00 25.63  ? 321 PHE B CG  1 
ATOM   6197  C  CD1 . PHE B 2 321 ? 15.847  -17.111 34.659  1.00 28.01  ? 321 PHE B CD1 1 
ATOM   6198  C  CD2 . PHE B 2 321 ? 16.586  -14.887 34.204  1.00 23.90  ? 321 PHE B CD2 1 
ATOM   6199  C  CE1 . PHE B 2 321 ? 17.134  -17.493 34.980  1.00 27.82  ? 321 PHE B CE1 1 
ATOM   6200  C  CE2 . PHE B 2 321 ? 17.870  -15.264 34.543  1.00 24.03  ? 321 PHE B CE2 1 
ATOM   6201  C  CZ  . PHE B 2 321 ? 18.144  -16.590 34.911  1.00 31.17  ? 321 PHE B CZ  1 
ATOM   6202  N  N   . LEU B 2 322 ? 11.847  -13.027 34.946  1.00 26.87  ? 322 LEU B N   1 
ATOM   6203  C  CA  . LEU B 2 322 ? 10.729  -12.286 34.397  1.00 25.61  ? 322 LEU B CA  1 
ATOM   6204  C  C   . LEU B 2 322 ? 11.300  -11.425 33.296  1.00 30.52  ? 322 LEU B C   1 
ATOM   6205  O  O   . LEU B 2 322 ? 12.148  -10.583 33.563  1.00 29.01  ? 322 LEU B O   1 
ATOM   6206  C  CB  . LEU B 2 322 ? 10.071  -11.412 35.458  1.00 27.71  ? 322 LEU B CB  1 
ATOM   6207  C  CG  . LEU B 2 322 ? 9.749   -12.188 36.754  1.00 28.57  ? 322 LEU B CG  1 
ATOM   6208  C  CD1 . LEU B 2 322 ? 9.145   -11.279 37.769  1.00 39.05  ? 322 LEU B CD1 1 
ATOM   6209  C  CD2 . LEU B 2 322 ? 8.726   -13.265 36.345  1.00 31.24  ? 322 LEU B CD2 1 
ATOM   6210  N  N   A GLN B 2 323 ? 10.895  -11.653 32.056  0.44 28.40  ? 323 GLN B N   1 
ATOM   6211  N  N   B GLN B 2 323 ? 10.886  -11.659 32.063  0.56 28.38  ? 323 GLN B N   1 
ATOM   6212  C  CA  A GLN B 2 323 ? 11.516  -10.899 30.970  0.44 29.05  ? 323 GLN B CA  1 
ATOM   6213  C  CA  B GLN B 2 323 ? 11.486  -10.912 30.964  0.56 29.06  ? 323 GLN B CA  1 
ATOM   6214  C  C   A GLN B 2 323 ? 10.504  -10.045 30.221  0.44 27.79  ? 323 GLN B C   1 
ATOM   6215  C  C   B GLN B 2 323 ? 10.470  -10.027 30.258  0.56 27.76  ? 323 GLN B C   1 
ATOM   6216  O  O   A GLN B 2 323 ? 9.452   -10.533 29.802  0.44 28.87  ? 323 GLN B O   1 
ATOM   6217  O  O   B GLN B 2 323 ? 9.387   -10.480 29.890  0.56 28.85  ? 323 GLN B O   1 
ATOM   6218  C  CB  A GLN B 2 323 ? 12.251  -11.828 30.010  0.44 29.27  ? 323 GLN B CB  1 
ATOM   6219  C  CB  B GLN B 2 323 ? 12.143  -11.853 29.972  0.56 29.24  ? 323 GLN B CB  1 
ATOM   6220  C  CG  A GLN B 2 323 ? 13.228  -11.032 29.147  0.44 32.10  ? 323 GLN B CG  1 
ATOM   6221  C  CG  B GLN B 2 323 ? 13.244  -11.124 29.231  0.56 32.19  ? 323 GLN B CG  1 
ATOM   6222  C  CD  A GLN B 2 323 ? 14.652  -11.487 29.347  0.44 30.69  ? 323 GLN B CD  1 
ATOM   6223  C  CD  B GLN B 2 323 ? 13.525  -11.760 27.897  0.56 28.16  ? 323 GLN B CD  1 
ATOM   6224  O  OE1 A GLN B 2 323 ? 15.275  -11.127 30.333  0.44 32.83  ? 323 GLN B OE1 1 
ATOM   6225  O  OE1 B GLN B 2 323 ? 14.305  -12.684 27.804  0.56 30.17  ? 323 GLN B OE1 1 
ATOM   6226  N  NE2 A GLN B 2 323 ? 15.168  -12.270 28.428  0.44 27.09  ? 323 GLN B NE2 1 
ATOM   6227  N  NE2 B GLN B 2 323 ? 12.891  -11.239 26.840  0.56 31.35  ? 323 GLN B NE2 1 
ATOM   6228  N  N   . GLN B 2 324 ? 10.841  -8.772  30.027  1.00 26.51  ? 324 GLN B N   1 
ATOM   6229  C  CA  . GLN B 2 324 ? 10.053  -7.925  29.139  1.00 27.24  ? 324 GLN B CA  1 
ATOM   6230  C  C   . GLN B 2 324 ? 10.264  -8.411  27.718  1.00 28.03  ? 324 GLN B C   1 
ATOM   6231  O  O   . GLN B 2 324 ? 11.392  -8.736  27.333  1.00 26.46  ? 324 GLN B O   1 
ATOM   6232  C  CB  . GLN B 2 324 ? 10.495  -6.458  29.233  1.00 23.28  ? 324 GLN B CB  1 
ATOM   6233  C  CG  . GLN B 2 324 ? 10.225  -5.807  30.577  1.00 30.47  ? 324 GLN B CG  1 
ATOM   6234  C  CD  . GLN B 2 324 ? 8.737   -5.557  30.761  1.00 34.55  ? 324 GLN B CD  1 
ATOM   6235  O  OE1 . GLN B 2 324 ? 8.131   -4.809  29.991  1.00 36.60  ? 324 GLN B OE1 1 
ATOM   6236  N  NE2 . GLN B 2 324 ? 8.132   -6.208  31.752  1.00 36.12  ? 324 GLN B NE2 1 
ATOM   6237  N  N   . LYS B 2 325 ? 9.161   -8.505  26.955  1.00 24.80  ? 325 LYS B N   1 
ATOM   6238  C  CA  . LYS B 2 325 ? 9.266   -8.738  25.531  1.00 27.89  ? 325 LYS B CA  1 
ATOM   6239  C  C   . LYS B 2 325 ? 10.260  -7.761  24.923  1.00 28.19  ? 325 LYS B C   1 
ATOM   6240  O  O   . LYS B 2 325 ? 10.278  -6.578  25.277  1.00 24.56  ? 325 LYS B O   1 
ATOM   6241  C  CB  . LYS B 2 325 ? 7.904   -8.550  24.878  1.00 31.14  ? 325 LYS B CB  1 
ATOM   6242  C  CG  . LYS B 2 325 ? 7.101   -9.802  24.762  1.00 38.51  ? 325 LYS B CG  1 
ATOM   6243  C  CD  . LYS B 2 325 ? 5.697   -9.462  24.217  1.00 43.03  ? 325 LYS B CD  1 
ATOM   6244  C  CE  . LYS B 2 325 ? 5.800   -9.117  22.720  1.00 47.03  ? 325 LYS B CE  1 
ATOM   6245  N  NZ  . LYS B 2 325 ? 5.576   -10.310 21.815  1.00 45.62  ? 325 LYS B NZ  1 
ATOM   6246  N  N   . PHE B 2 326 ? 11.093  -8.266  24.020  1.00 26.66  ? 326 PHE B N   1 
ATOM   6247  C  CA  . PHE B 2 326 ? 12.050  -7.483  23.245  1.00 24.28  ? 326 PHE B CA  1 
ATOM   6248  C  C   . PHE B 2 326 ? 13.245  -6.919  24.023  1.00 27.69  ? 326 PHE B C   1 
ATOM   6249  O  O   . PHE B 2 326 ? 13.980  -6.076  23.456  1.00 28.41  ? 326 PHE B O   1 
ATOM   6250  C  CB  . PHE B 2 326 ? 11.359  -6.316  22.525  1.00 24.75  ? 326 PHE B CB  1 
ATOM   6251  C  CG  . PHE B 2 326 ? 10.181  -6.766  21.683  1.00 27.42  ? 326 PHE B CG  1 
ATOM   6252  C  CD1 . PHE B 2 326 ? 10.359  -7.744  20.689  1.00 27.12  ? 326 PHE B CD1 1 
ATOM   6253  C  CD2 . PHE B 2 326 ? 8.926   -6.234  21.875  1.00 30.68  ? 326 PHE B CD2 1 
ATOM   6254  C  CE1 . PHE B 2 326 ? 9.298   -8.185  19.891  1.00 32.90  ? 326 PHE B CE1 1 
ATOM   6255  C  CE2 . PHE B 2 326 ? 7.861   -6.634  21.066  1.00 32.19  ? 326 PHE B CE2 1 
ATOM   6256  C  CZ  . PHE B 2 326 ? 8.032   -7.617  20.085  1.00 35.75  ? 326 PHE B CZ  1 
ATOM   6257  N  N   . CYS B 2 327 ? 13.458  -7.302  25.284  1.00 22.57  ? 327 CYS B N   1 
ATOM   6258  C  CA  . CYS B 2 327 ? 14.480  -6.681  26.130  1.00 23.78  ? 327 CYS B CA  1 
ATOM   6259  C  C   . CYS B 2 327 ? 15.882  -7.208  25.759  1.00 21.30  ? 327 CYS B C   1 
ATOM   6260  O  O   . CYS B 2 327 ? 16.327  -8.270  26.240  1.00 25.53  ? 327 CYS B O   1 
ATOM   6261  C  CB  . CYS B 2 327 ? 14.149  -6.932  27.607  1.00 22.79  ? 327 CYS B CB  1 
ATOM   6262  S  SG  . CYS B 2 327 ? 15.355  -6.312  28.744  1.00 22.98  ? 327 CYS B SG  1 
ATOM   6263  N  N   . ASP B 2 328 ? 16.561  -6.485  24.838  1.00 23.14  ? 328 ASP B N   1 
ATOM   6264  C  CA  . ASP B 2 328 ? 17.878  -6.927  24.377  1.00 23.70  ? 328 ASP B CA  1 
ATOM   6265  C  C   . ASP B 2 328 ? 18.940  -7.100  25.449  1.00 22.63  ? 328 ASP B C   1 
ATOM   6266  O  O   . ASP B 2 328 ? 19.626  -8.141  25.400  1.00 21.48  ? 328 ASP B O   1 
ATOM   6267  C  CB  . ASP B 2 328 ? 18.392  -6.028  23.243  1.00 25.98  ? 328 ASP B CB  1 
ATOM   6268  C  CG  . ASP B 2 328 ? 17.457  -6.051  22.055  1.00 25.72  ? 328 ASP B CG  1 
ATOM   6269  O  OD1 . ASP B 2 328 ? 17.311  -7.100  21.388  1.00 26.81  ? 328 ASP B OD1 1 
ATOM   6270  O  OD2 . ASP B 2 328 ? 16.736  -5.080  21.871  1.00 30.31  ? 328 ASP B OD2 1 
ATOM   6271  N  N   . PRO B 2 329 ? 19.167  -6.177  26.396  1.00 22.30  ? 329 PRO B N   1 
ATOM   6272  C  CA  . PRO B 2 329 ? 20.285  -6.402  27.332  1.00 21.67  ? 329 PRO B CA  1 
ATOM   6273  C  C   . PRO B 2 329 ? 20.095  -7.685  28.142  1.00 24.78  ? 329 PRO B C   1 
ATOM   6274  O  O   . PRO B 2 329 ? 21.051  -8.459  28.305  1.00 24.04  ? 329 PRO B O   1 
ATOM   6275  C  CB  . PRO B 2 329 ? 20.289  -5.111  28.220  1.00 22.37  ? 329 PRO B CB  1 
ATOM   6276  C  CG  . PRO B 2 329 ? 19.660  -4.129  27.386  1.00 22.62  ? 329 PRO B CG  1 
ATOM   6277  C  CD  . PRO B 2 329 ? 18.572  -4.850  26.632  1.00 22.67  ? 329 PRO B CD  1 
ATOM   6278  N  N   . HIS B 2 330 ? 18.868  -7.966  28.589  1.00 20.06  ? 330 HIS B N   1 
ATOM   6279  C  CA  . HIS B 2 330 ? 18.691  -9.139  29.430  1.00 24.71  ? 330 HIS B CA  1 
ATOM   6280  C  C   . HIS B 2 330 ? 18.589  -10.404 28.597  1.00 21.51  ? 330 HIS B C   1 
ATOM   6281  O  O   . HIS B 2 330 ? 18.951  -11.483 29.083  1.00 24.77  ? 330 HIS B O   1 
ATOM   6282  C  CB  . HIS B 2 330 ? 17.470  -8.945  30.299  1.00 24.40  ? 330 HIS B CB  1 
ATOM   6283  C  CG  . HIS B 2 330 ? 17.698  -7.901  31.345  1.00 22.48  ? 330 HIS B CG  1 
ATOM   6284  N  ND1 . HIS B 2 330 ? 17.986  -8.217  32.654  1.00 23.14  ? 330 HIS B ND1 1 
ATOM   6285  C  CD2 . HIS B 2 330 ? 17.836  -6.557  31.247  1.00 20.22  ? 330 HIS B CD2 1 
ATOM   6286  C  CE1 . HIS B 2 330 ? 18.187  -7.109  33.339  1.00 20.44  ? 330 HIS B CE1 1 
ATOM   6287  N  NE2 . HIS B 2 330 ? 18.116  -6.091  32.503  1.00 22.19  ? 330 HIS B NE2 1 
ATOM   6288  N  N   . GLU B 2 331 ? 18.017  -10.291 27.401  1.00 22.41  ? 331 GLU B N   1 
ATOM   6289  C  CA  . GLU B 2 331 ? 18.029  -11.400 26.430  1.00 23.14  ? 331 GLU B CA  1 
ATOM   6290  C  C   . GLU B 2 331 ? 19.452  -11.830 26.084  1.00 25.49  ? 331 GLU B C   1 
ATOM   6291  O  O   . GLU B 2 331 ? 19.736  -13.034 25.890  1.00 23.63  ? 331 GLU B O   1 
ATOM   6292  C  CB  . GLU B 2 331 ? 17.307  -10.991 25.145  1.00 22.57  ? 331 GLU B CB  1 
ATOM   6293  C  CG  . GLU B 2 331 ? 15.788  -11.022 25.249  1.00 22.07  ? 331 GLU B CG  1 
ATOM   6294  C  CD  . GLU B 2 331 ? 15.084  -10.468 24.015  1.00 23.47  ? 331 GLU B CD  1 
ATOM   6295  O  OE1 . GLU B 2 331 ? 15.634  -9.599  23.276  1.00 26.60  ? 331 GLU B OE1 1 
ATOM   6296  O  OE2 . GLU B 2 331 ? 13.913  -10.829 23.816  1.00 26.91  ? 331 GLU B OE2 1 
ATOM   6297  N  N   . GLY B 2 332 ? 20.362  -10.871 25.987  1.00 22.15  ? 332 GLY B N   1 
ATOM   6298  C  CA  . GLY B 2 332 ? 21.752  -11.192 25.683  1.00 24.43  ? 332 GLY B CA  1 
ATOM   6299  C  C   . GLY B 2 332 ? 22.453  -11.980 26.789  1.00 25.26  ? 332 GLY B C   1 
ATOM   6300  O  O   . GLY B 2 332 ? 23.271  -12.865 26.492  1.00 25.95  ? 332 GLY B O   1 
ATOM   6301  N  N   . ASP B 2 333 ? 22.111  -11.727 28.064  1.00 23.58  ? 333 ASP B N   1 
ATOM   6302  C  CA  . ASP B 2 333 ? 22.694  -12.441 29.212  1.00 22.07  ? 333 ASP B CA  1 
ATOM   6303  C  C   . ASP B 2 333 ? 21.986  -13.760 29.498  1.00 25.69  ? 333 ASP B C   1 
ATOM   6304  O  O   . ASP B 2 333 ? 22.571  -14.653 30.148  1.00 24.76  ? 333 ASP B O   1 
ATOM   6305  C  CB  . ASP B 2 333 ? 22.568  -11.571 30.488  1.00 23.52  ? 333 ASP B CB  1 
ATOM   6306  C  CG  . ASP B 2 333 ? 23.696  -10.550 30.655  1.00 26.18  ? 333 ASP B CG  1 
ATOM   6307  O  OD1 . ASP B 2 333 ? 24.530  -10.384 29.703  1.00 27.02  ? 333 ASP B OD1 1 
ATOM   6308  O  OD2 . ASP B 2 333 ? 23.721  -9.864  31.748  1.00 28.01  ? 333 ASP B OD2 1 
ATOM   6309  N  N   . TYR B 2 334 ? 20.712  -13.880 29.097  1.00 23.69  ? 334 TYR B N   1 
ATOM   6310  C  CA  . TYR B 2 334 ? 19.833  -14.892 29.686  1.00 22.79  ? 334 TYR B CA  1 
ATOM   6311  C  C   . TYR B 2 334 ? 20.320  -16.316 29.502  1.00 22.67  ? 334 TYR B C   1 
ATOM   6312  O  O   . TYR B 2 334 ? 20.301  -17.088 30.491  1.00 24.13  ? 334 TYR B O   1 
ATOM   6313  C  CB  . TYR B 2 334 ? 18.401  -14.725 29.138  1.00 25.94  ? 334 TYR B CB  1 
ATOM   6314  C  CG  . TYR B 2 334 ? 17.514  -15.896 29.447  1.00 25.87  ? 334 TYR B CG  1 
ATOM   6315  C  CD1 . TYR B 2 334 ? 17.064  -16.140 30.763  1.00 26.09  ? 334 TYR B CD1 1 
ATOM   6316  C  CD2 . TYR B 2 334 ? 17.220  -16.849 28.461  1.00 22.83  ? 334 TYR B CD2 1 
ATOM   6317  C  CE1 . TYR B 2 334 ? 16.301  -17.244 31.063  1.00 28.75  ? 334 TYR B CE1 1 
ATOM   6318  C  CE2 . TYR B 2 334 ? 16.433  -17.971 28.781  1.00 27.34  ? 334 TYR B CE2 1 
ATOM   6319  C  CZ  . TYR B 2 334 ? 15.990  -18.150 30.089  1.00 29.05  ? 334 TYR B CZ  1 
ATOM   6320  O  OH  . TYR B 2 334 ? 15.226  -19.268 30.361  1.00 30.62  ? 334 TYR B OH  1 
ATOM   6321  N  N   . PRO B 2 335 ? 20.713  -16.768 28.301  1.00 22.32  ? 335 PRO B N   1 
ATOM   6322  C  CA  . PRO B 2 335 ? 21.029  -18.187 28.165  1.00 26.17  ? 335 PRO B CA  1 
ATOM   6323  C  C   . PRO B 2 335 ? 22.149  -18.617 29.071  1.00 25.42  ? 335 PRO B C   1 
ATOM   6324  O  O   . PRO B 2 335 ? 22.015  -19.654 29.744  1.00 26.07  ? 335 PRO B O   1 
ATOM   6325  C  CB  . PRO B 2 335 ? 21.399  -18.331 26.686  1.00 24.98  ? 335 PRO B CB  1 
ATOM   6326  C  CG  . PRO B 2 335 ? 20.577  -17.223 26.007  1.00 23.79  ? 335 PRO B CG  1 
ATOM   6327  C  CD  . PRO B 2 335 ? 20.705  -16.073 26.990  1.00 23.29  ? 335 PRO B CD  1 
ATOM   6328  N  N   . ASP B 2 336 ? 23.211  -17.825 29.174  1.00 23.24  ? 336 ASP B N   1 
ATOM   6329  C  CA  . ASP B 2 336 ? 24.293  -18.275 30.042  1.00 25.62  ? 336 ASP B CA  1 
ATOM   6330  C  C   . ASP B 2 336 ? 24.035  -17.963 31.513  1.00 26.44  ? 336 ASP B C   1 
ATOM   6331  O  O   . ASP B 2 336 ? 24.557  -18.676 32.377  1.00 24.76  ? 336 ASP B O   1 
ATOM   6332  C  CB  . ASP B 2 336 ? 25.624  -17.710 29.566  1.00 24.91  ? 336 ASP B CB  1 
ATOM   6333  C  CG  . ASP B 2 336 ? 26.135  -18.462 28.330  1.00 30.20  ? 336 ASP B CG  1 
ATOM   6334  O  OD1 . ASP B 2 336 ? 25.343  -19.224 27.743  1.00 30.35  ? 336 ASP B OD1 1 
ATOM   6335  O  OD2 . ASP B 2 336 ? 27.327  -18.390 27.995  1.00 32.98  ? 336 ASP B OD2 1 
ATOM   6336  N  N   . LEU B 2 337 ? 23.290  -16.908 31.853  1.00 22.45  ? 337 LEU B N   1 
ATOM   6337  C  CA  . LEU B 2 337 ? 22.975  -16.756 33.288  1.00 20.61  ? 337 LEU B CA  1 
ATOM   6338  C  C   . LEU B 2 337 ? 22.078  -17.884 33.790  1.00 25.73  ? 337 LEU B C   1 
ATOM   6339  O  O   . LEU B 2 337 ? 22.268  -18.393 34.909  1.00 26.03  ? 337 LEU B O   1 
ATOM   6340  C  CB  . LEU B 2 337 ? 22.279  -15.422 33.549  1.00 24.63  ? 337 LEU B CB  1 
ATOM   6341  C  CG  . LEU B 2 337 ? 21.902  -15.148 34.998  1.00 22.71  ? 337 LEU B CG  1 
ATOM   6342  C  CD1 . LEU B 2 337 ? 23.127  -15.274 35.945  1.00 21.89  ? 337 LEU B CD1 1 
ATOM   6343  C  CD2 . LEU B 2 337 ? 21.311  -13.678 34.973  1.00 24.22  ? 337 LEU B CD2 1 
ATOM   6344  N  N   . LYS B 2 338 ? 21.066  -18.272 32.999  1.00 24.94  ? 338 LYS B N   1 
ATOM   6345  C  CA  . LYS B 2 338 ? 20.306  -19.485 33.319  1.00 26.66  ? 338 LYS B CA  1 
ATOM   6346  C  C   . LYS B 2 338 ? 21.241  -20.656 33.567  1.00 26.64  ? 338 LYS B C   1 
ATOM   6347  O  O   . LYS B 2 338 ? 21.152  -21.341 34.610  1.00 29.69  ? 338 LYS B O   1 
ATOM   6348  C  CB  . LYS B 2 338 ? 19.320  -19.779 32.170  1.00 29.10  ? 338 LYS B CB  1 
ATOM   6349  C  CG  . LYS B 2 338 ? 18.550  -21.118 32.239  1.00 29.93  ? 338 LYS B CG  1 
ATOM   6350  C  CD  . LYS B 2 338 ? 17.721  -21.278 30.969  1.00 32.89  ? 338 LYS B CD  1 
ATOM   6351  C  CE  . LYS B 2 338 ? 16.803  -22.451 31.046  1.00 37.82  ? 338 LYS B CE  1 
ATOM   6352  N  NZ  . LYS B 2 338 ? 17.568  -23.679 31.006  1.00 38.65  ? 338 LYS B NZ  1 
ATOM   6353  N  N   . ARG B 2 339 ? 22.156  -20.919 32.628  1.00 27.75  ? 339 ARG B N   1 
ATOM   6354  C  CA  . ARG B 2 339 ? 23.039  -22.079 32.778  1.00 29.64  ? 339 ARG B CA  1 
ATOM   6355  C  C   . ARG B 2 339 ? 23.850  -21.986 34.051  1.00 28.98  ? 339 ARG B C   1 
ATOM   6356  O  O   . ARG B 2 339 ? 24.001  -22.984 34.775  1.00 28.96  ? 339 ARG B O   1 
ATOM   6357  C  CB  . ARG B 2 339 ? 23.986  -22.205 31.583  1.00 31.36  ? 339 ARG B CB  1 
ATOM   6358  C  CG  . ARG B 2 339 ? 23.290  -22.753 30.354  1.00 34.10  ? 339 ARG B CG  1 
ATOM   6359  C  CD  . ARG B 2 339 ? 24.224  -22.790 29.186  1.00 36.85  ? 339 ARG B CD  1 
ATOM   6360  N  NE  . ARG B 2 339 ? 25.204  -23.859 29.300  1.00 32.75  ? 339 ARG B NE  1 
ATOM   6361  C  CZ  . ARG B 2 339 ? 26.264  -23.993 28.511  1.00 35.27  ? 339 ARG B CZ  1 
ATOM   6362  N  NH1 . ARG B 2 339 ? 26.566  -23.088 27.584  1.00 35.73  ? 339 ARG B NH1 1 
ATOM   6363  N  NH2 . ARG B 2 339 ? 27.002  -25.109 28.599  1.00 36.18  ? 339 ARG B NH2 1 
ATOM   6364  N  N   . HIS B 2 340 ? 24.365  -20.782 34.345  1.00 26.12  ? 340 HIS B N   1 
ATOM   6365  C  CA  . HIS B 2 340 ? 25.193  -20.568 35.536  1.00 28.15  ? 340 HIS B CA  1 
ATOM   6366  C  C   . HIS B 2 340 ? 24.445  -20.952 36.807  1.00 29.34  ? 340 HIS B C   1 
ATOM   6367  O  O   . HIS B 2 340 ? 24.991  -21.629 37.704  1.00 30.74  ? 340 HIS B O   1 
ATOM   6368  C  CB  . HIS B 2 340 ? 25.640  -19.093 35.581  1.00 25.95  ? 340 HIS B CB  1 
ATOM   6369  C  CG  . HIS B 2 340 ? 26.707  -18.821 36.589  1.00 29.52  ? 340 HIS B CG  1 
ATOM   6370  N  ND1 . HIS B 2 340 ? 27.909  -19.491 36.604  1.00 29.99  ? 340 HIS B ND1 1 
ATOM   6371  C  CD2 . HIS B 2 340 ? 26.764  -17.917 37.603  1.00 29.46  ? 340 HIS B CD2 1 
ATOM   6372  C  CE1 . HIS B 2 340 ? 28.649  -19.041 37.601  1.00 31.92  ? 340 HIS B CE1 1 
ATOM   6373  N  NE2 . HIS B 2 340 ? 27.986  -18.071 38.211  1.00 33.08  ? 340 HIS B NE2 1 
ATOM   6374  N  N   . LEU B 2 341 ? 23.194  -20.531 36.903  1.00 27.26  ? 341 LEU B N   1 
ATOM   6375  C  CA  . LEU B 2 341 ? 22.392  -20.857 38.077  1.00 25.96  ? 341 LEU B CA  1 
ATOM   6376  C  C   . LEU B 2 341 ? 22.101  -22.346 38.127  1.00 30.56  ? 341 LEU B C   1 
ATOM   6377  O  O   . LEU B 2 341 ? 22.263  -22.998 39.172  1.00 31.23  ? 341 LEU B O   1 
ATOM   6378  C  CB  . LEU B 2 341 ? 21.090  -20.078 38.019  1.00 27.57  ? 341 LEU B CB  1 
ATOM   6379  C  CG  . LEU B 2 341 ? 21.301  -18.580 38.156  1.00 31.15  ? 341 LEU B CG  1 
ATOM   6380  C  CD1 . LEU B 2 341 ? 19.918  -17.940 38.152  1.00 30.52  ? 341 LEU B CD1 1 
ATOM   6381  C  CD2 . LEU B 2 341 ? 22.007  -18.311 39.443  1.00 32.90  ? 341 LEU B CD2 1 
ATOM   6382  N  N   . GLU B 2 342 ? 21.670  -22.908 36.998  1.00 28.94  ? 342 GLU B N   1 
ATOM   6383  C  CA  . GLU B 2 342 ? 21.268  -24.311 36.991  1.00 29.54  ? 342 GLU B CA  1 
ATOM   6384  C  C   . GLU B 2 342 ? 22.458  -25.217 37.275  1.00 30.80  ? 342 GLU B C   1 
ATOM   6385  O  O   . GLU B 2 342 ? 22.316  -26.257 37.933  1.00 31.08  ? 342 GLU B O   1 
ATOM   6386  C  CB  . GLU B 2 342 ? 20.637  -24.620 35.640  1.00 29.65  ? 342 GLU B CB  1 
ATOM   6387  C  CG  . GLU B 2 342 ? 19.366  -23.805 35.468  1.00 34.25  ? 342 GLU B CG  1 
ATOM   6388  C  CD  . GLU B 2 342 ? 18.362  -24.281 34.435  1.00 40.26  ? 342 GLU B CD  1 
ATOM   6389  O  OE1 . GLU B 2 342 ? 17.145  -24.049 34.656  1.00 42.09  ? 342 GLU B OE1 1 
ATOM   6390  O  OE2 . GLU B 2 342 ? 18.756  -24.906 33.436  1.00 42.93  ? 342 GLU B OE2 1 
ATOM   6391  N  N   . GLU B 2 343 ? 23.635  -24.870 36.750  1.00 28.88  ? 343 GLU B N   1 
ATOM   6392  C  CA  . GLU B 2 343 ? 24.834  -25.658 37.041  1.00 31.87  ? 343 GLU B CA  1 
ATOM   6393  C  C   . GLU B 2 343 ? 25.220  -25.603 38.516  1.00 31.84  ? 343 GLU B C   1 
ATOM   6394  O  O   . GLU B 2 343 ? 25.922  -26.494 38.999  1.00 35.19  ? 343 GLU B O   1 
ATOM   6395  C  CB  . GLU B 2 343 ? 26.014  -25.195 36.176  1.00 33.85  ? 343 GLU B CB  1 
ATOM   6396  C  CG  . GLU B 2 343 ? 25.783  -25.509 34.728  1.00 31.83  ? 343 GLU B CG  1 
ATOM   6397  C  CD  . GLU B 2 343 ? 26.776  -24.879 33.730  1.00 36.10  ? 343 GLU B CD  1 
ATOM   6398  O  OE1 . GLU B 2 343 ? 27.666  -24.092 34.108  1.00 41.04  ? 343 GLU B OE1 1 
ATOM   6399  O  OE2 . GLU B 2 343 ? 26.603  -25.197 32.521  1.00 42.46  ? 343 GLU B OE2 1 
ATOM   6400  N  N   . ASN B 2 344 ? 24.777  -24.590 39.243  1.00 28.26  ? 344 ASN B N   1 
ATOM   6401  C  CA  . ASN B 2 344 ? 25.066  -24.406 40.647  1.00 32.64  ? 344 ASN B CA  1 
ATOM   6402  C  C   . ASN B 2 344 ? 23.883  -24.787 41.512  1.00 38.30  ? 344 ASN B C   1 
ATOM   6403  O  O   . ASN B 2 344 ? 23.774  -24.324 42.651  1.00 40.80  ? 344 ASN B O   1 
ATOM   6404  C  CB  . ASN B 2 344 ? 25.515  -22.966 40.911  1.00 34.51  ? 344 ASN B CB  1 
ATOM   6405  C  CG  . ASN B 2 344 ? 26.942  -22.736 40.434  1.00 36.47  ? 344 ASN B CG  1 
ATOM   6406  O  OD1 . ASN B 2 344 ? 27.879  -23.069 41.146  1.00 36.76  ? 344 ASN B OD1 1 
ATOM   6407  N  ND2 . ASN B 2 344 ? 27.119  -22.174 39.244  1.00 33.00  ? 344 ASN B ND2 1 
ATOM   6408  N  N   . GLY B 2 345 ? 22.970  -25.580 40.976  1.00 35.23  ? 345 GLY B N   1 
ATOM   6409  C  CA  . GLY B 2 345 ? 21.957  -26.226 41.773  1.00 36.72  ? 345 GLY B CA  1 
ATOM   6410  C  C   . GLY B 2 345 ? 20.643  -25.501 41.900  1.00 34.52  ? 345 GLY B C   1 
ATOM   6411  O  O   . GLY B 2 345 ? 19.810  -25.907 42.715  1.00 38.83  ? 345 GLY B O   1 
ATOM   6412  N  N   . ILE B 2 346 ? 20.423  -24.449 41.129  1.00 32.40  ? 346 ILE B N   1 
ATOM   6413  C  CA  . ILE B 2 346 ? 19.224  -23.639 41.259  1.00 32.58  ? 346 ILE B CA  1 
ATOM   6414  C  C   . ILE B 2 346 ? 18.416  -23.796 39.983  1.00 33.57  ? 346 ILE B C   1 
ATOM   6415  O  O   . ILE B 2 346 ? 18.777  -23.179 38.971  1.00 32.71  ? 346 ILE B O   1 
ATOM   6416  C  CB  . ILE B 2 346 ? 19.580  -22.160 41.490  1.00 32.93  ? 346 ILE B CB  1 
ATOM   6417  C  CG1 . ILE B 2 346 ? 20.477  -22.049 42.718  1.00 35.05  ? 346 ILE B CG1 1 
ATOM   6418  C  CG2 . ILE B 2 346 ? 18.301  -21.332 41.673  1.00 31.30  ? 346 ILE B CG2 1 
ATOM   6419  C  CD1 . ILE B 2 346 ? 21.362  -20.882 42.676  1.00 36.70  ? 346 ILE B CD1 1 
ATOM   6420  N  N   . PRO B 2 347 ? 17.307  -24.545 40.006  1.00 34.56  ? 347 PRO B N   1 
ATOM   6421  C  CA  . PRO B 2 347 ? 16.426  -24.598 38.840  1.00 36.29  ? 347 PRO B CA  1 
ATOM   6422  C  C   . PRO B 2 347 ? 15.781  -23.258 38.547  1.00 31.25  ? 347 PRO B C   1 
ATOM   6423  O  O   . PRO B 2 347 ? 15.602  -22.403 39.435  1.00 29.52  ? 347 PRO B O   1 
ATOM   6424  C  CB  . PRO B 2 347 ? 15.394  -25.675 39.205  1.00 36.67  ? 347 PRO B CB  1 
ATOM   6425  C  CG  . PRO B 2 347 ? 15.584  -26.007 40.631  1.00 38.22  ? 347 PRO B CG  1 
ATOM   6426  C  CD  . PRO B 2 347 ? 16.744  -25.234 41.186  1.00 38.60  ? 347 PRO B CD  1 
ATOM   6427  N  N   . THR B 2 348 ? 15.452  -23.066 37.269  1.00 32.98  ? 348 THR B N   1 
ATOM   6428  C  CA  . THR B 2 348 ? 14.918  -21.786 36.813  1.00 26.69  ? 348 THR B CA  1 
ATOM   6429  C  C   . THR B 2 348 ? 13.632  -21.934 35.989  1.00 29.40  ? 348 THR B C   1 
ATOM   6430  O  O   . THR B 2 348 ? 13.306  -22.994 35.424  1.00 28.42  ? 348 THR B O   1 
ATOM   6431  C  CB  . THR B 2 348 ? 15.996  -21.021 36.027  1.00 31.45  ? 348 THR B CB  1 
ATOM   6432  O  OG1 . THR B 2 348 ? 16.248  -21.684 34.789  1.00 35.37  ? 348 THR B OG1 1 
ATOM   6433  C  CG2 . THR B 2 348 ? 17.302  -20.901 36.846  1.00 29.21  ? 348 THR B CG2 1 
ATOM   6434  N  N   . LEU B 2 349 ? 12.887  -20.830 35.946  1.00 26.97  ? 349 LEU B N   1 
ATOM   6435  C  CA  . LEU B 2 349 ? 11.637  -20.694 35.204  1.00 30.40  ? 349 LEU B CA  1 
ATOM   6436  C  C   . LEU B 2 349 ? 11.711  -19.394 34.408  1.00 27.84  ? 349 LEU B C   1 
ATOM   6437  O  O   . LEU B 2 349 ? 12.225  -18.403 34.905  1.00 28.39  ? 349 LEU B O   1 
ATOM   6438  C  CB  . LEU B 2 349 ? 10.450  -20.664 36.155  1.00 25.53  ? 349 LEU B CB  1 
ATOM   6439  C  CG  . LEU B 2 349 ? 9.085   -20.425 35.525  1.00 29.54  ? 349 LEU B CG  1 
ATOM   6440  C  CD1 . LEU B 2 349 ? 8.706   -21.577 34.580  1.00 32.22  ? 349 LEU B CD1 1 
ATOM   6441  C  CD2 . LEU B 2 349 ? 8.000   -20.204 36.582  1.00 31.49  ? 349 LEU B CD2 1 
ATOM   6442  N  N   . PHE B 2 350 ? 11.237  -19.406 33.167  1.00 28.86  ? 350 PHE B N   1 
ATOM   6443  C  CA  . PHE B 2 350 ? 11.273  -18.227 32.289  1.00 28.33  ? 350 PHE B CA  1 
ATOM   6444  C  C   . PHE B 2 350 ? 9.856   -17.765 31.987  1.00 30.12  ? 350 PHE B C   1 
ATOM   6445  O  O   . PHE B 2 350 ? 9.042   -18.544 31.477  1.00 30.48  ? 350 PHE B O   1 
ATOM   6446  C  CB  . PHE B 2 350 ? 12.024  -18.537 30.990  1.00 25.63  ? 350 PHE B CB  1 
ATOM   6447  C  CG  . PHE B 2 350 ? 12.036  -17.386 30.006  1.00 29.54  ? 350 PHE B CG  1 
ATOM   6448  C  CD1 . PHE B 2 350 ? 12.973  -16.359 30.131  1.00 29.76  ? 350 PHE B CD1 1 
ATOM   6449  C  CD2 . PHE B 2 350 ? 11.103  -17.335 28.962  1.00 29.52  ? 350 PHE B CD2 1 
ATOM   6450  C  CE1 . PHE B 2 350 ? 12.992  -15.321 29.253  1.00 31.68  ? 350 PHE B CE1 1 
ATOM   6451  C  CE2 . PHE B 2 350 ? 11.105  -16.262 28.060  1.00 34.22  ? 350 PHE B CE2 1 
ATOM   6452  C  CZ  . PHE B 2 350 ? 12.050  -15.252 28.204  1.00 33.82  ? 350 PHE B CZ  1 
ATOM   6453  N  N   . LEU B 2 351 ? 9.549   -16.507 32.293  1.00 28.36  ? 351 LEU B N   1 
ATOM   6454  C  CA  . LEU B 2 351 ? 8.226   -15.960 31.982  1.00 26.97  ? 351 LEU B CA  1 
ATOM   6455  C  C   . LEU B 2 351 ? 8.414   -14.639 31.238  1.00 27.97  ? 351 LEU B C   1 
ATOM   6456  O  O   . LEU B 2 351 ? 9.290   -13.845 31.593  1.00 28.78  ? 351 LEU B O   1 
ATOM   6457  C  CB  . LEU B 2 351 ? 7.429   -15.733 33.241  1.00 26.64  ? 351 LEU B CB  1 
ATOM   6458  C  CG  . LEU B 2 351 ? 7.199   -16.943 34.173  1.00 28.27  ? 351 LEU B CG  1 
ATOM   6459  C  CD1 . LEU B 2 351 ? 6.540   -16.420 35.504  1.00 32.00  ? 351 LEU B CD1 1 
ATOM   6460  C  CD2 . LEU B 2 351 ? 6.308   -17.978 33.529  1.00 34.24  ? 351 LEU B CD2 1 
ATOM   6461  N  N   . GLU B 2 352 ? 7.583   -14.391 30.231  1.00 26.75  ? 352 GLU B N   1 
ATOM   6462  C  CA  . GLU B 2 352 ? 7.742   -13.233 29.357  1.00 28.33  ? 352 GLU B CA  1 
ATOM   6463  C  C   . GLU B 2 352 ? 6.489   -12.358 29.400  1.00 30.89  ? 352 GLU B C   1 
ATOM   6464  O  O   . GLU B 2 352 ? 5.372   -12.884 29.339  1.00 32.23  ? 352 GLU B O   1 
ATOM   6465  C  CB  . GLU B 2 352 ? 8.031   -13.686 27.905  1.00 32.16  ? 352 GLU B CB  1 
ATOM   6466  C  CG  . GLU B 2 352 ? 8.237   -12.503 26.973  1.00 34.42  ? 352 GLU B CG  1 
ATOM   6467  C  CD  . GLU B 2 352 ? 8.917   -12.897 25.652  1.00 41.42  ? 352 GLU B CD  1 
ATOM   6468  O  OE1 . GLU B 2 352 ? 10.079  -12.458 25.436  1.00 40.11  ? 352 GLU B OE1 1 
ATOM   6469  O  OE2 . GLU B 2 352 ? 8.286   -13.623 24.846  1.00 46.11  ? 352 GLU B OE2 1 
ATOM   6470  N  N   . PHE B 2 353 ? 6.674   -11.012 29.447  1.00 28.11  ? 353 PHE B N   1 
ATOM   6471  C  CA  . PHE B 2 353 ? 5.612   -10.059 29.752  1.00 34.69  ? 353 PHE B CA  1 
ATOM   6472  C  C   . PHE B 2 353 ? 5.435   -9.002  28.673  1.00 33.80  ? 353 PHE B C   1 
ATOM   6473  O  O   . PHE B 2 353 ? 6.410   -8.488  28.125  1.00 32.27  ? 353 PHE B O   1 
ATOM   6474  C  CB  . PHE B 2 353 ? 5.902   -9.370  31.097  1.00 32.36  ? 353 PHE B CB  1 
ATOM   6475  C  CG  . PHE B 2 353 ? 5.865   -10.341 32.240  1.00 32.57  ? 353 PHE B CG  1 
ATOM   6476  C  CD1 . PHE B 2 353 ? 6.988   -11.075 32.562  1.00 29.76  ? 353 PHE B CD1 1 
ATOM   6477  C  CD2 . PHE B 2 353 ? 4.687   -10.575 32.926  1.00 39.11  ? 353 PHE B CD2 1 
ATOM   6478  C  CE1 . PHE B 2 353 ? 6.955   -11.996 33.586  1.00 32.38  ? 353 PHE B CE1 1 
ATOM   6479  C  CE2 . PHE B 2 353 ? 4.635   -11.510 33.948  1.00 36.00  ? 353 PHE B CE2 1 
ATOM   6480  C  CZ  . PHE B 2 353 ? 5.777   -12.222 34.277  1.00 35.31  ? 353 PHE B CZ  1 
ATOM   6481  N  N   . ASP B 2 354 ? 4.172   -8.659  28.415  1.00 37.89  ? 354 ASP B N   1 
ATOM   6482  C  CA  . ASP B 2 354 ? 3.747   -7.487  27.673  1.00 38.42  ? 354 ASP B CA  1 
ATOM   6483  C  C   . ASP B 2 354 ? 3.385   -6.364  28.677  1.00 41.42  ? 354 ASP B C   1 
ATOM   6484  O  O   . ASP B 2 354 ? 3.655   -6.478  29.884  1.00 40.23  ? 354 ASP B O   1 
ATOM   6485  C  CB  . ASP B 2 354 ? 2.596   -7.908  26.759  1.00 42.60  ? 354 ASP B CB  1 
ATOM   6486  C  CG  . ASP B 2 354 ? 2.674   -7.259  25.413  1.00 53.27  ? 354 ASP B CG  1 
ATOM   6487  O  OD1 . ASP B 2 354 ? 2.831   -6.012  25.369  1.00 48.52  ? 354 ASP B OD1 1 
ATOM   6488  O  OD2 . ASP B 2 354 ? 2.601   -7.991  24.401  1.00 58.92  ? 354 ASP B OD2 1 
ATOM   6489  N  N   . ILE B 2 355 ? 2.806   -5.258  28.176  1.00 39.64  ? 355 ILE B N   1 
ATOM   6490  C  CA  . ILE B 2 355 ? 2.328   -4.167  29.037  1.00 43.75  ? 355 ILE B CA  1 
ATOM   6491  C  C   . ILE B 2 355 ? 1.268   -4.688  30.005  1.00 46.80  ? 355 ILE B C   1 
ATOM   6492  O  O   . ILE B 2 355 ? 1.217   -4.307  31.182  1.00 43.49  ? 355 ILE B O   1 
ATOM   6493  C  CB  . ILE B 2 355 ? 1.774   -3.008  28.186  1.00 44.06  ? 355 ILE B CB  1 
ATOM   6494  C  CG1 . ILE B 2 355 ? 2.841   -2.357  27.296  1.00 42.78  ? 355 ILE B CG1 1 
ATOM   6495  C  CG2 . ILE B 2 355 ? 1.131   -1.936  29.065  1.00 44.51  ? 355 ILE B CG2 1 
ATOM   6496  C  CD1 . ILE B 2 355 ? 2.402   -0.969  26.759  1.00 43.36  ? 355 ILE B CD1 1 
ATOM   6497  N  N   . THR B 2 356 ? 0.389   -5.550  29.514  1.00 47.00  ? 356 THR B N   1 
ATOM   6498  C  CA  . THR B 2 356 ? -0.568  -6.253  30.348  1.00 46.44  ? 356 THR B CA  1 
ATOM   6499  C  C   . THR B 2 356 ? -0.583  -7.718  29.925  1.00 44.04  ? 356 THR B C   1 
ATOM   6500  O  O   . THR B 2 356 ? -0.281  -8.044  28.776  1.00 46.55  ? 356 THR B O   1 
ATOM   6501  C  CB  . THR B 2 356 ? -1.963  -5.632  30.240  1.00 48.78  ? 356 THR B CB  1 
ATOM   6502  O  OG1 . THR B 2 356 ? -2.580  -6.030  29.011  1.00 51.55  ? 356 THR B OG1 1 
ATOM   6503  C  CG2 . THR B 2 356 ? -1.921  -4.115  30.290  1.00 45.91  ? 356 THR B CG2 1 
ATOM   6504  N  N   . ASN B 2 357 ? -0.884  -8.612  30.863  1.00 50.26  ? 357 ASN B N   1 
ATOM   6505  C  CA  . ASN B 2 357 ? -1.063  -10.013 30.490  1.00 47.60  ? 357 ASN B CA  1 
ATOM   6506  C  C   . ASN B 2 357 ? -2.080  -10.629 31.442  1.00 48.97  ? 357 ASN B C   1 
ATOM   6507  O  O   . ASN B 2 357 ? -2.077  -10.307 32.638  1.00 47.06  ? 357 ASN B O   1 
ATOM   6508  C  CB  . ASN B 2 357 ? 0.241   -10.847 30.550  1.00 46.12  ? 357 ASN B CB  1 
ATOM   6509  C  CG  . ASN B 2 357 ? 1.457   -10.183 29.860  1.00 47.41  ? 357 ASN B CG  1 
ATOM   6510  O  OD1 . ASN B 2 357 ? 2.050   -9.240  30.381  1.00 42.54  ? 357 ASN B OD1 1 
ATOM   6511  N  ND2 . ASN B 2 357 ? 1.802   -10.673 28.673  1.00 46.56  ? 357 ASN B ND2 1 
ATOM   6512  N  N   . PRO B 2 358 ? -2.913  -11.554 30.972  1.00 52.76  ? 358 PRO B N   1 
ATOM   6513  C  CA  . PRO B 2 358 ? -3.796  -12.260 31.914  1.00 54.23  ? 358 PRO B CA  1 
ATOM   6514  C  C   . PRO B 2 358 ? -2.958  -13.132 32.835  1.00 52.75  ? 358 PRO B C   1 
ATOM   6515  O  O   . PRO B 2 358 ? -2.039  -13.826 32.389  1.00 48.36  ? 358 PRO B O   1 
ATOM   6516  C  CB  . PRO B 2 358 ? -4.715  -13.087 31.007  1.00 55.24  ? 358 PRO B CB  1 
ATOM   6517  C  CG  . PRO B 2 358 ? -3.966  -13.229 29.688  1.00 57.42  ? 358 PRO B CG  1 
ATOM   6518  C  CD  . PRO B 2 358 ? -2.744  -12.310 29.717  1.00 56.18  ? 358 PRO B CD  1 
ATOM   6519  N  N   . ILE B 2 359 ? -3.254  -13.062 34.136  1.00 52.49  ? 359 ILE B N   1 
ATOM   6520  C  CA  . ILE B 2 359 ? -2.352  -13.647 35.124  1.00 48.71  ? 359 ILE B CA  1 
ATOM   6521  C  C   . ILE B 2 359 ? -2.493  -15.165 35.259  1.00 47.74  ? 359 ILE B C   1 
ATOM   6522  O  O   . ILE B 2 359 ? -1.542  -15.818 35.714  1.00 43.86  ? 359 ILE B O   1 
ATOM   6523  C  CB  . ILE B 2 359 ? -2.544  -12.944 36.480  1.00 51.28  ? 359 ILE B CB  1 
ATOM   6524  C  CG1 . ILE B 2 359 ? -1.210  -12.929 37.239  1.00 53.41  ? 359 ILE B CG1 1 
ATOM   6525  C  CG2 . ILE B 2 359 ? -3.687  -13.543 37.262  1.00 52.54  ? 359 ILE B CG2 1 
ATOM   6526  C  CD1 . ILE B 2 359 ? -1.167  -11.941 38.376  1.00 53.75  ? 359 ILE B CD1 1 
ATOM   6527  N  N   . GLY B 2 360 ? -3.623  -15.740 34.836  1.00 46.47  ? 360 GLY B N   1 
ATOM   6528  C  CA  . GLY B 2 360 ? -3.901  -17.157 34.963  1.00 45.47  ? 360 GLY B CA  1 
ATOM   6529  C  C   . GLY B 2 360 ? -2.897  -18.118 34.342  1.00 45.22  ? 360 GLY B C   1 
ATOM   6530  O  O   . GLY B 2 360 ? -2.480  -19.084 34.993  1.00 44.26  ? 360 GLY B O   1 
ATOM   6531  N  N   . PRO B 2 361 ? -2.513  -17.913 33.067  1.00 45.49  ? 361 PRO B N   1 
ATOM   6532  C  CA  . PRO B 2 361 ? -1.462  -18.766 32.486  1.00 45.21  ? 361 PRO B CA  1 
ATOM   6533  C  C   . PRO B 2 361 ? -0.148  -18.684 33.235  1.00 43.27  ? 361 PRO B C   1 
ATOM   6534  O  O   . PRO B 2 361 ? 0.566   -19.689 33.340  1.00 40.48  ? 361 PRO B O   1 
ATOM   6535  C  CB  . PRO B 2 361 ? -1.321  -18.232 31.046  1.00 45.47  ? 361 PRO B CB  1 
ATOM   6536  C  CG  . PRO B 2 361 ? -2.607  -17.592 30.759  1.00 46.27  ? 361 PRO B CG  1 
ATOM   6537  C  CD  . PRO B 2 361 ? -3.024  -16.958 32.067  1.00 48.58  ? 361 PRO B CD  1 
ATOM   6538  N  N   . PHE B 2 362 ? 0.185   -17.520 33.790  1.00 40.38  ? 362 PHE B N   1 
ATOM   6539  C  CA  . PHE B 2 362 ? 1.401   -17.416 34.588  1.00 38.01  ? 362 PHE B CA  1 
ATOM   6540  C  C   . PHE B 2 362 ? 1.263   -18.193 35.895  1.00 38.97  ? 362 PHE B C   1 
ATOM   6541  O  O   . PHE B 2 362 ? 2.218   -18.833 36.344  1.00 40.53  ? 362 PHE B O   1 
ATOM   6542  C  CB  . PHE B 2 362 ? 1.724   -15.945 34.857  1.00 37.82  ? 362 PHE B CB  1 
ATOM   6543  C  CG  . PHE B 2 362 ? 2.146   -15.181 33.622  1.00 40.80  ? 362 PHE B CG  1 
ATOM   6544  C  CD1 . PHE B 2 362 ? 3.463   -15.186 33.205  1.00 38.35  ? 362 PHE B CD1 1 
ATOM   6545  C  CD2 . PHE B 2 362 ? 1.214   -14.493 32.863  1.00 45.09  ? 362 PHE B CD2 1 
ATOM   6546  C  CE1 . PHE B 2 362 ? 3.860   -14.498 32.067  1.00 37.07  ? 362 PHE B CE1 1 
ATOM   6547  C  CE2 . PHE B 2 362 ? 1.600   -13.804 31.715  1.00 43.64  ? 362 PHE B CE2 1 
ATOM   6548  C  CZ  . PHE B 2 362 ? 2.921   -13.815 31.316  1.00 40.29  ? 362 PHE B CZ  1 
ATOM   6549  N  N   . ARG B 2 363 ? 0.089   -18.162 36.519  1.00 38.33  ? 363 ARG B N   1 
ATOM   6550  C  CA  . ARG B 2 363 ? -0.072  -18.880 37.774  1.00 38.17  ? 363 ARG B CA  1 
ATOM   6551  C  C   . ARG B 2 363 ? 0.088   -20.387 37.549  1.00 40.59  ? 363 ARG B C   1 
ATOM   6552  O  O   . ARG B 2 363 ? 0.770   -21.076 38.315  1.00 39.90  ? 363 ARG B O   1 
ATOM   6553  C  CB  . ARG B 2 363 ? -1.442  -18.573 38.378  1.00 45.44  ? 363 ARG B CB  1 
ATOM   6554  C  CG  . ARG B 2 363 ? -1.728  -19.264 39.699  1.00 41.69  ? 363 ARG B CG  1 
ATOM   6555  C  CD  . ARG B 2 363 ? -3.179  -19.002 40.122  1.00 48.36  ? 363 ARG B CD  1 
ATOM   6556  N  NE  . ARG B 2 363 ? -3.373  -17.608 40.506  1.00 60.96  ? 363 ARG B NE  1 
ATOM   6557  C  CZ  . ARG B 2 363 ? -4.230  -16.772 39.925  1.00 59.55  ? 363 ARG B CZ  1 
ATOM   6558  N  NH1 . ARG B 2 363 ? -5.041  -17.172 38.951  1.00 55.58  ? 363 ARG B NH1 1 
ATOM   6559  N  NH2 . ARG B 2 363 ? -4.272  -15.502 40.330  1.00 57.46  ? 363 ARG B NH2 1 
ATOM   6560  N  N   . ILE B 2 364 ? -0.537  -20.913 36.497  1.00 39.66  ? 364 ILE B N   1 
ATOM   6561  C  CA  . ILE B 2 364 ? -0.412  -22.342 36.195  1.00 41.75  ? 364 ILE B CA  1 
ATOM   6562  C  C   . ILE B 2 364 ? 1.056   -22.739 36.046  1.00 39.96  ? 364 ILE B C   1 
ATOM   6563  O  O   . ILE B 2 364 ? 1.487   -23.783 36.552  1.00 39.74  ? 364 ILE B O   1 
ATOM   6564  C  CB  . ILE B 2 364 ? -1.221  -22.682 34.932  1.00 42.42  ? 364 ILE B CB  1 
ATOM   6565  C  CG1 . ILE B 2 364 ? -2.698  -22.404 35.190  1.00 41.12  ? 364 ILE B CG1 1 
ATOM   6566  C  CG2 . ILE B 2 364 ? -1.061  -24.162 34.578  1.00 43.66  ? 364 ILE B CG2 1 
ATOM   6567  C  CD1 . ILE B 2 364 ? -3.530  -22.390 33.952  1.00 43.99  ? 364 ILE B CD1 1 
ATOM   6568  N  N   . ARG B 2 365 ? 1.839   -21.925 35.332  1.00 38.02  ? 365 ARG B N   1 
ATOM   6569  C  CA  . ARG B 2 365 ? 3.260   -22.210 35.136  1.00 39.87  ? 365 ARG B CA  1 
ATOM   6570  C  C   . ARG B 2 365 ? 4.043   -22.170 36.440  1.00 36.20  ? 365 ARG B C   1 
ATOM   6571  O  O   . ARG B 2 365 ? 4.994   -22.932 36.617  1.00 36.63  ? 365 ARG B O   1 
ATOM   6572  C  CB  . ARG B 2 365 ? 3.841   -21.198 34.150  1.00 41.70  ? 365 ARG B CB  1 
ATOM   6573  C  CG  . ARG B 2 365 ? 3.200   -21.276 32.771  1.00 43.75  ? 365 ARG B CG  1 
ATOM   6574  C  CD  . ARG B 2 365 ? 4.254   -21.404 31.733  1.00 49.16  ? 365 ARG B CD  1 
ATOM   6575  N  NE  . ARG B 2 365 ? 5.366   -22.243 32.166  1.00 48.23  ? 365 ARG B NE  1 
ATOM   6576  C  CZ  . ARG B 2 365 ? 6.574   -22.192 31.619  1.00 54.03  ? 365 ARG B CZ  1 
ATOM   6577  N  NH1 . ARG B 2 365 ? 6.879   -21.274 30.712  1.00 52.18  ? 365 ARG B NH1 1 
ATOM   6578  N  NH2 . ARG B 2 365 ? 7.494   -23.085 31.988  1.00 51.69  ? 365 ARG B NH2 1 
ATOM   6579  N  N   . ILE B 2 366 ? 3.722   -21.225 37.329  1.00 36.64  ? 366 ILE B N   1 
ATOM   6580  C  CA  . ILE B 2 366 ? 4.412   -21.160 38.614  1.00 35.36  ? 366 ILE B CA  1 
ATOM   6581  C  C   . ILE B 2 366 ? 4.057   -22.366 39.473  1.00 37.81  ? 366 ILE B C   1 
ATOM   6582  O  O   . ILE B 2 366 ? 4.926   -22.962 40.120  1.00 37.89  ? 366 ILE B O   1 
ATOM   6583  C  CB  . ILE B 2 366 ? 4.081   -19.832 39.314  1.00 38.07  ? 366 ILE B CB  1 
ATOM   6584  C  CG1 . ILE B 2 366 ? 4.496   -18.678 38.388  1.00 36.50  ? 366 ILE B CG1 1 
ATOM   6585  C  CG2 . ILE B 2 366 ? 4.732   -19.758 40.656  1.00 37.74  ? 366 ILE B CG2 1 
ATOM   6586  C  CD1 . ILE B 2 366 ? 4.648   -17.343 39.054  1.00 39.76  ? 366 ILE B CD1 1 
ATOM   6587  N  N   . GLU B 2 367 ? 2.786   -22.764 39.472  1.00 37.31  ? 367 GLU B N   1 
ATOM   6588  C  CA  . GLU B 2 367 ? 2.401   -23.958 40.217  1.00 41.19  ? 367 GLU B CA  1 
ATOM   6589  C  C   . GLU B 2 367 ? 3.137   -25.194 39.715  1.00 38.50  ? 367 GLU B C   1 
ATOM   6590  O  O   . GLU B 2 367 ? 3.557   -26.034 40.517  1.00 39.35  ? 367 GLU B O   1 
ATOM   6591  C  CB  . GLU B 2 367 ? 0.890   -24.145 40.159  1.00 43.37  ? 367 GLU B CB  1 
ATOM   6592  C  CG  . GLU B 2 367 ? 0.142   -23.065 40.918  1.00 45.31  ? 367 GLU B CG  1 
ATOM   6593  C  CD  . GLU B 2 367 ? -1.341  -22.952 40.532  1.00 52.36  ? 367 GLU B CD  1 
ATOM   6594  O  OE1 . GLU B 2 367 ? -1.746  -23.354 39.415  1.00 47.20  ? 367 GLU B OE1 1 
ATOM   6595  O  OE2 . GLU B 2 367 ? -2.121  -22.518 41.405  1.00 54.67  ? 367 GLU B OE2 1 
ATOM   6596  N  N   . ALA B 2 368 ? 3.339   -25.301 38.399  1.00 41.26  ? 368 ALA B N   1 
ATOM   6597  C  CA  . ALA B 2 368 ? 4.066   -26.439 37.832  1.00 39.53  ? 368 ALA B CA  1 
ATOM   6598  C  C   . ALA B 2 368 ? 5.539   -26.399 38.227  1.00 41.01  ? 368 ALA B C   1 
ATOM   6599  O  O   . ALA B 2 368 ? 6.128   -27.440 38.559  1.00 39.21  ? 368 ALA B O   1 
ATOM   6600  C  CB  . ALA B 2 368 ? 3.910   -26.456 36.301  1.00 40.56  ? 368 ALA B CB  1 
ATOM   6601  N  N   . PHE B 2 369 ? 6.146   -25.206 38.192  1.00 38.26  ? 369 PHE B N   1 
ATOM   6602  C  CA  . PHE B 2 369 ? 7.518   -25.031 38.657  1.00 35.59  ? 369 PHE B CA  1 
ATOM   6603  C  C   . PHE B 2 369 ? 7.643   -25.495 40.097  1.00 38.08  ? 369 PHE B C   1 
ATOM   6604  O  O   . PHE B 2 369 ? 8.639   -26.120 40.468  1.00 38.63  ? 369 PHE B O   1 
ATOM   6605  C  CB  . PHE B 2 369 ? 7.913   -23.546 38.535  1.00 37.03  ? 369 PHE B CB  1 
ATOM   6606  C  CG  . PHE B 2 369 ? 9.383   -23.232 38.816  1.00 33.42  ? 369 PHE B CG  1 
ATOM   6607  C  CD1 . PHE B 2 369 ? 10.409  -23.953 38.232  1.00 33.76  ? 369 PHE B CD1 1 
ATOM   6608  C  CD2 . PHE B 2 369 ? 9.713   -22.196 39.682  1.00 32.98  ? 369 PHE B CD2 1 
ATOM   6609  C  CE1 . PHE B 2 369 ? 11.739  -23.628 38.518  1.00 33.92  ? 369 PHE B CE1 1 
ATOM   6610  C  CE2 . PHE B 2 369 ? 11.033  -21.872 39.961  1.00 34.55  ? 369 PHE B CE2 1 
ATOM   6611  C  CZ  . PHE B 2 369 ? 12.039  -22.579 39.387  1.00 32.64  ? 369 PHE B CZ  1 
ATOM   6612  N  N   . LEU B 2 370 ? 6.676   -25.124 40.942  1.00 38.47  ? 370 LEU B N   1 
ATOM   6613  C  CA  . LEU B 2 370 ? 6.735   -25.512 42.345  1.00 42.64  ? 370 LEU B CA  1 
ATOM   6614  C  C   . LEU B 2 370 ? 6.814   -27.024 42.462  1.00 44.79  ? 370 LEU B C   1 
ATOM   6615  O  O   . LEU B 2 370 ? 7.515   -27.560 43.330  1.00 47.09  ? 370 LEU B O   1 
ATOM   6616  C  CB  . LEU B 2 370 ? 5.511   -24.978 43.083  1.00 45.49  ? 370 LEU B CB  1 
ATOM   6617  C  CG  . LEU B 2 370 ? 5.566   -24.696 44.591  1.00 48.82  ? 370 LEU B CG  1 
ATOM   6618  C  CD1 . LEU B 2 370 ? 6.527   -23.571 44.895  1.00 46.02  ? 370 LEU B CD1 1 
ATOM   6619  C  CD2 . LEU B 2 370 ? 4.193   -24.375 45.078  1.00 51.60  ? 370 LEU B CD2 1 
ATOM   6620  N  N   . GLU B 2 371 ? 6.128   -27.725 41.557  1.00 46.88  ? 371 GLU B N   1 
ATOM   6621  C  CA  . GLU B 2 371 ? 6.143   -29.188 41.557  1.00 51.18  ? 371 GLU B CA  1 
ATOM   6622  C  C   . GLU B 2 371 ? 7.530   -29.727 41.230  1.00 56.67  ? 371 GLU B C   1 
ATOM   6623  O  O   . GLU B 2 371 ? 7.977   -30.712 41.825  1.00 57.94  ? 371 GLU B O   1 
ATOM   6624  C  CB  . GLU B 2 371 ? 5.141   -29.711 40.535  1.00 51.57  ? 371 GLU B CB  1 
ATOM   6625  C  CG  . GLU B 2 371 ? 3.690   -29.706 40.992  1.00 57.56  ? 371 GLU B CG  1 
ATOM   6626  C  CD  . GLU B 2 371 ? 3.387   -30.749 42.057  1.00 69.66  ? 371 GLU B CD  1 
ATOM   6627  O  OE1 . GLU B 2 371 ? 3.808   -31.926 41.905  1.00 69.35  ? 371 GLU B OE1 1 
ATOM   6628  O  OE2 . GLU B 2 371 ? 2.711   -30.387 43.046  1.00 72.00  ? 371 GLU B OE2 1 
ATOM   6629  N  N   . THR B 2 372 ? 8.209   -29.111 40.259  1.00 50.86  ? 372 THR B N   1 
ATOM   6630  C  CA  . THR B 2 372 ? 9.556   -29.544 39.905  1.00 55.33  ? 372 THR B CA  1 
ATOM   6631  C  C   . THR B 2 372 ? 10.481  -29.451 41.104  1.00 55.70  ? 372 THR B C   1 
ATOM   6632  O  O   . THR B 2 372 ? 11.324  -30.323 41.316  1.00 58.33  ? 372 THR B O   1 
ATOM   6633  C  CB  . THR B 2 372 ? 10.104  -28.681 38.767  1.00 57.46  ? 372 THR B CB  1 
ATOM   6634  O  OG1 . THR B 2 372 ? 9.274   -28.833 37.615  1.00 57.72  ? 372 THR B OG1 1 
ATOM   6635  C  CG2 . THR B 2 372 ? 11.536  -29.117 38.410  1.00 61.33  ? 372 THR B CG2 1 
ATOM   6636  N  N   . LEU B 2 373 ? 10.342  -28.375 41.884  1.00 52.33  ? 373 LEU B N   1 
ATOM   6637  C  CA  . LEU B 2 373 ? 11.187  -28.166 43.051  1.00 53.10  ? 373 LEU B CA  1 
ATOM   6638  C  C   . LEU B 2 373 ? 11.007  -29.294 44.057  1.00 56.86  ? 373 LEU B C   1 
ATOM   6639  O  O   . LEU B 2 373 ? 11.982  -29.764 44.654  1.00 56.49  ? 373 LEU B O   1 
ATOM   6640  C  CB  . LEU B 2 373 ? 10.853  -26.810 43.689  1.00 46.70  ? 373 LEU B CB  1 
ATOM   6641  C  CG  . LEU B 2 373 ? 11.287  -25.532 42.986  1.00 46.64  ? 373 LEU B CG  1 
ATOM   6642  C  CD1 . LEU B 2 373 ? 11.270  -24.329 43.951  1.00 42.05  ? 373 LEU B CD1 1 
ATOM   6643  C  CD2 . LEU B 2 373 ? 12.663  -25.747 42.428  1.00 42.76  ? 373 LEU B CD2 1 
ATOM   6644  N  N   . SER B 2 374 ? 9.761   -29.751 44.242  1.00 59.53  ? 374 SER B N   1 
ATOM   6645  C  CA  . SER B 2 374 ? 9.413   -30.761 45.240  1.00 63.92  ? 374 SER B CA  1 
ATOM   6646  C  C   . SER B 2 374 ? 9.892   -32.166 44.882  1.00 66.85  ? 374 SER B C   1 
ATOM   6647  O  O   . SER B 2 374 ? 9.789   -33.056 45.729  1.00 67.48  ? 374 SER B O   1 
ATOM   6648  C  CB  . SER B 2 374 ? 7.892   -30.760 45.478  1.00 58.32  ? 374 SER B CB  1 
ATOM   6649  O  OG  . SER B 2 374 ? 7.221   -31.743 44.701  1.00 65.37  ? 374 SER B OG  1 
ATOM   6650  N  N   . GLU B 2 375 ? 10.394  -32.396 43.672  1.00 73.38  ? 375 GLU B N   1 
ATOM   6651  C  CA  . GLU B 2 375 ? 11.056  -33.650 43.331  1.00 81.96  ? 375 GLU B CA  1 
ATOM   6652  C  C   . GLU B 2 375 ? 12.568  -33.446 43.288  1.00 87.97  ? 375 GLU B C   1 
ATOM   6653  O  O   . GLU B 2 375 ? 13.063  -32.324 43.119  1.00 81.42  ? 375 GLU B O   1 
ATOM   6654  C  CB  . GLU B 2 375 ? 10.569  -34.202 41.986  1.00 80.77  ? 375 GLU B CB  1 
ATOM   6655  C  CG  . GLU B 2 375 ? 9.519   -33.353 41.329  1.00 78.30  ? 375 GLU B CG  1 
ATOM   6656  C  CD  . GLU B 2 375 ? 9.484   -33.521 39.829  1.00 83.77  ? 375 GLU B CD  1 
ATOM   6657  O  OE1 . GLU B 2 375 ? 10.442  -33.056 39.166  1.00 80.98  ? 375 GLU B OE1 1 
ATOM   6658  O  OE2 . GLU B 2 375 ? 8.509   -34.109 39.315  1.00 84.89  ? 375 GLU B OE2 1 
ATOM   6659  N  N   . GLU B 2 376 ? 13.298  -34.556 43.440  1.00 95.13  ? 376 GLU B N   1 
ATOM   6660  C  CA  . GLU B 2 376 ? 14.764  -34.548 43.492  1.00 95.99  ? 376 GLU B CA  1 
ATOM   6661  C  C   . GLU B 2 376 ? 15.311  -33.557 44.523  1.00 94.70  ? 376 GLU B C   1 
ATOM   6662  O  O   . GLU B 2 376 ? 16.144  -32.706 44.198  1.00 89.80  ? 376 GLU B O   1 
ATOM   6663  C  CB  . GLU B 2 376 ? 15.350  -34.226 42.115  1.00 97.40  ? 376 GLU B CB  1 
ATOM   6664  C  CG  . GLU B 2 376 ? 14.752  -35.012 40.962  1.00 93.04  ? 376 GLU B CG  1 
ATOM   6665  C  CD  . GLU B 2 376 ? 15.808  -35.434 39.966  1.00 90.74  ? 376 GLU B CD  1 
ATOM   6666  O  OE1 . GLU B 2 376 ? 16.637  -34.575 39.601  1.00 92.79  ? 376 GLU B OE1 1 
ATOM   6667  O  OE2 . GLU B 2 376 ? 15.810  -36.609 39.543  1.00 93.71  ? 376 GLU B OE2 1 
ATOM   6668  N  N   . ASN C 1 6   ? -0.876  -58.342 49.123  1.00 74.46  ? 6   ASN C N   1 
ATOM   6669  C  CA  . ASN C 1 6   ? -0.660  -58.485 47.677  1.00 80.75  ? 6   ASN C CA  1 
ATOM   6670  C  C   . ASN C 1 6   ? -0.271  -59.928 47.366  1.00 77.31  ? 6   ASN C C   1 
ATOM   6671  O  O   . ASN C 1 6   ? -0.415  -60.793 48.233  1.00 79.91  ? 6   ASN C O   1 
ATOM   6672  C  CB  . ASN C 1 6   ? 0.416   -57.522 47.177  1.00 76.40  ? 6   ASN C CB  1 
ATOM   6673  C  CG  . ASN C 1 6   ? -0.082  -56.626 46.063  1.00 73.81  ? 6   ASN C CG  1 
ATOM   6674  O  OD1 . ASN C 1 6   ? -0.642  -57.106 45.075  1.00 74.23  ? 6   ASN C OD1 1 
ATOM   6675  N  ND2 . ASN C 1 6   ? 0.141   -55.318 46.202  1.00 72.64  ? 6   ASN C ND2 1 
ATOM   6676  N  N   . LYS C 1 7   ? 0.225   -60.205 46.153  1.00 72.68  ? 7   LYS C N   1 
ATOM   6677  C  CA  . LYS C 1 7   ? 0.523   -61.596 45.823  1.00 64.65  ? 7   LYS C CA  1 
ATOM   6678  C  C   . LYS C 1 7   ? 1.956   -61.944 46.224  1.00 60.74  ? 7   LYS C C   1 
ATOM   6679  O  O   . LYS C 1 7   ? 2.178   -62.897 46.978  1.00 61.46  ? 7   LYS C O   1 
ATOM   6680  C  CB  . LYS C 1 7   ? 0.257   -61.869 44.333  1.00 64.36  ? 7   LYS C CB  1 
ATOM   6681  C  CG  . LYS C 1 7   ? 0.832   -63.178 43.688  1.00 60.52  ? 7   LYS C CG  1 
ATOM   6682  C  CD  . LYS C 1 7   ? 0.939   -64.463 44.568  1.00 65.59  ? 7   LYS C CD  1 
ATOM   6683  C  CE  . LYS C 1 7   ? -0.325  -64.795 45.370  1.00 70.99  ? 7   LYS C CE  1 
ATOM   6684  N  NZ  . LYS C 1 7   ? -0.115  -65.841 46.438  1.00 70.08  ? 7   LYS C NZ  1 
ATOM   6685  N  N   . TYR C 1 8   ? 2.928   -61.177 45.756  1.00 54.16  ? 8   TYR C N   1 
ATOM   6686  C  CA  . TYR C 1 8   ? 4.300   -61.481 46.109  1.00 50.30  ? 8   TYR C CA  1 
ATOM   6687  C  C   . TYR C 1 8   ? 4.857   -60.366 46.987  1.00 49.97  ? 8   TYR C C   1 
ATOM   6688  O  O   . TYR C 1 8   ? 4.477   -59.198 46.829  1.00 47.54  ? 8   TYR C O   1 
ATOM   6689  C  CB  . TYR C 1 8   ? 5.207   -61.592 44.871  1.00 47.16  ? 8   TYR C CB  1 
ATOM   6690  C  CG  . TYR C 1 8   ? 4.766   -62.619 43.847  1.00 49.77  ? 8   TYR C CG  1 
ATOM   6691  C  CD1 . TYR C 1 8   ? 4.929   -63.979 44.073  1.00 49.14  ? 8   TYR C CD1 1 
ATOM   6692  C  CD2 . TYR C 1 8   ? 4.183   -62.216 42.644  1.00 47.21  ? 8   TYR C CD2 1 
ATOM   6693  C  CE1 . TYR C 1 8   ? 4.524   -64.916 43.147  1.00 48.51  ? 8   TYR C CE1 1 
ATOM   6694  C  CE2 . TYR C 1 8   ? 3.768   -63.158 41.697  1.00 46.76  ? 8   TYR C CE2 1 
ATOM   6695  C  CZ  . TYR C 1 8   ? 3.938   -64.511 41.957  1.00 51.82  ? 8   TYR C CZ  1 
ATOM   6696  O  OH  . TYR C 1 8   ? 3.540   -65.467 41.032  1.00 52.10  ? 8   TYR C OH  1 
ATOM   6697  N  N   . PRO C 1 9   ? 5.813   -60.681 47.863  1.00 49.03  ? 9   PRO C N   1 
ATOM   6698  C  CA  . PRO C 1 9   ? 6.566   -59.617 48.554  1.00 45.00  ? 9   PRO C CA  1 
ATOM   6699  C  C   . PRO C 1 9   ? 7.336   -58.768 47.574  1.00 44.72  ? 9   PRO C C   1 
ATOM   6700  O  O   . PRO C 1 9   ? 7.741   -59.230 46.500  1.00 41.23  ? 9   PRO C O   1 
ATOM   6701  C  CB  . PRO C 1 9   ? 7.531   -60.385 49.471  1.00 43.89  ? 9   PRO C CB  1 
ATOM   6702  C  CG  . PRO C 1 9   ? 7.706   -61.724 48.761  1.00 47.24  ? 9   PRO C CG  1 
ATOM   6703  C  CD  . PRO C 1 9   ? 6.316   -62.024 48.188  1.00 44.74  ? 9   PRO C CD  1 
ATOM   6704  N  N   . THR C 1 10  ? 7.585   -57.519 47.963  1.00 43.45  ? 10  THR C N   1 
ATOM   6705  C  CA  . THR C 1 10  ? 8.331   -56.608 47.097  1.00 43.68  ? 10  THR C CA  1 
ATOM   6706  C  C   . THR C 1 10  ? 9.268   -55.763 47.957  1.00 44.03  ? 10  THR C C   1 
ATOM   6707  O  O   . THR C 1 10  ? 9.074   -55.630 49.172  1.00 46.43  ? 10  THR C O   1 
ATOM   6708  C  CB  . THR C 1 10  ? 7.368   -55.721 46.286  1.00 43.84  ? 10  THR C CB  1 
ATOM   6709  O  OG1 . THR C 1 10  ? 8.001   -55.219 45.107  1.00 49.14  ? 10  THR C OG1 1 
ATOM   6710  C  CG2 . THR C 1 10  ? 6.892   -54.542 47.162  1.00 47.89  ? 10  THR C CG2 1 
ATOM   6711  N  N   . GLU C 1 11  ? 10.281  -55.183 47.312  1.00 42.54  ? 11  GLU C N   1 
ATOM   6712  C  CA  . GLU C 1 11  ? 11.272  -54.360 48.002  1.00 42.75  ? 11  GLU C CA  1 
ATOM   6713  C  C   . GLU C 1 11  ? 12.071  -53.562 46.983  1.00 39.28  ? 11  GLU C C   1 
ATOM   6714  O  O   . GLU C 1 11  ? 12.301  -54.031 45.866  1.00 38.13  ? 11  GLU C O   1 
ATOM   6715  C  CB  . GLU C 1 11  ? 12.189  -55.236 48.867  1.00 49.07  ? 11  GLU C CB  1 
ATOM   6716  C  CG  . GLU C 1 11  ? 13.622  -54.754 49.039  1.00 48.54  ? 11  GLU C CG  1 
ATOM   6717  C  CD  . GLU C 1 11  ? 14.465  -55.747 49.829  1.00 56.16  ? 11  GLU C CD  1 
ATOM   6718  O  OE1 . GLU C 1 11  ? 13.876  -56.680 50.456  1.00 51.03  ? 11  GLU C OE1 1 
ATOM   6719  O  OE2 . GLU C 1 11  ? 15.714  -55.612 49.755  1.00 51.81  ? 11  GLU C OE2 1 
ATOM   6720  N  N   . GLN C 1 12  ? 12.445  -52.333 47.331  1.00 37.13  ? 12  GLN C N   1 
ATOM   6721  C  CA  . GLN C 1 12  ? 13.313  -51.502 46.470  1.00 38.56  ? 12  GLN C CA  1 
ATOM   6722  C  C   . GLN C 1 12  ? 14.755  -52.006 46.529  1.00 39.67  ? 12  GLN C C   1 
ATOM   6723  O  O   . GLN C 1 12  ? 15.199  -52.436 47.543  1.00 41.34  ? 12  GLN C O   1 
ATOM   6724  C  CB  . GLN C 1 12  ? 13.312  -50.072 46.975  1.00 36.37  ? 12  GLN C CB  1 
ATOM   6725  C  CG  . GLN C 1 12  ? 11.918  -49.604 47.309  1.00 42.50  ? 12  GLN C CG  1 
ATOM   6726  C  CD  . GLN C 1 12  ? 11.467  -48.657 46.240  1.00 42.78  ? 12  GLN C CD  1 
ATOM   6727  O  OE1 . GLN C 1 12  ? 11.568  -48.986 45.082  1.00 50.31  ? 12  GLN C OE1 1 
ATOM   6728  N  NE2 . GLN C 1 12  ? 11.026  -47.472 46.621  1.00 51.74  ? 12  GLN C NE2 1 
ATOM   6729  N  N   . LEU C 1 13  ? 15.448  -51.915 45.417  1.00 37.03  ? 13  LEU C N   1 
ATOM   6730  C  CA  . LEU C 1 13  ? 16.842  -52.299 45.298  1.00 38.20  ? 13  LEU C CA  1 
ATOM   6731  C  C   . LEU C 1 13  ? 17.698  -51.409 46.181  1.00 40.72  ? 13  LEU C C   1 
ATOM   6732  O  O   . LEU C 1 13  ? 17.681  -50.178 46.037  1.00 39.29  ? 13  LEU C O   1 
ATOM   6733  C  CB  . LEU C 1 13  ? 17.280  -52.173 43.847  1.00 36.05  ? 13  LEU C CB  1 
ATOM   6734  C  CG  . LEU C 1 13  ? 18.460  -52.952 43.345  1.00 38.33  ? 13  LEU C CG  1 
ATOM   6735  C  CD1 . LEU C 1 13  ? 18.338  -54.452 43.556  1.00 40.50  ? 13  LEU C CD1 1 
ATOM   6736  C  CD2 . LEU C 1 13  ? 18.608  -52.620 41.837  1.00 38.30  ? 13  LEU C CD2 1 
ATOM   6737  N  N   . LYS C 1 14  ? 18.452  -52.035 47.081  1.00 39.16  ? 14  LYS C N   1 
ATOM   6738  C  CA  . LYS C 1 14  ? 19.342  -51.279 47.961  1.00 40.32  ? 14  LYS C CA  1 
ATOM   6739  C  C   . LYS C 1 14  ? 20.437  -50.580 47.158  1.00 38.62  ? 14  LYS C C   1 
ATOM   6740  O  O   . LYS C 1 14  ? 20.826  -49.447 47.479  1.00 39.11  ? 14  LYS C O   1 
ATOM   6741  C  CB  . LYS C 1 14  ? 19.970  -52.206 49.011  1.00 41.25  ? 14  LYS C CB  1 
ATOM   6742  C  CG  . LYS C 1 14  ? 19.004  -52.701 50.093  1.00 46.10  ? 14  LYS C CG  1 
ATOM   6743  C  CD  . LYS C 1 14  ? 19.507  -53.986 50.779  1.00 45.84  ? 14  LYS C CD  1 
ATOM   6744  C  CE  . LYS C 1 14  ? 18.692  -55.201 50.330  1.00 46.70  ? 14  LYS C CE  1 
ATOM   6745  N  NZ  . LYS C 1 14  ? 17.757  -55.690 51.430  1.00 58.84  ? 14  LYS C NZ  1 
ATOM   6746  N  N   . LEU C 1 15  ? 20.934  -51.228 46.091  1.00 34.82  ? 15  LEU C N   1 
ATOM   6747  C  CA  . LEU C 1 15  ? 22.067  -50.688 45.358  1.00 34.49  ? 15  LEU C CA  1 
ATOM   6748  C  C   . LEU C 1 15  ? 21.656  -49.638 44.330  1.00 33.14  ? 15  LEU C C   1 
ATOM   6749  O  O   . LEU C 1 15  ? 22.514  -49.193 43.563  1.00 33.38  ? 15  LEU C O   1 
ATOM   6750  C  CB  . LEU C 1 15  ? 22.845  -51.832 44.682  1.00 31.47  ? 15  LEU C CB  1 
ATOM   6751  C  CG  . LEU C 1 15  ? 23.538  -52.742 45.695  1.00 34.98  ? 15  LEU C CG  1 
ATOM   6752  C  CD1 . LEU C 1 15  ? 23.928  -54.101 45.021  1.00 33.66  ? 15  LEU C CD1 1 
ATOM   6753  C  CD2 . LEU C 1 15  ? 24.765  -52.062 46.281  1.00 33.98  ? 15  LEU C CD2 1 
ATOM   6754  N  N   . TRP C 1 16  ? 20.368  -49.274 44.293  1.00 33.57  ? 16  TRP C N   1 
ATOM   6755  C  CA  . TRP C 1 16  ? 19.875  -48.273 43.358  1.00 33.96  ? 16  TRP C CA  1 
ATOM   6756  C  C   . TRP C 1 16  ? 20.723  -47.021 43.401  1.00 35.81  ? 16  TRP C C   1 
ATOM   6757  O  O   . TRP C 1 16  ? 21.244  -46.559 42.379  1.00 32.02  ? 16  TRP C O   1 
ATOM   6758  C  CB  . TRP C 1 16  ? 18.432  -47.936 43.716  1.00 39.27  ? 16  TRP C CB  1 
ATOM   6759  C  CG  . TRP C 1 16  ? 17.696  -47.126 42.655  1.00 42.68  ? 16  TRP C CG  1 
ATOM   6760  C  CD1 . TRP C 1 16  ? 17.232  -45.817 42.757  1.00 45.37  ? 16  TRP C CD1 1 
ATOM   6761  C  CD2 . TRP C 1 16  ? 17.378  -47.565 41.349  1.00 43.31  ? 16  TRP C CD2 1 
ATOM   6762  N  NE1 . TRP C 1 16  ? 16.630  -45.443 41.572  1.00 47.22  ? 16  TRP C NE1 1 
ATOM   6763  C  CE2 . TRP C 1 16  ? 16.718  -46.499 40.692  1.00 43.56  ? 16  TRP C CE2 1 
ATOM   6764  C  CE3 . TRP C 1 16  ? 17.602  -48.765 40.659  1.00 43.31  ? 16  TRP C CE3 1 
ATOM   6765  C  CZ2 . TRP C 1 16  ? 16.264  -46.617 39.395  1.00 44.26  ? 16  TRP C CZ2 1 
ATOM   6766  C  CZ3 . TRP C 1 16  ? 17.166  -48.887 39.412  1.00 36.68  ? 16  TRP C CZ3 1 
ATOM   6767  C  CH2 . TRP C 1 16  ? 16.500  -47.814 38.763  1.00 36.98  ? 16  TRP C CH2 1 
ATOM   6768  N  N   . GLY C 1 17  ? 20.882  -46.480 44.595  1.00 32.31  ? 17  GLY C N   1 
ATOM   6769  C  CA  . GLY C 1 17  ? 21.605  -45.230 44.760  1.00 36.53  ? 17  GLY C CA  1 
ATOM   6770  C  C   . GLY C 1 17  ? 23.027  -45.324 44.243  1.00 38.30  ? 17  GLY C C   1 
ATOM   6771  O  O   . GLY C 1 17  ? 23.524  -44.400 43.582  1.00 31.59  ? 17  GLY C O   1 
ATOM   6772  N  N   . LYS C 1 18  ? 23.701  -46.446 44.531  1.00 32.40  ? 18  LYS C N   1 
ATOM   6773  C  CA  . LYS C 1 18  ? 25.053  -46.613 44.026  1.00 30.83  ? 18  LYS C CA  1 
ATOM   6774  C  C   . LYS C 1 18  ? 25.071  -46.687 42.504  1.00 29.83  ? 18  LYS C C   1 
ATOM   6775  O  O   . LYS C 1 18  ? 25.964  -46.124 41.871  1.00 31.68  ? 18  LYS C O   1 
ATOM   6776  C  CB  . LYS C 1 18  ? 25.706  -47.846 44.663  1.00 29.03  ? 18  LYS C CB  1 
ATOM   6777  C  CG  . LYS C 1 18  ? 27.183  -47.935 44.319  1.00 33.80  ? 18  LYS C CG  1 
ATOM   6778  C  CD  . LYS C 1 18  ? 27.909  -48.957 45.173  1.00 37.19  ? 18  LYS C CD  1 
ATOM   6779  C  CE  . LYS C 1 18  ? 29.412  -48.888 44.990  1.00 38.00  ? 18  LYS C CE  1 
ATOM   6780  N  NZ  . LYS C 1 18  ? 29.969  -49.850 45.999  1.00 42.86  ? 18  LYS C NZ  1 
ATOM   6781  N  N   . ALA C 1 19  ? 24.074  -47.337 41.875  1.00 25.97  ? 19  ALA C N   1 
ATOM   6782  C  CA  . ALA C 1 19  ? 24.053  -47.393 40.407  1.00 30.34  ? 19  ALA C CA  1 
ATOM   6783  C  C   . ALA C 1 19  ? 23.942  -45.994 39.841  1.00 28.84  ? 19  ALA C C   1 
ATOM   6784  O  O   . ALA C 1 19  ? 24.641  -45.646 38.895  1.00 26.75  ? 19  ALA C O   1 
ATOM   6785  C  CB  . ALA C 1 19  ? 22.882  -48.234 39.888  1.00 28.92  ? 19  ALA C CB  1 
ATOM   6786  N  N   . LYS C 1 20  ? 23.127  -45.163 40.485  1.00 29.90  ? 20  LYS C N   1 
ATOM   6787  C  CA  . LYS C 1 20  ? 22.968  -43.786 40.032  1.00 30.90  ? 20  LYS C CA  1 
ATOM   6788  C  C   . LYS C 1 20  ? 24.253  -42.990 40.227  1.00 28.29  ? 20  LYS C C   1 
ATOM   6789  O  O   . LYS C 1 20  ? 24.651  -42.213 39.339  1.00 31.28  ? 20  LYS C O   1 
ATOM   6790  C  CB  . LYS C 1 20  ? 21.810  -43.131 40.794  1.00 33.24  ? 20  LYS C CB  1 
ATOM   6791  C  CG  . LYS C 1 20  ? 20.431  -43.755 40.553  1.00 36.90  ? 20  LYS C CG  1 
ATOM   6792  C  CD  . LYS C 1 20  ? 20.046  -43.732 39.099  1.00 43.87  ? 20  LYS C CD  1 
ATOM   6793  C  CE  . LYS C 1 20  ? 18.524  -43.690 38.945  1.00 48.63  ? 20  LYS C CE  1 
ATOM   6794  N  NZ  . LYS C 1 20  ? 18.067  -43.960 37.554  1.00 46.10  ? 20  LYS C NZ  1 
ATOM   6795  N  N   . GLU C 1 21  ? 24.900  -43.154 41.370  1.00 31.01  ? 21  GLU C N   1 
ATOM   6796  C  CA  . GLU C 1 21  ? 26.101  -42.365 41.660  1.00 32.68  ? 21  GLU C CA  1 
ATOM   6797  C  C   . GLU C 1 21  ? 27.258  -42.758 40.755  1.00 27.41  ? 21  GLU C C   1 
ATOM   6798  O  O   . GLU C 1 21  ? 27.989  -41.884 40.271  1.00 30.83  ? 21  GLU C O   1 
ATOM   6799  C  CB  . GLU C 1 21  ? 26.511  -42.512 43.113  1.00 32.85  ? 21  GLU C CB  1 
ATOM   6800  C  CG  . GLU C 1 21  ? 27.994  -42.197 43.375  1.00 45.41  ? 21  GLU C CG  1 
ATOM   6801  C  CD  . GLU C 1 21  ? 28.379  -42.314 44.861  1.00 60.35  ? 21  GLU C CD  1 
ATOM   6802  O  OE1 . GLU C 1 21  ? 29.019  -43.317 45.261  1.00 63.74  ? 21  GLU C OE1 1 
ATOM   6803  O  OE2 . GLU C 1 21  ? 28.046  -41.381 45.622  1.00 65.76  ? 21  GLU C OE2 1 
ATOM   6804  N  N   . LEU C 1 22  ? 27.420  -44.064 40.457  1.00 26.02  ? 22  LEU C N   1 
ATOM   6805  C  CA  . LEU C 1 22  ? 28.487  -44.476 39.552  1.00 27.47  ? 22  LEU C CA  1 
ATOM   6806  C  C   . LEU C 1 22  ? 28.309  -43.852 38.168  1.00 24.43  ? 22  LEU C C   1 
ATOM   6807  O  O   . LEU C 1 22  ? 29.277  -43.436 37.521  1.00 27.04  ? 22  LEU C O   1 
ATOM   6808  C  CB  . LEU C 1 22  ? 28.544  -46.017 39.448  1.00 23.83  ? 22  LEU C CB  1 
ATOM   6809  C  CG  . LEU C 1 22  ? 29.095  -46.730 40.692  1.00 25.79  ? 22  LEU C CG  1 
ATOM   6810  C  CD1 . LEU C 1 22  ? 28.690  -48.215 40.495  1.00 28.92  ? 22  LEU C CD1 1 
ATOM   6811  C  CD2 . LEU C 1 22  ? 30.624  -46.634 40.932  1.00 26.59  ? 22  LEU C CD2 1 
ATOM   6812  N  N   . ARG C 1 23  ? 27.077  -43.769 37.707  1.00 21.91  ? 23  ARG C N   1 
ATOM   6813  C  CA  . ARG C 1 23  ? 26.784  -43.183 36.419  1.00 26.33  ? 23  ARG C CA  1 
ATOM   6814  C  C   . ARG C 1 23  ? 27.069  -41.699 36.455  1.00 23.09  ? 23  ARG C C   1 
ATOM   6815  O  O   . ARG C 1 23  ? 27.634  -41.145 35.516  1.00 24.91  ? 23  ARG C O   1 
ATOM   6816  C  CB  . ARG C 1 23  ? 25.308  -43.434 36.071  1.00 27.23  ? 23  ARG C CB  1 
ATOM   6817  C  CG  . ARG C 1 23  ? 24.862  -42.750 34.806  1.00 25.02  ? 23  ARG C CG  1 
ATOM   6818  C  CD  . ARG C 1 23  ? 23.429  -43.116 34.383  1.00 26.53  ? 23  ARG C CD  1 
ATOM   6819  N  NE  . ARG C 1 23  ? 22.945  -42.258 33.284  1.00 29.35  ? 23  ARG C NE  1 
ATOM   6820  C  CZ  . ARG C 1 23  ? 22.390  -41.060 33.470  1.00 34.43  ? 23  ARG C CZ  1 
ATOM   6821  N  NH1 . ARG C 1 23  ? 22.187  -40.575 34.685  1.00 33.34  ? 23  ARG C NH1 1 
ATOM   6822  N  NH2 . ARG C 1 23  ? 21.962  -40.363 32.420  1.00 33.63  ? 23  ARG C NH2 1 
ATOM   6823  N  N   . GLU C 1 24  ? 26.667  -41.034 37.515  1.00 25.41  ? 24  GLU C N   1 
ATOM   6824  C  CA  . GLU C 1 24  ? 26.958  -39.598 37.559  1.00 25.75  ? 24  GLU C CA  1 
ATOM   6825  C  C   . GLU C 1 24  ? 28.449  -39.331 37.624  1.00 28.26  ? 24  GLU C C   1 
ATOM   6826  O  O   . GLU C 1 24  ? 28.938  -38.352 37.024  1.00 26.98  ? 24  GLU C O   1 
ATOM   6827  C  CB  . GLU C 1 24  ? 26.281  -38.934 38.754  1.00 32.35  ? 24  GLU C CB  1 
ATOM   6828  C  CG  . GLU C 1 24  ? 24.765  -38.944 38.710  1.00 38.24  ? 24  GLU C CG  1 
ATOM   6829  C  CD  . GLU C 1 24  ? 24.144  -37.812 37.842  1.00 52.16  ? 24  GLU C CD  1 
ATOM   6830  O  OE1 . GLU C 1 24  ? 22.980  -37.992 37.415  1.00 59.22  ? 24  GLU C OE1 1 
ATOM   6831  O  OE2 . GLU C 1 24  ? 24.795  -36.769 37.557  1.00 55.89  ? 24  GLU C OE2 1 
ATOM   6832  N  N   . GLN C 1 25  ? 29.179  -40.132 38.420  1.00 25.38  ? 25  GLN C N   1 
ATOM   6833  C  CA  . GLN C 1 25  ? 30.628  -39.977 38.499  1.00 27.38  ? 25  GLN C CA  1 
ATOM   6834  C  C   . GLN C 1 25  ? 31.286  -40.179 37.144  1.00 26.44  ? 25  GLN C C   1 
ATOM   6835  O  O   . GLN C 1 25  ? 32.273  -39.506 36.822  1.00 28.04  ? 25  GLN C O   1 
ATOM   6836  C  CB  . GLN C 1 25  ? 31.251  -40.957 39.481  1.00 26.52  ? 25  GLN C CB  1 
ATOM   6837  C  CG  . GLN C 1 25  ? 32.488  -40.414 40.101  1.00 34.90  ? 25  GLN C CG  1 
ATOM   6838  C  CD  . GLN C 1 25  ? 32.206  -39.235 41.064  1.00 45.14  ? 25  GLN C CD  1 
ATOM   6839  O  OE1 . GLN C 1 25  ? 32.250  -38.044 40.670  1.00 47.12  ? 25  GLN C OE1 1 
ATOM   6840  N  NE2 . GLN C 1 25  ? 31.917  -39.561 42.318  1.00 51.50  ? 25  GLN C NE2 1 
ATOM   6841  N  N   . TYR C 1 26  ? 30.789  -41.134 36.361  1.00 24.29  ? 26  TYR C N   1 
ATOM   6842  C  CA  . TYR C 1 26  ? 31.358  -41.365 35.039  1.00 22.77  ? 26  TYR C CA  1 
ATOM   6843  C  C   . TYR C 1 26  ? 31.300  -40.112 34.193  1.00 24.98  ? 26  TYR C C   1 
ATOM   6844  O  O   . TYR C 1 26  ? 32.308  -39.713 33.625  1.00 24.39  ? 26  TYR C O   1 
ATOM   6845  C  CB  . TYR C 1 26  ? 30.638  -42.518 34.369  1.00 23.08  ? 26  TYR C CB  1 
ATOM   6846  C  CG  . TYR C 1 26  ? 30.929  -42.683 32.897  1.00 24.38  ? 26  TYR C CG  1 
ATOM   6847  C  CD1 . TYR C 1 26  ? 32.023  -43.450 32.444  1.00 23.79  ? 26  TYR C CD1 1 
ATOM   6848  C  CD2 . TYR C 1 26  ? 30.096  -42.101 31.957  1.00 19.68  ? 26  TYR C CD2 1 
ATOM   6849  C  CE1 . TYR C 1 26  ? 32.279  -43.633 31.074  1.00 22.74  ? 26  TYR C CE1 1 
ATOM   6850  C  CE2 . TYR C 1 26  ? 30.316  -42.287 30.563  1.00 20.60  ? 26  TYR C CE2 1 
ATOM   6851  C  CZ  . TYR C 1 26  ? 31.412  -43.053 30.129  1.00 23.70  ? 26  TYR C CZ  1 
ATOM   6852  O  OH  . TYR C 1 26  ? 31.629  -43.261 28.777  1.00 22.58  ? 26  TYR C OH  1 
ATOM   6853  N  N   . TYR C 1 27  ? 30.127  -39.465 34.116  1.00 26.65  ? 27  TYR C N   1 
ATOM   6854  C  CA  . TYR C 1 27  ? 29.995  -38.239 33.308  1.00 25.72  ? 27  TYR C CA  1 
ATOM   6855  C  C   . TYR C 1 27  ? 30.769  -37.075 33.926  1.00 28.17  ? 27  TYR C C   1 
ATOM   6856  O  O   . TYR C 1 27  ? 31.335  -36.248 33.196  1.00 26.50  ? 27  TYR C O   1 
ATOM   6857  C  CB  . TYR C 1 27  ? 28.504  -37.904 33.147  1.00 23.81  ? 27  TYR C CB  1 
ATOM   6858  C  CG  . TYR C 1 27  ? 27.824  -38.880 32.213  1.00 24.48  ? 27  TYR C CG  1 
ATOM   6859  C  CD1 . TYR C 1 27  ? 28.167  -38.928 30.828  1.00 23.56  ? 27  TYR C CD1 1 
ATOM   6860  C  CD2 . TYR C 1 27  ? 26.846  -39.753 32.694  1.00 24.32  ? 27  TYR C CD2 1 
ATOM   6861  C  CE1 . TYR C 1 27  ? 27.561  -39.853 29.970  1.00 23.01  ? 27  TYR C CE1 1 
ATOM   6862  C  CE2 . TYR C 1 27  ? 26.227  -40.692 31.832  1.00 25.59  ? 27  TYR C CE2 1 
ATOM   6863  C  CZ  . TYR C 1 27  ? 26.599  -40.727 30.488  1.00 24.26  ? 27  TYR C CZ  1 
ATOM   6864  O  OH  . TYR C 1 27  ? 26.010  -41.601 29.601  1.00 23.22  ? 27  TYR C OH  1 
ATOM   6865  N  N   A MET C 1 28  ? 30.839  -36.987 35.254  0.59 26.54  ? 28  MET C N   1 
ATOM   6866  N  N   B MET C 1 28  ? 30.825  -36.996 35.257  0.41 26.57  ? 28  MET C N   1 
ATOM   6867  C  CA  A MET C 1 28  ? 31.629  -35.904 35.829  0.59 29.28  ? 28  MET C CA  1 
ATOM   6868  C  CA  B MET C 1 28  ? 31.628  -35.950 35.880  0.41 29.28  ? 28  MET C CA  1 
ATOM   6869  C  C   A MET C 1 28  ? 33.124  -36.121 35.572  0.59 28.80  ? 28  MET C C   1 
ATOM   6870  C  C   B MET C 1 28  ? 33.103  -36.136 35.538  0.41 28.80  ? 28  MET C C   1 
ATOM   6871  O  O   A MET C 1 28  ? 33.846  -35.170 35.249  0.59 29.18  ? 28  MET C O   1 
ATOM   6872  O  O   B MET C 1 28  ? 33.786  -35.186 35.141  0.41 29.12  ? 28  MET C O   1 
ATOM   6873  C  CB  A MET C 1 28  ? 31.308  -35.761 37.320  0.59 30.57  ? 28  MET C CB  1 
ATOM   6874  C  CB  B MET C 1 28  ? 31.412  -35.954 37.395  0.41 30.56  ? 28  MET C CB  1 
ATOM   6875  C  CG  A MET C 1 28  ? 30.013  -35.003 37.648  0.59 31.57  ? 28  MET C CG  1 
ATOM   6876  C  CG  B MET C 1 28  ? 32.565  -35.346 38.173  0.41 33.31  ? 28  MET C CG  1 
ATOM   6877  S  SD  A MET C 1 28  ? 29.396  -33.734 36.475  0.59 42.49  ? 28  MET C SD  1 
ATOM   6878  S  SD  B MET C 1 28  ? 32.124  -34.921 39.857  0.41 38.35  ? 28  MET C SD  1 
ATOM   6879  C  CE  A MET C 1 28  ? 30.714  -32.514 36.581  0.59 40.97  ? 28  MET C CE  1 
ATOM   6880  C  CE  B MET C 1 28  ? 33.736  -34.782 40.617  0.41 39.60  ? 28  MET C CE  1 
ATOM   6881  N  N   . ASN C 1 29  ? 33.597  -37.373 35.647  1.00 28.86  ? 29  ASN C N   1 
ATOM   6882  C  CA  . ASN C 1 29  ? 35.016  -37.651 35.408  1.00 27.83  ? 29  ASN C CA  1 
ATOM   6883  C  C   . ASN C 1 29  ? 35.423  -37.293 33.969  1.00 27.49  ? 29  ASN C C   1 
ATOM   6884  O  O   . ASN C 1 29  ? 36.532  -36.793 33.725  1.00 28.27  ? 29  ASN C O   1 
ATOM   6885  C  CB  . ASN C 1 29  ? 35.292  -39.148 35.667  1.00 28.33  ? 29  ASN C CB  1 
ATOM   6886  C  CG  . ASN C 1 29  ? 35.303  -39.491 37.125  1.00 29.72  ? 29  ASN C CG  1 
ATOM   6887  O  OD1 . ASN C 1 29  ? 35.425  -38.619 37.999  1.00 36.26  ? 29  ASN C OD1 1 
ATOM   6888  N  ND2 . ASN C 1 29  ? 35.149  -40.782 37.412  1.00 36.47  ? 29  ASN C ND2 1 
ATOM   6889  N  N   . TYR C 1 30  ? 34.535  -37.515 33.015  1.00 25.54  ? 30  TYR C N   1 
ATOM   6890  C  CA  . TYR C 1 30  ? 34.871  -37.143 31.636  1.00 25.39  ? 30  TYR C CA  1 
ATOM   6891  C  C   . TYR C 1 30  ? 35.048  -35.635 31.530  1.00 27.30  ? 30  TYR C C   1 
ATOM   6892  O  O   . TYR C 1 30  ? 36.026  -35.151 30.945  1.00 28.24  ? 30  TYR C O   1 
ATOM   6893  C  CB  . TYR C 1 30  ? 33.798  -37.623 30.680  1.00 24.74  ? 30  TYR C CB  1 
ATOM   6894  C  CG  . TYR C 1 30  ? 34.100  -37.314 29.240  1.00 21.88  ? 30  TYR C CG  1 
ATOM   6895  C  CD1 . TYR C 1 30  ? 34.942  -38.154 28.511  1.00 23.91  ? 30  TYR C CD1 1 
ATOM   6896  C  CD2 . TYR C 1 30  ? 33.481  -36.241 28.572  1.00 23.67  ? 30  TYR C CD2 1 
ATOM   6897  C  CE1 . TYR C 1 30  ? 35.182  -37.926 27.159  1.00 25.94  ? 30  TYR C CE1 1 
ATOM   6898  C  CE2 . TYR C 1 30  ? 33.710  -36.033 27.191  1.00 26.66  ? 30  TYR C CE2 1 
ATOM   6899  C  CZ  . TYR C 1 30  ? 34.580  -36.886 26.519  1.00 27.12  ? 30  TYR C CZ  1 
ATOM   6900  O  OH  . TYR C 1 30  ? 34.862  -36.724 25.177  1.00 32.70  ? 30  TYR C OH  1 
ATOM   6901  N  N   . ALA C 1 31  ? 34.115  -34.883 32.112  1.00 26.41  ? 31  ALA C N   1 
ATOM   6902  C  CA  . ALA C 1 31  ? 34.200  -33.420 32.098  1.00 26.70  ? 31  ALA C CA  1 
ATOM   6903  C  C   . ALA C 1 31  ? 35.454  -32.903 32.809  1.00 27.90  ? 31  ALA C C   1 
ATOM   6904  O  O   . ALA C 1 31  ? 36.046  -31.908 32.366  1.00 28.94  ? 31  ALA C O   1 
ATOM   6905  C  CB  . ALA C 1 31  ? 32.943  -32.804 32.726  1.00 27.19  ? 31  ALA C CB  1 
ATOM   6906  N  N   . ARG C 1 32  ? 35.854  -33.539 33.916  1.00 24.83  ? 32  ARG C N   1 
ATOM   6907  C  CA  . ARG C 1 32  ? 36.971  -33.087 34.737  1.00 25.55  ? 32  ARG C CA  1 
ATOM   6908  C  C   . ARG C 1 32  ? 38.297  -33.759 34.410  1.00 28.25  ? 32  ARG C C   1 
ATOM   6909  O  O   . ARG C 1 32  ? 39.303  -33.457 35.083  1.00 29.93  ? 32  ARG C O   1 
ATOM   6910  C  CB  . ARG C 1 32  ? 36.649  -33.263 36.234  1.00 30.24  ? 32  ARG C CB  1 
ATOM   6911  C  CG  . ARG C 1 32  ? 35.295  -32.713 36.636  1.00 33.51  ? 32  ARG C CG  1 
ATOM   6912  C  CD  . ARG C 1 32  ? 35.150  -32.642 38.144  1.00 36.96  ? 32  ARG C CD  1 
ATOM   6913  N  NE  . ARG C 1 32  ? 35.918  -31.563 38.751  1.00 45.83  ? 32  ARG C NE  1 
ATOM   6914  C  CZ  . ARG C 1 32  ? 36.275  -31.520 40.029  1.00 48.89  ? 32  ARG C CZ  1 
ATOM   6915  N  NH1 . ARG C 1 32  ? 35.986  -32.507 40.861  1.00 51.28  ? 32  ARG C NH1 1 
ATOM   6916  N  NH2 . ARG C 1 32  ? 36.919  -30.449 40.489  1.00 50.14  ? 32  ARG C NH2 1 
ATOM   6917  N  N   . ALA C 1 33  ? 38.340  -34.584 33.336  1.00 27.71  ? 33  ALA C N   1 
ATOM   6918  C  CA  . ALA C 1 33  ? 39.516  -35.384 33.003  1.00 28.31  ? 33  ALA C CA  1 
ATOM   6919  C  C   . ALA C 1 33  ? 40.811  -34.595 32.922  1.00 28.51  ? 33  ALA C C   1 
ATOM   6920  O  O   . ALA C 1 33  ? 41.874  -35.110 33.281  1.00 30.21  ? 33  ALA C O   1 
ATOM   6921  C  CB  . ALA C 1 33  ? 39.276  -36.124 31.675  1.00 31.19  ? 33  ALA C CB  1 
ATOM   6922  N  N   . LYS C 1 34  ? 40.759  -33.347 32.475  1.00 28.73  ? 34  LYS C N   1 
ATOM   6923  C  CA  . LYS C 1 34  ? 41.985  -32.602 32.240  1.00 32.76  ? 34  LYS C CA  1 
ATOM   6924  C  C   . LYS C 1 34  ? 42.535  -31.886 33.466  1.00 33.81  ? 34  LYS C C   1 
ATOM   6925  O  O   . LYS C 1 34  ? 43.703  -31.453 33.440  1.00 36.54  ? 34  LYS C O   1 
ATOM   6926  C  CB  . LYS C 1 34  ? 41.740  -31.581 31.119  1.00 31.96  ? 34  LYS C CB  1 
ATOM   6927  C  CG  . LYS C 1 34  ? 41.559  -32.200 29.791  1.00 30.49  ? 34  LYS C CG  1 
ATOM   6928  C  CD  . LYS C 1 34  ? 42.776  -33.037 29.417  1.00 34.39  ? 34  LYS C CD  1 
ATOM   6929  C  CE  . LYS C 1 34  ? 42.540  -33.744 28.133  1.00 30.24  ? 34  LYS C CE  1 
ATOM   6930  N  NZ  . LYS C 1 34  ? 43.734  -34.593 27.754  1.00 26.94  ? 34  LYS C NZ  1 
ATOM   6931  N  N   . GLU C 1 35  ? 41.756  -31.765 34.549  1.00 31.95  ? 35  GLU C N   1 
ATOM   6932  C  CA  . GLU C 1 35  ? 42.248  -31.101 35.760  1.00 33.92  ? 35  GLU C CA  1 
ATOM   6933  C  C   . GLU C 1 35  ? 43.575  -31.673 36.251  1.00 35.19  ? 35  GLU C C   1 
ATOM   6934  O  O   . GLU C 1 35  ? 44.443  -30.930 36.717  1.00 35.32  ? 35  GLU C O   1 
ATOM   6935  C  CB  . GLU C 1 35  ? 41.196  -31.183 36.865  1.00 34.82  ? 35  GLU C CB  1 
ATOM   6936  C  CG  . GLU C 1 35  ? 39.926  -30.447 36.451  1.00 40.03  ? 35  GLU C CG  1 
ATOM   6937  C  CD  . GLU C 1 35  ? 38.846  -30.448 37.519  1.00 41.60  ? 35  GLU C CD  1 
ATOM   6938  O  OE1 . GLU C 1 35  ? 39.092  -30.986 38.625  1.00 46.64  ? 35  GLU C OE1 1 
ATOM   6939  O  OE2 . GLU C 1 35  ? 37.754  -29.897 37.239  1.00 41.93  ? 35  GLU C OE2 1 
ATOM   6940  N  N   . LYS C 1 36  ? 43.744  -33.003 36.179  1.00 33.34  ? 36  LYS C N   1 
ATOM   6941  C  CA  . LYS C 1 36  ? 44.976  -33.644 36.617  1.00 32.40  ? 36  LYS C CA  1 
ATOM   6942  C  C   . LYS C 1 36  ? 45.661  -34.345 35.452  1.00 34.05  ? 36  LYS C C   1 
ATOM   6943  O  O   . LYS C 1 36  ? 46.403  -35.306 35.646  1.00 33.83  ? 36  LYS C O   1 
ATOM   6944  C  CB  . LYS C 1 36  ? 44.716  -34.634 37.755  1.00 35.59  ? 36  LYS C CB  1 
ATOM   6945  C  CG  . LYS C 1 36  ? 44.212  -33.979 39.046  1.00 41.31  ? 36  LYS C CG  1 
ATOM   6946  C  CD  . LYS C 1 36  ? 45.057  -32.771 39.516  1.00 49.86  ? 36  LYS C CD  1 
ATOM   6947  C  CE  . LYS C 1 36  ? 46.599  -33.046 39.662  1.00 47.57  ? 36  LYS C CE  1 
ATOM   6948  N  NZ  . LYS C 1 36  ? 47.239  -32.066 40.612  1.00 45.70  ? 36  LYS C NZ  1 
ATOM   6949  N  N   . GLY C 1 37  ? 45.407  -33.878 34.238  1.00 31.36  ? 37  GLY C N   1 
ATOM   6950  C  CA  . GLY C 1 37  ? 46.158  -34.356 33.100  1.00 31.92  ? 37  GLY C CA  1 
ATOM   6951  C  C   . GLY C 1 37  ? 45.712  -35.718 32.615  1.00 29.26  ? 37  GLY C C   1 
ATOM   6952  O  O   . GLY C 1 37  ? 46.481  -36.422 31.956  1.00 29.23  ? 37  GLY C O   1 
ATOM   6953  N  N   . GLY C 1 38  ? 44.448  -36.070 32.833  1.00 27.50  ? 38  GLY C N   1 
ATOM   6954  C  CA  . GLY C 1 38  ? 43.922  -37.304 32.306  1.00 25.69  ? 38  GLY C CA  1 
ATOM   6955  C  C   . GLY C 1 38  ? 43.658  -37.280 30.796  1.00 29.05  ? 38  GLY C C   1 
ATOM   6956  O  O   . GLY C 1 38  ? 43.814  -36.264 30.112  1.00 27.72  ? 38  GLY C O   1 
ATOM   6957  N  N   . ILE C 1 39  ? 43.216  -38.426 30.294  1.00 28.51  ? 39  ILE C N   1 
ATOM   6958  C  CA  . ILE C 1 39  ? 42.871  -38.624 28.884  1.00 26.36  ? 39  ILE C CA  1 
ATOM   6959  C  C   . ILE C 1 39  ? 41.354  -38.738 28.748  1.00 26.65  ? 39  ILE C C   1 
ATOM   6960  O  O   . ILE C 1 39  ? 40.694  -39.368 29.579  1.00 29.57  ? 39  ILE C O   1 
ATOM   6961  C  CB  . ILE C 1 39  ? 43.573  -39.874 28.345  1.00 29.07  ? 39  ILE C CB  1 
ATOM   6962  C  CG1 . ILE C 1 39  ? 45.071  -39.607 28.263  1.00 29.60  ? 39  ILE C CG1 1 
ATOM   6963  C  CG2 . ILE C 1 39  ? 43.019  -40.319 27.001  1.00 29.35  ? 39  ILE C CG2 1 
ATOM   6964  C  CD1 . ILE C 1 39  ? 45.847  -40.845 27.986  1.00 31.36  ? 39  ILE C CD1 1 
ATOM   6965  N  N   . ARG C 1 40  ? 40.804  -38.086 27.727  1.00 23.09  ? 40  ARG C N   1 
ATOM   6966  C  CA  . ARG C 1 40  ? 39.414  -38.219 27.272  1.00 24.62  ? 40  ARG C CA  1 
ATOM   6967  C  C   . ARG C 1 40  ? 39.380  -38.893 25.904  1.00 25.89  ? 40  ARG C C   1 
ATOM   6968  O  O   . ARG C 1 40  ? 40.118  -38.481 24.999  1.00 24.39  ? 40  ARG C O   1 
ATOM   6969  C  CB  . ARG C 1 40  ? 38.757  -36.843 27.075  1.00 27.18  ? 40  ARG C CB  1 
ATOM   6970  C  CG  . ARG C 1 40  ? 38.376  -36.154 28.318  1.00 32.33  ? 40  ARG C CG  1 
ATOM   6971  C  CD  . ARG C 1 40  ? 37.272  -35.153 28.076  1.00 33.14  ? 40  ARG C CD  1 
ATOM   6972  N  NE  . ARG C 1 40  ? 37.804  -33.902 27.596  1.00 35.00  ? 40  ARG C NE  1 
ATOM   6973  C  CZ  . ARG C 1 40  ? 38.002  -32.817 28.337  1.00 32.10  ? 40  ARG C CZ  1 
ATOM   6974  N  NH1 . ARG C 1 40  ? 37.747  -32.794 29.634  1.00 37.14  ? 40  ARG C NH1 1 
ATOM   6975  N  NH2 . ARG C 1 40  ? 38.479  -31.726 27.764  1.00 32.93  ? 40  ARG C NH2 1 
ATOM   6976  N  N   . TRP C 1 41  ? 38.450  -39.828 25.689  1.00 23.43  ? 41  TRP C N   1 
ATOM   6977  C  CA  . TRP C 1 41  ? 38.204  -40.318 24.312  1.00 21.59  ? 41  TRP C CA  1 
ATOM   6978  C  C   . TRP C 1 41  ? 36.719  -40.581 24.119  1.00 21.47  ? 41  TRP C C   1 
ATOM   6979  O  O   . TRP C 1 41  ? 35.952  -40.714 25.093  1.00 21.31  ? 41  TRP C O   1 
ATOM   6980  C  CB  . TRP C 1 41  ? 39.041  -41.544 23.986  1.00 22.68  ? 41  TRP C CB  1 
ATOM   6981  C  CG  . TRP C 1 41  ? 38.738  -42.711 24.825  1.00 22.43  ? 41  TRP C CG  1 
ATOM   6982  C  CD1 . TRP C 1 41  ? 39.288  -42.999 26.075  1.00 23.21  ? 41  TRP C CD1 1 
ATOM   6983  C  CD2 . TRP C 1 41  ? 37.855  -43.794 24.517  1.00 23.23  ? 41  TRP C CD2 1 
ATOM   6984  N  NE1 . TRP C 1 41  ? 38.782  -44.207 26.542  1.00 22.24  ? 41  TRP C NE1 1 
ATOM   6985  C  CE2 . TRP C 1 41  ? 37.884  -44.687 25.618  1.00 24.39  ? 41  TRP C CE2 1 
ATOM   6986  C  CE3 . TRP C 1 41  ? 36.984  -44.061 23.446  1.00 24.87  ? 41  TRP C CE3 1 
ATOM   6987  C  CZ2 . TRP C 1 41  ? 37.109  -45.877 25.644  1.00 23.46  ? 41  TRP C CZ2 1 
ATOM   6988  C  CZ3 . TRP C 1 41  ? 36.197  -45.261 23.479  1.00 23.94  ? 41  TRP C CZ3 1 
ATOM   6989  C  CH2 . TRP C 1 41  ? 36.231  -46.106 24.599  1.00 23.24  ? 41  TRP C CH2 1 
ATOM   6990  N  N   . SER C 1 42  ? 36.301  -40.635 22.856  1.00 19.05  ? 42  SER C N   1 
ATOM   6991  C  CA  . SER C 1 42  ? 34.886  -40.866 22.608  1.00 21.59  ? 42  SER C CA  1 
ATOM   6992  C  C   . SER C 1 42  ? 34.737  -41.992 21.591  1.00 24.08  ? 42  SER C C   1 
ATOM   6993  O  O   . SER C 1 42  ? 35.565  -42.167 20.686  1.00 23.77  ? 42  SER C O   1 
ATOM   6994  C  CB  . SER C 1 42  ? 34.131  -39.661 22.087  1.00 31.63  ? 42  SER C CB  1 
ATOM   6995  O  OG  . SER C 1 42  ? 34.929  -38.969 21.143  1.00 37.26  ? 42  SER C OG  1 
ATOM   6996  N  N   . GLY C 1 43  ? 33.604  -42.653 21.680  1.00 23.80  ? 43  GLY C N   1 
ATOM   6997  C  CA  . GLY C 1 43  ? 33.319  -43.789 20.809  1.00 21.51  ? 43  GLY C CA  1 
ATOM   6998  C  C   . GLY C 1 43  ? 32.024  -44.412 21.278  1.00 22.63  ? 43  GLY C C   1 
ATOM   6999  O  O   . GLY C 1 43  ? 31.435  -44.005 22.285  1.00 21.21  ? 43  GLY C O   1 
ATOM   7000  N  N   . SER C 1 44  ? 31.622  -45.456 20.571  1.00 21.26  ? 44  SER C N   1 
ATOM   7001  C  CA  . SER C 1 44  ? 30.416  -46.173 20.920  1.00 18.20  ? 44  SER C CA  1 
ATOM   7002  C  C   . SER C 1 44  ? 30.547  -46.902 22.261  1.00 20.92  ? 44  SER C C   1 
ATOM   7003  O  O   . SER C 1 44  ? 31.658  -47.282 22.720  1.00 20.14  ? 44  SER C O   1 
ATOM   7004  C  CB  . SER C 1 44  ? 30.157  -47.248 19.841  1.00 20.37  ? 44  SER C CB  1 
ATOM   7005  O  OG  . SER C 1 44  ? 29.047  -48.088 20.133  1.00 22.36  ? 44  SER C OG  1 
ATOM   7006  N  N   . ALA C 1 45  ? 29.379  -47.211 22.821  1.00 20.84  ? 45  ALA C N   1 
ATOM   7007  C  CA  . ALA C 1 45  ? 29.304  -48.190 23.909  1.00 20.61  ? 45  ALA C CA  1 
ATOM   7008  C  C   . ALA C 1 45  ? 29.899  -49.526 23.496  1.00 22.47  ? 45  ALA C C   1 
ATOM   7009  O  O   . ALA C 1 45  ? 30.288  -50.320 24.366  1.00 21.79  ? 45  ALA C O   1 
ATOM   7010  C  CB  . ALA C 1 45  ? 27.849  -48.395 24.373  1.00 22.42  ? 45  ALA C CB  1 
ATOM   7011  N  N   . TRP C 1 46  ? 29.980  -49.788 22.197  1.00 19.72  ? 46  TRP C N   1 
ATOM   7012  C  CA  . TRP C 1 46  ? 30.541  -51.022 21.677  1.00 21.53  ? 46  TRP C CA  1 
ATOM   7013  C  C   . TRP C 1 46  ? 32.025  -50.898 21.337  1.00 23.45  ? 46  TRP C C   1 
ATOM   7014  O  O   . TRP C 1 46  ? 32.623  -51.865 20.874  1.00 21.03  ? 46  TRP C O   1 
ATOM   7015  C  CB  . TRP C 1 46  ? 29.746  -51.434 20.456  1.00 19.16  ? 46  TRP C CB  1 
ATOM   7016  C  CG  . TRP C 1 46  ? 28.457  -52.063 20.735  1.00 22.49  ? 46  TRP C CG  1 
ATOM   7017  C  CD1 . TRP C 1 46  ? 28.039  -52.607 21.925  1.00 22.45  ? 46  TRP C CD1 1 
ATOM   7018  C  CD2 . TRP C 1 46  ? 27.373  -52.241 19.803  1.00 22.54  ? 46  TRP C CD2 1 
ATOM   7019  N  NE1 . TRP C 1 46  ? 26.764  -53.135 21.776  1.00 22.73  ? 46  TRP C NE1 1 
ATOM   7020  C  CE2 . TRP C 1 46  ? 26.351  -52.935 20.478  1.00 23.59  ? 46  TRP C CE2 1 
ATOM   7021  C  CE3 . TRP C 1 46  ? 27.215  -51.947 18.437  1.00 22.40  ? 46  TRP C CE3 1 
ATOM   7022  C  CZ2 . TRP C 1 46  ? 25.168  -53.320 19.848  1.00 23.23  ? 46  TRP C CZ2 1 
ATOM   7023  C  CZ3 . TRP C 1 46  ? 26.036  -52.297 17.815  1.00 24.92  ? 46  TRP C CZ3 1 
ATOM   7024  C  CH2 . TRP C 1 46  ? 25.023  -52.991 18.516  1.00 24.88  ? 46  TRP C CH2 1 
ATOM   7025  N  N   . ALA C 1 47  ? 32.641  -49.736 21.558  1.00 20.00  ? 47  ALA C N   1 
ATOM   7026  C  CA  . ALA C 1 47  ? 34.091  -49.630 21.480  1.00 18.90  ? 47  ALA C CA  1 
ATOM   7027  C  C   . ALA C 1 47  ? 34.754  -50.606 22.437  1.00 20.44  ? 47  ALA C C   1 
ATOM   7028  O  O   . ALA C 1 47  ? 34.228  -50.917 23.539  1.00 24.29  ? 47  ALA C O   1 
ATOM   7029  C  CB  . ALA C 1 47  ? 34.546  -48.199 21.831  1.00 20.56  ? 47  ALA C CB  1 
ATOM   7030  N  N   . LEU C 1 48  ? 35.934  -51.081 22.012  1.00 22.58  ? 48  LEU C N   1 
ATOM   7031  C  CA  . LEU C 1 48  ? 36.718  -52.037 22.802  1.00 22.20  ? 48  LEU C CA  1 
ATOM   7032  C  C   . LEU C 1 48  ? 37.549  -51.230 23.785  1.00 22.00  ? 48  LEU C C   1 
ATOM   7033  O  O   . LEU C 1 48  ? 38.756  -51.016 23.649  1.00 21.59  ? 48  LEU C O   1 
ATOM   7034  C  CB  . LEU C 1 48  ? 37.524  -52.997 21.898  1.00 19.93  ? 48  LEU C CB  1 
ATOM   7035  C  CG  . LEU C 1 48  ? 36.762  -54.336 21.744  1.00 23.12  ? 48  LEU C CG  1 
ATOM   7036  C  CD1 . LEU C 1 48  ? 35.378  -54.073 20.993  1.00 25.04  ? 48  LEU C CD1 1 
ATOM   7037  C  CD2 . LEU C 1 48  ? 37.582  -55.320 20.940  1.00 23.25  ? 48  LEU C CD2 1 
ATOM   7038  N  N   . ASP C 1 49  ? 36.865  -50.781 24.854  1.00 21.36  ? 49  ASP C N   1 
ATOM   7039  C  CA  . ASP C 1 49  ? 37.450  -49.802 25.784  1.00 23.03  ? 49  ASP C CA  1 
ATOM   7040  C  C   . ASP C 1 49  ? 38.625  -50.272 26.615  1.00 21.60  ? 49  ASP C C   1 
ATOM   7041  O  O   . ASP C 1 49  ? 39.312  -49.428 27.211  1.00 22.01  ? 49  ASP C O   1 
ATOM   7042  C  CB  . ASP C 1 49  ? 36.405  -49.195 26.732  1.00 23.20  ? 49  ASP C CB  1 
ATOM   7043  C  CG  . ASP C 1 49  ? 35.486  -50.205 27.334  1.00 25.07  ? 49  ASP C CG  1 
ATOM   7044  O  OD1 . ASP C 1 49  ? 34.690  -50.771 26.559  1.00 25.90  ? 49  ASP C OD1 1 
ATOM   7045  O  OD2 . ASP C 1 49  ? 35.533  -50.402 28.571  1.00 25.17  ? 49  ASP C OD2 1 
ATOM   7046  N  N   . ALA C 1 50  ? 38.916  -51.575 26.675  1.00 18.69  ? 50  ALA C N   1 
ATOM   7047  C  CA  . ALA C 1 50  ? 40.118  -51.983 27.380  1.00 21.71  ? 50  ALA C CA  1 
ATOM   7048  C  C   . ALA C 1 50  ? 41.390  -51.542 26.669  1.00 21.63  ? 50  ALA C C   1 
ATOM   7049  O  O   . ALA C 1 50  ? 42.430  -51.462 27.328  1.00 24.06  ? 50  ALA C O   1 
ATOM   7050  C  CB  . ALA C 1 50  ? 40.152  -53.510 27.505  1.00 20.53  ? 50  ALA C CB  1 
ATOM   7051  N  N   . ILE C 1 51  ? 41.353  -51.279 25.349  1.00 21.21  ? 51  ILE C N   1 
ATOM   7052  C  CA  . ILE C 1 51  ? 42.547  -50.796 24.640  1.00 22.36  ? 51  ILE C CA  1 
ATOM   7053  C  C   . ILE C 1 51  ? 42.934  -49.412 25.181  1.00 20.04  ? 51  ILE C C   1 
ATOM   7054  O  O   . ILE C 1 51  ? 44.077  -49.278 25.634  1.00 22.85  ? 51  ILE C O   1 
ATOM   7055  C  CB  . ILE C 1 51  ? 42.346  -50.810 23.104  1.00 23.81  ? 51  ILE C CB  1 
ATOM   7056  C  CG1 . ILE C 1 51  ? 42.208  -52.255 22.555  1.00 25.20  ? 51  ILE C CG1 1 
ATOM   7057  C  CG2 . ILE C 1 51  ? 43.454  -50.054 22.428  1.00 23.24  ? 51  ILE C CG2 1 
ATOM   7058  C  CD1 . ILE C 1 51  ? 43.436  -53.026 22.544  1.00 25.58  ? 51  ILE C CD1 1 
ATOM   7059  N  N   . PRO C 1 52  ? 42.104  -48.363 25.119  1.00 23.17  ? 52  PRO C N   1 
ATOM   7060  C  CA  . PRO C 1 52  ? 42.518  -47.094 25.738  1.00 23.71  ? 52  PRO C CA  1 
ATOM   7061  C  C   . PRO C 1 52  ? 42.827  -47.237 27.229  1.00 23.49  ? 52  PRO C C   1 
ATOM   7062  O  O   . PRO C 1 52  ? 43.640  -46.477 27.746  1.00 23.24  ? 52  PRO C O   1 
ATOM   7063  C  CB  . PRO C 1 52  ? 41.304  -46.169 25.512  1.00 22.86  ? 52  PRO C CB  1 
ATOM   7064  C  CG  . PRO C 1 52  ? 40.545  -46.723 24.415  1.00 24.85  ? 52  PRO C CG  1 
ATOM   7065  C  CD  . PRO C 1 52  ? 40.811  -48.226 24.418  1.00 21.49  ? 52  PRO C CD  1 
ATOM   7066  N  N   . ALA C 1 53  ? 42.235  -48.229 27.930  1.00 22.07  ? 53  ALA C N   1 
ATOM   7067  C  CA  . ALA C 1 53  ? 42.558  -48.429 29.359  1.00 25.79  ? 53  ALA C CA  1 
ATOM   7068  C  C   . ALA C 1 53  ? 44.017  -48.810 29.591  1.00 23.79  ? 53  ALA C C   1 
ATOM   7069  O  O   . ALA C 1 53  ? 44.540  -48.625 30.708  1.00 23.72  ? 53  ALA C O   1 
ATOM   7070  C  CB  . ALA C 1 53  ? 41.675  -49.516 29.977  1.00 22.83  ? 53  ALA C CB  1 
ATOM   7071  N  N   . GLY C 1 54  ? 44.702  -49.339 28.577  1.00 22.98  ? 54  GLY C N   1 
ATOM   7072  C  CA  . GLY C 1 54  ? 46.119  -49.633 28.764  1.00 21.08  ? 54  GLY C CA  1 
ATOM   7073  C  C   . GLY C 1 54  ? 46.992  -48.397 28.910  1.00 21.66  ? 54  GLY C C   1 
ATOM   7074  O  O   . GLY C 1 54  ? 48.186  -48.522 29.208  1.00 24.16  ? 54  GLY C O   1 
ATOM   7075  N  N   . LEU C 1 55  ? 46.420  -47.214 28.719  1.00 22.69  ? 55  LEU C N   1 
ATOM   7076  C  CA  . LEU C 1 55  ? 47.170  -45.983 28.817  1.00 22.43  ? 55  LEU C CA  1 
ATOM   7077  C  C   . LEU C 1 55  ? 47.111  -45.367 30.217  1.00 28.70  ? 55  LEU C C   1 
ATOM   7078  O  O   . LEU C 1 55  ? 47.658  -44.290 30.421  1.00 24.98  ? 55  LEU C O   1 
ATOM   7079  C  CB  . LEU C 1 55  ? 46.630  -44.998 27.789  1.00 22.52  ? 55  LEU C CB  1 
ATOM   7080  C  CG  . LEU C 1 55  ? 46.612  -45.328 26.280  1.00 24.95  ? 55  LEU C CG  1 
ATOM   7081  C  CD1 . LEU C 1 55  ? 46.009  -44.126 25.498  1.00 25.34  ? 55  LEU C CD1 1 
ATOM   7082  C  CD2 . LEU C 1 55  ? 47.996  -45.581 25.882  1.00 26.30  ? 55  LEU C CD2 1 
ATOM   7083  N  N   . GLY C 1 56  ? 46.474  -46.013 31.188  1.00 24.98  ? 56  GLY C N   1 
ATOM   7084  C  CA  . GLY C 1 56  ? 46.423  -45.516 32.549  1.00 25.84  ? 56  GLY C CA  1 
ATOM   7085  C  C   . GLY C 1 56  ? 45.026  -45.634 33.133  1.00 28.73  ? 56  GLY C C   1 
ATOM   7086  O  O   . GLY C 1 56  ? 44.045  -45.921 32.442  1.00 25.47  ? 56  GLY C O   1 
ATOM   7087  N  N   . GLU C 1 57  ? 44.963  -45.400 34.448  1.00 26.96  ? 57  GLU C N   1 
ATOM   7088  C  CA  . GLU C 1 57  ? 43.725  -45.434 35.195  1.00 28.12  ? 57  GLU C CA  1 
ATOM   7089  C  C   . GLU C 1 57  ? 42.993  -44.101 35.176  1.00 31.11  ? 57  GLU C C   1 
ATOM   7090  O  O   . GLU C 1 57  ? 41.910  -44.015 35.749  1.00 34.27  ? 57  GLU C O   1 
ATOM   7091  C  CB  . GLU C 1 57  ? 44.002  -45.848 36.634  1.00 29.50  ? 57  GLU C CB  1 
ATOM   7092  C  CG  . GLU C 1 57  ? 44.725  -47.179 36.660  1.00 36.82  ? 57  GLU C CG  1 
ATOM   7093  C  CD  . GLU C 1 57  ? 44.680  -47.847 38.011  1.00 47.45  ? 57  GLU C CD  1 
ATOM   7094  O  OE1 . GLU C 1 57  ? 43.977  -48.878 38.128  1.00 56.10  ? 57  GLU C OE1 1 
ATOM   7095  O  OE2 . GLU C 1 57  ? 45.358  -47.357 38.937  1.00 54.35  ? 57  GLU C OE2 1 
ATOM   7096  N  N   . ASP C 1 58  ? 43.563  -43.092 34.534  1.00 27.22  ? 58  ASP C N   1 
ATOM   7097  C  CA  . ASP C 1 58  ? 42.989  -41.752 34.390  1.00 28.88  ? 58  ASP C CA  1 
ATOM   7098  C  C   . ASP C 1 58  ? 42.636  -41.519 32.926  1.00 28.75  ? 58  ASP C C   1 
ATOM   7099  O  O   . ASP C 1 58  ? 42.902  -40.467 32.360  1.00 27.24  ? 58  ASP C O   1 
ATOM   7100  C  CB  . ASP C 1 58  ? 43.959  -40.686 34.892  1.00 28.99  ? 58  ASP C CB  1 
ATOM   7101  C  CG  . ASP C 1 58  ? 45.258  -40.672 34.092  1.00 32.19  ? 58  ASP C CG  1 
ATOM   7102  O  OD1 . ASP C 1 58  ? 45.616  -41.703 33.502  1.00 27.98  ? 58  ASP C OD1 1 
ATOM   7103  O  OD2 . ASP C 1 58  ? 45.930  -39.651 34.014  1.00 28.26  ? 58  ASP C OD2 1 
ATOM   7104  N  N   . VAL C 1 59  ? 42.054  -42.532 32.305  1.00 24.06  ? 59  VAL C N   1 
ATOM   7105  C  CA  . VAL C 1 59  ? 41.609  -42.491 30.913  1.00 26.28  ? 59  VAL C CA  1 
ATOM   7106  C  C   . VAL C 1 59  ? 40.084  -42.613 30.936  1.00 27.67  ? 59  VAL C C   1 
ATOM   7107  O  O   . VAL C 1 59  ? 39.531  -43.634 31.373  1.00 25.93  ? 59  VAL C O   1 
ATOM   7108  C  CB  . VAL C 1 59  ? 42.281  -43.601 30.088  1.00 29.38  ? 59  VAL C CB  1 
ATOM   7109  C  CG1 . VAL C 1 59  ? 41.843  -43.539 28.613  1.00 31.35  ? 59  VAL C CG1 1 
ATOM   7110  C  CG2 . VAL C 1 59  ? 43.817  -43.494 30.177  1.00 26.47  ? 59  VAL C CG2 1 
ATOM   7111  N  N   . TYR C 1 60  ? 39.404  -41.571 30.479  1.00 24.65  ? 60  TYR C N   1 
ATOM   7112  C  CA  . TYR C 1 60  ? 37.965  -41.447 30.647  1.00 25.38  ? 60  TYR C CA  1 
ATOM   7113  C  C   . TYR C 1 60  ? 37.284  -41.414 29.305  1.00 26.87  ? 60  TYR C C   1 
ATOM   7114  O  O   . TYR C 1 60  ? 37.592  -40.535 28.465  1.00 25.37  ? 60  TYR C O   1 
ATOM   7115  C  CB  . TYR C 1 60  ? 37.627  -40.167 31.425  1.00 24.61  ? 60  TYR C CB  1 
ATOM   7116  C  CG  . TYR C 1 60  ? 38.328  -40.145 32.767  1.00 28.34  ? 60  TYR C CG  1 
ATOM   7117  C  CD1 . TYR C 1 60  ? 37.839  -40.883 33.845  1.00 30.42  ? 60  TYR C CD1 1 
ATOM   7118  C  CD2 . TYR C 1 60  ? 39.520  -39.483 32.919  1.00 30.25  ? 60  TYR C CD2 1 
ATOM   7119  C  CE1 . TYR C 1 60  ? 38.496  -40.874 35.067  1.00 34.00  ? 60  TYR C CE1 1 
ATOM   7120  C  CE2 . TYR C 1 60  ? 40.170  -39.457 34.122  1.00 32.28  ? 60  TYR C CE2 1 
ATOM   7121  C  CZ  . TYR C 1 60  ? 39.676  -40.157 35.179  1.00 33.34  ? 60  TYR C CZ  1 
ATOM   7122  O  OH  . TYR C 1 60  ? 40.381  -40.113 36.347  1.00 39.38  ? 60  TYR C OH  1 
ATOM   7123  N  N   . SER C 1 61  ? 36.318  -42.322 29.123  1.00 23.08  ? 61  SER C N   1 
ATOM   7124  C  CA  . SER C 1 61  ? 35.529  -42.285 27.910  1.00 22.65  ? 61  SER C CA  1 
ATOM   7125  C  C   . SER C 1 61  ? 34.255  -41.491 28.073  1.00 21.14  ? 61  SER C C   1 
ATOM   7126  O  O   . SER C 1 61  ? 33.788  -41.180 29.191  1.00 21.63  ? 61  SER C O   1 
ATOM   7127  C  CB  . SER C 1 61  ? 35.169  -43.708 27.451  1.00 21.62  ? 61  SER C CB  1 
ATOM   7128  O  OG  . SER C 1 61  ? 34.196  -44.295 28.348  1.00 23.94  ? 61  SER C OG  1 
ATOM   7129  N  N   . LEU C 1 62  ? 33.714  -41.108 26.934  1.00 20.27  ? 62  LEU C N   1 
ATOM   7130  C  CA  . LEU C 1 62  ? 32.295  -40.746 26.802  1.00 20.81  ? 62  LEU C CA  1 
ATOM   7131  C  C   . LEU C 1 62  ? 31.688  -41.616 25.696  1.00 22.60  ? 62  LEU C C   1 
ATOM   7132  O  O   . LEU C 1 62  ? 31.982  -41.420 24.504  1.00 22.85  ? 62  LEU C O   1 
ATOM   7133  C  CB  . LEU C 1 62  ? 32.120  -39.248 26.452  1.00 21.62  ? 62  LEU C CB  1 
ATOM   7134  C  CG  . LEU C 1 62  ? 30.654  -38.762 26.409  1.00 23.02  ? 62  LEU C CG  1 
ATOM   7135  C  CD1 . LEU C 1 62  ? 30.013  -38.668 27.777  1.00 22.63  ? 62  LEU C CD1 1 
ATOM   7136  C  CD2 . LEU C 1 62  ? 30.600  -37.367 25.726  1.00 22.76  ? 62  LEU C CD2 1 
ATOM   7137  N  N   . THR C 1 63  ? 30.793  -42.548 26.055  1.00 21.97  ? 63  THR C N   1 
ATOM   7138  C  CA  . THR C 1 63  ? 30.218  -43.421 25.036  1.00 22.24  ? 63  THR C CA  1 
ATOM   7139  C  C   . THR C 1 63  ? 29.000  -42.736 24.413  1.00 22.13  ? 63  THR C C   1 
ATOM   7140  O  O   . THR C 1 63  ? 28.193  -42.112 25.128  1.00 21.53  ? 63  THR C O   1 
ATOM   7141  C  CB  . THR C 1 63  ? 29.846  -44.792 25.625  1.00 22.76  ? 63  THR C CB  1 
ATOM   7142  O  OG1 . THR C 1 63  ? 29.073  -44.593 26.813  1.00 22.30  ? 63  THR C OG1 1 
ATOM   7143  C  CG2 . THR C 1 63  ? 31.145  -45.582 25.979  1.00 25.63  ? 63  THR C CG2 1 
ATOM   7144  N  N   . GLY C 1 64  ? 28.957  -42.749 23.070  1.00 20.65  ? 64  GLY C N   1 
ATOM   7145  C  CA  . GLY C 1 64  ? 28.056  -41.870 22.326  1.00 22.20  ? 64  GLY C CA  1 
ATOM   7146  C  C   . GLY C 1 64  ? 26.578  -42.184 22.491  1.00 21.97  ? 64  GLY C C   1 
ATOM   7147  O  O   . GLY C 1 64  ? 25.773  -41.275 22.708  1.00 23.43  ? 64  GLY C O   1 
ATOM   7148  N  N   . GLU C 1 65  ? 26.200  -43.486 22.474  1.00 20.92  ? 65  GLU C N   1 
ATOM   7149  C  CA  . GLU C 1 65  ? 24.766  -43.792 22.507  1.00 19.82  ? 65  GLU C CA  1 
ATOM   7150  C  C   . GLU C 1 65  ? 24.185  -43.552 23.910  1.00 20.91  ? 65  GLU C C   1 
ATOM   7151  O  O   . GLU C 1 65  ? 23.058  -43.040 24.019  1.00 21.68  ? 65  GLU C O   1 
ATOM   7152  C  CB  . GLU C 1 65  ? 24.487  -45.256 22.076  1.00 22.74  ? 65  GLU C CB  1 
ATOM   7153  C  CG  . GLU C 1 65  ? 25.044  -45.609 20.671  1.00 22.50  ? 65  GLU C CG  1 
ATOM   7154  C  CD  . GLU C 1 65  ? 26.489  -46.063 20.721  1.00 20.49  ? 65  GLU C CD  1 
ATOM   7155  O  OE1 . GLU C 1 65  ? 27.045  -46.049 21.842  1.00 22.66  ? 65  GLU C OE1 1 
ATOM   7156  O  OE2 . GLU C 1 65  ? 27.062  -46.426 19.672  1.00 23.32  ? 65  GLU C OE2 1 
ATOM   7157  N  N   . PRO C 1 66  ? 24.855  -43.993 24.995  1.00 21.00  ? 66  PRO C N   1 
ATOM   7158  C  CA  . PRO C 1 66  ? 24.304  -43.726 26.335  1.00 20.10  ? 66  PRO C CA  1 
ATOM   7159  C  C   . PRO C 1 66  ? 24.237  -42.261 26.657  1.00 20.52  ? 66  PRO C C   1 
ATOM   7160  O  O   . PRO C 1 66  ? 23.255  -41.813 27.272  1.00 22.99  ? 66  PRO C O   1 
ATOM   7161  C  CB  . PRO C 1 66  ? 25.266  -44.478 27.286  1.00 26.40  ? 66  PRO C CB  1 
ATOM   7162  C  CG  . PRO C 1 66  ? 25.861  -45.646 26.383  1.00 20.71  ? 66  PRO C CG  1 
ATOM   7163  C  CD  . PRO C 1 66  ? 26.031  -44.896 25.033  1.00 20.56  ? 66  PRO C CD  1 
ATOM   7164  N  N   . TYR C 1 67  ? 25.243  -41.508 26.217  1.00 20.92  ? 67  TYR C N   1 
ATOM   7165  C  CA  . TYR C 1 67  ? 25.182  -40.047 26.389  1.00 20.99  ? 67  TYR C CA  1 
ATOM   7166  C  C   . TYR C 1 67  ? 23.988  -39.473 25.628  1.00 22.59  ? 67  TYR C C   1 
ATOM   7167  O  O   . TYR C 1 67  ? 23.213  -38.692 26.195  1.00 22.24  ? 67  TYR C O   1 
ATOM   7168  C  CB  . TYR C 1 67  ? 26.475  -39.389 25.938  1.00 19.81  ? 67  TYR C CB  1 
ATOM   7169  C  CG  . TYR C 1 67  ? 26.382  -37.869 26.047  1.00 20.83  ? 67  TYR C CG  1 
ATOM   7170  C  CD1 . TYR C 1 67  ? 26.428  -37.249 27.284  1.00 24.55  ? 67  TYR C CD1 1 
ATOM   7171  C  CD2 . TYR C 1 67  ? 26.198  -37.088 24.913  1.00 22.70  ? 67  TYR C CD2 1 
ATOM   7172  C  CE1 . TYR C 1 67  ? 26.302  -35.863 27.417  1.00 21.23  ? 67  TYR C CE1 1 
ATOM   7173  C  CE2 . TYR C 1 67  ? 26.101  -35.685 25.022  1.00 20.94  ? 67  TYR C CE2 1 
ATOM   7174  C  CZ  . TYR C 1 67  ? 26.150  -35.104 26.300  1.00 23.45  ? 67  TYR C CZ  1 
ATOM   7175  O  OH  . TYR C 1 67  ? 26.011  -33.757 26.393  1.00 24.74  ? 67  TYR C OH  1 
ATOM   7176  N  N   . ALA C 1 68  ? 23.810  -39.843 24.336  1.00 21.12  ? 68  ALA C N   1 
ATOM   7177  C  CA  . ALA C 1 68  ? 22.657  -39.332 23.592  1.00 24.56  ? 68  ALA C CA  1 
ATOM   7178  C  C   . ALA C 1 68  ? 21.334  -39.719 24.232  1.00 22.64  ? 68  ALA C C   1 
ATOM   7179  O  O   . ALA C 1 68  ? 20.359  -38.984 24.101  1.00 23.96  ? 68  ALA C O   1 
ATOM   7180  C  CB  . ALA C 1 68  ? 22.669  -39.754 22.092  1.00 22.74  ? 68  ALA C CB  1 
ATOM   7181  N  N   . ALA C 1 69  ? 21.227  -40.920 24.803  1.00 20.84  ? 69  ALA C N   1 
ATOM   7182  C  CA  . ALA C 1 69  ? 19.987  -41.301 25.487  1.00 19.68  ? 69  ALA C CA  1 
ATOM   7183  C  C   . ALA C 1 69  ? 19.761  -40.491 26.755  1.00 22.30  ? 69  ALA C C   1 
ATOM   7184  O  O   . ALA C 1 69  ? 18.631  -40.134 27.061  1.00 26.05  ? 69  ALA C O   1 
ATOM   7185  C  CB  . ALA C 1 69  ? 20.026  -42.807 25.846  1.00 22.64  ? 69  ALA C CB  1 
ATOM   7186  N  N   . ALA C 1 70  ? 20.827  -40.117 27.446  1.00 22.00  ? 70  ALA C N   1 
ATOM   7187  C  CA  . ALA C 1 70  ? 20.700  -39.179 28.561  1.00 23.22  ? 70  ALA C CA  1 
ATOM   7188  C  C   . ALA C 1 70  ? 20.168  -37.827 28.096  1.00 24.88  ? 70  ALA C C   1 
ATOM   7189  O  O   . ALA C 1 70  ? 19.322  -37.229 28.769  1.00 28.07  ? 70  ALA C O   1 
ATOM   7190  C  CB  . ALA C 1 70  ? 22.065  -39.017 29.245  1.00 22.91  ? 70  ALA C CB  1 
ATOM   7191  N  N   . VAL C 1 71  ? 20.625  -37.342 26.933  1.00 25.02  ? 71  VAL C N   1 
ATOM   7192  C  CA  . VAL C 1 71  ? 20.088  -36.094 26.388  1.00 22.62  ? 71  VAL C CA  1 
ATOM   7193  C  C   . VAL C 1 71  ? 18.620  -36.289 26.001  1.00 26.73  ? 71  VAL C C   1 
ATOM   7194  O  O   . VAL C 1 71  ? 17.777  -35.450 26.292  1.00 26.71  ? 71  VAL C O   1 
ATOM   7195  C  CB  . VAL C 1 71  ? 20.934  -35.645 25.183  1.00 21.37  ? 71  VAL C CB  1 
ATOM   7196  C  CG1 . VAL C 1 71  ? 20.191  -34.518 24.449  1.00 22.83  ? 71  VAL C CG1 1 
ATOM   7197  C  CG2 . VAL C 1 71  ? 22.351  -35.205 25.656  1.00 23.39  ? 71  VAL C CG2 1 
ATOM   7198  N  N   . ALA C 1 72  ? 18.289  -37.436 25.363  1.00 24.30  ? 72  ALA C N   1 
ATOM   7199  C  CA  . ALA C 1 72  ? 16.918  -37.694 24.920  1.00 22.40  ? 72  ALA C CA  1 
ATOM   7200  C  C   . ALA C 1 72  ? 15.931  -37.649 26.075  1.00 27.79  ? 72  ALA C C   1 
ATOM   7201  O  O   . ALA C 1 72  ? 14.753  -37.353 25.860  1.00 31.33  ? 72  ALA C O   1 
ATOM   7202  C  CB  . ALA C 1 72  ? 16.874  -39.041 24.189  1.00 25.22  ? 72  ALA C CB  1 
ATOM   7203  N  N   . HIS C 1 73  ? 16.383  -37.955 27.295  1.00 26.93  ? 73  HIS C N   1 
ATOM   7204  C  CA  . HIS C 1 73  ? 15.527  -37.880 28.472  1.00 32.02  ? 73  HIS C CA  1 
ATOM   7205  C  C   . HIS C 1 73  ? 15.068  -36.449 28.749  1.00 30.42  ? 73  HIS C C   1 
ATOM   7206  O  O   . HIS C 1 73  ? 14.009  -36.234 29.366  1.00 33.33  ? 73  HIS C O   1 
ATOM   7207  C  CB  . HIS C 1 73  ? 16.300  -38.425 29.666  1.00 34.32  ? 73  HIS C CB  1 
ATOM   7208  C  CG  . HIS C 1 73  ? 15.537  -38.382 30.947  1.00 40.18  ? 73  HIS C CG  1 
ATOM   7209  N  ND1 . HIS C 1 73  ? 14.760  -39.435 31.381  1.00 44.28  ? 73  HIS C ND1 1 
ATOM   7210  C  CD2 . HIS C 1 73  ? 15.414  -37.408 31.877  1.00 36.29  ? 73  HIS C CD2 1 
ATOM   7211  C  CE1 . HIS C 1 73  ? 14.211  -39.118 32.539  1.00 41.87  ? 73  HIS C CE1 1 
ATOM   7212  N  NE2 . HIS C 1 73  ? 14.580  -37.889 32.856  1.00 43.31  ? 73  HIS C NE2 1 
ATOM   7213  N  N   . ASP C 1 74  ? 15.855  -35.459 28.330  1.00 29.12  ? 74  ASP C N   1 
ATOM   7214  C  CA  . ASP C 1 74  ? 15.521  -34.024 28.419  1.00 28.77  ? 74  ASP C CA  1 
ATOM   7215  C  C   . ASP C 1 74  ? 14.961  -33.608 27.055  1.00 26.85  ? 74  ASP C C   1 
ATOM   7216  O  O   . ASP C 1 74  ? 15.715  -33.193 26.173  1.00 27.61  ? 74  ASP C O   1 
ATOM   7217  C  CB  . ASP C 1 74  ? 16.783  -33.256 28.805  1.00 30.71  ? 74  ASP C CB  1 
ATOM   7218  C  CG  . ASP C 1 74  ? 16.586  -31.727 28.900  1.00 32.02  ? 74  ASP C CG  1 
ATOM   7219  O  OD1 . ASP C 1 74  ? 15.591  -31.150 28.398  1.00 31.06  ? 74  ASP C OD1 1 
ATOM   7220  O  OD2 . ASP C 1 74  ? 17.498  -31.089 29.454  1.00 37.89  ? 74  ASP C OD2 1 
ATOM   7221  N  N   . ARG C 1 75  ? 13.624  -33.741 26.880  1.00 27.57  ? 75  ARG C N   1 
ATOM   7222  C  CA  . ARG C 1 75  ? 13.000  -33.573 25.573  1.00 27.72  ? 75  ARG C CA  1 
ATOM   7223  C  C   . ARG C 1 75  ? 13.374  -32.226 24.933  1.00 27.17  ? 75  ARG C C   1 
ATOM   7224  O  O   . ARG C 1 75  ? 13.715  -32.148 23.745  1.00 25.53  ? 75  ARG C O   1 
ATOM   7225  C  CB  . ARG C 1 75  ? 11.483  -33.704 25.733  1.00 36.57  ? 75  ARG C CB  1 
ATOM   7226  C  CG  . ARG C 1 75  ? 10.992  -35.124 25.983  1.00 40.43  ? 75  ARG C CG  1 
ATOM   7227  C  CD  . ARG C 1 75  ? 9.497   -35.248 25.606  1.00 53.90  ? 75  ARG C CD  1 
ATOM   7228  N  NE  . ARG C 1 75  ? 8.770   -36.173 26.479  1.00 58.85  ? 75  ARG C NE  1 
ATOM   7229  C  CZ  . ARG C 1 75  ? 8.227   -35.848 27.650  1.00 64.24  ? 75  ARG C CZ  1 
ATOM   7230  N  NH1 . ARG C 1 75  ? 8.291   -34.612 28.130  1.00 64.97  ? 75  ARG C NH1 1 
ATOM   7231  N  NH2 . ARG C 1 75  ? 7.626   -36.793 28.371  1.00 61.73  ? 75  ARG C NH2 1 
ATOM   7232  N  N   . LYS C 1 76  ? 13.353  -31.168 25.716  1.00 25.74  ? 76  LYS C N   1 
ATOM   7233  C  CA  . LYS C 1 76  ? 13.694  -29.861 25.166  1.00 24.63  ? 76  LYS C CA  1 
ATOM   7234  C  C   . LYS C 1 76  ? 15.144  -29.784 24.693  1.00 25.54  ? 76  LYS C C   1 
ATOM   7235  O  O   . LYS C 1 76  ? 15.415  -29.253 23.604  1.00 27.15  ? 76  LYS C O   1 
ATOM   7236  C  CB  . LYS C 1 76  ? 13.393  -28.778 26.203  1.00 24.19  ? 76  LYS C CB  1 
ATOM   7237  C  CG  . LYS C 1 76  ? 13.883  -27.401 25.797  1.00 30.01  ? 76  LYS C CG  1 
ATOM   7238  C  CD  . LYS C 1 76  ? 13.647  -26.445 26.978  1.00 39.56  ? 76  LYS C CD  1 
ATOM   7239  C  CE  . LYS C 1 76  ? 14.320  -25.057 26.789  1.00 43.03  ? 76  LYS C CE  1 
ATOM   7240  N  NZ  . LYS C 1 76  ? 14.124  -24.527 25.455  1.00 42.67  ? 76  LYS C NZ  1 
ATOM   7241  N  N   . PHE C 1 77  ? 16.113  -30.266 25.499  1.00 24.99  ? 77  PHE C N   1 
ATOM   7242  C  CA  . PHE C 1 77  ? 17.494  -30.204 25.053  1.00 23.65  ? 77  PHE C CA  1 
ATOM   7243  C  C   . PHE C 1 77  ? 17.726  -31.141 23.860  1.00 22.96  ? 77  PHE C C   1 
ATOM   7244  O  O   . PHE C 1 77  ? 18.498  -30.830 22.938  1.00 22.63  ? 77  PHE C O   1 
ATOM   7245  C  CB  . PHE C 1 77  ? 18.437  -30.562 26.180  1.00 26.10  ? 77  PHE C CB  1 
ATOM   7246  C  CG  . PHE C 1 77  ? 19.912  -30.383 25.849  1.00 25.62  ? 77  PHE C CG  1 
ATOM   7247  C  CD1 . PHE C 1 77  ? 20.390  -29.239 25.135  1.00 25.31  ? 77  PHE C CD1 1 
ATOM   7248  C  CD2 . PHE C 1 77  ? 20.840  -31.336 26.266  1.00 23.57  ? 77  PHE C CD2 1 
ATOM   7249  C  CE1 . PHE C 1 77  ? 21.788  -29.120 24.848  1.00 24.79  ? 77  PHE C CE1 1 
ATOM   7250  C  CE2 . PHE C 1 77  ? 22.232  -31.205 25.991  1.00 24.36  ? 77  PHE C CE2 1 
ATOM   7251  C  CZ  . PHE C 1 77  ? 22.699  -30.094 25.270  1.00 26.08  ? 77  PHE C CZ  1 
ATOM   7252  N  N   . ALA C 1 78  ? 17.084  -32.315 23.867  1.00 23.12  ? 78  ALA C N   1 
ATOM   7253  C  CA  . ALA C 1 78  ? 17.201  -33.197 22.702  1.00 21.03  ? 78  ALA C CA  1 
ATOM   7254  C  C   . ALA C 1 78  ? 16.703  -32.526 21.437  1.00 21.87  ? 78  ALA C C   1 
ATOM   7255  O  O   . ALA C 1 78  ? 17.359  -32.623 20.379  1.00 22.84  ? 78  ALA C O   1 
ATOM   7256  C  CB  . ALA C 1 78  ? 16.446  -34.498 22.963  1.00 23.14  ? 78  ALA C CB  1 
ATOM   7257  N  N   . LYS C 1 79  ? 15.544  -31.843 21.518  1.00 23.91  ? 79  LYS C N   1 
ATOM   7258  C  CA  . LYS C 1 79  ? 15.025  -31.123 20.360  1.00 24.20  ? 79  LYS C CA  1 
ATOM   7259  C  C   . LYS C 1 79  ? 16.015  -30.089 19.879  1.00 24.15  ? 79  LYS C C   1 
ATOM   7260  O  O   . LYS C 1 79  ? 16.311  -30.012 18.686  1.00 23.59  ? 79  LYS C O   1 
ATOM   7261  C  CB  . LYS C 1 79  ? 13.659  -30.500 20.687  1.00 25.94  ? 79  LYS C CB  1 
ATOM   7262  C  CG  . LYS C 1 79  ? 12.946  -29.861 19.512  1.00 33.88  ? 79  LYS C CG  1 
ATOM   7263  C  CD  . LYS C 1 79  ? 12.260  -28.590 19.970  1.00 41.03  ? 79  LYS C CD  1 
ATOM   7264  C  CE  . LYS C 1 79  ? 11.685  -27.778 18.793  1.00 43.77  ? 79  LYS C CE  1 
ATOM   7265  N  NZ  . LYS C 1 79  ? 12.196  -26.384 18.861  1.00 45.82  ? 79  LYS C NZ  1 
ATOM   7266  N  N   . GLU C 1 80  ? 16.540  -29.277 20.798  1.00 25.16  ? 80  GLU C N   1 
ATOM   7267  C  CA  . GLU C 1 80  ? 17.560  -28.274 20.445  1.00 24.50  ? 80  GLU C CA  1 
ATOM   7268  C  C   . GLU C 1 80  ? 18.759  -28.927 19.747  1.00 24.00  ? 80  GLU C C   1 
ATOM   7269  O  O   . GLU C 1 80  ? 19.230  -28.440 18.702  1.00 21.10  ? 80  GLU C O   1 
ATOM   7270  C  CB  . GLU C 1 80  ? 17.995  -27.536 21.721  1.00 23.80  ? 80  GLU C CB  1 
ATOM   7271  C  CG  . GLU C 1 80  ? 16.882  -26.691 22.302  1.00 27.49  ? 80  GLU C CG  1 
ATOM   7272  C  CD  . GLU C 1 80  ? 17.185  -26.178 23.721  1.00 30.38  ? 80  GLU C CD  1 
ATOM   7273  O  OE1 . GLU C 1 80  ? 17.915  -26.887 24.489  1.00 30.14  ? 80  GLU C OE1 1 
ATOM   7274  O  OE2 . GLU C 1 80  ? 16.667  -25.086 24.073  1.00 31.59  ? 80  GLU C OE2 1 
ATOM   7275  N  N   . CYS C 1 81  ? 19.264  -30.064 20.293  1.00 23.06  ? 81  CYS C N   1 
ATOM   7276  C  CA  . CYS C 1 81  ? 20.406  -30.722 19.661  1.00 24.15  ? 81  CYS C CA  1 
ATOM   7277  C  C   . CYS C 1 81  ? 20.068  -31.194 18.251  1.00 25.17  ? 81  CYS C C   1 
ATOM   7278  O  O   . CYS C 1 81  ? 20.860  -30.983 17.325  1.00 22.94  ? 81  CYS C O   1 
ATOM   7279  C  CB  . CYS C 1 81  ? 20.872  -31.926 20.498  1.00 24.11  ? 81  CYS C CB  1 
ATOM   7280  S  SG  . CYS C 1 81  ? 21.698  -31.434 22.001  1.00 24.38  ? 81  CYS C SG  1 
ATOM   7281  N  N   . MET C 1 82  ? 18.887  -31.845 18.074  1.00 22.84  ? 82  MET C N   1 
ATOM   7282  C  CA  . MET C 1 82  ? 18.513  -32.278 16.713  1.00 23.53  ? 82  MET C CA  1 
ATOM   7283  C  C   . MET C 1 82  ? 18.302  -31.095 15.776  1.00 22.57  ? 82  MET C C   1 
ATOM   7284  O  O   . MET C 1 82  ? 18.600  -31.200 14.577  1.00 24.46  ? 82  MET C O   1 
ATOM   7285  C  CB  . MET C 1 82  ? 17.308  -33.226 16.650  1.00 24.32  ? 82  MET C CB  1 
ATOM   7286  C  CG  . MET C 1 82  ? 17.551  -34.478 17.530  1.00 25.90  ? 82  MET C CG  1 
ATOM   7287  S  SD  . MET C 1 82  ? 16.181  -35.565 17.552  1.00 27.17  ? 82  MET C SD  1 
ATOM   7288  C  CE  . MET C 1 82  ? 15.514  -34.958 19.115  1.00 31.61  ? 82  MET C CE  1 
ATOM   7289  N  N   . ASP C 1 83  ? 17.792  -29.980 16.302  1.00 23.41  ? 83  ASP C N   1 
ATOM   7290  C  CA  . ASP C 1 83  ? 17.626  -28.812 15.427  1.00 23.47  ? 83  ASP C CA  1 
ATOM   7291  C  C   . ASP C 1 83  ? 18.971  -28.265 14.988  1.00 22.73  ? 83  ASP C C   1 
ATOM   7292  O  O   . ASP C 1 83  ? 19.107  -27.798 13.842  1.00 23.44  ? 83  ASP C O   1 
ATOM   7293  C  CB  . ASP C 1 83  ? 16.838  -27.716 16.110  1.00 24.56  ? 83  ASP C CB  1 
ATOM   7294  C  CG  . ASP C 1 83  ? 15.368  -28.094 16.291  1.00 28.91  ? 83  ASP C CG  1 
ATOM   7295  O  OD1 . ASP C 1 83  ? 14.905  -29.074 15.643  1.00 30.11  ? 83  ASP C OD1 1 
ATOM   7296  O  OD2 . ASP C 1 83  ? 14.709  -27.446 17.080  1.00 27.49  ? 83  ASP C OD2 1 
ATOM   7297  N  N   . ALA C 1 84  ? 19.977  -28.304 15.865  1.00 22.24  ? 84  ALA C N   1 
ATOM   7298  C  CA  . ALA C 1 84  ? 21.316  -27.868 15.422  1.00 23.15  ? 84  ALA C CA  1 
ATOM   7299  C  C   . ALA C 1 84  ? 21.897  -28.776 14.343  1.00 23.34  ? 84  ALA C C   1 
ATOM   7300  O  O   . ALA C 1 84  ? 22.486  -28.268 13.373  1.00 22.74  ? 84  ALA C O   1 
ATOM   7301  C  CB  . ALA C 1 84  ? 22.296  -27.784 16.582  1.00 22.38  ? 84  ALA C CB  1 
ATOM   7302  N  N   . ALA C 1 85  ? 21.759  -30.113 14.508  1.00 21.64  ? 85  ALA C N   1 
ATOM   7303  C  CA  . ALA C 1 85  ? 22.231  -31.068 13.498  1.00 23.87  ? 85  ALA C CA  1 
ATOM   7304  C  C   . ALA C 1 85  ? 21.541  -30.853 12.158  1.00 20.89  ? 85  ALA C C   1 
ATOM   7305  O  O   . ALA C 1 85  ? 22.147  -31.034 11.088  1.00 21.43  ? 85  ALA C O   1 
ATOM   7306  C  CB  . ALA C 1 85  ? 22.002  -32.507 13.987  1.00 21.71  ? 85  ALA C CB  1 
ATOM   7307  N  N   . GLU C 1 86  ? 20.255  -30.544 12.195  1.00 22.33  ? 86  GLU C N   1 
ATOM   7308  C  CA  . GLU C 1 86  ? 19.510  -30.335 10.978  1.00 24.62  ? 86  GLU C CA  1 
ATOM   7309  C  C   . GLU C 1 86  ? 19.958  -29.056 10.298  1.00 24.29  ? 86  GLU C C   1 
ATOM   7310  O  O   . GLU C 1 86  ? 20.152  -29.036 9.082   1.00 24.05  ? 86  GLU C O   1 
ATOM   7311  C  CB  . GLU C 1 86  ? 18.026  -30.301 11.311  1.00 25.12  ? 86  GLU C CB  1 
ATOM   7312  C  CG  . GLU C 1 86  ? 17.147  -30.024 10.112  1.00 28.32  ? 86  GLU C CG  1 
ATOM   7313  C  CD  . GLU C 1 86  ? 15.796  -30.642 10.274  1.00 32.79  ? 86  GLU C CD  1 
ATOM   7314  O  OE1 . GLU C 1 86  ? 15.661  -31.654 11.011  1.00 31.78  ? 86  GLU C OE1 1 
ATOM   7315  O  OE2 . GLU C 1 86  ? 14.863  -30.080 9.724   1.00 33.59  ? 86  GLU C OE2 1 
ATOM   7316  N  N   . ALA C 1 87  ? 20.220  -28.021 11.096  1.00 23.02  ? 87  ALA C N   1 
ATOM   7317  C  CA  . ALA C 1 87  ? 20.712  -26.749 10.577  1.00 25.03  ? 87  ALA C CA  1 
ATOM   7318  C  C   . ALA C 1 87  ? 22.041  -26.934 9.856   1.00 25.28  ? 87  ALA C C   1 
ATOM   7319  O  O   . ALA C 1 87  ? 22.306  -26.269 8.844   1.00 25.12  ? 87  ALA C O   1 
ATOM   7320  C  CB  . ALA C 1 87  ? 20.882  -25.772 11.738  1.00 22.12  ? 87  ALA C CB  1 
ATOM   7321  N  N   . TYR C 1 88  ? 22.894  -27.828 10.377  1.00 22.43  ? 88  TYR C N   1 
ATOM   7322  C  CA  . TYR C 1 88  ? 24.139  -28.143 9.680   1.00 24.16  ? 88  TYR C CA  1 
ATOM   7323  C  C   . TYR C 1 88  ? 23.866  -28.747 8.314   1.00 27.07  ? 88  TYR C C   1 
ATOM   7324  O  O   . TYR C 1 88  ? 24.597  -28.459 7.361   1.00 23.59  ? 88  TYR C O   1 
ATOM   7325  C  CB  . TYR C 1 88  ? 25.011  -29.087 10.504  1.00 20.13  ? 88  TYR C CB  1 
ATOM   7326  C  CG  . TYR C 1 88  ? 26.349  -29.275 9.872   1.00 19.74  ? 88  TYR C CG  1 
ATOM   7327  C  CD1 . TYR C 1 88  ? 26.567  -30.305 8.936   1.00 23.39  ? 88  TYR C CD1 1 
ATOM   7328  C  CD2 . TYR C 1 88  ? 27.428  -28.434 10.194  1.00 22.26  ? 88  TYR C CD2 1 
ATOM   7329  C  CE1 . TYR C 1 88  ? 27.844  -30.508 8.356   1.00 22.17  ? 88  TYR C CE1 1 
ATOM   7330  C  CE2 . TYR C 1 88  ? 28.699  -28.624 9.625   1.00 25.83  ? 88  TYR C CE2 1 
ATOM   7331  C  CZ  . TYR C 1 88  ? 28.886  -29.662 8.676   1.00 26.47  ? 88  TYR C CZ  1 
ATOM   7332  O  OH  . TYR C 1 88  ? 30.113  -29.888 8.135   1.00 28.14  ? 88  TYR C OH  1 
ATOM   7333  N  N   . GLY C 1 89  ? 22.792  -29.541 8.196   1.00 23.18  ? 89  GLY C N   1 
ATOM   7334  C  CA  . GLY C 1 89  ? 22.305  -30.025 6.912   1.00 22.72  ? 89  GLY C CA  1 
ATOM   7335  C  C   . GLY C 1 89  ? 22.090  -31.512 6.867   1.00 23.56  ? 89  GLY C C   1 
ATOM   7336  O  O   . GLY C 1 89  ? 21.744  -32.044 5.808   1.00 24.16  ? 89  GLY C O   1 
ATOM   7337  N  N   . PHE C 1 90  ? 22.205  -32.181 8.014   1.00 23.02  ? 90  PHE C N   1 
ATOM   7338  C  CA  . PHE C 1 90  ? 22.017  -33.634 8.058   1.00 21.96  ? 90  PHE C CA  1 
ATOM   7339  C  C   . PHE C 1 90  ? 20.532  -33.992 7.984   1.00 24.33  ? 90  PHE C C   1 
ATOM   7340  O  O   . PHE C 1 90  ? 19.676  -33.317 8.555   1.00 25.42  ? 90  PHE C O   1 
ATOM   7341  C  CB  . PHE C 1 90  ? 22.605  -34.217 9.346   1.00 23.99  ? 90  PHE C CB  1 
ATOM   7342  C  CG  . PHE C 1 90  ? 24.078  -34.367 9.278   1.00 22.82  ? 90  PHE C CG  1 
ATOM   7343  C  CD1 . PHE C 1 90  ? 24.635  -35.305 8.404   1.00 22.08  ? 90  PHE C CD1 1 
ATOM   7344  C  CD2 . PHE C 1 90  ? 24.900  -33.527 9.987   1.00 23.90  ? 90  PHE C CD2 1 
ATOM   7345  C  CE1 . PHE C 1 90  ? 25.998  -35.421 8.285   1.00 25.96  ? 90  PHE C CE1 1 
ATOM   7346  C  CE2 . PHE C 1 90  ? 26.295  -33.680 9.892   1.00 19.90  ? 90  PHE C CE2 1 
ATOM   7347  C  CZ  . PHE C 1 90  ? 26.818  -34.608 9.045   1.00 23.84  ? 90  PHE C CZ  1 
ATOM   7348  N  N   . ALA C 1 91  ? 20.241  -35.104 7.321   1.00 19.80  ? 91  ALA C N   1 
ATOM   7349  C  CA  . ALA C 1 91  ? 18.884  -35.584 7.169   1.00 21.55  ? 91  ALA C CA  1 
ATOM   7350  C  C   . ALA C 1 91  ? 18.281  -35.947 8.516   1.00 25.82  ? 91  ALA C C   1 
ATOM   7351  O  O   . ALA C 1 91  ? 18.937  -36.590 9.344   1.00 25.99  ? 91  ALA C O   1 
ATOM   7352  C  CB  . ALA C 1 91  ? 18.862  -36.882 6.332   1.00 21.33  ? 91  ALA C CB  1 
ATOM   7353  N  N   . ARG C 1 92  ? 16.975  -35.676 8.650   1.00 25.12  ? 92  ARG C N   1 
ATOM   7354  C  CA  . ARG C 1 92  ? 16.311  -35.939 9.916   1.00 26.25  ? 92  ARG C CA  1 
ATOM   7355  C  C   . ARG C 1 92  ? 16.092  -37.429 10.150  1.00 22.17  ? 92  ARG C C   1 
ATOM   7356  O  O   . ARG C 1 92  ? 15.817  -37.817 11.291  1.00 26.22  ? 92  ARG C O   1 
ATOM   7357  C  CB  . ARG C 1 92  ? 14.971  -35.190 9.987   1.00 28.93  ? 92  ARG C CB  1 
ATOM   7358  C  CG  . ARG C 1 92  ? 14.478  -35.066 11.417  1.00 30.09  ? 92  ARG C CG  1 
ATOM   7359  C  CD  . ARG C 1 92  ? 13.065  -34.454 11.461  1.00 33.02  ? 92  ARG C CD  1 
ATOM   7360  N  NE  . ARG C 1 92  ? 13.099  -33.028 11.117  1.00 28.51  ? 92  ARG C NE  1 
ATOM   7361  C  CZ  . ARG C 1 92  ? 12.026  -32.243 11.119  1.00 32.50  ? 92  ARG C CZ  1 
ATOM   7362  N  NH1 . ARG C 1 92  ? 10.812  -32.727 11.321  1.00 32.02  ? 92  ARG C NH1 1 
ATOM   7363  N  NH2 . ARG C 1 92  ? 12.169  -30.943 10.885  1.00 32.62  ? 92  ARG C NH2 1 
ATOM   7364  N  N   . ASP C 1 93  ? 16.197  -38.241 9.106   1.00 25.24  ? 93  ASP C N   1 
ATOM   7365  C  CA  . ASP C 1 93  ? 15.953  -39.697 9.276   1.00 23.48  ? 93  ASP C CA  1 
ATOM   7366  C  C   . ASP C 1 93  ? 17.246  -40.458 9.589   1.00 24.97  ? 93  ASP C C   1 
ATOM   7367  O  O   . ASP C 1 93  ? 17.176  -41.656 9.750   1.00 23.90  ? 93  ASP C O   1 
ATOM   7368  C  CB  . ASP C 1 93  ? 15.190  -40.296 8.114   1.00 26.29  ? 93  ASP C CB  1 
ATOM   7369  C  CG  . ASP C 1 93  ? 15.909  -39.994 6.832   1.00 29.06  ? 93  ASP C CG  1 
ATOM   7370  O  OD1 . ASP C 1 93  ? 15.608  -38.960 6.249   1.00 33.44  ? 93  ASP C OD1 1 
ATOM   7371  O  OD2 . ASP C 1 93  ? 16.821  -40.736 6.516   1.00 32.54  ? 93  ASP C OD2 1 
ATOM   7372  N  N   . LEU C 1 94  ? 18.373  -39.768 9.779   1.00 21.09  ? 94  LEU C N   1 
ATOM   7373  C  CA  . LEU C 1 94  ? 19.544  -40.433 10.321  1.00 22.84  ? 94  LEU C CA  1 
ATOM   7374  C  C   . LEU C 1 94  ? 19.302  -40.782 11.813  1.00 22.00  ? 94  LEU C C   1 
ATOM   7375  O  O   . LEU C 1 94  ? 18.413  -40.214 12.478  1.00 23.61  ? 94  LEU C O   1 
ATOM   7376  C  CB  . LEU C 1 94  ? 20.771  -39.538 10.181  1.00 21.47  ? 94  LEU C CB  1 
ATOM   7377  C  CG  . LEU C 1 94  ? 21.330  -39.385 8.770   1.00 20.39  ? 94  LEU C CG  1 
ATOM   7378  C  CD1 . LEU C 1 94  ? 22.226  -38.212 8.778   1.00 21.26  ? 94  LEU C CD1 1 
ATOM   7379  C  CD2 . LEU C 1 94  ? 22.154  -40.671 8.466   1.00 23.25  ? 94  LEU C CD2 1 
ATOM   7380  N  N   . CYS C 1 95  ? 20.102  -41.728 12.305  1.00 22.72  ? 95  CYS C N   1 
ATOM   7381  C  CA  . CYS C 1 95  ? 20.125  -42.190 13.689  1.00 20.02  ? 95  CYS C CA  1 
ATOM   7382  C  C   . CYS C 1 95  ? 19.886  -41.037 14.665  1.00 21.61  ? 95  CYS C C   1 
ATOM   7383  O  O   . CYS C 1 95  ? 20.635  -40.047 14.656  1.00 20.03  ? 95  CYS C O   1 
ATOM   7384  C  CB  . CYS C 1 95  ? 21.505  -42.812 13.969  1.00 22.63  ? 95  CYS C CB  1 
ATOM   7385  S  SG  . CYS C 1 95  ? 21.780  -43.245 15.738  1.00 20.73  ? 95  CYS C SG  1 
ATOM   7386  N  N   . SER C 1 96  ? 18.830  -41.134 15.476  1.00 21.50  ? 96  SER C N   1 
ATOM   7387  C  CA  . SER C 1 96  ? 18.535  -39.979 16.347  1.00 22.51  ? 96  SER C CA  1 
ATOM   7388  C  C   . SER C 1 96  ? 19.607  -39.768 17.437  1.00 21.02  ? 96  SER C C   1 
ATOM   7389  O  O   . SER C 1 96  ? 19.846  -38.599 17.844  1.00 20.41  ? 96  SER C O   1 
ATOM   7390  C  CB  . SER C 1 96  ? 17.101  -40.096 16.905  1.00 22.07  ? 96  SER C CB  1 
ATOM   7391  O  OG  . SER C 1 96  ? 16.961  -41.296 17.654  1.00 25.81  ? 96  SER C OG  1 
ATOM   7392  N  N   . TYR C 1 97  ? 20.284  -40.813 17.912  1.00 22.68  ? 97  TYR C N   1 
ATOM   7393  C  CA  . TYR C 1 97  ? 21.386  -40.609 18.867  1.00 21.33  ? 97  TYR C CA  1 
ATOM   7394  C  C   . TYR C 1 97  ? 22.533  -39.847 18.217  1.00 22.54  ? 97  TYR C C   1 
ATOM   7395  O  O   . TYR C 1 97  ? 23.063  -38.880 18.788  1.00 20.97  ? 97  TYR C O   1 
ATOM   7396  C  CB  . TYR C 1 97  ? 21.928  -41.935 19.429  1.00 22.54  ? 97  TYR C CB  1 
ATOM   7397  C  CG  . TYR C 1 97  ? 21.005  -42.620 20.408  1.00 23.79  ? 97  TYR C CG  1 
ATOM   7398  C  CD1 . TYR C 1 97  ? 20.002  -41.889 21.092  1.00 24.39  ? 97  TYR C CD1 1 
ATOM   7399  C  CD2 . TYR C 1 97  ? 21.204  -43.970 20.739  1.00 24.15  ? 97  TYR C CD2 1 
ATOM   7400  C  CE1 . TYR C 1 97  ? 19.137  -42.546 22.036  1.00 27.04  ? 97  TYR C CE1 1 
ATOM   7401  C  CE2 . TYR C 1 97  ? 20.367  -44.589 21.680  1.00 24.98  ? 97  TYR C CE2 1 
ATOM   7402  C  CZ  . TYR C 1 97  ? 19.356  -43.885 22.310  1.00 28.65  ? 97  TYR C CZ  1 
ATOM   7403  O  OH  . TYR C 1 97  ? 18.517  -44.542 23.243  1.00 33.07  ? 97  TYR C OH  1 
ATOM   7404  N  N   . MET C 1 98  ? 22.925  -40.278 17.002  1.00 18.01  ? 98  MET C N   1 
ATOM   7405  C  CA  . MET C 1 98  ? 23.937  -39.577 16.226  1.00 18.99  ? 98  MET C CA  1 
ATOM   7406  C  C   . MET C 1 98  ? 23.581  -38.120 16.040  1.00 20.46  ? 98  MET C C   1 
ATOM   7407  O  O   . MET C 1 98  ? 24.428  -37.247 16.234  1.00 20.68  ? 98  MET C O   1 
ATOM   7408  C  CB  . MET C 1 98  ? 24.119  -40.310 14.878  1.00 19.64  ? 98  MET C CB  1 
ATOM   7409  C  CG  . MET C 1 98  ? 25.368  -39.860 14.150  1.00 19.52  ? 98  MET C CG  1 
ATOM   7410  S  SD  . MET C 1 98  ? 25.737  -40.866 12.687  1.00 20.78  ? 98  MET C SD  1 
ATOM   7411  C  CE  . MET C 1 98  ? 24.263  -40.764 11.770  1.00 20.75  ? 98  MET C CE  1 
ATOM   7412  N  N   . ARG C 1 99  ? 22.312  -37.835 15.702  1.00 18.29  ? 99  ARG C N   1 
ATOM   7413  C  CA  . ARG C 1 99  ? 21.902  -36.436 15.443  1.00 17.39  ? 99  ARG C CA  1 
ATOM   7414  C  C   . ARG C 1 99  ? 21.925  -35.626 16.724  1.00 19.39  ? 99  ARG C C   1 
ATOM   7415  O  O   . ARG C 1 99  ? 22.457  -34.525 16.743  1.00 20.28  ? 99  ARG C O   1 
ATOM   7416  C  CB  . ARG C 1 99  ? 20.505  -36.379 14.811  1.00 21.83  ? 99  ARG C CB  1 
ATOM   7417  C  CG  . ARG C 1 99  ? 20.470  -36.924 13.339  1.00 23.91  ? 99  ARG C CG  1 
ATOM   7418  C  CD  . ARG C 1 99  ? 19.107  -36.715 12.684  1.00 21.85  ? 99  ARG C CD  1 
ATOM   7419  N  NE  . ARG C 1 99  ? 18.086  -37.508 13.390  1.00 22.14  ? 99  ARG C NE  1 
ATOM   7420  C  CZ  . ARG C 1 99  ? 17.055  -37.021 14.043  1.00 23.34  ? 99  ARG C CZ  1 
ATOM   7421  N  NH1 . ARG C 1 99  ? 16.937  -35.693 14.273  1.00 24.94  ? 99  ARG C NH1 1 
ATOM   7422  N  NH2 . ARG C 1 99  ? 16.038  -37.837 14.342  1.00 23.21  ? 99  ARG C NH2 1 
ATOM   7423  N  N   . ILE C 1 100 ? 21.481  -36.221 17.830  1.00 19.77  ? 100 ILE C N   1 
ATOM   7424  C  CA  . ILE C 1 100 ? 21.572  -35.561 19.142  1.00 18.91  ? 100 ILE C CA  1 
ATOM   7425  C  C   . ILE C 1 100 ? 23.019  -35.262 19.474  1.00 19.33  ? 100 ILE C C   1 
ATOM   7426  O  O   . ILE C 1 100 ? 23.378  -34.145 19.828  1.00 20.97  ? 100 ILE C O   1 
ATOM   7427  C  CB  . ILE C 1 100 ? 20.943  -36.456 20.226  1.00 19.85  ? 100 ILE C CB  1 
ATOM   7428  C  CG1 . ILE C 1 100 ? 19.426  -36.417 20.107  1.00 21.43  ? 100 ILE C CG1 1 
ATOM   7429  C  CG2 . ILE C 1 100 ? 21.344  -35.948 21.600  1.00 20.48  ? 100 ILE C CG2 1 
ATOM   7430  C  CD1 . ILE C 1 100 ? 18.704  -37.501 20.906  1.00 26.06  ? 100 ILE C CD1 1 
ATOM   7431  N  N   . TYR C 1 101 ? 23.877  -36.237 19.274  1.00 17.90  ? 101 TYR C N   1 
ATOM   7432  C  CA  . TYR C 1 101 ? 25.279  -36.086 19.643  1.00 19.65  ? 101 TYR C CA  1 
ATOM   7433  C  C   . TYR C 1 101 ? 25.921  -34.957 18.841  1.00 22.11  ? 101 TYR C C   1 
ATOM   7434  O  O   . TYR C 1 101 ? 26.559  -34.055 19.412  1.00 20.86  ? 101 TYR C O   1 
ATOM   7435  C  CB  . TYR C 1 101 ? 26.003  -37.420 19.446  1.00 19.52  ? 101 TYR C CB  1 
ATOM   7436  C  CG  . TYR C 1 101 ? 27.379  -37.449 20.066  1.00 18.68  ? 101 TYR C CG  1 
ATOM   7437  C  CD1 . TYR C 1 101 ? 28.481  -36.806 19.436  1.00 20.78  ? 101 TYR C CD1 1 
ATOM   7438  C  CD2 . TYR C 1 101 ? 27.576  -38.077 21.293  1.00 20.88  ? 101 TYR C CD2 1 
ATOM   7439  C  CE1 . TYR C 1 101 ? 29.760  -36.821 20.006  1.00 18.72  ? 101 TYR C CE1 1 
ATOM   7440  C  CE2 . TYR C 1 101 ? 28.832  -38.068 21.881  1.00 22.92  ? 101 TYR C CE2 1 
ATOM   7441  C  CZ  . TYR C 1 101 ? 29.889  -37.456 21.275  1.00 24.58  ? 101 TYR C CZ  1 
ATOM   7442  O  OH  . TYR C 1 101 ? 31.117  -37.550 21.930  1.00 25.23  ? 101 TYR C OH  1 
ATOM   7443  N  N   . TRP C 1 102 ? 25.736  -34.973 17.512  1.00 19.68  ? 102 TRP C N   1 
ATOM   7444  C  CA  . TRP C 1 102 ? 26.274  -33.896 16.679  1.00 19.78  ? 102 TRP C CA  1 
ATOM   7445  C  C   . TRP C 1 102 ? 25.769  -32.519 17.138  1.00 21.71  ? 102 TRP C C   1 
ATOM   7446  O  O   . TRP C 1 102 ? 26.542  -31.559 17.239  1.00 20.64  ? 102 TRP C O   1 
ATOM   7447  C  CB  . TRP C 1 102 ? 25.862  -34.162 15.251  1.00 20.52  ? 102 TRP C CB  1 
ATOM   7448  C  CG  . TRP C 1 102 ? 26.617  -35.281 14.581  1.00 19.58  ? 102 TRP C CG  1 
ATOM   7449  C  CD1 . TRP C 1 102 ? 27.823  -35.840 14.939  1.00 18.65  ? 102 TRP C CD1 1 
ATOM   7450  C  CD2 . TRP C 1 102 ? 26.205  -35.916 13.389  1.00 20.55  ? 102 TRP C CD2 1 
ATOM   7451  N  NE1 . TRP C 1 102 ? 28.178  -36.826 14.014  1.00 21.53  ? 102 TRP C NE1 1 
ATOM   7452  C  CE2 . TRP C 1 102 ? 27.167  -36.915 13.077  1.00 20.24  ? 102 TRP C CE2 1 
ATOM   7453  C  CE3 . TRP C 1 102 ? 25.053  -35.803 12.598  1.00 23.23  ? 102 TRP C CE3 1 
ATOM   7454  C  CZ2 . TRP C 1 102 ? 27.069  -37.697 11.927  1.00 19.25  ? 102 TRP C CZ2 1 
ATOM   7455  C  CZ3 . TRP C 1 102 ? 24.905  -36.675 11.485  1.00 20.85  ? 102 TRP C CZ3 1 
ATOM   7456  C  CH2 . TRP C 1 102 ? 25.904  -37.580 11.164  1.00 19.88  ? 102 TRP C CH2 1 
ATOM   7457  N  N   . GLY C 1 103 ? 24.451  -32.376 17.316  1.00 21.09  ? 103 GLY C N   1 
ATOM   7458  C  CA  . GLY C 1 103 ? 23.906  -31.069 17.695  1.00 20.97  ? 103 GLY C CA  1 
ATOM   7459  C  C   . GLY C 1 103 ? 24.485  -30.547 19.006  1.00 23.67  ? 103 GLY C C   1 
ATOM   7460  O  O   . GLY C 1 103 ? 24.791  -29.346 19.143  1.00 21.59  ? 103 GLY C O   1 
ATOM   7461  N  N   . GLY C 1 104 ? 24.598  -31.417 20.009  1.00 24.52  ? 104 GLY C N   1 
ATOM   7462  C  CA  . GLY C 1 104 ? 25.149  -30.965 21.284  1.00 24.43  ? 104 GLY C CA  1 
ATOM   7463  C  C   . GLY C 1 104 ? 26.614  -30.560 21.154  1.00 23.80  ? 104 GLY C C   1 
ATOM   7464  O  O   . GLY C 1 104 ? 27.094  -29.640 21.838  1.00 24.28  ? 104 GLY C O   1 
ATOM   7465  N  N   . MET C 1 105 ? 27.330  -31.172 20.229  1.00 22.71  ? 105 MET C N   1 
ATOM   7466  C  CA  . MET C 1 105 ? 28.696  -30.738 19.951  1.00 22.25  ? 105 MET C CA  1 
ATOM   7467  C  C   . MET C 1 105 ? 28.730  -29.349 19.322  1.00 20.35  ? 105 MET C C   1 
ATOM   7468  O  O   . MET C 1 105 ? 29.549  -28.502 19.708  1.00 23.93  ? 105 MET C O   1 
ATOM   7469  C  CB  . MET C 1 105 ? 29.379  -31.768 19.039  1.00 21.66  ? 105 MET C CB  1 
ATOM   7470  C  CG  . MET C 1 105 ? 30.895  -31.543 18.815  1.00 23.69  ? 105 MET C CG  1 
ATOM   7471  S  SD  . MET C 1 105 ? 31.577  -32.535 17.418  1.00 26.48  ? 105 MET C SD  1 
ATOM   7472  C  CE  . MET C 1 105 ? 30.348  -32.384 16.184  1.00 24.06  ? 105 MET C CE  1 
ATOM   7473  N  N   . HIS C 1 106 ? 27.939  -29.147 18.273  1.00 18.83  ? 106 HIS C N   1 
ATOM   7474  C  CA  . HIS C 1 106 ? 27.874  -27.824 17.637  1.00 20.83  ? 106 HIS C CA  1 
ATOM   7475  C  C   . HIS C 1 106 ? 27.397  -26.737 18.608  1.00 23.43  ? 106 HIS C C   1 
ATOM   7476  O  O   . HIS C 1 106 ? 27.924  -25.607 18.590  1.00 22.85  ? 106 HIS C O   1 
ATOM   7477  C  CB  . HIS C 1 106 ? 26.969  -27.915 16.420  1.00 23.10  ? 106 HIS C CB  1 
ATOM   7478  C  CG  . HIS C 1 106 ? 27.649  -28.568 15.256  1.00 20.67  ? 106 HIS C CG  1 
ATOM   7479  N  ND1 . HIS C 1 106 ? 28.506  -27.884 14.422  1.00 23.30  ? 106 HIS C ND1 1 
ATOM   7480  C  CD2 . HIS C 1 106 ? 27.643  -29.857 14.819  1.00 21.70  ? 106 HIS C CD2 1 
ATOM   7481  C  CE1 . HIS C 1 106 ? 28.966  -28.710 13.490  1.00 25.28  ? 106 HIS C CE1 1 
ATOM   7482  N  NE2 . HIS C 1 106 ? 28.433  -29.902 13.689  1.00 22.24  ? 106 HIS C NE2 1 
ATOM   7483  N  N   . LEU C 1 107 ? 26.363  -27.034 19.422  1.00 22.25  ? 107 LEU C N   1 
ATOM   7484  C  CA  . LEU C 1 107 ? 25.912  -26.082 20.450  1.00 21.63  ? 107 LEU C CA  1 
ATOM   7485  C  C   . LEU C 1 107 ? 26.956  -25.909 21.559  1.00 21.91  ? 107 LEU C C   1 
ATOM   7486  O  O   . LEU C 1 107 ? 26.911  -24.904 22.297  1.00 23.92  ? 107 LEU C O   1 
ATOM   7487  C  CB  . LEU C 1 107 ? 24.581  -26.546 21.063  1.00 21.58  ? 107 LEU C CB  1 
ATOM   7488  C  CG  . LEU C 1 107 ? 23.442  -26.568 20.074  1.00 24.74  ? 107 LEU C CG  1 
ATOM   7489  C  CD1 . LEU C 1 107 ? 22.217  -27.174 20.683  1.00 26.92  ? 107 LEU C CD1 1 
ATOM   7490  C  CD2 . LEU C 1 107 ? 23.154  -25.140 19.542  1.00 24.65  ? 107 LEU C CD2 1 
ATOM   7491  N  N   . ASN C 1 108 ? 27.877  -26.860 21.695  1.00 21.99  ? 108 ASN C N   1 
ATOM   7492  C  CA  . ASN C 1 108 ? 28.926  -26.829 22.723  1.00 23.06  ? 108 ASN C CA  1 
ATOM   7493  C  C   . ASN C 1 108 ? 28.353  -26.850 24.132  1.00 22.68  ? 108 ASN C C   1 
ATOM   7494  O  O   . ASN C 1 108 ? 28.720  -26.055 24.988  1.00 21.84  ? 108 ASN C O   1 
ATOM   7495  C  CB  . ASN C 1 108 ? 29.836  -25.622 22.512  1.00 24.29  ? 108 ASN C CB  1 
ATOM   7496  C  CG  . ASN C 1 108 ? 31.114  -25.709 23.307  1.00 27.67  ? 108 ASN C CG  1 
ATOM   7497  O  OD1 . ASN C 1 108 ? 31.550  -26.800 23.669  1.00 28.13  ? 108 ASN C OD1 1 
ATOM   7498  N  ND2 . ASN C 1 108 ? 31.692  -24.551 23.622  1.00 28.12  ? 108 ASN C ND2 1 
ATOM   7499  N  N   . LYS C 1 109 ? 27.448  -27.802 24.376  1.00 25.00  ? 109 LYS C N   1 
ATOM   7500  C  CA  . LYS C 1 109 ? 26.773  -27.895 25.668  1.00 23.89  ? 109 LYS C CA  1 
ATOM   7501  C  C   . LYS C 1 109 ? 26.819  -29.349 26.090  1.00 22.52  ? 109 LYS C C   1 
ATOM   7502  O  O   . LYS C 1 109 ? 26.506  -30.226 25.297  1.00 24.47  ? 109 LYS C O   1 
ATOM   7503  C  CB  . LYS C 1 109 ? 25.309  -27.434 25.608  1.00 21.02  ? 109 LYS C CB  1 
ATOM   7504  C  CG  . LYS C 1 109 ? 25.180  -25.952 25.261  1.00 22.60  ? 109 LYS C CG  1 
ATOM   7505  C  CD  . LYS C 1 109 ? 23.704  -25.523 25.067  1.00 26.44  ? 109 LYS C CD  1 
ATOM   7506  C  CE  . LYS C 1 109 ? 22.916  -25.718 26.327  1.00 25.12  ? 109 LYS C CE  1 
ATOM   7507  N  NZ  . LYS C 1 109 ? 21.521  -25.095 26.178  1.00 28.86  ? 109 LYS C NZ  1 
ATOM   7508  N  N   . TYR C 1 110 ? 27.258  -29.575 27.325  1.00 24.52  ? 110 TYR C N   1 
ATOM   7509  C  CA  . TYR C 1 110 ? 27.258  -30.924 27.921  1.00 22.40  ? 110 TYR C CA  1 
ATOM   7510  C  C   . TYR C 1 110 ? 25.975  -31.105 28.707  1.00 23.47  ? 110 TYR C C   1 
ATOM   7511  O  O   . TYR C 1 110 ? 25.566  -30.210 29.464  1.00 27.61  ? 110 TYR C O   1 
ATOM   7512  C  CB  . TYR C 1 110 ? 28.485  -31.036 28.818  1.00 21.49  ? 110 TYR C CB  1 
ATOM   7513  C  CG  . TYR C 1 110 ? 28.925  -32.426 29.276  1.00 24.24  ? 110 TYR C CG  1 
ATOM   7514  C  CD1 . TYR C 1 110 ? 29.005  -33.459 28.408  1.00 25.35  ? 110 TYR C CD1 1 
ATOM   7515  C  CD2 . TYR C 1 110 ? 29.322  -32.633 30.602  1.00 25.91  ? 110 TYR C CD2 1 
ATOM   7516  C  CE1 . TYR C 1 110 ? 29.437  -34.713 28.847  1.00 21.96  ? 110 TYR C CE1 1 
ATOM   7517  C  CE2 . TYR C 1 110 ? 29.782  -33.889 31.056  1.00 26.78  ? 110 TYR C CE2 1 
ATOM   7518  C  CZ  . TYR C 1 110 ? 29.842  -34.915 30.160  1.00 23.99  ? 110 TYR C CZ  1 
ATOM   7519  O  OH  . TYR C 1 110 ? 30.291  -36.197 30.557  1.00 24.16  ? 110 TYR C OH  1 
ATOM   7520  N  N   . ALA C 1 111 ? 25.357  -32.295 28.584  1.00 23.65  ? 111 ALA C N   1 
ATOM   7521  C  CA  . ALA C 1 111 ? 24.096  -32.525 29.264  1.00 26.66  ? 111 ALA C CA  1 
ATOM   7522  C  C   . ALA C 1 111 ? 24.238  -32.390 30.772  1.00 28.12  ? 111 ALA C C   1 
ATOM   7523  O  O   . ALA C 1 111 ? 23.246  -32.084 31.446  1.00 31.18  ? 111 ALA C O   1 
ATOM   7524  C  CB  . ALA C 1 111 ? 23.572  -33.934 28.939  1.00 25.76  ? 111 ALA C CB  1 
ATOM   7525  N  N   . PHE C 1 112 ? 25.452  -32.576 31.312  1.00 27.00  ? 112 PHE C N   1 
ATOM   7526  C  CA  . PHE C 1 112 ? 25.660  -32.528 32.751  1.00 29.69  ? 112 PHE C CA  1 
ATOM   7527  C  C   . PHE C 1 112 ? 26.283  -31.201 33.181  1.00 34.18  ? 112 PHE C C   1 
ATOM   7528  O  O   . PHE C 1 112 ? 26.839  -31.101 34.277  1.00 37.40  ? 112 PHE C O   1 
ATOM   7529  C  CB  . PHE C 1 112 ? 26.505  -33.721 33.186  1.00 31.58  ? 112 PHE C CB  1 
ATOM   7530  C  CG  . PHE C 1 112 ? 25.851  -35.041 32.835  1.00 31.64  ? 112 PHE C CG  1 
ATOM   7531  C  CD1 . PHE C 1 112 ? 26.023  -35.610 31.590  1.00 27.58  ? 112 PHE C CD1 1 
ATOM   7532  C  CD2 . PHE C 1 112 ? 25.001  -35.654 33.736  1.00 38.32  ? 112 PHE C CD2 1 
ATOM   7533  C  CE1 . PHE C 1 112 ? 25.388  -36.733 31.246  1.00 28.64  ? 112 PHE C CE1 1 
ATOM   7534  C  CE2 . PHE C 1 112 ? 24.375  -36.826 33.403  1.00 36.95  ? 112 PHE C CE2 1 
ATOM   7535  C  CZ  . PHE C 1 112 ? 24.574  -37.361 32.146  1.00 33.72  ? 112 PHE C CZ  1 
ATOM   7536  N  N   . GLY C 1 113 ? 26.199  -30.184 32.335  1.00 29.71  ? 113 GLY C N   1 
ATOM   7537  C  CA  . GLY C 1 113 ? 26.740  -28.896 32.709  1.00 31.50  ? 113 GLY C CA  1 
ATOM   7538  C  C   . GLY C 1 113 ? 28.042  -28.546 32.004  1.00 32.94  ? 113 GLY C C   1 
ATOM   7539  O  O   . GLY C 1 113 ? 28.967  -29.360 31.916  1.00 30.11  ? 113 GLY C O   1 
ATOM   7540  N  N   . GLY C 1 114 ? 28.138  -27.298 31.528  1.00 28.80  ? 114 GLY C N   1 
ATOM   7541  C  CA  . GLY C 1 114 ? 29.424  -26.854 31.030  1.00 28.48  ? 114 GLY C CA  1 
ATOM   7542  C  C   . GLY C 1 114 ? 29.521  -27.038 29.526  1.00 26.35  ? 114 GLY C C   1 
ATOM   7543  O  O   . GLY C 1 114 ? 28.541  -27.388 28.857  1.00 23.93  ? 114 GLY C O   1 
ATOM   7544  N  N   . GLU C 1 115 ? 30.721  -26.783 28.997  1.00 24.19  ? 115 GLU C N   1 
ATOM   7545  C  CA  . GLU C 1 115 ? 30.958  -26.895 27.556  1.00 26.43  ? 115 GLU C CA  1 
ATOM   7546  C  C   . GLU C 1 115 ? 30.951  -28.354 27.166  1.00 26.80  ? 115 GLU C C   1 
ATOM   7547  O  O   . GLU C 1 115 ? 31.055  -29.220 28.018  1.00 25.63  ? 115 GLU C O   1 
ATOM   7548  C  CB  . GLU C 1 115 ? 32.304  -26.289 27.146  1.00 29.78  ? 115 GLU C CB  1 
ATOM   7549  C  CG  . GLU C 1 115 ? 33.476  -27.019 27.759  1.00 32.91  ? 115 GLU C CG  1 
ATOM   7550  C  CD  . GLU C 1 115 ? 34.846  -26.412 27.520  1.00 39.50  ? 115 GLU C CD  1 
ATOM   7551  O  OE1 . GLU C 1 115 ? 34.975  -25.248 27.113  1.00 40.31  ? 115 GLU C OE1 1 
ATOM   7552  O  OE2 . GLU C 1 115 ? 35.830  -27.153 27.718  1.00 45.51  ? 115 GLU C OE2 1 
ATOM   7553  N  N   . PHE C 1 116 ? 30.806  -28.631 25.883  1.00 22.77  ? 116 PHE C N   1 
ATOM   7554  C  CA  . PHE C 1 116 ? 30.906  -30.041 25.446  1.00 21.79  ? 116 PHE C CA  1 
ATOM   7555  C  C   . PHE C 1 116 ? 32.375  -30.454 25.472  1.00 27.44  ? 116 PHE C C   1 
ATOM   7556  O  O   . PHE C 1 116 ? 33.188  -29.841 24.769  1.00 26.09  ? 116 PHE C O   1 
ATOM   7557  C  CB  . PHE C 1 116 ? 30.305  -30.267 24.070  1.00 21.83  ? 116 PHE C CB  1 
ATOM   7558  C  CG  . PHE C 1 116 ? 30.207  -31.727 23.756  1.00 23.65  ? 116 PHE C CG  1 
ATOM   7559  C  CD1 . PHE C 1 116 ? 29.387  -32.498 24.529  1.00 25.07  ? 116 PHE C CD1 1 
ATOM   7560  C  CD2 . PHE C 1 116 ? 31.036  -32.314 22.820  1.00 25.88  ? 116 PHE C CD2 1 
ATOM   7561  C  CE1 . PHE C 1 116 ? 29.295  -33.903 24.342  1.00 26.97  ? 116 PHE C CE1 1 
ATOM   7562  C  CE2 . PHE C 1 116 ? 30.939  -33.716 22.601  1.00 28.31  ? 116 PHE C CE2 1 
ATOM   7563  C  CZ  . PHE C 1 116 ? 30.047  -34.477 23.373  1.00 26.56  ? 116 PHE C CZ  1 
ATOM   7564  N  N   . PRO C 1 117 ? 32.789  -31.415 26.305  1.00 24.64  ? 117 PRO C N   1 
ATOM   7565  C  CA  . PRO C 1 117 ? 34.247  -31.572 26.501  1.00 26.14  ? 117 PRO C CA  1 
ATOM   7566  C  C   . PRO C 1 117 ? 34.901  -32.151 25.249  1.00 28.66  ? 117 PRO C C   1 
ATOM   7567  O  O   . PRO C 1 117 ? 34.401  -33.113 24.665  1.00 30.83  ? 117 PRO C O   1 
ATOM   7568  C  CB  . PRO C 1 117 ? 34.360  -32.509 27.720  1.00 27.27  ? 117 PRO C CB  1 
ATOM   7569  C  CG  . PRO C 1 117 ? 33.010  -32.383 28.404  1.00 27.12  ? 117 PRO C CG  1 
ATOM   7570  C  CD  . PRO C 1 117 ? 32.023  -32.204 27.275  1.00 24.37  ? 117 PRO C CD  1 
ATOM   7571  N  N   . LYS C 1 118 ? 36.027  -31.576 24.855  1.00 28.21  ? 118 LYS C N   1 
ATOM   7572  C  CA  . LYS C 1 118 ? 36.707  -32.044 23.645  1.00 28.59  ? 118 LYS C CA  1 
ATOM   7573  C  C   . LYS C 1 118 ? 37.422  -33.371 23.926  1.00 26.29  ? 118 LYS C C   1 
ATOM   7574  O  O   . LYS C 1 118 ? 38.213  -33.455 24.871  1.00 26.58  ? 118 LYS C O   1 
ATOM   7575  C  CB  . LYS C 1 118 ? 37.707  -31.015 23.142  1.00 31.11  ? 118 LYS C CB  1 
ATOM   7576  C  CG  . LYS C 1 118 ? 38.503  -31.505 21.918  1.00 34.70  ? 118 LYS C CG  1 
ATOM   7577  C  CD  . LYS C 1 118 ? 39.393  -30.420 21.361  1.00 38.81  ? 118 LYS C CD  1 
ATOM   7578  C  CE  . LYS C 1 118 ? 40.717  -30.941 20.819  1.00 43.46  ? 118 LYS C CE  1 
ATOM   7579  N  NZ  . LYS C 1 118 ? 41.410  -31.866 21.761  1.00 41.30  ? 118 LYS C NZ  1 
ATOM   7580  N  N   . PRO C 1 119 ? 37.185  -34.402 23.128  1.00 28.53  ? 119 PRO C N   1 
ATOM   7581  C  CA  . PRO C 1 119 ? 37.951  -35.658 23.271  1.00 26.12  ? 119 PRO C CA  1 
ATOM   7582  C  C   . PRO C 1 119 ? 39.358  -35.493 22.745  1.00 29.08  ? 119 PRO C C   1 
ATOM   7583  O  O   . PRO C 1 119 ? 39.634  -34.642 21.896  1.00 26.92  ? 119 PRO C O   1 
ATOM   7584  C  CB  . PRO C 1 119 ? 37.148  -36.685 22.445  1.00 25.25  ? 119 PRO C CB  1 
ATOM   7585  C  CG  . PRO C 1 119 ? 36.279  -35.857 21.516  1.00 28.36  ? 119 PRO C CG  1 
ATOM   7586  C  CD  . PRO C 1 119 ? 36.150  -34.462 22.081  1.00 28.49  ? 119 PRO C CD  1 
ATOM   7587  N  N   . ASP C 1 120 ? 40.277  -36.302 23.275  1.00 22.98  ? 120 ASP C N   1 
ATOM   7588  C  CA  . ASP C 1 120 ? 41.615  -36.324 22.705  1.00 24.01  ? 120 ASP C CA  1 
ATOM   7589  C  C   . ASP C 1 120 ? 41.664  -37.146 21.415  1.00 26.11  ? 120 ASP C C   1 
ATOM   7590  O  O   . ASP C 1 120 ? 42.453  -36.839 20.533  1.00 24.50  ? 120 ASP C O   1 
ATOM   7591  C  CB  . ASP C 1 120 ? 42.604  -36.907 23.711  1.00 22.08  ? 120 ASP C CB  1 
ATOM   7592  C  CG  . ASP C 1 120 ? 42.755  -36.037 24.940  1.00 28.02  ? 120 ASP C CG  1 
ATOM   7593  O  OD1 . ASP C 1 120 ? 42.762  -34.795 24.788  1.00 30.43  ? 120 ASP C OD1 1 
ATOM   7594  O  OD2 . ASP C 1 120 ? 42.863  -36.594 26.049  1.00 27.18  ? 120 ASP C OD2 1 
ATOM   7595  N  N   . PHE C 1 121 ? 40.814  -38.168 21.296  1.00 22.31  ? 121 PHE C N   1 
ATOM   7596  C  CA  . PHE C 1 121 ? 40.745  -38.998 20.089  1.00 23.05  ? 121 PHE C CA  1 
ATOM   7597  C  C   . PHE C 1 121 ? 39.423  -39.745 20.065  1.00 21.94  ? 121 PHE C C   1 
ATOM   7598  O  O   . PHE C 1 121 ? 38.718  -39.872 21.078  1.00 21.30  ? 121 PHE C O   1 
ATOM   7599  C  CB  . PHE C 1 121 ? 41.937  -39.985 19.983  1.00 21.63  ? 121 PHE C CB  1 
ATOM   7600  C  CG  . PHE C 1 121 ? 42.140  -40.877 21.187  1.00 21.06  ? 121 PHE C CG  1 
ATOM   7601  C  CD1 . PHE C 1 121 ? 41.513  -42.156 21.278  1.00 22.42  ? 121 PHE C CD1 1 
ATOM   7602  C  CD2 . PHE C 1 121 ? 42.965  -40.477 22.212  1.00 22.57  ? 121 PHE C CD2 1 
ATOM   7603  C  CE1 . PHE C 1 121 ? 41.721  -42.948 22.422  1.00 22.29  ? 121 PHE C CE1 1 
ATOM   7604  C  CE2 . PHE C 1 121 ? 43.203  -41.293 23.319  1.00 25.08  ? 121 PHE C CE2 1 
ATOM   7605  C  CZ  . PHE C 1 121 ? 42.581  -42.509 23.432  1.00 23.92  ? 121 PHE C CZ  1 
ATOM   7606  N  N   . VAL C 1 122 ? 39.152  -40.322 18.905  1.00 24.16  ? 122 VAL C N   1 
ATOM   7607  C  CA  . VAL C 1 122 ? 38.021  -41.220 18.688  1.00 21.91  ? 122 VAL C CA  1 
ATOM   7608  C  C   . VAL C 1 122 ? 38.564  -42.631 18.637  1.00 23.29  ? 122 VAL C C   1 
ATOM   7609  O  O   . VAL C 1 122 ? 39.578  -42.890 17.993  1.00 23.44  ? 122 VAL C O   1 
ATOM   7610  C  CB  . VAL C 1 122 ? 37.350  -40.881 17.357  1.00 21.87  ? 122 VAL C CB  1 
ATOM   7611  C  CG1 . VAL C 1 122 ? 36.439  -41.995 16.823  1.00 24.56  ? 122 VAL C CG1 1 
ATOM   7612  C  CG2 . VAL C 1 122 ? 36.682  -39.557 17.497  1.00 24.02  ? 122 VAL C CG2 1 
ATOM   7613  N  N   . PHE C 1 123 ? 37.924  -43.520 19.350  1.00 19.64  ? 123 PHE C N   1 
ATOM   7614  C  CA  . PHE C 1 123 ? 38.203  -44.955 19.279  1.00 20.56  ? 123 PHE C CA  1 
ATOM   7615  C  C   . PHE C 1 123 ? 36.851  -45.638 19.166  1.00 23.98  ? 123 PHE C C   1 
ATOM   7616  O  O   . PHE C 1 123 ? 36.072  -45.656 20.134  1.00 22.58  ? 123 PHE C O   1 
ATOM   7617  C  CB  . PHE C 1 123 ? 38.948  -45.400 20.531  1.00 22.18  ? 123 PHE C CB  1 
ATOM   7618  C  CG  . PHE C 1 123 ? 39.571  -46.772 20.396  1.00 23.23  ? 123 PHE C CG  1 
ATOM   7619  C  CD1 . PHE C 1 123 ? 40.825  -46.937 19.828  1.00 24.77  ? 123 PHE C CD1 1 
ATOM   7620  C  CD2 . PHE C 1 123 ? 38.917  -47.852 20.943  1.00 24.24  ? 123 PHE C CD2 1 
ATOM   7621  C  CE1 . PHE C 1 123 ? 41.427  -48.183 19.743  1.00 25.77  ? 123 PHE C CE1 1 
ATOM   7622  C  CE2 . PHE C 1 123 ? 39.466  -49.168 20.824  1.00 24.39  ? 123 PHE C CE2 1 
ATOM   7623  C  CZ  . PHE C 1 123 ? 40.735  -49.313 20.245  1.00 23.45  ? 123 PHE C CZ  1 
ATOM   7624  N  N   . GLN C 1 124 ? 36.607  -46.264 18.021  1.00 22.23  ? 124 GLN C N   1 
ATOM   7625  C  CA  . GLN C 1 124 ? 35.259  -46.619 17.619  1.00 19.96  ? 124 GLN C CA  1 
ATOM   7626  C  C   . GLN C 1 124 ? 35.231  -48.052 17.117  1.00 21.75  ? 124 GLN C C   1 
ATOM   7627  O  O   . GLN C 1 124 ? 36.244  -48.559 16.640  1.00 23.28  ? 124 GLN C O   1 
ATOM   7628  C  CB  . GLN C 1 124 ? 34.745  -45.614 16.515  1.00 20.51  ? 124 GLN C CB  1 
ATOM   7629  C  CG  . GLN C 1 124 ? 33.346  -45.945 15.875  1.00 19.28  ? 124 GLN C CG  1 
ATOM   7630  C  CD  . GLN C 1 124 ? 32.168  -45.958 16.834  1.00 20.04  ? 124 GLN C CD  1 
ATOM   7631  O  OE1 . GLN C 1 124 ? 32.293  -46.411 18.002  1.00 20.58  ? 124 GLN C OE1 1 
ATOM   7632  N  NE2 . GLN C 1 124 ? 30.984  -45.505 16.351  1.00 17.87  ? 124 GLN C NE2 1 
ATOM   7633  N  N   . THR C 1 125 ? 34.054  -48.689 17.236  1.00 19.38  ? 125 THR C N   1 
ATOM   7634  C  CA  . THR C 1 125 ? 33.758  -49.978 16.619  1.00 19.62  ? 125 THR C CA  1 
ATOM   7635  C  C   . THR C 1 125 ? 32.810  -49.711 15.471  1.00 23.32  ? 125 THR C C   1 
ATOM   7636  O  O   . THR C 1 125 ? 31.871  -48.915 15.618  1.00 23.06  ? 125 THR C O   1 
ATOM   7637  C  CB  . THR C 1 125 ? 33.154  -50.950 17.637  1.00 20.63  ? 125 THR C CB  1 
ATOM   7638  O  OG1 . THR C 1 125 ? 34.161  -51.354 18.583  1.00 22.11  ? 125 THR C OG1 1 
ATOM   7639  C  CG2 . THR C 1 125 ? 32.552  -52.225 16.929  1.00 20.89  ? 125 THR C CG2 1 
ATOM   7640  N  N   . GLN C 1 126 ? 33.059  -50.345 14.326  1.00 19.55  ? 126 GLN C N   1 
ATOM   7641  C  CA  . GLN C 1 126 ? 32.191  -50.149 13.172  1.00 22.51  ? 126 GLN C CA  1 
ATOM   7642  C  C   . GLN C 1 126 ? 31.500  -51.473 12.852  1.00 22.76  ? 126 GLN C C   1 
ATOM   7643  O  O   . GLN C 1 126 ? 32.157  -52.415 12.422  1.00 21.87  ? 126 GLN C O   1 
ATOM   7644  C  CB  . GLN C 1 126 ? 32.972  -49.608 11.963  1.00 20.34  ? 126 GLN C CB  1 
ATOM   7645  C  CG  . GLN C 1 126 ? 32.087  -49.037 10.862  1.00 19.98  ? 126 GLN C CG  1 
ATOM   7646  C  CD  . GLN C 1 126 ? 31.499  -50.113 9.946   1.00 21.61  ? 126 GLN C CD  1 
ATOM   7647  O  OE1 . GLN C 1 126 ? 32.231  -50.841 9.304   1.00 21.52  ? 126 GLN C OE1 1 
ATOM   7648  N  NE2 . GLN C 1 126 ? 30.137  -50.195 9.877   1.00 20.97  ? 126 GLN C NE2 1 
ATOM   7649  N  N   . ILE C 1 127 ? 30.164  -51.527 13.007  1.00 21.33  ? 127 ILE C N   1 
ATOM   7650  C  CA  . ILE C 1 127 ? 29.384  -52.660 12.533  1.00 19.13  ? 127 ILE C CA  1 
ATOM   7651  C  C   . ILE C 1 127 ? 28.091  -52.118 11.928  1.00 22.36  ? 127 ILE C C   1 
ATOM   7652  O  O   . ILE C 1 127 ? 27.674  -52.590 10.871  1.00 22.90  ? 127 ILE C O   1 
ATOM   7653  C  CB  . ILE C 1 127 ? 29.112  -53.705 13.649  1.00 19.04  ? 127 ILE C CB  1 
ATOM   7654  C  CG1 . ILE C 1 127 ? 28.416  -54.939 13.033  1.00 22.43  ? 127 ILE C CG1 1 
ATOM   7655  C  CG2 . ILE C 1 127 ? 28.412  -53.123 14.877  1.00 21.13  ? 127 ILE C CG2 1 
ATOM   7656  C  CD1 . ILE C 1 127 ? 28.320  -56.190 13.968  1.00 23.87  ? 127 ILE C CD1 1 
ATOM   7657  N  N   . CYS C 1 128 ? 27.473  -51.104 12.572  1.00 21.70  ? 128 CYS C N   1 
ATOM   7658  C  CA  . CYS C 1 128 ? 26.393  -50.318 11.941  1.00 20.88  ? 128 CYS C CA  1 
ATOM   7659  C  C   . CYS C 1 128 ? 27.003  -49.296 10.955  1.00 21.93  ? 128 CYS C C   1 
ATOM   7660  O  O   . CYS C 1 128 ? 28.059  -48.710 11.247  1.00 21.96  ? 128 CYS C O   1 
ATOM   7661  C  CB  . CYS C 1 128 ? 25.608  -49.543 13.027  1.00 20.28  ? 128 CYS C CB  1 
ATOM   7662  S  SG  . CYS C 1 128 ? 24.309  -48.483 12.335  1.00 22.29  ? 128 CYS C SG  1 
ATOM   7663  N  N   . CYS C 1 129 ? 26.386  -49.094 9.771   1.00 21.71  ? 129 CYS C N   1 
ATOM   7664  C  CA  . CYS C 1 129 ? 26.988  -48.100 8.848   1.00 21.24  ? 129 CYS C CA  1 
ATOM   7665  C  C   . CYS C 1 129 ? 27.182  -46.754 9.501   1.00 21.81  ? 129 CYS C C   1 
ATOM   7666  O  O   . CYS C 1 129 ? 28.160  -46.043 9.165   1.00 24.54  ? 129 CYS C O   1 
ATOM   7667  C  CB  . CYS C 1 129 ? 26.174  -47.920 7.585   1.00 19.98  ? 129 CYS C CB  1 
ATOM   7668  S  SG  . CYS C 1 129 ? 26.036  -49.493 6.722   1.00 24.27  ? 129 CYS C SG  1 
ATOM   7669  N  N   . SER C 1 130 ? 26.291  -46.376 10.423  1.00 23.45  ? 130 SER C N   1 
ATOM   7670  C  CA  . SER C 1 130 ? 26.385  -45.010 10.971  1.00 19.90  ? 130 SER C CA  1 
ATOM   7671  C  C   . SER C 1 130 ? 27.518  -44.878 11.981  1.00 20.62  ? 130 SER C C   1 
ATOM   7672  O  O   . SER C 1 130 ? 27.836  -43.768 12.411  1.00 21.12  ? 130 SER C O   1 
ATOM   7673  C  CB  . SER C 1 130 ? 25.011  -44.606 11.560  1.00 20.77  ? 130 SER C CB  1 
ATOM   7674  O  OG  . SER C 1 130 ? 24.034  -44.543 10.535  1.00 23.44  ? 130 SER C OG  1 
ATOM   7675  N  N   . HIS C 1 131 ? 28.137  -45.995 12.413  1.00 19.69  ? 131 HIS C N   1 
ATOM   7676  C  CA  . HIS C 1 131 ? 29.226  -45.933 13.380  1.00 19.69  ? 131 HIS C CA  1 
ATOM   7677  C  C   . HIS C 1 131 ? 30.417  -45.152 12.848  1.00 20.47  ? 131 HIS C C   1 
ATOM   7678  O  O   . HIS C 1 131 ? 31.089  -44.448 13.617  1.00 21.47  ? 131 HIS C O   1 
ATOM   7679  C  CB  . HIS C 1 131 ? 29.692  -47.352 13.730  1.00 21.99  ? 131 HIS C CB  1 
ATOM   7680  C  CG  . HIS C 1 131 ? 28.791  -48.051 14.663  1.00 22.31  ? 131 HIS C CG  1 
ATOM   7681  N  ND1 . HIS C 1 131 ? 28.617  -49.425 14.625  1.00 20.61  ? 131 HIS C ND1 1 
ATOM   7682  C  CD2 . HIS C 1 131 ? 28.037  -47.590 15.692  1.00 22.16  ? 131 HIS C CD2 1 
ATOM   7683  C  CE1 . HIS C 1 131 ? 27.772  -49.769 15.582  1.00 21.84  ? 131 HIS C CE1 1 
ATOM   7684  N  NE2 . HIS C 1 131 ? 27.419  -48.679 16.257  1.00 19.89  ? 131 HIS C NE2 1 
ATOM   7685  N  N   . SER C 1 132 ? 30.724  -45.302 11.539  1.00 21.22  ? 132 SER C N   1 
ATOM   7686  C  CA  . SER C 1 132 ? 31.798  -44.521 10.940  1.00 22.26  ? 132 SER C CA  1 
ATOM   7687  C  C   . SER C 1 132 ? 31.369  -43.089 10.783  1.00 19.86  ? 132 SER C C   1 
ATOM   7688  O  O   . SER C 1 132 ? 32.096  -42.170 11.178  1.00 23.37  ? 132 SER C O   1 
ATOM   7689  C  CB  . SER C 1 132 ? 32.234  -45.053 9.560   1.00 18.66  ? 132 SER C CB  1 
ATOM   7690  O  OG  . SER C 1 132 ? 31.177  -45.067 8.662   1.00 22.46  ? 132 SER C OG  1 
ATOM   7691  N  N   . LYS C 1 133 ? 30.184  -42.887 10.201  1.00 21.65  ? 133 LYS C N   1 
ATOM   7692  C  CA  . LYS C 1 133 ? 29.781  -41.506 9.863   1.00 20.20  ? 133 LYS C CA  1 
ATOM   7693  C  C   . LYS C 1 133 ? 29.652  -40.648 11.106  1.00 21.59  ? 133 LYS C C   1 
ATOM   7694  O  O   . LYS C 1 133 ? 30.012  -39.468 11.085  1.00 21.40  ? 133 LYS C O   1 
ATOM   7695  C  CB  . LYS C 1 133 ? 28.484  -41.476 9.035   1.00 22.14  ? 133 LYS C CB  1 
ATOM   7696  C  CG  . LYS C 1 133 ? 28.572  -42.357 7.718   1.00 22.20  ? 133 LYS C CG  1 
ATOM   7697  C  CD  . LYS C 1 133 ? 29.660  -41.868 6.800   1.00 23.77  ? 133 LYS C CD  1 
ATOM   7698  C  CE  . LYS C 1 133 ? 29.998  -42.894 5.680   1.00 23.39  ? 133 LYS C CE  1 
ATOM   7699  N  NZ  . LYS C 1 133 ? 31.379  -42.562 5.115   1.00 25.96  ? 133 LYS C NZ  1 
ATOM   7700  N  N   . TRP C 1 134 ? 29.149  -41.214 12.197  1.00 19.47  ? 134 TRP C N   1 
ATOM   7701  C  CA  . TRP C 1 134 ? 29.025  -40.464 13.450  1.00 17.35  ? 134 TRP C CA  1 
ATOM   7702  C  C   . TRP C 1 134 ? 30.342  -39.790 13.834  1.00 20.90  ? 134 TRP C C   1 
ATOM   7703  O  O   . TRP C 1 134 ? 30.386  -38.584 14.083  1.00 22.80  ? 134 TRP C O   1 
ATOM   7704  C  CB  . TRP C 1 134 ? 28.571  -41.494 14.520  1.00 18.48  ? 134 TRP C CB  1 
ATOM   7705  C  CG  . TRP C 1 134 ? 28.250  -40.969 15.878  1.00 18.88  ? 134 TRP C CG  1 
ATOM   7706  C  CD1 . TRP C 1 134 ? 28.869  -39.882 16.558  1.00 21.05  ? 134 TRP C CD1 1 
ATOM   7707  C  CD2 . TRP C 1 134 ? 27.303  -41.535 16.820  1.00 19.29  ? 134 TRP C CD2 1 
ATOM   7708  N  NE1 . TRP C 1 134 ? 28.327  -39.780 17.839  1.00 21.97  ? 134 TRP C NE1 1 
ATOM   7709  C  CE2 . TRP C 1 134 ? 27.353  -40.743 18.009  1.00 22.99  ? 134 TRP C CE2 1 
ATOM   7710  C  CE3 . TRP C 1 134 ? 26.394  -42.595 16.763  1.00 19.61  ? 134 TRP C CE3 1 
ATOM   7711  C  CZ2 . TRP C 1 134 ? 26.596  -41.063 19.154  1.00 21.16  ? 134 TRP C CZ2 1 
ATOM   7712  C  CZ3 . TRP C 1 134 ? 25.636  -42.916 17.876  1.00 21.08  ? 134 TRP C CZ3 1 
ATOM   7713  C  CH2 . TRP C 1 134 ? 25.720  -42.125 19.083  1.00 21.62  ? 134 TRP C CH2 1 
ATOM   7714  N  N   . TYR C 1 135 ? 31.429  -40.572 13.932  1.00 19.98  ? 135 TYR C N   1 
ATOM   7715  C  CA  . TYR C 1 135 ? 32.674  -40.014 14.450  1.00 20.51  ? 135 TYR C CA  1 
ATOM   7716  C  C   . TYR C 1 135 ? 33.587  -39.432 13.372  1.00 20.86  ? 135 TYR C C   1 
ATOM   7717  O  O   . TYR C 1 135 ? 34.501  -38.664 13.716  1.00 23.41  ? 135 TYR C O   1 
ATOM   7718  C  CB  . TYR C 1 135 ? 33.412  -41.012 15.316  1.00 22.40  ? 135 TYR C CB  1 
ATOM   7719  C  CG  . TYR C 1 135 ? 32.685  -41.167 16.636  1.00 21.55  ? 135 TYR C CG  1 
ATOM   7720  C  CD1 . TYR C 1 135 ? 32.776  -40.213 17.642  1.00 22.65  ? 135 TYR C CD1 1 
ATOM   7721  C  CD2 . TYR C 1 135 ? 31.810  -42.250 16.851  1.00 22.67  ? 135 TYR C CD2 1 
ATOM   7722  C  CE1 . TYR C 1 135 ? 32.073  -40.369 18.811  1.00 25.87  ? 135 TYR C CE1 1 
ATOM   7723  C  CE2 . TYR C 1 135 ? 31.110  -42.416 18.036  1.00 22.27  ? 135 TYR C CE2 1 
ATOM   7724  C  CZ  . TYR C 1 135 ? 31.258  -41.475 19.027  1.00 25.24  ? 135 TYR C CZ  1 
ATOM   7725  O  OH  . TYR C 1 135 ? 30.570  -41.622 20.208  1.00 26.07  ? 135 TYR C OH  1 
ATOM   7726  N  N   . GLN C 1 136 ? 33.342  -39.727 12.094  1.00 21.54  ? 136 GLN C N   1 
ATOM   7727  C  CA  . GLN C 1 136 ? 33.976  -38.945 11.030  1.00 19.36  ? 136 GLN C CA  1 
ATOM   7728  C  C   . GLN C 1 136 ? 33.616  -37.467 11.163  1.00 20.81  ? 136 GLN C C   1 
ATOM   7729  O  O   . GLN C 1 136 ? 34.482  -36.611 11.004  1.00 22.51  ? 136 GLN C O   1 
ATOM   7730  C  CB  . GLN C 1 136 ? 33.582  -39.472 9.650   1.00 20.40  ? 136 GLN C CB  1 
ATOM   7731  C  CG  . GLN C 1 136 ? 34.299  -40.824 9.392   1.00 23.64  ? 136 GLN C CG  1 
ATOM   7732  C  CD  . GLN C 1 136 ? 34.050  -41.365 7.990   1.00 21.99  ? 136 GLN C CD  1 
ATOM   7733  O  OE1 . GLN C 1 136 ? 32.891  -41.569 7.643   1.00 23.86  ? 136 GLN C OE1 1 
ATOM   7734  N  NE2 . GLN C 1 136 ? 35.056  -41.381 7.151   1.00 22.54  ? 136 GLN C NE2 1 
ATOM   7735  N  N   . HIS C 1 137 ? 32.341  -37.158 11.402  1.00 19.17  ? 137 HIS C N   1 
ATOM   7736  C  CA  . HIS C 1 137 ? 31.979  -35.740 11.569  1.00 20.81  ? 137 HIS C CA  1 
ATOM   7737  C  C   . HIS C 1 137 ? 32.601  -35.169 12.833  1.00 21.58  ? 137 HIS C C   1 
ATOM   7738  O  O   . HIS C 1 137 ? 33.176  -34.080 12.801  1.00 22.03  ? 137 HIS C O   1 
ATOM   7739  C  CB  . HIS C 1 137 ? 30.437  -35.616 11.550  1.00 18.99  ? 137 HIS C CB  1 
ATOM   7740  C  CG  . HIS C 1 137 ? 29.965  -34.207 11.639  1.00 19.39  ? 137 HIS C CG  1 
ATOM   7741  N  ND1 . HIS C 1 137 ? 30.196  -33.286 10.643  1.00 22.86  ? 137 HIS C ND1 1 
ATOM   7742  C  CD2 . HIS C 1 137 ? 29.380  -33.546 12.654  1.00 21.45  ? 137 HIS C CD2 1 
ATOM   7743  C  CE1 . HIS C 1 137 ? 29.738  -32.100 11.034  1.00 22.78  ? 137 HIS C CE1 1 
ATOM   7744  N  NE2 . HIS C 1 137 ? 29.233  -32.230 12.254  1.00 21.21  ? 137 HIS C NE2 1 
ATOM   7745  N  N   . VAL C 1 138 ? 32.532  -35.913 13.960  1.00 19.92  ? 138 VAL C N   1 
ATOM   7746  C  CA  . VAL C 1 138 ? 33.106  -35.454 15.215  1.00 21.85  ? 138 VAL C CA  1 
ATOM   7747  C  C   . VAL C 1 138 ? 34.608  -35.216 15.081  1.00 21.77  ? 138 VAL C C   1 
ATOM   7748  O  O   . VAL C 1 138 ? 35.124  -34.190 15.517  1.00 20.59  ? 138 VAL C O   1 
ATOM   7749  C  CB  . VAL C 1 138 ? 32.815  -36.470 16.342  1.00 21.43  ? 138 VAL C CB  1 
ATOM   7750  C  CG1 . VAL C 1 138 ? 33.626  -36.110 17.564  1.00 24.02  ? 138 VAL C CG1 1 
ATOM   7751  C  CG2 . VAL C 1 138 ? 31.331  -36.513 16.681  1.00 21.23  ? 138 VAL C CG2 1 
ATOM   7752  N  N   . ALA C 1 139 ? 35.347  -36.170 14.483  1.00 20.35  ? 139 ALA C N   1 
ATOM   7753  C  CA  . ALA C 1 139 ? 36.809  -36.021 14.428  1.00 22.71  ? 139 ALA C CA  1 
ATOM   7754  C  C   . ALA C 1 139 ? 37.198  -34.823 13.581  1.00 23.91  ? 139 ALA C C   1 
ATOM   7755  O  O   . ALA C 1 139 ? 38.188  -34.133 13.876  1.00 23.43  ? 139 ALA C O   1 
ATOM   7756  C  CB  . ALA C 1 139 ? 37.455  -37.319 13.912  1.00 25.11  ? 139 ALA C CB  1 
ATOM   7757  N  N   . LYS C 1 140 ? 36.400  -34.536 12.549  1.00 23.58  ? 140 LYS C N   1 
ATOM   7758  C  CA  . LYS C 1 140 ? 36.682  -33.370 11.713  1.00 23.45  ? 140 LYS C CA  1 
ATOM   7759  C  C   . LYS C 1 140 ? 36.358  -32.059 12.434  1.00 23.09  ? 140 LYS C C   1 
ATOM   7760  O  O   . LYS C 1 140 ? 37.103  -31.079 12.301  1.00 24.99  ? 140 LYS C O   1 
ATOM   7761  C  CB  . LYS C 1 140 ? 35.902  -33.502 10.420  1.00 24.21  ? 140 LYS C CB  1 
ATOM   7762  C  CG  . LYS C 1 140 ? 36.120  -32.383 9.418   1.00 30.10  ? 140 LYS C CG  1 
ATOM   7763  C  CD  . LYS C 1 140 ? 35.037  -31.407 9.528   1.00 29.89  ? 140 LYS C CD  1 
ATOM   7764  C  CE  . LYS C 1 140 ? 33.716  -32.010 9.302   1.00 31.69  ? 140 LYS C CE  1 
ATOM   7765  N  NZ  . LYS C 1 140 ? 32.760  -30.908 9.005   1.00 33.74  ? 140 LYS C NZ  1 
ATOM   7766  N  N   . GLU C 1 141 ? 35.236  -32.004 13.164  1.00 23.99  ? 141 GLU C N   1 
ATOM   7767  C  CA  . GLU C 1 141 ? 34.870  -30.770 13.880  1.00 26.32  ? 141 GLU C CA  1 
ATOM   7768  C  C   . GLU C 1 141 ? 35.785  -30.507 15.069  1.00 25.02  ? 141 GLU C C   1 
ATOM   7769  O  O   . GLU C 1 141 ? 36.006  -29.335 15.438  1.00 26.99  ? 141 GLU C O   1 
ATOM   7770  C  CB  . GLU C 1 141 ? 33.435  -30.858 14.369  1.00 26.16  ? 141 GLU C CB  1 
ATOM   7771  C  CG  . GLU C 1 141 ? 32.444  -30.797 13.247  1.00 27.47  ? 141 GLU C CG  1 
ATOM   7772  C  CD  . GLU C 1 141 ? 32.463  -29.443 12.573  1.00 28.60  ? 141 GLU C CD  1 
ATOM   7773  O  OE1 . GLU C 1 141 ? 32.511  -28.464 13.330  1.00 27.94  ? 141 GLU C OE1 1 
ATOM   7774  O  OE2 . GLU C 1 141 ? 32.416  -29.389 11.323  1.00 29.83  ? 141 GLU C OE2 1 
ATOM   7775  N  N   . GLU C 1 142 ? 36.318  -31.564 15.688  1.00 24.35  ? 142 GLU C N   1 
ATOM   7776  C  CA  . GLU C 1 142 ? 37.208  -31.402 16.824  1.00 23.08  ? 142 GLU C CA  1 
ATOM   7777  C  C   . GLU C 1 142 ? 38.685  -31.399 16.416  1.00 23.94  ? 142 GLU C C   1 
ATOM   7778  O  O   . GLU C 1 142 ? 39.534  -31.061 17.238  1.00 27.75  ? 142 GLU C O   1 
ATOM   7779  C  CB  . GLU C 1 142 ? 36.974  -32.535 17.868  1.00 23.30  ? 142 GLU C CB  1 
ATOM   7780  C  CG  . GLU C 1 142 ? 35.540  -32.663 18.415  1.00 27.88  ? 142 GLU C CG  1 
ATOM   7781  C  CD  . GLU C 1 142 ? 35.227  -31.638 19.518  1.00 32.19  ? 142 GLU C CD  1 
ATOM   7782  O  OE1 . GLU C 1 142 ? 35.931  -30.573 19.551  1.00 30.58  ? 142 GLU C OE1 1 
ATOM   7783  O  OE2 . GLU C 1 142 ? 34.272  -31.886 20.326  1.00 26.32  ? 142 GLU C OE2 1 
ATOM   7784  N  N   . LYS C 1 143 ? 39.027  -31.797 15.178  1.00 24.01  ? 143 LYS C N   1 
ATOM   7785  C  CA  . LYS C 1 143 ? 40.407  -31.942 14.716  1.00 22.95  ? 143 LYS C CA  1 
ATOM   7786  C  C   . LYS C 1 143 ? 41.228  -32.858 15.623  1.00 24.26  ? 143 LYS C C   1 
ATOM   7787  O  O   . LYS C 1 143 ? 42.265  -32.455 16.188  1.00 25.59  ? 143 LYS C O   1 
ATOM   7788  C  CB  . LYS C 1 143 ? 41.147  -30.603 14.549  1.00 27.58  ? 143 LYS C CB  1 
ATOM   7789  C  CG  . LYS C 1 143 ? 40.542  -29.553 13.583  1.00 38.26  ? 143 LYS C CG  1 
ATOM   7790  C  CD  . LYS C 1 143 ? 40.950  -28.165 14.104  1.00 41.61  ? 143 LYS C CD  1 
ATOM   7791  C  CE  . LYS C 1 143 ? 40.593  -27.014 13.166  1.00 42.57  ? 143 LYS C CE  1 
ATOM   7792  N  NZ  . LYS C 1 143 ? 40.711  -27.414 11.714  1.00 52.05  ? 143 LYS C NZ  1 
ATOM   7793  N  N   . ILE C 1 144 ? 40.776  -34.108 15.714  1.00 23.07  ? 144 ILE C N   1 
ATOM   7794  C  CA  . ILE C 1 144 ? 41.417  -35.109 16.574  1.00 22.93  ? 144 ILE C CA  1 
ATOM   7795  C  C   . ILE C 1 144 ? 41.622  -36.397 15.791  1.00 23.45  ? 144 ILE C C   1 
ATOM   7796  O  O   . ILE C 1 144 ? 40.895  -36.672 14.821  1.00 25.17  ? 144 ILE C O   1 
ATOM   7797  C  CB  . ILE C 1 144 ? 40.599  -35.394 17.858  1.00 21.48  ? 144 ILE C CB  1 
ATOM   7798  C  CG1 . ILE C 1 144 ? 39.148  -35.821 17.518  1.00 25.83  ? 144 ILE C CG1 1 
ATOM   7799  C  CG2 . ILE C 1 144 ? 40.584  -34.118 18.728  1.00 24.07  ? 144 ILE C CG2 1 
ATOM   7800  C  CD1 . ILE C 1 144 ? 38.351  -36.335 18.714  1.00 25.16  ? 144 ILE C CD1 1 
ATOM   7801  N  N   . PRO C 1 145 ? 42.588  -37.223 16.211  1.00 22.19  ? 145 PRO C N   1 
ATOM   7802  C  CA  . PRO C 1 145 ? 42.773  -38.526 15.554  1.00 21.31  ? 145 PRO C CA  1 
ATOM   7803  C  C   . PRO C 1 145 ? 41.625  -39.451 15.818  1.00 21.74  ? 145 PRO C C   1 
ATOM   7804  O  O   . PRO C 1 145 ? 40.920  -39.355 16.835  1.00 23.08  ? 145 PRO C O   1 
ATOM   7805  C  CB  . PRO C 1 145 ? 44.099  -39.060 16.131  1.00 24.75  ? 145 PRO C CB  1 
ATOM   7806  C  CG  . PRO C 1 145 ? 44.476  -38.113 17.233  1.00 29.04  ? 145 PRO C CG  1 
ATOM   7807  C  CD  . PRO C 1 145 ? 43.684  -36.901 17.135  1.00 26.74  ? 145 PRO C CD  1 
ATOM   7808  N  N   . GLU C 1 146 ? 41.498  -40.428 14.902  1.00 20.17  ? 146 GLU C N   1 
ATOM   7809  C  CA  . GLU C 1 146 ? 40.351  -41.313 14.940  1.00 19.82  ? 146 GLU C CA  1 
ATOM   7810  C  C   . GLU C 1 146 ? 40.745  -42.692 14.451  1.00 21.43  ? 146 GLU C C   1 
ATOM   7811  O  O   . GLU C 1 146 ? 41.470  -42.828 13.457  1.00 22.56  ? 146 GLU C O   1 
ATOM   7812  C  CB  . GLU C 1 146 ? 39.187  -40.750 14.076  1.00 21.98  ? 146 GLU C CB  1 
ATOM   7813  C  CG  . GLU C 1 146 ? 39.588  -40.515 12.568  1.00 23.79  ? 146 GLU C CG  1 
ATOM   7814  C  CD  . GLU C 1 146 ? 38.534  -39.777 11.746  1.00 28.46  ? 146 GLU C CD  1 
ATOM   7815  O  OE1 . GLU C 1 146 ? 37.326  -40.084 11.807  1.00 26.27  ? 146 GLU C OE1 1 
ATOM   7816  O  OE2 . GLU C 1 146 ? 38.902  -38.817 11.044  1.00 33.17  ? 146 GLU C OE2 1 
ATOM   7817  N  N   . PHE C 1 147 ? 40.259  -43.711 15.172  1.00 20.63  ? 147 PHE C N   1 
ATOM   7818  C  CA  . PHE C 1 147 ? 40.517  -45.103 14.857  1.00 22.39  ? 147 PHE C CA  1 
ATOM   7819  C  C   . PHE C 1 147 ? 39.192  -45.850 14.878  1.00 20.56  ? 147 PHE C C   1 
ATOM   7820  O  O   . PHE C 1 147 ? 38.357  -45.637 15.767  1.00 22.04  ? 147 PHE C O   1 
ATOM   7821  C  CB  . PHE C 1 147 ? 41.480  -45.706 15.863  1.00 18.97  ? 147 PHE C CB  1 
ATOM   7822  C  CG  . PHE C 1 147 ? 41.794  -47.120 15.584  1.00 20.42  ? 147 PHE C CG  1 
ATOM   7823  C  CD1 . PHE C 1 147 ? 42.804  -47.447 14.716  1.00 24.60  ? 147 PHE C CD1 1 
ATOM   7824  C  CD2 . PHE C 1 147 ? 41.022  -48.089 16.204  1.00 22.33  ? 147 PHE C CD2 1 
ATOM   7825  C  CE1 . PHE C 1 147 ? 43.095  -48.798 14.465  1.00 28.68  ? 147 PHE C CE1 1 
ATOM   7826  C  CE2 . PHE C 1 147 ? 41.319  -49.436 15.949  1.00 26.71  ? 147 PHE C CE2 1 
ATOM   7827  C  CZ  . PHE C 1 147 ? 42.344  -49.750 15.077  1.00 24.84  ? 147 PHE C CZ  1 
ATOM   7828  N  N   . TYR C 1 148 ? 39.005  -46.739 13.896  1.00 19.49  ? 148 TYR C N   1 
ATOM   7829  C  CA  . TYR C 1 148 ? 37.811  -47.579 13.812  1.00 18.77  ? 148 TYR C CA  1 
ATOM   7830  C  C   . TYR C 1 148 ? 38.215  -49.032 13.739  1.00 21.56  ? 148 TYR C C   1 
ATOM   7831  O  O   . TYR C 1 148 ? 39.044  -49.388 12.892  1.00 21.39  ? 148 TYR C O   1 
ATOM   7832  C  CB  . TYR C 1 148 ? 37.001  -47.261 12.537  1.00 20.38  ? 148 TYR C CB  1 
ATOM   7833  C  CG  . TYR C 1 148 ? 36.600  -45.798 12.568  1.00 20.60  ? 148 TYR C CG  1 
ATOM   7834  C  CD1 . TYR C 1 148 ? 37.517  -44.814 12.163  1.00 21.61  ? 148 TYR C CD1 1 
ATOM   7835  C  CD2 . TYR C 1 148 ? 35.323  -45.411 13.002  1.00 21.01  ? 148 TYR C CD2 1 
ATOM   7836  C  CE1 . TYR C 1 148 ? 37.149  -43.451 12.199  1.00 22.30  ? 148 TYR C CE1 1 
ATOM   7837  C  CE2 . TYR C 1 148 ? 34.967  -44.036 13.067  1.00 21.22  ? 148 TYR C CE2 1 
ATOM   7838  C  CZ  . TYR C 1 148 ? 35.844  -43.110 12.633  1.00 22.68  ? 148 TYR C CZ  1 
ATOM   7839  O  OH  . TYR C 1 148 ? 35.463  -41.774 12.735  1.00 24.04  ? 148 TYR C OH  1 
ATOM   7840  N  N   . LEU C 1 149 ? 37.587  -49.841 14.586  1.00 20.65  ? 149 LEU C N   1 
ATOM   7841  C  CA  . LEU C 1 149 ? 37.713  -51.303 14.559  1.00 22.38  ? 149 LEU C CA  1 
ATOM   7842  C  C   . LEU C 1 149 ? 36.570  -51.880 13.715  1.00 20.47  ? 149 LEU C C   1 
ATOM   7843  O  O   . LEU C 1 149 ? 35.414  -51.787 14.096  1.00 22.83  ? 149 LEU C O   1 
ATOM   7844  C  CB  . LEU C 1 149 ? 37.688  -51.783 16.003  1.00 20.77  ? 149 LEU C CB  1 
ATOM   7845  C  CG  . LEU C 1 149 ? 37.809  -53.294 16.053  1.00 19.62  ? 149 LEU C CG  1 
ATOM   7846  C  CD1 . LEU C 1 149 ? 39.239  -53.767 15.664  1.00 23.35  ? 149 LEU C CD1 1 
ATOM   7847  C  CD2 . LEU C 1 149 ? 37.419  -53.763 17.439  1.00 21.95  ? 149 LEU C CD2 1 
ATOM   7848  N  N   . ASP C 1 150 ? 36.887  -52.496 12.564  1.00 21.23  ? 150 ASP C N   1 
ATOM   7849  C  CA  . ASP C 1 150 ? 35.890  -53.111 11.704  1.00 20.90  ? 150 ASP C CA  1 
ATOM   7850  C  C   . ASP C 1 150 ? 35.659  -54.520 12.238  1.00 21.43  ? 150 ASP C C   1 
ATOM   7851  O  O   . ASP C 1 150 ? 36.535  -55.368 12.084  1.00 22.19  ? 150 ASP C O   1 
ATOM   7852  C  CB  . ASP C 1 150 ? 36.433  -53.101 10.268  1.00 20.43  ? 150 ASP C CB  1 
ATOM   7853  C  CG  . ASP C 1 150 ? 35.615  -53.938 9.287   1.00 23.59  ? 150 ASP C CG  1 
ATOM   7854  O  OD1 . ASP C 1 150 ? 34.481  -54.311 9.647   1.00 21.80  ? 150 ASP C OD1 1 
ATOM   7855  O  OD2 . ASP C 1 150 ? 36.117  -54.165 8.144   1.00 21.88  ? 150 ASP C OD2 1 
ATOM   7856  N  N   . VAL C 1 151 ? 34.506  -54.754 12.889  1.00 17.80  ? 151 VAL C N   1 
ATOM   7857  C  CA  . VAL C 1 151 ? 34.208  -56.087 13.455  1.00 21.99  ? 151 VAL C CA  1 
ATOM   7858  C  C   . VAL C 1 151 ? 33.307  -56.914 12.534  1.00 21.03  ? 151 VAL C C   1 
ATOM   7859  O  O   . VAL C 1 151 ? 32.820  -57.951 12.957  1.00 22.00  ? 151 VAL C O   1 
ATOM   7860  C  CB  . VAL C 1 151 ? 33.590  -56.007 14.854  1.00 21.23  ? 151 VAL C CB  1 
ATOM   7861  C  CG1 . VAL C 1 151 ? 34.530  -55.326 15.851  1.00 22.59  ? 151 VAL C CG1 1 
ATOM   7862  C  CG2 . VAL C 1 151 ? 32.213  -55.348 14.755  1.00 22.40  ? 151 VAL C CG2 1 
ATOM   7863  N  N   . GLY C 1 152 ? 33.176  -56.534 11.245  1.00 21.86  ? 152 GLY C N   1 
ATOM   7864  C  CA  . GLY C 1 152 ? 32.229  -57.134 10.343  1.00 21.33  ? 152 GLY C CA  1 
ATOM   7865  C  C   . GLY C 1 152 ? 32.780  -58.420 9.735   1.00 22.82  ? 152 GLY C C   1 
ATOM   7866  O  O   . GLY C 1 152 ? 33.112  -58.455 8.535   1.00 25.90  ? 152 GLY C O   1 
ATOM   7867  N  N   . VAL C 1 153 ? 32.870  -59.478 10.548  1.00 23.29  ? 153 VAL C N   1 
ATOM   7868  C  CA  . VAL C 1 153 ? 33.423  -60.740 10.081  1.00 25.61  ? 153 VAL C CA  1 
ATOM   7869  C  C   . VAL C 1 153 ? 32.361  -61.826 10.040  1.00 24.52  ? 153 VAL C C   1 
ATOM   7870  O  O   . VAL C 1 153 ? 32.689  -62.983 9.826   1.00 25.04  ? 153 VAL C O   1 
ATOM   7871  C  CB  . VAL C 1 153 ? 34.623  -61.201 10.923  1.00 24.58  ? 153 VAL C CB  1 
ATOM   7872  C  CG1 . VAL C 1 153 ? 35.815  -60.210 10.731  1.00 24.87  ? 153 VAL C CG1 1 
ATOM   7873  C  CG2 . VAL C 1 153 ? 34.213  -61.361 12.434  1.00 25.79  ? 153 VAL C CG2 1 
ATOM   7874  N  N   . GLY C 1 154 ? 31.088  -61.468 10.145  1.00 24.04  ? 154 GLY C N   1 
ATOM   7875  C  CA  . GLY C 1 154 ? 30.012  -62.439 10.012  1.00 22.84  ? 154 GLY C CA  1 
ATOM   7876  C  C   . GLY C 1 154 ? 29.716  -63.086 11.362  1.00 21.86  ? 154 GLY C C   1 
ATOM   7877  O  O   . GLY C 1 154 ? 30.317  -62.732 12.391  1.00 23.96  ? 154 GLY C O   1 
ATOM   7878  N  N   . PRO C 1 155 ? 28.766  -64.035 11.367  1.00 22.80  ? 155 PRO C N   1 
ATOM   7879  C  CA  . PRO C 1 155 ? 28.279  -64.631 12.632  1.00 27.21  ? 155 PRO C CA  1 
ATOM   7880  C  C   . PRO C 1 155 ? 29.390  -65.275 13.435  1.00 25.11  ? 155 PRO C C   1 
ATOM   7881  O  O   . PRO C 1 155 ? 30.212  -66.014 12.883  1.00 23.03  ? 155 PRO C O   1 
ATOM   7882  C  CB  . PRO C 1 155 ? 27.287  -65.708 12.163  1.00 25.68  ? 155 PRO C CB  1 
ATOM   7883  C  CG  . PRO C 1 155 ? 26.819  -65.230 10.800  1.00 27.65  ? 155 PRO C CG  1 
ATOM   7884  C  CD  . PRO C 1 155 ? 28.026  -64.503 10.198  1.00 26.29  ? 155 PRO C CD  1 
ATOM   7885  N  N   . TYR C 1 156 ? 29.333  -65.075 14.764  1.00 25.51  ? 156 TYR C N   1 
ATOM   7886  C  CA  . TYR C 1 156 ? 30.269  -65.745 15.658  1.00 24.42  ? 156 TYR C CA  1 
ATOM   7887  C  C   . TYR C 1 156 ? 30.314  -67.265 15.434  1.00 23.27  ? 156 TYR C C   1 
ATOM   7888  O  O   . TYR C 1 156 ? 31.373  -67.909 15.509  1.00 25.14  ? 156 TYR C O   1 
ATOM   7889  C  CB  . TYR C 1 156 ? 29.880  -65.477 17.112  1.00 24.89  ? 156 TYR C CB  1 
ATOM   7890  C  CG  . TYR C 1 156 ? 30.902  -65.999 18.083  1.00 24.32  ? 156 TYR C CG  1 
ATOM   7891  C  CD1 . TYR C 1 156 ? 32.174  -65.432 18.116  1.00 24.27  ? 156 TYR C CD1 1 
ATOM   7892  C  CD2 . TYR C 1 156 ? 30.607  -67.060 18.959  1.00 25.61  ? 156 TYR C CD2 1 
ATOM   7893  C  CE1 . TYR C 1 156 ? 33.134  -65.894 18.976  1.00 22.67  ? 156 TYR C CE1 1 
ATOM   7894  C  CE2 . TYR C 1 156 ? 31.564  -67.512 19.853  1.00 27.87  ? 156 TYR C CE2 1 
ATOM   7895  C  CZ  . TYR C 1 156 ? 32.815  -66.928 19.856  1.00 24.20  ? 156 TYR C CZ  1 
ATOM   7896  O  OH  . TYR C 1 156 ? 33.733  -67.446 20.730  1.00 27.52  ? 156 TYR C OH  1 
ATOM   7897  N  N   . ARG C 1 157 ? 29.172  -67.869 15.170  1.00 22.02  ? 157 ARG C N   1 
ATOM   7898  C  CA  . ARG C 1 157 ? 29.148  -69.311 15.047  1.00 25.46  ? 157 ARG C CA  1 
ATOM   7899  C  C   . ARG C 1 157 ? 29.782  -69.837 13.758  1.00 25.30  ? 157 ARG C C   1 
ATOM   7900  O  O   . ARG C 1 157 ? 30.008  -71.058 13.677  1.00 27.28  ? 157 ARG C O   1 
ATOM   7901  C  CB  . ARG C 1 157 ? 27.710  -69.816 15.154  1.00 30.39  ? 157 ARG C CB  1 
ATOM   7902  C  CG  . ARG C 1 157 ? 26.884  -69.597 13.892  1.00 31.46  ? 157 ARG C CG  1 
ATOM   7903  C  CD  . ARG C 1 157 ? 25.410  -70.002 14.189  1.00 36.38  ? 157 ARG C CD  1 
ATOM   7904  N  NE  . ARG C 1 157 ? 24.489  -69.630 13.119  1.00 35.05  ? 157 ARG C NE  1 
ATOM   7905  C  CZ  . ARG C 1 157 ? 23.161  -69.664 13.226  1.00 42.26  ? 157 ARG C CZ  1 
ATOM   7906  N  NH1 . ARG C 1 157 ? 22.558  -69.983 14.372  1.00 39.75  ? 157 ARG C NH1 1 
ATOM   7907  N  NH2 . ARG C 1 157 ? 22.419  -69.343 12.169  1.00 43.70  ? 157 ARG C NH2 1 
ATOM   7908  N  N   . ASP C 1 158 ? 30.028  -68.964 12.772  1.00 24.50  ? 158 ASP C N   1 
ATOM   7909  C  CA  . ASP C 1 158 ? 30.749  -69.289 11.539  1.00 27.13  ? 158 ASP C CA  1 
ATOM   7910  C  C   . ASP C 1 158 ? 32.209  -68.844 11.591  1.00 25.67  ? 158 ASP C C   1 
ATOM   7911  O  O   . ASP C 1 158 ? 32.882  -68.854 10.550  1.00 27.61  ? 158 ASP C O   1 
ATOM   7912  C  CB  . ASP C 1 158 ? 30.079  -68.606 10.348  1.00 28.56  ? 158 ASP C CB  1 
ATOM   7913  C  CG  . ASP C 1 158 ? 28.675  -69.085 10.103  1.00 30.52  ? 158 ASP C CG  1 
ATOM   7914  O  OD1 . ASP C 1 158 ? 28.341  -70.226 10.500  1.00 34.87  ? 158 ASP C OD1 1 
ATOM   7915  O  OD2 . ASP C 1 158 ? 27.901  -68.295 9.512   1.00 35.00  ? 158 ASP C OD2 1 
ATOM   7916  N  N   . MET C 1 159 ? 32.707  -68.442 12.754  1.00 23.36  ? 159 MET C N   1 
ATOM   7917  C  CA  . MET C 1 159 ? 34.017  -67.793 12.792  1.00 25.29  ? 159 MET C CA  1 
ATOM   7918  C  C   . MET C 1 159 ? 35.139  -68.704 12.286  1.00 27.19  ? 159 MET C C   1 
ATOM   7919  O  O   . MET C 1 159 ? 35.134  -69.929 12.470  1.00 26.40  ? 159 MET C O   1 
ATOM   7920  C  CB  . MET C 1 159 ? 34.290  -67.274 14.211  1.00 29.20  ? 159 MET C CB  1 
ATOM   7921  C  CG  . MET C 1 159 ? 35.583  -66.575 14.329  1.00 32.38  ? 159 MET C CG  1 
ATOM   7922  S  SD  . MET C 1 159 ? 35.369  -64.870 13.883  1.00 34.64  ? 159 MET C SD  1 
ATOM   7923  C  CE  . MET C 1 159 ? 33.622  -64.602 13.997  1.00 30.49  ? 159 MET C CE  1 
ATOM   7924  N  N   . THR C 1 160 ? 36.096  -68.095 11.604  1.00 25.28  ? 160 THR C N   1 
ATOM   7925  C  CA  . THR C 1 160 ? 37.286  -68.766 11.129  1.00 23.50  ? 160 THR C CA  1 
ATOM   7926  C  C   . THR C 1 160 ? 38.507  -68.132 11.778  1.00 26.46  ? 160 THR C C   1 
ATOM   7927  O  O   . THR C 1 160 ? 38.430  -67.003 12.292  1.00 23.70  ? 160 THR C O   1 
ATOM   7928  C  CB  . THR C 1 160 ? 37.399  -68.633 9.600   1.00 26.00  ? 160 THR C CB  1 
ATOM   7929  O  OG1 . THR C 1 160 ? 37.701  -67.271 9.250   1.00 24.10  ? 160 THR C OG1 1 
ATOM   7930  C  CG2 . THR C 1 160 ? 36.060  -69.025 8.928   1.00 31.31  ? 160 THR C CG2 1 
ATOM   7931  N  N   . ASP C 1 161 ? 39.651  -68.840 11.673  1.00 25.93  ? 161 ASP C N   1 
ATOM   7932  C  CA  . ASP C 1 161 ? 40.932  -68.290 12.102  1.00 24.32  ? 161 ASP C CA  1 
ATOM   7933  C  C   . ASP C 1 161 ? 41.210  -66.935 11.428  1.00 26.46  ? 161 ASP C C   1 
ATOM   7934  O  O   . ASP C 1 161 ? 41.613  -65.971 12.093  1.00 24.01  ? 161 ASP C O   1 
ATOM   7935  C  CB  . ASP C 1 161 ? 42.066  -69.248 11.777  1.00 29.63  ? 161 ASP C CB  1 
ATOM   7936  C  CG  . ASP C 1 161 ? 41.960  -70.600 12.538  1.00 34.00  ? 161 ASP C CG  1 
ATOM   7937  O  OD1 . ASP C 1 161 ? 41.595  -70.603 13.729  1.00 35.06  ? 161 ASP C OD1 1 
ATOM   7938  O  OD2 . ASP C 1 161 ? 42.353  -71.638 11.953  1.00 40.15  ? 161 ASP C OD2 1 
ATOM   7939  N  N   . ALA C 1 162 ? 41.072  -66.884 10.085  1.00 23.23  ? 162 ALA C N   1 
ATOM   7940  C  CA  . ALA C 1 162 ? 41.360  -65.649 9.357   1.00 25.00  ? 162 ALA C CA  1 
ATOM   7941  C  C   . ALA C 1 162 ? 40.444  -64.505 9.784   1.00 24.01  ? 162 ALA C C   1 
ATOM   7942  O  O   . ALA C 1 162 ? 40.883  -63.356 9.809   1.00 23.96  ? 162 ALA C O   1 
ATOM   7943  C  CB  . ALA C 1 162 ? 41.282  -65.872 7.835   1.00 27.36  ? 162 ALA C CB  1 
ATOM   7944  N  N   . ARG C 1 163 ? 39.143  -64.760 10.027  1.00 22.48  ? 163 ARG C N   1 
ATOM   7945  C  CA  . ARG C 1 163 ? 38.285  -63.674 10.497  1.00 21.20  ? 163 ARG C CA  1 
ATOM   7946  C  C   . ARG C 1 163 ? 38.770  -63.134 11.843  1.00 24.92  ? 163 ARG C C   1 
ATOM   7947  O  O   . ARG C 1 163 ? 38.802  -61.901 12.073  1.00 20.38  ? 163 ARG C O   1 
ATOM   7948  C  CB  . ARG C 1 163 ? 36.825  -64.165 10.615  1.00 24.55  ? 163 ARG C CB  1 
ATOM   7949  C  CG  . ARG C 1 163 ? 36.236  -64.433 9.216   1.00 24.54  ? 163 ARG C CG  1 
ATOM   7950  C  CD  . ARG C 1 163 ? 34.854  -65.154 9.254   1.00 23.09  ? 163 ARG C CD  1 
ATOM   7951  N  NE  . ARG C 1 163 ? 34.373  -65.265 7.876   1.00 24.97  ? 163 ARG C NE  1 
ATOM   7952  C  CZ  . ARG C 1 163 ? 33.222  -65.834 7.540   1.00 26.92  ? 163 ARG C CZ  1 
ATOM   7953  N  NH1 . ARG C 1 163 ? 32.415  -66.347 8.456   1.00 24.42  ? 163 ARG C NH1 1 
ATOM   7954  N  NH2 . ARG C 1 163 ? 32.871  -65.882 6.253   1.00 24.44  ? 163 ARG C NH2 1 
ATOM   7955  N  N   . LEU C 1 164 ? 39.115  -64.039 12.762  1.00 22.77  ? 164 LEU C N   1 
ATOM   7956  C  CA  . LEU C 1 164 ? 39.605  -63.609 14.063  1.00 24.48  ? 164 LEU C CA  1 
ATOM   7957  C  C   . LEU C 1 164 ? 40.949  -62.885 13.933  1.00 23.81  ? 164 LEU C C   1 
ATOM   7958  O  O   . LEU C 1 164 ? 41.162  -61.847 14.588  1.00 22.36  ? 164 LEU C O   1 
ATOM   7959  C  CB  . LEU C 1 164 ? 39.651  -64.844 14.978  1.00 24.66  ? 164 LEU C CB  1 
ATOM   7960  C  CG  . LEU C 1 164 ? 40.087  -64.598 16.410  1.00 24.98  ? 164 LEU C CG  1 
ATOM   7961  C  CD1 . LEU C 1 164 ? 39.354  -63.461 17.109  1.00 25.42  ? 164 LEU C CD1 1 
ATOM   7962  C  CD2 . LEU C 1 164 ? 39.891  -65.896 17.242  1.00 24.35  ? 164 LEU C CD2 1 
ATOM   7963  N  N   . ASP C 1 165 ? 41.822  -63.348 13.032  1.00 23.58  ? 165 ASP C N   1 
ATOM   7964  C  CA  . ASP C 1 165 ? 43.070  -62.636 12.730  1.00 22.42  ? 165 ASP C CA  1 
ATOM   7965  C  C   . ASP C 1 165 ? 42.782  -61.200 12.331  1.00 23.12  ? 165 ASP C C   1 
ATOM   7966  O  O   . ASP C 1 165 ? 43.497  -60.276 12.746  1.00 23.89  ? 165 ASP C O   1 
ATOM   7967  C  CB  . ASP C 1 165 ? 43.852  -63.273 11.577  1.00 24.23  ? 165 ASP C CB  1 
ATOM   7968  C  CG  . ASP C 1 165 ? 44.484  -64.609 11.921  1.00 29.56  ? 165 ASP C CG  1 
ATOM   7969  O  OD1 . ASP C 1 165 ? 44.636  -64.965 13.121  1.00 27.33  ? 165 ASP C OD1 1 
ATOM   7970  O  OD2 . ASP C 1 165 ? 44.833  -65.306 10.931  1.00 26.33  ? 165 ASP C OD2 1 
ATOM   7971  N  N   . TYR C 1 166 ? 41.746  -60.999 11.507  1.00 19.94  ? 166 TYR C N   1 
ATOM   7972  C  CA  . TYR C 1 166 ? 41.461  -59.646 11.009  1.00 18.84  ? 166 TYR C CA  1 
ATOM   7973  C  C   . TYR C 1 166 ? 41.148  -58.707 12.162  1.00 21.03  ? 166 TYR C C   1 
ATOM   7974  O  O   . TYR C 1 166 ? 41.668  -57.582 12.227  1.00 22.83  ? 166 TYR C O   1 
ATOM   7975  C  CB  . TYR C 1 166 ? 40.288  -59.687 10.067  1.00 18.89  ? 166 TYR C CB  1 
ATOM   7976  C  CG  . TYR C 1 166 ? 39.896  -58.318 9.542   1.00 19.31  ? 166 TYR C CG  1 
ATOM   7977  C  CD1 . TYR C 1 166 ? 40.855  -57.455 9.043   1.00 20.16  ? 166 TYR C CD1 1 
ATOM   7978  C  CD2 . TYR C 1 166 ? 38.536  -57.949 9.493   1.00 20.43  ? 166 TYR C CD2 1 
ATOM   7979  C  CE1 . TYR C 1 166 ? 40.473  -56.180 8.513   1.00 20.30  ? 166 TYR C CE1 1 
ATOM   7980  C  CE2 . TYR C 1 166 ? 38.123  -56.694 8.972   1.00 21.28  ? 166 TYR C CE2 1 
ATOM   7981  C  CZ  . TYR C 1 166 ? 39.102  -55.824 8.483   1.00 21.94  ? 166 TYR C CZ  1 
ATOM   7982  O  OH  . TYR C 1 166 ? 38.630  -54.614 8.016   1.00 22.23  ? 166 TYR C OH  1 
ATOM   7983  N  N   . VAL C 1 167 ? 40.309  -59.149 13.107  1.00 20.35  ? 167 VAL C N   1 
ATOM   7984  C  CA  . VAL C 1 167 ? 39.981  -58.263 14.234  1.00 21.45  ? 167 VAL C CA  1 
ATOM   7985  C  C   . VAL C 1 167 ? 41.177  -58.114 15.189  1.00 23.93  ? 167 VAL C C   1 
ATOM   7986  O  O   . VAL C 1 167 ? 41.462  -57.019 15.691  1.00 21.48  ? 167 VAL C O   1 
ATOM   7987  C  CB  . VAL C 1 167 ? 38.721  -58.796 14.915  1.00 24.01  ? 167 VAL C CB  1 
ATOM   7988  C  CG1 . VAL C 1 167 ? 38.341  -57.927 16.137  1.00 22.78  ? 167 VAL C CG1 1 
ATOM   7989  C  CG2 . VAL C 1 167 ? 37.576  -58.793 13.874  1.00 22.61  ? 167 VAL C CG2 1 
ATOM   7990  N  N   . ALA C 1 168 ? 41.852  -59.223 15.514  1.00 20.08  ? 168 ALA C N   1 
ATOM   7991  C  CA  . ALA C 1 168 ? 42.995  -59.159 16.427  1.00 23.52  ? 168 ALA C CA  1 
ATOM   7992  C  C   . ALA C 1 168 ? 44.111  -58.253 15.895  1.00 24.75  ? 168 ALA C C   1 
ATOM   7993  O  O   . ALA C 1 168 ? 44.649  -57.400 16.641  1.00 22.56  ? 168 ALA C O   1 
ATOM   7994  C  CB  . ALA C 1 168 ? 43.528  -60.577 16.710  1.00 23.53  ? 168 ALA C CB  1 
ATOM   7995  N  N   . ASN C 1 169 ? 44.424  -58.358 14.585  1.00 21.07  ? 169 ASN C N   1 
ATOM   7996  C  CA  . ASN C 1 169 ? 45.482  -57.552 14.008  1.00 21.97  ? 169 ASN C CA  1 
ATOM   7997  C  C   . ASN C 1 169 ? 45.072  -56.097 13.975  1.00 20.24  ? 169 ASN C C   1 
ATOM   7998  O  O   . ASN C 1 169 ? 45.907  -55.220 14.227  1.00 24.28  ? 169 ASN C O   1 
ATOM   7999  C  CB  . ASN C 1 169 ? 45.845  -58.033 12.599  1.00 22.87  ? 169 ASN C CB  1 
ATOM   8000  C  CG  . ASN C 1 169 ? 46.483  -59.453 12.635  1.00 24.96  ? 169 ASN C CG  1 
ATOM   8001  O  OD1 . ASN C 1 169 ? 46.871  -59.926 13.699  1.00 28.38  ? 169 ASN C OD1 1 
ATOM   8002  N  ND2 . ASN C 1 169 ? 46.588  -60.104 11.498  1.00 28.64  ? 169 ASN C ND2 1 
ATOM   8003  N  N   . GLN C 1 170 ? 43.792  -55.805 13.692  1.00 18.91  ? 170 GLN C N   1 
ATOM   8004  C  CA  . GLN C 1 170 ? 43.356  -54.399 13.820  1.00 17.56  ? 170 GLN C CA  1 
ATOM   8005  C  C   . GLN C 1 170 ? 43.506  -53.879 15.257  1.00 24.45  ? 170 GLN C C   1 
ATOM   8006  O  O   . GLN C 1 170 ? 43.875  -52.717 15.469  1.00 21.41  ? 170 GLN C O   1 
ATOM   8007  C  CB  . GLN C 1 170 ? 41.897  -54.263 13.412  1.00 19.86  ? 170 GLN C CB  1 
ATOM   8008  C  CG  . GLN C 1 170 ? 41.584  -54.361 11.943  1.00 21.70  ? 170 GLN C CG  1 
ATOM   8009  C  CD  . GLN C 1 170 ? 40.102  -54.193 11.777  1.00 26.21  ? 170 GLN C CD  1 
ATOM   8010  O  OE1 . GLN C 1 170 ? 39.570  -53.077 11.892  1.00 23.41  ? 170 GLN C OE1 1 
ATOM   8011  N  NE2 . GLN C 1 170 ? 39.390  -55.318 11.592  1.00 23.37  ? 170 GLN C NE2 1 
ATOM   8012  N  N   . LEU C 1 171 ? 43.207  -54.705 16.266  1.00 20.59  ? 171 LEU C N   1 
ATOM   8013  C  CA  . LEU C 1 171 ? 43.385  -54.237 17.646  1.00 22.69  ? 171 LEU C CA  1 
ATOM   8014  C  C   . LEU C 1 171 ? 44.844  -53.896 17.909  1.00 24.84  ? 171 LEU C C   1 
ATOM   8015  O  O   . LEU C 1 171 ? 45.133  -52.950 18.648  1.00 23.84  ? 171 LEU C O   1 
ATOM   8016  C  CB  . LEU C 1 171 ? 42.923  -55.295 18.636  1.00 21.39  ? 171 LEU C CB  1 
ATOM   8017  C  CG  . LEU C 1 171 ? 41.389  -55.316 18.754  1.00 21.65  ? 171 LEU C CG  1 
ATOM   8018  C  CD1 . LEU C 1 171 ? 41.015  -56.633 19.488  1.00 25.75  ? 171 LEU C CD1 1 
ATOM   8019  C  CD2 . LEU C 1 171 ? 40.855  -54.093 19.556  1.00 23.38  ? 171 LEU C CD2 1 
ATOM   8020  N  N   . HIS C 1 172 ? 45.776  -54.620 17.296  1.00 23.96  ? 172 HIS C N   1 
ATOM   8021  C  CA  . HIS C 1 172 ? 47.187  -54.256 17.505  1.00 24.15  ? 172 HIS C CA  1 
ATOM   8022  C  C   . HIS C 1 172 ? 47.466  -52.899 16.887  1.00 24.88  ? 172 HIS C C   1 
ATOM   8023  O  O   . HIS C 1 172 ? 48.185  -52.105 17.493  1.00 26.10  ? 172 HIS C O   1 
ATOM   8024  C  CB  . HIS C 1 172 ? 48.148  -55.326 16.947  1.00 25.47  ? 172 HIS C CB  1 
ATOM   8025  C  CG  . HIS C 1 172 ? 48.263  -56.544 17.825  1.00 26.52  ? 172 HIS C CG  1 
ATOM   8026  N  ND1 . HIS C 1 172 ? 48.986  -56.582 19.002  1.00 26.77  ? 172 HIS C ND1 1 
ATOM   8027  C  CD2 . HIS C 1 172 ? 47.690  -57.763 17.692  1.00 27.51  ? 172 HIS C CD2 1 
ATOM   8028  C  CE1 . HIS C 1 172 ? 48.855  -57.782 19.552  1.00 28.94  ? 172 HIS C CE1 1 
ATOM   8029  N  NE2 . HIS C 1 172 ? 48.083  -58.525 18.769  1.00 26.72  ? 172 HIS C NE2 1 
ATOM   8030  N  N   . ASP C 1 173 ? 46.895  -52.626 15.698  1.00 25.30  ? 173 ASP C N   1 
ATOM   8031  C  CA  . ASP C 1 173 ? 46.950  -51.248 15.141  1.00 23.68  ? 173 ASP C CA  1 
ATOM   8032  C  C   . ASP C 1 173 ? 46.373  -50.239 16.116  1.00 25.36  ? 173 ASP C C   1 
ATOM   8033  O  O   . ASP C 1 173 ? 46.856  -49.083 16.223  1.00 23.61  ? 173 ASP C O   1 
ATOM   8034  C  CB  . ASP C 1 173 ? 46.160  -51.143 13.839  1.00 24.52  ? 173 ASP C CB  1 
ATOM   8035  C  CG  . ASP C 1 173 ? 46.780  -51.928 12.663  1.00 30.96  ? 173 ASP C CG  1 
ATOM   8036  O  OD1 . ASP C 1 173 ? 47.850  -52.533 12.794  1.00 30.95  ? 173 ASP C OD1 1 
ATOM   8037  O  OD2 . ASP C 1 173 ? 46.211  -51.828 11.562  1.00 32.65  ? 173 ASP C OD2 1 
ATOM   8038  N  N   . GLY C 1 174 ? 45.284  -50.633 16.774  1.00 23.70  ? 174 GLY C N   1 
ATOM   8039  C  CA  . GLY C 1 174 ? 44.617  -49.743 17.714  1.00 24.21  ? 174 GLY C CA  1 
ATOM   8040  C  C   . GLY C 1 174 ? 45.482  -49.394 18.908  1.00 23.59  ? 174 GLY C C   1 
ATOM   8041  O  O   . GLY C 1 174 ? 45.409  -48.274 19.424  1.00 24.02  ? 174 GLY C O   1 
ATOM   8042  N  N   . ILE C 1 175 ? 46.260  -50.370 19.411  1.00 22.86  ? 175 ILE C N   1 
ATOM   8043  C  CA  . ILE C 1 175 ? 47.226  -50.081 20.482  1.00 22.21  ? 175 ILE C CA  1 
ATOM   8044  C  C   . ILE C 1 175 ? 48.228  -49.028 20.003  1.00 27.78  ? 175 ILE C C   1 
ATOM   8045  O  O   . ILE C 1 175 ? 48.446  -48.005 20.672  1.00 26.24  ? 175 ILE C O   1 
ATOM   8046  C  CB  . ILE C 1 175 ? 47.920  -51.380 20.926  1.00 25.13  ? 175 ILE C CB  1 
ATOM   8047  C  CG1 . ILE C 1 175 ? 46.901  -52.223 21.629  1.00 23.87  ? 175 ILE C CG1 1 
ATOM   8048  C  CG2 . ILE C 1 175 ? 49.112  -51.092 21.836  1.00 26.34  ? 175 ILE C CG2 1 
ATOM   8049  C  CD1 . ILE C 1 175 ? 47.424  -53.672 21.942  1.00 24.19  ? 175 ILE C CD1 1 
ATOM   8050  N  N   . ALA C 1 176 ? 48.790  -49.215 18.790  1.00 20.42  ? 176 ALA C N   1 
ATOM   8051  C  CA  . ALA C 1 176 ? 49.744  -48.223 18.308  1.00 24.59  ? 176 ALA C CA  1 
ATOM   8052  C  C   . ALA C 1 176 ? 49.081  -46.870 18.138  1.00 24.83  ? 176 ALA C C   1 
ATOM   8053  O  O   . ALA C 1 176 ? 49.708  -45.828 18.383  1.00 25.25  ? 176 ALA C O   1 
ATOM   8054  C  CB  . ALA C 1 176 ? 50.373  -48.675 16.989  1.00 26.03  ? 176 ALA C CB  1 
ATOM   8055  N  N   . PHE C 1 177 ? 47.812  -46.861 17.705  1.00 21.48  ? 177 PHE C N   1 
ATOM   8056  C  CA  . PHE C 1 177 ? 47.095  -45.605 17.476  1.00 21.13  ? 177 PHE C CA  1 
ATOM   8057  C  C   . PHE C 1 177 ? 46.901  -44.882 18.787  1.00 24.84  ? 177 PHE C C   1 
ATOM   8058  O  O   . PHE C 1 177 ? 47.132  -43.675 18.855  1.00 23.00  ? 177 PHE C O   1 
ATOM   8059  C  CB  . PHE C 1 177 ? 45.731  -45.898 16.825  1.00 23.99  ? 177 PHE C CB  1 
ATOM   8060  C  CG  . PHE C 1 177 ? 44.764  -44.743 16.900  1.00 22.41  ? 177 PHE C CG  1 
ATOM   8061  C  CD1 . PHE C 1 177 ? 43.948  -44.578 18.017  1.00 23.37  ? 177 PHE C CD1 1 
ATOM   8062  C  CD2 . PHE C 1 177 ? 44.680  -43.822 15.848  1.00 22.80  ? 177 PHE C CD2 1 
ATOM   8063  C  CE1 . PHE C 1 177 ? 43.055  -43.480 18.119  1.00 23.78  ? 177 PHE C CE1 1 
ATOM   8064  C  CE2 . PHE C 1 177 ? 43.765  -42.737 15.900  1.00 23.19  ? 177 PHE C CE2 1 
ATOM   8065  C  CZ  . PHE C 1 177 ? 42.949  -42.566 17.048  1.00 21.45  ? 177 PHE C CZ  1 
ATOM   8066  N  N   . VAL C 1 178 ? 46.496  -45.592 19.856  1.00 22.57  ? 178 VAL C N   1 
ATOM   8067  C  CA  . VAL C 1 178 ? 46.193  -44.809 21.071  1.00 20.35  ? 178 VAL C CA  1 
ATOM   8068  C  C   . VAL C 1 178 ? 47.477  -44.335 21.724  1.00 23.70  ? 178 VAL C C   1 
ATOM   8069  O  O   . VAL C 1 178 ? 47.482  -43.310 22.414  1.00 24.95  ? 178 VAL C O   1 
ATOM   8070  C  CB  . VAL C 1 178 ? 45.308  -45.594 22.058  1.00 23.73  ? 178 VAL C CB  1 
ATOM   8071  C  CG1 . VAL C 1 178 ? 43.950  -45.982 21.447  1.00 22.40  ? 178 VAL C CG1 1 
ATOM   8072  C  CG2 . VAL C 1 178 ? 46.048  -46.790 22.637  1.00 25.00  ? 178 VAL C CG2 1 
ATOM   8073  N  N   . GLU C 1 179 ? 48.583  -45.052 21.521  1.00 21.62  ? 179 GLU C N   1 
ATOM   8074  C  CA  . GLU C 1 179 ? 49.877  -44.572 22.000  1.00 25.26  ? 179 GLU C CA  1 
ATOM   8075  C  C   . GLU C 1 179 ? 50.255  -43.281 21.295  1.00 24.79  ? 179 GLU C C   1 
ATOM   8076  O  O   . GLU C 1 179 ? 50.679  -42.311 21.937  1.00 27.05  ? 179 GLU C O   1 
ATOM   8077  C  CB  . GLU C 1 179 ? 50.946  -45.614 21.747  1.00 28.86  ? 179 GLU C CB  1 
ATOM   8078  C  CG  . GLU C 1 179 ? 50.875  -46.790 22.683  1.00 28.10  ? 179 GLU C CG  1 
ATOM   8079  C  CD  . GLU C 1 179 ? 52.070  -47.707 22.520  1.00 30.02  ? 179 GLU C CD  1 
ATOM   8080  O  OE1 . GLU C 1 179 ? 52.260  -48.273 21.394  1.00 31.62  ? 179 GLU C OE1 1 
ATOM   8081  O  OE2 . GLU C 1 179 ? 52.779  -47.929 23.536  1.00 28.91  ? 179 GLU C OE2 1 
ATOM   8082  N  N   . LYS C 1 180 ? 50.183  -43.295 19.967  1.00 24.13  ? 180 LYS C N   1 
ATOM   8083  C  CA  . LYS C 1 180 ? 50.491  -42.092 19.189  1.00 28.55  ? 180 LYS C CA  1 
ATOM   8084  C  C   . LYS C 1 180 ? 49.577  -40.941 19.585  1.00 27.36  ? 180 LYS C C   1 
ATOM   8085  O  O   . LYS C 1 180 ? 50.019  -39.795 19.765  1.00 29.38  ? 180 LYS C O   1 
ATOM   8086  C  CB  . LYS C 1 180 ? 50.343  -42.412 17.704  1.00 25.58  ? 180 LYS C CB  1 
ATOM   8087  C  CG  . LYS C 1 180 ? 50.646  -41.217 16.779  1.00 32.71  ? 180 LYS C CG  1 
ATOM   8088  C  CD  . LYS C 1 180 ? 50.679  -41.728 15.318  1.00 33.48  ? 180 LYS C CD  1 
ATOM   8089  C  CE  . LYS C 1 180 ? 50.871  -40.566 14.314  1.00 48.16  ? 180 LYS C CE  1 
ATOM   8090  N  NZ  . LYS C 1 180 ? 50.469  -40.963 12.919  1.00 47.15  ? 180 LYS C NZ  1 
ATOM   8091  N  N   . ALA C 1 181 ? 48.279  -41.216 19.681  1.00 25.64  ? 181 ALA C N   1 
ATOM   8092  C  CA  . ALA C 1 181 ? 47.316  -40.133 19.870  1.00 26.07  ? 181 ALA C CA  1 
ATOM   8093  C  C   . ALA C 1 181 ? 47.426  -39.507 21.251  1.00 26.96  ? 181 ALA C C   1 
ATOM   8094  O  O   . ALA C 1 181 ? 47.152  -38.308 21.402  1.00 27.38  ? 181 ALA C O   1 
ATOM   8095  C  CB  . ALA C 1 181 ? 45.885  -40.653 19.609  1.00 23.91  ? 181 ALA C CB  1 
ATOM   8096  N  N   . SER C 1 182 ? 47.795  -40.289 22.283  1.00 24.13  ? 182 SER C N   1 
ATOM   8097  C  CA  . SER C 1 182 ? 47.872  -39.830 23.666  1.00 23.48  ? 182 SER C CA  1 
ATOM   8098  C  C   . SER C 1 182 ? 49.277  -39.377 24.052  1.00 26.44  ? 182 SER C C   1 
ATOM   8099  O  O   . SER C 1 182 ? 49.426  -38.663 25.031  1.00 31.18  ? 182 SER C O   1 
ATOM   8100  C  CB  . SER C 1 182 ? 47.470  -40.978 24.605  1.00 26.50  ? 182 SER C CB  1 
ATOM   8101  O  OG  . SER C 1 182 ? 48.515  -41.950 24.597  1.00 26.95  ? 182 SER C OG  1 
ATOM   8102  N  N   . GLY C 1 183 ? 50.298  -39.836 23.336  1.00 24.99  ? 183 GLY C N   1 
ATOM   8103  C  CA  . GLY C 1 183 ? 51.692  -39.662 23.729  1.00 27.23  ? 183 GLY C CA  1 
ATOM   8104  C  C   . GLY C 1 183 ? 52.115  -40.495 24.930  1.00 30.86  ? 183 GLY C C   1 
ATOM   8105  O  O   . GLY C 1 183 ? 53.189  -40.251 25.494  1.00 31.41  ? 183 GLY C O   1 
ATOM   8106  N  N   . ARG C 1 184 ? 51.310  -41.459 25.333  1.00 26.81  ? 184 ARG C N   1 
ATOM   8107  C  CA  . ARG C 1 184 ? 51.654  -42.342 26.443  1.00 24.16  ? 184 ARG C CA  1 
ATOM   8108  C  C   . ARG C 1 184 ? 52.077  -43.712 25.936  1.00 26.58  ? 184 ARG C C   1 
ATOM   8109  O  O   . ARG C 1 184 ? 51.752  -44.106 24.827  1.00 27.07  ? 184 ARG C O   1 
ATOM   8110  C  CB  . ARG C 1 184 ? 50.491  -42.503 27.411  1.00 25.43  ? 184 ARG C CB  1 
ATOM   8111  C  CG  . ARG C 1 184 ? 50.055  -41.175 28.033  1.00 28.97  ? 184 ARG C CG  1 
ATOM   8112  C  CD  . ARG C 1 184 ? 49.138  -41.464 29.218  1.00 26.98  ? 184 ARG C CD  1 
ATOM   8113  N  NE  . ARG C 1 184 ? 48.535  -40.281 29.813  1.00 27.75  ? 184 ARG C NE  1 
ATOM   8114  C  CZ  . ARG C 1 184 ? 47.682  -40.374 30.824  1.00 29.92  ? 184 ARG C CZ  1 
ATOM   8115  N  NH1 . ARG C 1 184 ? 47.392  -41.550 31.382  1.00 27.23  ? 184 ARG C NH1 1 
ATOM   8116  N  NH2 . ARG C 1 184 ? 47.125  -39.268 31.315  1.00 26.42  ? 184 ARG C NH2 1 
ATOM   8117  N  N   . LYS C 1 185 ? 52.843  -44.415 26.772  1.00 28.84  ? 185 LYS C N   1 
ATOM   8118  C  CA  . LYS C 1 185 ? 53.227  -45.790 26.507  1.00 28.86  ? 185 LYS C CA  1 
ATOM   8119  C  C   . LYS C 1 185 ? 52.165  -46.717 27.070  1.00 30.52  ? 185 LYS C C   1 
ATOM   8120  O  O   . LYS C 1 185 ? 51.799  -46.613 28.242  1.00 30.63  ? 185 LYS C O   1 
ATOM   8121  C  CB  . LYS C 1 185 ? 54.588  -46.110 27.143  1.00 33.05  ? 185 LYS C CB  1 
ATOM   8122  C  CG  . LYS C 1 185 ? 55.037  -47.549 26.800  1.00 35.30  ? 185 LYS C CG  1 
ATOM   8123  C  CD  . LYS C 1 185 ? 56.443  -47.854 27.298  1.00 42.23  ? 185 LYS C CD  1 
ATOM   8124  C  CE  . LYS C 1 185 ? 56.812  -49.294 26.898  1.00 47.27  ? 185 LYS C CE  1 
ATOM   8125  N  NZ  . LYS C 1 185 ? 56.856  -49.520 25.429  1.00 51.62  ? 185 LYS C NZ  1 
ATOM   8126  N  N   . PHE C 1 186 ? 51.710  -47.633 26.230  1.00 30.88  ? 186 PHE C N   1 
ATOM   8127  C  CA  . PHE C 1 186 ? 50.720  -48.640 26.587  1.00 27.05  ? 186 PHE C CA  1 
ATOM   8128  C  C   . PHE C 1 186 ? 51.316  -49.628 27.556  1.00 30.25  ? 186 PHE C C   1 
ATOM   8129  O  O   . PHE C 1 186 ? 52.474  -50.035 27.414  1.00 30.91  ? 186 PHE C O   1 
ATOM   8130  C  CB  . PHE C 1 186 ? 50.316  -49.326 25.287  1.00 23.62  ? 186 PHE C CB  1 
ATOM   8131  C  CG  . PHE C 1 186 ? 49.218  -50.302 25.378  1.00 23.38  ? 186 PHE C CG  1 
ATOM   8132  C  CD1 . PHE C 1 186 ? 47.908  -49.912 25.216  1.00 23.74  ? 186 PHE C CD1 1 
ATOM   8133  C  CD2 . PHE C 1 186 ? 49.523  -51.661 25.522  1.00 25.96  ? 186 PHE C CD2 1 
ATOM   8134  C  CE1 . PHE C 1 186 ? 46.874  -50.872 25.178  1.00 26.40  ? 186 PHE C CE1 1 
ATOM   8135  C  CE2 . PHE C 1 186 ? 48.509  -52.624 25.473  1.00 24.10  ? 186 PHE C CE2 1 
ATOM   8136  C  CZ  . PHE C 1 186 ? 47.171  -52.220 25.324  1.00 23.73  ? 186 PHE C CZ  1 
ATOM   8137  N  N   . ASP C 1 187 ? 50.537  -49.995 28.562  1.00 23.78  ? 187 ASP C N   1 
ATOM   8138  C  CA  . ASP C 1 187 ? 51.014  -50.872 29.617  1.00 24.64  ? 187 ASP C CA  1 
ATOM   8139  C  C   . ASP C 1 187 ? 50.276  -52.202 29.571  1.00 25.78  ? 187 ASP C C   1 
ATOM   8140  O  O   . ASP C 1 187 ? 49.050  -52.252 29.805  1.00 23.70  ? 187 ASP C O   1 
ATOM   8141  C  CB  . ASP C 1 187 ? 50.823  -50.217 30.980  1.00 27.73  ? 187 ASP C CB  1 
ATOM   8142  C  CG  . ASP C 1 187 ? 51.410  -51.031 32.053  1.00 29.39  ? 187 ASP C CG  1 
ATOM   8143  O  OD1 . ASP C 1 187 ? 52.644  -50.945 32.266  1.00 33.43  ? 187 ASP C OD1 1 
ATOM   8144  O  OD2 . ASP C 1 187 ? 50.657  -51.805 32.673  1.00 30.17  ? 187 ASP C OD2 1 
ATOM   8145  N  N   . ASP C 1 188 ? 51.015  -53.294 29.289  1.00 28.14  ? 188 ASP C N   1 
ATOM   8146  C  CA  . ASP C 1 188 ? 50.349  -54.589 29.132  1.00 27.80  ? 188 ASP C CA  1 
ATOM   8147  C  C   . ASP C 1 188 ? 49.575  -54.993 30.391  1.00 27.79  ? 188 ASP C C   1 
ATOM   8148  O  O   . ASP C 1 188 ? 48.487  -55.598 30.303  1.00 28.42  ? 188 ASP C O   1 
ATOM   8149  C  CB  . ASP C 1 188 ? 51.379  -55.675 28.821  1.00 27.00  ? 188 ASP C CB  1 
ATOM   8150  C  CG  . ASP C 1 188 ? 51.902  -55.581 27.393  1.00 31.45  ? 188 ASP C CG  1 
ATOM   8151  O  OD1 . ASP C 1 188 ? 51.223  -54.947 26.595  1.00 34.33  ? 188 ASP C OD1 1 
ATOM   8152  O  OD2 . ASP C 1 188 ? 52.995  -56.135 27.095  1.00 37.80  ? 188 ASP C OD2 1 
ATOM   8153  N  N   . GLU C 1 189 ? 50.124  -54.712 31.561  1.00 25.38  ? 189 GLU C N   1 
ATOM   8154  C  CA  . GLU C 1 189 ? 49.450  -55.141 32.799  1.00 26.75  ? 189 GLU C CA  1 
ATOM   8155  C  C   . GLU C 1 189 ? 48.108  -54.425 32.958  1.00 30.21  ? 189 GLU C C   1 
ATOM   8156  O  O   . GLU C 1 189 ? 47.092  -55.066 33.245  1.00 27.16  ? 189 GLU C O   1 
ATOM   8157  C  CB  . GLU C 1 189 ? 50.326  -54.885 34.029  1.00 30.28  ? 189 GLU C CB  1 
ATOM   8158  C  CG  . GLU C 1 189 ? 49.599  -55.222 35.382  1.00 34.44  ? 189 GLU C CG  1 
ATOM   8159  C  CD  . GLU C 1 189 ? 50.526  -55.206 36.619  1.00 48.34  ? 189 GLU C CD  1 
ATOM   8160  O  OE1 . GLU C 1 189 ? 51.176  -54.163 36.835  1.00 43.03  ? 189 GLU C OE1 1 
ATOM   8161  O  OE2 . GLU C 1 189 ? 50.541  -56.177 37.424  1.00 54.37  ? 189 GLU C OE2 1 
ATOM   8162  N  N   . LEU C 1 190 ? 48.075  -53.086 32.755  1.00 27.75  ? 190 LEU C N   1 
ATOM   8163  C  CA  . LEU C 1 190 ? 46.789  -52.378 32.799  1.00 26.41  ? 190 LEU C CA  1 
ATOM   8164  C  C   . LEU C 1 190 ? 45.842  -52.912 31.742  1.00 23.43  ? 190 LEU C C   1 
ATOM   8165  O  O   . LEU C 1 190 ? 44.624  -52.968 31.959  1.00 25.48  ? 190 LEU C O   1 
ATOM   8166  C  CB  . LEU C 1 190 ? 46.975  -50.861 32.577  1.00 22.50  ? 190 LEU C CB  1 
ATOM   8167  C  CG  . LEU C 1 190 ? 47.709  -50.119 33.725  1.00 27.90  ? 190 LEU C CG  1 
ATOM   8168  C  CD1 . LEU C 1 190 ? 47.761  -48.617 33.384  1.00 27.25  ? 190 LEU C CD1 1 
ATOM   8169  C  CD2 . LEU C 1 190 ? 47.033  -50.258 35.093  1.00 29.30  ? 190 LEU C CD2 1 
ATOM   8170  N  N   . PHE C 1 191 ? 46.349  -53.157 30.526  1.00 25.19  ? 191 PHE C N   1 
ATOM   8171  C  CA  . PHE C 1 191 ? 45.499  -53.689 29.476  1.00 26.04  ? 191 PHE C CA  1 
ATOM   8172  C  C   . PHE C 1 191 ? 44.891  -55.033 29.889  1.00 25.12  ? 191 PHE C C   1 
ATOM   8173  O  O   . PHE C 1 191 ? 43.703  -55.293 29.680  1.00 25.33  ? 191 PHE C O   1 
ATOM   8174  C  CB  . PHE C 1 191 ? 46.308  -53.869 28.185  1.00 22.93  ? 191 PHE C CB  1 
ATOM   8175  C  CG  . PHE C 1 191 ? 45.548  -54.579 27.100  1.00 23.92  ? 191 PHE C CG  1 
ATOM   8176  C  CD1 . PHE C 1 191 ? 44.336  -54.058 26.645  1.00 24.71  ? 191 PHE C CD1 1 
ATOM   8177  C  CD2 . PHE C 1 191 ? 46.063  -55.724 26.509  1.00 25.13  ? 191 PHE C CD2 1 
ATOM   8178  C  CE1 . PHE C 1 191 ? 43.610  -54.717 25.587  1.00 23.98  ? 191 PHE C CE1 1 
ATOM   8179  C  CE2 . PHE C 1 191 ? 45.393  -56.425 25.461  1.00 23.63  ? 191 PHE C CE2 1 
ATOM   8180  C  CZ  . PHE C 1 191 ? 44.131  -55.914 25.003  1.00 23.20  ? 191 PHE C CZ  1 
ATOM   8181  N  N   . ILE C 1 192 ? 45.720  -55.954 30.356  1.00 27.94  ? 192 ILE C N   1 
ATOM   8182  C  CA  . ILE C 1 192 ? 45.193  -57.283 30.710  1.00 26.45  ? 192 ILE C CA  1 
ATOM   8183  C  C   . ILE C 1 192 ? 44.183  -57.160 31.845  1.00 25.43  ? 192 ILE C C   1 
ATOM   8184  O  O   . ILE C 1 192 ? 43.134  -57.819 31.841  1.00 28.64  ? 192 ILE C O   1 
ATOM   8185  C  CB  . ILE C 1 192 ? 46.361  -58.221 31.052  1.00 27.33  ? 192 ILE C CB  1 
ATOM   8186  C  CG1 . ILE C 1 192 ? 47.161  -58.469 29.779  1.00 26.62  ? 192 ILE C CG1 1 
ATOM   8187  C  CG2 . ILE C 1 192 ? 45.839  -59.518 31.733  1.00 27.25  ? 192 ILE C CG2 1 
ATOM   8188  C  CD1 . ILE C 1 192 ? 48.448  -59.235 30.022  1.00 32.26  ? 192 ILE C CD1 1 
ATOM   8189  N  N   . LYS C 1 193 ? 44.456  -56.296 32.817  1.00 25.23  ? 193 LYS C N   1 
ATOM   8190  C  CA  . LYS C 1 193 ? 43.477  -56.075 33.880  1.00 24.94  ? 193 LYS C CA  1 
ATOM   8191  C  C   . LYS C 1 193 ? 42.144  -55.623 33.311  1.00 25.47  ? 193 LYS C C   1 
ATOM   8192  O  O   . LYS C 1 193 ? 41.075  -56.032 33.806  1.00 24.65  ? 193 LYS C O   1 
ATOM   8193  C  CB  . LYS C 1 193 ? 43.999  -55.050 34.905  1.00 28.74  ? 193 LYS C CB  1 
ATOM   8194  C  CG  . LYS C 1 193 ? 45.206  -55.532 35.666  1.00 38.75  ? 193 LYS C CG  1 
ATOM   8195  C  CD  . LYS C 1 193 ? 45.316  -54.836 37.061  1.00 45.08  ? 193 LYS C CD  1 
ATOM   8196  C  CE  . LYS C 1 193 ? 46.780  -54.739 37.549  1.00 51.32  ? 193 LYS C CE  1 
ATOM   8197  N  NZ  . LYS C 1 193 ? 46.947  -55.076 39.009  1.00 54.19  ? 193 LYS C NZ  1 
ATOM   8198  N  N   . ALA C 1 194 ? 42.188  -54.698 32.320  1.00 25.74  ? 194 ALA C N   1 
ATOM   8199  C  CA  . ALA C 1 194 ? 40.960  -54.135 31.737  1.00 25.74  ? 194 ALA C CA  1 
ATOM   8200  C  C   . ALA C 1 194 ? 40.212  -55.176 30.929  1.00 24.37  ? 194 ALA C C   1 
ATOM   8201  O  O   . ALA C 1 194 ? 38.979  -55.229 30.967  1.00 25.88  ? 194 ALA C O   1 
ATOM   8202  C  CB  . ALA C 1 194 ? 41.294  -52.910 30.858  1.00 23.63  ? 194 ALA C CB  1 
ATOM   8203  N  N   . VAL C 1 195 ? 40.938  -56.011 30.191  1.00 22.94  ? 195 VAL C N   1 
ATOM   8204  C  CA  . VAL C 1 195 ? 40.320  -57.144 29.496  1.00 25.87  ? 195 VAL C CA  1 
ATOM   8205  C  C   . VAL C 1 195 ? 39.597  -58.031 30.490  1.00 25.20  ? 195 VAL C C   1 
ATOM   8206  O  O   . VAL C 1 195 ? 38.422  -58.387 30.302  1.00 23.94  ? 195 VAL C O   1 
ATOM   8207  C  CB  . VAL C 1 195 ? 41.377  -57.940 28.715  1.00 24.22  ? 195 VAL C CB  1 
ATOM   8208  C  CG1 . VAL C 1 195 ? 40.742  -59.250 28.215  1.00 23.71  ? 195 VAL C CG1 1 
ATOM   8209  C  CG2 . VAL C 1 195 ? 41.893  -57.061 27.542  1.00 24.61  ? 195 VAL C CG2 1 
ATOM   8210  N  N   . LYS C 1 196 ? 40.279  -58.382 31.560  1.00 26.25  ? 196 LYS C N   1 
ATOM   8211  C  CA  . LYS C 1 196 ? 39.702  -59.317 32.536  1.00 26.66  ? 196 LYS C CA  1 
ATOM   8212  C  C   . LYS C 1 196 ? 38.510  -58.674 33.234  1.00 26.55  ? 196 LYS C C   1 
ATOM   8213  O  O   . LYS C 1 196 ? 37.472  -59.298 33.403  1.00 24.76  ? 196 LYS C O   1 
ATOM   8214  C  CB  . LYS C 1 196 ? 40.755  -59.733 33.579  1.00 27.38  ? 196 LYS C CB  1 
ATOM   8215  C  CG  . LYS C 1 196 ? 42.004  -60.443 32.968  1.00 30.21  ? 196 LYS C CG  1 
ATOM   8216  C  CD  . LYS C 1 196 ? 42.664  -61.319 34.007  1.00 32.39  ? 196 LYS C CD  1 
ATOM   8217  C  CE  . LYS C 1 196 ? 42.985  -60.558 35.281  1.00 42.62  ? 196 LYS C CE  1 
ATOM   8218  N  NZ  . LYS C 1 196 ? 44.248  -61.029 36.044  1.00 44.51  ? 196 LYS C NZ  1 
ATOM   8219  N  N   . ASN C 1 197 ? 38.595  -57.392 33.537  1.00 23.96  ? 197 ASN C N   1 
ATOM   8220  C  CA  . ASN C 1 197 ? 37.448  -56.710 34.132  1.00 23.23  ? 197 ASN C CA  1 
ATOM   8221  C  C   . ASN C 1 197 ? 36.259  -56.629 33.159  1.00 24.20  ? 197 ASN C C   1 
ATOM   8222  O  O   . ASN C 1 197 ? 35.102  -56.747 33.582  1.00 23.78  ? 197 ASN C O   1 
ATOM   8223  C  CB  . ASN C 1 197 ? 37.884  -55.316 34.613  1.00 27.26  ? 197 ASN C CB  1 
ATOM   8224  C  CG  . ASN C 1 197 ? 38.586  -55.398 35.982  1.00 28.86  ? 197 ASN C CG  1 
ATOM   8225  O  OD1 . ASN C 1 197 ? 38.323  -56.319 36.767  1.00 29.53  ? 197 ASN C OD1 1 
ATOM   8226  N  ND2 . ASN C 1 197 ? 39.427  -54.410 36.286  1.00 32.30  ? 197 ASN C ND2 1 
ATOM   8227  N  N   . GLU C 1 198 ? 36.520  -56.402 31.863  1.00 22.65  ? 198 GLU C N   1 
ATOM   8228  C  CA  . GLU C 1 198 ? 35.410  -56.369 30.899  1.00 24.18  ? 198 GLU C CA  1 
ATOM   8229  C  C   . GLU C 1 198 ? 34.760  -57.745 30.776  1.00 24.45  ? 198 GLU C C   1 
ATOM   8230  O  O   . GLU C 1 198 ? 33.516  -57.867 30.722  1.00 24.16  ? 198 GLU C O   1 
ATOM   8231  C  CB  . GLU C 1 198 ? 35.867  -55.850 29.530  1.00 22.68  ? 198 GLU C CB  1 
ATOM   8232  C  CG  . GLU C 1 198 ? 34.747  -55.935 28.481  1.00 22.05  ? 198 GLU C CG  1 
ATOM   8233  C  CD  . GLU C 1 198 ? 35.096  -55.209 27.193  1.00 26.63  ? 198 GLU C CD  1 
ATOM   8234  O  OE1 . GLU C 1 198 ? 35.948  -54.272 27.303  1.00 26.01  ? 198 GLU C OE1 1 
ATOM   8235  O  OE2 . GLU C 1 198 ? 34.571  -55.583 26.125  1.00 27.60  ? 198 GLU C OE2 1 
ATOM   8236  N  N   . MET C 1 199 ? 35.581  -58.786 30.715  1.00 22.10  ? 199 MET C N   1 
ATOM   8237  C  CA  . MET C 1 199 ? 35.052  -60.151 30.741  1.00 22.30  ? 199 MET C CA  1 
ATOM   8238  C  C   . MET C 1 199 ? 34.180  -60.382 31.991  1.00 23.15  ? 199 MET C C   1 
ATOM   8239  O  O   . MET C 1 199 ? 33.051  -60.902 31.913  1.00 23.70  ? 199 MET C O   1 
ATOM   8240  C  CB  . MET C 1 199 ? 36.242  -61.105 30.732  1.00 27.99  ? 199 MET C CB  1 
ATOM   8241  C  CG  . MET C 1 199 ? 36.784  -61.205 29.269  1.00 28.34  ? 199 MET C CG  1 
ATOM   8242  S  SD  . MET C 1 199 ? 38.266  -62.203 29.311  1.00 28.29  ? 199 MET C SD  1 
ATOM   8243  C  CE  . MET C 1 199 ? 38.558  -62.296 27.517  1.00 28.06  ? 199 MET C CE  1 
ATOM   8244  N  N   . ARG C 1 200 ? 34.678  -59.968 33.168  1.00 22.00  ? 200 ARG C N   1 
ATOM   8245  C  CA  . ARG C 1 200 ? 33.902  -60.103 34.401  1.00 27.05  ? 200 ARG C CA  1 
ATOM   8246  C  C   . ARG C 1 200 ? 32.573  -59.346 34.314  1.00 27.51  ? 200 ARG C C   1 
ATOM   8247  O  O   . ARG C 1 200 ? 31.515  -59.910 34.611  1.00 26.40  ? 200 ARG C O   1 
ATOM   8248  C  CB  . ARG C 1 200 ? 34.691  -59.564 35.594  1.00 23.88  ? 200 ARG C CB  1 
ATOM   8249  C  CG  . ARG C 1 200 ? 35.852  -60.414 36.107  1.00 26.45  ? 200 ARG C CG  1 
ATOM   8250  C  CD  . ARG C 1 200 ? 36.566  -59.616 37.271  1.00 33.17  ? 200 ARG C CD  1 
ATOM   8251  N  NE  . ARG C 1 200 ? 35.675  -59.289 38.394  1.00 31.34  ? 200 ARG C NE  1 
ATOM   8252  C  CZ  . ARG C 1 200 ? 35.841  -58.247 39.210  1.00 34.47  ? 200 ARG C CZ  1 
ATOM   8253  N  NH1 . ARG C 1 200 ? 36.828  -57.371 39.027  1.00 34.12  ? 200 ARG C NH1 1 
ATOM   8254  N  NH2 . ARG C 1 200 ? 35.050  -58.121 40.289  1.00 32.34  ? 200 ARG C NH2 1 
ATOM   8255  N  N   . SER C 1 201 ? 32.597  -58.070 33.883  1.00 24.80  ? 201 SER C N   1 
ATOM   8256  C  CA  . SER C 1 201 ? 31.372  -57.271 34.019  1.00 22.69  ? 201 SER C CA  1 
ATOM   8257  C  C   . SER C 1 201 ? 30.298  -57.711 33.010  1.00 23.84  ? 201 SER C C   1 
ATOM   8258  O  O   . SER C 1 201 ? 29.106  -57.789 33.362  1.00 25.63  ? 201 SER C O   1 
ATOM   8259  C  CB  . SER C 1 201 ? 31.648  -55.750 33.867  1.00 21.54  ? 201 SER C CB  1 
ATOM   8260  O  OG  . SER C 1 201 ? 31.944  -55.483 32.550  1.00 25.12  ? 201 SER C OG  1 
ATOM   8261  N  N   . THR C 1 202 ? 30.703  -58.024 31.774  1.00 22.61  ? 202 THR C N   1 
ATOM   8262  C  CA  . THR C 1 202 ? 29.743  -58.449 30.763  1.00 21.10  ? 202 THR C CA  1 
ATOM   8263  C  C   . THR C 1 202 ? 29.192  -59.845 31.075  1.00 23.35  ? 202 THR C C   1 
ATOM   8264  O  O   . THR C 1 202 ? 27.996  -60.125 30.831  1.00 24.08  ? 202 THR C O   1 
ATOM   8265  C  CB  . THR C 1 202 ? 30.401  -58.415 29.356  1.00 22.86  ? 202 THR C CB  1 
ATOM   8266  O  OG1 . THR C 1 202 ? 31.592  -59.242 29.375  1.00 24.57  ? 202 THR C OG1 1 
ATOM   8267  C  CG2 . THR C 1 202 ? 30.788  -56.951 29.052  1.00 23.29  ? 202 THR C CG2 1 
ATOM   8268  N  N   . SER C 1 203 ? 30.045  -60.764 31.569  1.00 21.16  ? 203 SER C N   1 
ATOM   8269  C  CA  . SER C 1 203 ? 29.527  -62.051 31.993  1.00 22.81  ? 203 SER C CA  1 
ATOM   8270  C  C   . SER C 1 203 ? 28.604  -61.915 33.191  1.00 26.52  ? 203 SER C C   1 
ATOM   8271  O  O   . SER C 1 203 ? 27.531  -62.541 33.233  1.00 24.37  ? 203 SER C O   1 
ATOM   8272  C  CB  . SER C 1 203 ? 30.690  -62.980 32.340  1.00 25.80  ? 203 SER C CB  1 
ATOM   8273  O  OG  . SER C 1 203 ? 30.191  -64.278 32.689  1.00 26.33  ? 203 SER C OG  1 
ATOM   8274  N  N   . ARG C 1 204 ? 29.006  -61.094 34.174  1.00 22.89  ? 204 ARG C N   1 
ATOM   8275  C  CA  . ARG C 1 204 ? 28.199  -60.926 35.382  1.00 26.61  ? 204 ARG C CA  1 
ATOM   8276  C  C   . ARG C 1 204 ? 26.851  -60.267 35.076  1.00 27.56  ? 204 ARG C C   1 
ATOM   8277  O  O   . ARG C 1 204 ? 25.814  -60.699 35.624  1.00 26.83  ? 204 ARG C O   1 
ATOM   8278  C  CB  . ARG C 1 204 ? 28.981  -60.147 36.445  1.00 28.44  ? 204 ARG C CB  1 
ATOM   8279  C  CG  . ARG C 1 204 ? 28.615  -60.373 37.875  1.00 28.71  ? 204 ARG C CG  1 
ATOM   8280  C  CD  . ARG C 1 204 ? 28.553  -61.891 38.132  1.00 29.05  ? 204 ARG C CD  1 
ATOM   8281  N  NE  . ARG C 1 204 ? 28.993  -62.238 39.449  1.00 36.87  ? 204 ARG C NE  1 
ATOM   8282  C  CZ  . ARG C 1 204 ? 29.035  -63.498 39.876  1.00 45.01  ? 204 ARG C CZ  1 
ATOM   8283  N  NH1 . ARG C 1 204 ? 28.784  -64.512 39.056  1.00 38.83  ? 204 ARG C NH1 1 
ATOM   8284  N  NH2 . ARG C 1 204 ? 29.285  -63.741 41.165  1.00 40.68  ? 204 ARG C NH2 1 
ATOM   8285  N  N   . TRP C 1 205 ? 26.831  -59.248 34.192  1.00 24.69  ? 205 TRP C N   1 
ATOM   8286  C  CA  . TRP C 1 205 ? 25.536  -58.691 33.813  1.00 24.36  ? 205 TRP C CA  1 
ATOM   8287  C  C   . TRP C 1 205 ? 24.631  -59.769 33.191  1.00 25.15  ? 205 TRP C C   1 
ATOM   8288  O  O   . TRP C 1 205 ? 23.444  -59.879 33.541  1.00 25.43  ? 205 TRP C O   1 
ATOM   8289  C  CB  . TRP C 1 205 ? 25.712  -57.503 32.874  1.00 23.47  ? 205 TRP C CB  1 
ATOM   8290  C  CG  . TRP C 1 205 ? 24.354  -57.045 32.445  1.00 27.08  ? 205 TRP C CG  1 
ATOM   8291  C  CD1 . TRP C 1 205 ? 23.811  -57.109 31.194  1.00 24.58  ? 205 TRP C CD1 1 
ATOM   8292  C  CD2 . TRP C 1 205 ? 23.339  -56.512 33.299  1.00 23.15  ? 205 TRP C CD2 1 
ATOM   8293  N  NE1 . TRP C 1 205 ? 22.512  -56.663 31.211  1.00 22.86  ? 205 TRP C NE1 1 
ATOM   8294  C  CE2 . TRP C 1 205 ? 22.196  -56.289 32.496  1.00 23.27  ? 205 TRP C CE2 1 
ATOM   8295  C  CE3 . TRP C 1 205 ? 23.291  -56.175 34.668  1.00 24.54  ? 205 TRP C CE3 1 
ATOM   8296  C  CZ2 . TRP C 1 205 ? 21.014  -55.725 33.010  1.00 25.03  ? 205 TRP C CZ2 1 
ATOM   8297  C  CZ3 . TRP C 1 205 ? 22.122  -55.621 35.182  1.00 29.04  ? 205 TRP C CZ3 1 
ATOM   8298  C  CH2 . TRP C 1 205 ? 20.995  -55.391 34.350  1.00 27.02  ? 205 TRP C CH2 1 
ATOM   8299  N  N   . ALA C 1 206 ? 25.170  -60.617 32.329  1.00 21.92  ? 206 ALA C N   1 
ATOM   8300  C  CA  . ALA C 1 206 ? 24.340  -61.753 31.865  1.00 24.40  ? 206 ALA C CA  1 
ATOM   8301  C  C   . ALA C 1 206 ? 23.882  -62.634 33.022  1.00 24.62  ? 206 ALA C C   1 
ATOM   8302  O  O   . ALA C 1 206 ? 22.712  -63.032 33.076  1.00 25.41  ? 206 ALA C O   1 
ATOM   8303  C  CB  . ALA C 1 206 ? 25.073  -62.593 30.819  1.00 23.52  ? 206 ALA C CB  1 
ATOM   8304  N  N   . ASP C 1 207 ? 24.767  -62.935 33.961  1.00 26.38  ? 207 ASP C N   1 
ATOM   8305  C  CA  . ASP C 1 207 ? 24.344  -63.751 35.115  1.00 27.01  ? 207 ASP C CA  1 
ATOM   8306  C  C   . ASP C 1 207 ? 23.160  -63.116 35.846  1.00 27.32  ? 207 ASP C C   1 
ATOM   8307  O  O   . ASP C 1 207 ? 22.214  -63.805 36.251  1.00 28.06  ? 207 ASP C O   1 
ATOM   8308  C  CB  . ASP C 1 207 ? 25.479  -63.923 36.137  1.00 30.94  ? 207 ASP C CB  1 
ATOM   8309  C  CG  . ASP C 1 207 ? 26.617  -64.800 35.648  1.00 31.63  ? 207 ASP C CG  1 
ATOM   8310  O  OD1 . ASP C 1 207 ? 26.423  -65.656 34.741  1.00 30.71  ? 207 ASP C OD1 1 
ATOM   8311  O  OD2 . ASP C 1 207 ? 27.723  -64.630 36.219  1.00 31.37  ? 207 ASP C OD2 1 
ATOM   8312  N  N   . ILE C 1 208 ? 23.209  -61.797 36.033  1.00 24.14  ? 208 ILE C N   1 
ATOM   8313  C  CA  . ILE C 1 208 ? 22.130  -61.116 36.724  1.00 26.02  ? 208 ILE C CA  1 
ATOM   8314  C  C   . ILE C 1 208 ? 20.829  -61.249 35.932  1.00 24.59  ? 208 ILE C C   1 
ATOM   8315  O  O   . ILE C 1 208 ? 19.770  -61.501 36.511  1.00 26.40  ? 208 ILE C O   1 
ATOM   8316  C  CB  . ILE C 1 208 ? 22.522  -59.646 36.947  1.00 25.63  ? 208 ILE C CB  1 
ATOM   8317  C  CG1 . ILE C 1 208 ? 23.677  -59.553 37.975  1.00 28.30  ? 208 ILE C CG1 1 
ATOM   8318  C  CG2 . ILE C 1 208 ? 21.350  -58.855 37.350  1.00 23.79  ? 208 ILE C CG2 1 
ATOM   8319  C  CD1 . ILE C 1 208 ? 24.445  -58.233 37.927  1.00 30.23  ? 208 ILE C CD1 1 
ATOM   8320  N  N   . CYS C 1 209 ? 20.908  -61.086 34.609  1.00 25.95  ? 209 CYS C N   1 
ATOM   8321  C  CA  . CYS C 1 209 ? 19.731  -61.172 33.738  1.00 23.44  ? 209 CYS C CA  1 
ATOM   8322  C  C   . CYS C 1 209 ? 19.111  -62.557 33.818  1.00 24.99  ? 209 CYS C C   1 
ATOM   8323  O  O   . CYS C 1 209 ? 17.870  -62.705 33.826  1.00 25.71  ? 209 CYS C O   1 
ATOM   8324  C  CB  . CYS C 1 209 ? 20.106  -60.857 32.290  1.00 24.37  ? 209 CYS C CB  1 
ATOM   8325  S  SG  . CYS C 1 209 ? 20.477  -59.094 32.092  1.00 26.65  ? 209 CYS C SG  1 
ATOM   8326  N  N   . ALA C 1 210 ? 19.967  -63.572 33.919  1.00 27.27  ? 210 ALA C N   1 
ATOM   8327  C  CA  . ALA C 1 210 ? 19.485  -64.960 33.974  1.00 28.69  ? 210 ALA C CA  1 
ATOM   8328  C  C   . ALA C 1 210 ? 18.776  -65.274 35.289  1.00 28.20  ? 210 ALA C C   1 
ATOM   8329  O  O   . ALA C 1 210 ? 17.949  -66.198 35.330  1.00 30.91  ? 210 ALA C O   1 
ATOM   8330  C  CB  . ALA C 1 210 ? 20.644  -65.940 33.727  1.00 28.08  ? 210 ALA C CB  1 
ATOM   8331  N  N   . LEU C 1 211 ? 19.029  -64.501 36.358  1.00 28.92  ? 211 LEU C N   1 
ATOM   8332  C  CA  . LEU C 1 211 ? 18.237  -64.656 37.577  1.00 28.13  ? 211 LEU C CA  1 
ATOM   8333  C  C   . LEU C 1 211 ? 16.788  -64.217 37.373  1.00 29.53  ? 211 LEU C C   1 
ATOM   8334  O  O   . LEU C 1 211 ? 15.928  -64.586 38.176  1.00 29.43  ? 211 LEU C O   1 
ATOM   8335  C  CB  . LEU C 1 211 ? 18.841  -63.858 38.738  1.00 27.14  ? 211 LEU C CB  1 
ATOM   8336  C  CG  . LEU C 1 211 ? 20.227  -64.310 39.214  1.00 30.48  ? 211 LEU C CG  1 
ATOM   8337  C  CD1 . LEU C 1 211 ? 20.717  -63.333 40.294  1.00 30.70  ? 211 LEU C CD1 1 
ATOM   8338  C  CD2 . LEU C 1 211 ? 20.112  -65.722 39.856  1.00 31.50  ? 211 LEU C CD2 1 
ATOM   8339  N  N   . ASN C 1 212 ? 16.513  -63.405 36.329  1.00 28.90  ? 212 ASN C N   1 
ATOM   8340  C  CA  . ASN C 1 212 ? 15.152  -62.941 36.071  1.00 26.76  ? 212 ASN C CA  1 
ATOM   8341  C  C   . ASN C 1 212 ? 14.258  -63.996 35.454  1.00 30.14  ? 212 ASN C C   1 
ATOM   8342  O  O   . ASN C 1 212 ? 13.069  -63.731 35.204  1.00 29.47  ? 212 ASN C O   1 
ATOM   8343  C  CB  . ASN C 1 212 ? 15.165  -61.698 35.178  1.00 25.77  ? 212 ASN C CB  1 
ATOM   8344  C  CG  . ASN C 1 212 ? 14.286  -60.624 35.754  1.00 30.40  ? 212 ASN C CG  1 
ATOM   8345  O  OD1 . ASN C 1 212 ? 14.030  -60.625 36.982  1.00 29.57  ? 212 ASN C OD1 1 
ATOM   8346  N  ND2 . ASN C 1 212 ? 13.777  -59.735 34.893  1.00 25.93  ? 212 ASN C ND2 1 
ATOM   8347  N  N   . LYS C 1 213 ? 14.777  -65.199 35.239  1.00 31.21  ? 213 LYS C N   1 
ATOM   8348  C  CA  . LYS C 1 213 ? 13.967  -66.288 34.714  1.00 30.68  ? 213 LYS C CA  1 
ATOM   8349  C  C   . LYS C 1 213 ? 12.887  -66.774 35.674  1.00 34.46  ? 213 LYS C C   1 
ATOM   8350  O  O   . LYS C 1 213 ? 11.889  -67.332 35.206  1.00 34.98  ? 213 LYS C O   1 
ATOM   8351  C  CB  . LYS C 1 213 ? 14.878  -67.430 34.327  1.00 27.93  ? 213 LYS C CB  1 
ATOM   8352  C  CG  . LYS C 1 213 ? 15.867  -67.127 33.237  1.00 30.82  ? 213 LYS C CG  1 
ATOM   8353  C  CD  . LYS C 1 213 ? 16.669  -68.413 32.869  1.00 30.13  ? 213 LYS C CD  1 
ATOM   8354  C  CE  . LYS C 1 213 ? 17.851  -68.031 31.946  1.00 27.98  ? 213 LYS C CE  1 
ATOM   8355  N  NZ  . LYS C 1 213 ? 18.538  -69.241 31.466  1.00 30.31  ? 213 LYS C NZ  1 
ATOM   8356  N  N   . VAL C 1 214 ? 13.035  -66.553 36.997  1.00 31.13  ? 214 VAL C N   1 
ATOM   8357  C  CA  . VAL C 1 214 ? 12.114  -67.135 37.968  1.00 37.87  ? 214 VAL C CA  1 
ATOM   8358  C  C   . VAL C 1 214 ? 10.819  -66.333 38.001  1.00 35.04  ? 214 VAL C C   1 
ATOM   8359  O  O   . VAL C 1 214 ? 10.775  -65.140 37.641  1.00 34.20  ? 214 VAL C O   1 
ATOM   8360  C  CB  . VAL C 1 214 ? 12.754  -67.169 39.358  1.00 38.76  ? 214 VAL C CB  1 
ATOM   8361  C  CG1 . VAL C 1 214 ? 14.003  -67.988 39.332  1.00 41.41  ? 214 VAL C CG1 1 
ATOM   8362  C  CG2 . VAL C 1 214 ? 13.032  -65.718 39.837  1.00 33.68  ? 214 VAL C CG2 1 
ATOM   8363  N  N   . LYS C 1 215 ? 9.751   -66.996 38.493  1.00 35.45  ? 215 LYS C N   1 
ATOM   8364  C  CA  . LYS C 1 215 ? 8.546   -66.284 38.888  1.00 36.15  ? 215 LYS C CA  1 
ATOM   8365  C  C   . LYS C 1 215 ? 8.528   -66.127 40.403  1.00 37.10  ? 215 LYS C C   1 
ATOM   8366  O  O   . LYS C 1 215 ? 8.677   -67.118 41.127  1.00 36.82  ? 215 LYS C O   1 
ATOM   8367  C  CB  . LYS C 1 215 ? 7.286   -67.023 38.443  1.00 38.89  ? 215 LYS C CB  1 
ATOM   8368  C  CG  . LYS C 1 215 ? 7.176   -67.266 36.940  1.00 37.01  ? 215 LYS C CG  1 
ATOM   8369  C  CD  . LYS C 1 215 ? 5.820   -67.942 36.624  1.00 39.12  ? 215 LYS C CD  1 
ATOM   8370  C  CE  . LYS C 1 215 ? 5.479   -67.780 35.134  1.00 42.25  ? 215 LYS C CE  1 
ATOM   8371  N  NZ  . LYS C 1 215 ? 4.353   -68.630 34.581  1.00 46.47  ? 215 LYS C NZ  1 
ATOM   8372  N  N   . PRO C 1 216 ? 8.308   -64.938 40.946  1.00 36.02  ? 216 PRO C N   1 
ATOM   8373  C  CA  . PRO C 1 216 ? 8.115   -63.659 40.274  1.00 35.34  ? 216 PRO C CA  1 
ATOM   8374  C  C   . PRO C 1 216 ? 9.471   -63.130 39.817  1.00 34.83  ? 216 PRO C C   1 
ATOM   8375  O  O   . PRO C 1 216 ? 10.514  -63.530 40.369  1.00 33.58  ? 216 PRO C O   1 
ATOM   8376  C  CB  . PRO C 1 216 ? 7.493   -62.803 41.372  1.00 36.49  ? 216 PRO C CB  1 
ATOM   8377  C  CG  . PRO C 1 216 ? 8.234   -63.272 42.615  1.00 37.71  ? 216 PRO C CG  1 
ATOM   8378  C  CD  . PRO C 1 216 ? 8.368   -64.776 42.411  1.00 37.31  ? 216 PRO C CD  1 
ATOM   8379  N  N   . ALA C 1 217 ? 9.503   -62.248 38.829  1.00 32.54  ? 217 ALA C N   1 
ATOM   8380  C  CA  . ALA C 1 217 ? 10.776  -61.699 38.378  1.00 32.06  ? 217 ALA C CA  1 
ATOM   8381  C  C   . ALA C 1 217 ? 11.332  -60.799 39.476  1.00 31.99  ? 217 ALA C C   1 
ATOM   8382  O  O   . ALA C 1 217 ? 10.617  -59.920 39.952  1.00 32.69  ? 217 ALA C O   1 
ATOM   8383  C  CB  . ALA C 1 217 ? 10.606  -60.889 37.092  1.00 31.95  ? 217 ALA C CB  1 
ATOM   8384  N  N   . PRO C 1 218 ? 12.604  -60.940 39.868  1.00 29.45  ? 218 PRO C N   1 
ATOM   8385  C  CA  . PRO C 1 218 ? 13.128  -60.030 40.905  1.00 31.94  ? 218 PRO C CA  1 
ATOM   8386  C  C   . PRO C 1 218 ? 13.430  -58.658 40.363  1.00 28.01  ? 218 PRO C C   1 
ATOM   8387  O  O   . PRO C 1 218 ? 13.562  -57.719 41.152  1.00 30.82  ? 218 PRO C O   1 
ATOM   8388  C  CB  . PRO C 1 218 ? 14.425  -60.706 41.364  1.00 33.69  ? 218 PRO C CB  1 
ATOM   8389  C  CG  . PRO C 1 218 ? 14.805  -61.610 40.166  1.00 30.18  ? 218 PRO C CG  1 
ATOM   8390  C  CD  . PRO C 1 218 ? 13.503  -62.079 39.625  1.00 29.66  ? 218 PRO C CD  1 
ATOM   8391  N  N   . LEU C 1 219 ? 13.604  -58.521 39.057  1.00 27.30  ? 219 LEU C N   1 
ATOM   8392  C  CA  . LEU C 1 219 ? 13.848  -57.230 38.427  1.00 30.86  ? 219 LEU C CA  1 
ATOM   8393  C  C   . LEU C 1 219 ? 12.827  -56.995 37.332  1.00 31.70  ? 219 LEU C C   1 
ATOM   8394  O  O   . LEU C 1 219 ? 12.418  -57.937 36.642  1.00 34.65  ? 219 LEU C O   1 
ATOM   8395  C  CB  . LEU C 1 219 ? 15.230  -57.156 37.825  1.00 30.53  ? 219 LEU C CB  1 
ATOM   8396  C  CG  . LEU C 1 219 ? 16.379  -57.211 38.819  1.00 34.43  ? 219 LEU C CG  1 
ATOM   8397  C  CD1 . LEU C 1 219 ? 17.716  -57.314 38.094  1.00 34.10  ? 219 LEU C CD1 1 
ATOM   8398  C  CD2 . LEU C 1 219 ? 16.264  -55.960 39.726  1.00 32.59  ? 219 LEU C CD2 1 
ATOM   8399  N  N   . ASP C 1 220 ? 12.389  -55.752 37.202  1.00 32.47  ? 220 ASP C N   1 
ATOM   8400  C  CA  . ASP C 1 220 ? 11.623  -55.276 36.064  1.00 32.50  ? 220 ASP C CA  1 
ATOM   8401  C  C   . ASP C 1 220 ? 12.534  -54.522 35.099  1.00 34.44  ? 220 ASP C C   1 
ATOM   8402  O  O   . ASP C 1 220 ? 13.590  -54.008 35.473  1.00 31.87  ? 220 ASP C O   1 
ATOM   8403  C  CB  . ASP C 1 220 ? 10.503  -54.380 36.549  1.00 34.32  ? 220 ASP C CB  1 
ATOM   8404  C  CG  . ASP C 1 220 ? 11.045  -53.147 37.205  1.00 36.70  ? 220 ASP C CG  1 
ATOM   8405  O  OD1 . ASP C 1 220 ? 11.485  -53.240 38.364  1.00 46.72  ? 220 ASP C OD1 1 
ATOM   8406  O  OD2 . ASP C 1 220 ? 11.229  -52.139 36.535  1.00 43.30  ? 220 ASP C OD2 1 
ATOM   8407  N  N   . GLU C 1 221 ? 12.103  -54.419 33.850  1.00 30.07  ? 221 GLU C N   1 
ATOM   8408  C  CA  . GLU C 1 221 ? 13.063  -53.898 32.886  1.00 33.01  ? 221 GLU C CA  1 
ATOM   8409  C  C   . GLU C 1 221 ? 13.305  -52.402 33.080  1.00 32.62  ? 221 GLU C C   1 
ATOM   8410  O  O   . GLU C 1 221 ? 14.417  -51.925 32.846  1.00 32.52  ? 221 GLU C O   1 
ATOM   8411  C  CB  . GLU C 1 221 ? 12.630  -54.213 31.462  1.00 31.72  ? 221 GLU C CB  1 
ATOM   8412  C  CG  . GLU C 1 221 ? 13.649  -53.703 30.421  1.00 33.40  ? 221 GLU C CG  1 
ATOM   8413  C  CD  . GLU C 1 221 ? 13.394  -54.296 29.048  1.00 34.44  ? 221 GLU C CD  1 
ATOM   8414  O  OE1 . GLU C 1 221 ? 12.174  -54.497 28.752  1.00 34.93  ? 221 GLU C OE1 1 
ATOM   8415  O  OE2 . GLU C 1 221 ? 14.391  -54.482 28.284  1.00 32.74  ? 221 GLU C OE2 1 
ATOM   8416  N  N   . LYS C 1 222 ? 12.323  -51.648 33.555  1.00 31.52  ? 222 LYS C N   1 
ATOM   8417  C  CA  . LYS C 1 222 ? 12.616  -50.217 33.672  1.00 34.27  ? 222 LYS C CA  1 
ATOM   8418  C  C   . LYS C 1 222 ? 13.637  -49.973 34.786  1.00 33.04  ? 222 LYS C C   1 
ATOM   8419  O  O   . LYS C 1 222 ? 14.529  -49.134 34.622  1.00 34.56  ? 222 LYS C O   1 
ATOM   8420  C  CB  . LYS C 1 222 ? 11.321  -49.464 33.873  1.00 38.30  ? 222 LYS C CB  1 
ATOM   8421  C  CG  . LYS C 1 222 ? 10.621  -49.829 35.084  1.00 44.71  ? 222 LYS C CG  1 
ATOM   8422  C  CD  . LYS C 1 222 ? 9.222   -49.269 35.112  1.00 53.07  ? 222 LYS C CD  1 
ATOM   8423  C  CE  . LYS C 1 222 ? 8.241   -50.440 34.954  1.00 54.87  ? 222 LYS C CE  1 
ATOM   8424  N  NZ  . LYS C 1 222 ? 8.468   -51.563 35.950  1.00 55.44  ? 222 LYS C NZ  1 
ATOM   8425  N  N   . THR C 1 223 ? 13.632  -50.821 35.829  1.00 33.41  ? 223 THR C N   1 
ATOM   8426  C  CA  . THR C 1 223 ? 14.695  -50.817 36.847  1.00 32.98  ? 223 THR C CA  1 
ATOM   8427  C  C   . THR C 1 223 ? 16.047  -51.248 36.267  1.00 30.44  ? 223 THR C C   1 
ATOM   8428  O  O   . THR C 1 223 ? 17.088  -50.626 36.519  1.00 30.95  ? 223 THR C O   1 
ATOM   8429  C  CB  . THR C 1 223 ? 14.313  -51.733 38.034  1.00 36.05  ? 223 THR C CB  1 
ATOM   8430  O  OG1 . THR C 1 223 ? 13.114  -51.255 38.656  1.00 33.51  ? 223 THR C OG1 1 
ATOM   8431  C  CG2 . THR C 1 223 ? 15.414  -51.732 39.104  1.00 30.71  ? 223 THR C CG2 1 
ATOM   8432  N  N   . MET C 1 224 ? 16.065  -52.326 35.481  1.00 27.80  ? 224 MET C N   1 
ATOM   8433  C  CA  . MET C 1 224 ? 17.310  -52.671 34.843  1.00 29.05  ? 224 MET C CA  1 
ATOM   8434  C  C   . MET C 1 224 ? 17.858  -51.627 33.854  1.00 28.55  ? 224 MET C C   1 
ATOM   8435  O  O   . MET C 1 224 ? 19.056  -51.697 33.551  1.00 28.03  ? 224 MET C O   1 
ATOM   8436  C  CB  . MET C 1 224 ? 17.228  -54.065 34.206  1.00 31.46  ? 224 MET C CB  1 
ATOM   8437  C  CG  . MET C 1 224 ? 16.176  -55.008 34.788  1.00 32.79  ? 224 MET C CG  1 
ATOM   8438  S  SD  . MET C 1 224 ? 15.879  -56.511 33.818  1.00 39.95  ? 224 MET C SD  1 
ATOM   8439  C  CE  . MET C 1 224 ? 17.529  -57.203 33.746  1.00 39.58  ? 224 MET C CE  1 
ATOM   8440  N  N   . TYR C 1 225 ? 17.072  -50.640 33.400  1.00 28.11  ? 225 TYR C N   1 
ATOM   8441  C  CA  . TYR C 1 225 ? 17.684  -49.601 32.571  1.00 32.02  ? 225 TYR C CA  1 
ATOM   8442  C  C   . TYR C 1 225 ? 18.769  -48.825 33.352  1.00 30.61  ? 225 TYR C C   1 
ATOM   8443  O  O   . TYR C 1 225 ? 19.753  -48.375 32.752  1.00 30.63  ? 225 TYR C O   1 
ATOM   8444  C  CB  . TYR C 1 225 ? 16.620  -48.636 31.987  1.00 33.72  ? 225 TYR C CB  1 
ATOM   8445  C  CG  . TYR C 1 225 ? 15.799  -49.269 30.855  1.00 30.36  ? 225 TYR C CG  1 
ATOM   8446  C  CD1 . TYR C 1 225 ? 16.397  -50.137 29.947  1.00 33.38  ? 225 TYR C CD1 1 
ATOM   8447  C  CD2 . TYR C 1 225 ? 14.424  -49.023 30.719  1.00 36.67  ? 225 TYR C CD2 1 
ATOM   8448  C  CE1 . TYR C 1 225 ? 15.664  -50.750 28.925  1.00 35.62  ? 225 TYR C CE1 1 
ATOM   8449  C  CE2 . TYR C 1 225 ? 13.673  -49.624 29.700  1.00 37.80  ? 225 TYR C CE2 1 
ATOM   8450  C  CZ  . TYR C 1 225 ? 14.299  -50.501 28.807  1.00 40.27  ? 225 TYR C CZ  1 
ATOM   8451  O  OH  . TYR C 1 225 ? 13.596  -51.110 27.769  1.00 40.77  ? 225 TYR C OH  1 
ATOM   8452  N  N   . SER C 1 226 ? 18.644  -48.684 34.684  1.00 28.11  ? 226 SER C N   1 
ATOM   8453  C  CA  . SER C 1 226 ? 19.695  -47.997 35.430  1.00 27.62  ? 226 SER C CA  1 
ATOM   8454  C  C   . SER C 1 226 ? 20.863  -48.901 35.809  1.00 30.17  ? 226 SER C C   1 
ATOM   8455  O  O   . SER C 1 226 ? 21.860  -48.433 36.384  1.00 28.49  ? 226 SER C O   1 
ATOM   8456  C  CB  . SER C 1 226 ? 19.076  -47.331 36.663  1.00 32.45  ? 226 SER C CB  1 
ATOM   8457  O  OG  . SER C 1 226 ? 18.186  -46.304 36.208  1.00 33.13  ? 226 SER C OG  1 
ATOM   8458  N  N   . LEU C 1 227 ? 20.766  -50.187 35.506  1.00 27.20  ? 227 LEU C N   1 
ATOM   8459  C  CA  . LEU C 1 227 ? 21.784  -51.154 35.860  1.00 26.75  ? 227 LEU C CA  1 
ATOM   8460  C  C   . LEU C 1 227 ? 22.534  -51.657 34.643  1.00 26.83  ? 227 LEU C C   1 
ATOM   8461  O  O   . LEU C 1 227 ? 23.772  -51.671 34.655  1.00 24.53  ? 227 LEU C O   1 
ATOM   8462  C  CB  . LEU C 1 227 ? 21.121  -52.321 36.598  1.00 24.49  ? 227 LEU C CB  1 
ATOM   8463  C  CG  . LEU C 1 227 ? 20.209  -52.014 37.812  1.00 28.35  ? 227 LEU C CG  1 
ATOM   8464  C  CD1 . LEU C 1 227 ? 19.455  -53.248 38.376  1.00 30.41  ? 227 LEU C CD1 1 
ATOM   8465  C  CD2 . LEU C 1 227 ? 21.016  -51.272 38.893  1.00 28.91  ? 227 LEU C CD2 1 
ATOM   8466  N  N   . TYR C 1 228 ? 21.821  -51.978 33.545  1.00 25.11  ? 228 TYR C N   1 
ATOM   8467  C  CA  . TYR C 1 228 ? 22.518  -52.414 32.335  1.00 27.62  ? 228 TYR C CA  1 
ATOM   8468  C  C   . TYR C 1 228 ? 23.335  -51.265 31.756  1.00 25.87  ? 228 TYR C C   1 
ATOM   8469  O  O   . TYR C 1 228 ? 24.319  -51.507 31.041  1.00 25.85  ? 228 TYR C O   1 
ATOM   8470  C  CB  . TYR C 1 228 ? 21.550  -52.902 31.248  1.00 23.82  ? 228 TYR C CB  1 
ATOM   8471  C  CG  . TYR C 1 228 ? 21.135  -51.847 30.254  1.00 25.35  ? 228 TYR C CG  1 
ATOM   8472  C  CD1 . TYR C 1 228 ? 20.493  -50.666 30.629  1.00 29.20  ? 228 TYR C CD1 1 
ATOM   8473  C  CD2 . TYR C 1 228 ? 21.431  -52.037 28.908  1.00 27.76  ? 228 TYR C CD2 1 
ATOM   8474  C  CE1 . TYR C 1 228 ? 20.129  -49.697 29.650  1.00 25.63  ? 228 TYR C CE1 1 
ATOM   8475  C  CE2 . TYR C 1 228 ? 21.064  -51.097 27.932  1.00 30.51  ? 228 TYR C CE2 1 
ATOM   8476  C  CZ  . TYR C 1 228 ? 20.389  -49.927 28.331  1.00 30.55  ? 228 TYR C CZ  1 
ATOM   8477  O  OH  . TYR C 1 228 ? 19.998  -48.944 27.410  1.00 29.89  ? 228 TYR C OH  1 
ATOM   8478  N  N   . VAL C 1 229 ? 23.029  -50.025 32.164  1.00 22.09  ? 229 VAL C N   1 
ATOM   8479  C  CA  . VAL C 1 229 ? 23.715  -48.917 31.508  1.00 23.75  ? 229 VAL C CA  1 
ATOM   8480  C  C   . VAL C 1 229 ? 25.189  -48.875 31.949  1.00 23.76  ? 229 VAL C C   1 
ATOM   8481  O  O   . VAL C 1 229 ? 26.031  -48.342 31.239  1.00 23.46  ? 229 VAL C O   1 
ATOM   8482  C  CB  . VAL C 1 229 ? 22.941  -47.615 31.799  1.00 24.62  ? 229 VAL C CB  1 
ATOM   8483  C  CG1 . VAL C 1 229 ? 22.963  -47.298 33.284  1.00 26.91  ? 229 VAL C CG1 1 
ATOM   8484  C  CG2 . VAL C 1 229 ? 23.528  -46.482 30.980  1.00 24.47  ? 229 VAL C CG2 1 
ATOM   8485  N  N   . LEU C 1 230 ? 25.540  -49.414 33.123  1.00 22.75  ? 230 LEU C N   1 
ATOM   8486  C  CA  . LEU C 1 230 ? 26.923  -49.263 33.586  1.00 24.21  ? 230 LEU C CA  1 
ATOM   8487  C  C   . LEU C 1 230 ? 27.935  -49.923 32.636  1.00 24.31  ? 230 LEU C C   1 
ATOM   8488  O  O   . LEU C 1 230 ? 29.022  -49.369 32.384  1.00 24.78  ? 230 LEU C O   1 
ATOM   8489  C  CB  . LEU C 1 230 ? 27.039  -49.808 35.025  1.00 24.04  ? 230 LEU C CB  1 
ATOM   8490  C  CG  . LEU C 1 230 ? 26.157  -49.018 36.014  1.00 23.55  ? 230 LEU C CG  1 
ATOM   8491  C  CD1 . LEU C 1 230 ? 26.105  -49.537 37.421  1.00 30.34  ? 230 LEU C CD1 1 
ATOM   8492  C  CD2 . LEU C 1 230 ? 26.554  -47.482 36.022  1.00 25.79  ? 230 LEU C CD2 1 
ATOM   8493  N  N   . CYS C 1 231 ? 27.625  -51.099 32.112  1.00 22.12  ? 231 CYS C N   1 
ATOM   8494  C  CA  . CYS C 1 231 ? 28.527  -51.711 31.138  1.00 24.22  ? 231 CYS C CA  1 
ATOM   8495  C  C   . CYS C 1 231 ? 28.623  -50.899 29.841  1.00 24.17  ? 231 CYS C C   1 
ATOM   8496  O  O   . CYS C 1 231 ? 29.565  -51.103 29.066  1.00 25.85  ? 231 CYS C O   1 
ATOM   8497  C  CB  . CYS C 1 231 ? 28.093  -53.118 30.768  1.00 26.75  ? 231 CYS C CB  1 
ATOM   8498  S  SG  . CYS C 1 231 ? 28.459  -54.325 32.072  1.00 28.12  ? 231 CYS C SG  1 
ATOM   8499  N  N   . THR C 1 232 ? 27.635  -50.049 29.542  1.00 22.78  ? 232 THR C N   1 
ATOM   8500  C  CA  . THR C 1 232 ? 27.707  -49.215 28.354  1.00 22.61  ? 232 THR C CA  1 
ATOM   8501  C  C   . THR C 1 232 ? 28.517  -47.970 28.581  1.00 22.33  ? 232 THR C C   1 
ATOM   8502  O  O   . THR C 1 232 ? 28.822  -47.274 27.603  1.00 23.81  ? 232 THR C O   1 
ATOM   8503  C  CB  . THR C 1 232 ? 26.317  -48.774 27.890  1.00 23.00  ? 232 THR C CB  1 
ATOM   8504  O  OG1 . THR C 1 232 ? 25.859  -47.703 28.762  1.00 24.17  ? 232 THR C OG1 1 
ATOM   8505  C  CG2 . THR C 1 232 ? 25.355  -49.922 27.920  1.00 26.10  ? 232 THR C CG2 1 
ATOM   8506  N  N   . LEU C 1 233 ? 28.865  -47.695 29.837  1.00 22.67  ? 233 LEU C N   1 
ATOM   8507  C  CA  . LEU C 1 233 ? 29.707  -46.544 30.170  1.00 23.84  ? 233 LEU C CA  1 
ATOM   8508  C  C   . LEU C 1 233 ? 31.185  -46.957 30.197  1.00 25.07  ? 233 LEU C C   1 
ATOM   8509  O  O   . LEU C 1 233 ? 31.995  -46.432 29.418  1.00 23.68  ? 233 LEU C O   1 
ATOM   8510  C  CB  . LEU C 1 233 ? 29.277  -45.932 31.512  1.00 22.19  ? 233 LEU C CB  1 
ATOM   8511  C  CG  . LEU C 1 233 ? 27.770  -45.631 31.639  1.00 24.56  ? 233 LEU C CG  1 
ATOM   8512  C  CD1 . LEU C 1 233 ? 27.512  -44.932 32.975  1.00 23.78  ? 233 LEU C CD1 1 
ATOM   8513  C  CD2 . LEU C 1 233 ? 27.299  -44.628 30.513  1.00 22.42  ? 233 LEU C CD2 1 
ATOM   8514  N  N   . SER C 1 234 ? 31.541  -47.955 31.022  1.00 25.15  ? 234 SER C N   1 
ATOM   8515  C  CA  . SER C 1 234 ? 32.931  -48.423 31.043  1.00 24.06  ? 234 SER C CA  1 
ATOM   8516  C  C   . SER C 1 234 ? 32.974  -49.893 31.491  1.00 23.67  ? 234 SER C C   1 
ATOM   8517  O  O   . SER C 1 234 ? 33.387  -50.207 32.587  1.00 25.05  ? 234 SER C O   1 
ATOM   8518  C  CB  . SER C 1 234 ? 33.812  -47.567 31.954  1.00 26.02  ? 234 SER C CB  1 
ATOM   8519  O  OG  . SER C 1 234 ? 35.201  -47.896 31.783  1.00 26.28  ? 234 SER C OG  1 
ATOM   8520  N  N   . LYS C 1 235 ? 32.667  -50.815 30.577  1.00 22.50  ? 235 LYS C N   1 
ATOM   8521  C  CA  . LYS C 1 235 ? 32.622  -52.234 30.985  1.00 23.60  ? 235 LYS C CA  1 
ATOM   8522  C  C   . LYS C 1 235 ? 34.012  -52.757 31.393  1.00 24.57  ? 235 LYS C C   1 
ATOM   8523  O  O   . LYS C 1 235 ? 34.108  -53.704 32.192  1.00 24.81  ? 235 LYS C O   1 
ATOM   8524  C  CB  . LYS C 1 235 ? 32.019  -53.076 29.856  1.00 21.97  ? 235 LYS C CB  1 
ATOM   8525  C  CG  . LYS C 1 235 ? 32.644  -52.825 28.469  1.00 22.36  ? 235 LYS C CG  1 
ATOM   8526  C  CD  . LYS C 1 235 ? 31.926  -53.616 27.354  1.00 23.30  ? 235 LYS C CD  1 
ATOM   8527  C  CE  . LYS C 1 235 ? 31.998  -53.126 25.921  1.00 30.26  ? 235 LYS C CE  1 
ATOM   8528  N  NZ  . LYS C 1 235 ? 33.446  -53.000 25.623  1.00 28.63  ? 235 LYS C NZ  1 
ATOM   8529  N  N   . SER C 1 236 ? 35.096  -52.162 30.864  1.00 22.64  ? 236 SER C N   1 
ATOM   8530  C  CA  . SER C 1 236 ? 36.443  -52.620 31.259  1.00 24.79  ? 236 SER C CA  1 
ATOM   8531  C  C   . SER C 1 236 ? 36.960  -52.043 32.581  1.00 25.52  ? 236 SER C C   1 
ATOM   8532  O  O   . SER C 1 236 ? 38.108  -52.324 32.955  1.00 25.71  ? 236 SER C O   1 
ATOM   8533  C  CB  . SER C 1 236 ? 37.458  -52.348 30.123  1.00 22.77  ? 236 SER C CB  1 
ATOM   8534  O  OG  . SER C 1 236 ? 37.693  -50.942 29.925  1.00 26.93  ? 236 SER C OG  1 
ATOM   8535  N  N   . SER C 1 237 ? 36.201  -51.221 33.304  1.00 24.78  ? 237 SER C N   1 
ATOM   8536  C  CA  . SER C 1 237 ? 36.737  -50.676 34.536  1.00 25.53  ? 237 SER C CA  1 
ATOM   8537  C  C   . SER C 1 237 ? 36.533  -51.591 35.735  1.00 27.44  ? 237 SER C C   1 
ATOM   8538  O  O   . SER C 1 237 ? 35.585  -52.382 35.815  1.00 25.83  ? 237 SER C O   1 
ATOM   8539  C  CB  . SER C 1 237 ? 36.093  -49.333 34.857  1.00 29.39  ? 237 SER C CB  1 
ATOM   8540  O  OG  . SER C 1 237 ? 34.731  -49.611 35.127  1.00 31.02  ? 237 SER C OG  1 
ATOM   8541  N  N   . GLN C 1 238 ? 37.422  -51.434 36.715  1.00 29.94  ? 238 GLN C N   1 
ATOM   8542  C  CA  . GLN C 1 238 ? 37.247  -52.174 37.965  1.00 29.09  ? 238 GLN C CA  1 
ATOM   8543  C  C   . GLN C 1 238 ? 35.917  -51.833 38.620  1.00 28.56  ? 238 GLN C C   1 
ATOM   8544  O  O   . GLN C 1 238 ? 35.251  -52.710 39.177  1.00 28.28  ? 238 GLN C O   1 
ATOM   8545  C  CB  . GLN C 1 238 ? 38.397  -51.864 38.928  1.00 30.38  ? 238 GLN C CB  1 
ATOM   8546  C  CG  . GLN C 1 238 ? 38.424  -52.682 40.240  1.00 35.52  ? 238 GLN C CG  1 
ATOM   8547  C  CD  . GLN C 1 238 ? 38.979  -54.027 40.027  1.00 41.59  ? 238 GLN C CD  1 
ATOM   8548  O  OE1 . GLN C 1 238 ? 39.874  -54.194 39.191  1.00 41.41  ? 238 GLN C OE1 1 
ATOM   8549  N  NE2 . GLN C 1 238 ? 38.509  -55.023 40.817  1.00 42.26  ? 238 GLN C NE2 1 
ATOM   8550  N  N   . TRP C 1 239 ? 35.521  -50.553 38.585  1.00 28.58  ? 239 TRP C N   1 
ATOM   8551  C  CA  . TRP C 1 239 ? 34.305  -50.157 39.283  1.00 29.97  ? 239 TRP C CA  1 
ATOM   8552  C  C   . TRP C 1 239 ? 33.072  -50.831 38.695  1.00 27.81  ? 239 TRP C C   1 
ATOM   8553  O  O   . TRP C 1 239 ? 32.110  -51.139 39.434  1.00 29.35  ? 239 TRP C O   1 
ATOM   8554  C  CB  . TRP C 1 239 ? 34.149  -48.615 39.301  1.00 29.42  ? 239 TRP C CB  1 
ATOM   8555  C  CG  . TRP C 1 239 ? 33.883  -47.917 37.994  1.00 27.00  ? 239 TRP C CG  1 
ATOM   8556  C  CD1 . TRP C 1 239 ? 34.775  -47.176 37.221  1.00 31.14  ? 239 TRP C CD1 1 
ATOM   8557  C  CD2 . TRP C 1 239 ? 32.628  -47.829 37.325  1.00 29.63  ? 239 TRP C CD2 1 
ATOM   8558  N  NE1 . TRP C 1 239 ? 34.136  -46.666 36.113  1.00 30.83  ? 239 TRP C NE1 1 
ATOM   8559  C  CE2 . TRP C 1 239 ? 32.823  -47.068 36.151  1.00 34.28  ? 239 TRP C CE2 1 
ATOM   8560  C  CE3 . TRP C 1 239 ? 31.348  -48.336 37.598  1.00 31.54  ? 239 TRP C CE3 1 
ATOM   8561  C  CZ2 . TRP C 1 239 ? 31.785  -46.823 35.249  1.00 30.44  ? 239 TRP C CZ2 1 
ATOM   8562  C  CZ3 . TRP C 1 239 ? 30.311  -48.080 36.692  1.00 29.86  ? 239 TRP C CZ3 1 
ATOM   8563  C  CH2 . TRP C 1 239 ? 30.534  -47.335 35.558  1.00 29.21  ? 239 TRP C CH2 1 
ATOM   8564  N  N   . CYS C 1 240 ? 33.052  -51.017 37.375  1.00 28.11  ? 240 CYS C N   1 
ATOM   8565  C  CA  . CYS C 1 240 ? 31.901  -51.632 36.735  1.00 27.34  ? 240 CYS C CA  1 
ATOM   8566  C  C   . CYS C 1 240 ? 31.816  -53.098 37.092  1.00 28.38  ? 240 CYS C C   1 
ATOM   8567  O  O   . CYS C 1 240 ? 30.753  -53.592 37.525  1.00 28.04  ? 240 CYS C O   1 
ATOM   8568  C  CB  . CYS C 1 240 ? 31.990  -51.489 35.220  1.00 29.25  ? 240 CYS C CB  1 
ATOM   8569  S  SG  . CYS C 1 240 ? 30.404  -51.954 34.463  1.00 30.14  ? 240 CYS C SG  1 
ATOM   8570  N  N   . ALA C 1 241 ? 32.946  -53.801 36.932  1.00 26.14  ? 241 ALA C N   1 
ATOM   8571  C  CA  . ALA C 1 241 ? 33.025  -55.214 37.301  1.00 25.53  ? 241 ALA C CA  1 
ATOM   8572  C  C   . ALA C 1 241 ? 32.710  -55.442 38.795  1.00 27.66  ? 241 ALA C C   1 
ATOM   8573  O  O   . ALA C 1 241 ? 31.963  -56.350 39.152  1.00 29.75  ? 241 ALA C O   1 
ATOM   8574  C  CB  . ALA C 1 241 ? 34.415  -55.760 36.947  1.00 26.88  ? 241 ALA C CB  1 
ATOM   8575  N  N   . ASP C 1 242 ? 33.285  -54.648 39.690  1.00 26.05  ? 242 ASP C N   1 
ATOM   8576  C  CA  . ASP C 1 242 ? 33.012  -54.852 41.113  1.00 29.35  ? 242 ASP C CA  1 
ATOM   8577  C  C   . ASP C 1 242 ? 31.542  -54.555 41.424  1.00 31.62  ? 242 ASP C C   1 
ATOM   8578  O  O   . ASP C 1 242 ? 30.917  -55.225 42.245  1.00 32.04  ? 242 ASP C O   1 
ATOM   8579  C  CB  . ASP C 1 242 ? 33.922  -53.940 41.928  1.00 30.44  ? 242 ASP C CB  1 
ATOM   8580  C  CG  . ASP C 1 242 ? 35.375  -54.445 41.986  1.00 36.78  ? 242 ASP C CG  1 
ATOM   8581  O  OD1 . ASP C 1 242 ? 35.667  -55.581 41.544  1.00 34.22  ? 242 ASP C OD1 1 
ATOM   8582  O  OD2 . ASP C 1 242 ? 36.224  -53.672 42.475  1.00 33.61  ? 242 ASP C OD2 1 
ATOM   8583  N  N   . PHE C 1 243 ? 30.962  -53.550 40.771  1.00 28.39  ? 243 PHE C N   1 
ATOM   8584  C  CA  . PHE C 1 243 ? 29.550  -53.290 41.022  1.00 28.35  ? 243 PHE C CA  1 
ATOM   8585  C  C   . PHE C 1 243 ? 28.658  -54.432 40.527  1.00 27.98  ? 243 PHE C C   1 
ATOM   8586  O  O   . PHE C 1 243 ? 27.738  -54.846 41.239  1.00 27.31  ? 243 PHE C O   1 
ATOM   8587  C  CB  . PHE C 1 243 ? 29.135  -51.968 40.390  1.00 28.56  ? 243 PHE C CB  1 
ATOM   8588  C  CG  . PHE C 1 243 ? 27.752  -51.591 40.743  1.00 28.27  ? 243 PHE C CG  1 
ATOM   8589  C  CD1 . PHE C 1 243 ? 27.456  -51.212 42.036  1.00 29.33  ? 243 PHE C CD1 1 
ATOM   8590  C  CD2 . PHE C 1 243 ? 26.728  -51.712 39.822  1.00 33.49  ? 243 PHE C CD2 1 
ATOM   8591  C  CE1 . PHE C 1 243 ? 26.144  -50.900 42.415  1.00 34.03  ? 243 PHE C CE1 1 
ATOM   8592  C  CE2 . PHE C 1 243 ? 25.416  -51.364 40.175  1.00 30.46  ? 243 PHE C CE2 1 
ATOM   8593  C  CZ  . PHE C 1 243 ? 25.130  -50.962 41.495  1.00 29.51  ? 243 PHE C CZ  1 
ATOM   8594  N  N   . MET C 1 244 ? 28.924  -54.972 39.324  1.00 26.91  ? 244 MET C N   1 
ATOM   8595  C  CA  . MET C 1 244 ? 28.150  -56.115 38.859  1.00 28.56  ? 244 MET C CA  1 
ATOM   8596  C  C   . MET C 1 244 ? 28.206  -57.263 39.876  1.00 28.09  ? 244 MET C C   1 
ATOM   8597  O  O   . MET C 1 244 ? 27.172  -57.859 40.203  1.00 27.57  ? 244 MET C O   1 
ATOM   8598  C  CB  . MET C 1 244 ? 28.657  -56.551 37.470  1.00 25.95  ? 244 MET C CB  1 
ATOM   8599  C  CG  . MET C 1 244 ? 28.444  -55.433 36.407  1.00 24.36  ? 244 MET C CG  1 
ATOM   8600  S  SD  . MET C 1 244 ? 26.678  -55.168 36.140  1.00 31.13  ? 244 MET C SD  1 
ATOM   8601  C  CE  . MET C 1 244 ? 26.483  -53.479 36.642  1.00 32.00  ? 244 MET C CE  1 
ATOM   8602  N  N   . ASP C 1 245 ? 29.387  -57.559 40.465  1.00 27.60  ? 245 ASP C N   1 
ATOM   8603  C  CA  . ASP C 1 245 ? 29.428  -58.599 41.505  1.00 29.14  ? 245 ASP C CA  1 
ATOM   8604  C  C   . ASP C 1 245 ? 28.518  -58.264 42.697  1.00 29.71  ? 245 ASP C C   1 
ATOM   8605  O  O   . ASP C 1 245 ? 27.779  -59.127 43.181  1.00 31.35  ? 245 ASP C O   1 
ATOM   8606  C  CB  . ASP C 1 245 ? 30.858  -58.821 42.000  1.00 30.63  ? 245 ASP C CB  1 
ATOM   8607  C  CG  . ASP C 1 245 ? 31.674  -59.650 41.051  1.00 33.15  ? 245 ASP C CG  1 
ATOM   8608  O  OD1 . ASP C 1 245 ? 31.074  -60.322 40.163  1.00 35.34  ? 245 ASP C OD1 1 
ATOM   8609  O  OD2 . ASP C 1 245 ? 32.932  -59.628 41.202  1.00 33.05  ? 245 ASP C OD2 1 
ATOM   8610  N  N   . GLU C 1 246 ? 28.553  -57.008 43.172  1.00 27.10  ? 246 GLU C N   1 
ATOM   8611  C  CA  . GLU C 1 246 ? 27.737  -56.586 44.309  1.00 29.74  ? 246 GLU C CA  1 
ATOM   8612  C  C   . GLU C 1 246 ? 26.254  -56.769 43.999  1.00 27.98  ? 246 GLU C C   1 
ATOM   8613  O  O   . GLU C 1 246 ? 25.476  -57.222 44.844  1.00 29.05  ? 246 GLU C O   1 
ATOM   8614  C  CB  . GLU C 1 246 ? 27.967  -55.101 44.598  1.00 34.00  ? 246 GLU C CB  1 
ATOM   8615  C  CG  . GLU C 1 246 ? 29.059  -54.702 45.494  1.00 37.27  ? 246 GLU C CG  1 
ATOM   8616  C  CD  . GLU C 1 246 ? 28.827  -53.255 45.963  1.00 45.84  ? 246 GLU C CD  1 
ATOM   8617  O  OE1 . GLU C 1 246 ? 28.148  -53.074 47.012  1.00 51.78  ? 246 GLU C OE1 1 
ATOM   8618  O  OE2 . GLU C 1 246 ? 29.212  -52.313 45.234  1.00 42.82  ? 246 GLU C OE2 1 
ATOM   8619  N  N   . LEU C 1 247 ? 25.859  -56.364 42.777  1.00 30.25  ? 247 LEU C N   1 
ATOM   8620  C  CA  . LEU C 1 247 ? 24.471  -56.373 42.337  1.00 30.86  ? 247 LEU C CA  1 
ATOM   8621  C  C   . LEU C 1 247 ? 23.965  -57.792 42.201  1.00 32.52  ? 247 LEU C C   1 
ATOM   8622  O  O   . LEU C 1 247 ? 22.838  -58.095 42.610  1.00 30.82  ? 247 LEU C O   1 
ATOM   8623  C  CB  . LEU C 1 247 ? 24.341  -55.623 40.988  1.00 28.71  ? 247 LEU C CB  1 
ATOM   8624  C  CG  . LEU C 1 247 ? 22.937  -55.510 40.367  1.00 30.75  ? 247 LEU C CG  1 
ATOM   8625  C  CD1 . LEU C 1 247 ? 21.960  -54.812 41.287  1.00 31.15  ? 247 LEU C CD1 1 
ATOM   8626  C  CD2 . LEU C 1 247 ? 23.010  -54.796 38.956  1.00 28.74  ? 247 LEU C CD2 1 
ATOM   8627  N  N   . TYR C 1 248 ? 24.794  -58.670 41.638  1.00 28.79  ? 248 TYR C N   1 
ATOM   8628  C  CA  . TYR C 1 248 ? 24.446  -60.088 41.574  1.00 29.73  ? 248 TYR C CA  1 
ATOM   8629  C  C   . TYR C 1 248 ? 24.120  -60.622 42.971  1.00 31.36  ? 248 TYR C C   1 
ATOM   8630  O  O   . TYR C 1 248 ? 23.143  -61.359 43.145  1.00 33.30  ? 248 TYR C O   1 
ATOM   8631  C  CB  . TYR C 1 248 ? 25.605  -60.880 40.956  1.00 29.46  ? 248 TYR C CB  1 
ATOM   8632  C  CG  . TYR C 1 248 ? 25.442  -62.372 40.863  1.00 30.67  ? 248 TYR C CG  1 
ATOM   8633  C  CD1 . TYR C 1 248 ? 24.626  -62.940 39.884  1.00 31.41  ? 248 TYR C CD1 1 
ATOM   8634  C  CD2 . TYR C 1 248 ? 26.053  -63.220 41.786  1.00 34.02  ? 248 TYR C CD2 1 
ATOM   8635  C  CE1 . TYR C 1 248 ? 24.465  -64.350 39.773  1.00 28.60  ? 248 TYR C CE1 1 
ATOM   8636  C  CE2 . TYR C 1 248 ? 25.885  -64.609 41.694  1.00 40.27  ? 248 TYR C CE2 1 
ATOM   8637  C  CZ  . TYR C 1 248 ? 25.105  -65.146 40.666  1.00 38.99  ? 248 TYR C CZ  1 
ATOM   8638  O  OH  . TYR C 1 248 ? 24.931  -66.514 40.574  1.00 39.64  ? 248 TYR C OH  1 
ATOM   8639  N  N   . GLU C 1 249 ? 24.927  -60.278 43.977  1.00 29.39  ? 249 GLU C N   1 
ATOM   8640  C  CA  . GLU C 1 249 ? 24.608  -60.757 45.339  1.00 30.73  ? 249 GLU C CA  1 
ATOM   8641  C  C   . GLU C 1 249 ? 23.247  -60.269 45.806  1.00 30.55  ? 249 GLU C C   1 
ATOM   8642  O  O   . GLU C 1 249 ? 22.471  -61.039 46.415  1.00 32.78  ? 249 GLU C O   1 
ATOM   8643  C  CB  . GLU C 1 249 ? 25.663  -60.332 46.341  1.00 33.46  ? 249 GLU C CB  1 
ATOM   8644  C  CG  . GLU C 1 249 ? 27.030  -60.927 46.098  1.00 38.25  ? 249 GLU C CG  1 
ATOM   8645  C  CD  . GLU C 1 249 ? 27.050  -62.462 46.099  1.00 41.84  ? 249 GLU C CD  1 
ATOM   8646  O  OE1 . GLU C 1 249 ? 26.419  -63.114 46.985  1.00 41.96  ? 249 GLU C OE1 1 
ATOM   8647  O  OE2 . GLU C 1 249 ? 27.722  -63.011 45.203  1.00 40.26  ? 249 GLU C OE2 1 
ATOM   8648  N  N   . GLU C 1 250 ? 22.914  -59.007 45.494  1.00 32.43  ? 250 GLU C N   1 
ATOM   8649  C  CA  . GLU C 1 250 ? 21.620  -58.495 45.923  1.00 33.11  ? 250 GLU C CA  1 
ATOM   8650  C  C   . GLU C 1 250 ? 20.503  -59.198 45.182  1.00 33.14  ? 250 GLU C C   1 
ATOM   8651  O  O   . GLU C 1 250 ? 19.506  -59.602 45.792  1.00 34.39  ? 250 GLU C O   1 
ATOM   8652  C  CB  . GLU C 1 250 ? 21.505  -56.975 45.738  1.00 33.49  ? 250 GLU C CB  1 
ATOM   8653  C  CG  . GLU C 1 250 ? 20.125  -56.541 46.193  1.00 35.10  ? 250 GLU C CG  1 
ATOM   8654  C  CD  . GLU C 1 250 ? 19.911  -55.048 46.365  1.00 40.67  ? 250 GLU C CD  1 
ATOM   8655  O  OE1 . GLU C 1 250 ? 20.874  -54.251 46.168  1.00 38.24  ? 250 GLU C OE1 1 
ATOM   8656  O  OE2 . GLU C 1 250 ? 18.743  -54.673 46.711  1.00 39.51  ? 250 GLU C OE2 1 
ATOM   8657  N  N   . VAL C 1 251 ? 20.681  -59.429 43.880  1.00 34.32  ? 251 VAL C N   1 
ATOM   8658  C  CA  . VAL C 1 251 ? 19.603  -60.036 43.107  1.00 29.69  ? 251 VAL C CA  1 
ATOM   8659  C  C   . VAL C 1 251 ? 19.429  -61.503 43.479  1.00 32.99  ? 251 VAL C C   1 
ATOM   8660  O  O   . VAL C 1 251 ? 18.292  -62.002 43.521  1.00 32.56  ? 251 VAL C O   1 
ATOM   8661  C  CB  . VAL C 1 251 ? 19.838  -59.869 41.608  1.00 27.22  ? 251 VAL C CB  1 
ATOM   8662  C  CG1 . VAL C 1 251 ? 18.678  -60.513 40.869  1.00 29.46  ? 251 VAL C CG1 1 
ATOM   8663  C  CG2 . VAL C 1 251 ? 19.921  -58.331 41.275  1.00 29.11  ? 251 VAL C CG2 1 
ATOM   8664  N  N   . LYS C 1 252 ? 20.543  -62.220 43.742  1.00 29.56  ? 252 LYS C N   1 
ATOM   8665  C  CA  . LYS C 1 252 ? 20.453  -63.578 44.273  1.00 36.81  ? 252 LYS C CA  1 
ATOM   8666  C  C   . LYS C 1 252 ? 19.590  -63.595 45.534  1.00 35.51  ? 252 LYS C C   1 
ATOM   8667  O  O   . LYS C 1 252 ? 18.778  -64.509 45.752  1.00 38.03  ? 252 LYS C O   1 
ATOM   8668  C  CB  . LYS C 1 252 ? 21.862  -64.100 44.620  1.00 39.86  ? 252 LYS C CB  1 
ATOM   8669  C  CG  . LYS C 1 252 ? 22.555  -64.870 43.522  1.00 43.29  ? 252 LYS C CG  1 
ATOM   8670  C  CD  . LYS C 1 252 ? 22.577  -66.382 43.806  1.00 49.28  ? 252 LYS C CD  1 
ATOM   8671  C  CE  . LYS C 1 252 ? 22.666  -67.148 42.462  1.00 49.71  ? 252 LYS C CE  1 
ATOM   8672  N  NZ  . LYS C 1 252 ? 23.312  -68.495 42.518  1.00 54.75  ? 252 LYS C NZ  1 
ATOM   8673  N  N   . ASP C 1 253 ? 19.776  -62.594 46.402  1.00 36.10  ? 253 ASP C N   1 
ATOM   8674  C  CA  . ASP C 1 253 ? 19.024  -62.563 47.664  1.00 35.98  ? 253 ASP C CA  1 
ATOM   8675  C  C   . ASP C 1 253 ? 17.534  -62.320 47.434  1.00 37.66  ? 253 ASP C C   1 
ATOM   8676  O  O   . ASP C 1 253 ? 16.683  -62.956 48.078  1.00 36.11  ? 253 ASP C O   1 
ATOM   8677  C  CB  . ASP C 1 253 ? 19.612  -61.497 48.577  1.00 36.92  ? 253 ASP C CB  1 
ATOM   8678  C  CG  . ASP C 1 253 ? 18.889  -61.399 49.923  1.00 47.62  ? 253 ASP C CG  1 
ATOM   8679  O  OD1 . ASP C 1 253 ? 18.836  -62.382 50.714  1.00 41.32  ? 253 ASP C OD1 1 
ATOM   8680  O  OD2 . ASP C 1 253 ? 18.374  -60.290 50.184  1.00 48.64  ? 253 ASP C OD2 1 
ATOM   8681  N  N   . ARG C 1 254 ? 17.204  -61.398 46.524  1.00 34.24  ? 254 ARG C N   1 
ATOM   8682  C  CA  . ARG C 1 254 ? 15.820  -61.225 46.100  1.00 34.08  ? 254 ARG C CA  1 
ATOM   8683  C  C   . ARG C 1 254 ? 15.217  -62.557 45.655  1.00 34.24  ? 254 ARG C C   1 
ATOM   8684  O  O   . ARG C 1 254 ? 14.116  -62.925 46.080  1.00 36.57  ? 254 ARG C O   1 
ATOM   8685  C  CB  . ARG C 1 254 ? 15.748  -60.177 44.987  1.00 31.09  ? 254 ARG C CB  1 
ATOM   8686  C  CG  . ARG C 1 254 ? 16.012  -58.787 45.486  1.00 33.38  ? 254 ARG C CG  1 
ATOM   8687  C  CD  . ARG C 1 254 ? 16.167  -57.804 44.318  1.00 34.18  ? 254 ARG C CD  1 
ATOM   8688  N  NE  . ARG C 1 254 ? 14.884  -57.459 43.700  1.00 33.27  ? 254 ARG C NE  1 
ATOM   8689  C  CZ  . ARG C 1 254 ? 14.090  -56.494 44.159  1.00 35.05  ? 254 ARG C CZ  1 
ATOM   8690  N  NH1 . ARG C 1 254 ? 14.405  -55.807 45.239  1.00 37.12  ? 254 ARG C NH1 1 
ATOM   8691  N  NH2 . ARG C 1 254 ? 12.926  -56.257 43.550  1.00 34.50  ? 254 ARG C NH2 1 
ATOM   8692  N  N   . VAL C 1 255 ? 15.932  -63.308 44.825  1.00 33.17  ? 255 VAL C N   1 
ATOM   8693  C  CA  . VAL C 1 255 ? 15.373  -64.587 44.395  1.00 35.00  ? 255 VAL C CA  1 
ATOM   8694  C  C   . VAL C 1 255 ? 15.240  -65.531 45.586  1.00 36.13  ? 255 VAL C C   1 
ATOM   8695  O  O   . VAL C 1 255 ? 14.202  -66.199 45.767  1.00 39.57  ? 255 VAL C O   1 
ATOM   8696  C  CB  . VAL C 1 255 ? 16.217  -65.207 43.280  1.00 30.04  ? 255 VAL C CB  1 
ATOM   8697  C  CG1 . VAL C 1 255 ? 15.741  -66.631 42.998  1.00 34.33  ? 255 VAL C CG1 1 
ATOM   8698  C  CG2 . VAL C 1 255 ? 16.153  -64.302 41.991  1.00 29.19  ? 255 VAL C CG2 1 
ATOM   8699  N  N   . ALA C 1 256 ? 16.263  -65.585 46.443  1.00 35.22  ? 256 ALA C N   1 
ATOM   8700  C  CA  . ALA C 1 256 ? 16.170  -66.426 47.648  1.00 36.95  ? 256 ALA C CA  1 
ATOM   8701  C  C   . ALA C 1 256 ? 14.946  -66.104 48.494  1.00 36.47  ? 256 ALA C C   1 
ATOM   8702  O  O   . ALA C 1 256 ? 14.400  -66.987 49.159  1.00 40.31  ? 256 ALA C O   1 
ATOM   8703  C  CB  . ALA C 1 256 ? 17.416  -66.282 48.527  1.00 41.82  ? 256 ALA C CB  1 
ATOM   8704  N  N   . ARG C 1 257 ? 14.511  -64.855 48.506  1.00 37.07  ? 257 ARG C N   1 
ATOM   8705  C  CA  . ARG C 1 257 ? 13.455  -64.429 49.397  1.00 39.43  ? 257 ARG C CA  1 
ATOM   8706  C  C   . ARG C 1 257 ? 12.087  -64.371 48.706  1.00 44.35  ? 257 ARG C C   1 
ATOM   8707  O  O   . ARG C 1 257 ? 11.089  -64.009 49.360  1.00 42.43  ? 257 ARG C O   1 
ATOM   8708  C  CB  . ARG C 1 257 ? 13.846  -63.074 49.995  1.00 41.27  ? 257 ARG C CB  1 
ATOM   8709  C  CG  . ARG C 1 257 ? 14.780  -63.209 51.168  1.00 48.66  ? 257 ARG C CG  1 
ATOM   8710  C  CD  . ARG C 1 257 ? 14.945  -61.866 51.849  1.00 50.90  ? 257 ARG C CD  1 
ATOM   8711  N  NE  . ARG C 1 257 ? 15.648  -60.941 50.985  1.00 45.69  ? 257 ARG C NE  1 
ATOM   8712  C  CZ  . ARG C 1 257 ? 15.383  -59.644 50.921  1.00 51.55  ? 257 ARG C CZ  1 
ATOM   8713  N  NH1 . ARG C 1 257 ? 14.352  -59.127 51.554  1.00 53.39  ? 257 ARG C NH1 1 
ATOM   8714  N  NH2 . ARG C 1 257 ? 16.130  -58.861 50.141  1.00 48.56  ? 257 ARG C NH2 1 
ATOM   8715  N  N   . GLY C 1 258 ? 12.029  -64.704 47.409  1.00 39.63  ? 258 GLY C N   1 
ATOM   8716  C  CA  . GLY C 1 258 ? 10.788  -64.705 46.641  1.00 37.49  ? 258 GLY C CA  1 
ATOM   8717  C  C   . GLY C 1 258 ? 10.297  -63.307 46.344  1.00 39.78  ? 258 GLY C C   1 
ATOM   8718  O  O   . GLY C 1 258 ? 9.087   -63.084 46.197  1.00 37.39  ? 258 GLY C O   1 
ATOM   8719  N  N   . ILE C 1 259 ? 11.220  -62.362 46.250  1.00 36.43  ? 259 ILE C N   1 
ATOM   8720  C  CA  . ILE C 1 259 ? 10.881  -60.948 46.129  1.00 38.43  ? 259 ILE C CA  1 
ATOM   8721  C  C   . ILE C 1 259 ? 10.577  -60.627 44.674  1.00 35.84  ? 259 ILE C C   1 
ATOM   8722  O  O   . ILE C 1 259 ? 11.354  -60.966 43.769  1.00 34.47  ? 259 ILE C O   1 
ATOM   8723  C  CB  . ILE C 1 259 ? 12.050  -60.078 46.608  1.00 41.29  ? 259 ILE C CB  1 
ATOM   8724  C  CG1 . ILE C 1 259 ? 12.204  -60.099 48.129  1.00 41.59  ? 259 ILE C CG1 1 
ATOM   8725  C  CG2 . ILE C 1 259 ? 11.837  -58.652 46.094  1.00 40.59  ? 259 ILE C CG2 1 
ATOM   8726  C  CD1 . ILE C 1 259 ? 10.953  -60.121 48.858  1.00 45.34  ? 259 ILE C CD1 1 
ATOM   8727  N  N   . ALA C 1 260 ? 9.489   -59.899 44.444  1.00 38.16  ? 260 ALA C N   1 
ATOM   8728  C  CA  . ALA C 1 260 ? 9.081   -59.511 43.099  1.00 36.56  ? 260 ALA C CA  1 
ATOM   8729  C  C   . ALA C 1 260 ? 9.297   -58.017 42.891  1.00 34.14  ? 260 ALA C C   1 
ATOM   8730  O  O   . ALA C 1 260 ? 8.977   -57.198 43.778  1.00 34.00  ? 260 ALA C O   1 
ATOM   8731  C  CB  . ALA C 1 260 ? 7.613   -59.826 42.870  1.00 37.03  ? 260 ALA C CB  1 
ATOM   8732  N  N   . ALA C 1 261 ? 9.830   -57.681 41.722  1.00 31.57  ? 261 ALA C N   1 
ATOM   8733  C  CA  . ALA C 1 261 ? 9.844   -56.297 41.256  1.00 33.75  ? 261 ALA C CA  1 
ATOM   8734  C  C   . ALA C 1 261 ? 8.430   -55.741 41.193  1.00 33.43  ? 261 ALA C C   1 
ATOM   8735  O  O   . ALA C 1 261 ? 8.182   -54.590 41.578  1.00 37.30  ? 261 ALA C O   1 
ATOM   8736  C  CB  . ALA C 1 261 ? 10.528  -56.221 39.883  1.00 34.72  ? 261 ALA C CB  1 
ATOM   8737  N  N   . VAL C 1 262 ? 7.479   -56.555 40.753  1.00 35.53  ? 262 VAL C N   1 
ATOM   8738  C  CA  . VAL C 1 262 ? 6.098   -56.093 40.613  1.00 39.17  ? 262 VAL C CA  1 
ATOM   8739  C  C   . VAL C 1 262 ? 5.191   -56.968 41.471  1.00 39.01  ? 262 VAL C C   1 
ATOM   8740  O  O   . VAL C 1 262 ? 4.957   -58.134 41.127  1.00 35.37  ? 262 VAL C O   1 
ATOM   8741  C  CB  . VAL C 1 262 ? 5.672   -56.128 39.145  1.00 38.68  ? 262 VAL C CB  1 
ATOM   8742  C  CG1 . VAL C 1 262 ? 4.208   -55.887 39.022  1.00 43.30  ? 262 VAL C CG1 1 
ATOM   8743  C  CG2 . VAL C 1 262 ? 6.483   -55.135 38.336  1.00 43.86  ? 262 VAL C CG2 1 
ATOM   8744  N  N   . PRO C 1 263 ? 4.656   -56.446 42.575  1.00 42.66  ? 263 PRO C N   1 
ATOM   8745  C  CA  . PRO C 1 263 ? 4.030   -57.332 43.577  1.00 42.65  ? 263 PRO C CA  1 
ATOM   8746  C  C   . PRO C 1 263 ? 2.816   -58.096 43.055  1.00 45.80  ? 263 PRO C C   1 
ATOM   8747  O  O   . PRO C 1 263 ? 2.520   -59.187 43.555  1.00 48.18  ? 263 PRO C O   1 
ATOM   8748  C  CB  . PRO C 1 263 ? 3.652   -56.369 44.722  1.00 46.65  ? 263 PRO C CB  1 
ATOM   8749  C  CG  . PRO C 1 263 ? 3.683   -54.980 44.128  1.00 44.58  ? 263 PRO C CG  1 
ATOM   8750  C  CD  . PRO C 1 263 ? 4.639   -55.021 42.965  1.00 42.47  ? 263 PRO C CD  1 
ATOM   8751  N  N   . ASN C 1 264 ? 2.111   -57.573 42.049  1.00 45.97  ? 264 ASN C N   1 
ATOM   8752  C  CA  . ASN C 1 264 ? 0.938   -58.257 41.513  1.00 46.92  ? 264 ASN C CA  1 
ATOM   8753  C  C   . ASN C 1 264 ? 1.216   -58.931 40.174  1.00 45.16  ? 264 ASN C C   1 
ATOM   8754  O  O   . ASN C 1 264 ? 0.301   -59.078 39.356  1.00 44.15  ? 264 ASN C O   1 
ATOM   8755  C  CB  . ASN C 1 264 ? -0.235  -57.282 41.388  1.00 49.68  ? 264 ASN C CB  1 
ATOM   8756  C  CG  . ASN C 1 264 ? 0.027   -56.168 40.400  1.00 49.59  ? 264 ASN C CG  1 
ATOM   8757  O  OD1 . ASN C 1 264 ? 1.174   -55.787 40.145  1.00 51.41  ? 264 ASN C OD1 1 
ATOM   8758  N  ND2 . ASN C 1 264 ? -1.044  -55.654 39.811  1.00 49.42  ? 264 ASN C ND2 1 
ATOM   8759  N  N   . GLU C 1 265 ? 2.461   -59.330 39.922  1.00 42.28  ? 265 GLU C N   1 
ATOM   8760  C  CA  . GLU C 1 265 ? 2.826   -59.950 38.644  1.00 39.29  ? 265 GLU C CA  1 
ATOM   8761  C  C   . GLU C 1 265 ? 1.866   -61.071 38.259  1.00 38.20  ? 265 GLU C C   1 
ATOM   8762  O  O   . GLU C 1 265 ? 1.673   -62.038 39.011  1.00 39.73  ? 265 GLU C O   1 
ATOM   8763  C  CB  . GLU C 1 265 ? 4.263   -60.499 38.714  1.00 38.82  ? 265 GLU C CB  1 
ATOM   8764  C  CG  . GLU C 1 265 ? 4.675   -61.329 37.492  1.00 34.58  ? 265 GLU C CG  1 
ATOM   8765  C  CD  . GLU C 1 265 ? 6.052   -61.949 37.639  1.00 36.45  ? 265 GLU C CD  1 
ATOM   8766  O  OE1 . GLU C 1 265 ? 6.955   -61.310 38.210  1.00 35.03  ? 265 GLU C OE1 1 
ATOM   8767  O  OE2 . GLU C 1 265 ? 6.243   -63.108 37.207  1.00 35.22  ? 265 GLU C OE2 1 
ATOM   8768  N  N   . ALA C 1 266 ? 1.298   -60.953 37.062  1.00 39.18  ? 266 ALA C N   1 
ATOM   8769  C  CA  . ALA C 1 266 ? 0.408   -61.958 36.496  1.00 42.29  ? 266 ALA C CA  1 
ATOM   8770  C  C   . ALA C 1 266 ? 0.798   -62.267 35.051  1.00 41.10  ? 266 ALA C C   1 
ATOM   8771  O  O   . ALA C 1 266 ? 0.522   -63.352 34.527  1.00 41.71  ? 266 ALA C O   1 
ATOM   8772  C  CB  . ALA C 1 266 ? -1.042  -61.467 36.554  1.00 43.62  ? 266 ALA C CB  1 
ATOM   8773  N  N   . ILE C 1 267 ? 1.412   -61.294 34.384  1.00 36.65  ? 267 ILE C N   1 
ATOM   8774  C  CA  . ILE C 1 267 ? 1.833   -61.426 32.991  1.00 35.23  ? 267 ILE C CA  1 
ATOM   8775  C  C   . ILE C 1 267 ? 3.289   -60.989 32.881  1.00 32.75  ? 267 ILE C C   1 
ATOM   8776  O  O   . ILE C 1 267 ? 3.704   -60.004 33.506  1.00 39.07  ? 267 ILE C O   1 
ATOM   8777  C  CB  . ILE C 1 267 ? 0.930   -60.608 32.042  1.00 41.59  ? 267 ILE C CB  1 
ATOM   8778  C  CG1 . ILE C 1 267 ? -0.538  -60.837 32.405  1.00 47.29  ? 267 ILE C CG1 1 
ATOM   8779  C  CG2 . ILE C 1 267 ? 1.262   -60.896 30.566  1.00 43.29  ? 267 ILE C CG2 1 
ATOM   8780  C  CD1 . ILE C 1 267 ? -1.104  -62.046 31.663  1.00 50.70  ? 267 ILE C CD1 1 
ATOM   8781  N  N   . ARG C 1 268 ? 4.057   -61.727 32.096  1.00 33.10  ? 268 ARG C N   1 
ATOM   8782  C  CA  . ARG C 1 268 ? 5.467   -61.435 31.891  1.00 33.93  ? 268 ARG C CA  1 
ATOM   8783  C  C   . ARG C 1 268 ? 5.669   -61.092 30.425  1.00 29.04  ? 268 ARG C C   1 
ATOM   8784  O  O   . ARG C 1 268 ? 5.333   -61.887 29.545  1.00 31.78  ? 268 ARG C O   1 
ATOM   8785  C  CB  . ARG C 1 268 ? 6.339   -62.624 32.325  1.00 33.53  ? 268 ARG C CB  1 
ATOM   8786  C  CG  . ARG C 1 268 ? 6.283   -62.952 33.837  1.00 33.41  ? 268 ARG C CG  1 
ATOM   8787  C  CD  . ARG C 1 268 ? 6.738   -64.390 34.108  1.00 31.43  ? 268 ARG C CD  1 
ATOM   8788  N  NE  . ARG C 1 268 ? 8.174   -64.580 33.865  1.00 32.55  ? 268 ARG C NE  1 
ATOM   8789  C  CZ  . ARG C 1 268 ? 9.139   -64.356 34.752  1.00 31.90  ? 268 ARG C CZ  1 
ATOM   8790  N  NH1 . ARG C 1 268 ? 8.877   -63.893 35.969  1.00 31.92  ? 268 ARG C NH1 1 
ATOM   8791  N  NH2 . ARG C 1 268 ? 10.402  -64.565 34.399  1.00 32.14  ? 268 ARG C NH2 1 
ATOM   8792  N  N   . LEU C 1 269 ? 6.236   -59.920 30.165  1.00 29.75  ? 269 LEU C N   1 
ATOM   8793  C  CA  . LEU C 1 269 ? 6.436   -59.419 28.822  1.00 30.93  ? 269 LEU C CA  1 
ATOM   8794  C  C   . LEU C 1 269 ? 7.926   -59.379 28.498  1.00 29.77  ? 269 LEU C C   1 
ATOM   8795  O  O   . LEU C 1 269 ? 8.776   -59.329 29.396  1.00 32.39  ? 269 LEU C O   1 
ATOM   8796  C  CB  . LEU C 1 269 ? 5.828   -58.023 28.665  1.00 31.07  ? 269 LEU C CB  1 
ATOM   8797  C  CG  . LEU C 1 269 ? 4.317   -57.976 28.978  1.00 32.03  ? 269 LEU C CG  1 
ATOM   8798  C  CD1 . LEU C 1 269 ? 3.850   -56.510 28.890  1.00 34.32  ? 269 LEU C CD1 1 
ATOM   8799  C  CD2 . LEU C 1 269 ? 3.549   -58.846 28.004  1.00 35.83  ? 269 LEU C CD2 1 
ATOM   8800  N  N   . MET C 1 270 ? 8.224   -59.490 27.209  1.00 30.33  ? 270 MET C N   1 
ATOM   8801  C  CA  . MET C 1 270 ? 9.543   -59.247 26.666  1.00 28.82  ? 270 MET C CA  1 
ATOM   8802  C  C   . MET C 1 270 ? 9.407   -58.108 25.669  1.00 31.29  ? 270 MET C C   1 
ATOM   8803  O  O   . MET C 1 270 ? 8.465   -58.089 24.865  1.00 31.22  ? 270 MET C O   1 
ATOM   8804  C  CB  . MET C 1 270 ? 10.086  -60.467 25.920  1.00 32.38  ? 270 MET C CB  1 
ATOM   8805  C  CG  . MET C 1 270 ? 11.602  -60.456 25.677  1.00 32.04  ? 270 MET C CG  1 
ATOM   8806  S  SD  . MET C 1 270 ? 12.032  -61.763 24.482  1.00 33.63  ? 270 MET C SD  1 
ATOM   8807  C  CE  . MET C 1 270 ? 11.272  -61.241 22.978  1.00 30.00  ? 270 MET C CE  1 
ATOM   8808  N  N   . THR C 1 271 ? 10.364  -57.186 25.697  1.00 28.47  ? 271 THR C N   1 
ATOM   8809  C  CA  . THR C 1 271 ? 10.456  -56.168 24.680  1.00 25.66  ? 271 THR C CA  1 
ATOM   8810  C  C   . THR C 1 271 ? 11.655  -56.458 23.779  1.00 28.66  ? 271 THR C C   1 
ATOM   8811  O  O   . THR C 1 271 ? 12.235  -57.564 23.796  1.00 31.37  ? 271 THR C O   1 
ATOM   8812  C  CB  . THR C 1 271 ? 10.549  -54.778 25.331  1.00 29.35  ? 271 THR C CB  1 
ATOM   8813  O  OG1 . THR C 1 271 ? 11.814  -54.668 26.020  1.00 32.43  ? 271 THR C OG1 1 
ATOM   8814  C  CG2 . THR C 1 271 ? 9.404   -54.583 26.342  1.00 31.94  ? 271 THR C CG2 1 
ATOM   8815  N  N   . ASP C 1 272 ? 12.017  -55.465 22.969  1.00 31.14  ? 272 ASP C N   1 
ATOM   8816  C  CA  . ASP C 1 272 ? 13.160  -55.661 22.108  1.00 34.09  ? 272 ASP C CA  1 
ATOM   8817  C  C   . ASP C 1 272 ? 14.025  -54.416 22.228  1.00 35.61  ? 272 ASP C C   1 
ATOM   8818  O  O   . ASP C 1 272 ? 14.468  -54.065 23.334  1.00 38.27  ? 272 ASP C O   1 
ATOM   8819  C  CB  . ASP C 1 272 ? 12.692  -55.943 20.698  1.00 32.83  ? 272 ASP C CB  1 
ATOM   8820  C  CG  . ASP C 1 272 ? 13.798  -56.445 19.820  1.00 35.35  ? 272 ASP C CG  1 
ATOM   8821  O  OD1 . ASP C 1 272 ? 14.607  -57.244 20.317  1.00 35.54  ? 272 ASP C OD1 1 
ATOM   8822  O  OD2 . ASP C 1 272 ? 13.820  -56.100 18.622  1.00 37.77  ? 272 ASP C OD2 1 
ATOM   8823  N  N   . THR C 1 273 ? 14.176  -53.673 21.149  1.00 33.26  ? 273 THR C N   1 
ATOM   8824  C  CA  . THR C 1 273 ? 15.174  -52.616 21.192  1.00 36.63  ? 273 THR C CA  1 
ATOM   8825  C  C   . THR C 1 273 ? 14.747  -51.484 22.135  1.00 41.07  ? 273 THR C C   1 
ATOM   8826  O  O   . THR C 1 273 ? 13.623  -51.416 22.650  1.00 42.66  ? 273 THR C O   1 
ATOM   8827  C  CB  . THR C 1 273 ? 15.428  -52.031 19.801  1.00 37.75  ? 273 THR C CB  1 
ATOM   8828  O  OG1 . THR C 1 273 ? 14.228  -51.378 19.383  1.00 42.04  ? 273 THR C OG1 1 
ATOM   8829  C  CG2 . THR C 1 273 ? 15.841  -53.095 18.785  1.00 36.94  ? 273 THR C CG2 1 
ATOM   8830  N  N   . GLN C 1 274 ? 15.668  -50.590 22.329  1.00 40.54  ? 274 GLN C N   1 
ATOM   8831  C  CA  . GLN C 1 274 ? 15.560  -49.373 23.098  1.00 43.85  ? 274 GLN C CA  1 
ATOM   8832  C  C   . GLN C 1 274 ? 14.249  -48.588 22.925  1.00 34.32  ? 274 GLN C C   1 
ATOM   8833  O  O   . GLN C 1 274 ? 13.940  -48.114 21.832  1.00 39.63  ? 274 GLN C O   1 
ATOM   8834  C  CB  . GLN C 1 274 ? 16.861  -48.606 22.760  1.00 43.00  ? 274 GLN C CB  1 
ATOM   8835  C  CG  . GLN C 1 274 ? 16.953  -47.799 21.482  1.00 40.83  ? 274 GLN C CG  1 
ATOM   8836  C  CD  . GLN C 1 274 ? 17.751  -48.477 20.304  1.00 45.06  ? 274 GLN C CD  1 
ATOM   8837  O  OE1 . GLN C 1 274 ? 17.257  -49.439 19.658  1.00 41.08  ? 274 GLN C OE1 1 
ATOM   8838  N  NE2 . GLN C 1 274 ? 18.945  -47.905 19.966  1.00 33.54  ? 274 GLN C NE2 1 
ATOM   8839  N  N   . PRO C 1 275 ? 13.460  -48.412 23.983  1.00 35.87  ? 275 PRO C N   1 
ATOM   8840  C  CA  . PRO C 1 275 ? 12.175  -47.727 23.846  1.00 36.43  ? 275 PRO C CA  1 
ATOM   8841  C  C   . PRO C 1 275 ? 12.360  -46.214 23.925  1.00 37.24  ? 275 PRO C C   1 
ATOM   8842  O  O   . PRO C 1 275 ? 13.414  -45.740 24.374  1.00 36.52  ? 275 PRO C O   1 
ATOM   8843  C  CB  . PRO C 1 275 ? 11.377  -48.244 25.049  1.00 41.72  ? 275 PRO C CB  1 
ATOM   8844  C  CG  . PRO C 1 275 ? 12.436  -48.514 26.068  1.00 41.00  ? 275 PRO C CG  1 
ATOM   8845  C  CD  . PRO C 1 275 ? 13.764  -48.708 25.393  1.00 41.46  ? 275 PRO C CD  1 
ATOM   8846  N  N   . PRO C 1 276 ? 11.377  -45.420 23.496  1.00 37.19  ? 276 PRO C N   1 
ATOM   8847  C  CA  . PRO C 1 276 ? 11.425  -43.985 23.793  1.00 33.86  ? 276 PRO C CA  1 
ATOM   8848  C  C   . PRO C 1 276 ? 11.161  -43.774 25.280  1.00 39.77  ? 276 PRO C C   1 
ATOM   8849  O  O   . PRO C 1 276 ? 10.452  -44.556 25.914  1.00 44.06  ? 276 PRO C O   1 
ATOM   8850  C  CB  . PRO C 1 276 ? 10.279  -43.399 22.956  1.00 38.97  ? 276 PRO C CB  1 
ATOM   8851  C  CG  . PRO C 1 276 ? 10.020  -44.444 21.887  1.00 39.31  ? 276 PRO C CG  1 
ATOM   8852  C  CD  . PRO C 1 276 ? 10.248  -45.753 22.608  1.00 38.35  ? 276 PRO C CD  1 
ATOM   8853  N  N   . TRP C 1 277 ? 11.709  -42.690 25.824  1.00 42.97  ? 277 TRP C N   1 
ATOM   8854  C  CA  . TRP C 1 277 ? 11.594  -42.396 27.260  1.00 41.26  ? 277 TRP C CA  1 
ATOM   8855  C  C   . TRP C 1 277 ? 10.132  -42.338 27.718  1.00 42.70  ? 277 TRP C C   1 
ATOM   8856  O  O   . TRP C 1 277 ? 9.786   -42.837 28.801  1.00 47.61  ? 277 TRP C O   1 
ATOM   8857  C  CB  . TRP C 1 277 ? 12.323  -41.081 27.548  1.00 37.77  ? 277 TRP C CB  1 
ATOM   8858  C  CG  . TRP C 1 277 ? 13.778  -41.295 27.779  1.00 43.21  ? 277 TRP C CG  1 
ATOM   8859  C  CD1 . TRP C 1 277 ? 14.801  -40.804 26.998  1.00 41.24  ? 277 TRP C CD1 1 
ATOM   8860  C  CD2 . TRP C 1 277 ? 14.410  -42.034 28.839  1.00 48.68  ? 277 TRP C CD2 1 
ATOM   8861  N  NE1 . TRP C 1 277 ? 16.019  -41.215 27.490  1.00 40.70  ? 277 TRP C NE1 1 
ATOM   8862  C  CE2 . TRP C 1 277 ? 15.812  -41.972 28.616  1.00 48.07  ? 277 TRP C CE2 1 
ATOM   8863  C  CE3 . TRP C 1 277 ? 13.938  -42.739 29.952  1.00 51.62  ? 277 TRP C CE3 1 
ATOM   8864  C  CZ2 . TRP C 1 277 ? 16.738  -42.584 29.465  1.00 48.89  ? 277 TRP C CZ2 1 
ATOM   8865  C  CZ3 . TRP C 1 277 ? 14.870  -43.367 30.790  1.00 55.88  ? 277 TRP C CZ3 1 
ATOM   8866  C  CH2 . TRP C 1 277 ? 16.251  -43.281 30.539  1.00 52.42  ? 277 TRP C CH2 1 
ATOM   8867  N  N   . SER C 1 278 ? 9.261   -41.771 26.889  1.00 40.01  ? 278 SER C N   1 
ATOM   8868  C  CA  . SER C 1 278 ? 7.820   -41.688 27.104  1.00 43.63  ? 278 SER C CA  1 
ATOM   8869  C  C   . SER C 1 278 ? 7.132   -43.032 27.204  1.00 48.81  ? 278 SER C C   1 
ATOM   8870  O  O   . SER C 1 278 ? 5.963   -43.089 27.606  1.00 52.98  ? 278 SER C O   1 
ATOM   8871  C  CB  . SER C 1 278 ? 7.175   -40.897 25.964  1.00 48.80  ? 278 SER C CB  1 
ATOM   8872  O  OG  . SER C 1 278 ? 7.323   -39.512 26.201  1.00 55.59  ? 278 SER C OG  1 
ATOM   8873  N  N   . PHE C 1 279 ? 7.801   -44.102 26.809  1.00 44.07  ? 279 PHE C N   1 
ATOM   8874  C  CA  . PHE C 1 279 ? 7.255   -45.413 27.057  1.00 48.19  ? 279 PHE C CA  1 
ATOM   8875  C  C   . PHE C 1 279 ? 7.397   -45.808 28.521  1.00 52.95  ? 279 PHE C C   1 
ATOM   8876  O  O   . PHE C 1 279 ? 6.695   -46.720 28.968  1.00 54.43  ? 279 PHE C O   1 
ATOM   8877  C  CB  . PHE C 1 279 ? 7.959   -46.418 26.146  1.00 46.08  ? 279 PHE C CB  1 
ATOM   8878  C  CG  . PHE C 1 279 ? 7.236   -47.712 25.987  1.00 47.79  ? 279 PHE C CG  1 
ATOM   8879  C  CD1 . PHE C 1 279 ? 6.270   -47.859 25.010  1.00 45.49  ? 279 PHE C CD1 1 
ATOM   8880  C  CD2 . PHE C 1 279 ? 7.557   -48.808 26.780  1.00 48.85  ? 279 PHE C CD2 1 
ATOM   8881  C  CE1 . PHE C 1 279 ? 5.605   -49.076 24.849  1.00 46.04  ? 279 PHE C CE1 1 
ATOM   8882  C  CE2 . PHE C 1 279 ? 6.895   -50.013 26.625  1.00 49.21  ? 279 PHE C CE2 1 
ATOM   8883  C  CZ  . PHE C 1 279 ? 5.910   -50.142 25.659  1.00 46.90  ? 279 PHE C CZ  1 
ATOM   8884  N  N   . LEU C 1 280 ? 8.298   -45.162 29.276  1.00 53.05  ? 280 LEU C N   1 
ATOM   8885  C  CA  . LEU C 1 280 ? 8.571   -45.626 30.637  1.00 52.70  ? 280 LEU C CA  1 
ATOM   8886  C  C   . LEU C 1 280 ? 7.323   -45.533 31.488  1.00 54.64  ? 280 LEU C C   1 
ATOM   8887  O  O   . LEU C 1 280 ? 7.053   -46.410 32.318  1.00 56.23  ? 280 LEU C O   1 
ATOM   8888  C  CB  . LEU C 1 280 ? 9.731   -44.838 31.260  1.00 52.53  ? 280 LEU C CB  1 
ATOM   8889  C  CG  . LEU C 1 280 ? 11.167  -45.360 31.099  1.00 52.50  ? 280 LEU C CG  1 
ATOM   8890  C  CD1 . LEU C 1 280 ? 11.759  -45.340 29.672  1.00 48.43  ? 280 LEU C CD1 1 
ATOM   8891  C  CD2 . LEU C 1 280 ? 12.041  -44.622 32.053  1.00 54.74  ? 280 LEU C CD2 1 
ATOM   8892  N  N   . LYS C 1 281 ? 6.524   -44.501 31.258  1.00 54.48  ? 281 LYS C N   1 
ATOM   8893  C  CA  . LYS C 1 281 ? 5.235   -44.383 31.915  1.00 57.00  ? 281 LYS C CA  1 
ATOM   8894  C  C   . LYS C 1 281 ? 4.282   -45.493 31.481  1.00 57.62  ? 281 LYS C C   1 
ATOM   8895  O  O   . LYS C 1 281 ? 3.463   -45.949 32.285  1.00 56.38  ? 281 LYS C O   1 
ATOM   8896  C  CB  . LYS C 1 281 ? 4.672   -42.992 31.625  1.00 60.13  ? 281 LYS C CB  1 
ATOM   8897  C  CG  . LYS C 1 281 ? 3.637   -42.918 30.502  1.00 60.22  ? 281 LYS C CG  1 
ATOM   8898  C  CD  . LYS C 1 281 ? 3.760   -41.606 29.714  1.00 60.84  ? 281 LYS C CD  1 
ATOM   8899  C  CE  . LYS C 1 281 ? 3.310   -40.424 30.537  1.00 61.71  ? 281 LYS C CE  1 
ATOM   8900  N  NZ  . LYS C 1 281 ? 1.851   -40.452 30.835  1.00 70.32  ? 281 LYS C NZ  1 
ATOM   8901  N  N   . ILE C 1 282 ? 4.387   -45.966 30.234  1.00 56.81  ? 282 ILE C N   1 
ATOM   8902  C  CA  . ILE C 1 282 ? 3.554   -47.086 29.800  1.00 55.45  ? 282 ILE C CA  1 
ATOM   8903  C  C   . ILE C 1 282 ? 3.919   -48.350 30.572  1.00 53.03  ? 282 ILE C C   1 
ATOM   8904  O  O   . ILE C 1 282 ? 3.030   -49.132 30.940  1.00 55.86  ? 282 ILE C O   1 
ATOM   8905  C  CB  . ILE C 1 282 ? 3.667   -47.288 28.275  1.00 53.39  ? 282 ILE C CB  1 
ATOM   8906  C  CG1 . ILE C 1 282 ? 2.713   -46.350 27.540  1.00 55.34  ? 282 ILE C CG1 1 
ATOM   8907  C  CG2 . ILE C 1 282 ? 3.388   -48.721 27.882  1.00 53.84  ? 282 ILE C CG2 1 
ATOM   8908  C  CD1 . ILE C 1 282 ? 3.097   -46.136 26.075  1.00 51.58  ? 282 ILE C CD1 1 
ATOM   8909  N  N   . PHE C 1 283 ? 5.217   -48.547 30.860  1.00 47.91  ? 283 PHE C N   1 
ATOM   8910  C  CA  . PHE C 1 283 ? 5.654   -49.641 31.734  1.00 51.29  ? 283 PHE C CA  1 
ATOM   8911  C  C   . PHE C 1 283 ? 4.960   -49.548 33.095  1.00 52.82  ? 283 PHE C C   1 
ATOM   8912  O  O   . PHE C 1 283 ? 4.348   -50.512 33.571  1.00 52.75  ? 283 PHE C O   1 
ATOM   8913  C  CB  . PHE C 1 283 ? 7.178   -49.609 31.951  1.00 47.52  ? 283 PHE C CB  1 
ATOM   8914  C  CG  . PHE C 1 283 ? 8.012   -50.202 30.833  1.00 46.41  ? 283 PHE C CG  1 
ATOM   8915  C  CD1 . PHE C 1 283 ? 7.770   -51.486 30.354  1.00 48.66  ? 283 PHE C CD1 1 
ATOM   8916  C  CD2 . PHE C 1 283 ? 9.096   -49.495 30.324  1.00 44.40  ? 283 PHE C CD2 1 
ATOM   8917  C  CE1 . PHE C 1 283 ? 8.563   -52.026 29.329  1.00 44.40  ? 283 PHE C CE1 1 
ATOM   8918  C  CE2 . PHE C 1 283 ? 9.895   -50.022 29.310  1.00 47.10  ? 283 PHE C CE2 1 
ATOM   8919  C  CZ  . PHE C 1 283 ? 9.622   -51.299 28.808  1.00 41.54  ? 283 PHE C CZ  1 
ATOM   8920  N  N   . ARG C 1 284 ? 5.079   -48.389 33.753  1.00 51.02  ? 284 ARG C N   1 
ATOM   8921  C  CA  . ARG C 1 284 ? 4.401   -48.184 35.026  1.00 49.27  ? 284 ARG C CA  1 
ATOM   8922  C  C   . ARG C 1 284 ? 2.910   -48.433 34.883  1.00 54.68  ? 284 ARG C C   1 
ATOM   8923  O  O   . ARG C 1 284 ? 2.283   -49.051 35.748  1.00 57.24  ? 284 ARG C O   1 
ATOM   8924  C  CB  . ARG C 1 284 ? 4.669   -46.761 35.547  1.00 54.71  ? 284 ARG C CB  1 
ATOM   8925  C  CG  . ARG C 1 284 ? 6.145   -46.460 36.020  1.00 59.81  ? 284 ARG C CG  1 
ATOM   8926  C  CD  . ARG C 1 284 ? 6.777   -47.520 36.993  1.00 60.10  ? 284 ARG C CD  1 
ATOM   8927  N  NE  . ARG C 1 284 ? 8.044   -47.061 37.577  1.00 60.02  ? 284 ARG C NE  1 
ATOM   8928  C  CZ  . ARG C 1 284 ? 9.069   -47.838 37.925  1.00 58.65  ? 284 ARG C CZ  1 
ATOM   8929  N  NH1 . ARG C 1 284 ? 8.950   -49.160 37.988  1.00 60.63  ? 284 ARG C NH1 1 
ATOM   8930  N  NH2 . ARG C 1 284 ? 10.237  -47.274 38.247  1.00 55.44  ? 284 ARG C NH2 1 
ATOM   8931  N  N   . TYR C 1 285 ? 2.331   -48.002 33.775  1.00 54.23  ? 285 TYR C N   1 
ATOM   8932  C  CA  . TYR C 1 285 ? 0.923   -48.283 33.559  1.00 58.17  ? 285 TYR C CA  1 
ATOM   8933  C  C   . TYR C 1 285 ? 0.676   -49.780 33.401  1.00 55.41  ? 285 TYR C C   1 
ATOM   8934  O  O   . TYR C 1 285 ? -0.298  -50.318 33.931  1.00 61.69  ? 285 TYR C O   1 
ATOM   8935  C  CB  . TYR C 1 285 ? 0.446   -47.495 32.347  1.00 61.84  ? 285 TYR C CB  1 
ATOM   8936  C  CG  . TYR C 1 285 ? -0.959  -47.812 31.951  1.00 63.54  ? 285 TYR C CG  1 
ATOM   8937  C  CD1 . TYR C 1 285 ? -2.031  -47.219 32.599  1.00 70.06  ? 285 TYR C CD1 1 
ATOM   8938  C  CD2 . TYR C 1 285 ? -1.215  -48.667 30.888  1.00 65.72  ? 285 TYR C CD2 1 
ATOM   8939  C  CE1 . TYR C 1 285 ? -3.324  -47.505 32.235  1.00 74.91  ? 285 TYR C CE1 1 
ATOM   8940  C  CE2 . TYR C 1 285 ? -2.496  -48.951 30.510  1.00 72.44  ? 285 TYR C CE2 1 
ATOM   8941  C  CZ  . TYR C 1 285 ? -3.550  -48.369 31.189  1.00 76.44  ? 285 TYR C CZ  1 
ATOM   8942  O  OH  . TYR C 1 285 ? -4.835  -48.652 30.812  1.00 85.29  ? 285 TYR C OH  1 
ATOM   8943  N  N   . LEU C 1 286 ? 1.568   -50.479 32.711  1.00 56.34  ? 286 LEU C N   1 
ATOM   8944  C  CA  . LEU C 1 286 ? 1.372   -51.911 32.523  1.00 55.98  ? 286 LEU C CA  1 
ATOM   8945  C  C   . LEU C 1 286 ? 1.365   -52.635 33.862  1.00 54.79  ? 286 LEU C C   1 
ATOM   8946  O  O   . LEU C 1 286 ? 0.574   -53.559 34.076  1.00 53.40  ? 286 LEU C O   1 
ATOM   8947  C  CB  . LEU C 1 286 ? 2.474   -52.438 31.610  1.00 53.43  ? 286 LEU C CB  1 
ATOM   8948  C  CG  . LEU C 1 286 ? 1.960   -52.389 30.175  1.00 53.75  ? 286 LEU C CG  1 
ATOM   8949  C  CD1 . LEU C 1 286 ? 2.963   -52.894 29.192  1.00 47.43  ? 286 LEU C CD1 1 
ATOM   8950  C  CD2 . LEU C 1 286 ? 0.671   -53.160 30.090  1.00 54.31  ? 286 LEU C CD2 1 
ATOM   8951  N  N   . GLU C 1 287 ? 2.213   -52.191 34.787  1.00 55.15  ? 287 GLU C N   1 
ATOM   8952  C  CA  . GLU C 1 287 ? 2.238   -52.736 36.141  1.00 58.45  ? 287 GLU C CA  1 
ATOM   8953  C  C   . GLU C 1 287 ? 0.864   -52.727 36.817  1.00 60.82  ? 287 GLU C C   1 
ATOM   8954  O  O   . GLU C 1 287 ? 0.614   -53.555 37.701  1.00 62.70  ? 287 GLU C O   1 
ATOM   8955  C  CB  . GLU C 1 287 ? 3.264   -51.959 36.971  1.00 62.27  ? 287 GLU C CB  1 
ATOM   8956  C  CG  . GLU C 1 287 ? 3.151   -52.111 38.487  1.00 68.71  ? 287 GLU C CG  1 
ATOM   8957  C  CD  . GLU C 1 287 ? 4.497   -51.932 39.171  1.00 75.70  ? 287 GLU C CD  1 
ATOM   8958  O  OE1 . GLU C 1 287 ? 5.489   -51.657 38.431  1.00 69.96  ? 287 GLU C OE1 1 
ATOM   8959  O  OE2 . GLU C 1 287 ? 4.563   -52.079 40.423  1.00 77.84  ? 287 GLU C OE2 1 
ATOM   8960  N  N   . THR C 1 288 ? -0.056  -51.836 36.422  1.00 64.71  ? 288 THR C N   1 
ATOM   8961  C  CA  . THR C 1 288 ? -1.385  -51.893 37.048  1.00 64.87  ? 288 THR C CA  1 
ATOM   8962  C  C   . THR C 1 288 ? -2.204  -53.081 36.558  1.00 65.49  ? 288 THR C C   1 
ATOM   8963  O  O   . THR C 1 288 ? -3.152  -53.489 37.231  1.00 68.90  ? 288 THR C O   1 
ATOM   8964  C  CB  . THR C 1 288 ? -2.195  -50.602 36.831  1.00 70.29  ? 288 THR C CB  1 
ATOM   8965  O  OG1 . THR C 1 288 ? -2.934  -50.682 35.601  1.00 76.78  ? 288 THR C OG1 1 
ATOM   8966  C  CG2 . THR C 1 288 ? -1.300  -49.359 36.845  1.00 69.62  ? 288 THR C CG2 1 
ATOM   8967  N  N   . TYR C 1 289 ? -1.857  -53.637 35.402  1.00 66.53  ? 289 TYR C N   1 
ATOM   8968  C  CA  . TYR C 1 289 ? -2.422  -54.868 34.857  1.00 68.73  ? 289 TYR C CA  1 
ATOM   8969  C  C   . TYR C 1 289 ? -1.761  -56.121 35.444  1.00 62.43  ? 289 TYR C C   1 
ATOM   8970  O  O   . TYR C 1 289 ? -2.106  -57.230 35.029  1.00 59.46  ? 289 TYR C O   1 
ATOM   8971  C  CB  . TYR C 1 289 ? -2.206  -54.886 33.331  1.00 71.71  ? 289 TYR C CB  1 
ATOM   8972  C  CG  . TYR C 1 289 ? -3.130  -54.037 32.461  1.00 77.05  ? 289 TYR C CG  1 
ATOM   8973  C  CD1 . TYR C 1 289 ? -4.364  -54.497 32.023  1.00 84.06  ? 289 TYR C CD1 1 
ATOM   8974  C  CD2 . TYR C 1 289 ? -2.743  -52.752 32.084  1.00 75.91  ? 289 TYR C CD2 1 
ATOM   8975  C  CE1 . TYR C 1 289 ? -5.188  -53.697 31.208  1.00 86.70  ? 289 TYR C CE1 1 
ATOM   8976  C  CE2 . TYR C 1 289 ? -3.550  -51.955 31.290  1.00 80.48  ? 289 TYR C CE2 1 
ATOM   8977  C  CZ  . TYR C 1 289 ? -4.770  -52.423 30.854  1.00 84.91  ? 289 TYR C CZ  1 
ATOM   8978  O  OH  . TYR C 1 289 ? -5.557  -51.604 30.065  1.00 84.81  ? 289 TYR C OH  1 
ATOM   8979  N  N   . GLY C 1 290 ? -0.785  -55.977 36.352  1.00 53.61  ? 290 GLY C N   1 
ATOM   8980  C  CA  . GLY C 1 290 ? 0.033   -57.101 36.774  1.00 48.46  ? 290 GLY C CA  1 
ATOM   8981  C  C   . GLY C 1 290 ? 1.090   -57.520 35.773  1.00 46.33  ? 290 GLY C C   1 
ATOM   8982  O  O   . GLY C 1 290 ? 1.669   -58.606 35.900  1.00 40.08  ? 290 GLY C O   1 
ATOM   8983  N  N   . ALA C 1 291 ? 1.389   -56.674 34.800  1.00 38.98  ? 291 ALA C N   1 
ATOM   8984  C  CA  . ALA C 1 291 ? 2.290   -57.000 33.705  1.00 42.75  ? 291 ALA C CA  1 
ATOM   8985  C  C   . ALA C 1 291 ? 3.681   -56.450 34.004  1.00 40.32  ? 291 ALA C C   1 
ATOM   8986  O  O   . ALA C 1 291 ? 3.848   -55.238 34.185  1.00 41.84  ? 291 ALA C O   1 
ATOM   8987  C  CB  . ALA C 1 291 ? 1.754   -56.422 32.399  1.00 39.28  ? 291 ALA C CB  1 
ATOM   8988  N  N   . VAL C 1 292 ? 4.669   -57.327 34.060  1.00 34.44  ? 292 VAL C N   1 
ATOM   8989  C  CA  . VAL C 1 292 ? 6.068   -56.928 34.202  1.00 30.72  ? 292 VAL C CA  1 
ATOM   8990  C  C   . VAL C 1 292 ? 6.833   -57.284 32.926  1.00 34.47  ? 292 VAL C C   1 
ATOM   8991  O  O   . VAL C 1 292 ? 6.677   -58.384 32.377  1.00 33.33  ? 292 VAL C O   1 
ATOM   8992  C  CB  . VAL C 1 292 ? 6.745   -57.588 35.411  1.00 33.53  ? 292 VAL C CB  1 
ATOM   8993  C  CG1 . VAL C 1 292 ? 6.705   -59.078 35.261  1.00 34.51  ? 292 VAL C CG1 1 
ATOM   8994  C  CG2 . VAL C 1 292 ? 8.202   -57.103 35.536  1.00 35.41  ? 292 VAL C CG2 1 
ATOM   8995  N  N   . SER C 1 293 ? 7.690   -56.374 32.466  1.00 33.17  ? 293 SER C N   1 
ATOM   8996  C  CA  . SER C 1 293 ? 8.669   -56.749 31.446  1.00 32.10  ? 293 SER C CA  1 
ATOM   8997  C  C   . SER C 1 293 ? 9.912   -57.333 32.091  1.00 30.48  ? 293 SER C C   1 
ATOM   8998  O  O   . SER C 1 293 ? 10.533  -56.677 32.930  1.00 33.05  ? 293 SER C O   1 
ATOM   8999  C  CB  . SER C 1 293 ? 9.087   -55.568 30.574  1.00 30.67  ? 293 SER C CB  1 
ATOM   9000  O  OG  . SER C 1 293 ? 10.058  -56.034 29.642  1.00 33.63  ? 293 SER C OG  1 
ATOM   9001  N  N   . ILE C 1 294 ? 10.270  -58.569 31.712  1.00 26.67  ? 294 ILE C N   1 
ATOM   9002  C  CA  . ILE C 1 294 ? 11.432  -59.221 32.329  1.00 28.15  ? 294 ILE C CA  1 
ATOM   9003  C  C   . ILE C 1 294 ? 12.731  -58.894 31.630  1.00 30.28  ? 294 ILE C C   1 
ATOM   9004  O  O   . ILE C 1 294 ? 13.791  -59.357 32.066  1.00 30.34  ? 294 ILE C O   1 
ATOM   9005  C  CB  . ILE C 1 294 ? 11.290  -60.750 32.398  1.00 30.12  ? 294 ILE C CB  1 
ATOM   9006  C  CG1 . ILE C 1 294 ? 10.895  -61.369 31.038  1.00 26.98  ? 294 ILE C CG1 1 
ATOM   9007  C  CG2 . ILE C 1 294 ? 10.277  -61.079 33.471  1.00 36.37  ? 294 ILE C CG2 1 
ATOM   9008  C  CD1 . ILE C 1 294 ? 12.006  -61.392 29.939  1.00 29.87  ? 294 ILE C CD1 1 
ATOM   9009  N  N   . GLY C 1 295 ? 12.690  -58.138 30.546  1.00 28.22  ? 295 GLY C N   1 
ATOM   9010  C  CA  . GLY C 1 295 ? 13.900  -57.854 29.818  1.00 27.54  ? 295 GLY C CA  1 
ATOM   9011  C  C   . GLY C 1 295 ? 13.674  -57.980 28.317  1.00 28.35  ? 295 GLY C C   1 
ATOM   9012  O  O   . GLY C 1 295 ? 12.536  -57.942 27.811  1.00 27.82  ? 295 GLY C O   1 
ATOM   9013  N  N   . SER C 1 296 ? 14.800  -58.058 27.624  1.00 23.67  ? 296 SER C N   1 
ATOM   9014  C  CA  . SER C 1 296 ? 14.848  -58.036 26.158  1.00 26.41  ? 296 SER C CA  1 
ATOM   9015  C  C   . SER C 1 296 ? 16.240  -58.420 25.753  1.00 23.03  ? 296 SER C C   1 
ATOM   9016  O  O   . SER C 1 296 ? 17.168  -58.355 26.562  1.00 25.94  ? 296 SER C O   1 
ATOM   9017  C  CB  . SER C 1 296 ? 14.499  -56.659 25.592  1.00 26.41  ? 296 SER C CB  1 
ATOM   9018  O  OG  . SER C 1 296 ? 15.392  -55.680 26.067  1.00 27.60  ? 296 SER C OG  1 
ATOM   9019  N  N   . LEU C 1 297 ? 16.398  -58.790 24.475  1.00 24.38  ? 297 LEU C N   1 
ATOM   9020  C  CA  . LEU C 1 297 ? 17.726  -59.097 24.008  1.00 23.27  ? 297 LEU C CA  1 
ATOM   9021  C  C   . LEU C 1 297 ? 18.602  -57.858 24.092  1.00 24.10  ? 297 LEU C C   1 
ATOM   9022  O  O   . LEU C 1 297 ? 19.798  -57.959 24.362  1.00 25.52  ? 297 LEU C O   1 
ATOM   9023  C  CB  . LEU C 1 297 ? 17.672  -59.621 22.557  1.00 23.61  ? 297 LEU C CB  1 
ATOM   9024  C  CG  . LEU C 1 297 ? 18.970  -60.113 22.029  1.00 24.15  ? 297 LEU C CG  1 
ATOM   9025  C  CD1 . LEU C 1 297 ? 19.440  -61.337 22.723  1.00 23.83  ? 297 LEU C CD1 1 
ATOM   9026  C  CD2 . LEU C 1 297 ? 18.852  -60.313 20.491  1.00 28.49  ? 297 LEU C CD2 1 
ATOM   9027  N  N   . TYR C 1 298 ? 17.997  -56.674 23.932  1.00 25.52  ? 298 TYR C N   1 
ATOM   9028  C  CA  . TYR C 1 298 ? 18.729  -55.422 24.057  1.00 25.98  ? 298 TYR C CA  1 
ATOM   9029  C  C   . TYR C 1 298 ? 19.287  -55.247 25.463  1.00 26.17  ? 298 TYR C C   1 
ATOM   9030  O  O   . TYR C 1 298 ? 20.501  -55.099 25.662  1.00 24.90  ? 298 TYR C O   1 
ATOM   9031  C  CB  . TYR C 1 298 ? 17.790  -54.292 23.662  1.00 26.03  ? 298 TYR C CB  1 
ATOM   9032  C  CG  . TYR C 1 298 ? 18.353  -52.935 23.927  1.00 27.36  ? 298 TYR C CG  1 
ATOM   9033  C  CD1 . TYR C 1 298 ? 19.147  -52.299 22.997  1.00 31.09  ? 298 TYR C CD1 1 
ATOM   9034  C  CD2 . TYR C 1 298 ? 18.115  -52.297 25.146  1.00 30.74  ? 298 TYR C CD2 1 
ATOM   9035  C  CE1 . TYR C 1 298 ? 19.693  -51.018 23.256  1.00 29.45  ? 298 TYR C CE1 1 
ATOM   9036  C  CE2 . TYR C 1 298 ? 18.657  -51.035 25.401  1.00 29.25  ? 298 TYR C CE2 1 
ATOM   9037  C  CZ  . TYR C 1 298 ? 19.448  -50.421 24.474  1.00 32.02  ? 298 TYR C CZ  1 
ATOM   9038  O  OH  . TYR C 1 298 ? 19.966  -49.164 24.736  1.00 34.05  ? 298 TYR C OH  1 
ATOM   9039  N  N   . THR C 1 299 ? 18.409  -55.283 26.476  1.00 23.08  ? 299 THR C N   1 
ATOM   9040  C  CA  . THR C 1 299 ? 18.863  -55.184 27.860  1.00 23.10  ? 299 THR C CA  1 
ATOM   9041  C  C   . THR C 1 299 ? 19.852  -56.302 28.209  1.00 25.30  ? 299 THR C C   1 
ATOM   9042  O  O   . THR C 1 299 ? 20.864  -56.057 28.873  1.00 23.12  ? 299 THR C O   1 
ATOM   9043  C  CB  . THR C 1 299 ? 17.606  -55.211 28.745  1.00 26.51  ? 299 THR C CB  1 
ATOM   9044  O  OG1 . THR C 1 299 ? 16.853  -54.001 28.460  1.00 28.14  ? 299 THR C OG1 1 
ATOM   9045  C  CG2 . THR C 1 299 ? 17.947  -55.280 30.219  1.00 30.76  ? 299 THR C CG2 1 
ATOM   9046  N  N   . PHE C 1 300 ? 19.598  -57.525 27.737  1.00 25.53  ? 300 PHE C N   1 
ATOM   9047  C  CA  . PHE C 1 300 ? 20.417  -58.655 28.179  1.00 25.22  ? 300 PHE C CA  1 
ATOM   9048  C  C   . PHE C 1 300 ? 21.776  -58.650 27.495  1.00 23.82  ? 300 PHE C C   1 
ATOM   9049  O  O   . PHE C 1 300 ? 22.783  -59.052 28.091  1.00 24.16  ? 300 PHE C O   1 
ATOM   9050  C  CB  . PHE C 1 300 ? 19.718  -59.978 27.839  1.00 23.79  ? 300 PHE C CB  1 
ATOM   9051  C  CG  . PHE C 1 300 ? 18.449  -60.262 28.622  1.00 26.75  ? 300 PHE C CG  1 
ATOM   9052  C  CD1 . PHE C 1 300 ? 17.999  -59.462 29.668  1.00 25.68  ? 300 PHE C CD1 1 
ATOM   9053  C  CD2 . PHE C 1 300 ? 17.692  -61.397 28.270  1.00 28.30  ? 300 PHE C CD2 1 
ATOM   9054  C  CE1 . PHE C 1 300 ? 16.800  -59.804 30.353  1.00 26.67  ? 300 PHE C CE1 1 
ATOM   9055  C  CE2 . PHE C 1 300 ? 16.546  -61.747 28.943  1.00 23.17  ? 300 PHE C CE2 1 
ATOM   9056  C  CZ  . PHE C 1 300 ? 16.089  -60.955 29.983  1.00 26.83  ? 300 PHE C CZ  1 
ATOM   9057  N  N   . ALA C 1 301 ? 21.833  -58.186 26.227  1.00 23.07  ? 301 ALA C N   1 
ATOM   9058  C  CA  . ALA C 1 301 ? 23.018  -58.502 25.438  1.00 24.59  ? 301 ALA C CA  1 
ATOM   9059  C  C   . ALA C 1 301 ? 23.553  -57.313 24.640  1.00 23.63  ? 301 ALA C C   1 
ATOM   9060  O  O   . ALA C 1 301 ? 24.416  -57.512 23.761  1.00 23.17  ? 301 ALA C O   1 
ATOM   9061  C  CB  . ALA C 1 301 ? 22.696  -59.691 24.513  1.00 25.89  ? 301 ALA C CB  1 
ATOM   9062  N  N   . LEU C 1 302 ? 23.107  -56.103 24.919  1.00 21.29  ? 302 LEU C N   1 
ATOM   9063  C  CA  . LEU C 1 302 ? 23.812  -54.970 24.328  1.00 22.01  ? 302 LEU C CA  1 
ATOM   9064  C  C   . LEU C 1 302 ? 25.265  -55.011 24.745  1.00 25.01  ? 302 LEU C C   1 
ATOM   9065  O  O   . LEU C 1 302 ? 26.171  -54.712 23.945  1.00 23.56  ? 302 LEU C O   1 
ATOM   9066  C  CB  . LEU C 1 302 ? 23.186  -53.655 24.779  1.00 22.43  ? 302 LEU C CB  1 
ATOM   9067  C  CG  . LEU C 1 302 ? 23.669  -52.401 24.081  1.00 25.61  ? 302 LEU C CG  1 
ATOM   9068  C  CD1 . LEU C 1 302 ? 23.192  -52.404 22.663  1.00 24.76  ? 302 LEU C CD1 1 
ATOM   9069  C  CD2 . LEU C 1 302 ? 23.158  -51.109 24.803  1.00 28.44  ? 302 LEU C CD2 1 
ATOM   9070  N  N   . GLU C 1 303 ? 25.489  -55.343 26.021  1.00 20.44  ? 303 GLU C N   1 
ATOM   9071  C  CA  . GLU C 1 303 ? 26.828  -55.635 26.543  1.00 19.59  ? 303 GLU C CA  1 
ATOM   9072  C  C   . GLU C 1 303 ? 26.951  -56.999 27.212  1.00 21.86  ? 303 GLU C C   1 
ATOM   9073  O  O   . GLU C 1 303 ? 28.075  -57.503 27.278  1.00 24.86  ? 303 GLU C O   1 
ATOM   9074  C  CB  . GLU C 1 303 ? 27.265  -54.584 27.571  1.00 22.19  ? 303 GLU C CB  1 
ATOM   9075  C  CG  . GLU C 1 303 ? 27.159  -53.069 27.110  1.00 24.43  ? 303 GLU C CG  1 
ATOM   9076  C  CD  . GLU C 1 303 ? 28.165  -52.632 26.082  1.00 26.06  ? 303 GLU C CD  1 
ATOM   9077  O  OE1 . GLU C 1 303 ? 28.887  -53.501 25.542  1.00 26.67  ? 303 GLU C OE1 1 
ATOM   9078  O  OE2 . GLU C 1 303 ? 28.288  -51.403 25.852  1.00 23.03  ? 303 GLU C OE2 1 
ATOM   9079  N  N   . GLY C 1 304 ? 25.871  -57.591 27.711  1.00 20.85  ? 304 GLY C N   1 
ATOM   9080  C  CA  . GLY C 1 304 ? 25.978  -58.912 28.352  1.00 20.41  ? 304 GLY C CA  1 
ATOM   9081  C  C   . GLY C 1 304 ? 26.520  -59.946 27.369  1.00 21.34  ? 304 GLY C C   1 
ATOM   9082  O  O   . GLY C 1 304 ? 26.151  -59.966 26.202  1.00 22.99  ? 304 GLY C O   1 
ATOM   9083  N  N   . ILE C 1 305 ? 27.427  -60.806 27.848  1.00 22.29  ? 305 ILE C N   1 
ATOM   9084  C  CA  . ILE C 1 305 ? 28.086  -61.811 27.002  1.00 20.25  ? 305 ILE C CA  1 
ATOM   9085  C  C   . ILE C 1 305 ? 27.732  -63.175 27.554  1.00 22.94  ? 305 ILE C C   1 
ATOM   9086  O  O   . ILE C 1 305 ? 27.916  -63.423 28.748  1.00 22.92  ? 305 ILE C O   1 
ATOM   9087  C  CB  . ILE C 1 305 ? 29.623  -61.590 26.947  1.00 20.86  ? 305 ILE C CB  1 
ATOM   9088  C  CG1 . ILE C 1 305 ? 29.946  -60.275 26.216  1.00 24.40  ? 305 ILE C CG1 1 
ATOM   9089  C  CG2 . ILE C 1 305 ? 30.332  -62.702 26.176  1.00 24.01  ? 305 ILE C CG2 1 
ATOM   9090  C  CD1 . ILE C 1 305 ? 29.675  -60.327 24.707  1.00 22.77  ? 305 ILE C CD1 1 
ATOM   9091  N  N   . TRP C 1 306 ? 27.276  -64.075 26.672  1.00 22.06  ? 306 TRP C N   1 
ATOM   9092  C  CA  . TRP C 1 306 ? 26.485  -65.240 27.072  1.00 24.56  ? 306 TRP C CA  1 
ATOM   9093  C  C   . TRP C 1 306 ? 27.093  -66.513 26.512  1.00 24.07  ? 306 TRP C C   1 
ATOM   9094  O  O   . TRP C 1 306 ? 27.847  -66.478 25.538  1.00 24.35  ? 306 TRP C O   1 
ATOM   9095  C  CB  . TRP C 1 306 ? 25.032  -65.101 26.539  1.00 24.49  ? 306 TRP C CB  1 
ATOM   9096  C  CG  . TRP C 1 306 ? 24.236  -63.954 27.153  1.00 24.66  ? 306 TRP C CG  1 
ATOM   9097  C  CD1 . TRP C 1 306 ? 24.319  -62.599 26.852  1.00 24.67  ? 306 TRP C CD1 1 
ATOM   9098  C  CD2 . TRP C 1 306 ? 23.272  -64.073 28.200  1.00 24.43  ? 306 TRP C CD2 1 
ATOM   9099  N  NE1 . TRP C 1 306 ? 23.440  -61.902 27.636  1.00 22.87  ? 306 TRP C NE1 1 
ATOM   9100  C  CE2 . TRP C 1 306 ? 22.765  -62.763 28.459  1.00 25.81  ? 306 TRP C CE2 1 
ATOM   9101  C  CE3 . TRP C 1 306 ? 22.739  -65.170 28.924  1.00 26.78  ? 306 TRP C CE3 1 
ATOM   9102  C  CZ2 . TRP C 1 306 ? 21.807  -62.510 29.453  1.00 24.91  ? 306 TRP C CZ2 1 
ATOM   9103  C  CZ3 . TRP C 1 306 ? 21.748  -64.911 29.891  1.00 25.27  ? 306 TRP C CZ3 1 
ATOM   9104  C  CH2 . TRP C 1 306 ? 21.302  -63.582 30.146  1.00 24.24  ? 306 TRP C CH2 1 
ATOM   9105  N  N   . GLU C 1 307 ? 26.680  -67.659 27.083  1.00 21.76  ? 307 GLU C N   1 
ATOM   9106  C  CA  . GLU C 1 307 ? 27.078  -68.968 26.567  1.00 23.85  ? 307 GLU C CA  1 
ATOM   9107  C  C   . GLU C 1 307 ? 25.981  -69.962 26.914  1.00 23.78  ? 307 GLU C C   1 
ATOM   9108  O  O   . GLU C 1 307 ? 25.135  -69.720 27.779  1.00 25.74  ? 307 GLU C O   1 
ATOM   9109  C  CB  . GLU C 1 307 ? 28.425  -69.406 27.178  1.00 22.06  ? 307 GLU C CB  1 
ATOM   9110  C  CG  . GLU C 1 307 ? 28.285  -69.983 28.601  1.00 27.47  ? 307 GLU C CG  1 
ATOM   9111  C  CD  . GLU C 1 307 ? 29.616  -70.443 29.254  1.00 26.90  ? 307 GLU C CD  1 
ATOM   9112  O  OE1 . GLU C 1 307 ? 30.712  -70.166 28.648  1.00 28.38  ? 307 GLU C OE1 1 
ATOM   9113  O  OE2 . GLU C 1 307 ? 29.553  -71.012 30.402  1.00 29.99  ? 307 GLU C OE2 1 
ATOM   9114  N  N   . ASP C 1 308 ? 26.040  -71.121 26.254  1.00 22.87  ? 308 ASP C N   1 
ATOM   9115  C  CA  . ASP C 1 308 ? 25.162  -72.220 26.610  1.00 25.53  ? 308 ASP C CA  1 
ATOM   9116  C  C   . ASP C 1 308 ? 25.724  -72.928 27.834  1.00 30.54  ? 308 ASP C C   1 
ATOM   9117  O  O   . ASP C 1 308 ? 26.903  -73.323 27.864  1.00 26.44  ? 308 ASP C O   1 
ATOM   9118  C  CB  . ASP C 1 308 ? 25.037  -73.220 25.435  1.00 27.21  ? 308 ASP C CB  1 
ATOM   9119  C  CG  . ASP C 1 308 ? 24.431  -72.611 24.173  1.00 31.35  ? 308 ASP C CG  1 
ATOM   9120  O  OD1 . ASP C 1 308 ? 23.674  -71.634 24.264  1.00 32.86  ? 308 ASP C OD1 1 
ATOM   9121  O  OD2 . ASP C 1 308 ? 24.715  -73.116 23.053  1.00 34.50  ? 308 ASP C OD2 1 
ATOM   9122  N  N   . LYS C 1 309 ? 24.877  -73.121 28.822  1.00 26.21  ? 309 LYS C N   1 
ATOM   9123  C  CA  . LYS C 1 309 ? 25.256  -73.755 30.080  1.00 26.77  ? 309 LYS C CA  1 
ATOM   9124  C  C   . LYS C 1 309 ? 25.060  -75.259 29.988  1.00 27.42  ? 309 LYS C C   1 
ATOM   9125  O  O   . LYS C 1 309 ? 24.513  -75.776 29.013  1.00 29.46  ? 309 LYS C O   1 
ATOM   9126  C  CB  . LYS C 1 309 ? 24.418  -73.152 31.199  1.00 28.50  ? 309 LYS C CB  1 
ATOM   9127  C  CG  . LYS C 1 309 ? 24.702  -71.665 31.395  1.00 26.62  ? 309 LYS C CG  1 
ATOM   9128  C  CD  . LYS C 1 309 ? 26.131  -71.505 31.866  1.00 31.08  ? 309 LYS C CD  1 
ATOM   9129  C  CE  . LYS C 1 309 ? 26.448  -70.061 32.225  1.00 33.03  ? 309 LYS C CE  1 
ATOM   9130  N  NZ  . LYS C 1 309 ? 27.891  -70.003 32.731  1.00 31.54  ? 309 LYS C NZ  1 
ATOM   9131  N  N   . PRO C 1 310 ? 25.518  -76.021 30.996  1.00 30.78  ? 310 PRO C N   1 
ATOM   9132  C  CA  . PRO C 1 310 ? 25.484  -77.491 30.873  1.00 27.94  ? 310 PRO C CA  1 
ATOM   9133  C  C   . PRO C 1 310 ? 24.075  -78.089 30.810  1.00 31.06  ? 310 PRO C C   1 
ATOM   9134  O  O   . PRO C 1 310 ? 23.919  -79.251 30.381  1.00 30.21  ? 310 PRO C O   1 
ATOM   9135  C  CB  . PRO C 1 310 ? 26.217  -77.963 32.141  1.00 30.18  ? 310 PRO C CB  1 
ATOM   9136  C  CG  . PRO C 1 310 ? 27.196  -76.835 32.433  1.00 32.89  ? 310 PRO C CG  1 
ATOM   9137  C  CD  . PRO C 1 310 ? 26.383  -75.586 32.117  1.00 33.41  ? 310 PRO C CD  1 
ATOM   9138  N  N   . ASP C 1 311 ? 23.055  -77.348 31.260  1.00 27.04  ? 311 ASP C N   1 
ATOM   9139  C  CA  . ASP C 1 311 ? 21.661  -77.784 31.128  1.00 27.42  ? 311 ASP C CA  1 
ATOM   9140  C  C   . ASP C 1 311 ? 21.010  -77.240 29.875  1.00 28.68  ? 311 ASP C C   1 
ATOM   9141  O  O   . ASP C 1 311 ? 19.791  -77.381 29.714  1.00 32.45  ? 311 ASP C O   1 
ATOM   9142  C  CB  . ASP C 1 311 ? 20.826  -77.379 32.368  1.00 28.59  ? 311 ASP C CB  1 
ATOM   9143  C  CG  . ASP C 1 311 ? 20.597  -75.874 32.443  1.00 30.23  ? 311 ASP C CG  1 
ATOM   9144  O  OD1 . ASP C 1 311 ? 21.332  -75.131 31.775  1.00 29.69  ? 311 ASP C OD1 1 
ATOM   9145  O  OD2 . ASP C 1 311 ? 19.683  -75.429 33.171  1.00 32.87  ? 311 ASP C OD2 1 
ATOM   9146  N  N   . GLY C 1 312 ? 21.788  -76.612 28.998  1.00 27.83  ? 312 GLY C N   1 
ATOM   9147  C  CA  . GLY C 1 312 ? 21.263  -76.078 27.767  1.00 26.83  ? 312 GLY C CA  1 
ATOM   9148  C  C   . GLY C 1 312 ? 20.712  -74.680 27.899  1.00 28.41  ? 312 GLY C C   1 
ATOM   9149  O  O   . GLY C 1 312 ? 20.255  -74.127 26.897  1.00 30.24  ? 312 GLY C O   1 
ATOM   9150  N  N   . SER C 1 313 ? 20.716  -74.107 29.103  1.00 25.00  ? 313 SER C N   1 
ATOM   9151  C  CA  . SER C 1 313 ? 20.155  -72.759 29.291  1.00 26.71  ? 313 SER C CA  1 
ATOM   9152  C  C   . SER C 1 313 ? 21.149  -71.695 28.909  1.00 25.82  ? 313 SER C C   1 
ATOM   9153  O  O   . SER C 1 313 ? 22.352  -71.940 28.811  1.00 24.66  ? 313 SER C O   1 
ATOM   9154  C  CB  . SER C 1 313 ? 19.703  -72.590 30.750  1.00 26.35  ? 313 SER C CB  1 
ATOM   9155  O  OG  . SER C 1 313 ? 20.825  -72.623 31.608  1.00 27.67  ? 313 SER C OG  1 
ATOM   9156  N  N   . TRP C 1 314 ? 20.646  -70.451 28.824  1.00 25.13  ? 314 TRP C N   1 
ATOM   9157  C  CA  . TRP C 1 314 ? 21.487  -69.325 28.477  1.00 25.59  ? 314 TRP C CA  1 
ATOM   9158  C  C   . TRP C 1 314 ? 21.990  -68.696 29.762  1.00 23.16  ? 314 TRP C C   1 
ATOM   9159  O  O   . TRP C 1 314 ? 21.202  -68.492 30.702  1.00 24.10  ? 314 TRP C O   1 
ATOM   9160  C  CB  . TRP C 1 314 ? 20.712  -68.255 27.713  1.00 26.85  ? 314 TRP C CB  1 
ATOM   9161  C  CG  . TRP C 1 314 ? 21.507  -67.676 26.574  1.00 25.19  ? 314 TRP C CG  1 
ATOM   9162  C  CD1 . TRP C 1 314 ? 22.590  -68.237 25.936  1.00 24.15  ? 314 TRP C CD1 1 
ATOM   9163  C  CD2 . TRP C 1 314 ? 21.297  -66.392 25.956  1.00 26.89  ? 314 TRP C CD2 1 
ATOM   9164  N  NE1 . TRP C 1 314 ? 23.013  -67.407 24.902  1.00 24.97  ? 314 TRP C NE1 1 
ATOM   9165  C  CE2 . TRP C 1 314 ? 22.250  -66.253 24.935  1.00 25.97  ? 314 TRP C CE2 1 
ATOM   9166  C  CE3 . TRP C 1 314 ? 20.400  -65.350 26.185  1.00 29.03  ? 314 TRP C CE3 1 
ATOM   9167  C  CZ2 . TRP C 1 314 ? 22.310  -65.134 24.127  1.00 29.94  ? 314 TRP C CZ2 1 
ATOM   9168  C  CZ3 . TRP C 1 314 ? 20.491  -64.199 25.386  1.00 26.87  ? 314 TRP C CZ3 1 
ATOM   9169  C  CH2 . TRP C 1 314 ? 21.430  -64.110 24.388  1.00 27.83  ? 314 TRP C CH2 1 
ATOM   9170  N  N   . GLY C 1 315 ? 23.310  -68.481 29.855  1.00 24.08  ? 315 GLY C N   1 
ATOM   9171  C  CA  . GLY C 1 315 ? 23.858  -67.861 31.055  1.00 27.92  ? 315 GLY C CA  1 
ATOM   9172  C  C   . GLY C 1 315 ? 25.139  -67.093 30.745  1.00 25.45  ? 315 GLY C C   1 
ATOM   9173  O  O   . GLY C 1 315 ? 25.571  -67.014 29.595  1.00 23.64  ? 315 GLY C O   1 
ATOM   9174  N  N   . GLY C 1 316 ? 25.709  -66.436 31.753  1.00 25.60  ? 316 GLY C N   1 
ATOM   9175  C  CA  . GLY C 1 316 ? 26.920  -65.651 31.494  1.00 26.27  ? 316 GLY C CA  1 
ATOM   9176  C  C   . GLY C 1 316 ? 28.081  -66.524 31.014  1.00 29.95  ? 316 GLY C C   1 
ATOM   9177  O  O   . GLY C 1 316 ? 28.264  -67.670 31.462  1.00 24.96  ? 316 GLY C O   1 
ATOM   9178  N  N   . ARG C 1 317 ? 28.864  -65.973 30.071  1.00 24.05  ? 317 ARG C N   1 
ATOM   9179  C  CA  . ARG C 1 317 ? 29.977  -66.714 29.449  1.00 24.70  ? 317 ARG C CA  1 
ATOM   9180  C  C   . ARG C 1 317 ? 31.044  -66.985 30.490  1.00 24.31  ? 317 ARG C C   1 
ATOM   9181  O  O   . ARG C 1 317 ? 31.329  -66.123 31.318  1.00 28.06  ? 317 ARG C O   1 
ATOM   9182  C  CB  . ARG C 1 317 ? 30.618  -65.943 28.272  1.00 22.49  ? 317 ARG C CB  1 
ATOM   9183  C  CG  . ARG C 1 317 ? 31.654  -66.780 27.579  1.00 22.47  ? 317 ARG C CG  1 
ATOM   9184  C  CD  . ARG C 1 317 ? 32.126  -66.090 26.249  1.00 25.04  ? 317 ARG C CD  1 
ATOM   9185  N  NE  . ARG C 1 317 ? 33.280  -66.820 25.711  1.00 25.76  ? 317 ARG C NE  1 
ATOM   9186  C  CZ  . ARG C 1 317 ? 33.740  -66.686 24.475  1.00 26.81  ? 317 ARG C CZ  1 
ATOM   9187  N  NH1 . ARG C 1 317 ? 33.175  -65.827 23.605  1.00 26.09  ? 317 ARG C NH1 1 
ATOM   9188  N  NH2 . ARG C 1 317 ? 34.854  -67.338 24.135  1.00 26.81  ? 317 ARG C NH2 1 
ATOM   9189  N  N   . THR C 1 318 ? 31.570  -68.226 30.503  1.00 25.25  ? 318 THR C N   1 
ATOM   9190  C  CA  . THR C 1 318 ? 32.601  -68.623 31.486  1.00 26.14  ? 318 THR C CA  1 
ATOM   9191  C  C   . THR C 1 318 ? 33.890  -67.815 31.283  1.00 24.39  ? 318 THR C C   1 
ATOM   9192  O  O   . THR C 1 318 ? 34.370  -67.641 30.156  1.00 25.09  ? 318 THR C O   1 
ATOM   9193  C  CB  . THR C 1 318 ? 32.923  -70.127 31.393  1.00 29.06  ? 318 THR C CB  1 
ATOM   9194  O  OG1 . THR C 1 318 ? 31.779  -70.877 31.794  1.00 27.22  ? 318 THR C OG1 1 
ATOM   9195  C  CG2 . THR C 1 318 ? 34.027  -70.502 32.407  1.00 29.49  ? 318 THR C CG2 1 
ATOM   9196  N  N   . LEU C 1 319 ? 34.429  -67.281 32.374  1.00 26.43  ? 319 LEU C N   1 
ATOM   9197  C  CA  . LEU C 1 319 ? 35.654  -66.481 32.281  1.00 28.92  ? 319 LEU C CA  1 
ATOM   9198  C  C   . LEU C 1 319 ? 36.831  -67.399 31.924  1.00 32.09  ? 319 LEU C C   1 
ATOM   9199  O  O   . LEU C 1 319 ? 36.867  -68.566 32.383  1.00 28.43  ? 319 LEU C O   1 
ATOM   9200  C  CB  . LEU C 1 319 ? 35.891  -65.778 33.626  1.00 30.03  ? 319 LEU C CB  1 
ATOM   9201  C  CG  . LEU C 1 319 ? 34.645  -65.016 34.123  1.00 24.78  ? 319 LEU C CG  1 
ATOM   9202  C  CD1 . LEU C 1 319 ? 34.811  -64.556 35.559  1.00 29.88  ? 319 LEU C CD1 1 
ATOM   9203  C  CD2 . LEU C 1 319 ? 34.496  -63.765 33.261  1.00 30.79  ? 319 LEU C CD2 1 
ATOM   9204  N  N   . PRO C 1 320 ? 37.781  -66.944 31.078  1.00 29.52  ? 320 PRO C N   1 
ATOM   9205  C  CA  . PRO C 1 320 ? 38.816  -67.897 30.578  1.00 32.50  ? 320 PRO C CA  1 
ATOM   9206  C  C   . PRO C 1 320 ? 39.630  -68.543 31.679  1.00 33.98  ? 320 PRO C C   1 
ATOM   9207  O  O   . PRO C 1 320 ? 39.888  -69.760 31.644  1.00 36.16  ? 320 PRO C O   1 
ATOM   9208  C  CB  . PRO C 1 320 ? 39.697  -67.021 29.670  1.00 37.61  ? 320 PRO C CB  1 
ATOM   9209  C  CG  . PRO C 1 320 ? 38.760  -65.905 29.201  1.00 33.35  ? 320 PRO C CG  1 
ATOM   9210  C  CD  . PRO C 1 320 ? 37.863  -65.620 30.388  1.00 27.63  ? 320 PRO C CD  1 
ATOM   9211  N  N   . TRP C 1 321 ? 39.993  -67.768 32.703  1.00 32.10  ? 321 TRP C N   1 
ATOM   9212  C  CA  . TRP C 1 321 ? 40.762  -68.306 33.813  1.00 35.94  ? 321 TRP C CA  1 
ATOM   9213  C  C   . TRP C 1 321 ? 39.977  -69.325 34.640  1.00 35.42  ? 321 TRP C C   1 
ATOM   9214  O  O   . TRP C 1 321 ? 40.580  -70.060 35.421  1.00 39.03  ? 321 TRP C O   1 
ATOM   9215  C  CB  . TRP C 1 321 ? 41.274  -67.169 34.711  1.00 37.32  ? 321 TRP C CB  1 
ATOM   9216  C  CG  . TRP C 1 321 ? 40.245  -66.204 35.241  1.00 32.67  ? 321 TRP C CG  1 
ATOM   9217  C  CD1 . TRP C 1 321 ? 39.588  -66.259 36.440  1.00 36.15  ? 321 TRP C CD1 1 
ATOM   9218  C  CD2 . TRP C 1 321 ? 39.783  -65.020 34.582  1.00 27.95  ? 321 TRP C CD2 1 
ATOM   9219  N  NE1 . TRP C 1 321 ? 38.749  -65.153 36.573  1.00 31.84  ? 321 TRP C NE1 1 
ATOM   9220  C  CE2 . TRP C 1 321 ? 38.861  -64.390 35.446  1.00 27.23  ? 321 TRP C CE2 1 
ATOM   9221  C  CE3 . TRP C 1 321 ? 40.067  -64.430 33.335  1.00 28.35  ? 321 TRP C CE3 1 
ATOM   9222  C  CZ2 . TRP C 1 321 ? 38.219  -63.211 35.113  1.00 29.43  ? 321 TRP C CZ2 1 
ATOM   9223  C  CZ3 . TRP C 1 321 ? 39.423  -63.252 33.004  1.00 29.96  ? 321 TRP C CZ3 1 
ATOM   9224  C  CH2 . TRP C 1 321 ? 38.502  -62.666 33.882  1.00 28.30  ? 321 TRP C CH2 1 
ATOM   9225  N  N   . ASP C 1 322 ? 38.651  -69.387 34.499  1.00 35.00  ? 322 ASP C N   1 
ATOM   9226  C  CA  . ASP C 1 322 ? 37.849  -70.453 35.097  1.00 38.32  ? 322 ASP C CA  1 
ATOM   9227  C  C   . ASP C 1 322 ? 37.783  -71.728 34.260  1.00 35.88  ? 322 ASP C C   1 
ATOM   9228  O  O   . ASP C 1 322 ? 37.224  -72.724 34.735  1.00 39.08  ? 322 ASP C O   1 
ATOM   9229  C  CB  . ASP C 1 322 ? 36.443  -69.926 35.412  1.00 36.87  ? 322 ASP C CB  1 
ATOM   9230  C  CG  . ASP C 1 322 ? 36.456  -69.050 36.648  1.00 36.96  ? 322 ASP C CG  1 
ATOM   9231  O  OD1 . ASP C 1 322 ? 37.343  -69.277 37.487  1.00 44.72  ? 322 ASP C OD1 1 
ATOM   9232  O  OD2 . ASP C 1 322 ? 35.627  -68.159 36.791  1.00 37.02  ? 322 ASP C OD2 1 
ATOM   9233  N  N   . LYS C 1 323 ? 38.384  -71.733 33.069  1.00 35.82  ? 323 LYS C N   1 
ATOM   9234  C  CA  . LYS C 1 323 ? 38.474  -72.886 32.178  1.00 38.90  ? 323 LYS C CA  1 
ATOM   9235  C  C   . LYS C 1 323 ? 39.918  -73.229 31.900  1.00 37.21  ? 323 LYS C C   1 
ATOM   9236  O  O   . LYS C 1 323 ? 40.202  -73.790 30.839  1.00 42.06  ? 323 LYS C O   1 
ATOM   9237  C  CB  . LYS C 1 323 ? 37.839  -72.619 30.809  1.00 45.95  ? 323 LYS C CB  1 
ATOM   9238  C  CG  . LYS C 1 323 ? 36.497  -72.068 30.779  1.00 45.01  ? 323 LYS C CG  1 
ATOM   9239  C  CD  . LYS C 1 323 ? 36.236  -71.339 29.504  1.00 44.55  ? 323 LYS C CD  1 
ATOM   9240  C  CE  . LYS C 1 323 ? 36.061  -72.230 28.329  1.00 50.26  ? 323 LYS C CE  1 
ATOM   9241  N  NZ  . LYS C 1 323 ? 35.651  -71.242 27.278  1.00 49.13  ? 323 LYS C NZ  1 
ATOM   9242  N  N   . GLY C 1 324 ? 40.843  -72.797 32.750  1.00 38.08  ? 324 GLY C N   1 
ATOM   9243  C  CA  . GLY C 1 324 ? 42.243  -73.115 32.554  1.00 38.86  ? 324 GLY C CA  1 
ATOM   9244  C  C   . GLY C 1 324 ? 42.943  -72.408 31.415  1.00 40.64  ? 324 GLY C C   1 
ATOM   9245  O  O   . GLY C 1 324 ? 43.985  -72.894 30.961  1.00 38.30  ? 324 GLY C O   1 
ATOM   9246  N  N   . ILE C 1 325 ? 42.437  -71.254 30.968  1.00 36.69  ? 325 ILE C N   1 
ATOM   9247  C  CA  . ILE C 1 325 ? 43.046  -70.476 29.884  1.00 37.80  ? 325 ILE C CA  1 
ATOM   9248  C  C   . ILE C 1 325 ? 43.790  -69.316 30.527  1.00 39.59  ? 325 ILE C C   1 
ATOM   9249  O  O   . ILE C 1 325 ? 43.175  -68.501 31.226  1.00 39.90  ? 325 ILE C O   1 
ATOM   9250  C  CB  . ILE C 1 325 ? 41.990  -69.963 28.893  1.00 38.65  ? 325 ILE C CB  1 
ATOM   9251  C  CG1 . ILE C 1 325 ? 41.284  -71.135 28.207  1.00 41.22  ? 325 ILE C CG1 1 
ATOM   9252  C  CG2 . ILE C 1 325 ? 42.626  -69.007 27.837  1.00 34.05  ? 325 ILE C CG2 1 
ATOM   9253  C  CD1 . ILE C 1 325 ? 39.992  -70.701 27.458  1.00 39.25  ? 325 ILE C CD1 1 
ATOM   9254  N  N   . GLU C 1 326 ? 45.104  -69.243 30.308  1.00 39.81  ? 326 GLU C N   1 
ATOM   9255  C  CA  . GLU C 1 326 ? 45.893  -68.156 30.864  1.00 46.78  ? 326 GLU C CA  1 
ATOM   9256  C  C   . GLU C 1 326 ? 45.782  -66.923 29.988  1.00 41.73  ? 326 GLU C C   1 
ATOM   9257  O  O   . GLU C 1 326 ? 45.554  -67.012 28.771  1.00 37.77  ? 326 GLU C O   1 
ATOM   9258  C  CB  . GLU C 1 326 ? 47.372  -68.528 30.989  1.00 51.25  ? 326 GLU C CB  1 
ATOM   9259  C  CG  . GLU C 1 326 ? 47.719  -69.406 32.169  1.00 59.83  ? 326 GLU C CG  1 
ATOM   9260  C  CD  . GLU C 1 326 ? 48.790  -70.407 31.812  1.00 67.55  ? 326 GLU C CD  1 
ATOM   9261  O  OE1 . GLU C 1 326 ? 49.056  -70.557 30.596  1.00 67.78  ? 326 GLU C OE1 1 
ATOM   9262  O  OE2 . GLU C 1 326 ? 49.332  -71.060 32.733  1.00 69.40  ? 326 GLU C OE2 1 
ATOM   9263  N  N   . ILE C 1 327 ? 45.898  -65.756 30.624  1.00 39.19  ? 327 ILE C N   1 
ATOM   9264  C  CA  . ILE C 1 327 ? 45.933  -64.476 29.919  1.00 36.18  ? 327 ILE C CA  1 
ATOM   9265  C  C   . ILE C 1 327 ? 47.160  -63.757 30.462  1.00 39.52  ? 327 ILE C C   1 
ATOM   9266  O  O   . ILE C 1 327 ? 47.083  -62.988 31.428  1.00 39.89  ? 327 ILE C O   1 
ATOM   9267  C  CB  . ILE C 1 327 ? 44.663  -63.646 30.106  1.00 34.76  ? 327 ILE C CB  1 
ATOM   9268  C  CG1 . ILE C 1 327 ? 43.433  -64.517 29.895  1.00 39.37  ? 327 ILE C CG1 1 
ATOM   9269  C  CG2 . ILE C 1 327 ? 44.634  -62.464 29.119  1.00 32.58  ? 327 ILE C CG2 1 
ATOM   9270  C  CD1 . ILE C 1 327 ? 42.077  -63.742 29.866  1.00 38.46  ? 327 ILE C CD1 1 
ATOM   9271  N  N   . ASN C 1 328 ? 48.313  -64.048 29.886  1.00 37.06  ? 328 ASN C N   1 
ATOM   9272  C  CA  . ASN C 1 328 ? 49.538  -63.562 30.484  1.00 40.43  ? 328 ASN C CA  1 
ATOM   9273  C  C   . ASN C 1 328 ? 50.379  -62.696 29.599  1.00 37.97  ? 328 ASN C C   1 
ATOM   9274  O  O   . ASN C 1 328 ? 51.493  -62.366 30.016  1.00 39.48  ? 328 ASN C O   1 
ATOM   9275  C  CB  . ASN C 1 328 ? 50.434  -64.702 30.962  1.00 43.90  ? 328 ASN C CB  1 
ATOM   9276  C  CG  . ASN C 1 328 ? 49.868  -65.421 32.142  1.00 53.35  ? 328 ASN C CG  1 
ATOM   9277  O  OD1 . ASN C 1 328 ? 49.610  -66.624 32.087  1.00 58.80  ? 328 ASN C OD1 1 
ATOM   9278  N  ND2 . ASN C 1 328 ? 49.665  -64.680 33.240  1.00 54.28  ? 328 ASN C ND2 1 
ATOM   9279  N  N   . ASP C 1 329 ? 49.940  -62.377 28.382  1.00 33.58  ? 329 ASP C N   1 
ATOM   9280  C  CA  . ASP C 1 329 ? 50.737  -61.480 27.563  1.00 33.36  ? 329 ASP C CA  1 
ATOM   9281  C  C   . ASP C 1 329 ? 49.794  -60.764 26.613  1.00 30.65  ? 329 ASP C C   1 
ATOM   9282  O  O   . ASP C 1 329 ? 48.619  -61.131 26.477  1.00 27.08  ? 329 ASP C O   1 
ATOM   9283  C  CB  . ASP C 1 329 ? 51.854  -62.187 26.781  1.00 36.42  ? 329 ASP C CB  1 
ATOM   9284  C  CG  . ASP C 1 329 ? 51.371  -63.361 25.951  1.00 38.35  ? 329 ASP C CG  1 
ATOM   9285  O  OD1 . ASP C 1 329 ? 50.436  -63.165 25.141  1.00 36.30  ? 329 ASP C OD1 1 
ATOM   9286  O  OD2 . ASP C 1 329 ? 52.030  -64.429 25.966  1.00 48.15  ? 329 ASP C OD2 1 
ATOM   9287  N  N   . ARG C 1 330 ? 50.316  -59.699 25.982  1.00 25.63  ? 330 ARG C N   1 
ATOM   9288  C  CA  . ARG C 1 330 ? 49.488  -58.847 25.125  1.00 28.68  ? 330 ARG C CA  1 
ATOM   9289  C  C   . ARG C 1 330 ? 48.835  -59.621 23.977  1.00 25.87  ? 330 ARG C C   1 
ATOM   9290  O  O   . ARG C 1 330 ? 47.626  -59.462 23.708  1.00 23.90  ? 330 ARG C O   1 
ATOM   9291  C  CB  . ARG C 1 330 ? 50.350  -57.708 24.594  1.00 24.54  ? 330 ARG C CB  1 
ATOM   9292  C  CG  . ARG C 1 330 ? 49.607  -56.819 23.640  1.00 25.82  ? 330 ARG C CG  1 
ATOM   9293  C  CD  . ARG C 1 330 ? 50.545  -55.875 22.943  1.00 30.14  ? 330 ARG C CD  1 
ATOM   9294  N  NE  . ARG C 1 330 ? 51.208  -54.992 23.887  1.00 27.48  ? 330 ARG C NE  1 
ATOM   9295  C  CZ  . ARG C 1 330 ? 51.886  -53.913 23.520  1.00 30.56  ? 330 ARG C CZ  1 
ATOM   9296  N  NH1 . ARG C 1 330 ? 51.932  -53.525 22.245  1.00 27.13  ? 330 ARG C NH1 1 
ATOM   9297  N  NH2 . ARG C 1 330 ? 52.551  -53.226 24.438  1.00 29.87  ? 330 ARG C NH2 1 
ATOM   9298  N  N   . ASP C 1 331 ? 49.614  -60.444 23.268  1.00 28.17  ? 331 ASP C N   1 
ATOM   9299  C  CA  . ASP C 1 331 ? 49.070  -61.117 22.077  1.00 24.53  ? 331 ASP C CA  1 
ATOM   9300  C  C   . ASP C 1 331 ? 47.923  -62.050 22.442  1.00 27.59  ? 331 ASP C C   1 
ATOM   9301  O  O   . ASP C 1 331 ? 46.863  -62.033 21.798  1.00 26.85  ? 331 ASP C O   1 
ATOM   9302  C  CB  . ASP C 1 331 ? 50.206  -61.866 21.370  1.00 30.78  ? 331 ASP C CB  1 
ATOM   9303  C  CG  . ASP C 1 331 ? 51.050  -60.940 20.489  1.00 34.39  ? 331 ASP C CG  1 
ATOM   9304  O  OD1 . ASP C 1 331 ? 51.017  -59.718 20.737  1.00 32.40  ? 331 ASP C OD1 1 
ATOM   9305  O  OD2 . ASP C 1 331 ? 51.844  -61.437 19.669  1.00 43.19  ? 331 ASP C OD2 1 
ATOM   9306  N  N   . THR C 1 332 ? 48.089  -62.832 23.519  1.00 26.25  ? 332 THR C N   1 
ATOM   9307  C  CA  . THR C 1 332 ? 47.019  -63.706 23.976  1.00 26.33  ? 332 THR C CA  1 
ATOM   9308  C  C   . THR C 1 332 ? 45.780  -62.922 24.405  1.00 25.24  ? 332 THR C C   1 
ATOM   9309  O  O   . THR C 1 332 ? 44.638  -63.286 24.068  1.00 27.60  ? 332 THR C O   1 
ATOM   9310  C  CB  . THR C 1 332 ? 47.526  -64.559 25.138  1.00 30.19  ? 332 THR C CB  1 
ATOM   9311  O  OG1 . THR C 1 332 ? 48.721  -65.274 24.749  1.00 31.49  ? 332 THR C OG1 1 
ATOM   9312  C  CG2 . THR C 1 332 ? 46.435  -65.556 25.519  1.00 32.91  ? 332 THR C CG2 1 
ATOM   9313  N  N   . ALA C 1 333 ? 45.991  -61.838 25.176  1.00 23.37  ? 333 ALA C N   1 
ATOM   9314  C  CA  . ALA C 1 333 ? 44.880  -61.015 25.630  1.00 28.58  ? 333 ALA C CA  1 
ATOM   9315  C  C   . ALA C 1 333 ? 44.130  -60.385 24.459  1.00 24.01  ? 333 ALA C C   1 
ATOM   9316  O  O   . ALA C 1 333 ? 42.883  -60.348 24.456  1.00 22.14  ? 333 ALA C O   1 
ATOM   9317  C  CB  . ALA C 1 333 ? 45.402  -59.920 26.573  1.00 23.89  ? 333 ALA C CB  1 
ATOM   9318  N  N   . VAL C 1 334 ? 44.860  -59.896 23.445  1.00 23.81  ? 334 VAL C N   1 
ATOM   9319  C  CA  . VAL C 1 334 ? 44.194  -59.245 22.311  1.00 24.32  ? 334 VAL C CA  1 
ATOM   9320  C  C   . VAL C 1 334 ? 43.297  -60.236 21.586  1.00 23.99  ? 334 VAL C C   1 
ATOM   9321  O  O   . VAL C 1 334 ? 42.120  -59.957 21.322  1.00 22.74  ? 334 VAL C O   1 
ATOM   9322  C  CB  . VAL C 1 334 ? 45.231  -58.631 21.366  1.00 24.46  ? 334 VAL C CB  1 
ATOM   9323  C  CG1 . VAL C 1 334 ? 44.614  -58.323 20.032  1.00 23.97  ? 334 VAL C CG1 1 
ATOM   9324  C  CG2 . VAL C 1 334 ? 45.849  -57.352 22.076  1.00 22.68  ? 334 VAL C CG2 1 
ATOM   9325  N  N   . ARG C 1 335 ? 43.820  -61.437 21.305  1.00 25.55  ? 335 ARG C N   1 
ATOM   9326  C  CA  . ARG C 1 335 ? 43.019  -62.430 20.587  1.00 27.25  ? 335 ARG C CA  1 
ATOM   9327  C  C   . ARG C 1 335 ? 41.809  -62.860 21.410  1.00 25.16  ? 335 ARG C C   1 
ATOM   9328  O  O   . ARG C 1 335 ? 40.696  -62.962 20.875  1.00 23.25  ? 335 ARG C O   1 
ATOM   9329  C  CB  . ARG C 1 335 ? 43.899  -63.620 20.185  1.00 27.33  ? 335 ARG C CB  1 
ATOM   9330  C  CG  . ARG C 1 335 ? 43.300  -64.432 19.050  1.00 26.96  ? 335 ARG C CG  1 
ATOM   9331  C  CD  . ARG C 1 335 ? 44.146  -65.608 18.556  1.00 28.05  ? 335 ARG C CD  1 
ATOM   9332  N  NE  . ARG C 1 335 ? 43.546  -66.246 17.394  1.00 27.44  ? 335 ARG C NE  1 
ATOM   9333  C  CZ  . ARG C 1 335 ? 43.606  -65.763 16.159  1.00 27.28  ? 335 ARG C CZ  1 
ATOM   9334  N  NH1 . ARG C 1 335 ? 44.222  -64.623 15.897  1.00 27.93  ? 335 ARG C NH1 1 
ATOM   9335  N  NH2 . ARG C 1 335 ? 43.029  -66.441 15.168  1.00 27.17  ? 335 ARG C NH2 1 
ATOM   9336  N  N   . LEU C 1 336 ? 41.996  -63.092 22.730  1.00 23.09  ? 336 LEU C N   1 
ATOM   9337  C  CA  . LEU C 1 336 ? 40.865  -63.486 23.571  1.00 25.07  ? 336 LEU C CA  1 
ATOM   9338  C  C   . LEU C 1 336 ? 39.821  -62.381 23.677  1.00 23.65  ? 336 LEU C C   1 
ATOM   9339  O  O   . LEU C 1 336 ? 38.613  -62.659 23.730  1.00 25.85  ? 336 LEU C O   1 
ATOM   9340  C  CB  . LEU C 1 336 ? 41.332  -63.888 24.973  1.00 24.74  ? 336 LEU C CB  1 
ATOM   9341  C  CG  . LEU C 1 336 ? 42.034  -65.216 25.113  1.00 28.07  ? 336 LEU C CG  1 
ATOM   9342  C  CD1 . LEU C 1 336 ? 42.525  -65.351 26.580  1.00 33.64  ? 336 LEU C CD1 1 
ATOM   9343  C  CD2 . LEU C 1 336 ? 41.084  -66.354 24.809  1.00 31.36  ? 336 LEU C CD2 1 
ATOM   9344  N  N   . TYR C 1 337 ? 40.282  -61.125 23.729  1.00 21.56  ? 337 TYR C N   1 
ATOM   9345  C  CA  . TYR C 1 337 ? 39.406  -59.949 23.816  1.00 22.72  ? 337 TYR C CA  1 
ATOM   9346  C  C   . TYR C 1 337 ? 38.570  -59.791 22.551  1.00 20.07  ? 337 TYR C C   1 
ATOM   9347  O  O   . TYR C 1 337 ? 37.358  -59.528 22.628  1.00 21.41  ? 337 TYR C O   1 
ATOM   9348  C  CB  . TYR C 1 337 ? 40.286  -58.726 24.077  1.00 23.19  ? 337 TYR C CB  1 
ATOM   9349  C  CG  . TYR C 1 337 ? 39.536  -57.479 24.437  1.00 22.00  ? 337 TYR C CG  1 
ATOM   9350  C  CD1 . TYR C 1 337 ? 38.476  -57.476 25.320  1.00 22.21  ? 337 TYR C CD1 1 
ATOM   9351  C  CD2 . TYR C 1 337 ? 39.950  -56.272 23.899  1.00 21.79  ? 337 TYR C CD2 1 
ATOM   9352  C  CE1 . TYR C 1 337 ? 37.815  -56.253 25.671  1.00 23.89  ? 337 TYR C CE1 1 
ATOM   9353  C  CE2 . TYR C 1 337 ? 39.302  -55.105 24.217  1.00 22.32  ? 337 TYR C CE2 1 
ATOM   9354  C  CZ  . TYR C 1 337 ? 38.221  -55.103 25.048  1.00 22.09  ? 337 TYR C CZ  1 
ATOM   9355  O  OH  . TYR C 1 337 ? 37.620  -53.878 25.327  1.00 23.54  ? 337 TYR C OH  1 
ATOM   9356  N  N   . ALA C 1 338 ? 39.208  -59.932 21.386  1.00 21.65  ? 338 ALA C N   1 
ATOM   9357  C  CA  . ALA C 1 338 ? 38.500  -59.961 20.103  1.00 22.69  ? 338 ALA C CA  1 
ATOM   9358  C  C   . ALA C 1 338 ? 37.449  -61.054 20.073  1.00 24.06  ? 338 ALA C C   1 
ATOM   9359  O  O   . ALA C 1 338 ? 36.274  -60.802 19.737  1.00 24.47  ? 338 ALA C O   1 
ATOM   9360  C  CB  . ALA C 1 338 ? 39.484  -60.204 18.953  1.00 22.99  ? 338 ALA C CB  1 
ATOM   9361  N  N   . ASP C 1 339 ? 37.846  -62.281 20.459  1.00 23.42  ? 339 ASP C N   1 
ATOM   9362  C  CA  . ASP C 1 339 ? 36.883  -63.374 20.468  1.00 23.37  ? 339 ASP C CA  1 
ATOM   9363  C  C   . ASP C 1 339 ? 35.716  -63.103 21.412  1.00 23.35  ? 339 ASP C C   1 
ATOM   9364  O  O   . ASP C 1 339 ? 34.560  -63.420 21.081  1.00 23.78  ? 339 ASP C O   1 
ATOM   9365  C  CB  . ASP C 1 339 ? 37.598  -64.683 20.828  1.00 21.72  ? 339 ASP C CB  1 
ATOM   9366  C  CG  . ASP C 1 339 ? 36.632  -65.807 21.063  1.00 27.82  ? 339 ASP C CG  1 
ATOM   9367  O  OD1 . ASP C 1 339 ? 36.257  -66.435 20.067  1.00 27.20  ? 339 ASP C OD1 1 
ATOM   9368  O  OD2 . ASP C 1 339 ? 36.184  -66.005 22.218  1.00 29.05  ? 339 ASP C OD2 1 
ATOM   9369  N  N   . TRP C 1 340 ? 35.994  -62.576 22.616  1.00 21.57  ? 340 TRP C N   1 
ATOM   9370  C  CA  . TRP C 1 340 ? 34.932  -62.285 23.576  1.00 20.84  ? 340 TRP C CA  1 
ATOM   9371  C  C   . TRP C 1 340 ? 33.933  -61.308 22.991  1.00 22.51  ? 340 TRP C C   1 
ATOM   9372  O  O   . TRP C 1 340 ? 32.726  -61.552 22.995  1.00 21.30  ? 340 TRP C O   1 
ATOM   9373  C  CB  . TRP C 1 340 ? 35.544  -61.716 24.834  1.00 24.52  ? 340 TRP C CB  1 
ATOM   9374  C  CG  . TRP C 1 340 ? 34.651  -61.630 25.991  1.00 23.50  ? 340 TRP C CG  1 
ATOM   9375  C  CD1 . TRP C 1 340 ? 33.865  -60.555 26.370  1.00 21.69  ? 340 TRP C CD1 1 
ATOM   9376  C  CD2 . TRP C 1 340 ? 34.509  -62.615 27.015  1.00 23.97  ? 340 TRP C CD2 1 
ATOM   9377  N  NE1 . TRP C 1 340 ? 33.259  -60.827 27.571  1.00 20.89  ? 340 TRP C NE1 1 
ATOM   9378  C  CE2 . TRP C 1 340 ? 33.612  -62.106 27.965  1.00 22.37  ? 340 TRP C CE2 1 
ATOM   9379  C  CE3 . TRP C 1 340 ? 35.043  -63.906 27.195  1.00 23.93  ? 340 TRP C CE3 1 
ATOM   9380  C  CZ2 . TRP C 1 340 ? 33.245  -62.820 29.115  1.00 23.71  ? 340 TRP C CZ2 1 
ATOM   9381  C  CZ3 . TRP C 1 340 ? 34.659  -64.640 28.323  1.00 25.15  ? 340 TRP C CZ3 1 
ATOM   9382  C  CH2 . TRP C 1 340 ? 33.755  -64.074 29.285  1.00 24.34  ? 340 TRP C CH2 1 
ATOM   9383  N  N   . ASN C 1 341 ? 34.439  -60.207 22.393  1.00 21.92  ? 341 ASN C N   1 
ATOM   9384  C  CA  . ASN C 1 341 ? 33.512  -59.231 21.833  1.00 21.69  ? 341 ASN C CA  1 
ATOM   9385  C  C   . ASN C 1 341 ? 32.777  -59.766 20.614  1.00 24.07  ? 341 ASN C C   1 
ATOM   9386  O  O   . ASN C 1 341 ? 31.594  -59.449 20.419  1.00 22.29  ? 341 ASN C O   1 
ATOM   9387  C  CB  . ASN C 1 341 ? 34.269  -57.954 21.501  1.00 24.04  ? 341 ASN C CB  1 
ATOM   9388  C  CG  . ASN C 1 341 ? 34.363  -57.080 22.723  1.00 23.42  ? 341 ASN C CG  1 
ATOM   9389  O  OD1 . ASN C 1 341 ? 33.430  -56.337 23.038  1.00 24.33  ? 341 ASN C OD1 1 
ATOM   9390  N  ND2 . ASN C 1 341 ? 35.449  -57.209 23.476  1.00 24.43  ? 341 ASN C ND2 1 
ATOM   9391  N  N   . LEU C 1 342 ? 33.415  -60.622 19.822  1.00 20.17  ? 342 LEU C N   1 
ATOM   9392  C  CA  . LEU C 1 342 ? 32.752  -61.107 18.609  1.00 24.10  ? 342 LEU C CA  1 
ATOM   9393  C  C   . LEU C 1 342 ? 31.574  -62.026 18.935  1.00 24.32  ? 342 LEU C C   1 
ATOM   9394  O  O   . LEU C 1 342 ? 30.700  -62.231 18.075  1.00 22.70  ? 342 LEU C O   1 
ATOM   9395  C  CB  . LEU C 1 342 ? 33.766  -61.832 17.711  1.00 20.85  ? 342 LEU C CB  1 
ATOM   9396  C  CG  . LEU C 1 342 ? 34.672  -60.826 16.960  1.00 23.04  ? 342 LEU C CG  1 
ATOM   9397  C  CD1 . LEU C 1 342 ? 35.873  -61.504 16.270  1.00 24.54  ? 342 LEU C CD1 1 
ATOM   9398  C  CD2 . LEU C 1 342 ? 33.825  -60.008 15.930  1.00 22.63  ? 342 LEU C CD2 1 
ATOM   9399  N  N   . SER C 1 343 ? 31.526  -62.568 20.153  1.00 22.54  ? 343 SER C N   1 
ATOM   9400  C  CA  . SER C 1 343 ? 30.405  -63.405 20.553  1.00 22.49  ? 343 SER C CA  1 
ATOM   9401  C  C   . SER C 1 343 ? 29.169  -62.612 20.986  1.00 21.01  ? 343 SER C C   1 
ATOM   9402  O  O   . SER C 1 343 ? 28.161  -63.217 21.396  1.00 24.31  ? 343 SER C O   1 
ATOM   9403  C  CB  . SER C 1 343 ? 30.842  -64.373 21.661  1.00 25.68  ? 343 SER C CB  1 
ATOM   9404  O  OG  . SER C 1 343 ? 30.934  -63.767 22.923  1.00 23.29  ? 343 SER C OG  1 
ATOM   9405  N  N   . LYS C 1 344 ? 29.248  -61.276 21.016  1.00 22.07  ? 344 LYS C N   1 
ATOM   9406  C  CA  . LYS C 1 344 ? 28.128  -60.431 21.427  1.00 25.27  ? 344 LYS C CA  1 
ATOM   9407  C  C   . LYS C 1 344 ? 26.815  -60.829 20.745  1.00 22.04  ? 344 LYS C C   1 
ATOM   9408  O  O   . LYS C 1 344 ? 26.728  -60.781 19.516  1.00 23.62  ? 344 LYS C O   1 
ATOM   9409  C  CB  . LYS C 1 344 ? 28.466  -58.971 21.107  1.00 25.56  ? 344 LYS C CB  1 
ATOM   9410  C  CG  . LYS C 1 344 ? 29.541  -58.464 22.079  1.00 28.17  ? 344 LYS C CG  1 
ATOM   9411  C  CD  . LYS C 1 344 ? 30.111  -57.082 21.856  1.00 29.57  ? 344 LYS C CD  1 
ATOM   9412  C  CE  . LYS C 1 344 ? 29.062  -56.021 22.027  1.00 27.50  ? 344 LYS C CE  1 
ATOM   9413  N  NZ  . LYS C 1 344 ? 29.089  -55.548 23.418  1.00 26.47  ? 344 LYS C NZ  1 
ATOM   9414  N  N   . PRO C 1 345 ? 25.783  -61.214 21.493  1.00 21.22  ? 345 PRO C N   1 
ATOM   9415  C  CA  . PRO C 1 345 ? 24.537  -61.611 20.829  1.00 24.38  ? 345 PRO C CA  1 
ATOM   9416  C  C   . PRO C 1 345 ? 23.959  -60.493 19.989  1.00 23.31  ? 345 PRO C C   1 
ATOM   9417  O  O   . PRO C 1 345 ? 23.389  -60.785 18.934  1.00 21.77  ? 345 PRO C O   1 
ATOM   9418  C  CB  . PRO C 1 345 ? 23.601  -62.011 21.976  1.00 22.86  ? 345 PRO C CB  1 
ATOM   9419  C  CG  . PRO C 1 345 ? 24.520  -62.451 23.059  1.00 24.51  ? 345 PRO C CG  1 
ATOM   9420  C  CD  . PRO C 1 345 ? 25.765  -61.495 22.928  1.00 23.98  ? 345 PRO C CD  1 
ATOM   9421  N  N   . GLN C 1 346 ? 24.126  -59.211 20.412  1.00 22.16  ? 346 GLN C N   1 
ATOM   9422  C  CA  . GLN C 1 346 ? 23.503  -58.104 19.680  1.00 24.72  ? 346 GLN C CA  1 
ATOM   9423  C  C   . GLN C 1 346 ? 24.304  -57.674 18.473  1.00 25.48  ? 346 GLN C C   1 
ATOM   9424  O  O   . GLN C 1 346 ? 23.920  -56.678 17.834  1.00 23.64  ? 346 GLN C O   1 
ATOM   9425  C  CB  . GLN C 1 346 ? 23.256  -56.914 20.649  1.00 24.29  ? 346 GLN C CB  1 
ATOM   9426  C  CG  . GLN C 1 346 ? 21.890  -57.005 21.382  1.00 25.10  ? 346 GLN C CG  1 
ATOM   9427  C  CD  . GLN C 1 346 ? 20.710  -56.620 20.499  1.00 29.88  ? 346 GLN C CD  1 
ATOM   9428  O  OE1 . GLN C 1 346 ? 20.812  -56.560 19.255  1.00 32.99  ? 346 GLN C OE1 1 
ATOM   9429  N  NE2 . GLN C 1 346 ? 19.569  -56.499 21.103  1.00 30.49  ? 346 GLN C NE2 1 
ATOM   9430  N  N   . TRP C 1 347 ? 25.361  -58.411 18.083  1.00 22.87  ? 347 TRP C N   1 
ATOM   9431  C  CA  . TRP C 1 347 ? 25.987  -58.183 16.776  1.00 21.96  ? 347 TRP C CA  1 
ATOM   9432  C  C   . TRP C 1 347 ? 25.503  -59.165 15.709  1.00 20.25  ? 347 TRP C C   1 
ATOM   9433  O  O   . TRP C 1 347 ? 25.788  -58.958 14.527  1.00 23.73  ? 347 TRP C O   1 
ATOM   9434  C  CB  . TRP C 1 347 ? 27.534  -58.287 16.878  1.00 22.11  ? 347 TRP C CB  1 
ATOM   9435  C  CG  . TRP C 1 347 ? 28.169  -57.101 17.556  1.00 20.94  ? 347 TRP C CG  1 
ATOM   9436  C  CD1 . TRP C 1 347 ? 27.518  -55.976 18.044  1.00 23.62  ? 347 TRP C CD1 1 
ATOM   9437  C  CD2 . TRP C 1 347 ? 29.546  -56.941 17.863  1.00 20.17  ? 347 TRP C CD2 1 
ATOM   9438  N  NE1 . TRP C 1 347 ? 28.430  -55.108 18.560  1.00 23.47  ? 347 TRP C NE1 1 
ATOM   9439  C  CE2 . TRP C 1 347 ? 29.684  -55.666 18.488  1.00 22.03  ? 347 TRP C CE2 1 
ATOM   9440  C  CE3 . TRP C 1 347 ? 30.683  -57.716 17.646  1.00 21.72  ? 347 TRP C CE3 1 
ATOM   9441  C  CZ2 . TRP C 1 347 ? 30.895  -55.181 18.918  1.00 21.86  ? 347 TRP C CZ2 1 
ATOM   9442  C  CZ3 . TRP C 1 347 ? 31.943  -57.209 18.081  1.00 20.69  ? 347 TRP C CZ3 1 
ATOM   9443  C  CH2 . TRP C 1 347 ? 32.018  -55.929 18.706  1.00 22.33  ? 347 TRP C CH2 1 
ATOM   9444  N  N   . GLN C 1 348 ? 24.825  -60.260 16.103  1.00 22.85  ? 348 GLN C N   1 
ATOM   9445  C  CA  . GLN C 1 348 ? 24.612  -61.348 15.152  1.00 20.44  ? 348 GLN C CA  1 
ATOM   9446  C  C   . GLN C 1 348 ? 23.568  -60.987 14.103  1.00 21.37  ? 348 GLN C C   1 
ATOM   9447  O  O   . GLN C 1 348 ? 23.666  -61.442 12.949  1.00 24.33  ? 348 GLN C O   1 
ATOM   9448  C  CB  . GLN C 1 348 ? 24.226  -62.619 15.921  1.00 19.20  ? 348 GLN C CB  1 
ATOM   9449  C  CG  . GLN C 1 348 ? 25.254  -62.919 17.028  1.00 20.22  ? 348 GLN C CG  1 
ATOM   9450  C  CD  . GLN C 1 348 ? 26.702  -63.013 16.498  1.00 24.97  ? 348 GLN C CD  1 
ATOM   9451  O  OE1 . GLN C 1 348 ? 26.981  -63.782 15.527  1.00 25.74  ? 348 GLN C OE1 1 
ATOM   9452  N  NE2 . GLN C 1 348 ? 27.644  -62.297 17.160  1.00 25.40  ? 348 GLN C NE2 1 
ATOM   9453  N  N   . HIS C 1 349 ? 22.566  -60.183 14.464  1.00 21.58  ? 349 HIS C N   1 
ATOM   9454  C  CA  . HIS C 1 349 ? 21.489  -59.946 13.510  1.00 23.62  ? 349 HIS C CA  1 
ATOM   9455  C  C   . HIS C 1 349 ? 21.937  -58.985 12.405  1.00 21.89  ? 349 HIS C C   1 
ATOM   9456  O  O   . HIS C 1 349 ? 21.215  -58.814 11.400  1.00 24.70  ? 349 HIS C O   1 
ATOM   9457  C  CB  . HIS C 1 349 ? 20.301  -59.363 14.230  1.00 23.12  ? 349 HIS C CB  1 
ATOM   9458  C  CG  . HIS C 1 349 ? 20.551  -57.949 14.643  1.00 23.06  ? 349 HIS C CG  1 
ATOM   9459  N  ND1 . HIS C 1 349 ? 21.367  -57.645 15.713  1.00 23.53  ? 349 HIS C ND1 1 
ATOM   9460  C  CD2 . HIS C 1 349 ? 20.183  -56.767 14.096  1.00 25.03  ? 349 HIS C CD2 1 
ATOM   9461  C  CE1 . HIS C 1 349 ? 21.473  -56.332 15.819  1.00 26.94  ? 349 HIS C CE1 1 
ATOM   9462  N  NE2 . HIS C 1 349 ? 20.794  -55.778 14.833  1.00 25.53  ? 349 HIS C NE2 1 
ATOM   9463  N  N   . PHE C 1 350 ? 23.111  -58.362 12.564  1.00 22.36  ? 350 PHE C N   1 
ATOM   9464  C  CA  . PHE C 1 350 ? 23.622  -57.560 11.447  1.00 22.07  ? 350 PHE C CA  1 
ATOM   9465  C  C   . PHE C 1 350 ? 23.923  -58.426 10.241  1.00 22.69  ? 350 PHE C C   1 
ATOM   9466  O  O   . PHE C 1 350 ? 24.034  -57.901 9.122   1.00 25.19  ? 350 PHE C O   1 
ATOM   9467  C  CB  . PHE C 1 350 ? 24.882  -56.810 11.816  1.00 22.35  ? 350 PHE C CB  1 
ATOM   9468  C  CG  . PHE C 1 350 ? 24.655  -55.625 12.700  1.00 24.01  ? 350 PHE C CG  1 
ATOM   9469  C  CD1 . PHE C 1 350 ? 24.388  -54.355 12.166  1.00 20.96  ? 350 PHE C CD1 1 
ATOM   9470  C  CD2 . PHE C 1 350 ? 24.718  -55.773 14.063  1.00 22.70  ? 350 PHE C CD2 1 
ATOM   9471  C  CE1 . PHE C 1 350 ? 24.187  -53.243 12.995  1.00 22.60  ? 350 PHE C CE1 1 
ATOM   9472  C  CE2 . PHE C 1 350 ? 24.544  -54.678 14.906  1.00 20.79  ? 350 PHE C CE2 1 
ATOM   9473  C  CZ  . PHE C 1 350 ? 24.291  -53.369 14.356  1.00 22.05  ? 350 PHE C CZ  1 
ATOM   9474  N  N   . TYR C 1 351 ? 24.089  -59.727 10.437  1.00 23.26  ? 351 TYR C N   1 
ATOM   9475  C  CA  . TYR C 1 351 ? 24.363  -60.669 9.353   1.00 26.90  ? 351 TYR C CA  1 
ATOM   9476  C  C   . TYR C 1 351 ? 23.197  -61.583 9.033   1.00 27.36  ? 351 TYR C C   1 
ATOM   9477  O  O   . TYR C 1 351 ? 22.983  -61.924 7.872   1.00 26.19  ? 351 TYR C O   1 
ATOM   9478  C  CB  . TYR C 1 351 ? 25.547  -61.569 9.705   1.00 27.08  ? 351 TYR C CB  1 
ATOM   9479  C  CG  . TYR C 1 351 ? 26.689  -60.811 10.269  1.00 24.75  ? 351 TYR C CG  1 
ATOM   9480  C  CD1 . TYR C 1 351 ? 27.427  -59.943 9.461   1.00 24.86  ? 351 TYR C CD1 1 
ATOM   9481  C  CD2 . TYR C 1 351 ? 26.977  -60.861 11.635  1.00 24.27  ? 351 TYR C CD2 1 
ATOM   9482  C  CE1 . TYR C 1 351 ? 28.467  -59.197 9.984   1.00 25.54  ? 351 TYR C CE1 1 
ATOM   9483  C  CE2 . TYR C 1 351 ? 28.062  -60.157 12.172  1.00 24.80  ? 351 TYR C CE2 1 
ATOM   9484  C  CZ  . TYR C 1 351 ? 28.775  -59.276 11.347  1.00 26.45  ? 351 TYR C CZ  1 
ATOM   9485  O  OH  . TYR C 1 351 ? 29.850  -58.562 11.861  1.00 27.16  ? 351 TYR C OH  1 
ATOM   9486  N  N   . ASP C 1 352 ? 22.482  -62.044 10.032  1.00 25.93  ? 352 ASP C N   1 
ATOM   9487  C  CA  . ASP C 1 352 ? 21.439  -63.054 9.839   1.00 25.57  ? 352 ASP C CA  1 
ATOM   9488  C  C   . ASP C 1 352 ? 20.303  -62.820 10.836  1.00 26.03  ? 352 ASP C C   1 
ATOM   9489  O  O   . ASP C 1 352 ? 20.480  -63.113 12.020  1.00 26.03  ? 352 ASP C O   1 
ATOM   9490  C  CB  . ASP C 1 352 ? 22.055  -64.444 10.035  1.00 27.61  ? 352 ASP C CB  1 
ATOM   9491  C  CG  . ASP C 1 352 ? 21.091  -65.562 9.785   1.00 31.49  ? 352 ASP C CG  1 
ATOM   9492  O  OD1 . ASP C 1 352 ? 19.881  -65.317 9.591   1.00 28.79  ? 352 ASP C OD1 1 
ATOM   9493  O  OD2 . ASP C 1 352 ? 21.572  -66.722 9.774   1.00 32.29  ? 352 ASP C OD2 1 
ATOM   9494  N  N   . PRO C 1 353 ? 19.130  -62.343 10.392  1.00 28.22  ? 353 PRO C N   1 
ATOM   9495  C  CA  . PRO C 1 353 ? 18.051  -62.048 11.349  1.00 30.18  ? 353 PRO C CA  1 
ATOM   9496  C  C   . PRO C 1 353 ? 17.582  -63.282 12.073  1.00 27.72  ? 353 PRO C C   1 
ATOM   9497  O  O   . PRO C 1 353 ? 17.097  -63.154 13.205  1.00 26.26  ? 353 PRO C O   1 
ATOM   9498  C  CB  . PRO C 1 353 ? 16.911  -61.496 10.477  1.00 28.84  ? 353 PRO C CB  1 
ATOM   9499  C  CG  . PRO C 1 353 ? 17.151  -62.226 9.083   1.00 34.93  ? 353 PRO C CG  1 
ATOM   9500  C  CD  . PRO C 1 353 ? 18.673  -62.286 8.976   1.00 31.19  ? 353 PRO C CD  1 
ATOM   9501  N  N   . THR C 1 354 ? 17.683  -64.454 11.442  1.00 24.77  ? 354 THR C N   1 
ATOM   9502  C  CA  . THR C 1 354 ? 17.207  -65.673 12.111  1.00 27.40  ? 354 THR C CA  1 
ATOM   9503  C  C   . THR C 1 354 ? 18.014  -65.986 13.360  1.00 29.85  ? 354 THR C C   1 
ATOM   9504  O  O   . THR C 1 354 ? 17.502  -66.646 14.269  1.00 25.90  ? 354 THR C O   1 
ATOM   9505  C  CB  . THR C 1 354 ? 17.228  -66.900 11.180  1.00 31.00  ? 354 THR C CB  1 
ATOM   9506  O  OG1 . THR C 1 354 ? 18.564  -67.327 10.923  1.00 29.88  ? 354 THR C OG1 1 
ATOM   9507  C  CG2 . THR C 1 354 ? 16.528  -66.611 9.888   1.00 30.44  ? 354 THR C CG2 1 
ATOM   9508  N  N   . ILE C 1 355 ? 19.290  -65.569 13.424  1.00 27.12  ? 355 ILE C N   1 
ATOM   9509  C  CA  . ILE C 1 355 ? 19.987  -65.779 14.683  1.00 27.08  ? 355 ILE C CA  1 
ATOM   9510  C  C   . ILE C 1 355 ? 19.266  -65.035 15.811  1.00 24.42  ? 355 ILE C C   1 
ATOM   9511  O  O   . ILE C 1 355 ? 19.097  -65.550 16.921  1.00 25.86  ? 355 ILE C O   1 
ATOM   9512  C  CB  . ILE C 1 355 ? 21.461  -65.363 14.554  1.00 26.51  ? 355 ILE C CB  1 
ATOM   9513  C  CG1 . ILE C 1 355 ? 22.146  -66.188 13.452  1.00 28.27  ? 355 ILE C CG1 1 
ATOM   9514  C  CG2 . ILE C 1 355 ? 22.150  -65.520 15.865  1.00 26.05  ? 355 ILE C CG2 1 
ATOM   9515  C  CD1 . ILE C 1 355 ? 23.631  -65.770 13.230  1.00 26.52  ? 355 ILE C CD1 1 
ATOM   9516  N  N   . LYS C 1 356 ? 18.855  -63.805 15.555  1.00 24.72  ? 356 LYS C N   1 
ATOM   9517  C  CA  . LYS C 1 356 ? 18.117  -63.052 16.555  1.00 24.72  ? 356 LYS C CA  1 
ATOM   9518  C  C   . LYS C 1 356 ? 16.717  -63.622 16.786  1.00 28.44  ? 356 LYS C C   1 
ATOM   9519  O  O   . LYS C 1 356 ? 16.209  -63.601 17.924  1.00 28.73  ? 356 LYS C O   1 
ATOM   9520  C  CB  . LYS C 1 356 ? 18.055  -61.569 16.146  1.00 24.21  ? 356 LYS C CB  1 
ATOM   9521  C  CG  . LYS C 1 356 ? 17.283  -60.789 17.189  1.00 24.16  ? 356 LYS C CG  1 
ATOM   9522  C  CD  . LYS C 1 356 ? 17.422  -59.296 16.893  1.00 27.75  ? 356 LYS C CD  1 
ATOM   9523  C  CE  . LYS C 1 356 ? 16.577  -58.461 17.782  1.00 32.02  ? 356 LYS C CE  1 
ATOM   9524  N  NZ  . LYS C 1 356 ? 15.741  -57.464 17.074  1.00 30.75  ? 356 LYS C NZ  1 
ATOM   9525  N  N   . SER C 1 357 ? 16.057  -64.090 15.736  1.00 26.65  ? 357 SER C N   1 
ATOM   9526  C  CA  . SER C 1 357 ? 14.754  -64.723 15.935  1.00 26.47  ? 357 SER C CA  1 
ATOM   9527  C  C   . SER C 1 357 ? 14.898  -65.877 16.903  1.00 29.07  ? 357 SER C C   1 
ATOM   9528  O  O   . SER C 1 357 ? 14.118  -66.007 17.850  1.00 24.84  ? 357 SER C O   1 
ATOM   9529  C  CB  . SER C 1 357 ? 14.187  -65.257 14.618  1.00 25.38  ? 357 SER C CB  1 
ATOM   9530  O  OG  . SER C 1 357 ? 13.836  -64.222 13.718  1.00 29.10  ? 357 SER C OG  1 
ATOM   9531  N  N   . ASP C 1 358 ? 15.926  -66.713 16.683  1.00 26.90  ? 358 ASP C N   1 
ATOM   9532  C  CA  . ASP C 1 358 ? 16.133  -67.864 17.568  1.00 28.21  ? 358 ASP C CA  1 
ATOM   9533  C  C   . ASP C 1 358 ? 16.451  -67.400 18.990  1.00 29.79  ? 358 ASP C C   1 
ATOM   9534  O  O   . ASP C 1 358 ? 15.931  -67.951 19.984  1.00 24.93  ? 358 ASP C O   1 
ATOM   9535  C  CB  . ASP C 1 358 ? 17.255  -68.735 17.037  1.00 27.90  ? 358 ASP C CB  1 
ATOM   9536  C  CG  . ASP C 1 358 ? 16.895  -69.487 15.774  1.00 32.78  ? 358 ASP C CG  1 
ATOM   9537  O  OD1 . ASP C 1 358 ? 15.693  -69.654 15.456  1.00 32.57  ? 358 ASP C OD1 1 
ATOM   9538  O  OD2 . ASP C 1 358 ? 17.859  -69.979 15.128  1.00 34.18  ? 358 ASP C OD2 1 
ATOM   9539  N  N   . MET C 1 359 ? 17.294  -66.363 19.123  1.00 25.76  ? 359 MET C N   1 
ATOM   9540  C  CA  . MET C 1 359 ? 17.569  -65.865 20.463  1.00 25.40  ? 359 MET C CA  1 
ATOM   9541  C  C   . MET C 1 359 ? 16.313  -65.360 21.160  1.00 25.16  ? 359 MET C C   1 
ATOM   9542  O  O   . MET C 1 359 ? 16.145  -65.567 22.377  1.00 25.09  ? 359 MET C O   1 
ATOM   9543  C  CB  . MET C 1 359 ? 18.592  -64.724 20.489  1.00 26.33  ? 359 MET C CB  1 
ATOM   9544  C  CG  . MET C 1 359 ? 20.051  -65.121 20.500  1.00 28.53  ? 359 MET C CG  1 
ATOM   9545  S  SD  . MET C 1 359 ? 21.049  -63.831 19.739  1.00 27.58  ? 359 MET C SD  1 
ATOM   9546  C  CE  . MET C 1 359 ? 22.635  -64.608 19.647  1.00 28.41  ? 359 MET C CE  1 
ATOM   9547  N  N   . MET C 1 360 ? 15.463  -64.618 20.444  1.00 27.15  ? 360 MET C N   1 
ATOM   9548  C  CA  . MET C 1 360 ? 14.207  -64.130 21.039  1.00 26.65  ? 360 MET C CA  1 
ATOM   9549  C  C   . MET C 1 360 ? 13.304  -65.266 21.473  1.00 26.41  ? 360 MET C C   1 
ATOM   9550  O  O   . MET C 1 360 ? 12.798  -65.240 22.604  1.00 26.82  ? 360 MET C O   1 
ATOM   9551  C  CB  . MET C 1 360 ? 13.498  -63.122 20.115  1.00 24.96  ? 360 MET C CB  1 
ATOM   9552  C  CG  . MET C 1 360 ? 14.400  -62.038 19.720  1.00 27.93  ? 360 MET C CG  1 
ATOM   9553  S  SD  . MET C 1 360 ? 13.646  -60.863 18.566  1.00 30.11  ? 360 MET C SD  1 
ATOM   9554  C  CE  . MET C 1 360 ? 12.526  -59.859 19.523  1.00 32.11  ? 360 MET C CE  1 
ATOM   9555  N  N   . LEU C 1 361 ? 13.160  -66.305 20.639  1.00 24.48  ? 361 LEU C N   1 
ATOM   9556  C  CA  . LEU C 1 361 ? 12.314  -67.455 20.970  1.00 27.11  ? 361 LEU C CA  1 
ATOM   9557  C  C   . LEU C 1 361 ? 12.873  -68.191 22.191  1.00 29.29  ? 361 LEU C C   1 
ATOM   9558  O  O   . LEU C 1 361 ? 12.106  -68.676 23.040  1.00 27.20  ? 361 LEU C O   1 
ATOM   9559  C  CB  . LEU C 1 361 ? 12.203  -68.416 19.768  1.00 28.02  ? 361 LEU C CB  1 
ATOM   9560  C  CG  . LEU C 1 361 ? 11.467  -67.878 18.528  1.00 30.22  ? 361 LEU C CG  1 
ATOM   9561  C  CD1 . LEU C 1 361 ? 11.671  -68.749 17.258  1.00 29.92  ? 361 LEU C CD1 1 
ATOM   9562  C  CD2 . LEU C 1 361 ? 10.000  -67.751 18.814  1.00 32.50  ? 361 LEU C CD2 1 
ATOM   9563  N  N   . ARG C 1 362 ? 14.212  -68.247 22.301  1.00 24.28  ? 362 ARG C N   1 
ATOM   9564  C  CA  . ARG C 1 362 ? 14.855  -68.840 23.463  1.00 26.65  ? 362 ARG C CA  1 
ATOM   9565  C  C   . ARG C 1 362 ? 14.609  -67.996 24.710  1.00 27.16  ? 362 ARG C C   1 
ATOM   9566  O  O   . ARG C 1 362 ? 14.322  -68.522 25.771  1.00 26.99  ? 362 ARG C O   1 
ATOM   9567  C  CB  . ARG C 1 362 ? 16.348  -68.984 23.197  1.00 28.27  ? 362 ARG C CB  1 
ATOM   9568  C  CG  . ARG C 1 362 ? 17.047  -69.806 24.249  1.00 26.48  ? 362 ARG C CG  1 
ATOM   9569  C  CD  . ARG C 1 362 ? 18.528  -69.696 24.110  1.00 25.52  ? 362 ARG C CD  1 
ATOM   9570  N  NE  . ARG C 1 362 ? 19.268  -70.595 24.977  1.00 25.06  ? 362 ARG C NE  1 
ATOM   9571  C  CZ  . ARG C 1 362 ? 20.564  -70.852 24.843  1.00 26.42  ? 362 ARG C CZ  1 
ATOM   9572  N  NH1 . ARG C 1 362 ? 21.274  -70.330 23.858  1.00 26.01  ? 362 ARG C NH1 1 
ATOM   9573  N  NH2 . ARG C 1 362 ? 21.149  -71.713 25.682  1.00 27.76  ? 362 ARG C NH2 1 
ATOM   9574  N  N   . ILE C 1 363 ? 14.659  -66.684 24.589  1.00 24.92  ? 363 ILE C N   1 
ATOM   9575  C  CA  . ILE C 1 363 ? 14.378  -65.890 25.777  1.00 23.73  ? 363 ILE C CA  1 
ATOM   9576  C  C   . ILE C 1 363 ? 12.929  -66.087 26.219  1.00 26.35  ? 363 ILE C C   1 
ATOM   9577  O  O   . ILE C 1 363 ? 12.648  -66.238 27.413  1.00 26.92  ? 363 ILE C O   1 
ATOM   9578  C  CB  . ILE C 1 363 ? 14.695  -64.406 25.525  1.00 23.76  ? 363 ILE C CB  1 
ATOM   9579  C  CG1 . ILE C 1 363 ? 16.210  -64.171 25.415  1.00 21.87  ? 363 ILE C CG1 1 
ATOM   9580  C  CG2 . ILE C 1 363 ? 14.133  -63.579 26.672  1.00 27.48  ? 363 ILE C CG2 1 
ATOM   9581  C  CD1 . ILE C 1 363 ? 16.585  -62.752 24.753  1.00 25.65  ? 363 ILE C CD1 1 
ATOM   9582  N  N   . ILE C 1 364 ? 11.987  -66.095 25.266  1.00 28.41  ? 364 ILE C N   1 
ATOM   9583  C  CA  . ILE C 1 364 ? 10.581  -66.323 25.606  1.00 28.93  ? 364 ILE C CA  1 
ATOM   9584  C  C   . ILE C 1 364 ? 10.431  -67.620 26.397  1.00 29.43  ? 364 ILE C C   1 
ATOM   9585  O  O   . ILE C 1 364 ? 9.691   -67.685 27.384  1.00 28.53  ? 364 ILE C O   1 
ATOM   9586  C  CB  . ILE C 1 364 ? 9.728   -66.326 24.336  1.00 27.09  ? 364 ILE C CB  1 
ATOM   9587  C  CG1 . ILE C 1 364 ? 9.687   -64.889 23.765  1.00 28.25  ? 364 ILE C CG1 1 
ATOM   9588  C  CG2 . ILE C 1 364 ? 8.333   -66.894 24.618  1.00 31.90  ? 364 ILE C CG2 1 
ATOM   9589  C  CD1 . ILE C 1 364 ? 9.270   -64.845 22.316  1.00 27.83  ? 364 ILE C CD1 1 
ATOM   9590  N  N   . LYS C 1 365 ? 11.148  -68.655 25.981  1.00 28.24  ? 365 LYS C N   1 
ATOM   9591  C  CA  . LYS C 1 365 ? 11.056  -69.970 26.622  1.00 27.95  ? 365 LYS C CA  1 
ATOM   9592  C  C   . LYS C 1 365 ? 11.650  -69.922 28.024  1.00 28.71  ? 365 LYS C C   1 
ATOM   9593  O  O   . LYS C 1 365 ? 10.976  -70.225 29.008  1.00 30.81  ? 365 LYS C O   1 
ATOM   9594  C  CB  . LYS C 1 365 ? 11.794  -70.994 25.756  1.00 27.86  ? 365 LYS C CB  1 
ATOM   9595  C  CG  . LYS C 1 365 ? 11.542  -72.427 26.197  1.00 33.49  ? 365 LYS C CG  1 
ATOM   9596  C  CD  . LYS C 1 365 ? 12.327  -73.399 25.361  1.00 38.88  ? 365 LYS C CD  1 
ATOM   9597  C  CE  . LYS C 1 365 ? 13.678  -73.719 25.953  1.00 44.91  ? 365 LYS C CE  1 
ATOM   9598  N  NZ  . LYS C 1 365 ? 13.670  -75.161 26.375  1.00 49.28  ? 365 LYS C NZ  1 
ATOM   9599  N  N   . GLU C 1 366 ? 12.928  -69.551 28.125  1.00 25.87  ? 366 GLU C N   1 
ATOM   9600  C  CA  . GLU C 1 366 ? 13.622  -69.691 29.394  1.00 26.97  ? 366 GLU C CA  1 
ATOM   9601  C  C   . GLU C 1 366 ? 13.136  -68.675 30.410  1.00 29.26  ? 366 GLU C C   1 
ATOM   9602  O  O   . GLU C 1 366 ? 13.147  -68.954 31.622  1.00 28.48  ? 366 GLU C O   1 
ATOM   9603  C  CB  . GLU C 1 366 ? 15.132  -69.550 29.153  1.00 25.89  ? 366 GLU C CB  1 
ATOM   9604  C  CG  . GLU C 1 366 ? 15.700  -70.665 28.201  1.00 26.99  ? 366 GLU C CG  1 
ATOM   9605  C  CD  . GLU C 1 366 ? 17.239  -70.723 28.157  1.00 26.69  ? 366 GLU C CD  1 
ATOM   9606  O  OE1 . GLU C 1 366 ? 17.948  -70.056 28.961  1.00 28.43  ? 366 GLU C OE1 1 
ATOM   9607  O  OE2 . GLU C 1 366 ? 17.760  -71.412 27.242  1.00 28.74  ? 366 GLU C OE2 1 
ATOM   9608  N  N   . TRP C 1 367 ? 12.769  -67.467 29.955  1.00 24.28  ? 367 TRP C N   1 
ATOM   9609  C  CA  . TRP C 1 367 ? 12.267  -66.448 30.864  1.00 26.32  ? 367 TRP C CA  1 
ATOM   9610  C  C   . TRP C 1 367 ? 10.761  -66.520 31.072  1.00 27.08  ? 367 TRP C C   1 
ATOM   9611  O  O   . TRP C 1 367 ? 10.214  -65.683 31.800  1.00 26.28  ? 367 TRP C O   1 
ATOM   9612  C  CB  . TRP C 1 367 ? 12.676  -65.045 30.391  1.00 26.52  ? 367 TRP C CB  1 
ATOM   9613  C  CG  . TRP C 1 367 ? 14.048  -64.695 30.853  1.00 24.22  ? 367 TRP C CG  1 
ATOM   9614  C  CD1 . TRP C 1 367 ? 14.388  -63.921 31.948  1.00 26.23  ? 367 TRP C CD1 1 
ATOM   9615  C  CD2 . TRP C 1 367 ? 15.285  -65.057 30.226  1.00 23.21  ? 367 TRP C CD2 1 
ATOM   9616  N  NE1 . TRP C 1 367 ? 15.769  -63.783 32.029  1.00 24.08  ? 367 TRP C NE1 1 
ATOM   9617  C  CE2 . TRP C 1 367 ? 16.334  -64.474 30.985  1.00 26.31  ? 367 TRP C CE2 1 
ATOM   9618  C  CE3 . TRP C 1 367 ? 15.617  -65.794 29.056  1.00 23.77  ? 367 TRP C CE3 1 
ATOM   9619  C  CZ2 . TRP C 1 367 ? 17.699  -64.644 30.643  1.00 26.57  ? 367 TRP C CZ2 1 
ATOM   9620  C  CZ3 . TRP C 1 367 ? 16.963  -65.928 28.708  1.00 25.27  ? 367 TRP C CZ3 1 
ATOM   9621  C  CH2 . TRP C 1 367 ? 17.985  -65.383 29.507  1.00 22.52  ? 367 TRP C CH2 1 
ATOM   9622  N  N   . GLN C 1 368 ? 10.093  -67.530 30.519  1.00 27.10  ? 368 GLN C N   1 
ATOM   9623  C  CA  . GLN C 1 368 ? 8.677   -67.806 30.783  1.00 29.95  ? 368 GLN C CA  1 
ATOM   9624  C  C   . GLN C 1 368 ? 7.812   -66.605 30.417  1.00 30.68  ? 368 GLN C C   1 
ATOM   9625  O  O   . GLN C 1 368 ? 7.028   -66.097 31.229  1.00 30.53  ? 368 GLN C O   1 
ATOM   9626  C  CB  . GLN C 1 368 ? 8.439   -68.212 32.242  1.00 33.54  ? 368 GLN C CB  1 
ATOM   9627  C  CG  . GLN C 1 368 ? 9.410   -69.232 32.768  1.00 35.33  ? 368 GLN C CG  1 
ATOM   9628  C  CD  . GLN C 1 368 ? 8.964   -69.805 34.131  1.00 38.29  ? 368 GLN C CD  1 
ATOM   9629  O  OE1 . GLN C 1 368 ? 7.944   -70.472 34.237  1.00 39.93  ? 368 GLN C OE1 1 
ATOM   9630  N  NE2 . GLN C 1 368 ? 9.704   -69.472 35.174  1.00 41.29  ? 368 GLN C NE2 1 
ATOM   9631  N  N   . VAL C 1 369 ? 7.960   -66.164 29.171  1.00 27.64  ? 369 VAL C N   1 
ATOM   9632  C  CA  . VAL C 1 369 ? 7.334   -64.952 28.666  1.00 29.35  ? 369 VAL C CA  1 
ATOM   9633  C  C   . VAL C 1 369 ? 5.966   -65.290 28.094  1.00 30.87  ? 369 VAL C C   1 
ATOM   9634  O  O   . VAL C 1 369 ? 5.819   -66.254 27.341  1.00 28.97  ? 369 VAL C O   1 
ATOM   9635  C  CB  . VAL C 1 369 ? 8.216   -64.287 27.595  1.00 29.24  ? 369 VAL C CB  1 
ATOM   9636  C  CG1 . VAL C 1 369 ? 7.435   -63.128 26.951  1.00 28.36  ? 369 VAL C CG1 1 
ATOM   9637  C  CG2 . VAL C 1 369 ? 9.562   -63.801 28.210  1.00 31.12  ? 369 VAL C CG2 1 
ATOM   9638  N  N   . ASP C 1 370 ? 4.970   -64.474 28.445  1.00 29.37  ? 370 ASP C N   1 
ATOM   9639  C  CA  . ASP C 1 370 ? 3.586   -64.582 27.989  1.00 34.42  ? 370 ASP C CA  1 
ATOM   9640  C  C   . ASP C 1 370 ? 3.281   -63.753 26.751  1.00 33.94  ? 370 ASP C C   1 
ATOM   9641  O  O   . ASP C 1 370 ? 2.341   -64.087 26.013  1.00 31.88  ? 370 ASP C O   1 
ATOM   9642  C  CB  . ASP C 1 370 ? 2.655   -64.152 29.124  1.00 32.72  ? 370 ASP C CB  1 
ATOM   9643  C  CG  . ASP C 1 370 ? 2.909   -64.935 30.426  1.00 37.53  ? 370 ASP C CG  1 
ATOM   9644  O  OD1 . ASP C 1 370 ? 2.968   -66.182 30.340  1.00 40.90  ? 370 ASP C OD1 1 
ATOM   9645  O  OD2 . ASP C 1 370 ? 3.107   -64.309 31.503  1.00 34.49  ? 370 ASP C OD2 1 
ATOM   9646  N  N   . GLY C 1 371 ? 4.005   -62.664 26.513  1.00 30.63  ? 371 GLY C N   1 
ATOM   9647  C  CA  . GLY C 1 371 ? 3.730   -61.826 25.355  1.00 31.57  ? 371 GLY C CA  1 
ATOM   9648  C  C   . GLY C 1 371 ? 4.888   -60.902 25.064  1.00 29.85  ? 371 GLY C C   1 
ATOM   9649  O  O   . GLY C 1 371 ? 5.707   -60.618 25.940  1.00 28.10  ? 371 GLY C O   1 
ATOM   9650  N  N   . VAL C 1 372 ? 4.992   -60.468 23.799  1.00 28.94  ? 372 VAL C N   1 
ATOM   9651  C  CA  . VAL C 1 372 ? 6.130   -59.675 23.357  1.00 29.42  ? 372 VAL C CA  1 
ATOM   9652  C  C   . VAL C 1 372 ? 5.611   -58.362 22.786  1.00 30.78  ? 372 VAL C C   1 
ATOM   9653  O  O   . VAL C 1 372 ? 4.619   -58.359 22.049  1.00 31.41  ? 372 VAL C O   1 
ATOM   9654  C  CB  . VAL C 1 372 ? 6.954   -60.458 22.305  1.00 32.52  ? 372 VAL C CB  1 
ATOM   9655  C  CG1 . VAL C 1 372 ? 8.160   -59.632 21.815  1.00 32.39  ? 372 VAL C CG1 1 
ATOM   9656  C  CG2 . VAL C 1 372 ? 7.407   -61.814 22.854  1.00 31.25  ? 372 VAL C CG2 1 
ATOM   9657  N  N   . MET C 1 373 ? 6.279   -57.244 23.131  1.00 29.47  ? 373 MET C N   1 
ATOM   9658  C  CA  . MET C 1 373 ? 5.982   -55.905 22.606  1.00 32.55  ? 373 MET C CA  1 
ATOM   9659  C  C   . MET C 1 373 ? 7.233   -55.498 21.832  1.00 31.47  ? 373 MET C C   1 
ATOM   9660  O  O   . MET C 1 373 ? 8.304   -55.373 22.439  1.00 32.86  ? 373 MET C O   1 
ATOM   9661  C  CB  . MET C 1 373 ? 5.746   -54.937 23.764  1.00 29.82  ? 373 MET C CB  1 
ATOM   9662  C  CG  . MET C 1 373 ? 4.743   -55.406 24.783  1.00 34.32  ? 373 MET C CG  1 
ATOM   9663  S  SD  . MET C 1 373 ? 4.138   -54.040 25.818  1.00 39.47  ? 373 MET C SD  1 
ATOM   9664  C  CE  . MET C 1 373 ? 5.643   -53.825 26.758  1.00 42.74  ? 373 MET C CE  1 
ATOM   9665  N  N   . LEU C 1 374 ? 7.136   -55.369 20.502  1.00 28.91  ? 374 LEU C N   1 
ATOM   9666  C  CA  . LEU C 1 374 ? 8.283   -55.065 19.650  1.00 30.50  ? 374 LEU C CA  1 
ATOM   9667  C  C   . LEU C 1 374 ? 8.228   -53.593 19.245  1.00 29.62  ? 374 LEU C C   1 
ATOM   9668  O  O   . LEU C 1 374 ? 7.260   -53.165 18.624  1.00 28.97  ? 374 LEU C O   1 
ATOM   9669  C  CB  . LEU C 1 374 ? 8.243   -55.913 18.386  1.00 30.56  ? 374 LEU C CB  1 
ATOM   9670  C  CG  . LEU C 1 374 ? 8.465   -57.412 18.543  1.00 35.93  ? 374 LEU C CG  1 
ATOM   9671  C  CD1 . LEU C 1 374 ? 8.433   -58.057 17.135  1.00 33.73  ? 374 LEU C CD1 1 
ATOM   9672  C  CD2 . LEU C 1 374 ? 9.758   -57.731 19.266  1.00 33.44  ? 374 LEU C CD2 1 
ATOM   9673  N  N   . HIS C 1 375 ? 9.268   -52.843 19.566  1.00 28.70  ? 375 HIS C N   1 
ATOM   9674  C  CA  . HIS C 1 375 ? 9.409   -51.458 19.136  1.00 30.26  ? 375 HIS C CA  1 
ATOM   9675  C  C   . HIS C 1 375 ? 9.983   -51.461 17.729  1.00 28.88  ? 375 HIS C C   1 
ATOM   9676  O  O   . HIS C 1 375 ? 11.096  -51.955 17.523  1.00 30.60  ? 375 HIS C O   1 
ATOM   9677  C  CB  . HIS C 1 375 ? 10.339  -50.745 20.110  1.00 29.16  ? 375 HIS C CB  1 
ATOM   9678  C  CG  . HIS C 1 375 ? 10.600  -49.315 19.780  1.00 29.59  ? 375 HIS C CG  1 
ATOM   9679  N  ND1 . HIS C 1 375 ? 11.772  -48.690 20.144  1.00 29.94  ? 375 HIS C ND1 1 
ATOM   9680  C  CD2 . HIS C 1 375 ? 9.871   -48.406 19.087  1.00 29.05  ? 375 HIS C CD2 1 
ATOM   9681  C  CE1 . HIS C 1 375 ? 11.737  -47.431 19.713  1.00 31.07  ? 375 HIS C CE1 1 
ATOM   9682  N  NE2 . HIS C 1 375 ? 10.591  -47.226 19.080  1.00 29.49  ? 375 HIS C NE2 1 
ATOM   9683  N  N   . LEU C 1 376 ? 9.224   -50.946 16.754  1.00 26.64  ? 376 LEU C N   1 
ATOM   9684  C  CA  . LEU C 1 376 ? 9.722   -50.742 15.395  1.00 26.34  ? 376 LEU C CA  1 
ATOM   9685  C  C   . LEU C 1 376 ? 10.370  -49.372 15.435  1.00 30.10  ? 376 LEU C C   1 
ATOM   9686  O  O   . LEU C 1 376 ? 9.680   -48.348 15.363  1.00 29.16  ? 376 LEU C O   1 
ATOM   9687  C  CB  . LEU C 1 376 ? 8.616   -50.822 14.344  1.00 28.06  ? 376 LEU C CB  1 
ATOM   9688  C  CG  . LEU C 1 376 ? 7.747   -52.096 14.488  1.00 30.88  ? 376 LEU C CG  1 
ATOM   9689  C  CD1 . LEU C 1 376 ? 6.562   -52.145 13.511  1.00 32.81  ? 376 LEU C CD1 1 
ATOM   9690  C  CD2 . LEU C 1 376 ? 8.584   -53.406 14.389  1.00 30.40  ? 376 LEU C CD2 1 
ATOM   9691  N  N   . ASN C 1 377 ? 11.685  -49.357 15.647  1.00 24.82  ? 377 ASN C N   1 
ATOM   9692  C  CA  . ASN C 1 377 ? 12.382  -48.140 16.115  1.00 25.14  ? 377 ASN C CA  1 
ATOM   9693  C  C   . ASN C 1 377 ? 12.955  -47.412 14.892  1.00 24.72  ? 377 ASN C C   1 
ATOM   9694  O  O   . ASN C 1 377 ? 14.006  -47.775 14.346  1.00 24.38  ? 377 ASN C O   1 
ATOM   9695  C  CB  . ASN C 1 377 ? 13.453  -48.521 17.134  1.00 28.50  ? 377 ASN C CB  1 
ATOM   9696  C  CG  . ASN C 1 377 ? 14.249  -47.326 17.627  1.00 25.71  ? 377 ASN C CG  1 
ATOM   9697  O  OD1 . ASN C 1 377 ? 13.897  -46.138 17.361  1.00 25.83  ? 377 ASN C OD1 1 
ATOM   9698  N  ND2 . ASN C 1 377 ? 15.318  -47.622 18.380  1.00 27.65  ? 377 ASN C ND2 1 
ATOM   9699  N  N   . ARG C 1 378 ? 12.240  -46.379 14.452  1.00 26.13  ? 378 ARG C N   1 
ATOM   9700  C  CA  . ARG C 1 378 ? 12.650  -45.602 13.293  1.00 25.32  ? 378 ARG C CA  1 
ATOM   9701  C  C   . ARG C 1 378 ? 13.914  -44.796 13.572  1.00 25.84  ? 378 ARG C C   1 
ATOM   9702  O  O   . ARG C 1 378 ? 14.468  -44.230 12.642  1.00 26.84  ? 378 ARG C O   1 
ATOM   9703  C  CB  . ARG C 1 378 ? 11.561  -44.620 12.848  1.00 28.90  ? 378 ARG C CB  1 
ATOM   9704  C  CG  . ARG C 1 378 ? 10.243  -45.259 12.507  1.00 31.55  ? 378 ARG C CG  1 
ATOM   9705  C  CD  . ARG C 1 378 ? 9.242   -44.187 12.102  1.00 36.16  ? 378 ARG C CD  1 
ATOM   9706  N  NE  . ARG C 1 378 ? 8.077   -44.799 11.476  1.00 36.62  ? 378 ARG C NE  1 
ATOM   9707  C  CZ  . ARG C 1 378 ? 7.985   -45.107 10.191  1.00 40.16  ? 378 ARG C CZ  1 
ATOM   9708  N  NH1 . ARG C 1 378 ? 8.977   -44.860 9.346   1.00 38.35  ? 378 ARG C NH1 1 
ATOM   9709  N  NH2 . ARG C 1 378 ? 6.861   -45.661 9.741   1.00 38.68  ? 378 ARG C NH2 1 
ATOM   9710  N  N   . GLY C 1 379 ? 14.351  -44.705 14.826  1.00 27.21  ? 379 GLY C N   1 
ATOM   9711  C  CA  . GLY C 1 379 ? 15.524  -43.905 15.101  1.00 24.38  ? 379 GLY C CA  1 
ATOM   9712  C  C   . GLY C 1 379 ? 16.825  -44.625 15.088  1.00 25.72  ? 379 GLY C C   1 
ATOM   9713  O  O   . GLY C 1 379 ? 17.850  -43.984 15.317  1.00 25.85  ? 379 GLY C O   1 
ATOM   9714  N  N   . CYS C 1 380 ? 16.849  -45.930 14.736  1.00 24.58  ? 380 CYS C N   1 
ATOM   9715  C  CA  . CYS C 1 380 ? 18.051  -46.751 14.874  1.00 23.11  ? 380 CYS C CA  1 
ATOM   9716  C  C   . CYS C 1 380 ? 18.041  -47.842 13.784  1.00 23.86  ? 380 CYS C C   1 
ATOM   9717  O  O   . CYS C 1 380 ? 17.468  -48.917 14.010  1.00 24.43  ? 380 CYS C O   1 
ATOM   9718  C  CB  . CYS C 1 380 ? 18.092  -47.382 16.261  1.00 28.30  ? 380 CYS C CB  1 
ATOM   9719  S  SG  . CYS C 1 380 ? 19.495  -48.525 16.556  1.00 25.34  ? 380 CYS C SG  1 
ATOM   9720  N  N   . GLU C 1 381 ? 18.739  -47.608 12.660  1.00 24.33  ? 381 GLU C N   1 
ATOM   9721  C  CA  . GLU C 1 381 ? 18.804  -48.656 11.620  1.00 25.60  ? 381 GLU C CA  1 
ATOM   9722  C  C   . GLU C 1 381 ? 19.534  -49.896 12.146  1.00 25.84  ? 381 GLU C C   1 
ATOM   9723  O  O   . GLU C 1 381 ? 19.155  -51.028 11.822  1.00 22.95  ? 381 GLU C O   1 
ATOM   9724  C  CB  . GLU C 1 381 ? 19.500  -48.112 10.344  1.00 25.72  ? 381 GLU C CB  1 
ATOM   9725  C  CG  . GLU C 1 381 ? 20.953  -47.599 10.556  1.00 27.01  ? 381 GLU C CG  1 
ATOM   9726  C  CD  . GLU C 1 381 ? 21.852  -47.613 9.284   1.00 26.94  ? 381 GLU C CD  1 
ATOM   9727  O  OE1 . GLU C 1 381 ? 21.538  -48.334 8.294   1.00 26.21  ? 381 GLU C OE1 1 
ATOM   9728  O  OE2 . GLU C 1 381 ? 22.839  -46.797 9.272   1.00 27.30  ? 381 GLU C OE2 1 
ATOM   9729  N  N   . GLY C 1 382 ? 20.571  -49.723 12.964  1.00 24.99  ? 382 GLY C N   1 
ATOM   9730  C  CA  . GLY C 1 382 ? 21.438  -50.862 13.285  1.00 23.67  ? 382 GLY C CA  1 
ATOM   9731  C  C   . GLY C 1 382 ? 20.746  -51.933 14.103  1.00 23.61  ? 382 GLY C C   1 
ATOM   9732  O  O   . GLY C 1 382 ? 20.937  -53.135 13.858  1.00 25.12  ? 382 GLY C O   1 
ATOM   9733  N  N   . LEU C 1 383 ? 19.937  -51.528 15.093  1.00 24.84  ? 383 LEU C N   1 
ATOM   9734  C  CA  . LEU C 1 383 ? 19.252  -52.510 15.927  1.00 24.47  ? 383 LEU C CA  1 
ATOM   9735  C  C   . LEU C 1 383 ? 17.888  -52.891 15.373  1.00 25.57  ? 383 LEU C C   1 
ATOM   9736  O  O   . LEU C 1 383 ? 17.300  -53.895 15.828  1.00 25.83  ? 383 LEU C O   1 
ATOM   9737  C  CB  . LEU C 1 383 ? 19.106  -52.003 17.368  1.00 24.17  ? 383 LEU C CB  1 
ATOM   9738  C  CG  . LEU C 1 383 ? 20.453  -51.831 18.107  1.00 24.87  ? 383 LEU C CG  1 
ATOM   9739  C  CD1 . LEU C 1 383 ? 20.233  -51.536 19.589  1.00 26.32  ? 383 LEU C CD1 1 
ATOM   9740  C  CD2 . LEU C 1 383 ? 21.325  -53.085 17.918  1.00 25.02  ? 383 LEU C CD2 1 
ATOM   9741  N  N   . SER C 1 384 ? 17.406  -52.146 14.366  1.00 22.84  ? 384 SER C N   1 
ATOM   9742  C  CA  . SER C 1 384 ? 16.096  -52.440 13.764  1.00 25.43  ? 384 SER C CA  1 
ATOM   9743  C  C   . SER C 1 384 ? 16.168  -53.320 12.508  1.00 25.94  ? 384 SER C C   1 
ATOM   9744  O  O   . SER C 1 384 ? 15.118  -53.788 12.079  1.00 26.50  ? 384 SER C O   1 
ATOM   9745  C  CB  . SER C 1 384 ? 15.364  -51.153 13.386  1.00 27.16  ? 384 SER C CB  1 
ATOM   9746  O  OG  . SER C 1 384 ? 14.965  -50.468 14.576  1.00 26.53  ? 384 SER C OG  1 
ATOM   9747  N  N   . VAL C 1 385 ? 17.346  -53.533 11.898  1.00 25.64  ? 385 VAL C N   1 
ATOM   9748  C  CA  . VAL C 1 385 ? 17.412  -54.392 10.699  1.00 24.21  ? 385 VAL C CA  1 
ATOM   9749  C  C   . VAL C 1 385 ? 16.939  -55.776 11.084  1.00 25.93  ? 385 VAL C C   1 
ATOM   9750  O  O   . VAL C 1 385 ? 17.312  -56.305 12.141  1.00 26.90  ? 385 VAL C O   1 
ATOM   9751  C  CB  . VAL C 1 385 ? 18.813  -54.487 10.056  1.00 26.50  ? 385 VAL C CB  1 
ATOM   9752  C  CG1 . VAL C 1 385 ? 19.105  -53.191 9.260   1.00 28.35  ? 385 VAL C CG1 1 
ATOM   9753  C  CG2 . VAL C 1 385 ? 19.884  -54.680 11.077  1.00 26.90  ? 385 VAL C CG2 1 
ATOM   9754  N  N   . GLY C 1 386 ? 16.123  -56.372 10.224  1.00 27.32  ? 386 GLY C N   1 
ATOM   9755  C  CA  . GLY C 1 386 ? 15.632  -57.709 10.521  1.00 26.83  ? 386 GLY C CA  1 
ATOM   9756  C  C   . GLY C 1 386 ? 14.376  -57.746 11.370  1.00 30.56  ? 386 GLY C C   1 
ATOM   9757  O  O   . GLY C 1 386 ? 13.798  -58.824 11.554  1.00 29.34  ? 386 GLY C O   1 
ATOM   9758  N  N   . ILE C 1 387 ? 13.906  -56.605 11.883  1.00 26.23  ? 387 ILE C N   1 
ATOM   9759  C  CA  . ILE C 1 387 ? 12.896  -56.645 12.929  1.00 28.25  ? 387 ILE C CA  1 
ATOM   9760  C  C   . ILE C 1 387 ? 11.602  -57.339 12.468  1.00 27.24  ? 387 ILE C C   1 
ATOM   9761  O  O   . ILE C 1 387 ? 10.990  -58.095 13.235  1.00 33.72  ? 387 ILE C O   1 
ATOM   9762  C  CB  . ILE C 1 387 ? 12.654  -55.207 13.467  1.00 27.82  ? 387 ILE C CB  1 
ATOM   9763  C  CG1 . ILE C 1 387 ? 11.810  -55.238 14.746  1.00 31.12  ? 387 ILE C CG1 1 
ATOM   9764  C  CG2 . ILE C 1 387 ? 12.002  -54.298 12.412  1.00 25.28  ? 387 ILE C CG2 1 
ATOM   9765  C  CD1 . ILE C 1 387 ? 12.374  -56.100 15.873  1.00 34.12  ? 387 ILE C CD1 1 
ATOM   9766  N  N   . MET C 1 388 ? 11.167  -57.130 11.220  1.00 27.73  ? 388 MET C N   1 
ATOM   9767  C  CA  . MET C 1 388 ? 9.921   -57.762 10.754  1.00 29.76  ? 388 MET C CA  1 
ATOM   9768  C  C   . MET C 1 388 ? 10.063  -59.266 10.573  1.00 29.19  ? 388 MET C C   1 
ATOM   9769  O  O   . MET C 1 388 ? 9.097   -60.016 10.797  1.00 32.29  ? 388 MET C O   1 
ATOM   9770  C  CB  . MET C 1 388 ? 9.429   -57.102 9.453   1.00 33.71  ? 388 MET C CB  1 
ATOM   9771  C  CG  . MET C 1 388 ? 8.955   -55.622 9.486   1.00 35.92  ? 388 MET C CG  1 
ATOM   9772  S  SD  . MET C 1 388 ? 7.809   -55.265 10.879  1.00 38.18  ? 388 MET C SD  1 
ATOM   9773  C  CE  . MET C 1 388 ? 6.505   -56.433 10.460  1.00 36.62  ? 388 MET C CE  1 
ATOM   9774  N  N   . GLU C 1 389 ? 11.257  -59.728 10.229  1.00 31.15  ? 389 GLU C N   1 
ATOM   9775  C  CA  . GLU C 1 389 ? 11.458  -61.162 10.204  1.00 33.00  ? 389 GLU C CA  1 
ATOM   9776  C  C   . GLU C 1 389 ? 11.441  -61.724 11.618  1.00 28.27  ? 389 GLU C C   1 
ATOM   9777  O  O   . GLU C 1 389 ? 10.959  -62.842 11.830  1.00 29.25  ? 389 GLU C O   1 
ATOM   9778  C  CB  . GLU C 1 389 ? 12.761  -61.492 9.482   1.00 28.41  ? 389 GLU C CB  1 
ATOM   9779  C  CG  . GLU C 1 389 ? 12.778  -61.138 7.965   1.00 31.52  ? 389 GLU C CG  1 
ATOM   9780  C  CD  . GLU C 1 389 ? 11.851  -62.025 7.106   1.00 31.49  ? 389 GLU C CD  1 
ATOM   9781  O  OE1 . GLU C 1 389 ? 11.378  -63.115 7.555   1.00 28.98  ? 389 GLU C OE1 1 
ATOM   9782  O  OE2 . GLU C 1 389 ? 11.582  -61.643 5.955   1.00 30.20  ? 389 GLU C OE2 1 
ATOM   9783  N  N   . ASN C 1 390 ? 11.945  -60.968 12.593  1.00 30.65  ? 390 ASN C N   1 
ATOM   9784  C  CA  . ASN C 1 390 ? 11.831  -61.422 13.979  1.00 27.00  ? 390 ASN C CA  1 
ATOM   9785  C  C   . ASN C 1 390 ? 10.379  -61.494 14.393  1.00 27.72  ? 390 ASN C C   1 
ATOM   9786  O  O   . ASN C 1 390 ? 9.971   -62.462 15.029  1.00 28.15  ? 390 ASN C O   1 
ATOM   9787  C  CB  . ASN C 1 390 ? 12.565  -60.485 14.922  1.00 27.01  ? 390 ASN C CB  1 
ATOM   9788  C  CG  . ASN C 1 390 ? 14.059  -60.311 14.581  1.00 28.90  ? 390 ASN C CG  1 
ATOM   9789  O  OD1 . ASN C 1 390 ? 14.598  -59.224 14.802  1.00 27.35  ? 390 ASN C OD1 1 
ATOM   9790  N  ND2 . ASN C 1 390 ? 14.725  -61.357 14.071  1.00 28.58  ? 390 ASN C ND2 1 
ATOM   9791  N  N   . ARG C 1 391 ? 9.582   -60.462 14.041  1.00 28.21  ? 391 ARG C N   1 
ATOM   9792  C  CA  . ARG C 1 391 ? 8.148   -60.477 14.329  1.00 32.21  ? 391 ARG C CA  1 
ATOM   9793  C  C   . ARG C 1 391 ? 7.487   -61.709 13.744  1.00 31.56  ? 391 ARG C C   1 
ATOM   9794  O  O   . ARG C 1 391 ? 6.755   -62.415 14.440  1.00 30.52  ? 391 ARG C O   1 
ATOM   9795  C  CB  . ARG C 1 391 ? 7.483   -59.220 13.786  1.00 31.79  ? 391 ARG C CB  1 
ATOM   9796  C  CG  . ARG C 1 391 ? 6.076   -59.002 14.312  1.00 30.67  ? 391 ARG C CG  1 
ATOM   9797  C  CD  . ARG C 1 391 ? 5.172   -58.373 13.297  1.00 34.80  ? 391 ARG C CD  1 
ATOM   9798  N  NE  . ARG C 1 391 ? 4.815   -59.305 12.236  1.00 39.40  ? 391 ARG C NE  1 
ATOM   9799  C  CZ  . ARG C 1 391 ? 3.808   -60.174 12.282  1.00 38.94  ? 391 ARG C CZ  1 
ATOM   9800  N  NH1 . ARG C 1 391 ? 3.018   -60.280 13.348  1.00 37.09  ? 391 ARG C NH1 1 
ATOM   9801  N  NH2 . ARG C 1 391 ? 3.573   -60.943 11.218  1.00 39.59  ? 391 ARG C NH2 1 
ATOM   9802  N  N   . LEU C 1 392 ? 7.744   -61.987 12.450  1.00 30.48  ? 392 LEU C N   1 
ATOM   9803  C  CA  . LEU C 1 392 ? 7.161   -63.153 11.794  1.00 31.58  ? 392 LEU C CA  1 
ATOM   9804  C  C   . LEU C 1 392 ? 7.500   -64.465 12.518  1.00 33.40  ? 392 LEU C C   1 
ATOM   9805  O  O   . LEU C 1 392 ? 6.633   -65.341 12.675  1.00 34.64  ? 392 LEU C O   1 
ATOM   9806  C  CB  . LEU C 1 392 ? 7.641   -63.177 10.341  1.00 31.99  ? 392 LEU C CB  1 
ATOM   9807  C  CG  . LEU C 1 392 ? 6.909   -63.884 9.224   1.00 39.06  ? 392 LEU C CG  1 
ATOM   9808  C  CD1 . LEU C 1 392 ? 5.389   -63.565 9.161   1.00 40.53  ? 392 LEU C CD1 1 
ATOM   9809  C  CD2 . LEU C 1 392 ? 7.580   -63.459 7.901   1.00 36.51  ? 392 LEU C CD2 1 
ATOM   9810  N  N   . ALA C 1 393 ? 8.757   -64.624 12.951  1.00 27.72  ? 393 ALA C N   1 
ATOM   9811  C  CA  . ALA C 1 393 ? 9.195   -65.841 13.635  1.00 29.91  ? 393 ALA C CA  1 
ATOM   9812  C  C   . ALA C 1 393 ? 8.516   -65.994 14.987  1.00 31.78  ? 393 ALA C C   1 
ATOM   9813  O  O   . ALA C 1 393 ? 8.130   -67.100 15.382  1.00 32.70  ? 393 ALA C O   1 
ATOM   9814  C  CB  . ALA C 1 393 ? 10.717  -65.819 13.833  1.00 29.73  ? 393 ALA C CB  1 
ATOM   9815  N  N   . ILE C 1 394 ? 8.365   -64.897 15.715  1.00 27.06  ? 394 ILE C N   1 
ATOM   9816  C  CA  . ILE C 1 394 ? 7.651   -64.991 16.985  1.00 29.30  ? 394 ILE C CA  1 
ATOM   9817  C  C   . ILE C 1 394 ? 6.162   -65.280 16.770  1.00 30.60  ? 394 ILE C C   1 
ATOM   9818  O  O   . ILE C 1 394 ? 5.567   -66.097 17.493  1.00 31.79  ? 394 ILE C O   1 
ATOM   9819  C  CB  . ILE C 1 394 ? 7.870   -63.705 17.787  1.00 27.64  ? 394 ILE C CB  1 
ATOM   9820  C  CG1 . ILE C 1 394 ? 9.363   -63.515 18.124  1.00 25.90  ? 394 ILE C CG1 1 
ATOM   9821  C  CG2 . ILE C 1 394 ? 7.087   -63.765 19.060  1.00 29.26  ? 394 ILE C CG2 1 
ATOM   9822  C  CD1 . ILE C 1 394 ? 9.647   -62.114 18.639  1.00 29.50  ? 394 ILE C CD1 1 
ATOM   9823  N  N   . ALA C 1 395 ? 5.524   -64.607 15.798  1.00 31.86  ? 395 ALA C N   1 
ATOM   9824  C  CA  . ALA C 1 395 ? 4.113   -64.881 15.532  1.00 34.42  ? 395 ALA C CA  1 
ATOM   9825  C  C   . ALA C 1 395 ? 3.892   -66.349 15.178  1.00 35.73  ? 395 ALA C C   1 
ATOM   9826  O  O   . ALA C 1 395 ? 2.983   -66.995 15.714  1.00 37.90  ? 395 ALA C O   1 
ATOM   9827  C  CB  . ALA C 1 395 ? 3.594   -63.975 14.425  1.00 31.76  ? 395 ALA C CB  1 
ATOM   9828  N  N   . LYS C 1 396 ? 4.736   -66.897 14.297  1.00 34.51  ? 396 LYS C N   1 
ATOM   9829  C  CA  . LYS C 1 396 ? 4.626   -68.296 13.885  1.00 36.46  ? 396 LYS C CA  1 
ATOM   9830  C  C   . LYS C 1 396 ? 4.720   -69.244 15.078  1.00 35.85  ? 396 LYS C C   1 
ATOM   9831  O  O   . LYS C 1 396 ? 4.101   -70.310 15.072  1.00 33.68  ? 396 LYS C O   1 
ATOM   9832  C  CB  . LYS C 1 396 ? 5.721   -68.594 12.855  1.00 37.86  ? 396 LYS C CB  1 
ATOM   9833  C  CG  . LYS C 1 396 ? 5.552   -69.853 11.999  1.00 45.95  ? 396 LYS C CG  1 
ATOM   9834  C  CD  . LYS C 1 396 ? 6.531   -69.815 10.823  1.00 47.39  ? 396 LYS C CD  1 
ATOM   9835  C  CE  . LYS C 1 396 ? 6.257   -68.618 9.907   1.00 52.36  ? 396 LYS C CE  1 
ATOM   9836  N  NZ  . LYS C 1 396 ? 6.977   -68.699 8.582   1.00 57.65  ? 396 LYS C NZ  1 
ATOM   9837  N  N   . SER C 1 397 ? 5.488   -68.880 16.103  1.00 38.53  ? 397 SER C N   1 
ATOM   9838  C  CA  . SER C 1 397 ? 5.675   -69.782 17.233  1.00 36.55  ? 397 SER C CA  1 
ATOM   9839  C  C   . SER C 1 397 ? 4.441   -69.848 18.122  1.00 41.08  ? 397 SER C C   1 
ATOM   9840  O  O   . SER C 1 397 ? 4.344   -70.755 18.954  1.00 40.37  ? 397 SER C O   1 
ATOM   9841  C  CB  . SER C 1 397 ? 6.896   -69.355 18.030  1.00 38.11  ? 397 SER C CB  1 
ATOM   9842  O  OG  . SER C 1 397 ? 6.578   -68.230 18.813  1.00 36.32  ? 397 SER C OG  1 
ATOM   9843  N  N   . GLY C 1 398 ? 3.484   -68.927 17.963  1.00 39.50  ? 398 GLY C N   1 
ATOM   9844  C  CA  . GLY C 1 398 ? 2.292   -68.919 18.796  1.00 39.71  ? 398 GLY C CA  1 
ATOM   9845  C  C   . GLY C 1 398 ? 2.348   -67.995 20.007  1.00 37.34  ? 398 GLY C C   1 
ATOM   9846  O  O   . GLY C 1 398 ? 1.317   -67.804 20.664  1.00 41.87  ? 398 GLY C O   1 
ATOM   9847  N  N   . THR C 1 399 ? 3.490   -67.442 20.324  1.00 33.99  ? 399 THR C N   1 
ATOM   9848  C  CA  . THR C 1 399 ? 3.570   -66.440 21.381  1.00 37.16  ? 399 THR C CA  1 
ATOM   9849  C  C   . THR C 1 399 ? 2.920   -65.134 20.934  1.00 37.51  ? 399 THR C C   1 
ATOM   9850  O  O   . THR C 1 399 ? 3.251   -64.626 19.849  1.00 34.74  ? 399 THR C O   1 
ATOM   9851  C  CB  . THR C 1 399 ? 5.036   -66.208 21.767  1.00 36.93  ? 399 THR C CB  1 
ATOM   9852  O  OG1 . THR C 1 399 ? 5.492   -67.385 22.452  1.00 38.04  ? 399 THR C OG1 1 
ATOM   9853  C  CG2 . THR C 1 399 ? 5.172   -64.989 22.663  1.00 35.56  ? 399 THR C CG2 1 
ATOM   9854  N  N   . PRO C 1 400 ? 1.999   -64.570 21.728  1.00 39.11  ? 400 PRO C N   1 
ATOM   9855  C  CA  . PRO C 1 400 ? 1.367   -63.298 21.345  1.00 36.97  ? 400 PRO C CA  1 
ATOM   9856  C  C   . PRO C 1 400 ? 2.412   -62.212 21.163  1.00 36.27  ? 400 PRO C C   1 
ATOM   9857  O  O   . PRO C 1 400 ? 3.380   -62.108 21.938  1.00 34.62  ? 400 PRO C O   1 
ATOM   9858  C  CB  . PRO C 1 400 ? 0.424   -63.000 22.515  1.00 37.36  ? 400 PRO C CB  1 
ATOM   9859  C  CG  . PRO C 1 400 ? 0.120   -64.429 23.155  1.00 36.98  ? 400 PRO C CG  1 
ATOM   9860  C  CD  . PRO C 1 400 ? 1.436   -65.151 22.969  1.00 37.03  ? 400 PRO C CD  1 
ATOM   9861  N  N   . VAL C 1 401 ? 2.239   -61.414 20.112  1.00 34.81  ? 401 VAL C N   1 
ATOM   9862  C  CA  . VAL C 1 401 ? 3.237   -60.391 19.791  1.00 31.51  ? 401 VAL C CA  1 
ATOM   9863  C  C   . VAL C 1 401 ? 2.508   -59.207 19.167  1.00 37.36  ? 401 VAL C C   1 
ATOM   9864  O  O   . VAL C 1 401 ? 1.636   -59.377 18.306  1.00 35.91  ? 401 VAL C O   1 
ATOM   9865  C  CB  . VAL C 1 401 ? 4.374   -60.928 18.881  1.00 31.55  ? 401 VAL C CB  1 
ATOM   9866  C  CG1 . VAL C 1 401 ? 3.825   -61.518 17.606  1.00 32.90  ? 401 VAL C CG1 1 
ATOM   9867  C  CG2 . VAL C 1 401 ? 5.426   -59.827 18.552  1.00 31.08  ? 401 VAL C CG2 1 
ATOM   9868  N  N   . MET C 1 402 ? 2.809   -58.018 19.704  1.00 34.35  ? 402 MET C N   1 
ATOM   9869  C  CA  . MET C 1 402 ? 2.381   -56.727 19.201  1.00 38.88  ? 402 MET C CA  1 
ATOM   9870  C  C   . MET C 1 402 ? 3.575   -55.880 18.775  1.00 35.16  ? 402 MET C C   1 
ATOM   9871  O  O   . MET C 1 402 ? 4.703   -56.067 19.249  1.00 34.79  ? 402 MET C O   1 
ATOM   9872  C  CB  . MET C 1 402 ? 1.559   -55.994 20.260  1.00 39.88  ? 402 MET C CB  1 
ATOM   9873  C  CG  . MET C 1 402 ? 2.386   -55.348 21.322  1.00 42.03  ? 402 MET C CG  1 
ATOM   9874  S  SD  . MET C 1 402 ? 1.480   -54.075 22.234  1.00 52.34  ? 402 MET C SD  1 
ATOM   9875  C  CE  . MET C 1 402 ? 1.873   -52.707 21.123  1.00 42.03  ? 402 MET C CE  1 
ATOM   9876  N  N   . THR C 1 403 ? 3.317   -54.957 17.849  1.00 31.52  ? 403 THR C N   1 
ATOM   9877  C  CA  . THR C 1 403 ? 4.289   -53.960 17.442  1.00 32.31  ? 403 THR C CA  1 
ATOM   9878  C  C   . THR C 1 403 ? 3.745   -52.571 17.737  1.00 32.04  ? 403 THR C C   1 
ATOM   9879  O  O   . THR C 1 403 ? 2.530   -52.349 17.780  1.00 32.73  ? 403 THR C O   1 
ATOM   9880  C  CB  . THR C 1 403 ? 4.639   -54.040 15.929  1.00 32.62  ? 403 THR C CB  1 
ATOM   9881  O  OG1 . THR C 1 403 ? 3.476   -53.759 15.147  1.00 34.80  ? 403 THR C OG1 1 
ATOM   9882  C  CG2 . THR C 1 403 ? 5.167   -55.410 15.538  1.00 33.36  ? 403 THR C CG2 1 
ATOM   9883  N  N   . PHE C 1 404 ? 4.668   -51.641 17.916  1.00 32.55  ? 404 PHE C N   1 
ATOM   9884  C  CA  . PHE C 1 404 ? 4.360   -50.220 17.925  1.00 33.07  ? 404 PHE C CA  1 
ATOM   9885  C  C   . PHE C 1 404 ? 5.529   -49.475 17.297  1.00 34.85  ? 404 PHE C C   1 
ATOM   9886  O  O   . PHE C 1 404 ? 6.689   -49.825 17.523  1.00 32.46  ? 404 PHE C O   1 
ATOM   9887  C  CB  . PHE C 1 404 ? 4.095   -49.697 19.343  1.00 35.64  ? 404 PHE C CB  1 
ATOM   9888  C  CG  . PHE C 1 404 ? 5.296   -49.758 20.253  1.00 37.42  ? 404 PHE C CG  1 
ATOM   9889  C  CD1 . PHE C 1 404 ? 5.617   -50.937 20.921  1.00 36.63  ? 404 PHE C CD1 1 
ATOM   9890  C  CD2 . PHE C 1 404 ? 6.116   -48.643 20.425  1.00 36.01  ? 404 PHE C CD2 1 
ATOM   9891  C  CE1 . PHE C 1 404 ? 6.740   -51.007 21.758  1.00 39.04  ? 404 PHE C CE1 1 
ATOM   9892  C  CE2 . PHE C 1 404 ? 7.241   -48.697 21.267  1.00 35.97  ? 404 PHE C CE2 1 
ATOM   9893  C  CZ  . PHE C 1 404 ? 7.543   -49.862 21.957  1.00 35.16  ? 404 PHE C CZ  1 
ATOM   9894  N  N   . GLU C 1 405 ? 5.232   -48.435 16.523  1.00 30.30  ? 405 GLU C N   1 
ATOM   9895  C  CA  . GLU C 1 405 ? 6.279   -47.645 15.915  1.00 29.34  ? 405 GLU C CA  1 
ATOM   9896  C  C   . GLU C 1 405 ? 6.733   -46.552 16.881  1.00 33.10  ? 405 GLU C C   1 
ATOM   9897  O  O   . GLU C 1 405 ? 5.940   -46.024 17.659  1.00 31.02  ? 405 GLU C O   1 
ATOM   9898  C  CB  . GLU C 1 405 ? 5.781   -47.025 14.601  1.00 32.75  ? 405 GLU C CB  1 
ATOM   9899  C  CG  . GLU C 1 405 ? 5.343   -48.072 13.573  1.00 35.47  ? 405 GLU C CG  1 
ATOM   9900  C  CD  . GLU C 1 405 ? 5.110   -47.452 12.196  1.00 40.18  ? 405 GLU C CD  1 
ATOM   9901  O  OE1 . GLU C 1 405 ? 5.480   -46.269 11.997  1.00 42.00  ? 405 GLU C OE1 1 
ATOM   9902  O  OE2 . GLU C 1 405 ? 4.534   -48.124 11.317  1.00 39.70  ? 405 GLU C OE2 1 
ATOM   9903  N  N   . GLY C 1 406 ? 8.033   -46.269 16.881  1.00 29.79  ? 406 GLY C N   1 
ATOM   9904  C  CA  . GLY C 1 406 ? 8.529   -45.189 17.677  1.00 28.14  ? 406 GLY C CA  1 
ATOM   9905  C  C   . GLY C 1 406 ? 9.903   -44.752 17.218  1.00 28.05  ? 406 GLY C C   1 
ATOM   9906  O  O   . GLY C 1 406 ? 10.345  -45.071 16.114  1.00 29.31  ? 406 GLY C O   1 
ATOM   9907  N  N   . ASN C 1 407 ? 10.550  -43.976 18.075  1.00 26.92  ? 407 ASN C N   1 
ATOM   9908  C  CA  . ASN C 1 407 ? 11.929  -43.554 17.811  1.00 25.93  ? 407 ASN C CA  1 
ATOM   9909  C  C   . ASN C 1 407 ? 12.577  -43.321 19.156  1.00 27.48  ? 407 ASN C C   1 
ATOM   9910  O  O   . ASN C 1 407 ? 12.055  -42.526 19.935  1.00 27.74  ? 407 ASN C O   1 
ATOM   9911  C  CB  . ASN C 1 407 ? 11.920  -42.275 16.897  1.00 25.96  ? 407 ASN C CB  1 
ATOM   9912  C  CG  . ASN C 1 407 ? 13.318  -41.811 16.513  1.00 25.05  ? 407 ASN C CG  1 
ATOM   9913  O  OD1 . ASN C 1 407 ? 14.201  -41.801 17.338  1.00 25.98  ? 407 ASN C OD1 1 
ATOM   9914  N  ND2 . ASN C 1 407 ? 13.492  -41.358 15.269  1.00 25.28  ? 407 ASN C ND2 1 
ATOM   9915  N  N   . MET C 1 408 ? 13.648  -44.067 19.489  1.00 26.55  ? 408 MET C N   1 
ATOM   9916  C  CA  . MET C 1 408 ? 14.142  -43.991 20.866  1.00 30.25  ? 408 MET C CA  1 
ATOM   9917  C  C   . MET C 1 408 ? 14.650  -42.597 21.207  1.00 27.09  ? 408 MET C C   1 
ATOM   9918  O  O   . MET C 1 408 ? 14.599  -42.187 22.365  1.00 28.54  ? 408 MET C O   1 
ATOM   9919  C  CB  . MET C 1 408 ? 15.256  -45.006 21.150  1.00 28.52  ? 408 MET C CB  1 
ATOM   9920  C  CG  . MET C 1 408 ? 16.588  -44.547 20.562  1.00 29.03  ? 408 MET C CG  1 
ATOM   9921  S  SD  . MET C 1 408 ? 16.770  -44.533 18.739  1.00 27.88  ? 408 MET C SD  1 
ATOM   9922  C  CE  . MET C 1 408 ? 18.591  -44.432 18.546  1.00 27.56  ? 408 MET C CE  1 
ATOM   9923  N  N   . GLY C 1 409 ? 15.078  -41.824 20.217  1.00 26.21  ? 409 GLY C N   1 
ATOM   9924  C  CA  . GLY C 1 409 ? 15.726  -40.561 20.548  1.00 26.91  ? 409 GLY C CA  1 
ATOM   9925  C  C   . GLY C 1 409 ? 14.950  -39.323 20.164  1.00 27.45  ? 409 GLY C C   1 
ATOM   9926  O  O   . GLY C 1 409 ? 15.189  -38.221 20.695  1.00 29.45  ? 409 GLY C O   1 
ATOM   9927  N  N   . ASP C 1 410 ? 13.981  -39.501 19.278  1.00 28.45  ? 410 ASP C N   1 
ATOM   9928  C  CA  . ASP C 1 410 ? 13.234  -38.382 18.680  1.00 27.19  ? 410 ASP C CA  1 
ATOM   9929  C  C   . ASP C 1 410 ? 11.732  -38.610 18.835  1.00 28.34  ? 410 ASP C C   1 
ATOM   9930  O  O   . ASP C 1 410 ? 11.097  -39.244 17.979  1.00 28.51  ? 410 ASP C O   1 
ATOM   9931  C  CB  . ASP C 1 410 ? 13.674  -38.224 17.203  1.00 27.34  ? 410 ASP C CB  1 
ATOM   9932  C  CG  . ASP C 1 410 ? 13.157  -36.943 16.545  1.00 29.59  ? 410 ASP C CG  1 
ATOM   9933  O  OD1 . ASP C 1 410 ? 12.319  -36.209 17.171  1.00 30.74  ? 410 ASP C OD1 1 
ATOM   9934  O  OD2 . ASP C 1 410 ? 13.625  -36.688 15.385  1.00 30.50  ? 410 ASP C OD2 1 
ATOM   9935  N  N   . GLU C 1 411 ? 11.178  -38.015 19.910  1.00 29.86  ? 411 GLU C N   1 
ATOM   9936  C  CA  . GLU C 1 411 ? 9.763   -38.126 20.275  1.00 35.48  ? 411 GLU C CA  1 
ATOM   9937  C  C   . GLU C 1 411 ? 8.810   -37.752 19.140  1.00 35.50  ? 411 GLU C C   1 
ATOM   9938  O  O   . GLU C 1 411 ? 7.624   -38.114 19.202  1.00 34.63  ? 411 GLU C O   1 
ATOM   9939  C  CB  . GLU C 1 411 ? 9.442   -37.208 21.486  1.00 37.99  ? 411 GLU C CB  1 
ATOM   9940  C  CG  . GLU C 1 411 ? 9.550   -35.673 21.142  1.00 44.10  ? 411 GLU C CG  1 
ATOM   9941  C  CD  . GLU C 1 411 ? 9.139   -34.680 22.279  1.00 54.58  ? 411 GLU C CD  1 
ATOM   9942  O  OE1 . GLU C 1 411 ? 7.983   -34.733 22.769  1.00 50.37  ? 411 GLU C OE1 1 
ATOM   9943  O  OE2 . GLU C 1 411 ? 9.975   -33.810 22.649  1.00 52.14  ? 411 GLU C OE2 1 
ATOM   9944  N  N   . ARG C 1 412 ? 9.272   -36.976 18.137  1.00 31.51  ? 412 ARG C N   1 
ATOM   9945  C  CA  . ARG C 1 412 ? 8.394   -36.584 17.039  1.00 33.55  ? 412 ARG C CA  1 
ATOM   9946  C  C   . ARG C 1 412 ? 7.876   -37.784 16.272  1.00 33.23  ? 412 ARG C C   1 
ATOM   9947  O  O   . ARG C 1 412 ? 6.821   -37.697 15.627  1.00 33.45  ? 412 ARG C O   1 
ATOM   9948  C  CB  . ARG C 1 412 ? 9.102   -35.636 16.071  1.00 32.40  ? 412 ARG C CB  1 
ATOM   9949  C  CG  . ARG C 1 412 ? 9.373   -34.248 16.676  1.00 34.27  ? 412 ARG C CG  1 
ATOM   9950  C  CD  . ARG C 1 412 ? 10.226  -33.385 15.732  1.00 34.56  ? 412 ARG C CD  1 
ATOM   9951  N  NE  . ARG C 1 412 ? 11.597  -33.875 15.611  1.00 31.60  ? 412 ARG C NE  1 
ATOM   9952  C  CZ  . ARG C 1 412 ? 12.580  -33.179 15.054  1.00 31.76  ? 412 ARG C CZ  1 
ATOM   9953  N  NH1 . ARG C 1 412 ? 12.359  -31.971 14.513  1.00 31.65  ? 412 ARG C NH1 1 
ATOM   9954  N  NH2 . ARG C 1 412 ? 13.807  -33.699 15.048  1.00 32.16  ? 412 ARG C NH2 1 
ATOM   9955  N  N   . GLU C 1 413 ? 8.587   -38.901 16.321  1.00 35.07  ? 413 GLU C N   1 
ATOM   9956  C  CA  . GLU C 1 413 ? 8.142   -40.112 15.646  1.00 33.61  ? 413 GLU C CA  1 
ATOM   9957  C  C   . GLU C 1 413 ? 7.573   -41.152 16.609  1.00 36.00  ? 413 GLU C C   1 
ATOM   9958  O  O   . GLU C 1 413 ? 7.523   -42.336 16.275  1.00 31.12  ? 413 GLU C O   1 
ATOM   9959  C  CB  . GLU C 1 413 ? 9.288   -40.708 14.827  1.00 34.03  ? 413 GLU C CB  1 
ATOM   9960  C  CG  . GLU C 1 413 ? 9.657   -39.839 13.650  1.00 38.72  ? 413 GLU C CG  1 
ATOM   9961  C  CD  . GLU C 1 413 ? 10.716  -40.440 12.745  1.00 34.41  ? 413 GLU C CD  1 
ATOM   9962  O  OE1 . GLU C 1 413 ? 11.582  -41.179 13.224  1.00 34.97  ? 413 GLU C OE1 1 
ATOM   9963  O  OE2 . GLU C 1 413 ? 10.674  -40.125 11.529  1.00 40.21  ? 413 GLU C OE2 1 
ATOM   9964  N  N   . PHE C 1 414 ? 7.129   -40.739 17.790  1.00 35.16  ? 414 PHE C N   1 
ATOM   9965  C  CA  . PHE C 1 414 ? 6.471   -41.630 18.747  1.00 35.05  ? 414 PHE C CA  1 
ATOM   9966  C  C   . PHE C 1 414 ? 5.125   -41.021 19.140  1.00 38.83  ? 414 PHE C C   1 
ATOM   9967  O  O   . PHE C 1 414 ? 5.068   -39.888 19.639  1.00 38.31  ? 414 PHE C O   1 
ATOM   9968  C  CB  . PHE C 1 414 ? 7.372   -41.833 19.973  1.00 33.73  ? 414 PHE C CB  1 
ATOM   9969  C  CG  . PHE C 1 414 ? 6.801   -42.760 21.014  1.00 37.22  ? 414 PHE C CG  1 
ATOM   9970  C  CD1 . PHE C 1 414 ? 6.470   -44.084 20.694  1.00 36.50  ? 414 PHE C CD1 1 
ATOM   9971  C  CD2 . PHE C 1 414 ? 6.548   -42.285 22.302  1.00 36.60  ? 414 PHE C CD2 1 
ATOM   9972  C  CE1 . PHE C 1 414 ? 5.939   -44.943 21.680  1.00 37.94  ? 414 PHE C CE1 1 
ATOM   9973  C  CE2 . PHE C 1 414 ? 6.029   -43.122 23.283  1.00 42.47  ? 414 PHE C CE2 1 
ATOM   9974  C  CZ  . PHE C 1 414 ? 5.717   -44.462 22.964  1.00 40.11  ? 414 PHE C CZ  1 
ATOM   9975  N  N   . ASP C 1 415 ? 4.041   -41.758 18.893  1.00 36.03  ? 415 ASP C N   1 
ATOM   9976  C  CA  . ASP C 1 415 ? 2.685   -41.360 19.253  1.00 45.77  ? 415 ASP C CA  1 
ATOM   9977  C  C   . ASP C 1 415 ? 2.327   -42.154 20.504  1.00 47.23  ? 415 ASP C C   1 
ATOM   9978  O  O   . ASP C 1 415 ? 1.933   -43.324 20.418  1.00 42.53  ? 415 ASP C O   1 
ATOM   9979  C  CB  . ASP C 1 415 ? 1.715   -41.649 18.112  1.00 42.84  ? 415 ASP C CB  1 
ATOM   9980  C  CG  . ASP C 1 415 ? 0.318   -41.119 18.371  1.00 52.86  ? 415 ASP C CG  1 
ATOM   9981  O  OD1 . ASP C 1 415 ? -0.092  -40.933 19.548  1.00 49.56  ? 415 ASP C OD1 1 
ATOM   9982  O  OD2 . ASP C 1 415 ? -0.400  -40.930 17.368  1.00 56.48  ? 415 ASP C OD2 1 
ATOM   9983  N  N   . GLU C 1 416 ? 2.498   -41.532 21.675  1.00 47.89  ? 416 GLU C N   1 
ATOM   9984  C  CA  . GLU C 1 416 ? 2.284   -42.298 22.902  1.00 49.96  ? 416 GLU C CA  1 
ATOM   9985  C  C   . GLU C 1 416 ? 0.807   -42.605 23.141  1.00 50.19  ? 416 GLU C C   1 
ATOM   9986  O  O   . GLU C 1 416 ? 0.489   -43.681 23.659  1.00 49.83  ? 416 GLU C O   1 
ATOM   9987  C  CB  . GLU C 1 416 ? 2.918   -41.594 24.114  1.00 55.99  ? 416 GLU C CB  1 
ATOM   9988  C  CG  . GLU C 1 416 ? 2.653   -40.115 24.233  1.00 62.27  ? 416 GLU C CG  1 
ATOM   9989  C  CD  . GLU C 1 416 ? 3.569   -39.448 25.251  1.00 67.11  ? 416 GLU C CD  1 
ATOM   9990  O  OE1 . GLU C 1 416 ? 3.637   -39.935 26.417  1.00 61.02  ? 416 GLU C OE1 1 
ATOM   9991  O  OE2 . GLU C 1 416 ? 4.253   -38.473 24.853  1.00 66.50  ? 416 GLU C OE2 1 
ATOM   9992  N  N   . VAL C 1 417 ? -0.119  -41.720 22.756  1.00 52.97  ? 417 VAL C N   1 
ATOM   9993  C  CA  . VAL C 1 417 ? -1.523  -42.066 22.986  1.00 54.10  ? 417 VAL C CA  1 
ATOM   9994  C  C   . VAL C 1 417 ? -1.928  -43.260 22.120  1.00 52.09  ? 417 VAL C C   1 
ATOM   9995  O  O   . VAL C 1 417 ? -2.591  -44.189 22.595  1.00 49.67  ? 417 VAL C O   1 
ATOM   9996  C  CB  . VAL C 1 417 ? -2.453  -40.847 22.803  1.00 58.80  ? 417 VAL C CB  1 
ATOM   9997  C  CG1 . VAL C 1 417 ? -1.862  -39.610 23.464  1.00 60.23  ? 417 VAL C CG1 1 
ATOM   9998  C  CG2 . VAL C 1 417 ? -2.716  -40.547 21.337  1.00 62.02  ? 417 VAL C CG2 1 
ATOM   9999  N  N   . ARG C 1 418 ? -1.496  -43.297 20.862  1.00 50.00  ? 418 ARG C N   1 
ATOM   10000 C  CA  . ARG C 1 418 ? -1.827  -44.450 20.031  1.00 46.93  ? 418 ARG C CA  1 
ATOM   10001 C  C   . ARG C 1 418 ? -1.132  -45.710 20.538  1.00 47.65  ? 418 ARG C C   1 
ATOM   10002 O  O   . ARG C 1 418 ? -1.698  -46.811 20.474  1.00 47.95  ? 418 ARG C O   1 
ATOM   10003 C  CB  . ARG C 1 418 ? -1.448  -44.160 18.579  1.00 51.43  ? 418 ARG C CB  1 
ATOM   10004 C  CG  . ARG C 1 418 ? -1.561  -45.338 17.667  1.00 53.47  ? 418 ARG C CG  1 
ATOM   10005 C  CD  . ARG C 1 418 ? -0.555  -45.217 16.529  1.00 60.70  ? 418 ARG C CD  1 
ATOM   10006 N  NE  . ARG C 1 418 ? -0.999  -45.884 15.311  1.00 69.87  ? 418 ARG C NE  1 
ATOM   10007 C  CZ  . ARG C 1 418 ? -1.283  -47.178 15.202  1.00 73.63  ? 418 ARG C CZ  1 
ATOM   10008 N  NH1 . ARG C 1 418 ? -1.105  -48.021 16.209  1.00 69.29  ? 418 ARG C NH1 1 
ATOM   10009 N  NH2 . ARG C 1 418 ? -1.742  -47.643 14.044  1.00 76.06  ? 418 ARG C NH2 1 
ATOM   10010 N  N   . THR C 1 419 ? 0.101   -45.571 21.031  1.00 44.13  ? 419 THR C N   1 
ATOM   10011 C  CA  . THR C 1 419 ? 0.833   -46.726 21.545  1.00 42.44  ? 419 THR C CA  1 
ATOM   10012 C  C   . THR C 1 419 ? 0.174   -47.261 22.810  1.00 48.11  ? 419 THR C C   1 
ATOM   10013 O  O   . THR C 1 419 ? -0.061  -48.471 22.934  1.00 47.28  ? 419 THR C O   1 
ATOM   10014 C  CB  . THR C 1 419 ? 2.293   -46.344 21.806  1.00 38.11  ? 419 THR C CB  1 
ATOM   10015 O  OG1 . THR C 1 419 ? 2.870   -45.871 20.583  1.00 42.51  ? 419 THR C OG1 1 
ATOM   10016 C  CG2 . THR C 1 419 ? 3.136   -47.557 22.306  1.00 38.38  ? 419 THR C CG2 1 
ATOM   10017 N  N   . GLN C 1 420 ? -0.175  -46.361 23.747  1.00 48.22  ? 420 GLN C N   1 
ATOM   10018 C  CA  . GLN C 1 420 ? -0.834  -46.787 24.980  1.00 49.01  ? 420 GLN C CA  1 
ATOM   10019 C  C   . GLN C 1 420 ? -2.162  -47.460 24.680  1.00 55.05  ? 420 GLN C C   1 
ATOM   10020 O  O   . GLN C 1 420 ? -2.578  -48.372 25.407  1.00 55.12  ? 420 GLN C O   1 
ATOM   10021 C  CB  . GLN C 1 420 ? -1.045  -45.592 25.931  1.00 56.64  ? 420 GLN C CB  1 
ATOM   10022 C  CG  . GLN C 1 420 ? -1.473  -45.966 27.369  1.00 59.05  ? 420 GLN C CG  1 
ATOM   10023 C  CD  . GLN C 1 420 ? -2.909  -45.592 27.729  1.00 71.02  ? 420 GLN C CD  1 
ATOM   10024 O  OE1 . GLN C 1 420 ? -3.867  -46.062 27.111  1.00 74.06  ? 420 GLN C OE1 1 
ATOM   10025 N  NE2 . GLN C 1 420 ? -3.064  -44.793 28.785  1.00 69.53  ? 420 GLN C NE2 1 
ATOM   10026 N  N   . ALA C 1 421 ? -2.846  -47.025 23.619  1.00 52.32  ? 421 ALA C N   1 
ATOM   10027 C  CA  . ALA C 1 421 ? -4.071  -47.701 23.219  1.00 53.41  ? 421 ALA C CA  1 
ATOM   10028 C  C   . ALA C 1 421 ? -3.773  -49.105 22.711  1.00 53.39  ? 421 ALA C C   1 
ATOM   10029 O  O   . ALA C 1 421 ? -4.469  -50.061 23.073  1.00 55.10  ? 421 ALA C O   1 
ATOM   10030 C  CB  . ALA C 1 421 ? -4.797  -46.873 22.161  1.00 55.09  ? 421 ALA C CB  1 
ATOM   10031 N  N   . ARG C 1 422 ? -2.742  -49.244 21.875  1.00 51.47  ? 422 ARG C N   1 
ATOM   10032 C  CA  . ARG C 1 422 ? -2.368  -50.550 21.345  1.00 53.13  ? 422 ARG C CA  1 
ATOM   10033 C  C   . ARG C 1 422 ? -1.929  -51.509 22.459  1.00 53.74  ? 422 ARG C C   1 
ATOM   10034 O  O   . ARG C 1 422 ? -2.218  -52.712 22.395  1.00 51.89  ? 422 ARG C O   1 
ATOM   10035 C  CB  . ARG C 1 422 ? -1.270  -50.378 20.278  1.00 49.55  ? 422 ARG C CB  1 
ATOM   10036 C  CG  . ARG C 1 422 ? -0.919  -51.695 19.568  1.00 56.67  ? 422 ARG C CG  1 
ATOM   10037 C  CD  . ARG C 1 422 ? -2.058  -52.267 18.739  1.00 57.14  ? 422 ARG C CD  1 
ATOM   10038 N  NE  . ARG C 1 422 ? -1.702  -53.546 18.127  1.00 58.89  ? 422 ARG C NE  1 
ATOM   10039 C  CZ  . ARG C 1 422 ? -1.739  -54.713 18.764  1.00 57.00  ? 422 ARG C CZ  1 
ATOM   10040 N  NH1 . ARG C 1 422 ? -2.226  -54.819 19.999  1.00 52.51  ? 422 ARG C NH1 1 
ATOM   10041 N  NH2 . ARG C 1 422 ? -1.304  -55.808 18.140  1.00 55.19  ? 422 ARG C NH2 1 
ATOM   10042 N  N   . VAL C 1 423 ? -1.253  -50.988 23.490  1.00 52.38  ? 423 VAL C N   1 
ATOM   10043 C  CA  . VAL C 1 423 ? -0.912  -51.776 24.669  1.00 51.90  ? 423 VAL C CA  1 
ATOM   10044 C  C   . VAL C 1 423 ? -2.160  -52.236 25.416  1.00 53.36  ? 423 VAL C C   1 
ATOM   10045 O  O   . VAL C 1 423 ? -2.207  -53.373 25.903  1.00 54.90  ? 423 VAL C O   1 
ATOM   10046 C  CB  . VAL C 1 423 ? 0.029   -50.977 25.586  1.00 56.01  ? 423 VAL C CB  1 
ATOM   10047 C  CG1 . VAL C 1 423 ? 0.165   -51.668 26.938  1.00 54.78  ? 423 VAL C CG1 1 
ATOM   10048 C  CG2 . VAL C 1 423 ? 1.388   -50.849 24.931  1.00 51.44  ? 423 VAL C CG2 1 
ATOM   10049 N  N   . ASP C 1 424 ? -3.177  -51.370 25.548  1.00 57.40  ? 424 ASP C N   1 
ATOM   10050 C  CA  . ASP C 1 424 ? -4.440  -51.814 26.165  1.00 60.25  ? 424 ASP C CA  1 
ATOM   10051 C  C   . ASP C 1 424 ? -5.050  -52.974 25.404  1.00 58.51  ? 424 ASP C C   1 
ATOM   10052 O  O   . ASP C 1 424 ? -5.464  -53.970 26.005  1.00 61.41  ? 424 ASP C O   1 
ATOM   10053 C  CB  . ASP C 1 424 ? -5.504  -50.713 26.253  1.00 62.76  ? 424 ASP C CB  1 
ATOM   10054 C  CG  . ASP C 1 424 ? -5.022  -49.452 26.906  1.00 70.35  ? 424 ASP C CG  1 
ATOM   10055 O  OD1 . ASP C 1 424 ? -4.530  -49.551 28.053  1.00 72.60  ? 424 ASP C OD1 1 
ATOM   10056 O  OD2 . ASP C 1 424 ? -5.193  -48.363 26.300  1.00 70.79  ? 424 ASP C OD2 1 
ATOM   10057 N  N   . ALA C 1 425 ? -5.186  -52.823 24.086  1.00 58.43  ? 425 ALA C N   1 
ATOM   10058 C  CA  . ALA C 1 425 ? -5.706  -53.902 23.254  1.00 57.38  ? 425 ALA C CA  1 
ATOM   10059 C  C   . ALA C 1 425 ? -4.941  -55.194 23.494  1.00 58.02  ? 425 ALA C C   1 
ATOM   10060 O  O   . ALA C 1 425 ? -5.536  -56.267 23.661  1.00 57.99  ? 425 ALA C O   1 
ATOM   10061 C  CB  . ALA C 1 425 ? -5.621  -53.504 21.784  1.00 52.64  ? 425 ALA C CB  1 
ATOM   10062 N  N   . PHE C 1 426 ? -3.609  -55.100 23.507  1.00 53.63  ? 426 PHE C N   1 
ATOM   10063 C  CA  . PHE C 1 426 ? -2.771  -56.271 23.739  1.00 56.02  ? 426 PHE C CA  1 
ATOM   10064 C  C   . PHE C 1 426 ? -3.052  -56.898 25.093  1.00 55.07  ? 426 PHE C C   1 
ATOM   10065 O  O   . PHE C 1 426 ? -3.167  -58.125 25.204  1.00 57.70  ? 426 PHE C O   1 
ATOM   10066 C  CB  . PHE C 1 426 ? -1.302  -55.862 23.629  1.00 49.27  ? 426 PHE C CB  1 
ATOM   10067 C  CG  . PHE C 1 426 ? -0.342  -57.013 23.580  1.00 48.36  ? 426 PHE C CG  1 
ATOM   10068 C  CD1 . PHE C 1 426 ? -0.550  -58.081 22.730  1.00 47.37  ? 426 PHE C CD1 1 
ATOM   10069 C  CD2 . PHE C 1 426 ? 0.799   -56.998 24.382  1.00 46.01  ? 426 PHE C CD2 1 
ATOM   10070 C  CE1 . PHE C 1 426 ? 0.360   -59.124 22.678  1.00 43.19  ? 426 PHE C CE1 1 
ATOM   10071 C  CE2 . PHE C 1 426 ? 1.719   -58.026 24.338  1.00 46.18  ? 426 PHE C CE2 1 
ATOM   10072 C  CZ  . PHE C 1 426 ? 1.516   -59.084 23.487  1.00 42.22  ? 426 PHE C CZ  1 
ATOM   10073 N  N   . MET C 1 427 ? -3.171  -56.070 26.135  1.00 54.38  ? 427 MET C N   1 
ATOM   10074 C  CA  . MET C 1 427 ? -3.356  -56.596 27.482  1.00 58.34  ? 427 MET C CA  1 
ATOM   10075 C  C   . MET C 1 427 ? -4.649  -57.383 27.559  1.00 63.08  ? 427 MET C C   1 
ATOM   10076 O  O   . MET C 1 427 ? -4.685  -58.495 28.093  1.00 65.93  ? 427 MET C O   1 
ATOM   10077 C  CB  . MET C 1 427 ? -3.381  -55.464 28.498  1.00 59.15  ? 427 MET C CB  1 
ATOM   10078 C  CG  . MET C 1 427 ? -2.024  -55.064 29.070  1.00 61.27  ? 427 MET C CG  1 
ATOM   10079 S  SD  . MET C 1 427 ? -0.758  -56.304 29.451  1.00 68.87  ? 427 MET C SD  1 
ATOM   10080 C  CE  . MET C 1 427 ? 0.003   -56.566 27.872  1.00 47.74  ? 427 MET C CE  1 
ATOM   10081 N  N   . GLU C 1 428 ? -5.725  -56.821 27.003  1.00 64.80  ? 428 GLU C N   1 
ATOM   10082 C  CA  . GLU C 1 428 ? -6.987  -57.548 26.942  1.00 67.35  ? 428 GLU C CA  1 
ATOM   10083 C  C   . GLU C 1 428 ? -6.841  -58.851 26.168  1.00 64.01  ? 428 GLU C C   1 
ATOM   10084 O  O   . GLU C 1 428 ? -7.429  -59.867 26.548  1.00 66.45  ? 428 GLU C O   1 
ATOM   10085 C  CB  . GLU C 1 428 ? -8.080  -56.657 26.343  1.00 70.73  ? 428 GLU C CB  1 
ATOM   10086 C  CG  . GLU C 1 428 ? -8.486  -55.474 27.245  1.00 78.30  ? 428 GLU C CG  1 
ATOM   10087 C  CD  . GLU C 1 428 ? -8.715  -54.176 26.474  1.00 81.63  ? 428 GLU C CD  1 
ATOM   10088 O  OE1 . GLU C 1 428 ? -8.854  -53.105 27.123  1.00 81.30  ? 428 GLU C OE1 1 
ATOM   10089 O  OE2 . GLU C 1 428 ? -8.731  -54.229 25.220  1.00 77.72  ? 428 GLU C OE2 1 
ATOM   10090 N  N   . GLN C 1 429 ? -6.030  -58.859 25.107  1.00 63.91  ? 429 GLN C N   1 
ATOM   10091 C  CA  . GLN C 1 429 ? -5.826  -60.090 24.352  1.00 64.17  ? 429 GLN C CA  1 
ATOM   10092 C  C   . GLN C 1 429 ? -5.089  -61.141 25.178  1.00 65.02  ? 429 GLN C C   1 
ATOM   10093 O  O   . GLN C 1 429 ? -5.277  -62.342 24.944  1.00 66.28  ? 429 GLN C O   1 
ATOM   10094 C  CB  . GLN C 1 429 ? -5.058  -59.805 23.049  1.00 62.27  ? 429 GLN C CB  1 
ATOM   10095 C  CG  . GLN C 1 429 ? -4.353  -61.025 22.433  1.00 60.63  ? 429 GLN C CG  1 
ATOM   10096 C  CD  . GLN C 1 429 ? -3.346  -60.673 21.346  1.00 65.22  ? 429 GLN C CD  1 
ATOM   10097 O  OE1 . GLN C 1 429 ? -3.214  -59.511 20.956  1.00 68.24  ? 429 GLN C OE1 1 
ATOM   10098 N  NE2 . GLN C 1 429 ? -2.654  -61.688 20.825  1.00 57.24  ? 429 GLN C NE2 1 
ATOM   10099 N  N   . LEU C 1 430 ? -4.281  -60.724 26.156  1.00 60.68  ? 430 LEU C N   1 
ATOM   10100 C  CA  . LEU C 1 430 ? -3.584  -61.644 27.049  1.00 61.69  ? 430 LEU C CA  1 
ATOM   10101 C  C   . LEU C 1 430 ? -4.452  -62.116 28.225  1.00 65.73  ? 430 LEU C C   1 
ATOM   10102 O  O   . LEU C 1 430 ? -3.924  -62.703 29.173  1.00 69.16  ? 430 LEU C O   1 
ATOM   10103 C  CB  . LEU C 1 430 ? -2.299  -60.994 27.578  1.00 52.43  ? 430 LEU C CB  1 
ATOM   10104 C  CG  . LEU C 1 430 ? -1.238  -60.702 26.521  1.00 47.70  ? 430 LEU C CG  1 
ATOM   10105 C  CD1 . LEU C 1 430 ? 0.062   -60.197 27.151  1.00 48.58  ? 430 LEU C CD1 1 
ATOM   10106 C  CD2 . LEU C 1 430 ? -0.966  -61.936 25.674  1.00 48.60  ? 430 LEU C CD2 1 
ATOM   10107 N  N   . GLY C 1 431 ? -5.757  -61.880 28.192  1.00 70.14  ? 431 GLY C N   1 
ATOM   10108 C  CA  . GLY C 1 431 ? -6.615  -62.353 29.271  1.00 74.78  ? 431 GLY C CA  1 
ATOM   10109 C  C   . GLY C 1 431 ? -6.472  -61.608 30.585  1.00 83.54  ? 431 GLY C C   1 
ATOM   10110 O  O   . GLY C 1 431 ? -6.561  -62.226 31.656  1.00 88.28  ? 431 GLY C O   1 
ATOM   10111 N  N   . VAL C 1 432 ? -6.262  -60.290 30.535  1.00 83.52  ? 432 VAL C N   1 
ATOM   10112 C  CA  . VAL C 1 432 ? -6.040  -59.486 31.732  1.00 88.29  ? 432 VAL C CA  1 
ATOM   10113 C  C   . VAL C 1 432 ? -6.735  -58.135 31.565  1.00 90.90  ? 432 VAL C C   1 
ATOM   10114 O  O   . VAL C 1 432 ? -6.909  -57.642 30.445  1.00 87.89  ? 432 VAL C O   1 
ATOM   10115 C  CB  . VAL C 1 432 ? -4.519  -59.341 32.027  1.00 83.53  ? 432 VAL C CB  1 
ATOM   10116 C  CG1 . VAL C 1 432 ? -3.706  -59.806 30.845  1.00 77.26  ? 432 VAL C CG1 1 
ATOM   10117 C  CG2 . VAL C 1 432 ? -4.129  -57.909 32.393  1.00 83.71  ? 432 VAL C CG2 1 
ATOM   10118 N  N   . ARG C 1 433 ? -7.164  -57.553 32.696  1.00 92.13  ? 433 ARG C N   1 
ATOM   10119 C  CA  . ARG C 1 433 ? -7.828  -56.253 32.738  1.00 96.78  ? 433 ARG C CA  1 
ATOM   10120 C  C   . ARG C 1 433 ? -7.163  -55.363 33.787  1.00 101.43 ? 433 ARG C C   1 
ATOM   10121 O  O   . ARG C 1 433 ? -6.589  -55.854 34.766  1.00 101.16 ? 433 ARG C O   1 
ATOM   10122 C  CB  . ARG C 1 433 ? -9.319  -56.397 33.077  1.00 92.33  ? 433 ARG C CB  1 
ATOM   10123 C  CG  . ARG C 1 433 ? -9.584  -56.209 34.557  1.00 91.69  ? 433 ARG C CG  1 
ATOM   10124 C  CD  . ARG C 1 433 ? -10.882 -56.810 35.026  1.00 91.34  ? 433 ARG C CD  1 
ATOM   10125 N  NE  . ARG C 1 433 ? -11.122 -56.437 36.414  1.00 95.21  ? 433 ARG C NE  1 
ATOM   10126 C  CZ  . ARG C 1 433 ? -11.054 -57.266 37.448  1.00 98.27  ? 433 ARG C CZ  1 
ATOM   10127 N  NH1 . ARG C 1 433 ? -10.742 -58.542 37.293  1.00 100.27 ? 433 ARG C NH1 1 
ATOM   10128 N  NH2 . ARG C 1 433 ? -11.308 -56.801 38.669  1.00 96.67  ? 433 ARG C NH2 1 
ATOM   10129 N  N   . ARG C 1 434 ? -7.261  -54.047 33.595  1.00 107.44 ? 434 ARG C N   1 
ATOM   10130 C  CA  . ARG C 1 434 ? -6.682  -53.115 34.565  1.00 103.79 ? 434 ARG C CA  1 
ATOM   10131 C  C   . ARG C 1 434 ? -7.660  -52.870 35.709  1.00 106.55 ? 434 ARG C C   1 
ATOM   10132 O  O   . ARG C 1 434 ? -8.678  -52.202 35.535  1.00 107.75 ? 434 ARG C O   1 
ATOM   10133 C  CB  . ARG C 1 434 ? -6.294  -51.779 33.912  1.00 103.77 ? 434 ARG C CB  1 
ATOM   10134 C  CG  . ARG C 1 434 ? -7.226  -50.629 34.301  1.00 104.85 ? 434 ARG C CG  1 
ATOM   10135 C  CD  . ARG C 1 434 ? -7.105  -49.422 33.385  1.00 111.29 ? 434 ARG C CD  1 
ATOM   10136 N  NE  . ARG C 1 434 ? -8.210  -49.340 32.436  1.00 111.20 ? 434 ARG C NE  1 
ATOM   10137 C  CZ  . ARG C 1 434 ? -8.319  -48.420 31.486  1.00 110.43 ? 434 ARG C CZ  1 
ATOM   10138 N  NH1 . ARG C 1 434 ? -7.408  -47.473 31.332  1.00 109.59 ? 434 ARG C NH1 1 
ATOM   10139 N  NH2 . ARG C 1 434 ? -9.366  -48.458 30.666  1.00 100.16 ? 434 ARG C NH2 1 
ATOM   10140 N  N   . SER D 2 2   ? 16.664  -41.863 -34.654 1.00 93.84  ? 2   SER D N   1 
ATOM   10141 C  CA  . SER D 2 2   ? 18.081  -41.909 -34.308 1.00 87.55  ? 2   SER D CA  1 
ATOM   10142 C  C   . SER D 2 2   ? 18.730  -43.175 -34.851 1.00 83.89  ? 2   SER D C   1 
ATOM   10143 O  O   . SER D 2 2   ? 18.096  -43.922 -35.608 1.00 83.52  ? 2   SER D O   1 
ATOM   10144 C  CB  . SER D 2 2   ? 18.287  -41.829 -32.796 1.00 86.60  ? 2   SER D CB  1 
ATOM   10145 O  OG  . SER D 2 2   ? 17.327  -40.959 -32.214 1.00 84.78  ? 2   SER D OG  1 
ATOM   10146 N  N   . ASP D 2 3   ? 19.986  -43.422 -34.457 1.00 70.44  ? 3   ASP D N   1 
ATOM   10147 C  CA  . ASP D 2 3   ? 20.780  -44.451 -35.115 1.00 63.50  ? 3   ASP D CA  1 
ATOM   10148 C  C   . ASP D 2 3   ? 20.708  -45.805 -34.428 1.00 63.21  ? 3   ASP D C   1 
ATOM   10149 O  O   . ASP D 2 3   ? 21.112  -46.806 -35.028 1.00 59.56  ? 3   ASP D O   1 
ATOM   10150 C  CB  . ASP D 2 3   ? 22.239  -44.000 -35.250 1.00 56.61  ? 3   ASP D CB  1 
ATOM   10151 C  CG  . ASP D 2 3   ? 22.877  -43.632 -33.914 1.00 60.28  ? 3   ASP D CG  1 
ATOM   10152 O  OD1 . ASP D 2 3   ? 23.121  -44.507 -33.053 1.00 60.75  ? 3   ASP D OD1 1 
ATOM   10153 O  OD2 . ASP D 2 3   ? 23.101  -42.408 -33.735 1.00 64.93  ? 3   ASP D OD2 1 
ATOM   10154 N  N   . GLY D 2 4   ? 20.206  -45.868 -33.203 1.00 56.93  ? 4   GLY D N   1 
ATOM   10155 C  CA  . GLY D 2 4   ? 19.980  -47.164 -32.602 1.00 49.11  ? 4   GLY D CA  1 
ATOM   10156 C  C   . GLY D 2 4   ? 21.220  -47.929 -32.207 1.00 44.66  ? 4   GLY D C   1 
ATOM   10157 O  O   . GLY D 2 4   ? 21.131  -49.137 -31.972 1.00 45.17  ? 4   GLY D O   1 
ATOM   10158 N  N   . LEU D 2 5   ? 22.373  -47.259 -32.095 1.00 45.36  ? 5   LEU D N   1 
ATOM   10159 C  CA  . LEU D 2 5   ? 23.614  -47.967 -31.785 1.00 38.25  ? 5   LEU D CA  1 
ATOM   10160 C  C   . LEU D 2 5   ? 23.523  -48.706 -30.444 1.00 38.52  ? 5   LEU D C   1 
ATOM   10161 O  O   . LEU D 2 5   ? 24.088  -49.795 -30.298 1.00 41.74  ? 5   LEU D O   1 
ATOM   10162 C  CB  . LEU D 2 5   ? 24.786  -46.987 -31.767 1.00 41.10  ? 5   LEU D CB  1 
ATOM   10163 C  CG  . LEU D 2 5   ? 26.197  -47.557 -31.481 1.00 38.08  ? 5   LEU D CG  1 
ATOM   10164 C  CD1 . LEU D 2 5   ? 26.521  -48.697 -32.467 1.00 39.54  ? 5   LEU D CD1 1 
ATOM   10165 C  CD2 . LEU D 2 5   ? 27.237  -46.434 -31.540 1.00 37.11  ? 5   LEU D CD2 1 
ATOM   10166 N  N   . PHE D 2 6   ? 22.836  -48.123 -29.453 1.00 34.93  ? 6   PHE D N   1 
ATOM   10167 C  CA  . PHE D 2 6   ? 22.715  -48.707 -28.115 1.00 33.38  ? 6   PHE D CA  1 
ATOM   10168 C  C   . PHE D 2 6   ? 21.468  -49.566 -27.940 1.00 36.28  ? 6   PHE D C   1 
ATOM   10169 O  O   . PHE D 2 6   ? 21.196  -50.004 -26.818 1.00 38.48  ? 6   PHE D O   1 
ATOM   10170 C  CB  . PHE D 2 6   ? 22.769  -47.594 -27.049 1.00 34.04  ? 6   PHE D CB  1 
ATOM   10171 C  CG  . PHE D 2 6   ? 24.161  -47.054 -26.839 1.00 33.55  ? 6   PHE D CG  1 
ATOM   10172 C  CD1 . PHE D 2 6   ? 24.688  -46.122 -27.729 1.00 33.70  ? 6   PHE D CD1 1 
ATOM   10173 C  CD2 . PHE D 2 6   ? 24.955  -47.488 -25.778 1.00 32.01  ? 6   PHE D CD2 1 
ATOM   10174 C  CE1 . PHE D 2 6   ? 25.978  -45.629 -27.573 1.00 35.74  ? 6   PHE D CE1 1 
ATOM   10175 C  CE2 . PHE D 2 6   ? 26.267  -46.992 -25.626 1.00 35.82  ? 6   PHE D CE2 1 
ATOM   10176 C  CZ  . PHE D 2 6   ? 26.767  -46.071 -26.532 1.00 36.82  ? 6   PHE D CZ  1 
ATOM   10177 N  N   . ASP D 2 7   ? 20.757  -49.888 -29.028 1.00 38.82  ? 7   ASP D N   1 
ATOM   10178 C  CA  . ASP D 2 7   ? 19.486  -50.608 -28.907 1.00 40.36  ? 7   ASP D CA  1 
ATOM   10179 C  C   . ASP D 2 7   ? 19.649  -51.999 -28.292 1.00 38.19  ? 7   ASP D C   1 
ATOM   10180 O  O   . ASP D 2 7   ? 18.743  -52.463 -27.587 1.00 41.02  ? 7   ASP D O   1 
ATOM   10181 C  CB  . ASP D 2 7   ? 18.823  -50.703 -30.275 1.00 43.70  ? 7   ASP D CB  1 
ATOM   10182 C  CG  . ASP D 2 7   ? 17.944  -49.496 -30.567 1.00 47.79  ? 7   ASP D CG  1 
ATOM   10183 O  OD1 . ASP D 2 7   ? 18.123  -48.465 -29.880 1.00 51.18  ? 7   ASP D OD1 1 
ATOM   10184 O  OD2 . ASP D 2 7   ? 17.027  -49.609 -31.389 1.00 52.96  ? 7   ASP D OD2 1 
ATOM   10185 N  N   . GLN D 2 8   ? 20.760  -52.702 -28.559 1.00 38.39  ? 8   GLN D N   1 
ATOM   10186 C  CA  . GLN D 2 8   ? 20.948  -54.013 -27.927 1.00 39.02  ? 8   GLN D CA  1 
ATOM   10187 C  C   . GLN D 2 8   ? 20.986  -53.900 -26.406 1.00 37.00  ? 8   GLN D C   1 
ATOM   10188 O  O   . GLN D 2 8   ? 20.433  -54.756 -25.689 1.00 34.98  ? 8   GLN D O   1 
ATOM   10189 C  CB  . GLN D 2 8   ? 22.235  -54.677 -28.424 1.00 38.06  ? 8   GLN D CB  1 
ATOM   10190 C  CG  . GLN D 2 8   ? 22.536  -56.009 -27.721 1.00 36.27  ? 8   GLN D CG  1 
ATOM   10191 C  CD  . GLN D 2 8   ? 21.619  -57.158 -28.130 1.00 37.70  ? 8   GLN D CD  1 
ATOM   10192 O  OE1 . GLN D 2 8   ? 21.827  -57.776 -29.168 1.00 44.58  ? 8   GLN D OE1 1 
ATOM   10193 N  NE2 . GLN D 2 8   ? 20.620  -57.480 -27.274 1.00 36.09  ? 8   GLN D NE2 1 
ATOM   10194 N  N   . PHE D 2 9   ? 21.649  -52.861 -25.886 1.00 34.84  ? 9   PHE D N   1 
ATOM   10195 C  CA  . PHE D 2 9   ? 21.693  -52.667 -24.439 1.00 33.34  ? 9   PHE D CA  1 
ATOM   10196 C  C   . PHE D 2 9   ? 20.306  -52.339 -23.874 1.00 33.28  ? 9   PHE D C   1 
ATOM   10197 O  O   . PHE D 2 9   ? 19.954  -52.802 -22.781 1.00 32.62  ? 9   PHE D O   1 
ATOM   10198 C  CB  . PHE D 2 9   ? 22.688  -51.559 -24.057 1.00 31.76  ? 9   PHE D CB  1 
ATOM   10199 C  CG  . PHE D 2 9   ? 24.131  -51.814 -24.472 1.00 32.56  ? 9   PHE D CG  1 
ATOM   10200 C  CD1 . PHE D 2 9   ? 24.941  -52.710 -23.790 1.00 32.41  ? 9   PHE D CD1 1 
ATOM   10201 C  CD2 . PHE D 2 9   ? 24.675  -51.123 -25.565 1.00 34.07  ? 9   PHE D CD2 1 
ATOM   10202 C  CE1 . PHE D 2 9   ? 26.273  -52.904 -24.184 1.00 32.39  ? 9   PHE D CE1 1 
ATOM   10203 C  CE2 . PHE D 2 9   ? 25.999  -51.344 -25.960 1.00 34.12  ? 9   PHE D CE2 1 
ATOM   10204 C  CZ  . PHE D 2 9   ? 26.789  -52.238 -25.288 1.00 31.44  ? 9   PHE D CZ  1 
ATOM   10205 N  N   . LYS D 2 10  ? 19.498  -51.562 -24.610 1.00 35.30  ? 10  LYS D N   1 
ATOM   10206 C  CA  . LYS D 2 10  ? 18.141  -51.261 -24.165 1.00 32.47  ? 10  LYS D CA  1 
ATOM   10207 C  C   . LYS D 2 10  ? 17.289  -52.528 -24.134 1.00 38.65  ? 10  LYS D C   1 
ATOM   10208 O  O   . LYS D 2 10  ? 16.548  -52.778 -23.175 1.00 36.49  ? 10  LYS D O   1 
ATOM   10209 C  CB  . LYS D 2 10  ? 17.530  -50.233 -25.105 1.00 42.70  ? 10  LYS D CB  1 
ATOM   10210 C  CG  . LYS D 2 10  ? 18.359  -48.972 -25.172 1.00 43.78  ? 10  LYS D CG  1 
ATOM   10211 C  CD  . LYS D 2 10  ? 17.750  -47.904 -26.097 1.00 42.95  ? 10  LYS D CD  1 
ATOM   10212 C  CE  . LYS D 2 10  ? 16.466  -47.323 -25.518 1.00 47.60  ? 10  LYS D CE  1 
ATOM   10213 N  NZ  . LYS D 2 10  ? 15.260  -48.224 -25.393 1.00 52.56  ? 10  LYS D NZ  1 
ATOM   10214 N  N   . THR D 2 11  ? 17.379  -53.335 -25.197 1.00 36.25  ? 11  THR D N   1 
ATOM   10215 C  CA  . THR D 2 11  ? 16.712  -54.639 -25.229 1.00 38.91  ? 11  THR D CA  1 
ATOM   10216 C  C   . THR D 2 11  ? 17.147  -55.519 -24.058 1.00 33.95  ? 11  THR D C   1 
ATOM   10217 O  O   . THR D 2 11  ? 16.311  -56.124 -23.388 1.00 37.12  ? 11  THR D O   1 
ATOM   10218 C  CB  . THR D 2 11  ? 16.996  -55.341 -26.569 1.00 37.60  ? 11  THR D CB  1 
ATOM   10219 O  OG1 . THR D 2 11  ? 16.455  -54.575 -27.659 1.00 40.51  ? 11  THR D OG1 1 
ATOM   10220 C  CG2 . THR D 2 11  ? 16.385  -56.742 -26.616 1.00 39.11  ? 11  THR D CG2 1 
ATOM   10221 N  N   . TRP D 2 12  ? 18.462  -55.624 -23.807 1.00 31.39  ? 12  TRP D N   1 
ATOM   10222 C  CA  . TRP D 2 12  ? 18.921  -56.447 -22.690 1.00 34.27  ? 12  TRP D CA  1 
ATOM   10223 C  C   . TRP D 2 12  ? 18.342  -55.945 -21.365 1.00 36.55  ? 12  TRP D C   1 
ATOM   10224 O  O   . TRP D 2 12  ? 18.001  -56.744 -20.487 1.00 37.19  ? 12  TRP D O   1 
ATOM   10225 C  CB  . TRP D 2 12  ? 20.451  -56.444 -22.621 1.00 30.60  ? 12  TRP D CB  1 
ATOM   10226 C  CG  . TRP D 2 12  ? 21.114  -57.444 -23.553 1.00 33.19  ? 12  TRP D CG  1 
ATOM   10227 C  CD1 . TRP D 2 12  ? 20.552  -58.546 -24.122 1.00 31.77  ? 12  TRP D CD1 1 
ATOM   10228 C  CD2 . TRP D 2 12  ? 22.467  -57.396 -24.015 1.00 32.76  ? 12  TRP D CD2 1 
ATOM   10229 N  NE1 . TRP D 2 12  ? 21.485  -59.203 -24.904 1.00 31.89  ? 12  TRP D NE1 1 
ATOM   10230 C  CE2 . TRP D 2 12  ? 22.672  -58.519 -24.838 1.00 31.04  ? 12  TRP D CE2 1 
ATOM   10231 C  CE3 . TRP D 2 12  ? 23.554  -56.537 -23.743 1.00 30.97  ? 12  TRP D CE3 1 
ATOM   10232 C  CZ2 . TRP D 2 12  ? 23.912  -58.783 -25.457 1.00 36.39  ? 12  TRP D CZ2 1 
ATOM   10233 C  CZ3 . TRP D 2 12  ? 24.772  -56.803 -24.333 1.00 30.21  ? 12  TRP D CZ3 1 
ATOM   10234 C  CH2 . TRP D 2 12  ? 24.946  -57.919 -25.183 1.00 32.11  ? 12  TRP D CH2 1 
ATOM   10235 N  N   . TYR D 2 13  ? 18.242  -54.626 -21.195 1.00 33.70  ? 13  TYR D N   1 
ATOM   10236 C  CA  . TYR D 2 13  ? 17.701  -54.083 -19.951 1.00 35.12  ? 13  TYR D CA  1 
ATOM   10237 C  C   . TYR D 2 13  ? 16.207  -54.365 -19.855 1.00 38.00  ? 13  TYR D C   1 
ATOM   10238 O  O   . TYR D 2 13  ? 15.721  -54.860 -18.830 1.00 36.43  ? 13  TYR D O   1 
ATOM   10239 C  CB  . TYR D 2 13  ? 17.996  -52.582 -19.871 1.00 32.94  ? 13  TYR D CB  1 
ATOM   10240 C  CG  . TYR D 2 13  ? 17.284  -51.804 -18.778 1.00 37.19  ? 13  TYR D CG  1 
ATOM   10241 C  CD1 . TYR D 2 13  ? 17.695  -51.890 -17.434 1.00 38.39  ? 13  TYR D CD1 1 
ATOM   10242 C  CD2 . TYR D 2 13  ? 16.228  -50.949 -19.087 1.00 39.60  ? 13  TYR D CD2 1 
ATOM   10243 C  CE1 . TYR D 2 13  ? 17.028  -51.138 -16.429 1.00 37.63  ? 13  TYR D CE1 1 
ATOM   10244 C  CE2 . TYR D 2 13  ? 15.574  -50.208 -18.113 1.00 43.75  ? 13  TYR D CE2 1 
ATOM   10245 C  CZ  . TYR D 2 13  ? 15.975  -50.307 -16.783 1.00 46.38  ? 13  TYR D CZ  1 
ATOM   10246 O  OH  . TYR D 2 13  ? 15.281  -49.544 -15.842 1.00 50.86  ? 13  TYR D OH  1 
ATOM   10247 N  N   . GLU D 2 14  ? 15.459  -54.103 -20.933 1.00 35.24  ? 14  GLU D N   1 
ATOM   10248 C  CA  . GLU D 2 14  ? 14.019  -54.323 -20.877 1.00 38.60  ? 14  GLU D CA  1 
ATOM   10249 C  C   . GLU D 2 14  ? 13.681  -55.810 -20.782 1.00 40.62  ? 14  GLU D C   1 
ATOM   10250 O  O   . GLU D 2 14  ? 12.670  -56.173 -20.173 1.00 43.49  ? 14  GLU D O   1 
ATOM   10251 C  CB  . GLU D 2 14  ? 13.339  -53.680 -22.095 1.00 40.13  ? 14  GLU D CB  1 
ATOM   10252 C  CG  . GLU D 2 14  ? 13.353  -52.171 -21.974 1.00 43.73  ? 14  GLU D CG  1 
ATOM   10253 C  CD  . GLU D 2 14  ? 13.157  -51.422 -23.265 1.00 51.05  ? 14  GLU D CD  1 
ATOM   10254 O  OE1 . GLU D 2 14  ? 12.952  -52.055 -24.324 1.00 55.60  ? 14  GLU D OE1 1 
ATOM   10255 O  OE2 . GLU D 2 14  ? 13.209  -50.174 -23.211 1.00 54.79  ? 14  GLU D OE2 1 
ATOM   10256 N  N   . LYS D 2 15  ? 14.496  -56.677 -21.386 1.00 38.11  ? 15  LYS D N   1 
ATOM   10257 C  CA  . LYS D 2 15  ? 14.214  -58.111 -21.484 1.00 38.09  ? 15  LYS D CA  1 
ATOM   10258 C  C   . LYS D 2 15  ? 15.198  -58.941 -20.658 1.00 37.17  ? 15  LYS D C   1 
ATOM   10259 O  O   . LYS D 2 15  ? 15.512  -60.078 -21.013 1.00 36.20  ? 15  LYS D O   1 
ATOM   10260 C  CB  . LYS D 2 15  ? 14.206  -58.550 -22.954 1.00 44.68  ? 15  LYS D CB  1 
ATOM   10261 C  CG  . LYS D 2 15  ? 13.050  -57.889 -23.778 1.00 44.62  ? 15  LYS D CG  1 
ATOM   10262 C  CD  . LYS D 2 15  ? 12.426  -58.776 -24.881 1.00 51.02  ? 15  LYS D CD  1 
ATOM   10263 C  CE  . LYS D 2 15  ? 11.540  -59.870 -24.286 1.00 57.44  ? 15  LYS D CE  1 
ATOM   10264 N  NZ  . LYS D 2 15  ? 10.918  -59.506 -22.942 1.00 55.94  ? 15  LYS D NZ  1 
ATOM   10265 N  N   . ARG D 2 16  ? 15.663  -58.395 -19.527 1.00 39.22  ? 16  ARG D N   1 
ATOM   10266 C  CA  . ARG D 2 16  ? 16.723  -59.046 -18.750 1.00 33.81  ? 16  ARG D CA  1 
ATOM   10267 C  C   . ARG D 2 16  ? 16.299  -60.450 -18.299 1.00 33.17  ? 16  ARG D C   1 
ATOM   10268 O  O   . ARG D 2 16  ? 17.128  -61.364 -18.246 1.00 34.28  ? 16  ARG D O   1 
ATOM   10269 C  CB  . ARG D 2 16  ? 17.097  -58.177 -17.534 1.00 35.68  ? 16  ARG D CB  1 
ATOM   10270 C  CG  . ARG D 2 16  ? 15.937  -57.957 -16.574 1.00 37.43  ? 16  ARG D CG  1 
ATOM   10271 C  CD  . ARG D 2 16  ? 16.420  -57.349 -15.281 1.00 34.17  ? 16  ARG D CD  1 
ATOM   10272 N  NE  . ARG D 2 16  ? 17.377  -58.250 -14.643 1.00 33.91  ? 16  ARG D NE  1 
ATOM   10273 C  CZ  . ARG D 2 16  ? 18.121  -57.909 -13.607 1.00 32.66  ? 16  ARG D CZ  1 
ATOM   10274 N  NH1 . ARG D 2 16  ? 18.019  -56.704 -13.048 1.00 30.50  ? 16  ARG D NH1 1 
ATOM   10275 N  NH2 . ARG D 2 16  ? 19.014  -58.780 -13.130 1.00 29.15  ? 16  ARG D NH2 1 
ATOM   10276 N  N   . HIS D 2 17  ? 15.017  -60.645 -17.975 1.00 31.66  ? 17  HIS D N   1 
ATOM   10277 C  CA  . HIS D 2 17  ? 14.613  -61.954 -17.452 1.00 36.02  ? 17  HIS D CA  1 
ATOM   10278 C  C   . HIS D 2 17  ? 14.522  -62.981 -18.575 1.00 37.26  ? 17  HIS D C   1 
ATOM   10279 O  O   . HIS D 2 17  ? 14.944  -64.136 -18.418 1.00 38.00  ? 17  HIS D O   1 
ATOM   10280 C  CB  . HIS D 2 17  ? 13.286  -61.839 -16.719 1.00 37.91  ? 17  HIS D CB  1 
ATOM   10281 C  CG  . HIS D 2 17  ? 13.370  -61.014 -15.471 1.00 37.05  ? 17  HIS D CG  1 
ATOM   10282 N  ND1 . HIS D 2 17  ? 14.382  -61.156 -14.553 1.00 33.80  ? 17  HIS D ND1 1 
ATOM   10283 C  CD2 . HIS D 2 17  ? 12.577  -60.010 -15.013 1.00 37.79  ? 17  HIS D CD2 1 
ATOM   10284 C  CE1 . HIS D 2 17  ? 14.195  -60.294 -13.564 1.00 35.51  ? 17  HIS D CE1 1 
ATOM   10285 N  NE2 . HIS D 2 17  ? 13.100  -59.596 -13.814 1.00 36.03  ? 17  HIS D NE2 1 
ATOM   10286 N  N   . ASP D 2 18  ? 14.010  -62.562 -19.731 1.00 36.91  ? 18  ASP D N   1 
ATOM   10287 C  CA  . ASP D 2 18  ? 14.038  -63.420 -20.908 1.00 38.18  ? 18  ASP D CA  1 
ATOM   10288 C  C   . ASP D 2 18  ? 15.459  -63.758 -21.326 1.00 37.07  ? 18  ASP D C   1 
ATOM   10289 O  O   . ASP D 2 18  ? 15.729  -64.885 -21.754 1.00 38.33  ? 18  ASP D O   1 
ATOM   10290 C  CB  . ASP D 2 18  ? 13.274  -62.748 -22.043 1.00 40.43  ? 18  ASP D CB  1 
ATOM   10291 C  CG  . ASP D 2 18  ? 11.780  -62.988 -21.953 1.00 47.29  ? 18  ASP D CG  1 
ATOM   10292 O  OD1 . ASP D 2 18  ? 11.347  -63.959 -21.270 1.00 49.73  ? 18  ASP D OD1 1 
ATOM   10293 O  OD2 . ASP D 2 18  ? 11.041  -62.158 -22.503 1.00 49.98  ? 18  ASP D OD2 1 
ATOM   10294 N  N   . TYR D 2 19  ? 16.384  -62.804 -21.224 1.00 35.17  ? 19  TYR D N   1 
ATOM   10295 C  CA  . TYR D 2 19  ? 17.775  -63.124 -21.545 1.00 36.44  ? 19  TYR D CA  1 
ATOM   10296 C  C   . TYR D 2 19  ? 18.297  -64.251 -20.671 1.00 34.28  ? 19  TYR D C   1 
ATOM   10297 O  O   . TYR D 2 19  ? 18.947  -65.178 -21.163 1.00 34.00  ? 19  TYR D O   1 
ATOM   10298 C  CB  . TYR D 2 19  ? 18.657  -61.901 -21.390 1.00 36.59  ? 19  TYR D CB  1 
ATOM   10299 C  CG  . TYR D 2 19  ? 20.134  -62.233 -21.533 1.00 32.03  ? 19  TYR D CG  1 
ATOM   10300 C  CD1 . TYR D 2 19  ? 20.897  -62.633 -20.402 1.00 31.31  ? 19  TYR D CD1 1 
ATOM   10301 C  CD2 . TYR D 2 19  ? 20.763  -62.176 -22.760 1.00 31.70  ? 19  TYR D CD2 1 
ATOM   10302 C  CE1 . TYR D 2 19  ? 22.238  -62.938 -20.523 1.00 32.58  ? 19  TYR D CE1 1 
ATOM   10303 C  CE2 . TYR D 2 19  ? 22.092  -62.485 -22.881 1.00 31.79  ? 19  TYR D CE2 1 
ATOM   10304 C  CZ  . TYR D 2 19  ? 22.821  -62.873 -21.781 1.00 32.09  ? 19  TYR D CZ  1 
ATOM   10305 O  OH  . TYR D 2 19  ? 24.141  -63.181 -21.977 1.00 32.62  ? 19  TYR D OH  1 
ATOM   10306 N  N   . ALA D 2 20  ? 17.986  -64.195 -19.374 1.00 29.70  ? 20  ALA D N   1 
ATOM   10307 C  CA  . ALA D 2 20  ? 18.523  -65.145 -18.411 1.00 31.28  ? 20  ALA D CA  1 
ATOM   10308 C  C   . ALA D 2 20  ? 17.975  -66.542 -18.645 1.00 32.40  ? 20  ALA D C   1 
ATOM   10309 O  O   . ALA D 2 20  ? 18.727  -67.524 -18.650 1.00 34.64  ? 20  ALA D O   1 
ATOM   10310 C  CB  . ALA D 2 20  ? 18.202  -64.670 -17.008 1.00 27.54  ? 20  ALA D CB  1 
ATOM   10311 N  N   . ARG D 2 21  ? 16.671  -66.655 -18.856 1.00 32.62  ? 21  ARG D N   1 
ATOM   10312 C  CA  . ARG D 2 21  ? 16.113  -67.964 -19.115 1.00 36.41  ? 21  ARG D CA  1 
ATOM   10313 C  C   . ARG D 2 21  ? 16.712  -68.554 -20.385 1.00 39.17  ? 21  ARG D C   1 
ATOM   10314 O  O   . ARG D 2 21  ? 16.984  -69.757 -20.450 1.00 41.19  ? 21  ARG D O   1 
ATOM   10315 C  CB  . ARG D 2 21  ? 14.595  -67.860 -19.234 1.00 39.57  ? 21  ARG D CB  1 
ATOM   10316 C  CG  . ARG D 2 21  ? 13.958  -67.511 -17.946 1.00 33.61  ? 21  ARG D CG  1 
ATOM   10317 C  CD  . ARG D 2 21  ? 12.445  -67.550 -18.096 1.00 40.69  ? 21  ARG D CD  1 
ATOM   10318 N  NE  . ARG D 2 21  ? 11.958  -66.352 -18.761 1.00 47.00  ? 21  ARG D NE  1 
ATOM   10319 C  CZ  . ARG D 2 21  ? 11.433  -65.320 -18.116 1.00 46.40  ? 21  ARG D CZ  1 
ATOM   10320 N  NH1 . ARG D 2 21  ? 11.299  -65.333 -16.794 1.00 39.44  ? 21  ARG D NH1 1 
ATOM   10321 N  NH2 . ARG D 2 21  ? 11.026  -64.260 -18.816 1.00 45.10  ? 21  ARG D NH2 1 
ATOM   10322 N  N   . ASP D 2 22  ? 16.884  -67.729 -21.423 1.00 37.16  ? 22  ASP D N   1 
ATOM   10323 C  CA  . ASP D 2 22  ? 17.451  -68.224 -22.677 1.00 41.68  ? 22  ASP D CA  1 
ATOM   10324 C  C   . ASP D 2 22  ? 18.903  -68.610 -22.488 1.00 41.43  ? 22  ASP D C   1 
ATOM   10325 O  O   . ASP D 2 22  ? 19.366  -69.597 -23.067 1.00 38.88  ? 22  ASP D O   1 
ATOM   10326 C  CB  . ASP D 2 22  ? 17.327  -67.171 -23.793 1.00 44.05  ? 22  ASP D CB  1 
ATOM   10327 C  CG  . ASP D 2 22  ? 17.976  -67.627 -25.108 1.00 45.17  ? 22  ASP D CG  1 
ATOM   10328 O  OD1 . ASP D 2 22  ? 17.410  -68.494 -25.789 1.00 46.09  ? 22  ASP D OD1 1 
ATOM   10329 O  OD2 . ASP D 2 22  ? 19.077  -67.127 -25.443 1.00 50.16  ? 22  ASP D OD2 1 
ATOM   10330 N  N   . TRP D 2 23  ? 19.634  -67.829 -21.699 1.00 37.30  ? 23  TRP D N   1 
ATOM   10331 C  CA  . TRP D 2 23  ? 21.014  -68.169 -21.364 1.00 36.21  ? 23  TRP D CA  1 
ATOM   10332 C  C   . TRP D 2 23  ? 21.081  -69.549 -20.711 1.00 38.26  ? 23  TRP D C   1 
ATOM   10333 O  O   . TRP D 2 23  ? 21.984  -70.347 -21.004 1.00 40.27  ? 23  TRP D O   1 
ATOM   10334 C  CB  . TRP D 2 23  ? 21.598  -67.081 -20.453 1.00 35.31  ? 23  TRP D CB  1 
ATOM   10335 C  CG  . TRP D 2 23  ? 23.025  -67.319 -20.130 1.00 34.06  ? 23  TRP D CG  1 
ATOM   10336 C  CD1 . TRP D 2 23  ? 24.105  -66.819 -20.784 1.00 34.39  ? 23  TRP D CD1 1 
ATOM   10337 C  CD2 . TRP D 2 23  ? 23.536  -68.110 -19.047 1.00 30.73  ? 23  TRP D CD2 1 
ATOM   10338 N  NE1 . TRP D 2 23  ? 25.270  -67.267 -20.191 1.00 37.88  ? 23  TRP D NE1 1 
ATOM   10339 C  CE2 . TRP D 2 23  ? 24.940  -68.071 -19.131 1.00 30.98  ? 23  TRP D CE2 1 
ATOM   10340 C  CE3 . TRP D 2 23  ? 22.940  -68.899 -18.059 1.00 32.15  ? 23  TRP D CE3 1 
ATOM   10341 C  CZ2 . TRP D 2 23  ? 25.767  -68.756 -18.224 1.00 31.28  ? 23  TRP D CZ2 1 
ATOM   10342 C  CZ3 . TRP D 2 23  ? 23.761  -69.582 -17.177 1.00 34.87  ? 23  TRP D CZ3 1 
ATOM   10343 C  CH2 . TRP D 2 23  ? 25.165  -69.486 -17.254 1.00 28.82  ? 23  TRP D CH2 1 
ATOM   10344 N  N   . LYS D 2 24  ? 20.088  -69.890 -19.891 1.00 34.49  ? 24  LYS D N   1 
ATOM   10345 C  CA  . LYS D 2 24  ? 20.115  -71.221 -19.269 1.00 39.34  ? 24  LYS D CA  1 
ATOM   10346 C  C   . LYS D 2 24  ? 19.930  -72.324 -20.301 1.00 39.45  ? 24  LYS D C   1 
ATOM   10347 O  O   . LYS D 2 24  ? 20.581  -73.374 -20.230 1.00 39.39  ? 24  LYS D O   1 
ATOM   10348 C  CB  . LYS D 2 24  ? 19.056  -71.345 -18.192 1.00 38.66  ? 24  LYS D CB  1 
ATOM   10349 C  CG  . LYS D 2 24  ? 19.351  -70.487 -17.008 1.00 34.28  ? 24  LYS D CG  1 
ATOM   10350 C  CD  . LYS D 2 24  ? 18.203  -70.484 -16.022 1.00 38.42  ? 24  LYS D CD  1 
ATOM   10351 C  CE  . LYS D 2 24  ? 18.223  -71.711 -15.148 1.00 40.53  ? 24  LYS D CE  1 
ATOM   10352 N  NZ  . LYS D 2 24  ? 16.919  -71.811 -14.413 1.00 40.58  ? 24  LYS D NZ  1 
ATOM   10353 N  N   . VAL D 2 25  ? 19.021  -72.128 -21.241 1.00 42.71  ? 25  VAL D N   1 
ATOM   10354 C  CA  . VAL D 2 25  ? 18.826  -73.193 -22.212 1.00 44.06  ? 25  VAL D CA  1 
ATOM   10355 C  C   . VAL D 2 25  ? 20.060  -73.325 -23.093 1.00 45.91  ? 25  VAL D C   1 
ATOM   10356 O  O   . VAL D 2 25  ? 20.431  -74.439 -23.474 1.00 50.84  ? 25  VAL D O   1 
ATOM   10357 C  CB  . VAL D 2 25  ? 17.541  -72.968 -23.033 1.00 51.87  ? 25  VAL D CB  1 
ATOM   10358 C  CG1 . VAL D 2 25  ? 16.393  -72.528 -22.156 1.00 46.24  ? 25  VAL D CG1 1 
ATOM   10359 C  CG2 . VAL D 2 25  ? 17.771  -71.925 -24.126 1.00 52.76  ? 25  VAL D CG2 1 
ATOM   10360 N  N   . ARG D 2 26  ? 20.728  -72.209 -23.406 1.00 44.30  ? 26  ARG D N   1 
ATOM   10361 C  CA  . ARG D 2 26  ? 21.852  -72.243 -24.344 1.00 49.89  ? 26  ARG D CA  1 
ATOM   10362 C  C   . ARG D 2 26  ? 23.073  -72.896 -23.708 1.00 47.33  ? 26  ARG D C   1 
ATOM   10363 O  O   . ARG D 2 26  ? 23.852  -73.578 -24.386 1.00 49.31  ? 26  ARG D O   1 
ATOM   10364 C  CB  . ARG D 2 26  ? 22.220  -70.819 -24.806 1.00 44.66  ? 26  ARG D CB  1 
ATOM   10365 C  CG  . ARG D 2 26  ? 21.382  -70.238 -25.956 1.00 51.08  ? 26  ARG D CG  1 
ATOM   10366 C  CD  . ARG D 2 26  ? 21.923  -68.862 -26.418 1.00 50.08  ? 26  ARG D CD  1 
ATOM   10367 N  NE  . ARG D 2 26  ? 21.909  -67.820 -25.399 1.00 45.26  ? 26  ARG D NE  1 
ATOM   10368 C  CZ  . ARG D 2 26  ? 22.895  -66.930 -25.254 1.00 48.26  ? 26  ARG D CZ  1 
ATOM   10369 N  NH1 . ARG D 2 26  ? 23.970  -66.967 -26.025 1.00 52.94  ? 26  ARG D NH1 1 
ATOM   10370 N  NH2 . ARG D 2 26  ? 22.795  -65.975 -24.331 1.00 41.47  ? 26  ARG D NH2 1 
ATOM   10371 N  N   . THR D 2 27  ? 23.281  -72.651 -22.421 1.00 43.96  ? 27  THR D N   1 
ATOM   10372 C  CA  . THR D 2 27  ? 24.509  -73.024 -21.745 1.00 38.79  ? 27  THR D CA  1 
ATOM   10373 C  C   . THR D 2 27  ? 24.345  -74.208 -20.826 1.00 39.83  ? 27  THR D C   1 
ATOM   10374 O  O   . THR D 2 27  ? 25.342  -74.856 -20.501 1.00 46.32  ? 27  THR D O   1 
ATOM   10375 C  CB  . THR D 2 27  ? 25.048  -71.842 -20.914 1.00 39.87  ? 27  THR D CB  1 
ATOM   10376 O  OG1 . THR D 2 27  ? 24.222  -71.675 -19.752 1.00 38.93  ? 27  THR D OG1 1 
ATOM   10377 C  CG2 . THR D 2 27  ? 25.112  -70.550 -21.732 1.00 37.45  ? 27  THR D CG2 1 
ATOM   10378 N  N   . GLY D 2 28  ? 23.127  -74.499 -20.388 1.00 42.75  ? 28  GLY D N   1 
ATOM   10379 C  CA  . GLY D 2 28  ? 22.926  -75.425 -19.294 1.00 42.07  ? 28  GLY D CA  1 
ATOM   10380 C  C   . GLY D 2 28  ? 23.428  -74.973 -17.951 1.00 40.07  ? 28  GLY D C   1 
ATOM   10381 O  O   . GLY D 2 28  ? 23.531  -75.803 -17.041 1.00 40.57  ? 28  GLY D O   1 
ATOM   10382 N  N   . GLY D 2 29  ? 23.773  -73.668 -17.782 1.00 37.32  ? 29  GLY D N   1 
ATOM   10383 C  CA  . GLY D 2 29  ? 24.295  -73.197 -16.522 1.00 35.24  ? 29  GLY D CA  1 
ATOM   10384 C  C   . GLY D 2 29  ? 23.221  -72.744 -15.523 1.00 33.41  ? 29  GLY D C   1 
ATOM   10385 O  O   . GLY D 2 29  ? 22.018  -72.687 -15.808 1.00 38.49  ? 29  GLY D O   1 
ATOM   10386 N  N   . GLN D 2 30  ? 23.691  -72.479 -14.325 1.00 31.56  ? 30  GLN D N   1 
ATOM   10387 C  CA  . GLN D 2 30  ? 22.930  -71.941 -13.200 1.00 31.46  ? 30  GLN D CA  1 
ATOM   10388 C  C   . GLN D 2 30  ? 22.979  -70.419 -13.251 1.00 31.88  ? 30  GLN D C   1 
ATOM   10389 O  O   . GLN D 2 30  ? 23.993  -69.851 -13.651 1.00 30.27  ? 30  GLN D O   1 
ATOM   10390 C  CB  . GLN D 2 30  ? 23.549  -72.416 -11.888 1.00 35.20  ? 30  GLN D CB  1 
ATOM   10391 C  CG  . GLN D 2 30  ? 23.343  -73.900 -11.519 1.00 40.58  ? 30  GLN D CG  1 
ATOM   10392 C  CD  . GLN D 2 30  ? 23.728  -74.127 -10.046 1.00 45.24  ? 30  GLN D CD  1 
ATOM   10393 O  OE1 . GLN D 2 30  ? 23.170  -73.502 -9.143  1.00 40.67  ? 30  GLN D OE1 1 
ATOM   10394 N  NE2 . GLN D 2 30  ? 24.703  -75.022 -9.807  1.00 49.67  ? 30  GLN D NE2 1 
ATOM   10395 N  N   . VAL D 2 31  ? 21.888  -69.782 -12.816 1.00 27.15  ? 31  VAL D N   1 
ATOM   10396 C  CA  . VAL D 2 31  ? 21.809  -68.327 -12.647 1.00 26.80  ? 31  VAL D CA  1 
ATOM   10397 C  C   . VAL D 2 31  ? 21.858  -68.015 -11.153 1.00 27.03  ? 31  VAL D C   1 
ATOM   10398 O  O   . VAL D 2 31  ? 21.288  -68.731 -10.317 1.00 26.49  ? 31  VAL D O   1 
ATOM   10399 C  CB  . VAL D 2 31  ? 20.543  -67.734 -13.315 1.00 26.42  ? 31  VAL D CB  1 
ATOM   10400 C  CG1 . VAL D 2 31  ? 20.458  -66.189 -13.055 1.00 24.25  ? 31  VAL D CG1 1 
ATOM   10401 C  CG2 . VAL D 2 31  ? 20.580  -68.020 -14.859 1.00 29.18  ? 31  VAL D CG2 1 
ATOM   10402 N  N   . VAL D 2 32  ? 22.526  -66.926 -10.805 1.00 23.68  ? 32  VAL D N   1 
ATOM   10403 C  CA  . VAL D 2 32  ? 22.699  -66.593 -9.403  1.00 24.89  ? 32  VAL D CA  1 
ATOM   10404 C  C   . VAL D 2 32  ? 22.315  -65.132 -9.241  1.00 26.19  ? 32  VAL D C   1 
ATOM   10405 O  O   . VAL D 2 32  ? 22.908  -64.254 -9.876  1.00 24.97  ? 32  VAL D O   1 
ATOM   10406 C  CB  . VAL D 2 32  ? 24.133  -66.869 -8.899  1.00 27.21  ? 32  VAL D CB  1 
ATOM   10407 C  CG1 . VAL D 2 32  ? 25.166  -66.258 -9.792  1.00 30.77  ? 32  VAL D CG1 1 
ATOM   10408 C  CG2 . VAL D 2 32  ? 24.292  -66.360 -7.428  1.00 25.21  ? 32  VAL D CG2 1 
ATOM   10409 N  N   . ALA D 2 33  ? 21.277  -64.883 -8.458  1.00 22.65  ? 33  ALA D N   1 
ATOM   10410 C  CA  . ALA D 2 33  ? 20.900  -63.495 -8.151  1.00 22.77  ? 33  ALA D CA  1 
ATOM   10411 C  C   . ALA D 2 33  ? 21.942  -62.858 -7.219  1.00 25.50  ? 33  ALA D C   1 
ATOM   10412 O  O   . ALA D 2 33  ? 22.276  -63.404 -6.165  1.00 24.93  ? 33  ALA D O   1 
ATOM   10413 C  CB  . ALA D 2 33  ? 19.517  -63.485 -7.517  1.00 21.53  ? 33  ALA D CB  1 
ATOM   10414 N  N   . THR D 2 34  ? 22.493  -61.716 -7.605  1.00 23.29  ? 34  THR D N   1 
ATOM   10415 C  CA  . THR D 2 34  ? 23.579  -61.129 -6.835  1.00 22.62  ? 34  THR D CA  1 
ATOM   10416 C  C   . THR D 2 34  ? 23.082  -59.825 -6.245  1.00 24.06  ? 34  THR D C   1 
ATOM   10417 O  O   . THR D 2 34  ? 22.187  -59.172 -6.798  1.00 25.25  ? 34  THR D O   1 
ATOM   10418 C  CB  . THR D 2 34  ? 24.840  -60.872 -7.675  1.00 22.84  ? 34  THR D CB  1 
ATOM   10419 O  OG1 . THR D 2 34  ? 24.590  -59.872 -8.671  1.00 24.54  ? 34  THR D OG1 1 
ATOM   10420 C  CG2 . THR D 2 34  ? 25.316  -62.195 -8.383  1.00 22.64  ? 34  THR D CG2 1 
ATOM   10421 N  N   . MET D 2 35  ? 23.640  -59.487 -5.110  1.00 22.87  ? 35  MET D N   1 
ATOM   10422 C  CA  . MET D 2 35  ? 23.269  -58.238 -4.477  1.00 22.34  ? 35  MET D CA  1 
ATOM   10423 C  C   . MET D 2 35  ? 24.522  -57.480 -4.118  1.00 24.60  ? 35  MET D C   1 
ATOM   10424 O  O   . MET D 2 35  ? 25.491  -58.083 -3.642  1.00 26.31  ? 35  MET D O   1 
ATOM   10425 C  CB  . MET D 2 35  ? 22.439  -58.456 -3.237  1.00 25.59  ? 35  MET D CB  1 
ATOM   10426 C  CG  . MET D 2 35  ? 20.996  -59.000 -3.558  1.00 26.36  ? 35  MET D CG  1 
ATOM   10427 S  SD  . MET D 2 35  ? 20.205  -59.704 -2.062  1.00 26.80  ? 35  MET D SD  1 
ATOM   10428 C  CE  . MET D 2 35  ? 18.742  -60.441 -2.857  1.00 26.13  ? 35  MET D CE  1 
ATOM   10429 N  N   . CYS D 2 36  ? 24.445  -56.150 -4.264  1.00 24.90  ? 36  CYS D N   1 
ATOM   10430 C  CA  . CYS D 2 36  ? 25.579  -55.231 -4.134  1.00 27.71  ? 36  CYS D CA  1 
ATOM   10431 C  C   . CYS D 2 36  ? 26.684  -55.460 -5.175  1.00 28.74  ? 36  CYS D C   1 
ATOM   10432 O  O   . CYS D 2 36  ? 27.069  -56.597 -5.536  1.00 26.22  ? 36  CYS D O   1 
ATOM   10433 C  CB  . CYS D 2 36  ? 26.170  -55.282 -2.708  1.00 25.92  ? 36  CYS D CB  1 
ATOM   10434 S  SG  . CYS D 2 36  ? 27.477  -54.018 -2.426  1.00 24.41  ? 36  CYS D SG  1 
ATOM   10435 N  N   . THR D 2 37  ? 27.207  -54.360 -5.675  1.00 24.23  ? 37  THR D N   1 
ATOM   10436 C  CA  . THR D 2 37  ? 28.267  -54.394 -6.666  1.00 19.35  ? 37  THR D CA  1 
ATOM   10437 C  C   . THR D 2 37  ? 29.592  -54.956 -6.124  1.00 24.33  ? 37  THR D C   1 
ATOM   10438 O  O   . THR D 2 37  ? 30.512  -55.190 -6.913  1.00 23.59  ? 37  THR D O   1 
ATOM   10439 C  CB  . THR D 2 37  ? 28.538  -52.984 -7.184  1.00 24.99  ? 37  THR D CB  1 
ATOM   10440 O  OG1 . THR D 2 37  ? 28.800  -52.161 -6.036  1.00 25.32  ? 37  THR D OG1 1 
ATOM   10441 C  CG2 . THR D 2 37  ? 27.272  -52.488 -7.932  1.00 24.93  ? 37  THR D CG2 1 
ATOM   10442 N  N   . TYR D 2 38  ? 29.692  -55.268 -4.845  1.00 26.03  ? 38  TYR D N   1 
ATOM   10443 C  CA  . TYR D 2 38  ? 30.926  -55.875 -4.357  1.00 18.07  ? 38  TYR D CA  1 
ATOM   10444 C  C   . TYR D 2 38  ? 30.961  -57.404 -4.536  1.00 21.52  ? 38  TYR D C   1 
ATOM   10445 O  O   . TYR D 2 38  ? 31.972  -58.023 -4.186  1.00 23.88  ? 38  TYR D O   1 
ATOM   10446 C  CB  . TYR D 2 38  ? 31.118  -55.569 -2.868  1.00 21.06  ? 38  TYR D CB  1 
ATOM   10447 C  CG  . TYR D 2 38  ? 31.769  -54.207 -2.625  1.00 23.46  ? 38  TYR D CG  1 
ATOM   10448 C  CD1 . TYR D 2 38  ? 33.082  -53.937 -3.090  1.00 20.60  ? 38  TYR D CD1 1 
ATOM   10449 C  CD2 . TYR D 2 38  ? 31.093  -53.212 -1.920  1.00 24.32  ? 38  TYR D CD2 1 
ATOM   10450 C  CE1 . TYR D 2 38  ? 33.698  -52.687 -2.864  1.00 21.99  ? 38  TYR D CE1 1 
ATOM   10451 C  CE2 . TYR D 2 38  ? 31.711  -51.979 -1.680  1.00 23.48  ? 38  TYR D CE2 1 
ATOM   10452 C  CZ  . TYR D 2 38  ? 32.993  -51.746 -2.128  1.00 24.13  ? 38  TYR D CZ  1 
ATOM   10453 O  OH  . TYR D 2 38  ? 33.632  -50.548 -1.910  1.00 22.80  ? 38  TYR D OH  1 
ATOM   10454 N  N   . THR D 2 39  ? 29.910  -58.017 -5.088  1.00 22.75  ? 39  THR D N   1 
ATOM   10455 C  CA  . THR D 2 39  ? 29.910  -59.461 -5.355  1.00 23.37  ? 39  THR D CA  1 
ATOM   10456 C  C   . THR D 2 39  ? 31.114  -59.869 -6.201  1.00 21.50  ? 39  THR D C   1 
ATOM   10457 O  O   . THR D 2 39  ? 31.410  -59.226 -7.205  1.00 20.94  ? 39  THR D O   1 
ATOM   10458 C  CB  . THR D 2 39  ? 28.616  -59.883 -6.058  1.00 25.08  ? 39  THR D CB  1 
ATOM   10459 O  OG1 . THR D 2 39  ? 27.524  -59.812 -5.134  1.00 25.79  ? 39  THR D OG1 1 
ATOM   10460 C  CG2 . THR D 2 39  ? 28.737  -61.334 -6.577  1.00 21.39  ? 39  THR D CG2 1 
ATOM   10461 N  N   . PRO D 2 40  ? 31.862  -60.836 -5.799  1.00 26.43  ? 40  PRO D N   1 
ATOM   10462 C  CA  . PRO D 2 40  ? 33.060  -61.143 -6.578  1.00 26.48  ? 40  PRO D CA  1 
ATOM   10463 C  C   . PRO D 2 40  ? 32.653  -62.034 -7.749  1.00 23.21  ? 40  PRO D C   1 
ATOM   10464 O  O   . PRO D 2 40  ? 32.695  -63.275 -7.740  1.00 22.03  ? 40  PRO D O   1 
ATOM   10465 C  CB  . PRO D 2 40  ? 33.972  -61.806 -5.543  1.00 28.63  ? 40  PRO D CB  1 
ATOM   10466 C  CG  . PRO D 2 40  ? 32.980  -62.437 -4.574  1.00 26.24  ? 40  PRO D CG  1 
ATOM   10467 C  CD  . PRO D 2 40  ? 31.796  -61.583 -4.530  1.00 23.59  ? 40  PRO D CD  1 
ATOM   10468 N  N   . GLU D 2 41  ? 32.212  -61.383 -8.819  1.00 24.85  ? 41  GLU D N   1 
ATOM   10469 C  CA  . GLU D 2 41  ? 31.526  -62.164 -9.820  1.00 26.31  ? 41  GLU D CA  1 
ATOM   10470 C  C   . GLU D 2 41  ? 32.462  -63.040 -10.623 1.00 23.17  ? 41  GLU D C   1 
ATOM   10471 O  O   . GLU D 2 41  ? 31.963  -64.009 -11.215 1.00 27.04  ? 41  GLU D O   1 
ATOM   10472 C  CB  . GLU D 2 41  ? 30.650  -61.270 -10.696 1.00 31.02  ? 41  GLU D CB  1 
ATOM   10473 C  CG  . GLU D 2 41  ? 31.371  -60.169 -11.311 1.00 31.00  ? 41  GLU D CG  1 
ATOM   10474 C  CD  . GLU D 2 41  ? 30.409  -59.228 -12.063 1.00 35.79  ? 41  GLU D CD  1 
ATOM   10475 O  OE1 . GLU D 2 41  ? 29.253  -59.616 -12.363 1.00 39.83  ? 41  GLU D OE1 1 
ATOM   10476 O  OE2 . GLU D 2 41  ? 30.796  -58.087 -12.276 1.00 35.08  ? 41  GLU D OE2 1 
ATOM   10477 N  N   . GLU D 2 42  ? 33.794  -62.830 -10.538 1.00 19.65  ? 42  GLU D N   1 
ATOM   10478 C  CA  . GLU D 2 42  ? 34.750  -63.712 -11.224 1.00 22.54  ? 42  GLU D CA  1 
ATOM   10479 C  C   . GLU D 2 42  ? 34.569  -65.166 -10.805 1.00 21.82  ? 42  GLU D C   1 
ATOM   10480 O  O   . GLU D 2 42  ? 34.753  -66.110 -11.610 1.00 22.98  ? 42  GLU D O   1 
ATOM   10481 C  CB  . GLU D 2 42  ? 36.181  -63.270 -10.872 1.00 20.34  ? 42  GLU D CB  1 
ATOM   10482 C  CG  . GLU D 2 42  ? 36.550  -61.897 -11.484 1.00 22.94  ? 42  GLU D CG  1 
ATOM   10483 C  CD  . GLU D 2 42  ? 36.167  -60.695 -10.628 1.00 27.37  ? 42  GLU D CD  1 
ATOM   10484 O  OE1 . GLU D 2 42  ? 35.411  -60.864 -9.628  1.00 27.06  ? 42  GLU D OE1 1 
ATOM   10485 O  OE2 . GLU D 2 42  ? 36.716  -59.586 -10.908 1.00 27.42  ? 42  GLU D OE2 1 
ATOM   10486 N  N   . LEU D 2 43  ? 34.313  -65.359 -9.516  1.00 23.10  ? 43  LEU D N   1 
ATOM   10487 C  CA  . LEU D 2 43  ? 34.120  -66.697 -8.952  1.00 21.47  ? 43  LEU D CA  1 
ATOM   10488 C  C   . LEU D 2 43  ? 32.887  -67.348 -9.539  1.00 23.82  ? 43  LEU D C   1 
ATOM   10489 O  O   . LEU D 2 43  ? 32.878  -68.554 -9.812  1.00 24.82  ? 43  LEU D O   1 
ATOM   10490 C  CB  . LEU D 2 43  ? 33.964  -66.608 -7.414  1.00 22.38  ? 43  LEU D CB  1 
ATOM   10491 C  CG  . LEU D 2 43  ? 35.235  -66.686 -6.581  1.00 28.12  ? 43  LEU D CG  1 
ATOM   10492 C  CD1 . LEU D 2 43  ? 36.215  -65.696 -7.055  1.00 28.60  ? 43  LEU D CD1 1 
ATOM   10493 C  CD2 . LEU D 2 43  ? 34.916  -66.461 -5.095  1.00 25.48  ? 43  LEU D CD2 1 
ATOM   10494 N  N   . LEU D 2 44  ? 31.792  -66.591 -9.633  1.00 23.80  ? 44  LEU D N   1 
ATOM   10495 C  CA  . LEU D 2 44  ? 30.553  -67.157 -10.167 1.00 26.66  ? 44  LEU D CA  1 
ATOM   10496 C  C   . LEU D 2 44  ? 30.716  -67.536 -11.630 1.00 27.19  ? 44  LEU D C   1 
ATOM   10497 O  O   . LEU D 2 44  ? 30.276  -68.621 -12.062 1.00 26.35  ? 44  LEU D O   1 
ATOM   10498 C  CB  . LEU D 2 44  ? 29.410  -66.166 -9.990  1.00 23.76  ? 44  LEU D CB  1 
ATOM   10499 C  CG  . LEU D 2 44  ? 29.223  -65.723 -8.557  1.00 24.62  ? 44  LEU D CG  1 
ATOM   10500 C  CD1 . LEU D 2 44  ? 28.225  -64.604 -8.463  1.00 26.97  ? 44  LEU D CD1 1 
ATOM   10501 C  CD2 . LEU D 2 44  ? 28.722  -66.920 -7.750  1.00 28.46  ? 44  LEU D CD2 1 
ATOM   10502 N  N   . ILE D 2 45  ? 31.409  -66.687 -12.389 1.00 24.56  ? 45  ILE D N   1 
ATOM   10503 C  CA  . ILE D 2 45  ? 31.622  -66.951 -13.803 1.00 25.10  ? 45  ILE D CA  1 
ATOM   10504 C  C   . ILE D 2 45  ? 32.492  -68.186 -13.957 1.00 25.63  ? 45  ILE D C   1 
ATOM   10505 O  O   . ILE D 2 45  ? 32.182  -69.085 -14.739 1.00 29.46  ? 45  ILE D O   1 
ATOM   10506 C  CB  . ILE D 2 45  ? 32.245  -65.718 -14.483 1.00 24.53  ? 45  ILE D CB  1 
ATOM   10507 C  CG1 . ILE D 2 45  ? 31.217  -64.574 -14.469 1.00 25.14  ? 45  ILE D CG1 1 
ATOM   10508 C  CG2 . ILE D 2 45  ? 32.706  -65.979 -15.927 1.00 27.45  ? 45  ILE D CG2 1 
ATOM   10509 C  CD1 . ILE D 2 45  ? 31.825  -63.215 -14.864 1.00 27.78  ? 45  ILE D CD1 1 
ATOM   10510 N  N   . ALA D 2 46  ? 33.568  -68.260 -13.151 1.00 25.47  ? 46  ALA D N   1 
ATOM   10511 C  CA  . ALA D 2 46  ? 34.456  -69.422 -13.186 1.00 29.10  ? 46  ALA D CA  1 
ATOM   10512 C  C   . ALA D 2 46  ? 33.714  -70.697 -12.789 1.00 28.73  ? 46  ALA D C   1 
ATOM   10513 O  O   . ALA D 2 46  ? 34.070  -71.807 -13.246 1.00 29.90  ? 46  ALA D O   1 
ATOM   10514 C  CB  . ALA D 2 46  ? 35.659  -69.166 -12.263 1.00 25.60  ? 46  ALA D CB  1 
ATOM   10515 N  N   . ALA D 2 47  ? 32.684  -70.559 -11.961 1.00 27.11  ? 47  ALA D N   1 
ATOM   10516 C  CA  . ALA D 2 47  ? 31.858  -71.705 -11.567 1.00 31.85  ? 47  ALA D CA  1 
ATOM   10517 C  C   . ALA D 2 47  ? 30.844  -72.069 -12.641 1.00 30.22  ? 47  ALA D C   1 
ATOM   10518 O  O   . ALA D 2 47  ? 30.033  -72.982 -12.397 1.00 33.41  ? 47  ALA D O   1 
ATOM   10519 C  CB  . ALA D 2 47  ? 31.175  -71.423 -10.216 1.00 30.31  ? 47  ALA D CB  1 
ATOM   10520 N  N   . GLY D 2 48  ? 30.883  -71.398 -13.818 1.00 29.62  ? 48  GLY D N   1 
ATOM   10521 C  CA  . GLY D 2 48  ? 29.944  -71.634 -14.918 1.00 30.35  ? 48  GLY D CA  1 
ATOM   10522 C  C   . GLY D 2 48  ? 28.563  -71.018 -14.766 1.00 30.27  ? 48  GLY D C   1 
ATOM   10523 O  O   . GLY D 2 48  ? 27.593  -71.486 -15.375 1.00 29.43  ? 48  GLY D O   1 
ATOM   10524 N  N   . MET D 2 49  ? 28.444  -69.955 -13.993 1.00 27.80  ? 49  MET D N   1 
ATOM   10525 C  CA  . MET D 2 49  ? 27.173  -69.413 -13.556 1.00 26.52  ? 49  MET D CA  1 
ATOM   10526 C  C   . MET D 2 49  ? 26.994  -68.051 -14.211 1.00 27.41  ? 49  MET D C   1 
ATOM   10527 O  O   . MET D 2 49  ? 27.981  -67.441 -14.620 1.00 27.91  ? 49  MET D O   1 
ATOM   10528 C  CB  . MET D 2 49  ? 27.236  -69.285 -12.035 1.00 26.98  ? 49  MET D CB  1 
ATOM   10529 C  CG  . MET D 2 49  ? 27.212  -70.632 -11.351 1.00 24.47  ? 49  MET D CG  1 
ATOM   10530 S  SD  . MET D 2 49  ? 26.910  -70.328 -9.623  1.00 33.83  ? 49  MET D SD  1 
ATOM   10531 C  CE  . MET D 2 49  ? 27.416  -71.898 -8.860  1.00 29.83  ? 49  MET D CE  1 
ATOM   10532 N  N   . LEU D 2 50  ? 25.730  -67.644 -14.417 1.00 25.24  ? 50  LEU D N   1 
ATOM   10533 C  CA  . LEU D 2 50  ? 25.407  -66.266 -14.819 1.00 24.57  ? 50  LEU D CA  1 
ATOM   10534 C  C   . LEU D 2 50  ? 25.079  -65.418 -13.590 1.00 24.69  ? 50  LEU D C   1 
ATOM   10535 O  O   . LEU D 2 50  ? 23.955  -65.531 -13.063 1.00 26.83  ? 50  LEU D O   1 
ATOM   10536 C  CB  . LEU D 2 50  ? 24.202  -66.256 -15.751 1.00 25.69  ? 50  LEU D CB  1 
ATOM   10537 C  CG  . LEU D 2 50  ? 23.759  -64.878 -16.256 1.00 27.89  ? 50  LEU D CG  1 
ATOM   10538 C  CD1 . LEU D 2 50  ? 24.744  -64.282 -17.274 1.00 28.69  ? 50  LEU D CD1 1 
ATOM   10539 C  CD2 . LEU D 2 50  ? 22.344  -65.018 -16.846 1.00 29.89  ? 50  LEU D CD2 1 
ATOM   10540 N  N   . PRO D 2 51  ? 25.939  -64.486 -13.181 1.00 25.56  ? 51  PRO D N   1 
ATOM   10541 C  CA  . PRO D 2 51  ? 25.544  -63.510 -12.137 1.00 25.61  ? 51  PRO D CA  1 
ATOM   10542 C  C   . PRO D 2 51  ? 24.530  -62.518 -12.702 1.00 29.15  ? 51  PRO D C   1 
ATOM   10543 O  O   . PRO D 2 51  ? 24.759  -61.907 -13.751 1.00 27.49  ? 51  PRO D O   1 
ATOM   10544 C  CB  . PRO D 2 51  ? 26.865  -62.811 -11.761 1.00 28.05  ? 51  PRO D CB  1 
ATOM   10545 C  CG  . PRO D 2 51  ? 27.943  -63.341 -12.689 1.00 27.77  ? 51  PRO D CG  1 
ATOM   10546 C  CD  . PRO D 2 51  ? 27.263  -64.199 -13.756 1.00 28.16  ? 51  PRO D CD  1 
ATOM   10547 N  N   . VAL D 2 52  ? 23.406  -62.331 -12.009 1.00 26.26  ? 52  VAL D N   1 
ATOM   10548 C  CA  . VAL D 2 52  ? 22.451  -61.287 -12.436 1.00 24.17  ? 52  VAL D CA  1 
ATOM   10549 C  C   . VAL D 2 52  ? 22.150  -60.412 -11.230 1.00 24.80  ? 52  VAL D C   1 
ATOM   10550 O  O   . VAL D 2 52  ? 21.613  -60.893 -10.224 1.00 23.71  ? 52  VAL D O   1 
ATOM   10551 C  CB  . VAL D 2 52  ? 21.150  -61.860 -13.024 1.00 25.73  ? 52  VAL D CB  1 
ATOM   10552 C  CG1 . VAL D 2 52  ? 21.455  -62.681 -14.300 1.00 25.71  ? 52  VAL D CG1 1 
ATOM   10553 C  CG2 . VAL D 2 52  ? 20.400  -62.794 -12.002 1.00 25.71  ? 52  VAL D CG2 1 
ATOM   10554 N  N   . ARG D 2 53  ? 22.507  -59.125 -11.319 1.00 25.66  ? 53  ARG D N   1 
ATOM   10555 C  CA  . ARG D 2 53  ? 22.297  -58.248 -10.182 1.00 24.77  ? 53  ARG D CA  1 
ATOM   10556 C  C   . ARG D 2 53  ? 20.812  -57.943 -9.991  1.00 27.02  ? 53  ARG D C   1 
ATOM   10557 O  O   . ARG D 2 53  ? 20.132  -57.485 -10.923 1.00 28.38  ? 53  ARG D O   1 
ATOM   10558 C  CB  . ARG D 2 53  ? 23.084  -56.953 -10.379 1.00 26.88  ? 53  ARG D CB  1 
ATOM   10559 C  CG  . ARG D 2 53  ? 22.865  -56.027 -9.206  1.00 32.25  ? 53  ARG D CG  1 
ATOM   10560 C  CD  . ARG D 2 53  ? 24.112  -55.224 -8.821  1.00 34.21  ? 53  ARG D CD  1 
ATOM   10561 N  NE  . ARG D 2 53  ? 23.690  -54.297 -7.788  1.00 38.32  ? 53  ARG D NE  1 
ATOM   10562 C  CZ  . ARG D 2 53  ? 23.560  -52.994 -7.879  1.00 34.32  ? 53  ARG D CZ  1 
ATOM   10563 N  NH1 . ARG D 2 53  ? 23.904  -52.319 -8.976  1.00 33.31  ? 53  ARG D NH1 1 
ATOM   10564 N  NH2 . ARG D 2 53  ? 23.127  -52.338 -6.813  1.00 36.67  ? 53  ARG D NH2 1 
ATOM   10565 N  N   . VAL D 2 54  ? 20.317  -58.149 -8.761  1.00 25.35  ? 54  VAL D N   1 
ATOM   10566 C  CA  . VAL D 2 54  ? 18.950  -57.780 -8.437  1.00 23.47  ? 54  VAL D CA  1 
ATOM   10567 C  C   . VAL D 2 54  ? 18.823  -56.264 -8.485  1.00 28.53  ? 54  VAL D C   1 
ATOM   10568 O  O   . VAL D 2 54  ? 19.656  -55.534 -7.919  1.00 26.27  ? 54  VAL D O   1 
ATOM   10569 C  CB  . VAL D 2 54  ? 18.576  -58.314 -7.046  1.00 28.78  ? 54  VAL D CB  1 
ATOM   10570 C  CG1 . VAL D 2 54  ? 17.148  -57.908 -6.655  1.00 30.17  ? 54  VAL D CG1 1 
ATOM   10571 C  CG2 . VAL D 2 54  ? 18.733  -59.865 -7.044  1.00 27.85  ? 54  VAL D CG2 1 
ATOM   10572 N  N   . LEU D 2 55  ? 17.771  -55.796 -9.140  1.00 29.86  ? 55  LEU D N   1 
ATOM   10573 C  CA  . LEU D 2 55  ? 17.417  -54.394 -9.181  1.00 30.98  ? 55  LEU D CA  1 
ATOM   10574 C  C   . LEU D 2 55  ? 15.916  -54.257 -8.981  1.00 34.31  ? 55  LEU D C   1 
ATOM   10575 O  O   . LEU D 2 55  ? 15.134  -55.212 -9.150  1.00 34.60  ? 55  LEU D O   1 
ATOM   10576 C  CB  . LEU D 2 55  ? 17.803  -53.721 -10.500 1.00 30.55  ? 55  LEU D CB  1 
ATOM   10577 C  CG  . LEU D 2 55  ? 19.286  -53.798 -10.852 1.00 35.23  ? 55  LEU D CG  1 
ATOM   10578 C  CD1 . LEU D 2 55  ? 19.480  -53.412 -12.294 1.00 33.17  ? 55  LEU D CD1 1 
ATOM   10579 C  CD2 . LEU D 2 55  ? 20.144  -52.924 -9.907  1.00 32.33  ? 55  LEU D CD2 1 
ATOM   10580 N  N   . GLY D 2 56  ? 15.524  -53.057 -8.634  1.00 36.78  ? 56  GLY D N   1 
ATOM   10581 C  CA  . GLY D 2 56  ? 14.110  -52.797 -8.458  1.00 38.99  ? 56  GLY D CA  1 
ATOM   10582 C  C   . GLY D 2 56  ? 13.400  -52.549 -9.758  1.00 35.28  ? 56  GLY D C   1 
ATOM   10583 O  O   . GLY D 2 56  ? 13.992  -52.433 -10.825 1.00 38.28  ? 56  GLY D O   1 
ATOM   10584 N  N   . ALA D 2 57  ? 12.083  -52.497 -9.668  1.00 35.88  ? 57  ALA D N   1 
ATOM   10585 C  CA  . ALA D 2 57  ? 11.269  -52.297 -10.852 1.00 33.11  ? 57  ALA D CA  1 
ATOM   10586 C  C   . ALA D 2 57  ? 10.695  -50.887 -10.940 1.00 36.31  ? 57  ALA D C   1 
ATOM   10587 O  O   . ALA D 2 57  ? 10.102  -50.535 -11.966 1.00 40.85  ? 57  ALA D O   1 
ATOM   10588 C  CB  . ALA D 2 57  ? 10.137  -53.341 -10.878 1.00 37.69  ? 57  ALA D CB  1 
ATOM   10589 N  N   . HIS D 2 58  ? 10.866  -50.077 -9.903  1.00 32.87  ? 58  HIS D N   1 
ATOM   10590 C  CA  . HIS D 2 58  ? 10.367  -48.705 -9.846  1.00 39.29  ? 58  HIS D CA  1 
ATOM   10591 C  C   . HIS D 2 58  ? 8.869   -48.644 -10.156 1.00 40.04  ? 58  HIS D C   1 
ATOM   10592 O  O   . HIS D 2 58  ? 8.405   -47.828 -10.951 1.00 44.08  ? 58  HIS D O   1 
ATOM   10593 C  CB  . HIS D 2 58  ? 11.178  -47.796 -10.769 1.00 38.53  ? 58  HIS D CB  1 
ATOM   10594 C  CG  . HIS D 2 58  ? 12.629  -47.749 -10.403 1.00 39.52  ? 58  HIS D CG  1 
ATOM   10595 N  ND1 . HIS D 2 58  ? 13.116  -46.979 -9.369  1.00 42.45  ? 58  HIS D ND1 1 
ATOM   10596 C  CD2 . HIS D 2 58  ? 13.693  -48.397 -10.924 1.00 40.57  ? 58  HIS D CD2 1 
ATOM   10597 C  CE1 . HIS D 2 58  ? 14.421  -47.154 -9.274  1.00 39.14  ? 58  HIS D CE1 1 
ATOM   10598 N  NE2 . HIS D 2 58  ? 14.797  -48.008 -10.206 1.00 41.68  ? 58  HIS D NE2 1 
ATOM   10599 N  N   . GLU D 2 59  ? 8.108   -49.504 -9.484  1.00 41.74  ? 59  GLU D N   1 
ATOM   10600 C  CA  . GLU D 2 59  ? 6.658   -49.577 -9.619  1.00 41.64  ? 59  GLU D CA  1 
ATOM   10601 C  C   . GLU D 2 59  ? 6.034   -49.854 -8.255  1.00 42.59  ? 59  GLU D C   1 
ATOM   10602 O  O   . GLU D 2 59  ? 6.724   -50.295 -7.328  1.00 39.82  ? 59  GLU D O   1 
ATOM   10603 C  CB  . GLU D 2 59  ? 6.291   -50.645 -10.662 1.00 45.41  ? 59  GLU D CB  1 
ATOM   10604 C  CG  . GLU D 2 59  ? 6.495   -52.078 -10.217 1.00 46.85  ? 59  GLU D CG  1 
ATOM   10605 C  CD  . GLU D 2 59  ? 6.400   -53.051 -11.400 1.00 53.10  ? 59  GLU D CD  1 
ATOM   10606 O  OE1 . GLU D 2 59  ? 6.285   -52.567 -12.548 1.00 52.17  ? 59  GLU D OE1 1 
ATOM   10607 O  OE2 . GLU D 2 59  ? 6.491   -54.286 -11.188 1.00 54.59  ? 59  GLU D OE2 1 
ATOM   10608 N  N   . PRO D 2 60  ? 4.743   -49.557 -8.082  1.00 41.00  ? 60  PRO D N   1 
ATOM   10609 C  CA  . PRO D 2 60  ? 4.103   -49.813 -6.773  1.00 41.70  ? 60  PRO D CA  1 
ATOM   10610 C  C   . PRO D 2 60  ? 4.181   -51.285 -6.349  1.00 46.01  ? 60  PRO D C   1 
ATOM   10611 O  O   . PRO D 2 60  ? 4.043   -52.195 -7.169  1.00 42.97  ? 60  PRO D O   1 
ATOM   10612 C  CB  . PRO D 2 60  ? 2.655   -49.362 -7.001  1.00 44.28  ? 60  PRO D CB  1 
ATOM   10613 C  CG  . PRO D 2 60  ? 2.768   -48.348 -8.133  1.00 44.38  ? 60  PRO D CG  1 
ATOM   10614 C  CD  . PRO D 2 60  ? 3.850   -48.862 -9.022  1.00 44.44  ? 60  PRO D CD  1 
ATOM   10615 N  N   . GLN D 2 61  ? 4.435   -51.520 -5.056  1.00 44.06  ? 61  GLN D N   1 
ATOM   10616 C  CA  . GLN D 2 61  ? 4.504   -52.886 -4.535  1.00 46.52  ? 61  GLN D CA  1 
ATOM   10617 C  C   . GLN D 2 61  ? 4.132   -52.900 -3.056  1.00 47.66  ? 61  GLN D C   1 
ATOM   10618 O  O   . GLN D 2 61  ? 4.445   -51.970 -2.312  1.00 45.42  ? 61  GLN D O   1 
ATOM   10619 C  CB  . GLN D 2 61  ? 5.903   -53.514 -4.738  1.00 42.04  ? 61  GLN D CB  1 
ATOM   10620 C  CG  . GLN D 2 61  ? 7.047   -52.851 -3.976  1.00 39.40  ? 61  GLN D CG  1 
ATOM   10621 C  CD  . GLN D 2 61  ? 7.171   -53.367 -2.547  1.00 42.68  ? 61  GLN D CD  1 
ATOM   10622 O  OE1 . GLN D 2 61  ? 6.567   -54.387 -2.182  1.00 40.87  ? 61  GLN D OE1 1 
ATOM   10623 N  NE2 . GLN D 2 61  ? 7.964   -52.683 -1.741  1.00 38.74  ? 61  GLN D NE2 1 
ATOM   10624 N  N   A ASN D 2 62  ? 3.481   -53.988 -2.641  0.52 47.94  ? 62  ASN D N   1 
ATOM   10625 N  N   B ASN D 2 62  ? 3.481   -53.978 -2.628  0.48 47.94  ? 62  ASN D N   1 
ATOM   10626 C  CA  A ASN D 2 62  ? 3.029   -54.142 -1.268  0.52 50.56  ? 62  ASN D CA  1 
ATOM   10627 C  CA  B ASN D 2 62  ? 3.074   -54.123 -1.237  0.48 50.55  ? 62  ASN D CA  1 
ATOM   10628 C  C   A ASN D 2 62  ? 3.594   -55.377 -0.576  0.52 49.36  ? 62  ASN D C   1 
ATOM   10629 C  C   B ASN D 2 62  ? 3.609   -55.381 -0.563  0.48 49.34  ? 62  ASN D C   1 
ATOM   10630 O  O   A ASN D 2 62  ? 3.564   -55.439 0.664   0.52 49.27  ? 62  ASN D O   1 
ATOM   10631 O  O   B ASN D 2 62  ? 3.553   -55.474 0.674   0.48 49.21  ? 62  ASN D O   1 
ATOM   10632 C  CB  A ASN D 2 62  ? 1.493   -54.205 -1.230  0.52 53.83  ? 62  ASN D CB  1 
ATOM   10633 C  CB  B ASN D 2 62  ? 1.540   -54.112 -1.140  0.48 53.83  ? 62  ASN D CB  1 
ATOM   10634 C  CG  A ASN D 2 62  ? 0.860   -52.832 -1.130  0.52 54.61  ? 62  ASN D CG  1 
ATOM   10635 C  CG  B ASN D 2 62  ? 0.909   -55.188 -1.993  0.48 52.62  ? 62  ASN D CG  1 
ATOM   10636 O  OD1 A ASN D 2 62  ? 0.930   -52.167 -0.090  0.52 56.01  ? 62  ASN D OD1 1 
ATOM   10637 O  OD1 B ASN D 2 62  ? 1.609   -55.984 -2.613  0.48 52.81  ? 62  ASN D OD1 1 
ATOM   10638 N  ND2 A ASN D 2 62  ? 0.247   -52.391 -2.224  0.52 54.29  ? 62  ASN D ND2 1 
ATOM   10639 N  ND2 B ASN D 2 62  ? -0.413  -55.224 -2.025  0.48 53.24  ? 62  ASN D ND2 1 
ATOM   10640 N  N   . VAL D 2 63  ? 4.135   -56.338 -1.331  1.00 44.62  ? 63  VAL D N   1 
ATOM   10641 C  CA  . VAL D 2 63  ? 4.509   -57.631 -0.792  1.00 41.46  ? 63  VAL D CA  1 
ATOM   10642 C  C   . VAL D 2 63  ? 5.606   -57.572 0.260   1.00 38.42  ? 63  VAL D C   1 
ATOM   10643 O  O   . VAL D 2 63  ? 5.796   -58.561 0.952   1.00 36.09  ? 63  VAL D O   1 
ATOM   10644 C  CB  . VAL D 2 63  ? 4.968   -58.601 -1.903  1.00 39.25  ? 63  VAL D CB  1 
ATOM   10645 C  CG1 . VAL D 2 63  ? 3.773   -59.141 -2.687  1.00 47.66  ? 63  VAL D CG1 1 
ATOM   10646 C  CG2 . VAL D 2 63  ? 5.957   -57.919 -2.808  1.00 40.19  ? 63  VAL D CG2 1 
ATOM   10647 N  N   . THR D 2 64  ? 6.344   -56.464 0.405   1.00 33.62  ? 64  THR D N   1 
ATOM   10648 C  CA  . THR D 2 64  ? 7.457   -56.514 1.355   1.00 36.74  ? 64  THR D CA  1 
ATOM   10649 C  C   . THR D 2 64  ? 7.103   -56.029 2.764   1.00 32.28  ? 64  THR D C   1 
ATOM   10650 O  O   . THR D 2 64  ? 7.961   -56.110 3.656   1.00 32.36  ? 64  THR D O   1 
ATOM   10651 C  CB  . THR D 2 64  ? 8.660   -55.702 0.859   1.00 35.67  ? 64  THR D CB  1 
ATOM   10652 O  OG1 . THR D 2 64  ? 8.284   -54.324 0.780   1.00 38.23  ? 64  THR D OG1 1 
ATOM   10653 C  CG2 . THR D 2 64  ? 9.116   -56.207 -0.503  1.00 32.88  ? 64  THR D CG2 1 
ATOM   10654 N  N   . GLU D 2 65  ? 5.903   -55.498 2.987   1.00 39.77  ? 65  GLU D N   1 
ATOM   10655 C  CA  . GLU D 2 65  ? 5.574   -54.978 4.317   1.00 38.44  ? 65  GLU D CA  1 
ATOM   10656 C  C   . GLU D 2 65  ? 5.678   -56.008 5.443   1.00 36.04  ? 65  GLU D C   1 
ATOM   10657 O  O   . GLU D 2 65  ? 6.125   -55.624 6.539   1.00 36.26  ? 65  GLU D O   1 
ATOM   10658 C  CB  . GLU D 2 65  ? 4.191   -54.309 4.274   1.00 42.69  ? 65  GLU D CB  1 
ATOM   10659 C  CG  . GLU D 2 65  ? 4.158   -53.154 3.245   1.00 49.24  ? 65  GLU D CG  1 
ATOM   10660 C  CD  . GLU D 2 65  ? 4.513   -51.745 3.806   1.00 61.97  ? 65  GLU D CD  1 
ATOM   10661 O  OE1 . GLU D 2 65  ? 5.694   -51.437 4.160   1.00 57.29  ? 65  GLU D OE1 1 
ATOM   10662 O  OE2 . GLU D 2 65  ? 3.584   -50.908 3.842   1.00 67.99  ? 65  GLU D OE2 1 
ATOM   10663 N  N   . PRO D 2 66  ? 5.379   -57.297 5.257   1.00 35.91  ? 66  PRO D N   1 
ATOM   10664 C  CA  . PRO D 2 66  ? 5.613   -58.237 6.358   1.00 35.98  ? 66  PRO D CA  1 
ATOM   10665 C  C   . PRO D 2 66  ? 7.080   -58.585 6.557   1.00 32.15  ? 66  PRO D C   1 
ATOM   10666 O  O   . PRO D 2 66  ? 7.410   -59.262 7.553   1.00 33.28  ? 66  PRO D O   1 
ATOM   10667 C  CB  . PRO D 2 66  ? 4.796   -59.483 5.945   1.00 37.08  ? 66  PRO D CB  1 
ATOM   10668 C  CG  . PRO D 2 66  ? 3.935   -59.047 4.809   1.00 39.60  ? 66  PRO D CG  1 
ATOM   10669 C  CD  . PRO D 2 66  ? 4.704   -57.955 4.123   1.00 36.56  ? 66  PRO D CD  1 
ATOM   10670 N  N   . HIS D 2 67  ? 7.978   -58.136 5.672   1.00 31.77  ? 67  HIS D N   1 
ATOM   10671 C  CA  . HIS D 2 67  ? 9.373   -58.560 5.707   1.00 30.61  ? 67  HIS D CA  1 
ATOM   10672 C  C   . HIS D 2 67  ? 10.360  -57.482 6.079   1.00 33.17  ? 67  HIS D C   1 
ATOM   10673 O  O   . HIS D 2 67  ? 11.369  -57.803 6.713   1.00 31.24  ? 67  HIS D O   1 
ATOM   10674 C  CB  . HIS D 2 67  ? 9.805   -59.143 4.353   1.00 29.05  ? 67  HIS D CB  1 
ATOM   10675 C  CG  . HIS D 2 67  ? 8.991   -60.322 3.958   1.00 32.82  ? 67  HIS D CG  1 
ATOM   10676 N  ND1 . HIS D 2 67  ? 9.186   -61.569 4.512   1.00 32.46  ? 67  HIS D ND1 1 
ATOM   10677 C  CD2 . HIS D 2 67  ? 7.893   -60.423 3.172   1.00 34.69  ? 67  HIS D CD2 1 
ATOM   10678 C  CE1 . HIS D 2 67  ? 8.278   -62.402 4.032   1.00 31.59  ? 67  HIS D CE1 1 
ATOM   10679 N  NE2 . HIS D 2 67  ? 7.480   -61.732 3.222   1.00 33.49  ? 67  HIS D NE2 1 
ATOM   10680 N  N   . ILE D 2 68  ? 10.159  -56.237 5.631   1.00 31.97  ? 68  ILE D N   1 
ATOM   10681 C  CA  . ILE D 2 68  ? 11.097  -55.131 5.846   1.00 31.91  ? 68  ILE D CA  1 
ATOM   10682 C  C   . ILE D 2 68  ? 10.286  -53.928 6.304   1.00 31.74  ? 68  ILE D C   1 
ATOM   10683 O  O   . ILE D 2 68  ? 9.326   -53.524 5.633   1.00 33.34  ? 68  ILE D O   1 
ATOM   10684 C  CB  . ILE D 2 68  ? 11.929  -54.770 4.583   1.00 32.13  ? 68  ILE D CB  1 
ATOM   10685 C  CG1 . ILE D 2 68  ? 12.778  -55.948 4.102   1.00 28.83  ? 68  ILE D CG1 1 
ATOM   10686 C  CG2 . ILE D 2 68  ? 12.849  -53.560 4.853   1.00 30.38  ? 68  ILE D CG2 1 
ATOM   10687 C  CD1 . ILE D 2 68  ? 13.549  -55.645 2.837   1.00 29.48  ? 68  ILE D CD1 1 
ATOM   10688 N  N   . PHE D 2 69  ? 10.654  -53.388 7.458   1.00 30.38  ? 69  PHE D N   1 
ATOM   10689 C  CA  . PHE D 2 69  ? 9.984   -52.236 8.029   1.00 29.64  ? 69  PHE D CA  1 
ATOM   10690 C  C   . PHE D 2 69  ? 10.178  -50.996 7.158   1.00 31.17  ? 69  PHE D C   1 
ATOM   10691 O  O   . PHE D 2 69  ? 11.233  -50.795 6.541   1.00 30.84  ? 69  PHE D O   1 
ATOM   10692 C  CB  . PHE D 2 69  ? 10.516  -52.018 9.439   1.00 33.51  ? 69  PHE D CB  1 
ATOM   10693 C  CG  . PHE D 2 69  ? 9.914   -50.839 10.168  1.00 30.78  ? 69  PHE D CG  1 
ATOM   10694 C  CD1 . PHE D 2 69  ? 8.568   -50.495 10.027  1.00 31.91  ? 69  PHE D CD1 1 
ATOM   10695 C  CD2 . PHE D 2 69  ? 10.721  -50.093 11.036  1.00 32.09  ? 69  PHE D CD2 1 
ATOM   10696 C  CE1 . PHE D 2 69  ? 8.037   -49.415 10.754  1.00 34.93  ? 69  PHE D CE1 1 
ATOM   10697 C  CE2 . PHE D 2 69  ? 10.217  -49.042 11.768  1.00 27.98  ? 69  PHE D CE2 1 
ATOM   10698 C  CZ  . PHE D 2 69  ? 8.861   -48.685 11.610  1.00 33.21  ? 69  PHE D CZ  1 
ATOM   10699 N  N   . GLY D 2 70  ? 9.124   -50.193 7.072   1.00 30.79  ? 70  GLY D N   1 
ATOM   10700 C  CA  . GLY D 2 70  ? 9.091   -49.088 6.115   1.00 32.30  ? 70  GLY D CA  1 
ATOM   10701 C  C   . GLY D 2 70  ? 10.075  -47.971 6.402   1.00 35.30  ? 70  GLY D C   1 
ATOM   10702 O  O   . GLY D 2 70  ? 10.108  -46.979 5.660   1.00 37.41  ? 70  GLY D O   1 
ATOM   10703 N  N   . MET D 2 71  ? 10.912  -48.118 7.432   1.00 31.69  ? 71  MET D N   1 
ATOM   10704 C  CA  . MET D 2 71  ? 11.927  -47.102 7.693   1.00 29.92  ? 71  MET D CA  1 
ATOM   10705 C  C   . MET D 2 71  ? 13.171  -47.298 6.845   1.00 31.75  ? 71  MET D C   1 
ATOM   10706 O  O   . MET D 2 71  ? 14.061  -46.449 6.904   1.00 28.42  ? 71  MET D O   1 
ATOM   10707 C  CB  . MET D 2 71  ? 12.361  -47.117 9.175   1.00 31.92  ? 71  MET D CB  1 
ATOM   10708 C  CG  . MET D 2 71  ? 13.285  -48.327 9.496   1.00 30.65  ? 71  MET D CG  1 
ATOM   10709 S  SD  . MET D 2 71  ? 13.725  -48.412 11.248  1.00 29.16  ? 71  MET D SD  1 
ATOM   10710 C  CE  . MET D 2 71  ? 15.242  -47.424 11.213  1.00 22.92  ? 71  MET D CE  1 
ATOM   10711 N  N   . PHE D 2 72  ? 13.261  -48.388 6.078   1.00 28.98  ? 72  PHE D N   1 
ATOM   10712 C  CA  . PHE D 2 72  ? 14.419  -48.720 5.260   1.00 27.06  ? 72  PHE D CA  1 
ATOM   10713 C  C   . PHE D 2 72  ? 14.182  -48.296 3.816   1.00 26.91  ? 72  PHE D C   1 
ATOM   10714 O  O   . PHE D 2 72  ? 13.056  -47.978 3.407   1.00 27.57  ? 72  PHE D O   1 
ATOM   10715 C  CB  . PHE D 2 72  ? 14.718  -50.212 5.394   1.00 27.25  ? 72  PHE D CB  1 
ATOM   10716 C  CG  . PHE D 2 72  ? 15.110  -50.561 6.806   1.00 28.30  ? 72  PHE D CG  1 
ATOM   10717 C  CD1 . PHE D 2 72  ? 16.293  -50.018 7.351   1.00 30.53  ? 72  PHE D CD1 1 
ATOM   10718 C  CD2 . PHE D 2 72  ? 14.285  -51.319 7.620   1.00 24.57  ? 72  PHE D CD2 1 
ATOM   10719 C  CE1 . PHE D 2 72  ? 16.664  -50.282 8.657   1.00 26.45  ? 72  PHE D CE1 1 
ATOM   10720 C  CE2 . PHE D 2 72  ? 14.654  -51.576 8.934   1.00 32.49  ? 72  PHE D CE2 1 
ATOM   10721 C  CZ  . PHE D 2 72  ? 15.860  -51.076 9.435   1.00 27.84  ? 72  PHE D CZ  1 
ATOM   10722 N  N   . CYS D 2 73  ? 15.254  -48.244 3.060   1.00 25.60  ? 73  CYS D N   1 
ATOM   10723 C  CA  . CYS D 2 73  ? 15.193  -47.488 1.823   1.00 27.70  ? 73  CYS D CA  1 
ATOM   10724 C  C   . CYS D 2 73  ? 14.279  -48.150 0.789   1.00 28.79  ? 73  CYS D C   1 
ATOM   10725 O  O   . CYS D 2 73  ? 14.025  -49.359 0.832   1.00 26.40  ? 73  CYS D O   1 
ATOM   10726 C  CB  . CYS D 2 73  ? 16.610  -47.323 1.275   1.00 22.11  ? 73  CYS D CB  1 
ATOM   10727 S  SG  . CYS D 2 73  ? 17.294  -48.948 0.682   1.00 25.52  ? 73  CYS D SG  1 
ATOM   10728 N  N   . PRO D 2 74  ? 13.742  -47.368 -0.143  1.00 26.78  ? 74  PRO D N   1 
ATOM   10729 C  CA  . PRO D 2 74  ? 12.913  -47.963 -1.212  1.00 29.38  ? 74  PRO D CA  1 
ATOM   10730 C  C   . PRO D 2 74  ? 13.638  -49.023 -2.009  1.00 28.00  ? 74  PRO D C   1 
ATOM   10731 O  O   . PRO D 2 74  ? 12.991  -49.949 -2.511  1.00 31.27  ? 74  PRO D O   1 
ATOM   10732 C  CB  . PRO D 2 74  ? 12.542  -46.752 -2.095  1.00 34.16  ? 74  PRO D CB  1 
ATOM   10733 C  CG  . PRO D 2 74  ? 12.640  -45.583 -1.173  1.00 33.65  ? 74  PRO D CG  1 
ATOM   10734 C  CD  . PRO D 2 74  ? 13.766  -45.889 -0.203  1.00 30.34  ? 74  PRO D CD  1 
ATOM   10735 N  N   . PHE D 2 75  ? 14.960  -48.892 -2.189  1.00 26.74  ? 75  PHE D N   1 
ATOM   10736 C  CA  . PHE D 2 75  ? 15.682  -49.808 -3.071  1.00 30.86  ? 75  PHE D CA  1 
ATOM   10737 C  C   . PHE D 2 75  ? 15.751  -51.204 -2.463  1.00 26.96  ? 75  PHE D C   1 
ATOM   10738 O  O   . PHE D 2 75  ? 15.591  -52.214 -3.173  1.00 29.45  ? 75  PHE D O   1 
ATOM   10739 C  CB  . PHE D 2 75  ? 17.088  -49.271 -3.337  1.00 29.09  ? 75  PHE D CB  1 
ATOM   10740 C  CG  . PHE D 2 75  ? 17.942  -50.171 -4.194  1.00 26.19  ? 75  PHE D CG  1 
ATOM   10741 C  CD1 . PHE D 2 75  ? 17.492  -50.562 -5.464  1.00 30.74  ? 75  PHE D CD1 1 
ATOM   10742 C  CD2 . PHE D 2 75  ? 19.175  -50.643 -3.752  1.00 32.43  ? 75  PHE D CD2 1 
ATOM   10743 C  CE1 . PHE D 2 75  ? 18.274  -51.388 -6.283  1.00 33.46  ? 75  PHE D CE1 1 
ATOM   10744 C  CE2 . PHE D 2 75  ? 19.969  -51.494 -4.570  1.00 33.56  ? 75  PHE D CE2 1 
ATOM   10745 C  CZ  . PHE D 2 75  ? 19.518  -51.845 -5.835  1.00 33.75  ? 75  PHE D CZ  1 
ATOM   10746 N  N   . CYS D 2 76  ? 16.026  -51.294 -1.155  1.00 25.22  ? 76  CYS D N   1 
ATOM   10747 C  CA  . CYS D 2 76  ? 16.093  -52.637 -0.568  1.00 25.78  ? 76  CYS D CA  1 
ATOM   10748 C  C   . CYS D 2 76  ? 14.736  -53.309 -0.599  1.00 28.54  ? 76  CYS D C   1 
ATOM   10749 O  O   . CYS D 2 76  ? 14.645  -54.554 -0.770  1.00 28.94  ? 76  CYS D O   1 
ATOM   10750 C  CB  . CYS D 2 76  ? 16.690  -52.571 0.843   1.00 27.85  ? 76  CYS D CB  1 
ATOM   10751 S  SG  . CYS D 2 76  ? 15.671  -52.112 2.251   1.00 27.01  ? 76  CYS D SG  1 
ATOM   10752 N  N   . ARG D 2 77  ? 13.678  -52.510 -0.513  1.00 26.77  ? 77  ARG D N   1 
ATOM   10753 C  CA  . ARG D 2 77  ? 12.325  -53.044 -0.523  1.00 27.45  ? 77  ARG D CA  1 
ATOM   10754 C  C   . ARG D 2 77  ? 11.916  -53.415 -1.944  1.00 30.30  ? 77  ARG D C   1 
ATOM   10755 O  O   . ARG D 2 77  ? 11.455  -54.542 -2.178  1.00 28.30  ? 77  ARG D O   1 
ATOM   10756 C  CB  . ARG D 2 77  ? 11.382  -52.032 0.106   1.00 32.60  ? 77  ARG D CB  1 
ATOM   10757 C  CG  . ARG D 2 77  ? 11.574  -51.991 1.635   1.00 33.92  ? 77  ARG D CG  1 
ATOM   10758 C  CD  . ARG D 2 77  ? 10.595  -51.013 2.299   1.00 32.99  ? 77  ARG D CD  1 
ATOM   10759 N  NE  . ARG D 2 77  ? 11.081  -49.647 2.192   1.00 35.37  ? 77  ARG D NE  1 
ATOM   10760 C  CZ  . ARG D 2 77  ? 10.387  -48.648 1.665   1.00 38.14  ? 77  ARG D CZ  1 
ATOM   10761 N  NH1 . ARG D 2 77  ? 9.176   -48.843 1.165   1.00 40.98  ? 77  ARG D NH1 1 
ATOM   10762 N  NH2 . ARG D 2 77  ? 10.904  -47.415 1.683   1.00 35.47  ? 77  ARG D NH2 1 
ATOM   10763 N  N   . ASP D 2 78  ? 12.099  -52.485 -2.905  1.00 24.52  ? 78  ASP D N   1 
ATOM   10764 C  CA  . ASP D 2 78  ? 11.818  -52.759 -4.320  1.00 29.79  ? 78  ASP D CA  1 
ATOM   10765 C  C   . ASP D 2 78  ? 12.552  -54.021 -4.781  1.00 28.90  ? 78  ASP D C   1 
ATOM   10766 O  O   . ASP D 2 78  ? 11.981  -54.869 -5.495  1.00 28.33  ? 78  ASP D O   1 
ATOM   10767 C  CB  . ASP D 2 78  ? 12.233  -51.546 -5.162  1.00 28.86  ? 78  ASP D CB  1 
ATOM   10768 C  CG  . ASP D 2 78  ? 11.697  -51.580 -6.585  1.00 34.19  ? 78  ASP D CG  1 
ATOM   10769 O  OD1 . ASP D 2 78  ? 11.004  -52.554 -6.997  1.00 34.74  ? 78  ASP D OD1 1 
ATOM   10770 O  OD2 . ASP D 2 78  ? 12.024  -50.628 -7.324  1.00 34.70  ? 78  ASP D OD2 1 
ATOM   10771 N  N   . SER D 2 79  ? 13.810  -54.193 -4.340  1.00 24.56  ? 79  SER D N   1 
ATOM   10772 C  CA  . SER D 2 79  ? 14.607  -55.341 -4.754  1.00 24.84  ? 79  SER D CA  1 
ATOM   10773 C  C   . SER D 2 79  ? 14.009  -56.626 -4.192  1.00 27.17  ? 79  SER D C   1 
ATOM   10774 O  O   . SER D 2 79  ? 13.873  -57.631 -4.908  1.00 27.14  ? 79  SER D O   1 
ATOM   10775 C  CB  . SER D 2 79  ? 16.055  -55.190 -4.285  1.00 29.27  ? 79  SER D CB  1 
ATOM   10776 O  OG  . SER D 2 79  ? 16.751  -54.136 -4.956  1.00 28.65  ? 79  SER D OG  1 
ATOM   10777 N  N   . LEU D 2 80  ? 13.712  -56.639 -2.890  1.00 27.04  ? 80  LEU D N   1 
ATOM   10778 C  CA  . LEU D 2 80  ? 13.120  -57.844 -2.320  1.00 25.01  ? 80  LEU D CA  1 
ATOM   10779 C  C   . LEU D 2 80  ? 11.793  -58.167 -3.002  1.00 26.58  ? 80  LEU D C   1 
ATOM   10780 O  O   . LEU D 2 80  ? 11.467  -59.348 -3.225  1.00 28.91  ? 80  LEU D O   1 
ATOM   10781 C  CB  . LEU D 2 80  ? 12.924  -57.668 -0.810  1.00 28.34  ? 80  LEU D CB  1 
ATOM   10782 C  CG  . LEU D 2 80  ? 12.135  -58.793 -0.144  1.00 25.84  ? 80  LEU D CG  1 
ATOM   10783 C  CD1 . LEU D 2 80  ? 12.935  -60.112 -0.275  1.00 26.56  ? 80  LEU D CD1 1 
ATOM   10784 C  CD2 . LEU D 2 80  ? 11.814  -58.456 1.341   1.00 26.19  ? 80  LEU D CD2 1 
ATOM   10785 N  N   . ALA D 2 81  ? 10.995  -57.142 -3.328  1.00 28.73  ? 81  ALA D N   1 
ATOM   10786 C  CA  . ALA D 2 81  ? 9.710   -57.433 -3.971  1.00 30.60  ? 81  ALA D CA  1 
ATOM   10787 C  C   . ALA D 2 81  ? 9.911   -58.234 -5.257  1.00 30.57  ? 81  ALA D C   1 
ATOM   10788 O  O   . ALA D 2 81  ? 9.062   -59.067 -5.611  1.00 33.30  ? 81  ALA D O   1 
ATOM   10789 C  CB  . ALA D 2 81  ? 8.919   -56.144 -4.253  1.00 27.50  ? 81  ALA D CB  1 
ATOM   10790 N  N   . GLN D 2 82  ? 11.020  -58.007 -5.966  1.00 29.32  ? 82  GLN D N   1 
ATOM   10791 C  CA  . GLN D 2 82  ? 11.204  -58.719 -7.237  1.00 28.76  ? 82  GLN D CA  1 
ATOM   10792 C  C   . GLN D 2 82  ? 11.352  -60.213 -6.999  1.00 29.80  ? 82  GLN D C   1 
ATOM   10793 O  O   . GLN D 2 82  ? 10.873  -61.028 -7.799  1.00 32.30  ? 82  GLN D O   1 
ATOM   10794 C  CB  . GLN D 2 82  ? 12.417  -58.202 -7.997  1.00 29.78  ? 82  GLN D CB  1 
ATOM   10795 C  CG  . GLN D 2 82  ? 12.369  -56.696 -8.271  1.00 32.04  ? 82  GLN D CG  1 
ATOM   10796 C  CD  . GLN D 2 82  ? 11.039  -56.300 -8.805  1.00 32.24  ? 82  GLN D CD  1 
ATOM   10797 O  OE1 . GLN D 2 82  ? 10.660  -56.732 -9.888  1.00 34.32  ? 82  GLN D OE1 1 
ATOM   10798 N  NE2 . GLN D 2 82  ? 10.325  -55.450 -8.084  1.00 35.58  ? 82  GLN D NE2 1 
ATOM   10799 N  N   . GLY D 2 83  ? 12.052  -60.581 -5.921  1.00 28.45  ? 83  GLY D N   1 
ATOM   10800 C  CA  . GLY D 2 83  ? 12.163  -61.980 -5.541  1.00 28.42  ? 83  GLY D CA  1 
ATOM   10801 C  C   . GLY D 2 83  ? 10.836  -62.568 -5.090  1.00 29.07  ? 83  GLY D C   1 
ATOM   10802 O  O   . GLY D 2 83  ? 10.441  -63.647 -5.551  1.00 29.52  ? 83  GLY D O   1 
ATOM   10803 N  N   . LEU D 2 84  ? 10.138  -61.872 -4.173  1.00 29.59  ? 84  LEU D N   1 
ATOM   10804 C  CA  . LEU D 2 84  ? 8.868   -62.365 -3.637  1.00 29.19  ? 84  LEU D CA  1 
ATOM   10805 C  C   . LEU D 2 84  ? 7.818   -62.494 -4.724  1.00 32.67  ? 84  LEU D C   1 
ATOM   10806 O  O   . LEU D 2 84  ? 6.954   -63.375 -4.645  1.00 34.13  ? 84  LEU D O   1 
ATOM   10807 C  CB  . LEU D 2 84  ? 8.361   -61.416 -2.552  1.00 32.82  ? 84  LEU D CB  1 
ATOM   10808 C  CG  . LEU D 2 84  ? 9.272   -61.266 -1.349  1.00 32.38  ? 84  LEU D CG  1 
ATOM   10809 C  CD1 . LEU D 2 84  ? 8.691   -60.206 -0.457  1.00 26.82  ? 84  LEU D CD1 1 
ATOM   10810 C  CD2 . LEU D 2 84  ? 9.237   -62.582 -0.617  1.00 31.20  ? 84  LEU D CD2 1 
ATOM   10811 N  N   . LEU D 2 85  ? 7.904   -61.657 -5.774  1.00 32.09  ? 85  LEU D N   1 
ATOM   10812 C  CA  . LEU D 2 85  ? 6.969   -61.694 -6.890  1.00 32.76  ? 85  LEU D CA  1 
ATOM   10813 C  C   . LEU D 2 85  ? 7.274   -62.800 -7.896  1.00 34.69  ? 85  LEU D C   1 
ATOM   10814 O  O   . LEU D 2 85  ? 6.493   -62.987 -8.837  1.00 32.33  ? 85  LEU D O   1 
ATOM   10815 C  CB  . LEU D 2 85  ? 6.971   -60.342 -7.595  1.00 30.72  ? 85  LEU D CB  1 
ATOM   10816 C  CG  . LEU D 2 85  ? 6.253   -59.292 -6.759  1.00 30.78  ? 85  LEU D CG  1 
ATOM   10817 C  CD1 . LEU D 2 85  ? 6.512   -57.873 -7.331  1.00 38.14  ? 85  LEU D CD1 1 
ATOM   10818 C  CD2 . LEU D 2 85  ? 4.747   -59.539 -6.696  1.00 35.40  ? 85  LEU D CD2 1 
ATOM   10819 N  N   . GLY D 2 86  ? 8.382   -63.516 -7.732  1.00 30.26  ? 86  GLY D N   1 
ATOM   10820 C  CA  . GLY D 2 86  ? 8.702   -64.639 -8.597  1.00 31.27  ? 86  GLY D CA  1 
ATOM   10821 C  C   . GLY D 2 86  ? 9.469   -64.232 -9.836  1.00 33.44  ? 86  GLY D C   1 
ATOM   10822 O  O   . GLY D 2 86  ? 9.650   -65.056 -10.746 1.00 35.42  ? 86  GLY D O   1 
ATOM   10823 N  N   . ARG D 2 87  ? 9.932   -62.985 -9.904  1.00 31.56  ? 87  ARG D N   1 
ATOM   10824 C  CA  . ARG D 2 87  ? 10.559  -62.525 -11.137 1.00 35.38  ? 87  ARG D CA  1 
ATOM   10825 C  C   . ARG D 2 87  ? 11.974  -63.037 -11.310 1.00 31.44  ? 87  ARG D C   1 
ATOM   10826 O  O   . ARG D 2 87  ? 12.510  -62.966 -12.425 1.00 32.37  ? 87  ARG D O   1 
ATOM   10827 C  CB  . ARG D 2 87  ? 10.518  -61.010 -11.217 1.00 31.17  ? 87  ARG D CB  1 
ATOM   10828 C  CG  . ARG D 2 87  ? 9.087   -60.548 -11.320 1.00 37.55  ? 87  ARG D CG  1 
ATOM   10829 C  CD  . ARG D 2 87  ? 8.987   -59.066 -11.426 1.00 36.81  ? 87  ARG D CD  1 
ATOM   10830 N  NE  . ARG D 2 87  ? 7.585   -58.666 -11.501 1.00 39.11  ? 87  ARG D NE  1 
ATOM   10831 C  CZ  . ARG D 2 87  ? 7.161   -57.435 -11.270 1.00 40.03  ? 87  ARG D CZ  1 
ATOM   10832 N  NH1 . ARG D 2 87  ? 8.010   -56.453 -10.986 1.00 37.98  ? 87  ARG D NH1 1 
ATOM   10833 N  NH2 . ARG D 2 87  ? 5.868   -57.165 -11.407 1.00 47.36  ? 87  ARG D NH2 1 
ATOM   10834 N  N   . PHE D 2 88  ? 12.576  -63.569 -10.257 1.00 31.85  ? 88  PHE D N   1 
ATOM   10835 C  CA  . PHE D 2 88  ? 13.877  -64.202 -10.370 1.00 31.61  ? 88  PHE D CA  1 
ATOM   10836 C  C   . PHE D 2 88  ? 13.772  -65.700 -10.154 1.00 30.23  ? 88  PHE D C   1 
ATOM   10837 O  O   . PHE D 2 88  ? 14.715  -66.305 -9.641  1.00 30.53  ? 88  PHE D O   1 
ATOM   10838 C  CB  . PHE D 2 88  ? 14.871  -63.586 -9.400  1.00 30.04  ? 88  PHE D CB  1 
ATOM   10839 C  CG  . PHE D 2 88  ? 15.370  -62.258 -9.852  1.00 27.86  ? 88  PHE D CG  1 
ATOM   10840 C  CD1 . PHE D 2 88  ? 14.655  -61.098 -9.590  1.00 30.48  ? 88  PHE D CD1 1 
ATOM   10841 C  CD2 . PHE D 2 88  ? 16.574  -62.161 -10.560 1.00 29.72  ? 88  PHE D CD2 1 
ATOM   10842 C  CE1 . PHE D 2 88  ? 15.124  -59.843 -10.045 1.00 29.21  ? 88  PHE D CE1 1 
ATOM   10843 C  CE2 . PHE D 2 88  ? 17.059  -60.897 -11.010 1.00 30.85  ? 88  PHE D CE2 1 
ATOM   10844 C  CZ  . PHE D 2 88  ? 16.337  -59.754 -10.740 1.00 31.32  ? 88  PHE D CZ  1 
ATOM   10845 N  N   . ASP D 2 89  ? 12.620  -66.286 -10.526 1.00 31.17  ? 89  ASP D N   1 
ATOM   10846 C  CA  . ASP D 2 89  ? 12.377  -67.692 -10.225 1.00 31.01  ? 89  ASP D CA  1 
ATOM   10847 C  C   . ASP D 2 89  ? 13.339  -68.624 -10.957 1.00 34.42  ? 89  ASP D C   1 
ATOM   10848 O  O   . ASP D 2 89  ? 13.510  -69.765 -10.519 1.00 35.43  ? 89  ASP D O   1 
ATOM   10849 C  CB  . ASP D 2 89  ? 10.910  -68.088 -10.498 1.00 34.66  ? 89  ASP D CB  1 
ATOM   10850 C  CG  . ASP D 2 89  ? 10.447  -67.837 -11.941 1.00 38.47  ? 89  ASP D CG  1 
ATOM   10851 O  OD1 . ASP D 2 89  ? 11.215  -67.371 -12.807 1.00 37.92  ? 89  ASP D OD1 1 
ATOM   10852 O  OD2 . ASP D 2 89  ? 9.241   -68.092 -12.205 1.00 46.56  ? 89  ASP D OD2 1 
ATOM   10853 N  N   . TYR D 2 90  ? 14.010  -68.154 -12.014 1.00 34.49  ? 90  TYR D N   1 
ATOM   10854 C  CA  . TYR D 2 90  ? 14.992  -68.959 -12.730 1.00 33.22  ? 90  TYR D CA  1 
ATOM   10855 C  C   . TYR D 2 90  ? 16.360  -68.998 -12.049 1.00 32.26  ? 90  TYR D C   1 
ATOM   10856 O  O   . TYR D 2 90  ? 17.240  -69.718 -12.534 1.00 32.89  ? 90  TYR D O   1 
ATOM   10857 C  CB  . TYR D 2 90  ? 15.165  -68.397 -14.142 1.00 31.85  ? 90  TYR D CB  1 
ATOM   10858 C  CG  . TYR D 2 90  ? 15.448  -66.894 -14.105 1.00 30.45  ? 90  TYR D CG  1 
ATOM   10859 C  CD1 . TYR D 2 90  ? 16.720  -66.399 -13.791 1.00 29.26  ? 90  TYR D CD1 1 
ATOM   10860 C  CD2 . TYR D 2 90  ? 14.447  -65.974 -14.399 1.00 30.49  ? 90  TYR D CD2 1 
ATOM   10861 C  CE1 . TYR D 2 90  ? 16.965  -65.038 -13.772 1.00 30.54  ? 90  TYR D CE1 1 
ATOM   10862 C  CE2 . TYR D 2 90  ? 14.696  -64.625 -14.398 1.00 29.53  ? 90  TYR D CE2 1 
ATOM   10863 C  CZ  . TYR D 2 90  ? 15.961  -64.165 -14.068 1.00 31.07  ? 90  TYR D CZ  1 
ATOM   10864 O  OH  . TYR D 2 90  ? 16.229  -62.829 -14.022 1.00 29.30  ? 90  TYR D OH  1 
ATOM   10865 N  N   . ALA D 2 91  ? 16.591  -68.222 -10.977 1.00 28.93  ? 91  ALA D N   1 
ATOM   10866 C  CA  . ALA D 2 91  ? 17.923  -68.152 -10.377 1.00 28.58  ? 91  ALA D CA  1 
ATOM   10867 C  C   . ALA D 2 91  ? 18.016  -69.177 -9.253  1.00 31.16  ? 91  ALA D C   1 
ATOM   10868 O  O   . ALA D 2 91  ? 17.285  -69.076 -8.258  1.00 36.13  ? 91  ALA D O   1 
ATOM   10869 C  CB  . ALA D 2 91  ? 18.201  -66.750 -9.848  1.00 27.82  ? 91  ALA D CB  1 
ATOM   10870 N  N   . GLU D 2 92  ? 18.992  -70.084 -9.349  1.00 31.70  ? 92  GLU D N   1 
ATOM   10871 C  CA  . GLU D 2 92  ? 19.139  -71.108 -8.312  1.00 29.54  ? 92  GLU D CA  1 
ATOM   10872 C  C   . GLU D 2 92  ? 19.764  -70.538 -7.050  1.00 29.34  ? 92  GLU D C   1 
ATOM   10873 O  O   . GLU D 2 92  ? 19.508  -71.036 -5.956  1.00 26.83  ? 92  GLU D O   1 
ATOM   10874 C  CB  . GLU D 2 92  ? 19.995  -72.258 -8.840  1.00 32.03  ? 92  GLU D CB  1 
ATOM   10875 C  CG  . GLU D 2 92  ? 19.151  -73.100 -9.774  1.00 38.94  ? 92  GLU D CG  1 
ATOM   10876 C  CD  . GLU D 2 92  ? 19.312  -72.701 -11.284 1.00 40.59  ? 92  GLU D CD  1 
ATOM   10877 O  OE1 . GLU D 2 92  ? 19.174  -73.629 -12.103 1.00 36.59  ? 92  GLU D OE1 1 
ATOM   10878 O  OE2 . GLU D 2 92  ? 19.623  -71.500 -11.660 1.00 34.30  ? 92  GLU D OE2 1 
ATOM   10879 N  N   . GLY D 2 93  ? 20.621  -69.535 -7.190  1.00 29.19  ? 93  GLY D N   1 
ATOM   10880 C  CA  . GLY D 2 93  ? 21.435  -69.064 -6.083  1.00 27.02  ? 93  GLY D CA  1 
ATOM   10881 C  C   . GLY D 2 93  ? 21.091  -67.631 -5.743  1.00 25.30  ? 93  GLY D C   1 
ATOM   10882 O  O   . GLY D 2 93  ? 20.457  -66.945 -6.549  1.00 25.05  ? 93  GLY D O   1 
ATOM   10883 N  N   . VAL D 2 94  ? 21.466  -67.205 -4.559  1.00 22.23  ? 94  VAL D N   1 
ATOM   10884 C  CA  . VAL D 2 94  ? 21.455  -65.784 -4.210  1.00 23.78  ? 94  VAL D CA  1 
ATOM   10885 C  C   . VAL D 2 94  ? 22.694  -65.512 -3.386  1.00 24.97  ? 94  VAL D C   1 
ATOM   10886 O  O   . VAL D 2 94  ? 23.099  -66.339 -2.565  1.00 25.97  ? 94  VAL D O   1 
ATOM   10887 C  CB  . VAL D 2 94  ? 20.165  -65.371 -3.473  1.00 20.78  ? 94  VAL D CB  1 
ATOM   10888 C  CG1 . VAL D 2 94  ? 20.053  -66.063 -2.144  1.00 22.85  ? 94  VAL D CG1 1 
ATOM   10889 C  CG2 . VAL D 2 94  ? 20.068  -63.835 -3.288  1.00 22.14  ? 94  VAL D CG2 1 
ATOM   10890 N  N   . THR D 2 95  ? 23.301  -64.346 -3.596  1.00 18.71  ? 95  THR D N   1 
ATOM   10891 C  CA  . THR D 2 95  ? 24.537  -64.044 -2.879  1.00 19.58  ? 95  THR D CA  1 
ATOM   10892 C  C   . THR D 2 95  ? 24.645  -62.535 -2.699  1.00 24.53  ? 95  THR D C   1 
ATOM   10893 O  O   . THR D 2 95  ? 24.341  -61.762 -3.623  1.00 24.89  ? 95  THR D O   1 
ATOM   10894 C  CB  . THR D 2 95  ? 25.763  -64.591 -3.589  1.00 22.92  ? 95  THR D CB  1 
ATOM   10895 O  OG1 . THR D 2 95  ? 26.931  -64.342 -2.821  1.00 23.43  ? 95  THR D OG1 1 
ATOM   10896 C  CG2 . THR D 2 95  ? 25.935  -63.970 -4.984  1.00 21.79  ? 95  THR D CG2 1 
ATOM   10897 N  N   . LEU D 2 96  ? 25.078  -62.141 -1.500  1.00 20.95  ? 96  LEU D N   1 
ATOM   10898 C  CA  . LEU D 2 96  ? 25.353  -60.754 -1.144  1.00 21.61  ? 96  LEU D CA  1 
ATOM   10899 C  C   . LEU D 2 96  ? 26.791  -60.652 -0.622  1.00 20.95  ? 96  LEU D C   1 
ATOM   10900 O  O   . LEU D 2 96  ? 27.247  -61.505 0.133   1.00 22.00  ? 96  LEU D O   1 
ATOM   10901 C  CB  . LEU D 2 96  ? 24.346  -60.281 -0.081  1.00 20.31  ? 96  LEU D CB  1 
ATOM   10902 C  CG  . LEU D 2 96  ? 24.819  -58.963 0.576   1.00 21.23  ? 96  LEU D CG  1 
ATOM   10903 C  CD1 . LEU D 2 96  ? 24.664  -57.898 -0.497  1.00 29.38  ? 96  LEU D CD1 1 
ATOM   10904 C  CD2 . LEU D 2 96  ? 23.969  -58.653 1.787   1.00 28.62  ? 96  LEU D CD2 1 
ATOM   10905 N  N   . THR D 2 97  ? 27.487  -59.584 -0.976  1.00 22.45  ? 97  THR D N   1 
ATOM   10906 C  CA  . THR D 2 97  ? 28.778  -59.260 -0.375  1.00 20.15  ? 97  THR D CA  1 
ATOM   10907 C  C   . THR D 2 97  ? 28.539  -58.039 0.492   1.00 23.47  ? 97  THR D C   1 
ATOM   10908 O  O   . THR D 2 97  ? 27.888  -57.083 0.075   1.00 24.85  ? 97  THR D O   1 
ATOM   10909 C  CB  . THR D 2 97  ? 29.886  -59.064 -1.424  1.00 21.75  ? 97  THR D CB  1 
ATOM   10910 O  OG1 . THR D 2 97  ? 30.184  -60.334 -2.046  1.00 22.32  ? 97  THR D OG1 1 
ATOM   10911 C  CG2 . THR D 2 97  ? 31.148  -58.590 -0.764  1.00 21.72  ? 97  THR D CG2 1 
ATOM   10912 N  N   . GLN D 2 98  ? 29.009  -58.127 1.711   1.00 22.87  ? 98  GLN D N   1 
ATOM   10913 C  CA  . GLN D 2 98  ? 28.663  -57.193 2.780   1.00 20.99  ? 98  GLN D CA  1 
ATOM   10914 C  C   . GLN D 2 98  ? 29.024  -55.763 2.435   1.00 21.19  ? 98  GLN D C   1 
ATOM   10915 O  O   . GLN D 2 98  ? 30.127  -55.473 1.947   1.00 23.41  ? 98  GLN D O   1 
ATOM   10916 C  CB  . GLN D 2 98  ? 29.444  -57.655 4.009   1.00 24.72  ? 98  GLN D CB  1 
ATOM   10917 C  CG  . GLN D 2 98  ? 29.681  -56.699 5.124   1.00 24.87  ? 98  GLN D CG  1 
ATOM   10918 C  CD  . GLN D 2 98  ? 30.284  -57.473 6.248   1.00 25.39  ? 98  GLN D CD  1 
ATOM   10919 O  OE1 . GLN D 2 98  ? 29.572  -58.226 6.903   1.00 24.71  ? 98  GLN D OE1 1 
ATOM   10920 N  NE2 . GLN D 2 98  ? 31.618  -57.350 6.447   1.00 24.77  ? 98  GLN D NE2 1 
ATOM   10921 N  N   A SER D 2 99  ? 28.049  -54.879 2.627   0.55 21.83  ? 99  SER D N   1 
ATOM   10922 N  N   B SER D 2 99  ? 28.095  -54.861 2.759   0.45 21.80  ? 99  SER D N   1 
ATOM   10923 C  CA  A SER D 2 99  ? 28.287  -53.452 2.717   0.55 21.59  ? 99  SER D CA  1 
ATOM   10924 C  CA  B SER D 2 99  ? 28.292  -53.434 2.593   0.45 21.59  ? 99  SER D CA  1 
ATOM   10925 C  C   A SER D 2 99  ? 27.112  -52.926 3.521   0.55 24.25  ? 99  SER D C   1 
ATOM   10926 C  C   B SER D 2 99  ? 27.302  -52.730 3.518   0.45 24.29  ? 99  SER D C   1 
ATOM   10927 O  O   A SER D 2 99  ? 26.885  -53.373 4.653   0.55 21.23  ? 99  SER D O   1 
ATOM   10928 O  O   B SER D 2 99  ? 27.406  -52.855 4.745   0.45 22.75  ? 99  SER D O   1 
ATOM   10929 C  CB  A SER D 2 99  ? 28.436  -52.788 1.339   0.55 22.64  ? 99  SER D CB  1 
ATOM   10930 C  CB  B SER D 2 99  ? 28.125  -53.049 1.123   0.45 22.70  ? 99  SER D CB  1 
ATOM   10931 O  OG  A SER D 2 99  ? 29.032  -51.483 1.444   0.55 24.12  ? 99  SER D OG  1 
ATOM   10932 O  OG  B SER D 2 99  ? 26.850  -53.442 0.640   0.45 24.18  ? 99  SER D OG  1 
ATOM   10933 N  N   . CYS D 2 100 ? 26.328  -52.027 2.935   1.00 22.92  ? 100 CYS D N   1 
ATOM   10934 C  CA  . CYS D 2 100 ? 25.242  -51.387 3.690   1.00 25.72  ? 100 CYS D CA  1 
ATOM   10935 C  C   . CYS D 2 100 ? 24.387  -52.384 4.476   1.00 21.23  ? 100 CYS D C   1 
ATOM   10936 O  O   . CYS D 2 100 ? 24.008  -53.449 3.946   1.00 25.18  ? 100 CYS D O   1 
ATOM   10937 C  CB  . CYS D 2 100 ? 24.329  -50.654 2.699   1.00 25.85  ? 100 CYS D CB  1 
ATOM   10938 S  SG  . CYS D 2 100 ? 22.861  -49.945 3.443   1.00 26.50  ? 100 CYS D SG  1 
ATOM   10939 N  N   . ILE D 2 101 ? 24.041  -52.053 5.735   1.00 19.16  ? 101 ILE D N   1 
ATOM   10940 C  CA  . ILE D 2 101 ? 23.296  -53.049 6.526   1.00 20.84  ? 101 ILE D CA  1 
ATOM   10941 C  C   . ILE D 2 101 ? 21.845  -53.168 6.045   1.00 22.62  ? 101 ILE D C   1 
ATOM   10942 O  O   . ILE D 2 101 ? 21.206  -54.206 6.277   1.00 24.65  ? 101 ILE D O   1 
ATOM   10943 C  CB  . ILE D 2 101 ? 23.317  -52.772 8.053   1.00 22.67  ? 101 ILE D CB  1 
ATOM   10944 C  CG1 . ILE D 2 101 ? 22.765  -51.399 8.414   1.00 23.46  ? 101 ILE D CG1 1 
ATOM   10945 C  CG2 . ILE D 2 101 ? 24.779  -52.828 8.534   1.00 21.64  ? 101 ILE D CG2 1 
ATOM   10946 C  CD1 . ILE D 2 101 ? 22.454  -51.182 9.926   1.00 26.20  ? 101 ILE D CD1 1 
ATOM   10947 N  N   . GLN D 2 102 ? 21.266  -52.115 5.462   1.00 21.64  ? 102 GLN D N   1 
ATOM   10948 C  CA  . GLN D 2 102 ? 19.901  -52.238 4.968   1.00 22.84  ? 102 GLN D CA  1 
ATOM   10949 C  C   . GLN D 2 102 ? 19.793  -53.311 3.884   1.00 24.10  ? 102 GLN D C   1 
ATOM   10950 O  O   . GLN D 2 102 ? 18.820  -54.079 3.864   1.00 26.53  ? 102 GLN D O   1 
ATOM   10951 C  CB  . GLN D 2 102 ? 19.390  -50.886 4.448   1.00 24.74  ? 102 GLN D CB  1 
ATOM   10952 C  CG  . GLN D 2 102 ? 19.533  -49.774 5.489   1.00 23.55  ? 102 GLN D CG  1 
ATOM   10953 C  CD  . GLN D 2 102 ? 18.578  -48.610 5.177   1.00 29.26  ? 102 GLN D CD  1 
ATOM   10954 O  OE1 . GLN D 2 102 ? 17.602  -48.756 4.415   1.00 26.79  ? 102 GLN D OE1 1 
ATOM   10955 N  NE2 . GLN D 2 102 ? 18.869  -47.451 5.763   1.00 29.11  ? 102 GLN D NE2 1 
ATOM   10956 N  N   . TYR D 2 103 ? 20.767  -53.351 2.972   1.00 24.62  ? 103 TYR D N   1 
ATOM   10957 C  CA  . TYR D 2 103 ? 20.760  -54.331 1.901   1.00 25.57  ? 103 TYR D CA  1 
ATOM   10958 C  C   . TYR D 2 103 ? 20.875  -55.750 2.454   1.00 27.29  ? 103 TYR D C   1 
ATOM   10959 O  O   . TYR D 2 103 ? 20.383  -56.708 1.841   1.00 28.39  ? 103 TYR D O   1 
ATOM   10960 C  CB  . TYR D 2 103 ? 21.907  -53.954 0.951   1.00 27.46  ? 103 TYR D CB  1 
ATOM   10961 C  CG  . TYR D 2 103 ? 21.766  -54.175 -0.535  1.00 30.39  ? 103 TYR D CG  1 
ATOM   10962 C  CD1 . TYR D 2 103 ? 20.937  -55.178 -1.058  1.00 32.07  ? 103 TYR D CD1 1 
ATOM   10963 C  CD2 . TYR D 2 103 ? 22.545  -53.397 -1.436  1.00 36.56  ? 103 TYR D CD2 1 
ATOM   10964 C  CE1 . TYR D 2 103 ? 20.869  -55.395 -2.449  1.00 32.61  ? 103 TYR D CE1 1 
ATOM   10965 C  CE2 . TYR D 2 103 ? 22.489  -53.593 -2.812  1.00 32.95  ? 103 TYR D CE2 1 
ATOM   10966 C  CZ  . TYR D 2 103 ? 21.652  -54.582 -3.319  1.00 36.46  ? 103 TYR D CZ  1 
ATOM   10967 O  OH  . TYR D 2 103 ? 21.640  -54.763 -4.718  1.00 37.82  ? 103 TYR D OH  1 
ATOM   10968 N  N   . ARG D 2 104 ? 21.471  -55.912 3.638   1.00 26.05  ? 104 ARG D N   1 
ATOM   10969 C  CA  . ARG D 2 104 ? 21.517  -57.260 4.232   1.00 25.88  ? 104 ARG D CA  1 
ATOM   10970 C  C   . ARG D 2 104 ? 20.132  -57.835 4.515   1.00 25.88  ? 104 ARG D C   1 
ATOM   10971 O  O   . ARG D 2 104 ? 19.945  -59.056 4.458   1.00 24.92  ? 104 ARG D O   1 
ATOM   10972 C  CB  . ARG D 2 104 ? 22.374  -57.250 5.487   1.00 25.62  ? 104 ARG D CB  1 
ATOM   10973 C  CG  . ARG D 2 104 ? 23.752  -56.747 5.178   1.00 25.04  ? 104 ARG D CG  1 
ATOM   10974 C  CD  . ARG D 2 104 ? 24.654  -56.688 6.416   1.00 23.99  ? 104 ARG D CD  1 
ATOM   10975 N  NE  . ARG D 2 104 ? 25.781  -55.791 6.172   1.00 24.06  ? 104 ARG D NE  1 
ATOM   10976 C  CZ  . ARG D 2 104 ? 26.762  -55.627 7.054   1.00 24.49  ? 104 ARG D CZ  1 
ATOM   10977 N  NH1 . ARG D 2 104 ? 26.791  -56.323 8.183   1.00 23.45  ? 104 ARG D NH1 1 
ATOM   10978 N  NH2 . ARG D 2 104 ? 27.707  -54.713 6.825   1.00 22.20  ? 104 ARG D NH2 1 
ATOM   10979 N  N   . GLN D 2 105 ? 19.138  -56.990 4.746   1.00 25.65  ? 105 GLN D N   1 
ATOM   10980 C  CA  . GLN D 2 105 ? 17.752  -57.450 4.909   1.00 24.09  ? 105 GLN D CA  1 
ATOM   10981 C  C   . GLN D 2 105 ? 17.175  -58.023 3.637   1.00 26.39  ? 105 GLN D C   1 
ATOM   10982 O  O   . GLN D 2 105 ? 16.380  -58.982 3.686   1.00 27.50  ? 105 GLN D O   1 
ATOM   10983 C  CB  . GLN D 2 105 ? 16.869  -56.301 5.349   1.00 27.90  ? 105 GLN D CB  1 
ATOM   10984 C  CG  . GLN D 2 105 ? 17.237  -55.744 6.634   1.00 26.82  ? 105 GLN D CG  1 
ATOM   10985 C  CD  . GLN D 2 105 ? 16.313  -54.555 6.931   1.00 27.24  ? 105 GLN D CD  1 
ATOM   10986 O  OE1 . GLN D 2 105 ? 15.493  -54.634 7.828   1.00 27.73  ? 105 GLN D OE1 1 
ATOM   10987 N  NE2 . GLN D 2 105 ? 16.452  -53.460 6.150   1.00 26.58  ? 105 GLN D NE2 1 
ATOM   10988 N  N   . THR D 2 106 ? 17.469  -57.401 2.496   1.00 23.03  ? 106 THR D N   1 
ATOM   10989 C  CA  . THR D 2 106 ? 17.006  -57.919 1.224   1.00 25.82  ? 106 THR D CA  1 
ATOM   10990 C  C   . THR D 2 106 ? 17.475  -59.354 1.090   1.00 26.12  ? 106 THR D C   1 
ATOM   10991 O  O   . THR D 2 106 ? 16.694  -60.241 0.775   1.00 27.83  ? 106 THR D O   1 
ATOM   10992 C  CB  . THR D 2 106 ? 17.526  -57.072 0.050   1.00 24.55  ? 106 THR D CB  1 
ATOM   10993 O  OG1 . THR D 2 106 ? 17.144  -55.698 0.226   1.00 25.64  ? 106 THR D OG1 1 
ATOM   10994 C  CG2 . THR D 2 106 ? 17.148  -57.601 -1.361  1.00 24.19  ? 106 THR D CG2 1 
ATOM   10995 N  N   . PHE D 2 107 ? 18.761  -59.566 1.350   1.00 23.34  ? 107 PHE D N   1 
ATOM   10996 C  CA  . PHE D 2 107 ? 19.356  -60.884 1.237   1.00 22.65  ? 107 PHE D CA  1 
ATOM   10997 C  C   . PHE D 2 107 ? 18.729  -61.853 2.236   1.00 23.38  ? 107 PHE D C   1 
ATOM   10998 O  O   . PHE D 2 107 ? 18.371  -62.988 1.881   1.00 25.12  ? 107 PHE D O   1 
ATOM   10999 C  CB  . PHE D 2 107 ? 20.860  -60.777 1.477   1.00 23.58  ? 107 PHE D CB  1 
ATOM   11000 C  CG  . PHE D 2 107 ? 21.557  -62.141 1.539   1.00 23.60  ? 107 PHE D CG  1 
ATOM   11001 C  CD1 . PHE D 2 107 ? 21.890  -62.823 0.387   1.00 22.58  ? 107 PHE D CD1 1 
ATOM   11002 C  CD2 . PHE D 2 107 ? 21.833  -62.729 2.758   1.00 23.42  ? 107 PHE D CD2 1 
ATOM   11003 C  CE1 . PHE D 2 107 ? 22.530  -64.094 0.460   1.00 23.61  ? 107 PHE D CE1 1 
ATOM   11004 C  CE2 . PHE D 2 107 ? 22.478  -63.950 2.843   1.00 26.59  ? 107 PHE D CE2 1 
ATOM   11005 C  CZ  . PHE D 2 107 ? 22.810  -64.659 1.657   1.00 25.91  ? 107 PHE D CZ  1 
ATOM   11006 N  N   . GLY D 2 108 ? 18.603  -61.433 3.505   1.00 23.30  ? 108 GLY D N   1 
ATOM   11007 C  CA  . GLY D 2 108 ? 18.057  -62.345 4.511   1.00 23.28  ? 108 GLY D CA  1 
ATOM   11008 C  C   . GLY D 2 108 ? 16.603  -62.717 4.258   1.00 26.64  ? 108 GLY D C   1 
ATOM   11009 O  O   . GLY D 2 108 ? 16.228  -63.885 4.390   1.00 28.70  ? 108 GLY D O   1 
ATOM   11010 N  N   . SER D 2 109 ? 15.748  -61.742 3.879   1.00 24.01  ? 109 SER D N   1 
ATOM   11011 C  CA  . SER D 2 109 ? 14.367  -62.110 3.585   1.00 24.89  ? 109 SER D CA  1 
ATOM   11012 C  C   . SER D 2 109 ? 14.287  -62.951 2.322   1.00 26.86  ? 109 SER D C   1 
ATOM   11013 O  O   . SER D 2 109 ? 13.480  -63.899 2.267   1.00 26.62  ? 109 SER D O   1 
ATOM   11014 C  CB  . SER D 2 109 ? 13.464  -60.888 3.451   1.00 29.61  ? 109 SER D CB  1 
ATOM   11015 O  OG  . SER D 2 109 ? 13.356  -60.210 4.688   1.00 29.60  ? 109 SER D OG  1 
ATOM   11016 N  N   . TRP D 2 110 ? 15.116  -62.629 1.309   1.00 24.22  ? 110 TRP D N   1 
ATOM   11017 C  CA  . TRP D 2 110 ? 15.080  -63.371 0.034   1.00 24.97  ? 110 TRP D CA  1 
ATOM   11018 C  C   . TRP D 2 110 ? 15.417  -64.846 0.230   1.00 27.65  ? 110 TRP D C   1 
ATOM   11019 O  O   . TRP D 2 110 ? 14.659  -65.720 -0.178  1.00 27.46  ? 110 TRP D O   1 
ATOM   11020 C  CB  . TRP D 2 110 ? 16.026  -62.729 -0.962  1.00 23.98  ? 110 TRP D CB  1 
ATOM   11021 C  CG  . TRP D 2 110 ? 16.044  -63.252 -2.377  1.00 23.63  ? 110 TRP D CG  1 
ATOM   11022 C  CD1 . TRP D 2 110 ? 16.414  -64.538 -2.804  1.00 25.42  ? 110 TRP D CD1 1 
ATOM   11023 C  CD2 . TRP D 2 110 ? 15.845  -62.477 -3.566  1.00 24.37  ? 110 TRP D CD2 1 
ATOM   11024 N  NE1 . TRP D 2 110 ? 16.379  -64.586 -4.199  1.00 27.37  ? 110 TRP D NE1 1 
ATOM   11025 C  CE2 . TRP D 2 110 ? 16.050  -63.331 -4.674  1.00 24.95  ? 110 TRP D CE2 1 
ATOM   11026 C  CE3 . TRP D 2 110 ? 15.486  -61.136 -3.803  1.00 26.45  ? 110 TRP D CE3 1 
ATOM   11027 C  CZ2 . TRP D 2 110 ? 15.893  -62.897 -5.991  1.00 23.47  ? 110 TRP D CZ2 1 
ATOM   11028 C  CZ3 . TRP D 2 110 ? 15.349  -60.702 -5.145  1.00 25.96  ? 110 TRP D CZ3 1 
ATOM   11029 C  CH2 . TRP D 2 110 ? 15.552  -61.592 -6.205  1.00 27.06  ? 110 TRP D CH2 1 
ATOM   11030 N  N   A ARG D 2 111 ? 16.544  -65.154 0.868   0.51 26.96  ? 111 ARG D N   1 
ATOM   11031 N  N   B ARG D 2 111 ? 16.533  -65.133 0.903   0.49 26.95  ? 111 ARG D N   1 
ATOM   11032 C  CA  A ARG D 2 111 ? 16.873  -66.572 1.044   0.51 28.35  ? 111 ARG D CA  1 
ATOM   11033 C  CA  B ARG D 2 111 ? 16.928  -66.529 1.073   0.49 28.37  ? 111 ARG D CA  1 
ATOM   11034 C  C   A ARG D 2 111 ? 15.828  -67.301 1.892   0.51 28.90  ? 111 ARG D C   1 
ATOM   11035 C  C   B ARG D 2 111 ? 15.966  -67.297 1.983   0.49 28.83  ? 111 ARG D C   1 
ATOM   11036 O  O   A ARG D 2 111 ? 15.550  -68.486 1.658   0.51 28.38  ? 111 ARG D O   1 
ATOM   11037 O  O   B ARG D 2 111 ? 15.887  -68.524 1.870   0.49 28.57  ? 111 ARG D O   1 
ATOM   11038 C  CB  A ARG D 2 111 ? 18.283  -66.704 1.650   0.51 29.14  ? 111 ARG D CB  1 
ATOM   11039 C  CB  B ARG D 2 111 ? 18.389  -66.594 1.591   0.49 29.08  ? 111 ARG D CB  1 
ATOM   11040 C  CG  A ARG D 2 111 ? 18.404  -66.102 3.072   0.51 28.90  ? 111 ARG D CG  1 
ATOM   11041 C  CG  B ARG D 2 111 ? 18.560  -66.495 3.132   0.49 29.98  ? 111 ARG D CG  1 
ATOM   11042 C  CD  A ARG D 2 111 ? 19.483  -66.826 3.901   0.51 32.72  ? 111 ARG D CD  1 
ATOM   11043 C  CD  B ARG D 2 111 ? 20.000  -66.940 3.613   0.49 31.21  ? 111 ARG D CD  1 
ATOM   11044 N  NE  A ARG D 2 111 ? 20.212  -65.930 4.790   0.51 32.65  ? 111 ARG D NE  1 
ATOM   11045 N  NE  B ARG D 2 111 ? 20.429  -66.339 4.877   0.49 32.94  ? 111 ARG D NE  1 
ATOM   11046 C  CZ  A ARG D 2 111 ? 19.703  -65.230 5.801   0.51 34.20  ? 111 ARG D CZ  1 
ATOM   11047 C  CZ  B ARG D 2 111 ? 21.687  -66.282 5.318   0.49 31.84  ? 111 ARG D CZ  1 
ATOM   11048 N  NH1 A ARG D 2 111 ? 18.456  -65.420 6.229   0.51 30.45  ? 111 ARG D NH1 1 
ATOM   11049 N  NH1 B ARG D 2 111 ? 22.699  -66.741 4.600   0.49 33.48  ? 111 ARG D NH1 1 
ATOM   11050 N  NH2 A ARG D 2 111 ? 20.464  -64.303 6.393   0.51 28.75  ? 111 ARG D NH2 1 
ATOM   11051 N  NH2 B ARG D 2 111 ? 21.934  -65.747 6.511   0.49 32.59  ? 111 ARG D NH2 1 
ATOM   11052 N  N   . LEU D 2 112 ? 15.186  -66.613 2.843   1.00 27.39  ? 112 LEU D N   1 
ATOM   11053 C  CA  . LEU D 2 112 ? 14.217  -67.330 3.682   1.00 29.67  ? 112 LEU D CA  1 
ATOM   11054 C  C   . LEU D 2 112 ? 12.910  -67.584 2.946   1.00 28.37  ? 112 LEU D C   1 
ATOM   11055 O  O   . LEU D 2 112 ? 12.249  -68.601 3.189   1.00 32.28  ? 112 LEU D O   1 
ATOM   11056 C  CB  . LEU D 2 112 ? 13.873  -66.498 4.918   1.00 28.94  ? 112 LEU D CB  1 
ATOM   11057 C  CG  . LEU D 2 112 ? 14.942  -66.481 5.999   1.00 34.11  ? 112 LEU D CG  1 
ATOM   11058 C  CD1 . LEU D 2 112 ? 14.478  -65.444 7.065   1.00 34.18  ? 112 LEU D CD1 1 
ATOM   11059 C  CD2 . LEU D 2 112 ? 15.192  -67.901 6.611   1.00 32.99  ? 112 LEU D CD2 1 
ATOM   11060 N  N   . HIS D 2 113 ? 12.485  -66.648 2.092   1.00 27.69  ? 113 HIS D N   1 
ATOM   11061 C  CA  . HIS D 2 113 ? 11.114  -66.662 1.547   1.00 26.12  ? 113 HIS D CA  1 
ATOM   11062 C  C   . HIS D 2 113 ? 10.983  -66.854 0.030   1.00 30.33  ? 113 HIS D C   1 
ATOM   11063 O  O   . HIS D 2 113 ? 9.847   -67.036 -0.447  1.00 30.00  ? 113 HIS D O   1 
ATOM   11064 C  CB  . HIS D 2 113 ? 10.399  -65.365 1.929   1.00 26.54  ? 113 HIS D CB  1 
ATOM   11065 C  CG  . HIS D 2 113 ? 10.236  -65.209 3.407   1.00 26.96  ? 113 HIS D CG  1 
ATOM   11066 N  ND1 . HIS D 2 113 ? 9.392   -66.010 4.150   1.00 31.13  ? 113 HIS D ND1 1 
ATOM   11067 C  CD2 . HIS D 2 113 ? 10.823  -64.358 4.280   1.00 31.32  ? 113 HIS D CD2 1 
ATOM   11068 C  CE1 . HIS D 2 113 ? 9.449   -65.636 5.425   1.00 30.59  ? 113 HIS D CE1 1 
ATOM   11069 N  NE2 . HIS D 2 113 ? 10.328  -64.647 5.526   1.00 27.76  ? 113 HIS D NE2 1 
ATOM   11070 N  N   . VAL D 2 114 ? 12.060  -66.797 -0.741  1.00 28.13  ? 114 VAL D N   1 
ATOM   11071 C  CA  . VAL D 2 114 ? 11.934  -67.061 -2.188  1.00 25.61  ? 114 VAL D CA  1 
ATOM   11072 C  C   . VAL D 2 114 ? 12.082  -68.567 -2.389  1.00 29.59  ? 114 VAL D C   1 
ATOM   11073 O  O   . VAL D 2 114 ? 13.187  -69.111 -2.226  1.00 28.95  ? 114 VAL D O   1 
ATOM   11074 C  CB  . VAL D 2 114 ? 12.925  -66.240 -3.023  1.00 25.87  ? 114 VAL D CB  1 
ATOM   11075 C  CG1 . VAL D 2 114 ? 12.778  -66.556 -4.492  1.00 27.40  ? 114 VAL D CG1 1 
ATOM   11076 C  CG2 . VAL D 2 114 ? 12.651  -64.739 -2.817  1.00 27.08  ? 114 VAL D CG2 1 
ATOM   11077 N  N   . PRO D 2 115 ? 10.984  -69.273 -2.691  1.00 29.97  ? 115 PRO D N   1 
ATOM   11078 C  CA  . PRO D 2 115 ? 11.007  -70.753 -2.659  1.00 33.01  ? 115 PRO D CA  1 
ATOM   11079 C  C   . PRO D 2 115 ? 11.918  -71.371 -3.698  1.00 33.09  ? 115 PRO D C   1 
ATOM   11080 O  O   . PRO D 2 115 ? 12.297  -72.542 -3.542  1.00 33.36  ? 115 PRO D O   1 
ATOM   11081 C  CB  . PRO D 2 115 ? 9.547   -71.153 -2.912  1.00 34.75  ? 115 PRO D CB  1 
ATOM   11082 C  CG  . PRO D 2 115 ? 8.822   -69.913 -3.210  1.00 37.87  ? 115 PRO D CG  1 
ATOM   11083 C  CD  . PRO D 2 115 ? 9.760   -68.748 -3.308  1.00 31.94  ? 115 PRO D CD  1 
ATOM   11084 N  N   . THR D 2 116 ? 12.279  -70.634 -4.749  1.00 30.93  ? 116 THR D N   1 
ATOM   11085 C  CA  . THR D 2 116 ? 13.147  -71.192 -5.783  1.00 28.28  ? 116 THR D CA  1 
ATOM   11086 C  C   . THR D 2 116 ? 14.636  -71.139 -5.427  1.00 31.12  ? 116 THR D C   1 
ATOM   11087 O  O   . THR D 2 116 ? 15.454  -71.668 -6.188  1.00 32.43  ? 116 THR D O   1 
ATOM   11088 C  CB  . THR D 2 116 ? 12.895  -70.452 -7.110  1.00 32.24  ? 116 THR D CB  1 
ATOM   11089 O  OG1 . THR D 2 116 ? 12.899  -69.035 -6.856  1.00 30.95  ? 116 THR D OG1 1 
ATOM   11090 C  CG2 . THR D 2 116 ? 11.540  -70.832 -7.713  1.00 32.33  ? 116 THR D CG2 1 
ATOM   11091 N  N   . VAL D 2 117 ? 15.022  -70.506 -4.310  1.00 29.90  ? 117 VAL D N   1 
ATOM   11092 C  CA  . VAL D 2 117 ? 16.427  -70.477 -3.903  1.00 28.04  ? 117 VAL D CA  1 
ATOM   11093 C  C   . VAL D 2 117 ? 16.874  -71.878 -3.493  1.00 31.50  ? 117 VAL D C   1 
ATOM   11094 O  O   . VAL D 2 117 ? 16.297  -72.478 -2.576  1.00 33.00  ? 117 VAL D O   1 
ATOM   11095 C  CB  . VAL D 2 117 ? 16.638  -69.495 -2.754  1.00 25.76  ? 117 VAL D CB  1 
ATOM   11096 C  CG1 . VAL D 2 117 ? 18.127  -69.547 -2.251  1.00 27.82  ? 117 VAL D CG1 1 
ATOM   11097 C  CG2 . VAL D 2 117 ? 16.221  -68.071 -3.196  1.00 30.78  ? 117 VAL D CG2 1 
ATOM   11098 N  N   . LYS D 2 118 ? 17.935  -72.387 -4.142  1.00 31.20  ? 118 LYS D N   1 
ATOM   11099 C  CA  . LYS D 2 118 ? 18.555  -73.672 -3.774  1.00 30.21  ? 118 LYS D CA  1 
ATOM   11100 C  C   . LYS D 2 118 ? 19.821  -73.501 -2.953  1.00 31.39  ? 118 LYS D C   1 
ATOM   11101 O  O   . LYS D 2 118 ? 20.166  -74.405 -2.191  1.00 29.62  ? 118 LYS D O   1 
ATOM   11102 C  CB  . LYS D 2 118 ? 18.914  -74.518 -5.005  1.00 28.78  ? 118 LYS D CB  1 
ATOM   11103 C  CG  . LYS D 2 118 ? 17.835  -74.598 -6.095  1.00 34.14  ? 118 LYS D CG  1 
ATOM   11104 C  CD  . LYS D 2 118 ? 17.829  -75.949 -6.806  1.00 43.26  ? 118 LYS D CD  1 
ATOM   11105 C  CE  . LYS D 2 118 ? 16.513  -76.143 -7.578  1.00 49.52  ? 118 LYS D CE  1 
ATOM   11106 N  NZ  . LYS D 2 118 ? 16.608  -75.688 -9.013  1.00 51.97  ? 118 LYS D NZ  1 
ATOM   11107 N  N   . TRP D 2 119 ? 20.509  -72.371 -3.061  1.00 27.06  ? 119 TRP D N   1 
ATOM   11108 C  CA  . TRP D 2 119 ? 21.647  -72.109 -2.186  1.00 28.92  ? 119 TRP D CA  1 
ATOM   11109 C  C   . TRP D 2 119 ? 21.832  -70.609 -2.023  1.00 23.75  ? 119 TRP D C   1 
ATOM   11110 O  O   . TRP D 2 119 ? 21.409  -69.831 -2.878  1.00 27.11  ? 119 TRP D O   1 
ATOM   11111 C  CB  . TRP D 2 119 ? 22.924  -72.740 -2.735  1.00 26.09  ? 119 TRP D CB  1 
ATOM   11112 C  CG  . TRP D 2 119 ? 23.334  -72.230 -4.085  1.00 28.71  ? 119 TRP D CG  1 
ATOM   11113 C  CD1 . TRP D 2 119 ? 22.974  -72.753 -5.310  1.00 30.92  ? 119 TRP D CD1 1 
ATOM   11114 C  CD2 . TRP D 2 119 ? 24.165  -71.092 -4.352  1.00 27.84  ? 119 TRP D CD2 1 
ATOM   11115 N  NE1 . TRP D 2 119 ? 23.550  -71.985 -6.325  1.00 35.66  ? 119 TRP D NE1 1 
ATOM   11116 C  CE2 . TRP D 2 119 ? 24.286  -70.976 -5.760  1.00 30.97  ? 119 TRP D CE2 1 
ATOM   11117 C  CE3 . TRP D 2 119 ? 24.826  -70.156 -3.543  1.00 26.18  ? 119 TRP D CE3 1 
ATOM   11118 C  CZ2 . TRP D 2 119 ? 25.076  -69.961 -6.365  1.00 29.30  ? 119 TRP D CZ2 1 
ATOM   11119 C  CZ3 . TRP D 2 119 ? 25.612  -69.155 -4.159  1.00 28.95  ? 119 TRP D CZ3 1 
ATOM   11120 C  CH2 . TRP D 2 119 ? 25.717  -69.076 -5.555  1.00 30.43  ? 119 TRP D CH2 1 
ATOM   11121 N  N   . ASP D 2 120 ? 22.547  -70.230 -0.965  1.00 23.70  ? 120 ASP D N   1 
ATOM   11122 C  CA  . ASP D 2 120 ? 22.841  -68.817 -0.713  1.00 23.95  ? 120 ASP D CA  1 
ATOM   11123 C  C   . ASP D 2 120 ? 24.229  -68.680 -0.109  1.00 24.52  ? 120 ASP D C   1 
ATOM   11124 O  O   . ASP D 2 120 ? 24.785  -69.639 0.427   1.00 24.92  ? 120 ASP D O   1 
ATOM   11125 C  CB  . ASP D 2 120 ? 21.800  -68.201 0.208   1.00 23.43  ? 120 ASP D CB  1 
ATOM   11126 C  CG  . ASP D 2 120 ? 21.830  -68.802 1.616   1.00 29.28  ? 120 ASP D CG  1 
ATOM   11127 O  OD1 . ASP D 2 120 ? 22.597  -68.335 2.447   1.00 30.48  ? 120 ASP D OD1 1 
ATOM   11128 O  OD2 . ASP D 2 120 ? 21.129  -69.794 1.841   1.00 33.81  ? 120 ASP D OD2 1 
ATOM   11129 N  N   . TYR D 2 121 ? 24.807  -67.473 -0.217  1.00 21.27  ? 121 TYR D N   1 
ATOM   11130 C  CA  . TYR D 2 121 ? 26.124  -67.256 0.378   1.00 21.09  ? 121 TYR D CA  1 
ATOM   11131 C  C   . TYR D 2 121 ? 26.293  -65.780 0.671   1.00 21.34  ? 121 TYR D C   1 
ATOM   11132 O  O   . TYR D 2 121 ? 26.121  -64.946 -0.234  1.00 22.86  ? 121 TYR D O   1 
ATOM   11133 C  CB  . TYR D 2 121 ? 27.233  -67.714 -0.539  1.00 22.08  ? 121 TYR D CB  1 
ATOM   11134 C  CG  . TYR D 2 121 ? 28.567  -67.851 0.178   1.00 21.96  ? 121 TYR D CG  1 
ATOM   11135 C  CD1 . TYR D 2 121 ? 29.409  -66.738 0.336   1.00 22.81  ? 121 TYR D CD1 1 
ATOM   11136 C  CD2 . TYR D 2 121 ? 28.967  -69.086 0.731   1.00 23.96  ? 121 TYR D CD2 1 
ATOM   11137 C  CE1 . TYR D 2 121 ? 30.625  -66.834 1.001   1.00 23.25  ? 121 TYR D CE1 1 
ATOM   11138 C  CE2 . TYR D 2 121 ? 30.189  -69.201 1.379   1.00 25.05  ? 121 TYR D CE2 1 
ATOM   11139 C  CZ  . TYR D 2 121 ? 31.011  -68.093 1.515   1.00 22.85  ? 121 TYR D CZ  1 
ATOM   11140 O  OH  . TYR D 2 121 ? 32.233  -68.212 2.171   1.00 22.05  ? 121 TYR D OH  1 
ATOM   11141 N  N   . TYR D 2 122 ? 26.673  -65.479 1.915   1.00 20.72  ? 122 TYR D N   1 
ATOM   11142 C  CA  . TYR D 2 122 ? 26.969  -64.114 2.367   1.00 21.38  ? 122 TYR D CA  1 
ATOM   11143 C  C   . TYR D 2 122 ? 28.493  -63.974 2.471   1.00 21.72  ? 122 TYR D C   1 
ATOM   11144 O  O   . TYR D 2 122 ? 29.138  -64.719 3.213   1.00 21.70  ? 122 TYR D O   1 
ATOM   11145 C  CB  . TYR D 2 122 ? 26.286  -63.917 3.707   1.00 21.85  ? 122 TYR D CB  1 
ATOM   11146 C  CG  . TYR D 2 122 ? 26.495  -62.552 4.325   1.00 22.54  ? 122 TYR D CG  1 
ATOM   11147 C  CD1 . TYR D 2 122 ? 27.646  -62.294 5.076   1.00 21.85  ? 122 TYR D CD1 1 
ATOM   11148 C  CD2 . TYR D 2 122 ? 25.548  -61.568 4.222   1.00 31.71  ? 122 TYR D CD2 1 
ATOM   11149 C  CE1 . TYR D 2 122 ? 27.847  -61.045 5.699   1.00 23.03  ? 122 TYR D CE1 1 
ATOM   11150 C  CE2 . TYR D 2 122 ? 25.759  -60.306 4.825   1.00 27.52  ? 122 TYR D CE2 1 
ATOM   11151 C  CZ  . TYR D 2 122 ? 26.925  -60.052 5.519   1.00 25.91  ? 122 TYR D CZ  1 
ATOM   11152 O  OH  . TYR D 2 122 ? 27.179  -58.804 6.165   1.00 27.16  ? 122 TYR D OH  1 
ATOM   11153 N  N   . VAL D 2 123 ? 29.070  -63.027 1.736   1.00 19.84  ? 123 VAL D N   1 
ATOM   11154 C  CA  . VAL D 2 123 ? 30.510  -62.802 1.737   1.00 19.95  ? 123 VAL D CA  1 
ATOM   11155 C  C   . VAL D 2 123 ? 30.793  -61.632 2.691   1.00 20.90  ? 123 VAL D C   1 
ATOM   11156 O  O   . VAL D 2 123 ? 30.475  -60.490 2.346   1.00 22.28  ? 123 VAL D O   1 
ATOM   11157 C  CB  . VAL D 2 123 ? 31.025  -62.480 0.324   1.00 21.93  ? 123 VAL D CB  1 
ATOM   11158 C  CG1 . VAL D 2 123 ? 32.544  -62.261 0.431   1.00 24.01  ? 123 VAL D CG1 1 
ATOM   11159 C  CG2 . VAL D 2 123 ? 30.726  -63.552 -0.621  1.00 20.62  ? 123 VAL D CG2 1 
ATOM   11160 N  N   . PRO D 2 124 ? 31.421  -61.864 3.893   1.00 21.87  ? 124 PRO D N   1 
ATOM   11161 C  CA  . PRO D 2 124 ? 31.706  -60.694 4.818   1.00 20.93  ? 124 PRO D CA  1 
ATOM   11162 C  C   . PRO D 2 124 ? 32.982  -59.987 4.392   1.00 22.87  ? 124 PRO D C   1 
ATOM   11163 O  O   . PRO D 2 124 ? 34.050  -60.045 5.019   1.00 23.72  ? 124 PRO D O   1 
ATOM   11164 C  CB  . PRO D 2 124 ? 31.795  -61.372 6.198   1.00 25.25  ? 124 PRO D CB  1 
ATOM   11165 C  CG  . PRO D 2 124 ? 31.552  -62.871 5.962   1.00 27.42  ? 124 PRO D CG  1 
ATOM   11166 C  CD  . PRO D 2 124 ? 31.759  -63.153 4.516   1.00 20.67  ? 124 PRO D CD  1 
ATOM   11167 N  N   . MET D 2 125 ? 32.906  -59.332 3.237   1.00 21.51  ? 125 MET D N   1 
ATOM   11168 C  CA  . MET D 2 125 ? 33.989  -58.480 2.816   1.00 21.00  ? 125 MET D CA  1 
ATOM   11169 C  C   . MET D 2 125 ? 34.245  -57.377 3.816   1.00 19.53  ? 125 MET D C   1 
ATOM   11170 O  O   . MET D 2 125 ? 33.301  -56.672 4.208   1.00 20.32  ? 125 MET D O   1 
ATOM   11171 C  CB  . MET D 2 125 ? 33.705  -57.926 1.423   1.00 21.12  ? 125 MET D CB  1 
ATOM   11172 C  CG  . MET D 2 125 ? 34.842  -57.157 0.791   1.00 23.73  ? 125 MET D CG  1 
ATOM   11173 S  SD  . MET D 2 125 ? 34.309  -55.951 -0.468  1.00 22.27  ? 125 MET D SD  1 
ATOM   11174 C  CE  . MET D 2 125 ? 35.761  -54.890 -0.444  1.00 23.61  ? 125 MET D CE  1 
ATOM   11175 N  N   . PRO D 2 126 ? 35.494  -57.194 4.246   1.00 19.68  ? 126 PRO D N   1 
ATOM   11176 C  CA  . PRO D 2 126 ? 35.807  -56.078 5.144   1.00 21.47  ? 126 PRO D CA  1 
ATOM   11177 C  C   . PRO D 2 126 ? 35.204  -54.768 4.663   1.00 20.73  ? 126 PRO D C   1 
ATOM   11178 O  O   . PRO D 2 126 ? 35.216  -54.439 3.466   1.00 21.35  ? 126 PRO D O   1 
ATOM   11179 C  CB  . PRO D 2 126 ? 37.350  -56.017 5.114   1.00 21.11  ? 126 PRO D CB  1 
ATOM   11180 C  CG  . PRO D 2 126 ? 37.759  -57.457 4.827   1.00 22.57  ? 126 PRO D CG  1 
ATOM   11181 C  CD  . PRO D 2 126 ? 36.703  -57.956 3.878   1.00 22.84  ? 126 PRO D CD  1 
ATOM   11182 N  N   . ASN D 2 127 ? 34.666  -54.019 5.621   1.00 20.77  ? 127 ASN D N   1 
ATOM   11183 C  CA  . ASN D 2 127 ? 34.271  -52.645 5.330   1.00 20.29  ? 127 ASN D CA  1 
ATOM   11184 C  C   . ASN D 2 127 ? 35.474  -51.715 5.359   1.00 21.48  ? 127 ASN D C   1 
ATOM   11185 O  O   . ASN D 2 127 ? 35.529  -50.776 4.562   1.00 20.19  ? 127 ASN D O   1 
ATOM   11186 C  CB  . ASN D 2 127 ? 33.265  -52.126 6.348   1.00 18.15  ? 127 ASN D CB  1 
ATOM   11187 C  CG  . ASN D 2 127 ? 31.862  -52.632 6.096   1.00 23.08  ? 127 ASN D CG  1 
ATOM   11188 O  OD1 . ASN D 2 127 ? 31.507  -53.028 4.985   1.00 21.51  ? 127 ASN D OD1 1 
ATOM   11189 N  ND2 . ASN D 2 127 ? 31.064  -52.693 7.171   1.00 23.30  ? 127 ASN D ND2 1 
ATOM   11190 N  N   . GLU D 2 128 ? 36.442  -51.921 6.256   1.00 20.14  ? 128 GLU D N   1 
ATOM   11191 C  CA  . GLU D 2 128 ? 37.560  -50.962 6.383   1.00 22.15  ? 128 GLU D CA  1 
ATOM   11192 C  C   . GLU D 2 128 ? 38.679  -51.337 5.409   1.00 22.18  ? 128 GLU D C   1 
ATOM   11193 O  O   . GLU D 2 128 ? 39.778  -51.741 5.776   1.00 21.79  ? 128 GLU D O   1 
ATOM   11194 C  CB  . GLU D 2 128 ? 38.074  -50.868 7.826   1.00 19.43  ? 128 GLU D CB  1 
ATOM   11195 C  CG  . GLU D 2 128 ? 38.993  -49.726 8.032   1.00 21.65  ? 128 GLU D CG  1 
ATOM   11196 C  CD  . GLU D 2 128 ? 39.275  -49.421 9.460   1.00 22.88  ? 128 GLU D CD  1 
ATOM   11197 O  OE1 . GLU D 2 128 ? 38.703  -50.101 10.353  1.00 22.30  ? 128 GLU D OE1 1 
ATOM   11198 O  OE2 . GLU D 2 128 ? 40.159  -48.558 9.668   1.00 24.68  ? 128 GLU D OE2 1 
ATOM   11199 N  N   . VAL D 2 129 ? 38.385  -51.113 4.121   1.00 20.00  ? 129 VAL D N   1 
ATOM   11200 C  CA  . VAL D 2 129 ? 39.406  -51.350 3.075   1.00 21.77  ? 129 VAL D CA  1 
ATOM   11201 C  C   . VAL D 2 129 ? 40.654  -50.497 3.262   1.00 22.52  ? 129 VAL D C   1 
ATOM   11202 O  O   . VAL D 2 129 ? 41.715  -50.802 2.695   1.00 23.23  ? 129 VAL D O   1 
ATOM   11203 C  CB  . VAL D 2 129 ? 38.787  -51.146 1.677   1.00 22.51  ? 129 VAL D CB  1 
ATOM   11204 C  CG1 . VAL D 2 129 ? 37.709  -52.216 1.448   1.00 22.48  ? 129 VAL D CG1 1 
ATOM   11205 C  CG2 . VAL D 2 129 ? 38.202  -49.710 1.509   1.00 23.13  ? 129 VAL D CG2 1 
ATOM   11206 N  N   . GLN D 2 130 ? 40.553  -49.396 4.024   1.00 20.24  ? 130 GLN D N   1 
ATOM   11207 C  CA  . GLN D 2 130 ? 41.726  -48.611 4.356   1.00 18.92  ? 130 GLN D CA  1 
ATOM   11208 C  C   . GLN D 2 130 ? 42.647  -49.294 5.338   1.00 23.27  ? 130 GLN D C   1 
ATOM   11209 O  O   . GLN D 2 130 ? 43.767  -48.807 5.518   1.00 23.26  ? 130 GLN D O   1 
ATOM   11210 C  CB  . GLN D 2 130 ? 41.294  -47.239 4.913   1.00 20.07  ? 130 GLN D CB  1 
ATOM   11211 C  CG  . GLN D 2 130 ? 40.706  -46.338 3.806   1.00 21.67  ? 130 GLN D CG  1 
ATOM   11212 C  CD  . GLN D 2 130 ? 40.082  -45.041 4.329   1.00 21.26  ? 130 GLN D CD  1 
ATOM   11213 O  OE1 . GLN D 2 130 ? 40.596  -44.419 5.233   1.00 22.60  ? 130 GLN D OE1 1 
ATOM   11214 N  NE2 . GLN D 2 130 ? 38.950  -44.667 3.768   1.00 22.47  ? 130 GLN D NE2 1 
ATOM   11215 N  N   . SER D 2 131 ? 42.197  -50.375 6.000   1.00 20.89  ? 131 SER D N   1 
ATOM   11216 C  CA  . SER D 2 131 ? 43.017  -51.034 7.001   1.00 22.46  ? 131 SER D CA  1 
ATOM   11217 C  C   . SER D 2 131 ? 44.100  -51.842 6.309   1.00 21.95  ? 131 SER D C   1 
ATOM   11218 O  O   . SER D 2 131 ? 43.807  -52.511 5.327   1.00 22.21  ? 131 SER D O   1 
ATOM   11219 C  CB  . SER D 2 131 ? 42.200  -52.028 7.833   1.00 23.33  ? 131 SER D CB  1 
ATOM   11220 O  OG  . SER D 2 131 ? 43.091  -52.853 8.560   1.00 22.26  ? 131 SER D OG  1 
ATOM   11221 N  N   . PRO D 2 132 ? 45.326  -51.862 6.854   1.00 25.34  ? 132 PRO D N   1 
ATOM   11222 C  CA  . PRO D 2 132 ? 46.368  -52.726 6.286   1.00 21.35  ? 132 PRO D CA  1 
ATOM   11223 C  C   . PRO D 2 132 ? 46.070  -54.196 6.364   1.00 21.91  ? 132 PRO D C   1 
ATOM   11224 O  O   . PRO D 2 132 ? 46.820  -54.972 5.752   1.00 23.64  ? 132 PRO D O   1 
ATOM   11225 C  CB  . PRO D 2 132 ? 47.614  -52.383 7.106   1.00 25.24  ? 132 PRO D CB  1 
ATOM   11226 C  CG  . PRO D 2 132 ? 47.130  -51.591 8.307   1.00 29.50  ? 132 PRO D CG  1 
ATOM   11227 C  CD  . PRO D 2 132 ? 45.834  -50.930 7.880   1.00 22.04  ? 132 PRO D CD  1 
ATOM   11228 N  N   . HIS D 2 133 ? 45.056  -54.607 7.116   1.00 21.06  ? 133 HIS D N   1 
ATOM   11229 C  CA  . HIS D 2 133 ? 44.741  -56.030 7.288   1.00 20.27  ? 133 HIS D CA  1 
ATOM   11230 C  C   . HIS D 2 133 ? 43.563  -56.479 6.423   1.00 21.42  ? 133 HIS D C   1 
ATOM   11231 O  O   . HIS D 2 133 ? 43.251  -57.690 6.349   1.00 20.12  ? 133 HIS D O   1 
ATOM   11232 C  CB  . HIS D 2 133 ? 44.498  -56.265 8.781   1.00 21.35  ? 133 HIS D CB  1 
ATOM   11233 C  CG  . HIS D 2 133 ? 45.648  -55.823 9.624   1.00 23.44  ? 133 HIS D CG  1 
ATOM   11234 N  ND1 . HIS D 2 133 ? 46.866  -56.445 9.574   1.00 25.53  ? 133 HIS D ND1 1 
ATOM   11235 C  CD2 . HIS D 2 133 ? 45.781  -54.802 10.504  1.00 24.49  ? 133 HIS D CD2 1 
ATOM   11236 C  CE1 . HIS D 2 133 ? 47.711  -55.836 10.383  1.00 24.31  ? 133 HIS D CE1 1 
ATOM   11237 N  NE2 . HIS D 2 133 ? 47.077  -54.821 10.959  1.00 23.07  ? 133 HIS D NE2 1 
ATOM   11238 N  N   . ALA D 2 134 ? 42.918  -55.530 5.732   1.00 20.66  ? 134 ALA D N   1 
ATOM   11239 C  CA  . ALA D 2 134 ? 41.675  -55.879 5.065   1.00 21.94  ? 134 ALA D CA  1 
ATOM   11240 C  C   . ALA D 2 134 ? 41.937  -56.770 3.845   1.00 23.98  ? 134 ALA D C   1 
ATOM   11241 O  O   . ALA D 2 134 ? 41.138  -57.675 3.549   1.00 22.91  ? 134 ALA D O   1 
ATOM   11242 C  CB  . ALA D 2 134 ? 40.922  -54.595 4.685   1.00 21.66  ? 134 ALA D CB  1 
ATOM   11243 N  N   . ARG D 2 135 ? 43.062  -56.556 3.143   1.00 21.14  ? 135 ARG D N   1 
ATOM   11244 C  CA  . ARG D 2 135 ? 43.293  -57.306 1.904   1.00 21.17  ? 135 ARG D CA  1 
ATOM   11245 C  C   . ARG D 2 135 ? 43.605  -58.773 2.187   1.00 23.72  ? 135 ARG D C   1 
ATOM   11246 O  O   . ARG D 2 135 ? 43.176  -59.677 1.432   1.00 26.32  ? 135 ARG D O   1 
ATOM   11247 C  CB  . ARG D 2 135 ? 44.377  -56.604 1.082   1.00 23.11  ? 135 ARG D CB  1 
ATOM   11248 C  CG  . ARG D 2 135 ? 43.786  -55.413 0.334   1.00 23.45  ? 135 ARG D CG  1 
ATOM   11249 C  CD  . ARG D 2 135 ? 44.811  -54.423 -0.099  1.00 23.60  ? 135 ARG D CD  1 
ATOM   11250 N  NE  . ARG D 2 135 ? 44.154  -53.239 -0.652  1.00 22.86  ? 135 ARG D NE  1 
ATOM   11251 C  CZ  . ARG D 2 135 ? 43.525  -52.333 0.094   1.00 25.42  ? 135 ARG D CZ  1 
ATOM   11252 N  NH1 . ARG D 2 135 ? 43.476  -52.436 1.425   1.00 25.43  ? 135 ARG D NH1 1 
ATOM   11253 N  NH2 . ARG D 2 135 ? 42.889  -51.334 -0.514  1.00 26.07  ? 135 ARG D NH2 1 
ATOM   11254 N  N   . LYS D 2 136 ? 44.340  -59.029 3.244   1.00 21.85  ? 136 LYS D N   1 
ATOM   11255 C  CA  . LYS D 2 136 ? 44.540  -60.415 3.671   1.00 24.30  ? 136 LYS D CA  1 
ATOM   11256 C  C   . LYS D 2 136 ? 43.219  -61.054 4.119   1.00 26.54  ? 136 LYS D C   1 
ATOM   11257 O  O   . LYS D 2 136 ? 42.929  -62.213 3.756   1.00 22.72  ? 136 LYS D O   1 
ATOM   11258 C  CB  . LYS D 2 136 ? 45.592  -60.457 4.777   1.00 20.50  ? 136 LYS D CB  1 
ATOM   11259 C  CG  . LYS D 2 136 ? 45.817  -61.907 5.395   1.00 26.55  ? 136 LYS D CG  1 
ATOM   11260 C  CD  . LYS D 2 136 ? 46.314  -62.906 4.409   1.00 29.43  ? 136 LYS D CD  1 
ATOM   11261 C  CE  . LYS D 2 136 ? 46.370  -64.272 5.087   1.00 36.78  ? 136 LYS D CE  1 
ATOM   11262 N  NZ  . LYS D 2 136 ? 46.801  -65.384 4.206   1.00 37.50  ? 136 LYS D NZ  1 
ATOM   11263 N  N   . ALA D 2 137 ? 42.399  -60.327 4.903   1.00 21.76  ? 137 ALA D N   1 
ATOM   11264 C  CA  . ALA D 2 137 ? 41.089  -60.897 5.291   1.00 19.63  ? 137 ALA D CA  1 
ATOM   11265 C  C   . ALA D 2 137 ? 40.216  -61.177 4.070   1.00 21.88  ? 137 ALA D C   1 
ATOM   11266 O  O   . ALA D 2 137 ? 39.641  -62.263 3.952   1.00 21.15  ? 137 ALA D O   1 
ATOM   11267 C  CB  . ALA D 2 137 ? 40.360  -59.977 6.279   1.00 20.65  ? 137 ALA D CB  1 
ATOM   11268 N  N   . HIS D 2 138 ? 40.180  -60.256 3.099   1.00 22.72  ? 138 HIS D N   1 
ATOM   11269 C  CA  . HIS D 2 138 ? 39.316  -60.506 1.960   1.00 20.53  ? 138 HIS D CA  1 
ATOM   11270 C  C   . HIS D 2 138 ? 39.885  -61.575 1.043   1.00 20.58  ? 138 HIS D C   1 
ATOM   11271 O  O   . HIS D 2 138 ? 39.114  -62.325 0.449   1.00 22.26  ? 138 HIS D O   1 
ATOM   11272 C  CB  . HIS D 2 138 ? 39.051  -59.218 1.158   1.00 19.16  ? 138 HIS D CB  1 
ATOM   11273 C  CG  . HIS D 2 138 ? 37.847  -59.333 0.272   1.00 21.57  ? 138 HIS D CG  1 
ATOM   11274 N  ND1 . HIS D 2 138 ? 36.699  -59.999 0.670   1.00 21.81  ? 138 HIS D ND1 1 
ATOM   11275 C  CD2 . HIS D 2 138 ? 37.626  -58.927 -0.993  1.00 23.18  ? 138 HIS D CD2 1 
ATOM   11276 C  CE1 . HIS D 2 138 ? 35.809  -59.965 -0.292  1.00 21.29  ? 138 HIS D CE1 1 
ATOM   11277 N  NE2 . HIS D 2 138 ? 36.344  -59.313 -1.321  1.00 22.88  ? 138 HIS D NE2 1 
ATOM   11278 N  N   . TYR D 2 139 ? 41.213  -61.695 0.956   1.00 20.59  ? 139 TYR D N   1 
ATOM   11279 C  CA  . TYR D 2 139 ? 41.831  -62.848 0.274   1.00 20.92  ? 139 TYR D CA  1 
ATOM   11280 C  C   . TYR D 2 139 ? 41.222  -64.148 0.778   1.00 23.25  ? 139 TYR D C   1 
ATOM   11281 O  O   . TYR D 2 139 ? 40.830  -65.014 -0.013  1.00 22.70  ? 139 TYR D O   1 
ATOM   11282 C  CB  . TYR D 2 139 ? 43.356  -62.817 0.520   1.00 24.22  ? 139 TYR D CB  1 
ATOM   11283 C  CG  . TYR D 2 139 ? 44.150  -63.954 -0.129  1.00 22.91  ? 139 TYR D CG  1 
ATOM   11284 C  CD1 . TYR D 2 139 ? 44.269  -65.223 0.495   1.00 26.89  ? 139 TYR D CD1 1 
ATOM   11285 C  CD2 . TYR D 2 139 ? 44.736  -63.794 -1.387  1.00 21.79  ? 139 TYR D CD2 1 
ATOM   11286 C  CE1 . TYR D 2 139 ? 44.991  -66.265 -0.127  1.00 29.49  ? 139 TYR D CE1 1 
ATOM   11287 C  CE2 . TYR D 2 139 ? 45.438  -64.867 -2.020  1.00 24.36  ? 139 TYR D CE2 1 
ATOM   11288 C  CZ  . TYR D 2 139 ? 45.559  -66.071 -1.375  1.00 26.71  ? 139 TYR D CZ  1 
ATOM   11289 O  OH  . TYR D 2 139 ? 46.254  -67.092 -2.011  1.00 27.97  ? 139 TYR D OH  1 
ATOM   11290 N  N   . GLU D 2 140 ? 41.164  -64.313 2.102   1.00 20.04  ? 140 GLU D N   1 
ATOM   11291 C  CA  . GLU D 2 140 ? 40.631  -65.553 2.654   1.00 18.91  ? 140 GLU D CA  1 
ATOM   11292 C  C   . GLU D 2 140 ? 39.124  -65.670 2.442   1.00 19.61  ? 140 GLU D C   1 
ATOM   11293 O  O   . GLU D 2 140 ? 38.633  -66.780 2.229   1.00 22.18  ? 140 GLU D O   1 
ATOM   11294 C  CB  . GLU D 2 140 ? 41.010  -65.678 4.117   1.00 21.92  ? 140 GLU D CB  1 
ATOM   11295 C  CG  . GLU D 2 140 ? 42.520  -65.729 4.367   1.00 23.31  ? 140 GLU D CG  1 
ATOM   11296 C  CD  . GLU D 2 140 ? 43.267  -66.949 3.782   1.00 29.56  ? 140 GLU D CD  1 
ATOM   11297 O  OE1 . GLU D 2 140 ? 42.649  -67.913 3.271   1.00 30.17  ? 140 GLU D OE1 1 
ATOM   11298 O  OE2 . GLU D 2 140 ? 44.512  -66.943 3.850   1.00 30.45  ? 140 GLU D OE2 1 
ATOM   11299 N  N   . GLU D 2 141 ? 38.385  -64.561 2.439   1.00 20.66  ? 141 GLU D N   1 
ATOM   11300 C  CA  . GLU D 2 141 ? 36.950  -64.652 2.109   1.00 19.36  ? 141 GLU D CA  1 
ATOM   11301 C  C   . GLU D 2 141 ? 36.713  -65.101 0.683   1.00 20.16  ? 141 GLU D C   1 
ATOM   11302 O  O   . GLU D 2 141 ? 35.825  -65.935 0.423   1.00 22.68  ? 141 GLU D O   1 
ATOM   11303 C  CB  . GLU D 2 141 ? 36.236  -63.300 2.328   1.00 18.75  ? 141 GLU D CB  1 
ATOM   11304 C  CG  . GLU D 2 141 ? 36.262  -62.850 3.775   1.00 22.11  ? 141 GLU D CG  1 
ATOM   11305 C  CD  . GLU D 2 141 ? 35.417  -63.719 4.729   1.00 26.05  ? 141 GLU D CD  1 
ATOM   11306 O  OE1 . GLU D 2 141 ? 34.714  -64.693 4.326   1.00 25.16  ? 141 GLU D OE1 1 
ATOM   11307 O  OE2 . GLU D 2 141 ? 35.546  -63.474 5.933   1.00 24.89  ? 141 GLU D OE2 1 
ATOM   11308 N  N   . VAL D 2 142 ? 37.468  -64.554 -0.256  1.00 21.08  ? 142 VAL D N   1 
ATOM   11309 C  CA  . VAL D 2 142 ? 37.294  -64.945 -1.655  1.00 19.82  ? 142 VAL D CA  1 
ATOM   11310 C  C   . VAL D 2 142 ? 37.665  -66.409 -1.861  1.00 20.37  ? 142 VAL D C   1 
ATOM   11311 O  O   . VAL D 2 142 ? 36.940  -67.163 -2.530  1.00 21.92  ? 142 VAL D O   1 
ATOM   11312 C  CB  . VAL D 2 142 ? 38.101  -63.994 -2.531  1.00 23.55  ? 142 VAL D CB  1 
ATOM   11313 C  CG1 . VAL D 2 142 ? 38.119  -64.440 -3.972  1.00 21.58  ? 142 VAL D CG1 1 
ATOM   11314 C  CG2 . VAL D 2 142 ? 37.457  -62.568 -2.416  1.00 22.81  ? 142 VAL D CG2 1 
ATOM   11315 N  N   . GLN D 2 143 ? 38.801  -66.837 -1.295  1.00 21.38  ? 143 GLN D N   1 
ATOM   11316 C  CA  . GLN D 2 143 ? 39.136  -68.266 -1.330  1.00 22.42  ? 143 GLN D CA  1 
ATOM   11317 C  C   . GLN D 2 143 ? 38.046  -69.124 -0.676  1.00 25.16  ? 143 GLN D C   1 
ATOM   11318 O  O   . GLN D 2 143 ? 37.722  -70.221 -1.183  1.00 22.62  ? 143 GLN D O   1 
ATOM   11319 C  CB  . GLN D 2 143 ? 40.509  -68.514 -0.669  1.00 21.51  ? 143 GLN D CB  1 
ATOM   11320 C  CG  . GLN D 2 143 ? 40.941  -70.001 -0.559  1.00 24.46  ? 143 GLN D CG  1 
ATOM   11321 C  CD  . GLN D 2 143 ? 41.086  -70.718 -1.886  1.00 26.02  ? 143 GLN D CD  1 
ATOM   11322 O  OE1 . GLN D 2 143 ? 41.103  -70.105 -2.954  1.00 24.46  ? 143 GLN D OE1 1 
ATOM   11323 N  NE2 . GLN D 2 143 ? 41.200  -72.049 -1.824  1.00 27.38  ? 143 GLN D NE2 1 
ATOM   11324 N  N   . ALA D 2 144 ? 37.515  -68.704 0.499   1.00 20.76  ? 144 ALA D N   1 
ATOM   11325 C  CA  . ALA D 2 144 ? 36.452  -69.487 1.138   1.00 21.90  ? 144 ALA D CA  1 
ATOM   11326 C  C   . ALA D 2 144 ? 35.235  -69.616 0.212   1.00 23.43  ? 144 ALA D C   1 
ATOM   11327 O  O   . ALA D 2 144 ? 34.610  -70.688 0.132   1.00 23.45  ? 144 ALA D O   1 
ATOM   11328 C  CB  . ALA D 2 144 ? 36.032  -68.850 2.497   1.00 22.57  ? 144 ALA D CB  1 
ATOM   11329 N  N   . PHE D 2 145 ? 34.879  -68.536 -0.489  1.00 21.56  ? 145 PHE D N   1 
ATOM   11330 C  CA  . PHE D 2 145 ? 33.739  -68.595 -1.407  1.00 21.35  ? 145 PHE D CA  1 
ATOM   11331 C  C   . PHE D 2 145 ? 34.055  -69.529 -2.575  1.00 23.81  ? 145 PHE D C   1 
ATOM   11332 O  O   . PHE D 2 145 ? 33.188  -70.281 -3.036  1.00 23.52  ? 145 PHE D O   1 
ATOM   11333 C  CB  . PHE D 2 145 ? 33.418  -67.175 -1.920  1.00 20.54  ? 145 PHE D CB  1 
ATOM   11334 C  CG  . PHE D 2 145 ? 32.033  -67.018 -2.561  1.00 22.80  ? 145 PHE D CG  1 
ATOM   11335 C  CD1 . PHE D 2 145 ? 31.047  -67.985 -2.456  1.00 24.50  ? 145 PHE D CD1 1 
ATOM   11336 C  CD2 . PHE D 2 145 ? 31.752  -65.851 -3.308  1.00 24.15  ? 145 PHE D CD2 1 
ATOM   11337 C  CE1 . PHE D 2 145 ? 29.764  -67.845 -3.060  1.00 24.08  ? 145 PHE D CE1 1 
ATOM   11338 C  CE2 . PHE D 2 145 ? 30.471  -65.679 -3.876  1.00 24.98  ? 145 PHE D CE2 1 
ATOM   11339 C  CZ  . PHE D 2 145 ? 29.486  -66.652 -3.771  1.00 26.67  ? 145 PHE D CZ  1 
ATOM   11340 N  N   . ARG D 2 146 ? 35.299  -69.494 -3.040  1.00 22.86  ? 146 ARG D N   1 
ATOM   11341 C  CA  . ARG D 2 146 ? 35.719  -70.379 -4.113  1.00 22.44  ? 146 ARG D CA  1 
ATOM   11342 C  C   . ARG D 2 146 ? 35.572  -71.833 -3.691  1.00 23.16  ? 146 ARG D C   1 
ATOM   11343 O  O   . ARG D 2 146 ? 35.059  -72.659 -4.463  1.00 25.30  ? 146 ARG D O   1 
ATOM   11344 C  CB  . ARG D 2 146 ? 37.168  -70.076 -4.481  1.00 26.32  ? 146 ARG D CB  1 
ATOM   11345 C  CG  . ARG D 2 146 ? 37.675  -71.055 -5.558  1.00 27.98  ? 146 ARG D CG  1 
ATOM   11346 C  CD  . ARG D 2 146 ? 39.065  -71.503 -5.170  1.00 30.83  ? 146 ARG D CD  1 
ATOM   11347 N  NE  . ARG D 2 146 ? 39.812  -72.092 -6.283  1.00 30.94  ? 146 ARG D NE  1 
ATOM   11348 C  CZ  . ARG D 2 146 ? 41.094  -71.802 -6.464  1.00 32.57  ? 146 ARG D CZ  1 
ATOM   11349 N  NH1 . ARG D 2 146 ? 41.720  -70.929 -5.674  1.00 27.89  ? 146 ARG D NH1 1 
ATOM   11350 N  NH2 . ARG D 2 146 ? 41.748  -72.337 -7.494  1.00 31.77  ? 146 ARG D NH2 1 
ATOM   11351 N  N   . VAL D 2 147 ? 35.966  -72.156 -2.444  1.00 22.55  ? 147 VAL D N   1 
ATOM   11352 C  CA  . VAL D 2 147 ? 35.836  -73.540 -1.955  1.00 26.36  ? 147 VAL D CA  1 
ATOM   11353 C  C   . VAL D 2 147 ? 34.362  -73.922 -1.840  1.00 25.87  ? 147 VAL D C   1 
ATOM   11354 O  O   . VAL D 2 147 ? 33.941  -75.037 -2.219  1.00 23.90  ? 147 VAL D O   1 
ATOM   11355 C  CB  . VAL D 2 147 ? 36.554  -73.638 -0.605  1.00 26.70  ? 147 VAL D CB  1 
ATOM   11356 C  CG1 . VAL D 2 147 ? 36.170  -74.902 0.176   1.00 29.50  ? 147 VAL D CG1 1 
ATOM   11357 C  CG2 . VAL D 2 147 ? 38.083  -73.548 -0.835  1.00 25.91  ? 147 VAL D CG2 1 
ATOM   11358 N  N   . PHE D 2 148 ? 33.549  -72.998 -1.307  1.00 23.96  ? 148 PHE D N   1 
ATOM   11359 C  CA  . PHE D 2 148 ? 32.106  -73.213 -1.290  1.00 23.77  ? 148 PHE D CA  1 
ATOM   11360 C  C   . PHE D 2 148 ? 31.587  -73.564 -2.684  1.00 20.91  ? 148 PHE D C   1 
ATOM   11361 O  O   . PHE D 2 148 ? 30.822  -74.514 -2.852  1.00 24.39  ? 148 PHE D O   1 
ATOM   11362 C  CB  . PHE D 2 148 ? 31.421  -71.943 -0.757  1.00 22.16  ? 148 PHE D CB  1 
ATOM   11363 C  CG  . PHE D 2 148 ? 29.887  -71.973 -0.888  1.00 22.89  ? 148 PHE D CG  1 
ATOM   11364 C  CD1 . PHE D 2 148 ? 29.269  -71.495 -2.038  1.00 24.47  ? 148 PHE D CD1 1 
ATOM   11365 C  CD2 . PHE D 2 148 ? 29.093  -72.447 0.153   1.00 21.27  ? 148 PHE D CD2 1 
ATOM   11366 C  CE1 . PHE D 2 148 ? 27.881  -71.503 -2.183  1.00 21.90  ? 148 PHE D CE1 1 
ATOM   11367 C  CE2 . PHE D 2 148 ? 27.704  -72.452 0.036   1.00 26.22  ? 148 PHE D CE2 1 
ATOM   11368 C  CZ  . PHE D 2 148 ? 27.094  -71.961 -1.135  1.00 22.15  ? 148 PHE D CZ  1 
ATOM   11369 N  N   . LEU D 2 149 ? 31.906  -72.749 -3.684  1.00 21.45  ? 149 LEU D N   1 
ATOM   11370 C  CA  . LEU D 2 149 ? 31.342  -72.960 -5.008  1.00 23.48  ? 149 LEU D CA  1 
ATOM   11371 C  C   . LEU D 2 149 ? 31.828  -74.263 -5.627  1.00 24.11  ? 149 LEU D C   1 
ATOM   11372 O  O   . LEU D 2 149 ? 31.051  -74.951 -6.294  1.00 26.34  ? 149 LEU D O   1 
ATOM   11373 C  CB  . LEU D 2 149 ? 31.696  -71.780 -5.907  1.00 23.71  ? 149 LEU D CB  1 
ATOM   11374 C  CG  . LEU D 2 149 ? 31.045  -70.473 -5.519  1.00 22.73  ? 149 LEU D CG  1 
ATOM   11375 C  CD1 . LEU D 2 149 ? 31.784  -69.304 -6.232  1.00 24.87  ? 149 LEU D CD1 1 
ATOM   11376 C  CD2 . LEU D 2 149 ? 29.545  -70.541 -5.929  1.00 24.91  ? 149 LEU D CD2 1 
ATOM   11377 N  N   . GLN D 2 150 ? 33.085  -74.595 -5.382  1.00 24.51  ? 150 GLN D N   1 
ATOM   11378 C  CA  . GLN D 2 150 ? 33.681  -75.858 -5.856  1.00 25.30  ? 150 GLN D CA  1 
ATOM   11379 C  C   . GLN D 2 150 ? 32.896  -77.025 -5.272  1.00 25.37  ? 150 GLN D C   1 
ATOM   11380 O  O   . GLN D 2 150 ? 32.640  -77.980 -5.976  1.00 27.99  ? 150 GLN D O   1 
ATOM   11381 C  CB  . GLN D 2 150 ? 35.053  -75.984 -5.219  1.00 31.11  ? 150 GLN D CB  1 
ATOM   11382 C  CG  . GLN D 2 150 ? 36.124  -76.285 -6.211  1.00 33.34  ? 150 GLN D CG  1 
ATOM   11383 C  CD  . GLN D 2 150 ? 37.474  -75.838 -5.740  1.00 33.74  ? 150 GLN D CD  1 
ATOM   11384 O  OE1 . GLN D 2 150 ? 38.190  -75.216 -6.484  1.00 38.80  ? 150 GLN D OE1 1 
ATOM   11385 N  NE2 . GLN D 2 150 ? 37.818  -76.177 -4.515  1.00 34.20  ? 150 GLN D NE2 1 
ATOM   11386 N  N   . THR D 2 151 ? 32.595  -76.948 -3.987  1.00 24.91  ? 151 THR D N   1 
ATOM   11387 C  CA  . THR D 2 151 ? 31.881  -78.012 -3.317  1.00 26.82  ? 151 THR D CA  1 
ATOM   11388 C  C   . THR D 2 151 ? 30.476  -78.098 -3.859  1.00 28.80  ? 151 THR D C   1 
ATOM   11389 O  O   . THR D 2 151 ? 29.968  -79.193 -4.117  1.00 27.39  ? 151 THR D O   1 
ATOM   11390 C  CB  . THR D 2 151 ? 31.853  -77.761 -1.808  1.00 27.57  ? 151 THR D CB  1 
ATOM   11391 O  OG1 . THR D 2 151 ? 33.192  -77.578 -1.334  1.00 28.11  ? 151 THR D OG1 1 
ATOM   11392 C  CG2 . THR D 2 151 ? 31.239  -78.938 -1.145  1.00 25.49  ? 151 THR D CG2 1 
ATOM   11393 N  N   . LEU D 2 152 ? 29.852  -76.929 -4.056  1.00 24.54  ? 152 LEU D N   1 
ATOM   11394 C  CA  . LEU D 2 152 ? 28.458  -76.869 -4.468  1.00 24.11  ? 152 LEU D CA  1 
ATOM   11395 C  C   . LEU D 2 152 ? 28.259  -77.506 -5.829  1.00 28.60  ? 152 LEU D C   1 
ATOM   11396 O  O   . LEU D 2 152 ? 27.316  -78.286 -6.031  1.00 29.61  ? 152 LEU D O   1 
ATOM   11397 C  CB  . LEU D 2 152 ? 28.031  -75.391 -4.499  1.00 27.12  ? 152 LEU D CB  1 
ATOM   11398 C  CG  . LEU D 2 152 ? 26.645  -75.081 -5.032  1.00 28.17  ? 152 LEU D CG  1 
ATOM   11399 C  CD1 . LEU D 2 152 ? 25.696  -75.436 -3.921  1.00 31.27  ? 152 LEU D CD1 1 
ATOM   11400 C  CD2 . LEU D 2 152 ? 26.562  -73.568 -5.255  1.00 27.80  ? 152 LEU D CD2 1 
ATOM   11401 N  N   . THR D 2 153 ? 29.116  -77.131 -6.806  1.00 27.21  ? 153 THR D N   1 
ATOM   11402 C  CA  . THR D 2 153 ? 28.996  -77.632 -8.167  1.00 30.74  ? 153 THR D CA  1 
ATOM   11403 C  C   . THR D 2 153 ? 29.620  -78.995 -8.346  1.00 30.84  ? 153 THR D C   1 
ATOM   11404 O  O   . THR D 2 153 ? 29.334  -79.658 -9.348  1.00 34.48  ? 153 THR D O   1 
ATOM   11405 C  CB  . THR D 2 153 ? 29.664  -76.674 -9.129  1.00 31.69  ? 153 THR D CB  1 
ATOM   11406 O  OG1 . THR D 2 153 ? 31.068  -76.644 -8.823  1.00 33.09  ? 153 THR D OG1 1 
ATOM   11407 C  CG2 . THR D 2 153 ? 29.068  -75.280 -8.944  1.00 26.30  ? 153 THR D CG2 1 
ATOM   11408 N  N   . GLY D 2 154 ? 30.483  -79.401 -7.415  1.00 29.94  ? 154 GLY D N   1 
ATOM   11409 C  CA  . GLY D 2 154 ? 31.249  -80.626 -7.523  1.00 33.18  ? 154 GLY D CA  1 
ATOM   11410 C  C   . GLY D 2 154 ? 32.328  -80.591 -8.587  1.00 35.45  ? 154 GLY D C   1 
ATOM   11411 O  O   . GLY D 2 154 ? 32.831  -81.641 -8.978  1.00 36.06  ? 154 GLY D O   1 
ATOM   11412 N  N   . LYS D 2 155 ? 32.678  -79.427 -9.098  1.00 32.85  ? 155 LYS D N   1 
ATOM   11413 C  CA  . LYS D 2 155 ? 33.704  -79.295 -10.131 1.00 34.92  ? 155 LYS D CA  1 
ATOM   11414 C  C   . LYS D 2 155 ? 34.812  -78.384 -9.608  1.00 31.19  ? 155 LYS D C   1 
ATOM   11415 O  O   . LYS D 2 155 ? 34.526  -77.317 -9.055  1.00 31.96  ? 155 LYS D O   1 
ATOM   11416 C  CB  . LYS D 2 155 ? 33.110  -78.719 -11.433 1.00 37.39  ? 155 LYS D CB  1 
ATOM   11417 C  CG  . LYS D 2 155 ? 32.200  -79.672 -12.221 1.00 45.78  ? 155 LYS D CG  1 
ATOM   11418 C  CD  . LYS D 2 155 ? 30.816  -79.065 -12.530 1.00 50.02  ? 155 LYS D CD  1 
ATOM   11419 C  CE  . LYS D 2 155 ? 30.089  -79.843 -13.654 1.00 51.07  ? 155 LYS D CE  1 
ATOM   11420 N  NZ  . LYS D 2 155 ? 29.447  -78.873 -14.604 1.00 59.43  ? 155 LYS D NZ  1 
ATOM   11421 N  N   . GLU D 2 156 ? 36.069  -78.827 -9.731  1.00 30.50  ? 156 GLU D N   1 
ATOM   11422 C  CA  . GLU D 2 156 ? 37.207  -78.015 -9.312  1.00 30.31  ? 156 GLU D CA  1 
ATOM   11423 C  C   . GLU D 2 156 ? 37.216  -76.664 -10.039 1.00 28.82  ? 156 GLU D C   1 
ATOM   11424 O  O   . GLU D 2 156 ? 37.136  -76.607 -11.268 1.00 29.97  ? 156 GLU D O   1 
ATOM   11425 C  CB  . GLU D 2 156 ? 38.506  -78.765 -9.604  1.00 34.00  ? 156 GLU D CB  1 
ATOM   11426 C  CG  . GLU D 2 156 ? 39.751  -78.040 -9.049  1.00 34.13  ? 156 GLU D CG  1 
ATOM   11427 C  CD  . GLU D 2 156 ? 41.070  -78.633 -9.537  1.00 42.38  ? 156 GLU D CD  1 
ATOM   11428 O  OE1 . GLU D 2 156 ? 41.064  -79.453 -10.493 1.00 46.26  ? 156 GLU D OE1 1 
ATOM   11429 O  OE2 . GLU D 2 156 ? 42.133  -78.231 -9.005  1.00 42.98  ? 156 GLU D OE2 1 
ATOM   11430 N  N   . ILE D 2 157 ? 37.343  -75.574 -9.301  1.00 30.81  ? 157 ILE D N   1 
ATOM   11431 C  CA  . ILE D 2 157 ? 37.489  -74.251 -9.920  1.00 30.45  ? 157 ILE D CA  1 
ATOM   11432 C  C   . ILE D 2 157 ? 38.979  -73.929 -9.887  1.00 28.15  ? 157 ILE D C   1 
ATOM   11433 O  O   . ILE D 2 157 ? 39.505  -73.557 -8.839  1.00 30.43  ? 157 ILE D O   1 
ATOM   11434 C  CB  . ILE D 2 157 ? 36.661  -73.194 -9.186  1.00 29.83  ? 157 ILE D CB  1 
ATOM   11435 C  CG1 . ILE D 2 157 ? 35.159  -73.539 -9.288  1.00 30.57  ? 157 ILE D CG1 1 
ATOM   11436 C  CG2 . ILE D 2 157 ? 36.939  -71.759 -9.755  1.00 27.12  ? 157 ILE D CG2 1 
ATOM   11437 C  CD1 . ILE D 2 157 ? 34.300  -72.714 -8.342  1.00 29.61  ? 157 ILE D CD1 1 
ATOM   11438 N  N   . THR D 2 158 ? 39.681  -74.140 -11.001 1.00 26.95  ? 158 THR D N   1 
ATOM   11439 C  CA  . THR D 2 158 ? 41.143  -74.051 -11.037 1.00 28.22  ? 158 THR D CA  1 
ATOM   11440 C  C   . THR D 2 158 ? 41.583  -72.591 -11.126 1.00 27.68  ? 158 THR D C   1 
ATOM   11441 O  O   . THR D 2 158 ? 40.798  -71.721 -11.480 1.00 26.17  ? 158 THR D O   1 
ATOM   11442 C  CB  . THR D 2 158 ? 41.699  -74.758 -12.268 1.00 28.10  ? 158 THR D CB  1 
ATOM   11443 O  OG1 . THR D 2 158 ? 41.217  -74.062 -13.434 1.00 29.14  ? 158 THR D OG1 1 
ATOM   11444 C  CG2 . THR D 2 158 ? 41.237  -76.232 -12.325 1.00 28.12  ? 158 THR D CG2 1 
ATOM   11445 N  N   . ASP D 2 159 ? 42.873  -72.344 -10.882 1.00 24.81  ? 159 ASP D N   1 
ATOM   11446 C  CA  . ASP D 2 159 ? 43.409  -70.986 -11.043 1.00 28.49  ? 159 ASP D CA  1 
ATOM   11447 C  C   . ASP D 2 159 ? 43.230  -70.495 -12.481 1.00 30.68  ? 159 ASP D C   1 
ATOM   11448 O  O   . ASP D 2 159 ? 42.938  -69.307 -12.710 1.00 28.94  ? 159 ASP D O   1 
ATOM   11449 C  CB  . ASP D 2 159 ? 44.903  -70.981 -10.678 1.00 30.76  ? 159 ASP D CB  1 
ATOM   11450 C  CG  . ASP D 2 159 ? 45.163  -71.057 -9.174  1.00 37.09  ? 159 ASP D CG  1 
ATOM   11451 O  OD1 . ASP D 2 159 ? 44.207  -71.092 -8.375  1.00 38.74  ? 159 ASP D OD1 1 
ATOM   11452 O  OD2 . ASP D 2 159 ? 46.359  -71.156 -8.810  1.00 42.27  ? 159 ASP D OD2 1 
ATOM   11453 N  N   . ALA D 2 160 ? 43.409  -71.403 -13.464 1.00 28.30  ? 160 ALA D N   1 
ATOM   11454 C  CA  . ALA D 2 160 ? 43.204  -71.028 -14.865 1.00 29.44  ? 160 ALA D CA  1 
ATOM   11455 C  C   . ALA D 2 160 ? 41.772  -70.580 -15.104 1.00 28.82  ? 160 ALA D C   1 
ATOM   11456 O  O   . ALA D 2 160 ? 41.522  -69.620 -15.835 1.00 29.04  ? 160 ALA D O   1 
ATOM   11457 C  CB  . ALA D 2 160 ? 43.551  -72.187 -15.794 1.00 31.96  ? 160 ALA D CB  1 
ATOM   11458 N  N   . MET D 2 161 ? 40.827  -71.256 -14.483 1.00 28.23  ? 161 MET D N   1 
ATOM   11459 C  CA  . MET D 2 161 ? 39.437  -70.906 -14.644 1.00 27.15  ? 161 MET D CA  1 
ATOM   11460 C  C   . MET D 2 161 ? 39.184  -69.536 -14.020 1.00 28.60  ? 161 MET D C   1 
ATOM   11461 O  O   . MET D 2 161 ? 38.448  -68.712 -14.570 1.00 27.61  ? 161 MET D O   1 
ATOM   11462 C  CB  . MET D 2 161 ? 38.612  -71.983 -13.953 1.00 30.12  ? 161 MET D CB  1 
ATOM   11463 C  CG  . MET D 2 161 ? 38.089  -73.088 -14.927 1.00 27.80  ? 161 MET D CG  1 
ATOM   11464 S  SD  . MET D 2 161 ? 37.865  -74.611 -13.883 1.00 31.41  ? 161 MET D SD  1 
ATOM   11465 C  CE  . MET D 2 161 ? 36.126  -74.311 -13.604 1.00 30.36  ? 161 MET D CE  1 
ATOM   11466 N  N   . LEU D 2 162 ? 39.777  -69.291 -12.853 1.00 23.51  ? 162 LEU D N   1 
ATOM   11467 C  CA  . LEU D 2 162 ? 39.613  -67.979 -12.214 1.00 24.72  ? 162 LEU D CA  1 
ATOM   11468 C  C   . LEU D 2 162 ? 40.277  -66.879 -13.043 1.00 26.82  ? 162 LEU D C   1 
ATOM   11469 O  O   . LEU D 2 162 ? 39.732  -65.772 -13.172 1.00 23.70  ? 162 LEU D O   1 
ATOM   11470 C  CB  . LEU D 2 162 ? 40.195  -68.039 -10.807 1.00 26.42  ? 162 LEU D CB  1 
ATOM   11471 C  CG  . LEU D 2 162 ? 39.288  -68.844 -9.873  1.00 25.81  ? 162 LEU D CG  1 
ATOM   11472 C  CD1 . LEU D 2 162 ? 40.122  -69.249 -8.669  1.00 27.60  ? 162 LEU D CD1 1 
ATOM   11473 C  CD2 . LEU D 2 162 ? 38.079  -68.027 -9.425  1.00 26.63  ? 162 LEU D CD2 1 
ATOM   11474 N  N   . SER D 2 163 ? 41.442  -67.162 -13.608 1.00 24.79  ? 163 SER D N   1 
ATOM   11475 C  CA  . SER D 2 163 ? 42.125  -66.136 -14.411 1.00 27.81  ? 163 SER D CA  1 
ATOM   11476 C  C   . SER D 2 163 ? 41.343  -65.784 -15.658 1.00 27.14  ? 163 SER D C   1 
ATOM   11477 O  O   . SER D 2 163 ? 41.288  -64.605 -16.047 1.00 27.26  ? 163 SER D O   1 
ATOM   11478 C  CB  . SER D 2 163 ? 43.524  -66.597 -14.803 1.00 31.41  ? 163 SER D CB  1 
ATOM   11479 O  OG  . SER D 2 163 ? 44.351  -66.443 -13.662 1.00 35.30  ? 163 SER D OG  1 
ATOM   11480 N  N   . ASP D 2 164 ? 40.803  -66.794 -16.348 1.00 27.07  ? 164 ASP D N   1 
ATOM   11481 C  CA  . ASP D 2 164 ? 39.953  -66.538 -17.512 1.00 28.61  ? 164 ASP D CA  1 
ATOM   11482 C  C   . ASP D 2 164 ? 38.726  -65.692 -17.131 1.00 29.69  ? 164 ASP D C   1 
ATOM   11483 O  O   . ASP D 2 164 ? 38.389  -64.716 -17.825 1.00 28.69  ? 164 ASP D O   1 
ATOM   11484 C  CB  . ASP D 2 164 ? 39.553  -67.874 -18.175 1.00 30.15  ? 164 ASP D CB  1 
ATOM   11485 C  CG  . ASP D 2 164 ? 40.776  -68.767 -18.539 1.00 41.51  ? 164 ASP D CG  1 
ATOM   11486 O  OD1 . ASP D 2 164 ? 41.935  -68.279 -18.529 1.00 47.57  ? 164 ASP D OD1 1 
ATOM   11487 O  OD2 . ASP D 2 164 ? 40.579  -69.987 -18.852 1.00 45.87  ? 164 ASP D OD2 1 
ATOM   11488 N  N   . ALA D 2 165 ? 38.076  -66.009 -16.007 1.00 25.93  ? 165 ALA D N   1 
ATOM   11489 C  CA  . ALA D 2 165 ? 36.942  -65.205 -15.569 1.00 28.23  ? 165 ALA D CA  1 
ATOM   11490 C  C   . ALA D 2 165 ? 37.380  -63.775 -15.223 1.00 22.84  ? 165 ALA D C   1 
ATOM   11491 O  O   . ALA D 2 165 ? 36.699  -62.788 -15.562 1.00 25.27  ? 165 ALA D O   1 
ATOM   11492 C  CB  . ALA D 2 165 ? 36.278  -65.871 -14.361 1.00 25.75  ? 165 ALA D CB  1 
ATOM   11493 N  N   . LEU D 2 166 ? 38.518  -63.636 -14.556 1.00 22.20  ? 166 LEU D N   1 
ATOM   11494 C  CA  . LEU D 2 166 ? 38.961  -62.273 -14.247 1.00 23.67  ? 166 LEU D CA  1 
ATOM   11495 C  C   . LEU D 2 166 ? 39.271  -61.519 -15.534 1.00 25.63  ? 166 LEU D C   1 
ATOM   11496 O  O   . LEU D 2 166 ? 39.021  -60.303 -15.621 1.00 24.12  ? 166 LEU D O   1 
ATOM   11497 C  CB  . LEU D 2 166 ? 40.189  -62.319 -13.327 1.00 23.84  ? 166 LEU D CB  1 
ATOM   11498 C  CG  . LEU D 2 166 ? 40.885  -61.010 -12.917 1.00 26.56  ? 166 LEU D CG  1 
ATOM   11499 C  CD1 . LEU D 2 166 ? 39.873  -60.120 -12.207 1.00 24.68  ? 166 LEU D CD1 1 
ATOM   11500 C  CD2 . LEU D 2 166 ? 42.026  -61.291 -11.963 1.00 23.63  ? 166 LEU D CD2 1 
ATOM   11501 N  N   . ALA D 2 167 ? 39.828  -62.207 -16.550 1.00 25.06  ? 167 ALA D N   1 
ATOM   11502 C  CA  . ALA D 2 167 ? 40.183  -61.547 -17.802 1.00 26.56  ? 167 ALA D CA  1 
ATOM   11503 C  C   . ALA D 2 167 ? 38.932  -61.040 -18.496 1.00 27.29  ? 167 ALA D C   1 
ATOM   11504 O  O   . ALA D 2 167 ? 38.909  -59.924 -19.015 1.00 28.30  ? 167 ALA D O   1 
ATOM   11505 C  CB  . ALA D 2 167 ? 40.979  -62.505 -18.704 1.00 26.06  ? 167 ALA D CB  1 
ATOM   11506 N  N   . VAL D 2 168 ? 37.848  -61.803 -18.427 1.00 25.30  ? 168 VAL D N   1 
ATOM   11507 C  CA  . VAL D 2 168 ? 36.602  -61.335 -19.006 1.00 28.19  ? 168 VAL D CA  1 
ATOM   11508 C  C   . VAL D 2 168 ? 36.075  -60.121 -18.244 1.00 27.13  ? 168 VAL D C   1 
ATOM   11509 O  O   . VAL D 2 168 ? 35.656  -59.129 -18.852 1.00 27.33  ? 168 VAL D O   1 
ATOM   11510 C  CB  . VAL D 2 168 ? 35.590  -62.488 -19.028 1.00 34.32  ? 168 VAL D CB  1 
ATOM   11511 C  CG1 . VAL D 2 168 ? 34.225  -61.950 -19.307 1.00 37.91  ? 168 VAL D CG1 1 
ATOM   11512 C  CG2 . VAL D 2 168 ? 36.036  -63.567 -20.069 1.00 31.39  ? 168 VAL D CG2 1 
ATOM   11513 N  N   . CYS D 2 169 ? 36.049  -60.186 -16.914 1.00 23.66  ? 169 CYS D N   1 
ATOM   11514 C  CA  . CYS D 2 169 ? 35.581  -59.049 -16.104 1.00 25.71  ? 169 CYS D CA  1 
ATOM   11515 C  C   . CYS D 2 169 ? 36.467  -57.816 -16.289 1.00 26.17  ? 169 CYS D C   1 
ATOM   11516 O  O   . CYS D 2 169 ? 35.966  -56.696 -16.431 1.00 25.81  ? 169 CYS D O   1 
ATOM   11517 C  CB  . CYS D 2 169 ? 35.549  -59.461 -14.641 1.00 25.71  ? 169 CYS D CB  1 
ATOM   11518 S  SG  . CYS D 2 169 ? 34.238  -60.648 -14.359 1.00 27.11  ? 169 CYS D SG  1 
ATOM   11519 N  N   . ASP D 2 170 ? 37.786  -57.990 -16.279 1.00 23.09  ? 170 ASP D N   1 
ATOM   11520 C  CA  . ASP D 2 170 ? 38.656  -56.842 -16.521 1.00 27.68  ? 170 ASP D CA  1 
ATOM   11521 C  C   . ASP D 2 170 ? 38.461  -56.245 -17.917 1.00 28.30  ? 170 ASP D C   1 
ATOM   11522 O  O   . ASP D 2 170 ? 38.503  -55.020 -18.079 1.00 28.00  ? 170 ASP D O   1 
ATOM   11523 C  CB  . ASP D 2 170 ? 40.122  -57.248 -16.318 1.00 27.37  ? 170 ASP D CB  1 
ATOM   11524 C  CG  . ASP D 2 170 ? 40.520  -57.271 -14.859 1.00 28.42  ? 170 ASP D CG  1 
ATOM   11525 O  OD1 . ASP D 2 170 ? 39.830  -56.670 -14.008 1.00 24.80  ? 170 ASP D OD1 1 
ATOM   11526 O  OD2 . ASP D 2 170 ? 41.539  -57.909 -14.570 1.00 29.24  ? 170 ASP D OD2 1 
ATOM   11527 N  N   . GLU D 2 171 ? 38.279  -57.079 -18.948 1.00 24.61  ? 171 GLU D N   1 
ATOM   11528 C  CA  . GLU D 2 171 ? 38.021  -56.523 -20.284 1.00 26.88  ? 171 GLU D CA  1 
ATOM   11529 C  C   . GLU D 2 171 ? 36.748  -55.685 -20.268 1.00 29.05  ? 171 GLU D C   1 
ATOM   11530 O  O   . GLU D 2 171 ? 36.707  -54.600 -20.868 1.00 27.57  ? 171 GLU D O   1 
ATOM   11531 C  CB  . GLU D 2 171 ? 37.917  -57.644 -21.344 1.00 28.72  ? 171 GLU D CB  1 
ATOM   11532 C  CG  . GLU D 2 171 ? 37.750  -57.084 -22.746 1.00 27.21  ? 171 GLU D CG  1 
ATOM   11533 C  CD  . GLU D 2 171 ? 37.576  -58.148 -23.842 1.00 39.29  ? 171 GLU D CD  1 
ATOM   11534 O  OE1 . GLU D 2 171 ? 37.507  -59.369 -23.553 1.00 44.06  ? 171 GLU D OE1 1 
ATOM   11535 O  OE2 . GLU D 2 171 ? 37.538  -57.731 -25.012 1.00 48.60  ? 171 GLU D OE2 1 
ATOM   11536 N  N   . ASN D 2 172 ? 35.713  -56.158 -19.548 1.00 26.62  ? 172 ASN D N   1 
ATOM   11537 C  CA  . ASN D 2 172 ? 34.460  -55.411 -19.459 1.00 26.24  ? 172 ASN D CA  1 
ATOM   11538 C  C   . ASN D 2 172 ? 34.703  -54.086 -18.760 1.00 27.23  ? 172 ASN D C   1 
ATOM   11539 O  O   . ASN D 2 172 ? 34.250  -53.026 -19.232 1.00 28.16  ? 172 ASN D O   1 
ATOM   11540 C  CB  . ASN D 2 172 ? 33.400  -56.250 -18.716 1.00 27.85  ? 172 ASN D CB  1 
ATOM   11541 C  CG  . ASN D 2 172 ? 31.991  -55.672 -18.825 1.00 27.84  ? 172 ASN D CG  1 
ATOM   11542 O  OD1 . ASN D 2 172 ? 31.451  -55.129 -17.852 1.00 30.44  ? 172 ASN D OD1 1 
ATOM   11543 N  ND2 . ASN D 2 172 ? 31.381  -55.809 -19.989 1.00 28.75  ? 172 ASN D ND2 1 
ATOM   11544 N  N   . ARG D 2 173 ? 35.455  -54.127 -17.652 1.00 22.47  ? 173 ARG D N   1 
ATOM   11545 C  CA  . ARG D 2 173 ? 35.783  -52.894 -16.934 1.00 25.06  ? 173 ARG D CA  1 
ATOM   11546 C  C   . ARG D 2 173 ? 36.573  -51.941 -17.839 1.00 25.73  ? 173 ARG D C   1 
ATOM   11547 O  O   . ARG D 2 173 ? 36.309  -50.726 -17.869 1.00 24.06  ? 173 ARG D O   1 
ATOM   11548 C  CB  . ARG D 2 173 ? 36.558  -53.221 -15.659 1.00 26.81  ? 173 ARG D CB  1 
ATOM   11549 C  CG  . ARG D 2 173 ? 35.727  -53.982 -14.669 1.00 25.16  ? 173 ARG D CG  1 
ATOM   11550 C  CD  . ARG D 2 173 ? 36.586  -54.690 -13.620 1.00 25.33  ? 173 ARG D CD  1 
ATOM   11551 N  NE  . ARG D 2 173 ? 35.751  -55.444 -12.698 1.00 22.39  ? 173 ARG D NE  1 
ATOM   11552 C  CZ  . ARG D 2 173 ? 36.170  -56.533 -12.072 1.00 24.78  ? 173 ARG D CZ  1 
ATOM   11553 N  NH1 . ARG D 2 173 ? 37.420  -56.973 -12.240 1.00 24.64  ? 173 ARG D NH1 1 
ATOM   11554 N  NH2 . ARG D 2 173 ? 35.339  -57.176 -11.229 1.00 25.02  ? 173 ARG D NH2 1 
ATOM   11555 N  N   . ARG D 2 174 ? 37.508  -52.489 -18.625 1.00 26.95  ? 174 ARG D N   1 
ATOM   11556 C  CA  . ARG D 2 174 ? 38.325  -51.611 -19.463 1.00 27.72  ? 174 ARG D CA  1 
ATOM   11557 C  C   . ARG D 2 174 ? 37.505  -51.041 -20.598 1.00 28.69  ? 174 ARG D C   1 
ATOM   11558 O  O   . ARG D 2 174 ? 37.621  -49.842 -20.906 1.00 26.41  ? 174 ARG D O   1 
ATOM   11559 C  CB  . ARG D 2 174 ? 39.558  -52.350 -19.964 1.00 30.62  ? 174 ARG D CB  1 
ATOM   11560 C  CG  . ARG D 2 174 ? 40.520  -52.626 -18.856 1.00 33.56  ? 174 ARG D CG  1 
ATOM   11561 C  CD  . ARG D 2 174 ? 41.768  -53.237 -19.404 1.00 37.82  ? 174 ARG D CD  1 
ATOM   11562 N  NE  . ARG D 2 174 ? 42.686  -53.523 -18.315 1.00 41.98  ? 174 ARG D NE  1 
ATOM   11563 C  CZ  . ARG D 2 174 ? 43.031  -54.725 -17.877 1.00 38.59  ? 174 ARG D CZ  1 
ATOM   11564 N  NH1 . ARG D 2 174 ? 42.579  -55.834 -18.447 1.00 34.91  ? 174 ARG D NH1 1 
ATOM   11565 N  NH2 . ARG D 2 174 ? 43.879  -54.810 -16.854 1.00 43.23  ? 174 ARG D NH2 1 
ATOM   11566 N  N   . LEU D 2 175 ? 36.636  -51.869 -21.212 1.00 27.97  ? 175 LEU D N   1 
ATOM   11567 C  CA  . LEU D 2 175 ? 35.798  -51.361 -22.298 1.00 25.03  ? 175 LEU D CA  1 
ATOM   11568 C  C   . LEU D 2 175 ? 34.812  -50.309 -21.791 1.00 26.45  ? 175 LEU D C   1 
ATOM   11569 O  O   . LEU D 2 175 ? 34.556  -49.316 -22.493 1.00 28.07  ? 175 LEU D O   1 
ATOM   11570 C  CB  . LEU D 2 175 ? 35.047  -52.503 -22.972 1.00 28.86  ? 175 LEU D CB  1 
ATOM   11571 C  CG  . LEU D 2 175 ? 35.957  -53.457 -23.720 1.00 28.03  ? 175 LEU D CG  1 
ATOM   11572 C  CD1 . LEU D 2 175 ? 35.174  -54.779 -24.051 1.00 27.75  ? 175 LEU D CD1 1 
ATOM   11573 C  CD2 . LEU D 2 175 ? 36.548  -52.836 -25.017 1.00 27.09  ? 175 LEU D CD2 1 
ATOM   11574 N  N   . LEU D 2 176 ? 34.243  -50.498 -20.580 1.00 25.43  ? 176 LEU D N   1 
ATOM   11575 C  CA  . LEU D 2 176 ? 33.338  -49.482 -20.045 1.00 28.89  ? 176 LEU D CA  1 
ATOM   11576 C  C   . LEU D 2 176 ? 34.074  -48.186 -19.782 1.00 28.95  ? 176 LEU D C   1 
ATOM   11577 O  O   . LEU D 2 176 ? 33.537  -47.097 -20.050 1.00 28.66  ? 176 LEU D O   1 
ATOM   11578 C  CB  . LEU D 2 176 ? 32.664  -49.963 -18.757 1.00 26.93  ? 176 LEU D CB  1 
ATOM   11579 C  CG  . LEU D 2 176 ? 31.582  -50.996 -18.996 1.00 25.56  ? 176 LEU D CG  1 
ATOM   11580 C  CD1 . LEU D 2 176 ? 31.149  -51.628 -17.674 1.00 24.02  ? 176 LEU D CD1 1 
ATOM   11581 C  CD2 . LEU D 2 176 ? 30.389  -50.364 -19.733 1.00 25.95  ? 176 LEU D CD2 1 
ATOM   11582 N  N   . ARG D 2 177 ? 35.316  -48.269 -19.269 1.00 26.06  ? 177 ARG D N   1 
ATOM   11583 C  CA  . ARG D 2 177 ? 36.103  -47.038 -19.126 1.00 27.33  ? 177 ARG D CA  1 
ATOM   11584 C  C   . ARG D 2 177 ? 36.346  -46.379 -20.483 1.00 27.64  ? 177 ARG D C   1 
ATOM   11585 O  O   . ARG D 2 177 ? 36.320  -45.143 -20.611 1.00 29.98  ? 177 ARG D O   1 
ATOM   11586 C  CB  . ARG D 2 177 ? 37.464  -47.316 -18.458 1.00 30.46  ? 177 ARG D CB  1 
ATOM   11587 C  CG  . ARG D 2 177 ? 37.456  -47.536 -16.926 1.00 31.66  ? 177 ARG D CG  1 
ATOM   11588 C  CD  . ARG D 2 177 ? 37.026  -46.256 -16.153 1.00 27.36  ? 177 ARG D CD  1 
ATOM   11589 N  NE  . ARG D 2 177 ? 37.981  -45.138 -16.146 1.00 33.07  ? 177 ARG D NE  1 
ATOM   11590 C  CZ  . ARG D 2 177 ? 38.958  -45.016 -15.255 1.00 31.88  ? 177 ARG D CZ  1 
ATOM   11591 N  NH1 . ARG D 2 177 ? 39.222  -45.978 -14.383 1.00 31.73  ? 177 ARG D NH1 1 
ATOM   11592 N  NH2 . ARG D 2 177 ? 39.688  -43.906 -15.238 1.00 36.20  ? 177 ARG D NH2 1 
ATOM   11593 N  N   . GLU D 2 178 ? 36.658  -47.171 -21.504 1.00 26.07  ? 178 GLU D N   1 
ATOM   11594 C  CA  . GLU D 2 178 ? 36.922  -46.625 -22.826 1.00 27.58  ? 178 GLU D CA  1 
ATOM   11595 C  C   . GLU D 2 178 ? 35.667  -45.983 -23.403 1.00 26.74  ? 178 GLU D C   1 
ATOM   11596 O  O   . GLU D 2 178 ? 35.729  -44.905 -24.016 1.00 31.81  ? 178 GLU D O   1 
ATOM   11597 C  CB  . GLU D 2 178 ? 37.425  -47.758 -23.721 1.00 32.82  ? 178 GLU D CB  1 
ATOM   11598 C  CG  . GLU D 2 178 ? 37.512  -47.405 -25.169 1.00 39.07  ? 178 GLU D CG  1 
ATOM   11599 C  CD  . GLU D 2 178 ? 38.467  -48.333 -25.934 1.00 38.48  ? 178 GLU D CD  1 
ATOM   11600 O  OE1 . GLU D 2 178 ? 38.774  -49.460 -25.425 1.00 37.77  ? 178 GLU D OE1 1 
ATOM   11601 O  OE2 . GLU D 2 178 ? 38.838  -47.946 -27.068 1.00 45.65  ? 178 GLU D OE2 1 
ATOM   11602 N  N   . LEU D 2 179 ? 34.510  -46.591 -23.145 1.00 30.48  ? 179 LEU D N   1 
ATOM   11603 C  CA  . LEU D 2 179 ? 33.257  -45.963 -23.520 1.00 26.39  ? 179 LEU D CA  1 
ATOM   11604 C  C   . LEU D 2 179 ? 33.079  -44.646 -22.750 1.00 27.50  ? 179 LEU D C   1 
ATOM   11605 O  O   . LEU D 2 179 ? 32.694  -43.635 -23.347 1.00 31.03  ? 179 LEU D O   1 
ATOM   11606 C  CB  . LEU D 2 179 ? 32.097  -46.912 -23.224 1.00 28.25  ? 179 LEU D CB  1 
ATOM   11607 C  CG  . LEU D 2 179 ? 30.680  -46.445 -23.617 1.00 35.10  ? 179 LEU D CG  1 
ATOM   11608 C  CD1 . LEU D 2 179 ? 30.416  -46.638 -25.142 1.00 33.87  ? 179 LEU D CD1 1 
ATOM   11609 C  CD2 . LEU D 2 179 ? 29.593  -47.186 -22.872 1.00 31.01  ? 179 LEU D CD2 1 
ATOM   11610 N  N   . TYR D 2 180 ? 33.434  -44.617 -21.459 1.00 28.49  ? 180 TYR D N   1 
ATOM   11611 C  CA  . TYR D 2 180 ? 33.255  -43.371 -20.692 1.00 26.60  ? 180 TYR D CA  1 
ATOM   11612 C  C   . TYR D 2 180 ? 34.160  -42.262 -21.216 1.00 29.71  ? 180 TYR D C   1 
ATOM   11613 O  O   . TYR D 2 180 ? 33.835  -41.082 -21.059 1.00 31.12  ? 180 TYR D O   1 
ATOM   11614 C  CB  . TYR D 2 180 ? 33.555  -43.563 -19.212 1.00 28.91  ? 180 TYR D CB  1 
ATOM   11615 C  CG  . TYR D 2 180 ? 32.348  -43.897 -18.356 1.00 29.70  ? 180 TYR D CG  1 
ATOM   11616 C  CD1 . TYR D 2 180 ? 31.379  -44.822 -18.788 1.00 28.22  ? 180 TYR D CD1 1 
ATOM   11617 C  CD2 . TYR D 2 180 ? 32.200  -43.329 -17.100 1.00 26.09  ? 180 TYR D CD2 1 
ATOM   11618 C  CE1 . TYR D 2 180 ? 30.261  -45.138 -17.997 1.00 30.54  ? 180 TYR D CE1 1 
ATOM   11619 C  CE2 . TYR D 2 180 ? 31.093  -43.653 -16.287 1.00 29.57  ? 180 TYR D CE2 1 
ATOM   11620 C  CZ  . TYR D 2 180 ? 30.112  -44.537 -16.755 1.00 30.78  ? 180 TYR D CZ  1 
ATOM   11621 O  OH  . TYR D 2 180 ? 29.003  -44.827 -15.944 1.00 29.53  ? 180 TYR D OH  1 
ATOM   11622 N  N   . GLU D 2 181 ? 35.309  -42.599 -21.782 1.00 32.36  ? 181 GLU D N   1 
ATOM   11623 C  CA  . GLU D 2 181 ? 36.216  -41.553 -22.260 1.00 33.07  ? 181 GLU D CA  1 
ATOM   11624 C  C   . GLU D 2 181 ? 35.541  -40.651 -23.302 1.00 33.06  ? 181 GLU D C   1 
ATOM   11625 O  O   . GLU D 2 181 ? 35.891  -39.467 -23.407 1.00 33.26  ? 181 GLU D O   1 
ATOM   11626 C  CB  . GLU D 2 181 ? 37.507  -42.192 -22.812 1.00 34.92  ? 181 GLU D CB  1 
ATOM   11627 C  CG  . GLU D 2 181 ? 38.711  -41.256 -22.879 1.00 43.41  ? 181 GLU D CG  1 
ATOM   11628 C  CD  . GLU D 2 181 ? 39.423  -41.082 -21.517 1.00 42.63  ? 181 GLU D CD  1 
ATOM   11629 O  OE1 . GLU D 2 181 ? 39.032  -41.730 -20.507 1.00 45.79  ? 181 GLU D OE1 1 
ATOM   11630 O  OE2 . GLU D 2 181 ? 40.357  -40.258 -21.459 1.00 50.93  ? 181 GLU D OE2 1 
ATOM   11631 N  N   . TYR D 2 182 ? 34.523  -41.156 -24.034 1.00 31.18  ? 182 TYR D N   1 
ATOM   11632 C  CA  . TYR D 2 182 ? 33.876  -40.332 -25.071 1.00 31.94  ? 182 TYR D CA  1 
ATOM   11633 C  C   . TYR D 2 182 ? 33.009  -39.228 -24.465 1.00 31.55  ? 182 TYR D C   1 
ATOM   11634 O  O   . TYR D 2 182 ? 32.777  -38.195 -25.115 1.00 32.72  ? 182 TYR D O   1 
ATOM   11635 C  CB  . TYR D 2 182 ? 33.018  -41.193 -25.983 1.00 32.44  ? 182 TYR D CB  1 
ATOM   11636 C  CG  . TYR D 2 182 ? 33.801  -41.900 -27.065 1.00 32.12  ? 182 TYR D CG  1 
ATOM   11637 C  CD1 . TYR D 2 182 ? 34.359  -43.151 -26.829 1.00 36.09  ? 182 TYR D CD1 1 
ATOM   11638 C  CD2 . TYR D 2 182 ? 34.012  -41.307 -28.325 1.00 33.62  ? 182 TYR D CD2 1 
ATOM   11639 C  CE1 . TYR D 2 182 ? 35.078  -43.814 -27.804 1.00 38.85  ? 182 TYR D CE1 1 
ATOM   11640 C  CE2 . TYR D 2 182 ? 34.708  -41.966 -29.287 1.00 36.84  ? 182 TYR D CE2 1 
ATOM   11641 C  CZ  . TYR D 2 182 ? 35.236  -43.211 -29.038 1.00 37.29  ? 182 TYR D CZ  1 
ATOM   11642 O  OH  . TYR D 2 182 ? 35.933  -43.797 -30.088 1.00 43.81  ? 182 TYR D OH  1 
ATOM   11643 N  N   . ARG D 2 183 ? 32.585  -39.386 -23.210 1.00 32.30  ? 183 ARG D N   1 
ATOM   11644 C  CA  . ARG D 2 183 ? 31.750  -38.378 -22.565 1.00 30.67  ? 183 ARG D CA  1 
ATOM   11645 C  C   . ARG D 2 183 ? 32.533  -37.120 -22.210 1.00 32.25  ? 183 ARG D C   1 
ATOM   11646 O  O   . ARG D 2 183 ? 31.929  -36.083 -21.892 1.00 31.74  ? 183 ARG D O   1 
ATOM   11647 C  CB  . ARG D 2 183 ? 31.124  -38.985 -21.316 1.00 27.64  ? 183 ARG D CB  1 
ATOM   11648 C  CG  . ARG D 2 183 ? 30.492  -40.358 -21.639 1.00 31.60  ? 183 ARG D CG  1 
ATOM   11649 C  CD  . ARG D 2 183 ? 30.104  -41.095 -20.335 1.00 30.96  ? 183 ARG D CD  1 
ATOM   11650 N  NE  . ARG D 2 183 ? 28.914  -40.525 -19.710 1.00 33.28  ? 183 ARG D NE  1 
ATOM   11651 C  CZ  . ARG D 2 183 ? 28.442  -40.861 -18.517 1.00 34.15  ? 183 ARG D CZ  1 
ATOM   11652 N  NH1 . ARG D 2 183 ? 28.991  -41.823 -17.779 1.00 31.11  ? 183 ARG D NH1 1 
ATOM   11653 N  NH2 . ARG D 2 183 ? 27.377  -40.224 -18.048 1.00 32.77  ? 183 ARG D NH2 1 
ATOM   11654 N  N   . LYS D 2 184 ? 33.860  -37.199 -22.224 1.00 33.04  ? 184 LYS D N   1 
ATOM   11655 C  CA  . LYS D 2 184 ? 34.665  -36.024 -21.949 1.00 33.33  ? 184 LYS D CA  1 
ATOM   11656 C  C   . LYS D 2 184 ? 34.611  -35.003 -23.073 1.00 35.02  ? 184 LYS D C   1 
ATOM   11657 O  O   . LYS D 2 184 ? 34.895  -33.826 -22.819 1.00 37.24  ? 184 LYS D O   1 
ATOM   11658 C  CB  . LYS D 2 184 ? 36.133  -36.392 -21.711 1.00 34.77  ? 184 LYS D CB  1 
ATOM   11659 C  CG  . LYS D 2 184 ? 36.388  -37.365 -20.602 1.00 31.10  ? 184 LYS D CG  1 
ATOM   11660 C  CD  . LYS D 2 184 ? 37.900  -37.566 -20.464 1.00 35.56  ? 184 LYS D CD  1 
ATOM   11661 C  CE  . LYS D 2 184 ? 38.230  -38.454 -19.305 1.00 37.96  ? 184 LYS D CE  1 
ATOM   11662 N  NZ  . LYS D 2 184 ? 39.694  -38.602 -19.064 1.00 44.57  ? 184 LYS D NZ  1 
ATOM   11663 N  N   . ALA D 2 185 ? 34.246  -35.399 -24.290 1.00 30.93  ? 185 ALA D N   1 
ATOM   11664 C  CA  . ALA D 2 185 ? 34.280  -34.456 -25.403 1.00 35.88  ? 185 ALA D CA  1 
ATOM   11665 C  C   . ALA D 2 185 ? 33.233  -33.358 -25.221 1.00 39.93  ? 185 ALA D C   1 
ATOM   11666 O  O   . ALA D 2 185 ? 32.295  -33.478 -24.417 1.00 38.80  ? 185 ALA D O   1 
ATOM   11667 C  CB  . ALA D 2 185 ? 34.055  -35.187 -26.724 1.00 40.33  ? 185 ALA D CB  1 
ATOM   11668 N  N   . ALA D 2 186 ? 33.426  -32.253 -25.959 1.00 37.77  ? 186 ALA D N   1 
ATOM   11669 C  CA  . ALA D 2 186 ? 32.468  -31.151 -25.915 1.00 38.27  ? 186 ALA D CA  1 
ATOM   11670 C  C   . ALA D 2 186 ? 31.081  -31.602 -26.354 1.00 40.46  ? 186 ALA D C   1 
ATOM   11671 O  O   . ALA D 2 186 ? 30.062  -31.172 -25.804 1.00 38.48  ? 186 ALA D O   1 
ATOM   11672 C  CB  . ALA D 2 186 ? 32.940  -30.016 -26.822 1.00 36.97  ? 186 ALA D CB  1 
ATOM   11673 N  N   . ASP D 2 187 ? 31.025  -32.482 -27.347 1.00 37.51  ? 187 ASP D N   1 
ATOM   11674 C  CA  . ASP D 2 187 ? 29.774  -32.968 -27.927 1.00 37.82  ? 187 ASP D CA  1 
ATOM   11675 C  C   . ASP D 2 187 ? 29.804  -34.478 -27.793 1.00 40.54  ? 187 ASP D C   1 
ATOM   11676 O  O   . ASP D 2 187 ? 30.138  -35.182 -28.762 1.00 40.34  ? 187 ASP D O   1 
ATOM   11677 C  CB  . ASP D 2 187 ? 29.591  -32.544 -29.380 1.00 43.06  ? 187 ASP D CB  1 
ATOM   11678 C  CG  . ASP D 2 187 ? 29.552  -31.039 -29.564 1.00 48.11  ? 187 ASP D CG  1 
ATOM   11679 O  OD1 . ASP D 2 187 ? 29.051  -30.333 -28.673 1.00 44.60  ? 187 ASP D OD1 1 
ATOM   11680 O  OD2 . ASP D 2 187 ? 30.013  -30.572 -30.619 1.00 55.52  ? 187 ASP D OD2 1 
ATOM   11681 N  N   . PRO D 2 188 ? 29.448  -34.997 -26.617 1.00 36.92  ? 188 PRO D N   1 
ATOM   11682 C  CA  . PRO D 2 188 ? 29.633  -36.428 -26.338 1.00 33.68  ? 188 PRO D CA  1 
ATOM   11683 C  C   . PRO D 2 188 ? 28.931  -37.316 -27.363 1.00 34.73  ? 188 PRO D C   1 
ATOM   11684 O  O   . PRO D 2 188 ? 27.730  -37.180 -27.621 1.00 35.78  ? 188 PRO D O   1 
ATOM   11685 C  CB  . PRO D 2 188 ? 29.024  -36.603 -24.937 1.00 37.98  ? 188 PRO D CB  1 
ATOM   11686 C  CG  . PRO D 2 188 ? 29.088  -35.247 -24.284 1.00 37.30  ? 188 PRO D CG  1 
ATOM   11687 C  CD  . PRO D 2 188 ? 28.932  -34.250 -25.458 1.00 34.30  ? 188 PRO D CD  1 
ATOM   11688 N  N   . LYS D 2 189 ? 29.676  -38.289 -27.883 1.00 35.26  ? 189 LYS D N   1 
ATOM   11689 C  CA  . LYS D 2 189 ? 29.115  -39.311 -28.764 1.00 38.56  ? 189 LYS D CA  1 
ATOM   11690 C  C   . LYS D 2 189 ? 28.350  -40.405 -28.024 1.00 36.91  ? 189 LYS D C   1 
ATOM   11691 O  O   . LYS D 2 189 ? 27.912  -41.363 -28.667 1.00 39.07  ? 189 LYS D O   1 
ATOM   11692 C  CB  . LYS D 2 189 ? 30.240  -39.934 -29.595 1.00 39.39  ? 189 LYS D CB  1 
ATOM   11693 C  CG  . LYS D 2 189 ? 30.610  -38.994 -30.741 1.00 42.01  ? 189 LYS D CG  1 
ATOM   11694 C  CD  . LYS D 2 189 ? 31.656  -39.589 -31.649 1.00 44.83  ? 189 LYS D CD  1 
ATOM   11695 C  CE  . LYS D 2 189 ? 32.375  -38.572 -32.530 1.00 49.41  ? 189 LYS D CE  1 
ATOM   11696 N  NZ  . LYS D 2 189 ? 33.817  -38.981 -32.678 1.00 51.02  ? 189 LYS D NZ  1 
ATOM   11697 N  N   . VAL D 2 190 ? 28.255  -40.300 -26.699 1.00 37.22  ? 190 VAL D N   1 
ATOM   11698 C  CA  . VAL D 2 190 ? 27.562  -41.231 -25.818 1.00 30.85  ? 190 VAL D CA  1 
ATOM   11699 C  C   . VAL D 2 190 ? 26.856  -40.343 -24.814 1.00 33.14  ? 190 VAL D C   1 
ATOM   11700 O  O   . VAL D 2 190 ? 27.525  -39.576 -24.124 1.00 32.63  ? 190 VAL D O   1 
ATOM   11701 C  CB  . VAL D 2 190 ? 28.547  -42.163 -25.081 1.00 33.21  ? 190 VAL D CB  1 
ATOM   11702 C  CG1 . VAL D 2 190 ? 27.831  -43.067 -24.069 1.00 35.11  ? 190 VAL D CG1 1 
ATOM   11703 C  CG2 . VAL D 2 190 ? 29.438  -42.963 -26.053 1.00 39.82  ? 190 VAL D CG2 1 
ATOM   11704 N  N   . THR D 2 191 ? 25.525  -40.408 -24.752 1.00 31.47  ? 191 THR D N   1 
ATOM   11705 C  CA  . THR D 2 191 ? 24.792  -39.682 -23.724 1.00 29.02  ? 191 THR D CA  1 
ATOM   11706 C  C   . THR D 2 191 ? 24.857  -40.449 -22.403 1.00 34.98  ? 191 THR D C   1 
ATOM   11707 O  O   . THR D 2 191 ? 25.248  -41.619 -22.347 1.00 33.74  ? 191 THR D O   1 
ATOM   11708 C  CB  . THR D 2 191 ? 23.329  -39.504 -24.121 1.00 32.33  ? 191 THR D CB  1 
ATOM   11709 O  OG1 . THR D 2 191 ? 22.703  -40.799 -24.212 1.00 34.80  ? 191 THR D OG1 1 
ATOM   11710 C  CG2 . THR D 2 191 ? 23.202  -38.759 -25.454 1.00 33.11  ? 191 THR D CG2 1 
ATOM   11711 N  N   . GLY D 2 192 ? 24.445  -39.779 -21.324 1.00 30.61  ? 192 GLY D N   1 
ATOM   11712 C  CA  . GLY D 2 192 ? 24.362  -40.453 -20.041 1.00 29.54  ? 192 GLY D CA  1 
ATOM   11713 C  C   . GLY D 2 192 ? 23.407  -41.638 -20.065 1.00 32.34  ? 192 GLY D C   1 
ATOM   11714 O  O   . GLY D 2 192 ? 23.663  -42.661 -19.434 1.00 31.11  ? 192 GLY D O   1 
ATOM   11715 N  N   . VAL D 2 193 ? 22.264  -41.498 -20.741 1.00 29.80  ? 193 VAL D N   1 
ATOM   11716 C  CA  . VAL D 2 193 ? 21.338  -42.624 -20.830 1.00 32.57  ? 193 VAL D CA  1 
ATOM   11717 C  C   . VAL D 2 193 ? 21.992  -43.811 -21.534 1.00 33.17  ? 193 VAL D C   1 
ATOM   11718 O  O   . VAL D 2 193 ? 21.862  -44.959 -21.085 1.00 32.63  ? 193 VAL D O   1 
ATOM   11719 C  CB  . VAL D 2 193 ? 20.022  -42.199 -21.505 1.00 36.37  ? 193 VAL D CB  1 
ATOM   11720 C  CG1 . VAL D 2 193 ? 19.218  -43.454 -21.970 1.00 35.41  ? 193 VAL D CG1 1 
ATOM   11721 C  CG2 . VAL D 2 193 ? 19.204  -41.427 -20.491 1.00 32.48  ? 193 VAL D CG2 1 
ATOM   11722 N  N   . GLU D 2 194 ? 22.712  -43.562 -22.634 1.00 30.77  ? 194 GLU D N   1 
ATOM   11723 C  CA  . GLU D 2 194 ? 23.357  -44.668 -23.348 1.00 31.39  ? 194 GLU D CA  1 
ATOM   11724 C  C   . GLU D 2 194 ? 24.442  -45.312 -22.480 1.00 32.72  ? 194 GLU D C   1 
ATOM   11725 O  O   . GLU D 2 194 ? 24.535  -46.551 -22.363 1.00 29.66  ? 194 GLU D O   1 
ATOM   11726 C  CB  . GLU D 2 194 ? 23.927  -44.151 -24.677 1.00 30.27  ? 194 GLU D CB  1 
ATOM   11727 C  CG  . GLU D 2 194 ? 22.809  -43.701 -25.599 1.00 32.72  ? 194 GLU D CG  1 
ATOM   11728 C  CD  . GLU D 2 194 ? 23.291  -43.046 -26.884 1.00 37.60  ? 194 GLU D CD  1 
ATOM   11729 O  OE1 . GLU D 2 194 ? 24.367  -42.400 -26.872 1.00 37.68  ? 194 GLU D OE1 1 
ATOM   11730 O  OE2 . GLU D 2 194 ? 22.547  -43.130 -27.884 1.00 40.71  ? 194 GLU D OE2 1 
ATOM   11731 N  N   . ALA D 2 195 ? 25.279  -44.484 -21.855 1.00 30.00  ? 195 ALA D N   1 
ATOM   11732 C  CA  . ALA D 2 195 ? 26.271  -45.000 -20.917 1.00 31.29  ? 195 ALA D CA  1 
ATOM   11733 C  C   . ALA D 2 195 ? 25.622  -45.863 -19.826 1.00 30.67  ? 195 ALA D C   1 
ATOM   11734 O  O   . ALA D 2 195 ? 26.138  -46.932 -19.460 1.00 28.70  ? 195 ALA D O   1 
ATOM   11735 C  CB  . ALA D 2 195 ? 27.026  -43.833 -20.292 1.00 30.17  ? 195 ALA D CB  1 
ATOM   11736 N  N   . LEU D 2 196 ? 24.438  -45.459 -19.366 1.00 30.41  ? 196 LEU D N   1 
ATOM   11737 C  CA  . LEU D 2 196 ? 23.814  -46.185 -18.259 1.00 30.41  ? 196 LEU D CA  1 
ATOM   11738 C  C   . LEU D 2 196 ? 23.215  -47.519 -18.728 1.00 29.93  ? 196 LEU D C   1 
ATOM   11739 O  O   . LEU D 2 196 ? 23.284  -48.525 -18.020 1.00 30.77  ? 196 LEU D O   1 
ATOM   11740 C  CB  . LEU D 2 196 ? 22.780  -45.265 -17.633 1.00 31.61  ? 196 LEU D CB  1 
ATOM   11741 C  CG  . LEU D 2 196 ? 22.011  -45.806 -16.437 1.00 32.93  ? 196 LEU D CG  1 
ATOM   11742 C  CD1 . LEU D 2 196 ? 22.981  -46.123 -15.330 1.00 33.54  ? 196 LEU D CD1 1 
ATOM   11743 C  CD2 . LEU D 2 196 ? 21.067  -44.675 -15.984 1.00 35.51  ? 196 LEU D CD2 1 
ATOM   11744 N  N   . TYR D 2 197 ? 22.597  -47.541 -19.900 1.00 29.85  ? 197 TYR D N   1 
ATOM   11745 C  CA  . TYR D 2 197 ? 22.182  -48.824 -20.470 1.00 31.90  ? 197 TYR D CA  1 
ATOM   11746 C  C   . TYR D 2 197 ? 23.369  -49.786 -20.566 1.00 28.99  ? 197 TYR D C   1 
ATOM   11747 O  O   . TYR D 2 197 ? 23.255  -50.983 -20.250 1.00 31.20  ? 197 TYR D O   1 
ATOM   11748 C  CB  . TYR D 2 197 ? 21.576  -48.588 -21.828 1.00 31.17  ? 197 TYR D CB  1 
ATOM   11749 C  CG  . TYR D 2 197 ? 20.104  -48.206 -21.847 1.00 34.81  ? 197 TYR D CG  1 
ATOM   11750 C  CD1 . TYR D 2 197 ? 19.139  -49.061 -21.333 1.00 36.65  ? 197 TYR D CD1 1 
ATOM   11751 C  CD2 . TYR D 2 197 ? 19.682  -47.025 -22.450 1.00 35.84  ? 197 TYR D CD2 1 
ATOM   11752 C  CE1 . TYR D 2 197 ? 17.795  -48.743 -21.394 1.00 40.08  ? 197 TYR D CE1 1 
ATOM   11753 C  CE2 . TYR D 2 197 ? 18.326  -46.701 -22.522 1.00 41.23  ? 197 TYR D CE2 1 
ATOM   11754 C  CZ  . TYR D 2 197 ? 17.399  -47.570 -21.996 1.00 39.51  ? 197 TYR D CZ  1 
ATOM   11755 O  OH  . TYR D 2 197 ? 16.056  -47.276 -22.048 1.00 42.80  ? 197 TYR D OH  1 
ATOM   11756 N  N   . ALA D 2 198 ? 24.532  -49.273 -20.979 1.00 30.25  ? 198 ALA D N   1 
ATOM   11757 C  CA  . ALA D 2 198 ? 25.719  -50.122 -21.085 1.00 30.01  ? 198 ALA D CA  1 
ATOM   11758 C  C   . ALA D 2 198 ? 26.196  -50.614 -19.715 1.00 29.14  ? 198 ALA D C   1 
ATOM   11759 O  O   . ALA D 2 198 ? 26.464  -51.810 -19.545 1.00 28.94  ? 198 ALA D O   1 
ATOM   11760 C  CB  . ALA D 2 198 ? 26.849  -49.385 -21.780 1.00 32.31  ? 198 ALA D CB  1 
ATOM   11761 N  N   . SER D 2 199 ? 26.400  -49.699 -18.754 1.00 27.93  ? 199 SER D N   1 
ATOM   11762 C  CA  . SER D 2 199 ? 26.981  -50.071 -17.455 1.00 30.69  ? 199 SER D CA  1 
ATOM   11763 C  C   . SER D 2 199 ? 26.012  -50.892 -16.612 1.00 26.26  ? 199 SER D C   1 
ATOM   11764 O  O   . SER D 2 199 ? 26.434  -51.771 -15.825 1.00 30.65  ? 199 SER D O   1 
ATOM   11765 C  CB  . SER D 2 199 ? 27.424  -48.806 -16.661 1.00 28.97  ? 199 SER D CB  1 
ATOM   11766 O  OG  . SER D 2 199 ? 26.335  -47.941 -16.384 1.00 30.23  ? 199 SER D OG  1 
ATOM   11767 N  N   . LEU D 2 200 ? 24.714  -50.649 -16.766 1.00 29.02  ? 200 LEU D N   1 
ATOM   11768 C  CA  . LEU D 2 200 ? 23.759  -51.411 -15.967 1.00 29.21  ? 200 LEU D CA  1 
ATOM   11769 C  C   . LEU D 2 200 ? 23.637  -52.848 -16.473 1.00 28.96  ? 200 LEU D C   1 
ATOM   11770 O  O   . LEU D 2 200 ? 23.639  -53.802 -15.678 1.00 31.11  ? 200 LEU D O   1 
ATOM   11771 C  CB  . LEU D 2 200 ? 22.409  -50.711 -15.989 1.00 32.30  ? 200 LEU D CB  1 
ATOM   11772 C  CG  . LEU D 2 200 ? 21.452  -50.811 -14.797 1.00 36.66  ? 200 LEU D CG  1 
ATOM   11773 C  CD1 . LEU D 2 200 ? 22.133  -50.876 -13.426 1.00 33.21  ? 200 LEU D CD1 1 
ATOM   11774 C  CD2 . LEU D 2 200 ? 20.493  -49.619 -14.924 1.00 39.64  ? 200 LEU D CD2 1 
ATOM   11775 N  N   . THR D 2 201 ? 23.550  -53.030 -17.786 1.00 26.10  ? 201 THR D N   1 
ATOM   11776 C  CA  . THR D 2 201 ? 23.387  -54.375 -18.353 1.00 27.16  ? 201 THR D CA  1 
ATOM   11777 C  C   . THR D 2 201 ? 24.641  -55.208 -18.194 1.00 26.82  ? 201 THR D C   1 
ATOM   11778 O  O   . THR D 2 201 ? 24.552  -56.443 -18.235 1.00 27.31  ? 201 THR D O   1 
ATOM   11779 C  CB  . THR D 2 201 ? 23.022  -54.304 -19.842 1.00 29.34  ? 201 THR D CB  1 
ATOM   11780 O  OG1 . THR D 2 201 ? 24.013  -53.563 -20.593 1.00 27.64  ? 201 THR D OG1 1 
ATOM   11781 C  CG2 . THR D 2 201 ? 21.608  -53.587 -19.992 1.00 29.69  ? 201 THR D CG2 1 
ATOM   11782 N  N   . ALA D 2 202 ? 25.804  -54.562 -18.009 1.00 26.32  ? 202 ALA D N   1 
ATOM   11783 C  CA  . ALA D 2 202 ? 27.013  -55.284 -17.675 1.00 28.76  ? 202 ALA D CA  1 
ATOM   11784 C  C   . ALA D 2 202 ? 26.829  -56.161 -16.438 1.00 27.38  ? 202 ALA D C   1 
ATOM   11785 O  O   . ALA D 2 202 ? 27.560  -57.150 -16.295 1.00 29.39  ? 202 ALA D O   1 
ATOM   11786 C  CB  . ALA D 2 202 ? 28.145  -54.280 -17.472 1.00 26.81  ? 202 ALA D CB  1 
ATOM   11787 N  N   . GLN D 2 203 ? 25.857  -55.829 -15.552 1.00 24.67  ? 203 GLN D N   1 
ATOM   11788 C  CA  . GLN D 2 203 ? 25.638  -56.503 -14.279 1.00 25.28  ? 203 GLN D CA  1 
ATOM   11789 C  C   . GLN D 2 203 ? 24.624  -57.638 -14.340 1.00 28.04  ? 203 GLN D C   1 
ATOM   11790 O  O   . GLN D 2 203 ? 24.402  -58.301 -13.309 1.00 28.11  ? 203 GLN D O   1 
ATOM   11791 C  CB  . GLN D 2 203 ? 25.236  -55.455 -13.238 1.00 24.72  ? 203 GLN D CB  1 
ATOM   11792 C  CG  . GLN D 2 203 ? 26.256  -54.286 -13.251 1.00 24.42  ? 203 GLN D CG  1 
ATOM   11793 C  CD  . GLN D 2 203 ? 25.955  -53.266 -12.226 1.00 28.26  ? 203 GLN D CD  1 
ATOM   11794 O  OE1 . GLN D 2 203 ? 25.607  -53.619 -11.111 1.00 28.86  ? 203 GLN D OE1 1 
ATOM   11795 N  NE2 . GLN D 2 203 ? 26.085  -51.967 -12.585 1.00 29.46  ? 203 GLN D NE2 1 
ATOM   11796 N  N   . PHE D 2 204 ? 24.059  -57.941 -15.533 1.00 24.91  ? 204 PHE D N   1 
ATOM   11797 C  CA  . PHE D 2 204 ? 23.200  -59.124 -15.610 1.00 26.87  ? 204 PHE D CA  1 
ATOM   11798 C  C   . PHE D 2 204 ? 23.192  -59.765 -17.003 1.00 25.93  ? 204 PHE D C   1 
ATOM   11799 O  O   . PHE D 2 204 ? 22.324  -60.602 -17.272 1.00 30.33  ? 204 PHE D O   1 
ATOM   11800 C  CB  . PHE D 2 204 ? 21.747  -58.788 -15.187 1.00 26.12  ? 204 PHE D CB  1 
ATOM   11801 C  CG  . PHE D 2 204 ? 21.210  -57.509 -15.807 1.00 28.52  ? 204 PHE D CG  1 
ATOM   11802 C  CD1 . PHE D 2 204 ? 20.835  -57.487 -17.151 1.00 30.13  ? 204 PHE D CD1 1 
ATOM   11803 C  CD2 . PHE D 2 204 ? 21.012  -56.390 -15.032 1.00 30.77  ? 204 PHE D CD2 1 
ATOM   11804 C  CE1 . PHE D 2 204 ? 20.313  -56.354 -17.731 1.00 32.28  ? 204 PHE D CE1 1 
ATOM   11805 C  CE2 . PHE D 2 204 ? 20.476  -55.215 -15.586 1.00 32.14  ? 204 PHE D CE2 1 
ATOM   11806 C  CZ  . PHE D 2 204 ? 20.132  -55.200 -16.919 1.00 30.35  ? 204 PHE D CZ  1 
ATOM   11807 N  N   . ILE D 2 205 ? 24.124  -59.404 -17.884 1.00 25.70  ? 205 ILE D N   1 
ATOM   11808 C  CA  . ILE D 2 205 ? 24.361  -60.094 -19.160 1.00 26.94  ? 205 ILE D CA  1 
ATOM   11809 C  C   . ILE D 2 205 ? 25.704  -60.836 -19.090 1.00 25.65  ? 205 ILE D C   1 
ATOM   11810 O  O   . ILE D 2 205 ? 26.641  -60.411 -18.411 1.00 29.63  ? 205 ILE D O   1 
ATOM   11811 C  CB  . ILE D 2 205 ? 24.313  -59.023 -20.289 1.00 26.00  ? 205 ILE D CB  1 
ATOM   11812 C  CG1 . ILE D 2 205 ? 22.958  -58.296 -20.280 1.00 29.86  ? 205 ILE D CG1 1 
ATOM   11813 C  CG2 . ILE D 2 205 ? 24.639  -59.562 -21.670 1.00 28.97  ? 205 ILE D CG2 1 
ATOM   11814 C  CD1 . ILE D 2 205 ? 21.729  -59.178 -20.511 1.00 31.95  ? 205 ILE D CD1 1 
ATOM   11815 N  N   . ASP D 2 206 ? 25.805  -61.967 -19.812 1.00 31.80  ? 206 ASP D N   1 
ATOM   11816 C  CA  . ASP D 2 206 ? 27.066  -62.705 -19.862 1.00 32.08  ? 206 ASP D CA  1 
ATOM   11817 C  C   . ASP D 2 206 ? 28.191  -61.782 -20.329 1.00 33.97  ? 206 ASP D C   1 
ATOM   11818 O  O   . ASP D 2 206 ? 28.080  -61.122 -21.372 1.00 30.11  ? 206 ASP D O   1 
ATOM   11819 C  CB  . ASP D 2 206 ? 26.937  -63.926 -20.803 1.00 33.05  ? 206 ASP D CB  1 
ATOM   11820 C  CG  . ASP D 2 206 ? 28.168  -64.842 -20.769 1.00 38.15  ? 206 ASP D CG  1 
ATOM   11821 O  OD1 . ASP D 2 206 ? 29.296  -64.368 -21.051 1.00 39.29  ? 206 ASP D OD1 1 
ATOM   11822 O  OD2 . ASP D 2 206 ? 28.009  -66.051 -20.453 1.00 42.73  ? 206 ASP D OD2 1 
ATOM   11823 N  N   . LYS D 2 207 ? 29.274  -61.697 -19.543 1.00 32.64  ? 207 LYS D N   1 
ATOM   11824 C  CA  . LYS D 2 207 ? 30.256  -60.660 -19.866 1.00 30.76  ? 207 LYS D CA  1 
ATOM   11825 C  C   . LYS D 2 207 ? 30.961  -60.921 -21.200 1.00 32.12  ? 207 LYS D C   1 
ATOM   11826 O  O   . LYS D 2 207 ? 31.368  -59.970 -21.887 1.00 31.91  ? 207 LYS D O   1 
ATOM   11827 C  CB  . LYS D 2 207 ? 31.261  -60.518 -18.735 1.00 34.07  ? 207 LYS D CB  1 
ATOM   11828 C  CG  . LYS D 2 207 ? 30.615  -59.943 -17.496 1.00 39.25  ? 207 LYS D CG  1 
ATOM   11829 C  CD  . LYS D 2 207 ? 31.513  -58.966 -16.816 1.00 35.62  ? 207 LYS D CD  1 
ATOM   11830 C  CE  . LYS D 2 207 ? 30.759  -58.187 -15.730 1.00 39.20  ? 207 LYS D CE  1 
ATOM   11831 N  NZ  . LYS D 2 207 ? 29.814  -59.109 -15.053 1.00 39.85  ? 207 LYS D NZ  1 
ATOM   11832 N  N   . ARG D 2 208 ? 31.106  -62.177 -21.611 1.00 28.26  ? 208 ARG D N   1 
ATOM   11833 C  CA  . ARG D 2 208 ? 31.600  -62.392 -22.966 1.00 32.86  ? 208 ARG D CA  1 
ATOM   11834 C  C   . ARG D 2 208 ? 30.679  -61.741 -23.986 1.00 31.79  ? 208 ARG D C   1 
ATOM   11835 O  O   . ARG D 2 208 ? 31.137  -61.056 -24.900 1.00 34.43  ? 208 ARG D O   1 
ATOM   11836 C  CB  . ARG D 2 208 ? 31.776  -63.889 -23.271 1.00 35.82  ? 208 ARG D CB  1 
ATOM   11837 C  CG  . ARG D 2 208 ? 32.434  -64.624 -22.133 1.00 43.96  ? 208 ARG D CG  1 
ATOM   11838 C  CD  . ARG D 2 208 ? 32.562  -66.111 -22.450 1.00 47.04  ? 208 ARG D CD  1 
ATOM   11839 N  NE  . ARG D 2 208 ? 31.565  -66.882 -21.713 1.00 58.74  ? 208 ARG D NE  1 
ATOM   11840 C  CZ  . ARG D 2 208 ? 30.347  -67.167 -22.165 1.00 59.03  ? 208 ARG D CZ  1 
ATOM   11841 N  NH1 . ARG D 2 208 ? 29.933  -66.757 -23.358 1.00 57.15  ? 208 ARG D NH1 1 
ATOM   11842 N  NH2 . ARG D 2 208 ? 29.526  -67.894 -21.406 1.00 52.90  ? 208 ARG D NH2 1 
ATOM   11843 N  N   . GLU D 2 209 ? 29.373  -61.953 -23.852 1.00 31.20  ? 209 GLU D N   1 
ATOM   11844 C  CA  . GLU D 2 209 ? 28.446  -61.350 -24.808 1.00 32.59  ? 209 GLU D CA  1 
ATOM   11845 C  C   . GLU D 2 209 ? 28.468  -59.836 -24.711 1.00 31.26  ? 209 GLU D C   1 
ATOM   11846 O  O   . GLU D 2 209 ? 28.487  -59.141 -25.739 1.00 32.42  ? 209 GLU D O   1 
ATOM   11847 C  CB  . GLU D 2 209 ? 27.046  -61.906 -24.559 1.00 35.08  ? 209 GLU D CB  1 
ATOM   11848 C  CG  . GLU D 2 209 ? 27.043  -63.382 -24.836 1.00 40.09  ? 209 GLU D CG  1 
ATOM   11849 C  CD  . GLU D 2 209 ? 25.763  -64.120 -24.432 1.00 43.55  ? 209 GLU D CD  1 
ATOM   11850 O  OE1 . GLU D 2 209 ? 25.894  -65.326 -24.126 1.00 53.49  ? 209 GLU D OE1 1 
ATOM   11851 O  OE2 . GLU D 2 209 ? 24.669  -63.536 -24.357 1.00 44.99  ? 209 GLU D OE2 1 
ATOM   11852 N  N   . HIS D 2 210 ? 28.474  -59.312 -23.479 1.00 30.01  ? 210 HIS D N   1 
ATOM   11853 C  CA  . HIS D 2 210 ? 28.487  -57.871 -23.287 1.00 29.24  ? 210 HIS D CA  1 
ATOM   11854 C  C   . HIS D 2 210 ? 29.753  -57.235 -23.845 1.00 29.94  ? 210 HIS D C   1 
ATOM   11855 O  O   . HIS D 2 210 ? 29.691  -56.184 -24.508 1.00 30.37  ? 210 HIS D O   1 
ATOM   11856 C  CB  . HIS D 2 210 ? 28.331  -57.593 -21.793 1.00 26.36  ? 210 HIS D CB  1 
ATOM   11857 C  CG  . HIS D 2 210 ? 27.819  -56.222 -21.466 1.00 30.09  ? 210 HIS D CG  1 
ATOM   11858 N  ND1 . HIS D 2 210 ? 28.670  -55.180 -21.171 1.00 28.54  ? 210 HIS D ND1 1 
ATOM   11859 C  CD2 . HIS D 2 210 ? 26.560  -55.730 -21.349 1.00 28.10  ? 210 HIS D CD2 1 
ATOM   11860 C  CE1 . HIS D 2 210 ? 27.963  -54.098 -20.895 1.00 29.31  ? 210 HIS D CE1 1 
ATOM   11861 N  NE2 . HIS D 2 210 ? 26.680  -54.405 -20.994 1.00 27.87  ? 210 HIS D NE2 1 
ATOM   11862 N  N   . ASN D 2 211 ? 30.919  -57.858 -23.606 1.00 28.35  ? 211 ASN D N   1 
ATOM   11863 C  CA  . ASN D 2 211 ? 32.177  -57.324 -24.134 1.00 31.71  ? 211 ASN D CA  1 
ATOM   11864 C  C   . ASN D 2 211 ? 32.136  -57.212 -25.654 1.00 32.32  ? 211 ASN D C   1 
ATOM   11865 O  O   . ASN D 2 211 ? 32.669  -56.249 -26.232 1.00 29.98  ? 211 ASN D O   1 
ATOM   11866 C  CB  . ASN D 2 211 ? 33.357  -58.207 -23.720 1.00 32.87  ? 211 ASN D CB  1 
ATOM   11867 C  CG  . ASN D 2 211 ? 33.695  -58.066 -22.241 1.00 29.68  ? 211 ASN D CG  1 
ATOM   11868 O  OD1 . ASN D 2 211 ? 33.246  -57.131 -21.587 1.00 30.24  ? 211 ASN D OD1 1 
ATOM   11869 N  ND2 . ASN D 2 211 ? 34.471  -58.995 -21.710 1.00 31.79  ? 211 ASN D ND2 1 
ATOM   11870 N  N   . GLU D 2 212 ? 31.565  -58.226 -26.314 1.00 32.43  ? 212 GLU D N   1 
ATOM   11871 C  CA  . GLU D 2 212 ? 31.402  -58.183 -27.753 1.00 33.66  ? 212 GLU D CA  1 
ATOM   11872 C  C   . GLU D 2 212 ? 30.547  -56.987 -28.168 1.00 34.72  ? 212 GLU D C   1 
ATOM   11873 O  O   . GLU D 2 212 ? 30.848  -56.294 -29.159 1.00 32.04  ? 212 GLU D O   1 
ATOM   11874 C  CB  . GLU D 2 212 ? 30.807  -59.504 -28.205 1.00 35.41  ? 212 GLU D CB  1 
ATOM   11875 C  CG  . GLU D 2 212 ? 30.615  -59.528 -29.667 1.00 42.65  ? 212 GLU D CG  1 
ATOM   11876 C  CD  . GLU D 2 212 ? 31.741  -60.266 -30.347 1.00 50.57  ? 212 GLU D CD  1 
ATOM   11877 O  OE1 . GLU D 2 212 ? 32.929  -59.948 -30.056 1.00 49.69  ? 212 GLU D OE1 1 
ATOM   11878 O  OE2 . GLU D 2 212 ? 31.419  -61.169 -31.151 1.00 53.05  ? 212 GLU D OE2 1 
ATOM   11879 N  N   . MET D 2 213 ? 29.467  -56.732 -27.431 1.00 31.38  ? 213 MET D N   1 
ATOM   11880 C  CA  . MET D 2 213 ? 28.615  -55.594 -27.772 1.00 35.11  ? 213 MET D CA  1 
ATOM   11881 C  C   . MET D 2 213 ? 29.314  -54.260 -27.525 1.00 33.40  ? 213 MET D C   1 
ATOM   11882 O  O   . MET D 2 213 ? 29.145  -53.318 -28.318 1.00 33.12  ? 213 MET D O   1 
ATOM   11883 C  CB  . MET D 2 213 ? 27.293  -55.665 -27.012 1.00 37.52  ? 213 MET D CB  1 
ATOM   11884 C  CG  . MET D 2 213 ? 26.123  -54.752 -27.544 1.00 35.24  ? 213 MET D CG  1 
ATOM   11885 S  SD  . MET D 2 213 ? 25.876  -54.748 -29.311 1.00 45.42  ? 213 MET D SD  1 
ATOM   11886 C  CE  . MET D 2 213 ? 25.838  -52.979 -29.621 1.00 42.31  ? 213 MET D CE  1 
ATOM   11887 N  N   . LEU D 2 214 ? 30.097  -54.163 -26.449 1.00 29.08  ? 214 LEU D N   1 
ATOM   11888 C  CA  . LEU D 2 214 ? 30.866  -52.947 -26.218 1.00 29.19  ? 214 LEU D CA  1 
ATOM   11889 C  C   . LEU D 2 214 ? 31.903  -52.755 -27.312 1.00 28.89  ? 214 LEU D C   1 
ATOM   11890 O  O   . LEU D 2 214 ? 32.144  -51.629 -27.767 1.00 27.50  ? 214 LEU D O   1 
ATOM   11891 C  CB  . LEU D 2 214 ? 31.574  -53.009 -24.855 1.00 25.81  ? 214 LEU D CB  1 
ATOM   11892 C  CG  . LEU D 2 214 ? 30.708  -52.855 -23.596 1.00 29.40  ? 214 LEU D CG  1 
ATOM   11893 C  CD1 . LEU D 2 214 ? 31.502  -53.186 -22.385 1.00 27.52  ? 214 LEU D CD1 1 
ATOM   11894 C  CD2 . LEU D 2 214 ? 30.199  -51.402 -23.528 1.00 28.96  ? 214 LEU D CD2 1 
ATOM   11895 N  N   . LYS D 2 215 ? 32.536  -53.833 -27.756 1.00 28.92  ? 215 LYS D N   1 
ATOM   11896 C  CA  . LYS D 2 215 ? 33.497  -53.719 -28.856 1.00 31.35  ? 215 LYS D CA  1 
ATOM   11897 C  C   . LYS D 2 215 ? 32.834  -53.185 -30.123 1.00 28.73  ? 215 LYS D C   1 
ATOM   11898 O  O   . LYS D 2 215 ? 33.391  -52.326 -30.802 1.00 31.23  ? 215 LYS D O   1 
ATOM   11899 C  CB  . LYS D 2 215 ? 34.189  -55.072 -29.091 1.00 31.35  ? 215 LYS D CB  1 
ATOM   11900 C  CG  . LYS D 2 215 ? 35.394  -55.196 -28.104 1.00 34.71  ? 215 LYS D CG  1 
ATOM   11901 C  CD  . LYS D 2 215 ? 36.214  -56.498 -28.222 1.00 34.41  ? 215 LYS D CD  1 
ATOM   11902 C  CE  . LYS D 2 215 ? 35.600  -57.686 -27.500 1.00 42.84  ? 215 LYS D CE  1 
ATOM   11903 N  NZ  . LYS D 2 215 ? 36.629  -58.781 -27.368 1.00 43.58  ? 215 LYS D NZ  1 
ATOM   11904 N  N   . LYS D 2 216 ? 31.639  -53.680 -30.455 1.00 31.04  ? 216 LYS D N   1 
ATOM   11905 C  CA  . LYS D 2 216 ? 30.934  -53.200 -31.638 1.00 33.87  ? 216 LYS D CA  1 
ATOM   11906 C  C   . LYS D 2 216 ? 30.602  -51.717 -31.504 1.00 33.43  ? 216 LYS D C   1 
ATOM   11907 O  O   . LYS D 2 216 ? 30.655  -50.968 -32.492 1.00 34.20  ? 216 LYS D O   1 
ATOM   11908 C  CB  . LYS D 2 216 ? 29.654  -54.010 -31.850 1.00 35.93  ? 216 LYS D CB  1 
ATOM   11909 C  CG  . LYS D 2 216 ? 28.501  -53.199 -32.446 1.00 41.14  ? 216 LYS D CG  1 
ATOM   11910 C  CD  . LYS D 2 216 ? 27.295  -54.048 -32.820 1.00 41.43  ? 216 LYS D CD  1 
ATOM   11911 C  CE  . LYS D 2 216 ? 26.372  -53.282 -33.765 1.00 47.09  ? 216 LYS D CE  1 
ATOM   11912 N  NZ  . LYS D 2 216 ? 25.315  -54.150 -34.302 1.00 44.39  ? 216 LYS D NZ  1 
ATOM   11913 N  N   . THR D 2 217 ? 30.250  -51.288 -30.289 1.00 32.46  ? 217 THR D N   1 
ATOM   11914 C  CA  . THR D 2 217 ? 29.867  -49.905 -30.030 1.00 30.22  ? 217 THR D CA  1 
ATOM   11915 C  C   . THR D 2 217 ? 31.054  -48.983 -30.215 1.00 30.45  ? 217 THR D C   1 
ATOM   11916 O  O   . THR D 2 217 ? 30.986  -47.995 -30.974 1.00 34.28  ? 217 THR D O   1 
ATOM   11917 C  CB  . THR D 2 217 ? 29.308  -49.832 -28.600 1.00 33.61  ? 217 THR D CB  1 
ATOM   11918 O  OG1 . THR D 2 217 ? 28.198  -50.742 -28.508 1.00 33.33  ? 217 THR D OG1 1 
ATOM   11919 C  CG2 . THR D 2 217 ? 28.891  -48.413 -28.216 1.00 34.69  ? 217 THR D CG2 1 
ATOM   11920 N  N   . LEU D 2 218 ? 32.190  -49.360 -29.616 1.00 34.36  ? 218 LEU D N   1 
ATOM   11921 C  CA  . LEU D 2 218 ? 33.402  -48.555 -29.725 1.00 35.38  ? 218 LEU D CA  1 
ATOM   11922 C  C   . LEU D 2 218 ? 33.925  -48.492 -31.158 1.00 33.79  ? 218 LEU D C   1 
ATOM   11923 O  O   . LEU D 2 218 ? 34.614  -47.538 -31.518 1.00 39.19  ? 218 LEU D O   1 
ATOM   11924 C  CB  . LEU D 2 218 ? 34.480  -49.119 -28.816 1.00 33.21  ? 218 LEU D CB  1 
ATOM   11925 C  CG  . LEU D 2 218 ? 34.198  -48.984 -27.322 1.00 33.23  ? 218 LEU D CG  1 
ATOM   11926 C  CD1 . LEU D 2 218 ? 35.152  -49.834 -26.519 1.00 33.27  ? 218 LEU D CD1 1 
ATOM   11927 C  CD2 . LEU D 2 218 ? 34.054  -47.499 -26.851 1.00 26.08  ? 218 LEU D CD2 1 
ATOM   11928 N  N   . ALA D 2 219 ? 33.643  -49.498 -31.996 1.00 33.73  ? 219 ALA D N   1 
ATOM   11929 C  CA  . ALA D 2 219 ? 34.083  -49.438 -33.386 1.00 35.28  ? 219 ALA D CA  1 
ATOM   11930 C  C   . ALA D 2 219 ? 33.249  -48.452 -34.222 1.00 35.63  ? 219 ALA D C   1 
ATOM   11931 O  O   . ALA D 2 219 ? 33.750  -47.905 -35.219 1.00 36.27  ? 219 ALA D O   1 
ATOM   11932 C  CB  . ALA D 2 219 ? 34.032  -50.837 -33.989 1.00 37.03  ? 219 ALA D CB  1 
ATOM   11933 N  N   . ALA D 2 220 ? 31.997  -48.218 -33.814 1.00 35.46  ? 220 ALA D N   1 
ATOM   11934 C  CA  . ALA D 2 220 ? 31.084  -47.293 -34.474 1.00 38.58  ? 220 ALA D CA  1 
ATOM   11935 C  C   . ALA D 2 220 ? 31.215  -45.848 -33.982 1.00 37.62  ? 220 ALA D C   1 
ATOM   11936 O  O   . ALA D 2 220 ? 30.866  -44.916 -34.718 1.00 42.18  ? 220 ALA D O   1 
ATOM   11937 C  CB  . ALA D 2 220 ? 29.642  -47.748 -34.249 1.00 36.58  ? 220 ALA D CB  1 
ATOM   11938 N  N   . LEU D 2 221 ? 31.668  -45.649 -32.752 1.00 38.96  ? 221 LEU D N   1 
ATOM   11939 C  CA  . LEU D 2 221 ? 31.620  -44.320 -32.141 1.00 38.44  ? 221 LEU D CA  1 
ATOM   11940 C  C   . LEU D 2 221 ? 32.455  -43.283 -32.887 1.00 43.31  ? 221 LEU D C   1 
ATOM   11941 O  O   . LEU D 2 221 ? 31.953  -42.171 -33.099 1.00 39.97  ? 221 LEU D O   1 
ATOM   11942 C  CB  . LEU D 2 221 ? 32.077  -44.409 -30.680 1.00 36.28  ? 221 LEU D CB  1 
ATOM   11943 C  CG  . LEU D 2 221 ? 31.082  -44.941 -29.649 1.00 34.54  ? 221 LEU D CG  1 
ATOM   11944 C  CD1 . LEU D 2 221 ? 31.736  -45.118 -28.169 1.00 29.36  ? 221 LEU D CD1 1 
ATOM   11945 C  CD2 . LEU D 2 221 ? 29.843  -44.062 -29.668 1.00 40.06  ? 221 LEU D CD2 1 
ATOM   11946 N  N   . PRO D 2 222 ? 33.723  -43.544 -33.266 1.00 42.33  ? 222 PRO D N   1 
ATOM   11947 C  CA  . PRO D 2 222 ? 34.500  -42.515 -33.990 1.00 47.72  ? 222 PRO D CA  1 
ATOM   11948 C  C   . PRO D 2 222 ? 33.771  -41.869 -35.169 1.00 49.54  ? 222 PRO D C   1 
ATOM   11949 O  O   . PRO D 2 222 ? 34.000  -40.686 -35.453 1.00 49.48  ? 222 PRO D O   1 
ATOM   11950 C  CB  . PRO D 2 222 ? 35.733  -43.291 -34.476 1.00 51.75  ? 222 PRO D CB  1 
ATOM   11951 C  CG  . PRO D 2 222 ? 35.918  -44.362 -33.472 1.00 45.44  ? 222 PRO D CG  1 
ATOM   11952 C  CD  . PRO D 2 222 ? 34.538  -44.752 -33.013 1.00 40.73  ? 222 PRO D CD  1 
ATOM   11953 N  N   . ASN D 2 223 ? 32.881  -42.577 -35.857 1.00 41.86  ? 223 ASN D N   1 
ATOM   11954 C  CA  . ASN D 2 223 ? 32.203  -41.941 -36.986 1.00 48.69  ? 223 ASN D CA  1 
ATOM   11955 C  C   . ASN D 2 223 ? 30.716  -41.744 -36.755 1.00 46.35  ? 223 ASN D C   1 
ATOM   11956 O  O   . ASN D 2 223 ? 29.983  -41.466 -37.701 1.00 40.86  ? 223 ASN D O   1 
ATOM   11957 C  CB  . ASN D 2 223 ? 32.456  -42.739 -38.252 1.00 49.70  ? 223 ASN D CB  1 
ATOM   11958 C  CG  . ASN D 2 223 ? 33.895  -43.113 -38.380 1.00 54.28  ? 223 ASN D CG  1 
ATOM   11959 O  OD1 . ASN D 2 223 ? 34.754  -42.230 -38.443 1.00 56.90  ? 223 ASN D OD1 1 
ATOM   11960 N  ND2 . ASN D 2 223 ? 34.191  -44.417 -38.343 1.00 54.42  ? 223 ASN D ND2 1 
ATOM   11961 N  N   . ARG D 2 224 ? 30.275  -41.849 -35.506 1.00 43.31  ? 224 ARG D N   1 
ATOM   11962 C  CA  . ARG D 2 224 ? 28.885  -41.584 -35.161 1.00 42.09  ? 224 ARG D CA  1 
ATOM   11963 C  C   . ARG D 2 224 ? 28.630  -40.092 -35.265 1.00 45.74  ? 224 ARG D C   1 
ATOM   11964 O  O   . ARG D 2 224 ? 29.378  -39.294 -34.695 1.00 46.92  ? 224 ARG D O   1 
ATOM   11965 C  CB  . ARG D 2 224 ? 28.592  -42.084 -33.738 1.00 42.56  ? 224 ARG D CB  1 
ATOM   11966 C  CG  . ARG D 2 224 ? 27.125  -42.258 -33.439 1.00 43.01  ? 224 ARG D CG  1 
ATOM   11967 C  CD  . ARG D 2 224 ? 26.855  -42.512 -31.902 1.00 36.75  ? 224 ARG D CD  1 
ATOM   11968 N  NE  . ARG D 2 224 ? 25.467  -42.932 -31.756 1.00 42.41  ? 224 ARG D NE  1 
ATOM   11969 C  CZ  . ARG D 2 224 ? 24.817  -43.059 -30.607 1.00 41.76  ? 224 ARG D CZ  1 
ATOM   11970 N  NH1 . ARG D 2 224 ? 25.412  -42.817 -29.445 1.00 43.28  ? 224 ARG D NH1 1 
ATOM   11971 N  NH2 . ARG D 2 224 ? 23.517  -43.384 -30.631 1.00 41.57  ? 224 ARG D NH2 1 
ATOM   11972 N  N   . LYS D 2 225 ? 27.579  -39.721 -35.994 1.00 44.32  ? 225 LYS D N   1 
ATOM   11973 C  CA  . LYS D 2 225 ? 27.158  -38.326 -36.066 1.00 50.85  ? 225 LYS D CA  1 
ATOM   11974 C  C   . LYS D 2 225 ? 26.293  -37.975 -34.859 1.00 49.92  ? 225 LYS D C   1 
ATOM   11975 O  O   . LYS D 2 225 ? 25.378  -38.727 -34.509 1.00 53.88  ? 225 LYS D O   1 
ATOM   11976 C  CB  . LYS D 2 225 ? 26.402  -38.080 -37.359 1.00 54.67  ? 225 LYS D CB  1 
ATOM   11977 C  CG  . LYS D 2 225 ? 27.259  -37.371 -38.387 1.00 66.96  ? 225 LYS D CG  1 
ATOM   11978 C  CD  . LYS D 2 225 ? 28.009  -38.398 -39.269 1.00 72.77  ? 225 LYS D CD  1 
ATOM   11979 C  CE  . LYS D 2 225 ? 28.358  -37.820 -40.628 1.00 68.75  ? 225 LYS D CE  1 
ATOM   11980 N  NZ  . LYS D 2 225 ? 29.470  -36.844 -40.492 1.00 75.17  ? 225 LYS D NZ  1 
ATOM   11981 N  N   . VAL D 2 226 ? 26.593  -36.850 -34.203 1.00 47.26  ? 226 VAL D N   1 
ATOM   11982 C  CA  . VAL D 2 226 ? 25.785  -36.385 -33.076 1.00 47.36  ? 226 VAL D CA  1 
ATOM   11983 C  C   . VAL D 2 226 ? 24.894  -35.271 -33.587 1.00 52.75  ? 226 VAL D C   1 
ATOM   11984 O  O   . VAL D 2 226 ? 25.345  -34.411 -34.350 1.00 51.31  ? 226 VAL D O   1 
ATOM   11985 C  CB  . VAL D 2 226 ? 26.652  -35.917 -31.896 1.00 48.23  ? 226 VAL D CB  1 
ATOM   11986 C  CG1 . VAL D 2 226 ? 25.791  -35.245 -30.790 1.00 50.13  ? 226 VAL D CG1 1 
ATOM   11987 C  CG2 . VAL D 2 226 ? 27.399  -37.086 -31.315 1.00 48.20  ? 226 VAL D CG2 1 
ATOM   11988 N  N   . GLU D 2 227 ? 23.617  -35.313 -33.216 1.00 53.73  ? 227 GLU D N   1 
ATOM   11989 C  CA  . GLU D 2 227 ? 22.707  -34.255 -33.610 1.00 57.36  ? 227 GLU D CA  1 
ATOM   11990 C  C   . GLU D 2 227 ? 22.121  -33.457 -32.455 1.00 49.87  ? 227 GLU D C   1 
ATOM   11991 O  O   . GLU D 2 227 ? 21.721  -32.306 -32.679 1.00 47.79  ? 227 GLU D O   1 
ATOM   11992 C  CB  . GLU D 2 227 ? 21.582  -34.821 -34.491 1.00 59.72  ? 227 GLU D CB  1 
ATOM   11993 C  CG  . GLU D 2 227 ? 21.062  -33.806 -35.516 1.00 63.99  ? 227 GLU D CG  1 
ATOM   11994 C  CD  . GLU D 2 227 ? 21.876  -33.740 -36.796 1.00 66.88  ? 227 GLU D CD  1 
ATOM   11995 O  OE1 . GLU D 2 227 ? 21.753  -34.643 -37.657 1.00 73.63  ? 227 GLU D OE1 1 
ATOM   11996 O  OE2 . GLU D 2 227 ? 22.611  -32.737 -36.956 1.00 67.80  ? 227 GLU D OE2 1 
ATOM   11997 N  N   . ARG D 2 228 ? 22.080  -34.009 -31.251 1.00 50.95  ? 228 ARG D N   1 
ATOM   11998 C  CA  . ARG D 2 228 ? 21.588  -33.280 -30.080 1.00 43.94  ? 228 ARG D CA  1 
ATOM   11999 C  C   . ARG D 2 228 ? 22.605  -32.223 -29.641 1.00 45.69  ? 228 ARG D C   1 
ATOM   12000 O  O   . ARG D 2 228 ? 23.811  -32.325 -29.915 1.00 42.29  ? 228 ARG D O   1 
ATOM   12001 C  CB  . ARG D 2 228 ? 21.281  -34.254 -28.934 1.00 44.43  ? 228 ARG D CB  1 
ATOM   12002 C  CG  . ARG D 2 228 ? 22.475  -35.000 -28.437 1.00 44.27  ? 228 ARG D CG  1 
ATOM   12003 C  CD  . ARG D 2 228 ? 22.076  -36.151 -27.505 1.00 43.09  ? 228 ARG D CD  1 
ATOM   12004 N  NE  . ARG D 2 228 ? 21.483  -35.646 -26.280 1.00 43.58  ? 228 ARG D NE  1 
ATOM   12005 C  CZ  . ARG D 2 228 ? 22.185  -35.128 -25.282 1.00 42.65  ? 228 ARG D CZ  1 
ATOM   12006 N  NH1 . ARG D 2 228 ? 23.507  -35.030 -25.343 1.00 41.46  ? 228 ARG D NH1 1 
ATOM   12007 N  NH2 . ARG D 2 228 ? 21.545  -34.674 -24.206 1.00 43.01  ? 228 ARG D NH2 1 
ATOM   12008 N  N   . LYS D 2 229 ? 22.111  -31.176 -28.976 1.00 44.54  ? 229 LYS D N   1 
ATOM   12009 C  CA  . LYS D 2 229 ? 23.034  -30.221 -28.371 1.00 48.36  ? 229 LYS D CA  1 
ATOM   12010 C  C   . LYS D 2 229 ? 23.378  -30.651 -26.945 1.00 45.17  ? 229 LYS D C   1 
ATOM   12011 O  O   . LYS D 2 229 ? 22.553  -31.259 -26.254 1.00 43.14  ? 229 LYS D O   1 
ATOM   12012 C  CB  . LYS D 2 229 ? 22.450  -28.808 -28.393 1.00 55.25  ? 229 LYS D CB  1 
ATOM   12013 C  CG  . LYS D 2 229 ? 22.200  -28.295 -29.829 1.00 55.49  ? 229 LYS D CG  1 
ATOM   12014 C  CD  . LYS D 2 229 ? 23.507  -27.886 -30.559 1.00 63.76  ? 229 LYS D CD  1 
ATOM   12015 C  CE  . LYS D 2 229 ? 24.514  -27.055 -29.731 1.00 71.44  ? 229 LYS D CE  1 
ATOM   12016 N  NZ  . LYS D 2 229 ? 23.948  -26.012 -28.807 1.00 68.90  ? 229 LYS D NZ  1 
ATOM   12017 N  N   . THR D 2 230 ? 24.630  -30.387 -26.522 1.00 42.51  ? 230 THR D N   1 
ATOM   12018 C  CA  . THR D 2 230 ? 25.095  -30.922 -25.234 1.00 41.29  ? 230 THR D CA  1 
ATOM   12019 C  C   . THR D 2 230 ? 24.374  -30.233 -24.069 1.00 38.01  ? 230 THR D C   1 
ATOM   12020 O  O   . THR D 2 230 ? 24.008  -30.890 -23.077 1.00 37.93  ? 230 THR D O   1 
ATOM   12021 C  CB  . THR D 2 230 ? 26.624  -30.769 -25.100 1.00 40.97  ? 230 THR D CB  1 
ATOM   12022 O  OG1 . THR D 2 230 ? 27.286  -31.406 -26.212 1.00 39.81  ? 230 THR D OG1 1 
ATOM   12023 C  CG2 . THR D 2 230 ? 27.141  -31.424 -23.795 1.00 37.68  ? 230 THR D CG2 1 
ATOM   12024 N  N   . GLY D 2 231 ? 24.135  -28.908 -24.182 1.00 44.05  ? 231 GLY D N   1 
ATOM   12025 C  CA  . GLY D 2 231 ? 23.581  -28.256 -22.997 1.00 41.86  ? 231 GLY D CA  1 
ATOM   12026 C  C   . GLY D 2 231 ? 24.537  -28.349 -21.812 1.00 38.67  ? 231 GLY D C   1 
ATOM   12027 O  O   . GLY D 2 231 ? 25.745  -28.648 -21.947 1.00 42.23  ? 231 GLY D O   1 
ATOM   12028 N  N   . ALA D 2 232 ? 23.976  -28.150 -20.618 1.00 41.13  ? 232 ALA D N   1 
ATOM   12029 C  CA  . ALA D 2 232 ? 24.792  -28.198 -19.407 1.00 38.52  ? 232 ALA D CA  1 
ATOM   12030 C  C   . ALA D 2 232 ? 25.346  -29.586 -19.177 1.00 36.31  ? 232 ALA D C   1 
ATOM   12031 O  O   . ALA D 2 232 ? 24.667  -30.582 -19.430 1.00 38.23  ? 232 ALA D O   1 
ATOM   12032 C  CB  . ALA D 2 232 ? 23.993  -27.800 -18.171 1.00 38.48  ? 232 ALA D CB  1 
ATOM   12033 N  N   . ARG D 2 233 ? 26.572  -29.638 -18.650 1.00 35.43  ? 233 ARG D N   1 
ATOM   12034 C  CA  . ARG D 2 233 ? 27.262  -30.896 -18.371 1.00 32.28  ? 233 ARG D CA  1 
ATOM   12035 C  C   . ARG D 2 233 ? 26.973  -31.295 -16.923 1.00 33.98  ? 233 ARG D C   1 
ATOM   12036 O  O   . ARG D 2 233 ? 27.492  -30.669 -15.971 1.00 36.03  ? 233 ARG D O   1 
ATOM   12037 C  CB  . ARG D 2 233 ? 28.762  -30.742 -18.615 1.00 35.27  ? 233 ARG D CB  1 
ATOM   12038 C  CG  . ARG D 2 233 ? 29.102  -30.280 -20.079 1.00 35.23  ? 233 ARG D CG  1 
ATOM   12039 C  CD  . ARG D 2 233 ? 30.636  -30.138 -20.291 1.00 35.99  ? 233 ARG D CD  1 
ATOM   12040 N  NE  . ARG D 2 233 ? 31.343  -31.405 -20.118 1.00 36.48  ? 233 ARG D NE  1 
ATOM   12041 C  CZ  . ARG D 2 233 ? 31.521  -32.305 -21.086 1.00 35.40  ? 233 ARG D CZ  1 
ATOM   12042 N  NH1 . ARG D 2 233 ? 31.060  -32.099 -22.305 1.00 36.91  ? 233 ARG D NH1 1 
ATOM   12043 N  NH2 . ARG D 2 233 ? 32.154  -33.456 -20.813 1.00 34.76  ? 233 ARG D NH2 1 
ATOM   12044 N  N   . PHE D 2 234 ? 26.112  -32.291 -16.735 1.00 30.20  ? 234 PHE D N   1 
ATOM   12045 C  CA  . PHE D 2 234 ? 25.719  -32.701 -15.378 1.00 29.97  ? 234 PHE D CA  1 
ATOM   12046 C  C   . PHE D 2 234 ? 26.488  -33.946 -14.926 1.00 33.36  ? 234 PHE D C   1 
ATOM   12047 O  O   . PHE D 2 234 ? 26.977  -34.748 -15.735 1.00 30.67  ? 234 PHE D O   1 
ATOM   12048 C  CB  . PHE D 2 234 ? 24.227  -33.031 -15.305 1.00 32.07  ? 234 PHE D CB  1 
ATOM   12049 C  CG  . PHE D 2 234 ? 23.313  -31.838 -15.238 1.00 35.23  ? 234 PHE D CG  1 
ATOM   12050 C  CD1 . PHE D 2 234 ? 23.784  -30.577 -14.898 1.00 34.75  ? 234 PHE D CD1 1 
ATOM   12051 C  CD2 . PHE D 2 234 ? 21.973  -31.982 -15.537 1.00 36.01  ? 234 PHE D CD2 1 
ATOM   12052 C  CE1 . PHE D 2 234 ? 22.936  -29.502 -14.852 1.00 37.24  ? 234 PHE D CE1 1 
ATOM   12053 C  CE2 . PHE D 2 234 ? 21.108  -30.901 -15.477 1.00 41.33  ? 234 PHE D CE2 1 
ATOM   12054 C  CZ  . PHE D 2 234 ? 21.595  -29.662 -15.136 1.00 42.59  ? 234 PHE D CZ  1 
ATOM   12055 N  N   . MET D 2 235 ? 26.600  -34.118 -13.614 1.00 28.95  ? 235 MET D N   1 
ATOM   12056 C  CA  . MET D 2 235 ? 27.023  -35.382 -13.078 1.00 27.65  ? 235 MET D CA  1 
ATOM   12057 C  C   . MET D 2 235 ? 25.910  -35.862 -12.162 1.00 29.18  ? 235 MET D C   1 
ATOM   12058 O  O   . MET D 2 235 ? 25.245  -35.047 -11.526 1.00 31.80  ? 235 MET D O   1 
ATOM   12059 C  CB  . MET D 2 235 ? 28.330  -35.212 -12.314 1.00 31.53  ? 235 MET D CB  1 
ATOM   12060 C  CG  . MET D 2 235 ? 28.703  -36.351 -11.349 1.00 29.00  ? 235 MET D CG  1 
ATOM   12061 S  SD  . MET D 2 235 ? 30.278  -35.825 -10.574 1.00 31.85  ? 235 MET D SD  1 
ATOM   12062 C  CE  . MET D 2 235 ? 31.023  -37.404 -10.224 1.00 26.73  ? 235 MET D CE  1 
ATOM   12063 N  N   . THR D 2 236 ? 25.680  -37.169 -12.098 1.00 28.09  ? 236 THR D N   1 
ATOM   12064 C  CA  . THR D 2 236 ? 24.736  -37.696 -11.123 1.00 27.02  ? 236 THR D CA  1 
ATOM   12065 C  C   . THR D 2 236 ? 25.482  -38.449 -10.027 1.00 30.48  ? 236 THR D C   1 
ATOM   12066 O  O   . THR D 2 236 ? 26.484  -39.118 -10.283 1.00 28.57  ? 236 THR D O   1 
ATOM   12067 C  CB  . THR D 2 236 ? 23.645  -38.603 -11.766 1.00 25.99  ? 236 THR D CB  1 
ATOM   12068 O  OG1 . THR D 2 236 ? 24.254  -39.619 -12.553 1.00 27.46  ? 236 THR D OG1 1 
ATOM   12069 C  CG2 . THR D 2 236 ? 22.732  -37.792 -12.735 1.00 30.24  ? 236 THR D CG2 1 
ATOM   12070 N  N   . ILE D 2 237 ? 24.994  -38.323 -8.804  1.00 24.22  ? 237 ILE D N   1 
ATOM   12071 C  CA  . ILE D 2 237 ? 25.655  -38.898 -7.629  1.00 25.42  ? 237 ILE D CA  1 
ATOM   12072 C  C   . ILE D 2 237 ? 24.616  -39.635 -6.809  1.00 27.04  ? 237 ILE D C   1 
ATOM   12073 O  O   . ILE D 2 237 ? 23.515  -39.124 -6.575  1.00 27.95  ? 237 ILE D O   1 
ATOM   12074 C  CB  . ILE D 2 237 ? 26.347  -37.820 -6.765  1.00 25.86  ? 237 ILE D CB  1 
ATOM   12075 C  CG1 . ILE D 2 237 ? 27.397  -37.089 -7.596  1.00 26.38  ? 237 ILE D CG1 1 
ATOM   12076 C  CG2 . ILE D 2 237 ? 27.061  -38.461 -5.571  1.00 26.60  ? 237 ILE D CG2 1 
ATOM   12077 C  CD1 . ILE D 2 237 ? 27.911  -35.746 -6.957  1.00 28.37  ? 237 ILE D CD1 1 
ATOM   12078 N  N   . GLY D 2 238 ? 24.952  -40.833 -6.373  1.00 26.72  ? 238 GLY D N   1 
ATOM   12079 C  CA  . GLY D 2 238 ? 23.969  -41.572 -5.611  1.00 24.72  ? 238 GLY D CA  1 
ATOM   12080 C  C   . GLY D 2 238 ? 24.457  -42.950 -5.249  1.00 27.39  ? 238 GLY D C   1 
ATOM   12081 O  O   . GLY D 2 238 ? 25.612  -43.326 -5.480  1.00 25.80  ? 238 GLY D O   1 
ATOM   12082 N  N   . SER D 2 239 ? 23.531  -43.705 -4.674  1.00 25.53  ? 239 SER D N   1 
ATOM   12083 C  CA  . SER D 2 239 ? 23.816  -45.090 -4.353  1.00 28.25  ? 239 SER D CA  1 
ATOM   12084 C  C   . SER D 2 239 ? 23.689  -45.918 -5.629  1.00 28.49  ? 239 SER D C   1 
ATOM   12085 O  O   . SER D 2 239 ? 24.702  -46.187 -6.272  1.00 26.71  ? 239 SER D O   1 
ATOM   12086 C  CB  . SER D 2 239 ? 22.904  -45.554 -3.211  1.00 25.84  ? 239 SER D CB  1 
ATOM   12087 O  OG  . SER D 2 239 ? 21.531  -45.499 -3.573  1.00 25.19  ? 239 SER D OG  1 
ATOM   12088 N  N   . GLU D 2 240 ? 22.474  -46.339 -6.008  1.00 27.34  ? 240 GLU D N   1 
ATOM   12089 C  CA  . GLU D 2 240 ? 22.346  -47.172 -7.189  1.00 29.49  ? 240 GLU D CA  1 
ATOM   12090 C  C   . GLU D 2 240 ? 22.074  -46.339 -8.450  1.00 32.40  ? 240 GLU D C   1 
ATOM   12091 O  O   . GLU D 2 240 ? 22.833  -46.411 -9.419  1.00 31.62  ? 240 GLU D O   1 
ATOM   12092 C  CB  . GLU D 2 240 ? 21.299  -48.258 -6.943  1.00 33.42  ? 240 GLU D CB  1 
ATOM   12093 C  CG  . GLU D 2 240 ? 20.790  -48.833 -8.249  1.00 37.24  ? 240 GLU D CG  1 
ATOM   12094 C  CD  . GLU D 2 240 ? 21.814  -49.781 -8.870  1.00 38.50  ? 240 GLU D CD  1 
ATOM   12095 O  OE1 . GLU D 2 240 ? 22.843  -50.091 -8.209  1.00 40.14  ? 240 GLU D OE1 1 
ATOM   12096 O  OE2 . GLU D 2 240 ? 21.615  -50.198 -10.043 1.00 39.98  ? 240 GLU D OE2 1 
ATOM   12097 N  N   . ASN D 2 241 ? 21.032  -45.500 -8.419  1.00 29.97  ? 241 ASN D N   1 
ATOM   12098 C  CA  . ASN D 2 241 ? 20.650  -44.614 -9.520  1.00 28.31  ? 241 ASN D CA  1 
ATOM   12099 C  C   . ASN D 2 241 ? 20.414  -45.431 -10.796 1.00 30.92  ? 241 ASN D C   1 
ATOM   12100 O  O   . ASN D 2 241 ? 21.047  -45.234 -11.833 1.00 33.35  ? 241 ASN D O   1 
ATOM   12101 C  CB  . ASN D 2 241 ? 21.725  -43.557 -9.780  1.00 28.68  ? 241 ASN D CB  1 
ATOM   12102 C  CG  . ASN D 2 241 ? 21.718  -42.468 -8.721  1.00 30.34  ? 241 ASN D CG  1 
ATOM   12103 O  OD1 . ASN D 2 241 ? 20.788  -42.406 -7.905  1.00 29.75  ? 241 ASN D OD1 1 
ATOM   12104 N  ND2 . ASN D 2 241 ? 22.700  -41.540 -8.799  1.00 32.26  ? 241 ASN D ND2 1 
ATOM   12105 N  N   . ASP D 2 242 ? 19.498  -46.374 -10.705 1.00 35.44  ? 242 ASP D N   1 
ATOM   12106 C  CA  . ASP D 2 242 ? 19.224  -47.214 -11.853 1.00 38.26  ? 242 ASP D CA  1 
ATOM   12107 C  C   . ASP D 2 242 ? 17.923  -46.847 -12.542 1.00 38.20  ? 242 ASP D C   1 
ATOM   12108 O  O   . ASP D 2 242 ? 17.455  -47.632 -13.360 1.00 39.52  ? 242 ASP D O   1 
ATOM   12109 C  CB  . ASP D 2 242 ? 19.181  -48.693 -11.481 1.00 33.61  ? 242 ASP D CB  1 
ATOM   12110 C  CG  . ASP D 2 242 ? 18.161  -48.989 -10.408 1.00 39.62  ? 242 ASP D CG  1 
ATOM   12111 O  OD1 . ASP D 2 242 ? 17.588  -48.043 -9.832  1.00 40.71  ? 242 ASP D OD1 1 
ATOM   12112 O  OD2 . ASP D 2 242 ? 17.842  -50.171 -10.206 1.00 45.30  ? 242 ASP D OD2 1 
ATOM   12113 N  N   . ASP D 2 243 ? 17.310  -45.705 -12.211 1.00 36.64  ? 243 ASP D N   1 
ATOM   12114 C  CA  . ASP D 2 243 ? 16.088  -45.292 -12.915 1.00 41.51  ? 243 ASP D CA  1 
ATOM   12115 C  C   . ASP D 2 243 ? 16.444  -44.608 -14.238 1.00 37.03  ? 243 ASP D C   1 
ATOM   12116 O  O   . ASP D 2 243 ? 16.589  -43.390 -14.302 1.00 35.80  ? 243 ASP D O   1 
ATOM   12117 C  CB  . ASP D 2 243 ? 15.234  -44.384 -12.033 1.00 39.58  ? 243 ASP D CB  1 
ATOM   12118 C  CG  . ASP D 2 243 ? 13.814  -44.180 -12.589 1.00 44.01  ? 243 ASP D CG  1 
ATOM   12119 O  OD1 . ASP D 2 243 ? 13.589  -44.425 -13.800 1.00 41.97  ? 243 ASP D OD1 1 
ATOM   12120 O  OD2 . ASP D 2 243 ? 12.931  -43.753 -11.815 1.00 51.71  ? 243 ASP D OD2 1 
ATOM   12121 N  N   . ILE D 2 244 ? 16.540  -45.399 -15.317 1.00 40.19  ? 244 ILE D N   1 
ATOM   12122 C  CA  . ILE D 2 244 ? 16.897  -44.862 -16.639 1.00 39.30  ? 244 ILE D CA  1 
ATOM   12123 C  C   . ILE D 2 244 ? 15.914  -43.786 -17.088 1.00 41.08  ? 244 ILE D C   1 
ATOM   12124 O  O   . ILE D 2 244 ? 16.305  -42.786 -17.709 1.00 41.52  ? 244 ILE D O   1 
ATOM   12125 C  CB  . ILE D 2 244 ? 16.938  -45.973 -17.708 1.00 45.38  ? 244 ILE D CB  1 
ATOM   12126 C  CG1 . ILE D 2 244 ? 17.591  -47.241 -17.200 1.00 45.31  ? 244 ILE D CG1 1 
ATOM   12127 C  CG2 . ILE D 2 244 ? 17.614  -45.456 -19.019 1.00 43.77  ? 244 ILE D CG2 1 
ATOM   12128 C  CD1 . ILE D 2 244 ? 19.050  -47.144 -17.001 1.00 45.96  ? 244 ILE D CD1 1 
ATOM   12129 N  N   . ALA D 2 245 ? 14.614  -44.012 -16.864 1.00 42.69  ? 245 ALA D N   1 
ATOM   12130 C  CA  . ALA D 2 245 ? 13.618  -43.073 -17.373 1.00 41.19  ? 245 ALA D CA  1 
ATOM   12131 C  C   . ALA D 2 245 ? 13.730  -41.717 -16.694 1.00 42.53  ? 245 ALA D C   1 
ATOM   12132 O  O   . ALA D 2 245 ? 13.520  -40.668 -17.328 1.00 41.77  ? 245 ALA D O   1 
ATOM   12133 C  CB  . ALA D 2 245 ? 12.213  -43.640 -17.202 1.00 45.97  ? 245 ALA D CB  1 
ATOM   12134 N  N   . PHE D 2 246 ? 14.061  -41.710 -15.410 1.00 41.91  ? 246 PHE D N   1 
ATOM   12135 C  CA  . PHE D 2 246 ? 14.356  -40.441 -14.764 1.00 40.37  ? 246 PHE D CA  1 
ATOM   12136 C  C   . PHE D 2 246 ? 15.553  -39.768 -15.429 1.00 39.35  ? 246 PHE D C   1 
ATOM   12137 O  O   . PHE D 2 246 ? 15.516  -38.566 -15.723 1.00 40.41  ? 246 PHE D O   1 
ATOM   12138 C  CB  . PHE D 2 246 ? 14.613  -40.648 -13.263 1.00 41.21  ? 246 PHE D CB  1 
ATOM   12139 C  CG  . PHE D 2 246 ? 14.980  -39.372 -12.548 1.00 37.95  ? 246 PHE D CG  1 
ATOM   12140 C  CD1 . PHE D 2 246 ? 13.992  -38.551 -12.029 1.00 45.87  ? 246 PHE D CD1 1 
ATOM   12141 C  CD2 . PHE D 2 246 ? 16.305  -38.956 -12.462 1.00 39.64  ? 246 PHE D CD2 1 
ATOM   12142 C  CE1 . PHE D 2 246 ? 14.310  -37.375 -11.410 1.00 44.28  ? 246 PHE D CE1 1 
ATOM   12143 C  CE2 . PHE D 2 246 ? 16.625  -37.764 -11.842 1.00 40.07  ? 246 PHE D CE2 1 
ATOM   12144 C  CZ  . PHE D 2 246 ? 15.631  -36.980 -11.321 1.00 44.90  ? 246 PHE D CZ  1 
ATOM   12145 N  N   . MET D 2 247 ? 16.603  -40.543 -15.721 1.00 37.62  ? 247 MET D N   1 
ATOM   12146 C  CA  . MET D 2 247 ? 17.811  -39.965 -16.286 1.00 37.84  ? 247 MET D CA  1 
ATOM   12147 C  C   . MET D 2 247 ? 17.525  -39.383 -17.663 1.00 38.20  ? 247 MET D C   1 
ATOM   12148 O  O   . MET D 2 247 ? 18.084  -38.346 -18.039 1.00 39.28  ? 247 MET D O   1 
ATOM   12149 C  CB  . MET D 2 247 ? 18.908  -41.018 -16.423 1.00 34.55  ? 247 MET D CB  1 
ATOM   12150 C  CG  . MET D 2 247 ? 19.301  -41.651 -15.103 1.00 39.86  ? 247 MET D CG  1 
ATOM   12151 S  SD  . MET D 2 247 ? 19.901  -40.459 -13.883 1.00 39.42  ? 247 MET D SD  1 
ATOM   12152 C  CE  . MET D 2 247 ? 20.398  -41.671 -12.635 1.00 34.20  ? 247 MET D CE  1 
ATOM   12153 N  N   . GLY D 2 248 ? 16.670  -40.066 -18.444 1.00 39.68  ? 248 GLY D N   1 
ATOM   12154 C  CA  . GLY D 2 248 ? 16.286  -39.552 -19.739 1.00 37.94  ? 248 GLY D CA  1 
ATOM   12155 C  C   . GLY D 2 248 ? 15.545  -38.238 -19.642 1.00 40.02  ? 248 GLY D C   1 
ATOM   12156 O  O   . GLY D 2 248 ? 15.639  -37.400 -20.540 1.00 40.36  ? 248 GLY D O   1 
ATOM   12157 N  N   . MET D 2 249 ? 14.804  -38.032 -18.546 1.00 41.72  ? 249 MET D N   1 
ATOM   12158 C  CA  . MET D 2 249 ? 14.084  -36.769 -18.394 1.00 44.49  ? 249 MET D CA  1 
ATOM   12159 C  C   . MET D 2 249 ? 15.091  -35.650 -18.127 1.00 42.71  ? 249 MET D C   1 
ATOM   12160 O  O   . MET D 2 249 ? 14.981  -34.554 -18.696 1.00 43.52  ? 249 MET D O   1 
ATOM   12161 C  CB  . MET D 2 249 ? 13.088  -36.858 -17.235 1.00 42.66  ? 249 MET D CB  1 
ATOM   12162 C  CG  . MET D 2 249 ? 12.589  -35.468 -16.705 1.00 47.55  ? 249 MET D CG  1 
ATOM   12163 S  SD  . MET D 2 249 ? 13.642  -34.516 -15.572 1.00 44.66  ? 249 MET D SD  1 
ATOM   12164 C  CE  . MET D 2 249 ? 13.351  -35.251 -13.944 1.00 45.87  ? 249 MET D CE  1 
ATOM   12165 N  N   . VAL D 2 250 ? 16.111  -35.945 -17.300 1.00 40.69  ? 250 VAL D N   1 
ATOM   12166 C  CA  . VAL D 2 250 ? 17.197  -34.997 -17.028 1.00 44.60  ? 250 VAL D CA  1 
ATOM   12167 C  C   . VAL D 2 250 ? 17.847  -34.524 -18.324 1.00 42.20  ? 250 VAL D C   1 
ATOM   12168 O  O   . VAL D 2 250 ? 17.981  -33.320 -18.558 1.00 46.54  ? 250 VAL D O   1 
ATOM   12169 C  CB  . VAL D 2 250 ? 18.235  -35.617 -16.076 1.00 41.70  ? 250 VAL D CB  1 
ATOM   12170 C  CG1 . VAL D 2 250 ? 19.441  -34.697 -15.934 1.00 42.60  ? 250 VAL D CG1 1 
ATOM   12171 C  CG2 . VAL D 2 250 ? 17.641  -35.860 -14.691 1.00 39.36  ? 250 VAL D CG2 1 
ATOM   12172 N  N   . GLU D 2 251 ? 18.211  -35.460 -19.219 1.00 41.19  ? 251 GLU D N   1 
ATOM   12173 C  CA  . GLU D 2 251 ? 18.889  -35.094 -20.462 1.00 36.93  ? 251 GLU D CA  1 
ATOM   12174 C  C   . GLU D 2 251 ? 17.976  -34.479 -21.499 1.00 44.96  ? 251 GLU D C   1 
ATOM   12175 O  O   . GLU D 2 251 ? 18.472  -34.078 -22.556 1.00 54.69  ? 251 GLU D O   1 
ATOM   12176 C  CB  . GLU D 2 251 ? 19.591  -36.318 -21.081 1.00 37.22  ? 251 GLU D CB  1 
ATOM   12177 C  CG  . GLU D 2 251 ? 20.708  -36.841 -20.183 1.00 36.64  ? 251 GLU D CG  1 
ATOM   12178 C  CD  . GLU D 2 251 ? 21.689  -37.762 -20.894 1.00 37.91  ? 251 GLU D CD  1 
ATOM   12179 O  OE1 . GLU D 2 251 ? 21.223  -38.703 -21.570 1.00 36.34  ? 251 GLU D OE1 1 
ATOM   12180 O  OE2 . GLU D 2 251 ? 22.925  -37.593 -20.697 1.00 36.38  ? 251 GLU D OE2 1 
ATOM   12181 N  N   . SER D 2 252 ? 16.667  -34.425 -21.260 1.00 44.30  ? 252 SER D N   1 
ATOM   12182 C  CA  . SER D 2 252 ? 15.769  -33.782 -22.202 1.00 44.50  ? 252 SER D CA  1 
ATOM   12183 C  C   . SER D 2 252 ? 15.477  -32.334 -21.832 1.00 44.27  ? 252 SER D C   1 
ATOM   12184 O  O   . SER D 2 252 ? 14.861  -31.631 -22.631 1.00 47.38  ? 252 SER D O   1 
ATOM   12185 C  CB  . SER D 2 252 ? 14.440  -34.539 -22.290 1.00 48.63  ? 252 SER D CB  1 
ATOM   12186 O  OG  . SER D 2 252 ? 13.696  -34.389 -21.093 1.00 49.23  ? 252 SER D OG  1 
ATOM   12187 N  N   . VAL D 2 253 ? 15.884  -31.884 -20.638 1.00 45.95  ? 253 VAL D N   1 
ATOM   12188 C  CA  . VAL D 2 253 ? 15.677  -30.488 -20.250 1.00 49.46  ? 253 VAL D CA  1 
ATOM   12189 C  C   . VAL D 2 253 ? 16.678  -29.543 -20.903 1.00 44.49  ? 253 VAL D C   1 
ATOM   12190 O  O   . VAL D 2 253 ? 16.441  -28.332 -20.942 1.00 47.74  ? 253 VAL D O   1 
ATOM   12191 C  CB  . VAL D 2 253 ? 15.735  -30.315 -18.719 1.00 44.23  ? 253 VAL D CB  1 
ATOM   12192 C  CG1 . VAL D 2 253 ? 15.007  -31.425 -18.015 1.00 48.06  ? 253 VAL D CG1 1 
ATOM   12193 C  CG2 . VAL D 2 253 ? 17.168  -30.241 -18.222 1.00 47.69  ? 253 VAL D CG2 1 
ATOM   12194 N  N   . GLY D 2 254 ? 17.772  -30.063 -21.446 1.00 41.86  ? 254 GLY D N   1 
ATOM   12195 C  CA  . GLY D 2 254 ? 18.811  -29.225 -22.006 1.00 44.05  ? 254 GLY D CA  1 
ATOM   12196 C  C   . GLY D 2 254 ? 20.157  -29.495 -21.373 1.00 43.34  ? 254 GLY D C   1 
ATOM   12197 O  O   . GLY D 2 254 ? 20.892  -28.581 -20.992 1.00 42.53  ? 254 GLY D O   1 
ATOM   12198 N  N   . ALA D 2 255 ? 20.495  -30.767 -21.242 1.00 43.11  ? 255 ALA D N   1 
ATOM   12199 C  CA  . ALA D 2 255 ? 21.667  -31.113 -20.465 1.00 35.59  ? 255 ALA D CA  1 
ATOM   12200 C  C   . ALA D 2 255 ? 22.129  -32.473 -20.929 1.00 38.89  ? 255 ALA D C   1 
ATOM   12201 O  O   . ALA D 2 255 ? 21.406  -33.199 -21.615 1.00 39.11  ? 255 ALA D O   1 
ATOM   12202 C  CB  . ALA D 2 255 ? 21.359  -31.117 -18.958 1.00 39.24  ? 255 ALA D CB  1 
ATOM   12203 N  N   . THR D 2 256 ? 23.345  -32.809 -20.544 1.00 34.57  ? 256 THR D N   1 
ATOM   12204 C  CA  . THR D 2 256 ? 23.871  -34.150 -20.768 1.00 34.04  ? 256 THR D CA  1 
ATOM   12205 C  C   . THR D 2 256 ? 24.521  -34.599 -19.476 1.00 35.34  ? 256 THR D C   1 
ATOM   12206 O  O   . THR D 2 256 ? 25.297  -33.852 -18.873 1.00 35.37  ? 256 THR D O   1 
ATOM   12207 C  CB  . THR D 2 256 ? 24.894  -34.174 -21.920 1.00 36.33  ? 256 THR D CB  1 
ATOM   12208 O  OG1 . THR D 2 256 ? 24.317  -33.619 -23.108 1.00 36.70  ? 256 THR D OG1 1 
ATOM   12209 C  CG2 . THR D 2 256 ? 25.391  -35.592 -22.209 1.00 34.54  ? 256 THR D CG2 1 
ATOM   12210 N  N   . ILE D 2 257 ? 24.234  -35.827 -19.053 1.00 32.26  ? 257 ILE D N   1 
ATOM   12211 C  CA  . ILE D 2 257 ? 24.931  -36.398 -17.910 1.00 30.22  ? 257 ILE D CA  1 
ATOM   12212 C  C   . ILE D 2 257 ? 26.253  -36.947 -18.444 1.00 31.09  ? 257 ILE D C   1 
ATOM   12213 O  O   . ILE D 2 257 ? 26.267  -37.927 -19.206 1.00 31.74  ? 257 ILE D O   1 
ATOM   12214 C  CB  . ILE D 2 257 ? 24.101  -37.497 -17.246 1.00 32.04  ? 257 ILE D CB  1 
ATOM   12215 C  CG1 . ILE D 2 257 ? 22.773  -36.913 -16.740 1.00 34.52  ? 257 ILE D CG1 1 
ATOM   12216 C  CG2 . ILE D 2 257 ? 24.944  -38.127 -16.171 1.00 30.67  ? 257 ILE D CG2 1 
ATOM   12217 C  CD1 . ILE D 2 257 ? 21.685  -37.957 -16.496 1.00 35.80  ? 257 ILE D CD1 1 
ATOM   12218 N  N   . VAL D 2 258 ? 27.371  -36.309 -18.076 1.00 29.70  ? 258 VAL D N   1 
ATOM   12219 C  CA  . VAL D 2 258 ? 28.656  -36.692 -18.667 1.00 28.82  ? 258 VAL D CA  1 
ATOM   12220 C  C   . VAL D 2 258 ? 29.507  -37.575 -17.773 1.00 32.95  ? 258 VAL D C   1 
ATOM   12221 O  O   . VAL D 2 258 ? 30.521  -38.116 -18.250 1.00 27.66  ? 258 VAL D O   1 
ATOM   12222 C  CB  . VAL D 2 258 ? 29.474  -35.444 -19.106 1.00 30.64  ? 258 VAL D CB  1 
ATOM   12223 C  CG1 . VAL D 2 258 ? 28.735  -34.606 -20.194 1.00 33.39  ? 258 VAL D CG1 1 
ATOM   12224 C  CG2 . VAL D 2 258 ? 29.748  -34.566 -17.845 1.00 30.43  ? 258 VAL D CG2 1 
ATOM   12225 N  N   . ILE D 2 259 ? 29.134  -37.756 -16.503 1.00 27.16  ? 259 ILE D N   1 
ATOM   12226 C  CA  . ILE D 2 259 ? 29.854  -38.629 -15.583 1.00 27.71  ? 259 ILE D CA  1 
ATOM   12227 C  C   . ILE D 2 259 ? 28.928  -38.862 -14.408 1.00 27.64  ? 259 ILE D C   1 
ATOM   12228 O  O   . ILE D 2 259 ? 27.905  -38.188 -14.258 1.00 25.68  ? 259 ILE D O   1 
ATOM   12229 C  CB  . ILE D 2 259 ? 31.214  -38.024 -15.187 1.00 28.68  ? 259 ILE D CB  1 
ATOM   12230 C  CG1 . ILE D 2 259 ? 32.144  -39.040 -14.510 1.00 24.98  ? 259 ILE D CG1 1 
ATOM   12231 C  CG2 . ILE D 2 259 ? 31.035  -36.764 -14.352 1.00 28.65  ? 259 ILE D CG2 1 
ATOM   12232 C  CD1 . ILE D 2 259 ? 32.223  -40.383 -15.237 1.00 28.20  ? 259 ILE D CD1 1 
ATOM   12233 N  N   . ASP D 2 260 ? 29.250  -39.844 -13.588 1.00 25.47  ? 260 ASP D N   1 
ATOM   12234 C  CA  . ASP D 2 260 ? 28.353  -40.261 -12.527 1.00 29.05  ? 260 ASP D CA  1 
ATOM   12235 C  C   . ASP D 2 260 ? 29.219  -40.869 -11.432 1.00 25.38  ? 260 ASP D C   1 
ATOM   12236 O  O   . ASP D 2 260 ? 30.346  -41.326 -11.679 1.00 25.54  ? 260 ASP D O   1 
ATOM   12237 C  CB  . ASP D 2 260 ? 27.328  -41.290 -13.049 1.00 27.16  ? 260 ASP D CB  1 
ATOM   12238 C  CG  . ASP D 2 260 ? 28.007  -42.580 -13.537 1.00 29.22  ? 260 ASP D CG  1 
ATOM   12239 O  OD1 . ASP D 2 260 ? 28.189  -43.486 -12.711 1.00 31.08  ? 260 ASP D OD1 1 
ATOM   12240 O  OD2 . ASP D 2 260 ? 28.423  -42.684 -14.706 1.00 30.30  ? 260 ASP D OD2 1 
ATOM   12241 N  N   . ASP D 2 261 ? 28.694  -40.852 -10.208 1.00 26.03  ? 261 ASP D N   1 
ATOM   12242 C  CA  . ASP D 2 261 ? 29.243  -41.585 -9.053  1.00 24.68  ? 261 ASP D CA  1 
ATOM   12243 C  C   . ASP D 2 261 ? 28.096  -42.418 -8.500  1.00 24.42  ? 261 ASP D C   1 
ATOM   12244 O  O   . ASP D 2 261 ? 27.348  -41.963 -7.619  1.00 22.14  ? 261 ASP D O   1 
ATOM   12245 C  CB  . ASP D 2 261 ? 29.766  -40.597 -7.973  1.00 23.78  ? 261 ASP D CB  1 
ATOM   12246 C  CG  . ASP D 2 261 ? 30.293  -41.341 -6.730  1.00 24.78  ? 261 ASP D CG  1 
ATOM   12247 O  OD1 . ASP D 2 261 ? 31.163  -42.239 -6.921  1.00 27.04  ? 261 ASP D OD1 1 
ATOM   12248 O  OD2 . ASP D 2 261 ? 29.799  -41.114 -5.600  1.00 26.09  ? 261 ASP D OD2 1 
ATOM   12249 N  N   . GLN D 2 262 ? 27.946  -43.652 -9.003  1.00 23.39  ? 262 GLN D N   1 
ATOM   12250 C  CA  . GLN D 2 262 ? 26.806  -44.478 -8.617  1.00 24.51  ? 262 GLN D CA  1 
ATOM   12251 C  C   . GLN D 2 262 ? 27.107  -45.899 -9.040  1.00 22.88  ? 262 GLN D C   1 
ATOM   12252 O  O   . GLN D 2 262 ? 27.904  -46.132 -9.962  1.00 22.49  ? 262 GLN D O   1 
ATOM   12253 C  CB  . GLN D 2 262 ? 25.478  -44.039 -9.273  1.00 25.18  ? 262 GLN D CB  1 
ATOM   12254 C  CG  . GLN D 2 262 ? 25.505  -44.165 -10.826 1.00 27.27  ? 262 GLN D CG  1 
ATOM   12255 C  CD  . GLN D 2 262 ? 24.671  -43.121 -11.565 1.00 27.81  ? 262 GLN D CD  1 
ATOM   12256 O  OE1 . GLN D 2 262 ? 24.433  -42.021 -11.074 1.00 28.57  ? 262 GLN D OE1 1 
ATOM   12257 N  NE2 . GLN D 2 262 ? 24.303  -43.436 -12.805 1.00 27.65  ? 262 GLN D NE2 1 
ATOM   12258 N  N   . CYS D 2 263 ? 26.406  -46.841 -8.382  1.00 25.14  ? 263 CYS D N   1 
ATOM   12259 C  CA  . CYS D 2 263 ? 26.689  -48.254 -8.648  1.00 26.34  ? 263 CYS D CA  1 
ATOM   12260 C  C   . CYS D 2 263 ? 25.998  -48.797 -9.892  1.00 27.09  ? 263 CYS D C   1 
ATOM   12261 O  O   . CYS D 2 263 ? 26.329  -49.914 -10.330 1.00 24.58  ? 263 CYS D O   1 
ATOM   12262 C  CB  . CYS D 2 263 ? 26.327  -49.087 -7.374  1.00 24.05  ? 263 CYS D CB  1 
ATOM   12263 S  SG  . CYS D 2 263 ? 27.676  -49.091 -6.241  1.00 22.71  ? 263 CYS D SG  1 
ATOM   12264 N  N   . SER D 2 264 ? 25.037  -48.072 -10.485 1.00 24.26  ? 264 SER D N   1 
ATOM   12265 C  CA  . SER D 2 264 ? 24.611  -48.472 -11.821 1.00 27.81  ? 264 SER D CA  1 
ATOM   12266 C  C   . SER D 2 264 ? 25.667  -48.160 -12.865 1.00 29.68  ? 264 SER D C   1 
ATOM   12267 O  O   . SER D 2 264 ? 25.580  -48.652 -14.006 1.00 26.42  ? 264 SER D O   1 
ATOM   12268 C  CB  . SER D 2 264 ? 23.322  -47.747 -12.206 1.00 30.22  ? 264 SER D CB  1 
ATOM   12269 O  OG  . SER D 2 264 ? 23.567  -46.333 -12.230 1.00 27.13  ? 264 SER D OG  1 
ATOM   12270 N  N   . GLY D 2 265 ? 26.673  -47.393 -12.472 1.00 28.10  ? 265 GLY D N   1 
ATOM   12271 C  CA  . GLY D 2 265 ? 27.620  -46.748 -13.351 1.00 24.75  ? 265 GLY D CA  1 
ATOM   12272 C  C   . GLY D 2 265 ? 29.051  -46.866 -12.844 1.00 24.98  ? 265 GLY D C   1 
ATOM   12273 O  O   . GLY D 2 265 ? 29.530  -47.949 -12.544 1.00 26.41  ? 265 GLY D O   1 
ATOM   12274 N  N   . SER D 2 266 ? 29.752  -45.755 -12.694 1.00 22.92  ? 266 SER D N   1 
ATOM   12275 C  CA  . SER D 2 266 ? 31.210  -45.795 -12.450 1.00 22.42  ? 266 SER D CA  1 
ATOM   12276 C  C   . SER D 2 266 ? 31.628  -46.639 -11.248 1.00 26.52  ? 266 SER D C   1 
ATOM   12277 O  O   . SER D 2 266 ? 32.699  -47.271 -11.289 1.00 24.44  ? 266 SER D O   1 
ATOM   12278 C  CB  . SER D 2 266 ? 31.741  -44.376 -12.263 1.00 23.94  ? 266 SER D CB  1 
ATOM   12279 O  OG  . SER D 2 266 ? 31.102  -43.831 -11.127 1.00 24.10  ? 266 SER D OG  1 
ATOM   12280 N  N   . ARG D 2 267 ? 30.871  -46.611 -10.120 1.00 24.02  ? 267 ARG D N   1 
ATOM   12281 C  CA  . ARG D 2 267 ? 31.326  -47.295 -8.916  1.00 21.03  ? 267 ARG D CA  1 
ATOM   12282 C  C   . ARG D 2 267 ? 31.312  -48.817 -9.070  1.00 24.16  ? 267 ARG D C   1 
ATOM   12283 O  O   . ARG D 2 267 ? 31.998  -49.493 -8.324  1.00 27.41  ? 267 ARG D O   1 
ATOM   12284 C  CB  . ARG D 2 267 ? 30.473  -46.890 -7.682  1.00 20.02  ? 267 ARG D CB  1 
ATOM   12285 C  CG  . ARG D 2 267 ? 31.243  -47.074 -6.378  1.00 23.56  ? 267 ARG D CG  1 
ATOM   12286 C  CD  . ARG D 2 267 ? 30.398  -46.726 -5.129  1.00 24.96  ? 267 ARG D CD  1 
ATOM   12287 N  NE  . ARG D 2 267 ? 29.953  -45.330 -5.074  1.00 20.59  ? 267 ARG D NE  1 
ATOM   12288 C  CZ  . ARG D 2 267 ? 28.689  -44.933 -5.191  1.00 24.55  ? 267 ARG D CZ  1 
ATOM   12289 N  NH1 . ARG D 2 267 ? 27.702  -45.784 -5.395  1.00 22.91  ? 267 ARG D NH1 1 
ATOM   12290 N  NH2 . ARG D 2 267 ? 28.394  -43.635 -5.097  1.00 21.18  ? 267 ARG D NH2 1 
ATOM   12291 N  N   . TYR D 2 268 ? 30.558  -49.346 -10.025 1.00 22.08  ? 268 TYR D N   1 
ATOM   12292 C  CA  . TYR D 2 268 ? 30.589  -50.790 -10.282 1.00 22.47  ? 268 TYR D CA  1 
ATOM   12293 C  C   . TYR D 2 268 ? 31.931  -51.217 -10.911 1.00 26.20  ? 268 TYR D C   1 
ATOM   12294 O  O   . TYR D 2 268 ? 32.583  -52.170 -10.445 1.00 24.84  ? 268 TYR D O   1 
ATOM   12295 C  CB  . TYR D 2 268 ? 29.406  -51.152 -11.168 1.00 22.79  ? 268 TYR D CB  1 
ATOM   12296 C  CG  . TYR D 2 268 ? 29.553  -52.519 -11.791 1.00 24.78  ? 268 TYR D CG  1 
ATOM   12297 C  CD1 . TYR D 2 268 ? 29.507  -53.657 -10.987 1.00 24.95  ? 268 TYR D CD1 1 
ATOM   12298 C  CD2 . TYR D 2 268 ? 29.649  -52.648 -13.166 1.00 26.64  ? 268 TYR D CD2 1 
ATOM   12299 C  CE1 . TYR D 2 268 ? 29.633  -54.950 -11.568 1.00 26.39  ? 268 TYR D CE1 1 
ATOM   12300 C  CE2 . TYR D 2 268 ? 29.725  -53.925 -13.764 1.00 27.74  ? 268 TYR D CE2 1 
ATOM   12301 C  CZ  . TYR D 2 268 ? 29.710  -55.048 -12.953 1.00 28.70  ? 268 TYR D CZ  1 
ATOM   12302 O  OH  . TYR D 2 268 ? 29.802  -56.277 -13.619 1.00 30.13  ? 268 TYR D OH  1 
ATOM   12303 N  N   . PHE D 2 269 ? 32.393  -50.499 -11.951 1.00 23.07  ? 269 PHE D N   1 
ATOM   12304 C  CA  . PHE D 2 269 ? 33.392  -51.044 -12.865 1.00 22.23  ? 269 PHE D CA  1 
ATOM   12305 C  C   . PHE D 2 269 ? 34.739  -50.316 -12.863 1.00 24.73  ? 269 PHE D C   1 
ATOM   12306 O  O   . PHE D 2 269 ? 35.668  -50.758 -13.552 1.00 25.47  ? 269 PHE D O   1 
ATOM   12307 C  CB  . PHE D 2 269 ? 32.824  -51.006 -14.297 1.00 23.41  ? 269 PHE D CB  1 
ATOM   12308 C  CG  . PHE D 2 269 ? 32.727  -49.609 -14.896 1.00 21.57  ? 269 PHE D CG  1 
ATOM   12309 C  CD1 . PHE D 2 269 ? 33.827  -48.984 -15.459 1.00 23.90  ? 269 PHE D CD1 1 
ATOM   12310 C  CD2 . PHE D 2 269 ? 31.479  -48.980 -14.984 1.00 25.15  ? 269 PHE D CD2 1 
ATOM   12311 C  CE1 . PHE D 2 269 ? 33.693  -47.701 -16.057 1.00 26.25  ? 269 PHE D CE1 1 
ATOM   12312 C  CE2 . PHE D 2 269 ? 31.351  -47.686 -15.548 1.00 25.42  ? 269 PHE D CE2 1 
ATOM   12313 C  CZ  . PHE D 2 269 ? 32.433  -47.087 -16.093 1.00 24.82  ? 269 PHE D CZ  1 
ATOM   12314 N  N   . TRP D 2 270 ? 34.840  -49.181 -12.163 1.00 23.65  ? 270 TRP D N   1 
ATOM   12315 C  CA  . TRP D 2 270 ? 35.869  -48.185 -12.460 1.00 23.22  ? 270 TRP D CA  1 
ATOM   12316 C  C   . TRP D 2 270 ? 37.256  -48.794 -12.645 1.00 25.05  ? 270 TRP D C   1 
ATOM   12317 O  O   . TRP D 2 270 ? 37.932  -48.479 -13.621 1.00 26.47  ? 270 TRP D O   1 
ATOM   12318 C  CB  . TRP D 2 270 ? 35.929  -47.156 -11.341 1.00 24.51  ? 270 TRP D CB  1 
ATOM   12319 C  CG  . TRP D 2 270 ? 36.567  -45.833 -11.750 1.00 24.72  ? 270 TRP D CG  1 
ATOM   12320 C  CD1 . TRP D 2 270 ? 37.703  -45.292 -11.245 1.00 22.97  ? 270 TRP D CD1 1 
ATOM   12321 C  CD2 . TRP D 2 270 ? 36.079  -44.935 -12.744 1.00 26.72  ? 270 TRP D CD2 1 
ATOM   12322 N  NE1 . TRP D 2 270 ? 37.950  -44.073 -11.850 1.00 26.18  ? 270 TRP D NE1 1 
ATOM   12323 C  CE2 . TRP D 2 270 ? 36.964  -43.839 -12.783 1.00 29.82  ? 270 TRP D CE2 1 
ATOM   12324 C  CE3 . TRP D 2 270 ? 34.979  -44.957 -13.630 1.00 28.84  ? 270 TRP D CE3 1 
ATOM   12325 C  CZ2 . TRP D 2 270 ? 36.789  -42.764 -13.660 1.00 29.19  ? 270 TRP D CZ2 1 
ATOM   12326 C  CZ3 . TRP D 2 270 ? 34.796  -43.866 -14.508 1.00 30.94  ? 270 TRP D CZ3 1 
ATOM   12327 C  CH2 . TRP D 2 270 ? 35.702  -42.793 -14.507 1.00 31.21  ? 270 TRP D CH2 1 
ATOM   12328 N  N   . ASN D 2 271 ? 37.710  -49.638 -11.700 1.00 22.31  ? 271 ASN D N   1 
ATOM   12329 C  CA  . ASN D 2 271 ? 39.095  -50.129 -11.728 1.00 21.74  ? 271 ASN D CA  1 
ATOM   12330 C  C   . ASN D 2 271 ? 39.151  -51.586 -12.166 1.00 24.23  ? 271 ASN D C   1 
ATOM   12331 O  O   . ASN D 2 271 ? 38.304  -52.386 -11.782 1.00 25.70  ? 271 ASN D O   1 
ATOM   12332 C  CB  . ASN D 2 271 ? 39.780  -49.991 -10.378 1.00 23.38  ? 271 ASN D CB  1 
ATOM   12333 C  CG  . ASN D 2 271 ? 39.089  -50.804 -9.303  1.00 23.01  ? 271 ASN D CG  1 
ATOM   12334 O  OD1 . ASN D 2 271 ? 37.852  -50.749 -9.126  1.00 22.80  ? 271 ASN D OD1 1 
ATOM   12335 N  ND2 . ASN D 2 271 ? 39.853  -51.644 -8.637  1.00 24.34  ? 271 ASN D ND2 1 
ATOM   12336 N  N   . ALA D 2 272 ? 40.102  -51.888 -13.047 1.00 22.78  ? 272 ALA D N   1 
ATOM   12337 C  CA  . ALA D 2 272 ? 40.418  -53.289 -13.358 1.00 26.59  ? 272 ALA D CA  1 
ATOM   12338 C  C   . ALA D 2 272 ? 41.414  -53.809 -12.329 1.00 23.47  ? 272 ALA D C   1 
ATOM   12339 O  O   . ALA D 2 272 ? 42.093  -53.020 -11.669 1.00 26.47  ? 272 ALA D O   1 
ATOM   12340 C  CB  . ALA D 2 272 ? 41.036  -53.387 -14.742 1.00 29.00  ? 272 ALA D CB  1 
ATOM   12341 N  N   . SER D 2 273 ? 41.537  -55.143 -12.205 1.00 22.64  ? 273 SER D N   1 
ATOM   12342 C  CA  . SER D 2 273 ? 42.508  -55.678 -11.233 1.00 20.09  ? 273 SER D CA  1 
ATOM   12343 C  C   . SER D 2 273 ? 43.950  -55.330 -11.626 1.00 23.81  ? 273 SER D C   1 
ATOM   12344 O  O   . SER D 2 273 ? 44.257  -54.895 -12.748 1.00 26.58  ? 273 SER D O   1 
ATOM   12345 C  CB  . SER D 2 273 ? 42.385  -57.217 -11.093 1.00 22.56  ? 273 SER D CB  1 
ATOM   12346 O  OG  . SER D 2 273 ? 42.941  -57.787 -12.291 1.00 25.00  ? 273 SER D OG  1 
ATOM   12347 N  N   . LYS D 2 274 ? 44.792  -55.467 -10.707 1.00 23.18  ? 274 LYS D N   1 
ATOM   12348 C  CA  . LYS D 2 274 ? 46.216  -55.321 -10.969 1.00 22.38  ? 274 LYS D CA  1 
ATOM   12349 C  C   . LYS D 2 274 ? 46.793  -56.624 -11.479 1.00 26.21  ? 274 LYS D C   1 
ATOM   12350 O  O   . LYS D 2 274 ? 46.383  -57.693 -11.006 1.00 26.54  ? 274 LYS D O   1 
ATOM   12351 C  CB  . LYS D 2 274 ? 46.979  -54.945 -9.695  1.00 24.73  ? 274 LYS D CB  1 
ATOM   12352 C  CG  . LYS D 2 274 ? 46.520  -53.575 -9.098  1.00 28.32  ? 274 LYS D CG  1 
ATOM   12353 C  CD  . LYS D 2 274 ? 46.858  -52.453 -10.064 1.00 33.57  ? 274 LYS D CD  1 
ATOM   12354 C  CE  . LYS D 2 274 ? 46.339  -51.088 -9.559  1.00 38.73  ? 274 LYS D CE  1 
ATOM   12355 N  NZ  . LYS D 2 274 ? 46.569  -50.123 -10.663 1.00 37.54  ? 274 LYS D NZ  1 
ATOM   12356 N  N   . PRO D 2 275 ? 47.797  -56.537 -12.361 1.00 26.96  ? 275 PRO D N   1 
ATOM   12357 C  CA  . PRO D 2 275 ? 48.507  -57.758 -12.805 1.00 26.27  ? 275 PRO D CA  1 
ATOM   12358 C  C   . PRO D 2 275 ? 49.140  -58.403 -11.584 1.00 27.31  ? 275 PRO D C   1 
ATOM   12359 O  O   . PRO D 2 275 ? 49.716  -57.719 -10.736 1.00 25.81  ? 275 PRO D O   1 
ATOM   12360 C  CB  . PRO D 2 275 ? 49.558  -57.232 -13.797 1.00 27.53  ? 275 PRO D CB  1 
ATOM   12361 C  CG  . PRO D 2 275 ? 49.858  -55.783 -13.316 1.00 25.60  ? 275 PRO D CG  1 
ATOM   12362 C  CD  . PRO D 2 275 ? 48.478  -55.307 -12.813 1.00 23.66  ? 275 PRO D CD  1 
ATOM   12363 N  N   . GLU D 2 276 ? 48.951  -59.710 -11.459 1.00 25.44  ? 276 GLU D N   1 
ATOM   12364 C  CA  . GLU D 2 276 ? 49.249  -60.389 -10.214 1.00 26.31  ? 276 GLU D CA  1 
ATOM   12365 C  C   . GLU D 2 276 ? 49.148  -61.880 -10.459 1.00 27.22  ? 276 GLU D C   1 
ATOM   12366 O  O   . GLU D 2 276 ? 48.201  -62.338 -11.124 1.00 30.79  ? 276 GLU D O   1 
ATOM   12367 C  CB  . GLU D 2 276 ? 48.282  -59.904 -9.122  1.00 29.27  ? 276 GLU D CB  1 
ATOM   12368 C  CG  . GLU D 2 276 ? 48.166  -60.835 -7.928  1.00 28.92  ? 276 GLU D CG  1 
ATOM   12369 C  CD  . GLU D 2 276 ? 49.438  -60.895 -7.135  1.00 31.72  ? 276 GLU D CD  1 
ATOM   12370 O  OE1 . GLU D 2 276 ? 50.063  -59.841 -6.939  1.00 32.69  ? 276 GLU D OE1 1 
ATOM   12371 O  OE2 . GLU D 2 276 ? 49.848  -62.028 -6.727  1.00 32.91  ? 276 GLU D OE2 1 
ATOM   12372 N  N   . GLY D 2 277 ? 50.145  -62.635 -9.992  1.00 24.73  ? 277 GLY D N   1 
ATOM   12373 C  CA  . GLY D 2 277 ? 50.171  -64.061 -10.303 1.00 25.38  ? 277 GLY D CA  1 
ATOM   12374 C  C   . GLY D 2 277 ? 49.251  -64.902 -9.448  1.00 26.70  ? 277 GLY D C   1 
ATOM   12375 O  O   . GLY D 2 277 ? 48.889  -66.029 -9.847  1.00 30.86  ? 277 GLY D O   1 
ATOM   12376 N  N   . ASP D 2 278 ? 48.900  -64.412 -8.269  1.00 23.38  ? 278 ASP D N   1 
ATOM   12377 C  CA  . ASP D 2 278 ? 47.988  -65.132 -7.387  1.00 25.31  ? 278 ASP D CA  1 
ATOM   12378 C  C   . ASP D 2 278 ? 46.589  -64.624 -7.724  1.00 25.34  ? 278 ASP D C   1 
ATOM   12379 O  O   . ASP D 2 278 ? 46.210  -63.513 -7.319  1.00 24.38  ? 278 ASP D O   1 
ATOM   12380 C  CB  . ASP D 2 278 ? 48.340  -64.910 -5.919  1.00 27.17  ? 278 ASP D CB  1 
ATOM   12381 C  CG  . ASP D 2 278 ? 47.430  -65.696 -4.973  1.00 27.23  ? 278 ASP D CG  1 
ATOM   12382 O  OD1 . ASP D 2 278 ? 46.211  -65.914 -5.259  1.00 25.40  ? 278 ASP D OD1 1 
ATOM   12383 O  OD2 . ASP D 2 278 ? 47.887  -66.080 -3.914  1.00 27.30  ? 278 ASP D OD2 1 
ATOM   12384 N  N   . VAL D 2 279 ? 45.810  -65.435 -8.438  1.00 22.67  ? 279 VAL D N   1 
ATOM   12385 C  CA  . VAL D 2 279 ? 44.530  -64.924 -8.931  1.00 24.20  ? 279 VAL D CA  1 
ATOM   12386 C  C   . VAL D 2 279 ? 43.571  -64.566 -7.794  1.00 24.41  ? 279 VAL D C   1 
ATOM   12387 O  O   . VAL D 2 279 ? 42.808  -63.615 -7.914  1.00 22.04  ? 279 VAL D O   1 
ATOM   12388 C  CB  . VAL D 2 279 ? 43.896  -65.872 -9.948  1.00 27.01  ? 279 VAL D CB  1 
ATOM   12389 C  CG1 . VAL D 2 279 ? 43.469  -67.199 -9.341  1.00 24.45  ? 279 VAL D CG1 1 
ATOM   12390 C  CG2 . VAL D 2 279 ? 42.698  -65.200 -10.691 1.00 26.37  ? 279 VAL D CG2 1 
ATOM   12391 N  N   . ILE D 2 280 ? 43.547  -65.319 -6.700  1.00 20.46  ? 280 ILE D N   1 
ATOM   12392 C  CA  . ILE D 2 280 ? 42.658  -64.943 -5.609  1.00 21.09  ? 280 ILE D CA  1 
ATOM   12393 C  C   . ILE D 2 280 ? 43.017  -63.563 -5.067  1.00 23.21  ? 280 ILE D C   1 
ATOM   12394 O  O   . ILE D 2 280 ? 42.139  -62.754 -4.719  1.00 24.19  ? 280 ILE D O   1 
ATOM   12395 C  CB  . ILE D 2 280 ? 42.731  -65.990 -4.490  1.00 23.42  ? 280 ILE D CB  1 
ATOM   12396 C  CG1 . ILE D 2 280 ? 42.158  -67.314 -4.996  1.00 23.92  ? 280 ILE D CG1 1 
ATOM   12397 C  CG2 . ILE D 2 280 ? 41.992  -65.521 -3.197  1.00 24.26  ? 280 ILE D CG2 1 
ATOM   12398 C  CD1 . ILE D 2 280 ? 40.630  -67.210 -5.320  1.00 25.33  ? 280 ILE D CD1 1 
ATOM   12399 N  N   . LYS D 2 281 ? 44.313  -63.303 -4.897  1.00 21.37  ? 281 LYS D N   1 
ATOM   12400 C  CA  . LYS D 2 281 ? 44.730  -61.966 -4.467  1.00 23.08  ? 281 LYS D CA  1 
ATOM   12401 C  C   . LYS D 2 281 ? 44.320  -60.891 -5.463  1.00 24.52  ? 281 LYS D C   1 
ATOM   12402 O  O   . LYS D 2 281 ? 43.852  -59.809 -5.046  1.00 21.38  ? 281 LYS D O   1 
ATOM   12403 C  CB  . LYS D 2 281 ? 46.262  -61.944 -4.250  1.00 22.68  ? 281 LYS D CB  1 
ATOM   12404 C  CG  . LYS D 2 281 ? 46.823  -60.538 -3.936  1.00 25.65  ? 281 LYS D CG  1 
ATOM   12405 C  CD  . LYS D 2 281 ? 48.340  -60.659 -3.610  1.00 26.82  ? 281 LYS D CD  1 
ATOM   12406 C  CE  . LYS D 2 281 ? 48.965  -59.378 -3.113  1.00 35.19  ? 281 LYS D CE  1 
ATOM   12407 N  NZ  . LYS D 2 281 ? 49.078  -58.389 -4.226  1.00 33.47  ? 281 LYS D NZ  1 
ATOM   12408 N  N   . ALA D 2 282 ? 44.461  -61.163 -6.765  1.00 22.09  ? 282 ALA D N   1 
ATOM   12409 C  CA  . ALA D 2 282 ? 44.126  -60.157 -7.782  1.00 20.44  ? 282 ALA D CA  1 
ATOM   12410 C  C   . ALA D 2 282 ? 42.647  -59.817 -7.667  1.00 22.96  ? 282 ALA D C   1 
ATOM   12411 O  O   . ALA D 2 282 ? 42.239  -58.627 -7.697  1.00 24.40  ? 282 ALA D O   1 
ATOM   12412 C  CB  . ALA D 2 282 ? 44.472  -60.708 -9.199  1.00 20.91  ? 282 ALA D CB  1 
ATOM   12413 N  N   . ILE D 2 283 ? 41.822  -60.849 -7.447  1.00 22.17  ? 283 ILE D N   1 
ATOM   12414 C  CA  . ILE D 2 283 ? 40.377  -60.642 -7.341  1.00 20.70  ? 283 ILE D CA  1 
ATOM   12415 C  C   . ILE D 2 283 ? 40.034  -59.911 -6.073  1.00 22.93  ? 283 ILE D C   1 
ATOM   12416 O  O   . ILE D 2 283 ? 39.354  -58.883 -6.116  1.00 24.51  ? 283 ILE D O   1 
ATOM   12417 C  CB  . ILE D 2 283 ? 39.608  -61.967 -7.427  1.00 21.45  ? 283 ILE D CB  1 
ATOM   12418 C  CG1 . ILE D 2 283 ? 39.728  -62.560 -8.819  1.00 19.87  ? 283 ILE D CG1 1 
ATOM   12419 C  CG2 . ILE D 2 283 ? 38.091  -61.738 -7.157  1.00 21.56  ? 283 ILE D CG2 1 
ATOM   12420 C  CD1 . ILE D 2 283 ? 39.336  -64.103 -8.723  1.00 19.63  ? 283 ILE D CD1 1 
ATOM   12421 N  N   . ALA D 2 284 ? 40.510  -60.411 -4.923  1.00 21.22  ? 284 ALA D N   1 
ATOM   12422 C  CA  . ALA D 2 284 ? 40.097  -59.804 -3.664  1.00 21.69  ? 284 ALA D CA  1 
ATOM   12423 C  C   . ALA D 2 284 ? 40.557  -58.351 -3.608  1.00 21.61  ? 284 ALA D C   1 
ATOM   12424 O  O   . ALA D 2 284 ? 39.805  -57.467 -3.159  1.00 24.57  ? 284 ALA D O   1 
ATOM   12425 C  CB  . ALA D 2 284 ? 40.630  -60.602 -2.461  1.00 21.78  ? 284 ALA D CB  1 
ATOM   12426 N  N   . GLU D 2 285 ? 41.787  -58.065 -4.075  1.00 21.62  ? 285 GLU D N   1 
ATOM   12427 C  CA  . GLU D 2 285 ? 42.274  -56.683 -3.972  1.00 24.04  ? 285 GLU D CA  1 
ATOM   12428 C  C   . GLU D 2 285 ? 41.599  -55.754 -4.948  1.00 23.85  ? 285 GLU D C   1 
ATOM   12429 O  O   . GLU D 2 285 ? 41.507  -54.551 -4.632  1.00 21.72  ? 285 GLU D O   1 
ATOM   12430 C  CB  . GLU D 2 285 ? 43.796  -56.595 -4.137  1.00 20.59  ? 285 GLU D CB  1 
ATOM   12431 C  CG  . GLU D 2 285 ? 44.421  -57.436 -3.003  1.00 23.68  ? 285 GLU D CG  1 
ATOM   12432 C  CD  . GLU D 2 285 ? 45.916  -57.251 -2.841  1.00 29.92  ? 285 GLU D CD  1 
ATOM   12433 O  OE1 . GLU D 2 285 ? 46.584  -56.745 -3.782  1.00 30.26  ? 285 GLU D OE1 1 
ATOM   12434 O  OE2 . GLU D 2 285 ? 46.429  -57.657 -1.765  1.00 27.46  ? 285 GLU D OE2 1 
ATOM   12435 N  N   . ARG D 2 286 ? 41.175  -56.251 -6.129  1.00 23.83  ? 286 ARG D N   1 
ATOM   12436 C  CA  . ARG D 2 286 ? 40.402  -55.414 -7.039  1.00 22.19  ? 286 ARG D CA  1 
ATOM   12437 C  C   . ARG D 2 286 ? 39.248  -54.782 -6.286  1.00 26.66  ? 286 ARG D C   1 
ATOM   12438 O  O   . ARG D 2 286 ? 39.008  -53.584 -6.428  1.00 24.69  ? 286 ARG D O   1 
ATOM   12439 C  CB  . ARG D 2 286 ? 39.896  -56.200 -8.265  1.00 26.17  ? 286 ARG D CB  1 
ATOM   12440 C  CG  . ARG D 2 286 ? 39.203  -55.318 -9.277  1.00 23.23  ? 286 ARG D CG  1 
ATOM   12441 C  CD  . ARG D 2 286 ? 37.734  -55.254 -9.066  1.00 21.82  ? 286 ARG D CD  1 
ATOM   12442 N  NE  . ARG D 2 286 ? 37.148  -54.163 -9.831  1.00 25.20  ? 286 ARG D NE  1 
ATOM   12443 C  CZ  . ARG D 2 286 ? 35.867  -53.799 -9.799  1.00 23.15  ? 286 ARG D CZ  1 
ATOM   12444 N  NH1 . ARG D 2 286 ? 34.981  -54.438 -9.056  1.00 23.47  ? 286 ARG D NH1 1 
ATOM   12445 N  NH2 . ARG D 2 286 ? 35.492  -52.710 -10.463 1.00 20.42  ? 286 ARG D NH2 1 
ATOM   12446 N  N   . TYR D 2 287 ? 38.521  -55.574 -5.467  1.00 23.04  ? 287 TYR D N   1 
ATOM   12447 C  CA  . TYR D 2 287 ? 37.343  -55.032 -4.800  1.00 18.72  ? 287 TYR D CA  1 
ATOM   12448 C  C   . TYR D 2 287 ? 37.735  -54.155 -3.609  1.00 21.02  ? 287 TYR D C   1 
ATOM   12449 O  O   . TYR D 2 287 ? 37.081  -53.126 -3.349  1.00 23.04  ? 287 TYR D O   1 
ATOM   12450 C  CB  . TYR D 2 287 ? 36.446  -56.155 -4.338  1.00 20.10  ? 287 TYR D CB  1 
ATOM   12451 C  CG  . TYR D 2 287 ? 35.799  -56.841 -5.522  1.00 22.14  ? 287 TYR D CG  1 
ATOM   12452 C  CD1 . TYR D 2 287 ? 34.634  -56.310 -6.113  1.00 23.14  ? 287 TYR D CD1 1 
ATOM   12453 C  CD2 . TYR D 2 287 ? 36.340  -57.974 -6.079  1.00 25.29  ? 287 TYR D CD2 1 
ATOM   12454 C  CE1 . TYR D 2 287 ? 34.056  -56.893 -7.217  1.00 23.29  ? 287 TYR D CE1 1 
ATOM   12455 C  CE2 . TYR D 2 287 ? 35.786  -58.551 -7.202  1.00 26.18  ? 287 TYR D CE2 1 
ATOM   12456 C  CZ  . TYR D 2 287 ? 34.638  -58.042 -7.740  1.00 22.74  ? 287 TYR D CZ  1 
ATOM   12457 O  OH  . TYR D 2 287 ? 34.061  -58.595 -8.837  1.00 22.19  ? 287 TYR D OH  1 
ATOM   12458 N  N   . CYS D 2 288 ? 38.830  -54.487 -2.931  1.00 20.71  ? 288 CYS D N   1 
ATOM   12459 C  CA  . CYS D 2 288 ? 39.282  -53.585 -1.855  1.00 24.88  ? 288 CYS D CA  1 
ATOM   12460 C  C   . CYS D 2 288 ? 39.753  -52.239 -2.410  1.00 23.38  ? 288 CYS D C   1 
ATOM   12461 O  O   . CYS D 2 288 ? 39.611  -51.219 -1.718  1.00 23.81  ? 288 CYS D O   1 
ATOM   12462 C  CB  . CYS D 2 288 ? 40.436  -54.171 -1.048  1.00 24.10  ? 288 CYS D CB  1 
ATOM   12463 S  SG  . CYS D 2 288 ? 39.882  -55.648 -0.099  1.00 24.59  ? 288 CYS D SG  1 
ATOM   12464 N  N   . ASP D 2 289 ? 40.354  -52.239 -3.600  1.00 21.21  ? 289 ASP D N   1 
ATOM   12465 C  CA  . ASP D 2 289 ? 40.944  -51.044 -4.191  1.00 20.09  ? 289 ASP D CA  1 
ATOM   12466 C  C   . ASP D 2 289 ? 39.930  -50.197 -4.953  1.00 23.82  ? 289 ASP D C   1 
ATOM   12467 O  O   . ASP D 2 289 ? 40.260  -49.066 -5.375  1.00 23.83  ? 289 ASP D O   1 
ATOM   12468 C  CB  . ASP D 2 289 ? 42.113  -51.433 -5.116  1.00 26.90  ? 289 ASP D CB  1 
ATOM   12469 C  CG  . ASP D 2 289 ? 43.327  -52.009 -4.362  1.00 25.33  ? 289 ASP D CG  1 
ATOM   12470 O  OD1 . ASP D 2 289 ? 43.392  -51.837 -3.118  1.00 28.34  ? 289 ASP D OD1 1 
ATOM   12471 O  OD2 . ASP D 2 289 ? 44.257  -52.583 -5.003  1.00 25.04  ? 289 ASP D OD2 1 
ATOM   12472 N  N   . ARG D 2 290 ? 38.740  -50.739 -5.183  1.00 22.75  ? 290 ARG D N   1 
ATOM   12473 C  CA  . ARG D 2 290 ? 37.680  -50.084 -5.949  1.00 24.55  ? 290 ARG D CA  1 
ATOM   12474 C  C   . ARG D 2 290 ? 37.260  -48.797 -5.237  1.00 22.38  ? 290 ARG D C   1 
ATOM   12475 O  O   . ARG D 2 290 ? 37.322  -48.723 -3.993  1.00 21.68  ? 290 ARG D O   1 
ATOM   12476 C  CB  . ARG D 2 290 ? 36.464  -51.013 -6.040  1.00 21.84  ? 290 ARG D CB  1 
ATOM   12477 C  CG  . ARG D 2 290 ? 35.422  -50.588 -7.067  1.00 24.76  ? 290 ARG D CG  1 
ATOM   12478 C  CD  . ARG D 2 290 ? 34.030  -51.226 -6.754  1.00 23.34  ? 290 ARG D CD  1 
ATOM   12479 N  NE  . ARG D 2 290 ? 33.357  -50.451 -5.693  1.00 23.30  ? 290 ARG D NE  1 
ATOM   12480 C  CZ  . ARG D 2 290 ? 32.128  -50.753 -5.292  1.00 21.48  ? 290 ARG D CZ  1 
ATOM   12481 N  NH1 . ARG D 2 290 ? 31.495  -51.811 -5.798  1.00 24.25  ? 290 ARG D NH1 1 
ATOM   12482 N  NH2 . ARG D 2 290 ? 31.527  -49.990 -4.365  1.00 22.82  ? 290 ARG D NH2 1 
ATOM   12483 N  N   . PRO D 2 291 ? 36.837  -47.759 -5.971  1.00 23.77  ? 291 PRO D N   1 
ATOM   12484 C  CA  . PRO D 2 291 ? 36.239  -46.608 -5.261  1.00 22.40  ? 291 PRO D CA  1 
ATOM   12485 C  C   . PRO D 2 291 ? 35.194  -47.111 -4.279  1.00 24.23  ? 291 PRO D C   1 
ATOM   12486 O  O   . PRO D 2 291 ? 34.363  -47.963 -4.599  1.00 23.83  ? 291 PRO D O   1 
ATOM   12487 C  CB  . PRO D 2 291 ? 35.607  -45.763 -6.381  1.00 23.91  ? 291 PRO D CB  1 
ATOM   12488 C  CG  . PRO D 2 291 ? 36.094  -46.333 -7.692  1.00 27.87  ? 291 PRO D CG  1 
ATOM   12489 C  CD  . PRO D 2 291 ? 36.925  -47.533 -7.441  1.00 25.54  ? 291 PRO D CD  1 
ATOM   12490 N  N   . ALA D 2 292 ? 35.232  -46.580 -3.058  1.00 21.21  ? 292 ALA D N   1 
ATOM   12491 C  CA  . ALA D 2 292 ? 34.528  -47.194 -1.932  1.00 21.83  ? 292 ALA D CA  1 
ATOM   12492 C  C   . ALA D 2 292 ? 33.081  -46.725 -1.837  1.00 23.09  ? 292 ALA D C   1 
ATOM   12493 O  O   . ALA D 2 292 ? 32.790  -45.532 -2.064  1.00 24.99  ? 292 ALA D O   1 
ATOM   12494 C  CB  . ALA D 2 292 ? 35.265  -46.819 -0.665  1.00 23.37  ? 292 ALA D CB  1 
ATOM   12495 N  N   . CYS D 2 293 ? 32.181  -47.664 -1.520  1.00 23.28  ? 293 CYS D N   1 
ATOM   12496 C  CA  . CYS D 2 293 ? 30.884  -47.361 -0.920  1.00 22.43  ? 293 CYS D CA  1 
ATOM   12497 C  C   . CYS D 2 293 ? 31.100  -46.453 0.295   1.00 23.25  ? 293 CYS D C   1 
ATOM   12498 O  O   . CYS D 2 293 ? 32.087  -46.638 1.017   1.00 21.66  ? 293 CYS D O   1 
ATOM   12499 C  CB  . CYS D 2 293 ? 30.216  -48.668 -0.385  1.00 24.23  ? 293 CYS D CB  1 
ATOM   12500 S  SG  . CYS D 2 293 ? 28.517  -48.511 0.263   1.00 28.25  ? 293 CYS D SG  1 
ATOM   12501 N  N   . PRO D 2 294 ? 30.228  -45.465 0.537   1.00 24.79  ? 294 PRO D N   1 
ATOM   12502 C  CA  . PRO D 2 294 ? 30.318  -44.697 1.787   1.00 22.35  ? 294 PRO D CA  1 
ATOM   12503 C  C   . PRO D 2 294 ? 30.508  -45.565 3.030   1.00 20.60  ? 294 PRO D C   1 
ATOM   12504 O  O   . PRO D 2 294 ? 31.227  -45.184 3.947   1.00 23.25  ? 294 PRO D O   1 
ATOM   12505 C  CB  . PRO D 2 294 ? 28.976  -43.968 1.821   1.00 24.22  ? 294 PRO D CB  1 
ATOM   12506 C  CG  . PRO D 2 294 ? 28.707  -43.689 0.396   1.00 23.87  ? 294 PRO D CG  1 
ATOM   12507 C  CD  . PRO D 2 294 ? 29.128  -44.972 -0.333  1.00 22.47  ? 294 PRO D CD  1 
ATOM   12508 N  N   . THR D 2 295 ? 29.823  -46.713 3.076   1.00 19.51  ? 295 THR D N   1 
ATOM   12509 C  CA  . THR D 2 295 ? 29.915  -47.642 4.213   1.00 24.34  ? 295 THR D CA  1 
ATOM   12510 C  C   . THR D 2 295 ? 31.347  -48.110 4.418   1.00 20.70  ? 295 THR D C   1 
ATOM   12511 O  O   . THR D 2 295 ? 31.757  -48.356 5.576   1.00 21.69  ? 295 THR D O   1 
ATOM   12512 C  CB  . THR D 2 295 ? 28.995  -48.848 3.964   1.00 24.39  ? 295 THR D CB  1 
ATOM   12513 O  OG1 . THR D 2 295 ? 27.623  -48.421 4.060   1.00 30.61  ? 295 THR D OG1 1 
ATOM   12514 C  CG2 . THR D 2 295 ? 29.222  -50.058 4.967   1.00 24.67  ? 295 THR D CG2 1 
ATOM   12515 N  N   . LYS D 2 296 ? 32.114  -48.217 3.333   1.00 21.18  ? 296 LYS D N   1 
ATOM   12516 C  CA  . LYS D 2 296 ? 33.487  -48.682 3.379   1.00 21.11  ? 296 LYS D CA  1 
ATOM   12517 C  C   . LYS D 2 296 ? 34.482  -47.550 3.330   1.00 20.75  ? 296 LYS D C   1 
ATOM   12518 O  O   . LYS D 2 296 ? 35.677  -47.789 3.161   1.00 21.22  ? 296 LYS D O   1 
ATOM   12519 C  CB  . LYS D 2 296 ? 33.745  -49.706 2.250   1.00 19.52  ? 296 LYS D CB  1 
ATOM   12520 C  CG  . LYS D 2 296 ? 32.844  -50.934 2.308   1.00 20.33  ? 296 LYS D CG  1 
ATOM   12521 C  CD  . LYS D 2 296 ? 33.438  -52.032 1.424   1.00 19.09  ? 296 LYS D CD  1 
ATOM   12522 C  CE  . LYS D 2 296 ? 32.474  -53.234 1.328   1.00 23.73  ? 296 LYS D CE  1 
ATOM   12523 N  NZ  . LYS D 2 296 ? 32.440  -54.092 2.638   1.00 19.57  ? 296 LYS D NZ  1 
ATOM   12524 N  N   . ASP D 2 297 ? 34.031  -46.320 3.556   1.00 22.71  ? 297 ASP D N   1 
ATOM   12525 C  CA  . ASP D 2 297 ? 34.896  -45.169 3.388   1.00 22.54  ? 297 ASP D CA  1 
ATOM   12526 C  C   . ASP D 2 297 ? 35.137  -44.478 4.739   1.00 25.43  ? 297 ASP D C   1 
ATOM   12527 O  O   . ASP D 2 297 ? 34.515  -43.465 5.081   1.00 25.23  ? 297 ASP D O   1 
ATOM   12528 C  CB  . ASP D 2 297 ? 34.305  -44.233 2.350   1.00 23.16  ? 297 ASP D CB  1 
ATOM   12529 C  CG  . ASP D 2 297 ? 35.367  -43.409 1.681   1.00 24.74  ? 297 ASP D CG  1 
ATOM   12530 O  OD1 . ASP D 2 297 ? 36.536  -43.909 1.505   1.00 24.17  ? 297 ASP D OD1 1 
ATOM   12531 O  OD2 . ASP D 2 297 ? 35.065  -42.238 1.328   1.00 23.75  ? 297 ASP D OD2 1 
ATOM   12532 N  N   . TYR D 2 298 ? 36.076  -45.042 5.503   1.00 22.45  ? 298 TYR D N   1 
ATOM   12533 C  CA  . TYR D 2 298 ? 36.529  -44.517 6.774   1.00 20.78  ? 298 TYR D CA  1 
ATOM   12534 C  C   . TYR D 2 298 ? 37.887  -45.147 7.063   1.00 20.32  ? 298 TYR D C   1 
ATOM   12535 O  O   . TYR D 2 298 ? 38.161  -46.271 6.573   1.00 19.88  ? 298 TYR D O   1 
ATOM   12536 C  CB  . TYR D 2 298 ? 35.515  -44.819 7.886   1.00 19.71  ? 298 TYR D CB  1 
ATOM   12537 C  CG  . TYR D 2 298 ? 35.342  -46.271 8.175   1.00 18.54  ? 298 TYR D CG  1 
ATOM   12538 C  CD1 . TYR D 2 298 ? 36.174  -46.919 9.081   1.00 20.92  ? 298 TYR D CD1 1 
ATOM   12539 C  CD2 . TYR D 2 298 ? 34.351  -46.979 7.551   1.00 20.79  ? 298 TYR D CD2 1 
ATOM   12540 C  CE1 . TYR D 2 298 ? 35.987  -48.289 9.342   1.00 20.55  ? 298 TYR D CE1 1 
ATOM   12541 C  CE2 . TYR D 2 298 ? 34.137  -48.363 7.829   1.00 19.75  ? 298 TYR D CE2 1 
ATOM   12542 C  CZ  . TYR D 2 298 ? 34.971  -48.989 8.701   1.00 19.87  ? 298 TYR D CZ  1 
ATOM   12543 O  OH  . TYR D 2 298 ? 34.748  -50.342 9.006   1.00 20.69  ? 298 TYR D OH  1 
ATOM   12544 N  N   . PRO D 2 299 ? 38.755  -44.480 7.886   1.00 21.83  ? 299 PRO D N   1 
ATOM   12545 C  CA  . PRO D 2 299 ? 38.546  -43.157 8.522   1.00 22.08  ? 299 PRO D CA  1 
ATOM   12546 C  C   . PRO D 2 299 ? 38.500  -42.022 7.508   1.00 23.97  ? 299 PRO D C   1 
ATOM   12547 O  O   . PRO D 2 299 ? 37.891  -40.969 7.772   1.00 22.89  ? 299 PRO D O   1 
ATOM   12548 C  CB  . PRO D 2 299 ? 39.772  -43.001 9.414   1.00 22.63  ? 299 PRO D CB  1 
ATOM   12549 C  CG  . PRO D 2 299 ? 40.799  -43.871 8.762   1.00 22.77  ? 299 PRO D CG  1 
ATOM   12550 C  CD  . PRO D 2 299 ? 40.031  -45.063 8.312   1.00 23.31  ? 299 PRO D CD  1 
ATOM   12551 N  N   . ALA D 2 300 ? 39.177  -42.177 6.367   1.00 24.13  ? 300 ALA D N   1 
ATOM   12552 C  CA  . ALA D 2 300 ? 39.314  -41.073 5.407   1.00 21.26  ? 300 ALA D CA  1 
ATOM   12553 C  C   . ALA D 2 300 ? 38.131  -41.088 4.452   1.00 24.77  ? 300 ALA D C   1 
ATOM   12554 O  O   . ALA D 2 300 ? 37.663  -42.163 4.036   1.00 23.06  ? 300 ALA D O   1 
ATOM   12555 C  CB  . ALA D 2 300 ? 40.646  -41.151 4.655   1.00 27.07  ? 300 ALA D CB  1 
ATOM   12556 N  N   . HIS D 2 301 ? 37.643  -39.886 4.097   1.00 23.11  ? 301 HIS D N   1 
ATOM   12557 C  CA  . HIS D 2 301 ? 36.602  -39.792 3.078   1.00 20.34  ? 301 HIS D CA  1 
ATOM   12558 C  C   . HIS D 2 301 ? 37.261  -39.805 1.691   1.00 22.90  ? 301 HIS D C   1 
ATOM   12559 O  O   . HIS D 2 301 ? 37.280  -38.793 0.978   1.00 23.29  ? 301 HIS D O   1 
ATOM   12560 C  CB  . HIS D 2 301 ? 35.773  -38.495 3.243   1.00 22.32  ? 301 HIS D CB  1 
ATOM   12561 C  CG  . HIS D 2 301 ? 34.762  -38.491 4.359   1.00 27.53  ? 301 HIS D CG  1 
ATOM   12562 N  ND1 . HIS D 2 301 ? 33.617  -39.268 4.344   1.00 28.12  ? 301 HIS D ND1 1 
ATOM   12563 C  CD2 . HIS D 2 301 ? 34.675  -37.719 5.483   1.00 27.67  ? 301 HIS D CD2 1 
ATOM   12564 C  CE1 . HIS D 2 301 ? 32.891  -39.001 5.427   1.00 29.23  ? 301 HIS D CE1 1 
ATOM   12565 N  NE2 . HIS D 2 301 ? 33.501  -38.055 6.123   1.00 24.95  ? 301 HIS D NE2 1 
ATOM   12566 N  N   . THR D 2 302 ? 37.846  -40.953 1.303   1.00 23.22  ? 302 THR D N   1 
ATOM   12567 C  CA  . THR D 2 302 ? 38.503  -40.989 -0.017  1.00 24.25  ? 302 THR D CA  1 
ATOM   12568 C  C   . THR D 2 302 ? 37.522  -40.715 -1.147  1.00 23.88  ? 302 THR D C   1 
ATOM   12569 O  O   . THR D 2 302 ? 37.910  -40.235 -2.222  1.00 24.89  ? 302 THR D O   1 
ATOM   12570 C  CB  . THR D 2 302 ? 39.168  -42.355 -0.268  1.00 25.15  ? 302 THR D CB  1 
ATOM   12571 O  OG1 . THR D 2 302 ? 38.152  -43.303 -0.542  1.00 25.85  ? 302 THR D OG1 1 
ATOM   12572 C  CG2 . THR D 2 302 ? 39.988  -42.822 0.915   1.00 26.21  ? 302 THR D CG2 1 
ATOM   12573 N  N   . ARG D 2 303 ? 36.251  -40.974 -0.902  1.00 23.01  ? 303 ARG D N   1 
ATOM   12574 C  CA  . ARG D 2 303 ? 35.202  -40.741 -1.878  1.00 23.29  ? 303 ARG D CA  1 
ATOM   12575 C  C   . ARG D 2 303 ? 35.166  -39.289 -2.329  1.00 24.40  ? 303 ARG D C   1 
ATOM   12576 O  O   . ARG D 2 303 ? 34.950  -39.005 -3.525  1.00 25.70  ? 303 ARG D O   1 
ATOM   12577 C  CB  . ARG D 2 303 ? 33.855  -41.151 -1.291  1.00 23.79  ? 303 ARG D CB  1 
ATOM   12578 C  CG  . ARG D 2 303 ? 32.647  -40.918 -2.243  1.00 26.54  ? 303 ARG D CG  1 
ATOM   12579 C  CD  . ARG D 2 303 ? 31.390  -41.618 -1.700  1.00 25.29  ? 303 ARG D CD  1 
ATOM   12580 N  NE  . ARG D 2 303 ? 30.293  -41.289 -2.583  1.00 28.01  ? 303 ARG D NE  1 
ATOM   12581 C  CZ  . ARG D 2 303 ? 29.222  -40.591 -2.223  1.00 27.53  ? 303 ARG D CZ  1 
ATOM   12582 N  NH1 . ARG D 2 303 ? 28.997  -40.252 -0.945  1.00 23.91  ? 303 ARG D NH1 1 
ATOM   12583 N  NH2 . ARG D 2 303 ? 28.343  -40.265 -3.142  1.00 24.48  ? 303 ARG D NH2 1 
ATOM   12584 N  N   . PHE D 2 304 ? 35.421  -38.357 -1.410  1.00 22.93  ? 304 PHE D N   1 
ATOM   12585 C  CA  . PHE D 2 304 ? 35.335  -36.951 -1.779  1.00 22.27  ? 304 PHE D CA  1 
ATOM   12586 C  C   . PHE D 2 304 ? 36.309  -36.625 -2.913  1.00 25.15  ? 304 PHE D C   1 
ATOM   12587 O  O   . PHE D 2 304 ? 35.967  -35.861 -3.832  1.00 28.84  ? 304 PHE D O   1 
ATOM   12588 C  CB  . PHE D 2 304 ? 35.613  -36.036 -0.573  1.00 25.15  ? 304 PHE D CB  1 
ATOM   12589 C  CG  . PHE D 2 304 ? 34.566  -36.123 0.527   1.00 27.22  ? 304 PHE D CG  1 
ATOM   12590 C  CD1 . PHE D 2 304 ? 33.530  -37.037 0.470   1.00 28.46  ? 304 PHE D CD1 1 
ATOM   12591 C  CD2 . PHE D 2 304 ? 34.629  -35.247 1.631   1.00 28.89  ? 304 PHE D CD2 1 
ATOM   12592 C  CE1 . PHE D 2 304 ? 32.584  -37.136 1.500   1.00 31.07  ? 304 PHE D CE1 1 
ATOM   12593 C  CE2 . PHE D 2 304 ? 33.669  -35.314 2.662   1.00 29.77  ? 304 PHE D CE2 1 
ATOM   12594 C  CZ  . PHE D 2 304 ? 32.639  -36.252 2.588   1.00 30.78  ? 304 PHE D CZ  1 
ATOM   12595 N  N   . ASP D 2 305 ? 37.546  -37.154 -2.841  1.00 25.91  ? 305 ASP D N   1 
ATOM   12596 C  CA  . ASP D 2 305 ? 38.561  -36.883 -3.876  1.00 28.53  ? 305 ASP D CA  1 
ATOM   12597 C  C   . ASP D 2 305 ? 38.230  -37.602 -5.180  1.00 26.29  ? 305 ASP D C   1 
ATOM   12598 O  O   . ASP D 2 305 ? 38.510  -37.088 -6.278  1.00 25.80  ? 305 ASP D O   1 
ATOM   12599 C  CB  . ASP D 2 305 ? 39.967  -37.334 -3.422  1.00 32.28  ? 305 ASP D CB  1 
ATOM   12600 C  CG  . ASP D 2 305 ? 40.467  -36.646 -2.167  1.00 41.34  ? 305 ASP D CG  1 
ATOM   12601 O  OD1 . ASP D 2 305 ? 40.308  -35.416 -2.036  1.00 36.88  ? 305 ASP D OD1 1 
ATOM   12602 O  OD2 . ASP D 2 305 ? 40.985  -37.369 -1.271  1.00 44.90  ? 305 ASP D OD2 1 
ATOM   12603 N  N   . HIS D 2 306 ? 37.722  -38.824 -5.056  1.00 25.50  ? 306 HIS D N   1 
ATOM   12604 C  CA  . HIS D 2 306 ? 37.274  -39.576 -6.209  1.00 25.88  ? 306 HIS D CA  1 
ATOM   12605 C  C   . HIS D 2 306 ? 36.174  -38.820 -6.949  1.00 26.73  ? 306 HIS D C   1 
ATOM   12606 O  O   . HIS D 2 306 ? 36.254  -38.658 -8.178  1.00 25.39  ? 306 HIS D O   1 
ATOM   12607 C  CB  . HIS D 2 306 ? 36.793  -40.961 -5.763  1.00 21.38  ? 306 HIS D CB  1 
ATOM   12608 C  CG  . HIS D 2 306 ? 36.156  -41.729 -6.865  1.00 23.29  ? 306 HIS D CG  1 
ATOM   12609 N  ND1 . HIS D 2 306 ? 36.851  -42.125 -7.989  1.00 26.64  ? 306 HIS D ND1 1 
ATOM   12610 C  CD2 . HIS D 2 306 ? 34.886  -42.187 -7.028  1.00 23.48  ? 306 HIS D CD2 1 
ATOM   12611 C  CE1 . HIS D 2 306 ? 36.046  -42.803 -8.790  1.00 23.70  ? 306 HIS D CE1 1 
ATOM   12612 N  NE2 . HIS D 2 306 ? 34.860  -42.882 -8.216  1.00 25.20  ? 306 HIS D NE2 1 
ATOM   12613 N  N   . VAL D 2 307 ? 35.164  -38.310 -6.207  1.00 25.22  ? 307 VAL D N   1 
ATOM   12614 C  CA  . VAL D 2 307 ? 34.031  -37.630 -6.854  1.00 27.36  ? 307 VAL D CA  1 
ATOM   12615 C  C   . VAL D 2 307 ? 34.485  -36.297 -7.461  1.00 27.75  ? 307 VAL D C   1 
ATOM   12616 O  O   . VAL D 2 307 ? 34.206  -35.995 -8.637  1.00 27.68  ? 307 VAL D O   1 
ATOM   12617 C  CB  . VAL D 2 307 ? 32.854  -37.444 -5.876  1.00 24.42  ? 307 VAL D CB  1 
ATOM   12618 C  CG1 . VAL D 2 307 ? 31.723  -36.564 -6.513  1.00 26.29  ? 307 VAL D CG1 1 
ATOM   12619 C  CG2 . VAL D 2 307 ? 32.277  -38.787 -5.408  1.00 26.59  ? 307 VAL D CG2 1 
ATOM   12620 N  N   . LEU D 2 308 ? 35.273  -35.522 -6.715  1.00 25.37  ? 308 LEU D N   1 
ATOM   12621 C  CA  . LEU D 2 308 ? 35.766  -34.258 -7.286  1.00 25.58  ? 308 LEU D CA  1 
ATOM   12622 C  C   . LEU D 2 308 ? 36.661  -34.506 -8.495  1.00 28.60  ? 308 LEU D C   1 
ATOM   12623 O  O   . LEU D 2 308 ? 36.556  -33.792 -9.505  1.00 28.06  ? 308 LEU D O   1 
ATOM   12624 C  CB  . LEU D 2 308 ? 36.494  -33.447 -6.214  1.00 26.76  ? 308 LEU D CB  1 
ATOM   12625 C  CG  . LEU D 2 308 ? 36.955  -32.078 -6.768  1.00 29.57  ? 308 LEU D CG  1 
ATOM   12626 C  CD1 . LEU D 2 308 ? 35.762  -31.280 -7.267  1.00 29.64  ? 308 LEU D CD1 1 
ATOM   12627 C  CD2 . LEU D 2 308 ? 37.773  -31.329 -5.759  1.00 31.67  ? 308 LEU D CD2 1 
ATOM   12628 N  N   . GLY D 2 309 ? 37.509  -35.542 -8.436  1.00 29.05  ? 309 GLY D N   1 
ATOM   12629 C  CA  . GLY D 2 309 ? 38.395  -35.847 -9.554  1.00 28.31  ? 309 GLY D CA  1 
ATOM   12630 C  C   . GLY D 2 309 ? 37.638  -36.202 -10.817 1.00 30.67  ? 309 GLY D C   1 
ATOM   12631 O  O   . GLY D 2 309 ? 37.970  -35.716 -11.903 1.00 30.41  ? 309 GLY D O   1 
ATOM   12632 N  N   . MET D 2 310 ? 36.610  -37.059 -10.696 1.00 29.00  ? 310 MET D N   1 
ATOM   12633 C  CA  . MET D 2 310 ? 35.774  -37.353 -11.855 1.00 31.46  ? 310 MET D CA  1 
ATOM   12634 C  C   . MET D 2 310 ? 35.074  -36.098 -12.363 1.00 31.91  ? 310 MET D C   1 
ATOM   12635 O  O   . MET D 2 310 ? 34.958  -35.880 -13.578 1.00 29.13  ? 310 MET D O   1 
ATOM   12636 C  CB  . MET D 2 310 ? 34.741  -38.426 -11.537 1.00 30.60  ? 310 MET D CB  1 
ATOM   12637 C  CG  . MET D 2 310 ? 35.336  -39.813 -11.693 1.00 32.06  ? 310 MET D CG  1 
ATOM   12638 S  SD  . MET D 2 310 ? 34.125  -41.089 -11.443 1.00 30.68  ? 310 MET D SD  1 
ATOM   12639 C  CE  . MET D 2 310 ? 33.384  -40.492 -9.914  1.00 28.74  ? 310 MET D CE  1 
ATOM   12640 N  N   . ALA D 2 311 ? 34.609  -35.248 -11.446 1.00 26.41  ? 311 ALA D N   1 
ATOM   12641 C  CA  . ALA D 2 311 ? 33.899  -34.049 -11.872 1.00 29.71  ? 311 ALA D CA  1 
ATOM   12642 C  C   . ALA D 2 311 ? 34.803  -33.144 -12.668 1.00 30.09  ? 311 ALA D C   1 
ATOM   12643 O  O   . ALA D 2 311 ? 34.384  -32.573 -13.676 1.00 29.83  ? 311 ALA D O   1 
ATOM   12644 C  CB  . ALA D 2 311 ? 33.374  -33.281 -10.666 1.00 30.07  ? 311 ALA D CB  1 
ATOM   12645 N  N   . LYS D 2 312 ? 36.053  -32.993 -12.221 1.00 30.05  ? 312 LYS D N   1 
ATOM   12646 C  CA  . LYS D 2 312 ? 36.977  -32.118 -12.923 1.00 31.76  ? 312 LYS D CA  1 
ATOM   12647 C  C   . LYS D 2 312 ? 37.417  -32.721 -14.249 1.00 31.02  ? 312 LYS D C   1 
ATOM   12648 O  O   . LYS D 2 312 ? 37.494  -32.010 -15.266 1.00 32.20  ? 312 LYS D O   1 
ATOM   12649 C  CB  . LYS D 2 312 ? 38.165  -31.804 -12.028 1.00 32.79  ? 312 LYS D CB  1 
ATOM   12650 C  CG  . LYS D 2 312 ? 37.744  -30.990 -10.805 1.00 34.06  ? 312 LYS D CG  1 
ATOM   12651 C  CD  . LYS D 2 312 ? 37.626  -29.494 -11.168 1.00 42.84  ? 312 LYS D CD  1 
ATOM   12652 C  CE  . LYS D 2 312 ? 37.674  -28.597 -9.877  1.00 39.61  ? 312 LYS D CE  1 
ATOM   12653 N  NZ  . LYS D 2 312 ? 36.857  -27.352 -9.956  1.00 43.65  ? 312 LYS D NZ  1 
ATOM   12654 N  N   . GLU D 2 313 ? 37.632  -34.032 -14.254 1.00 31.36  ? 313 GLU D N   1 
ATOM   12655 C  CA  . GLU D 2 313 ? 38.128  -34.721 -15.430 1.00 33.99  ? 313 GLU D CA  1 
ATOM   12656 C  C   . GLU D 2 313 ? 37.102  -34.692 -16.540 1.00 31.38  ? 313 GLU D C   1 
ATOM   12657 O  O   . GLU D 2 313 ? 37.470  -34.581 -17.708 1.00 36.17  ? 313 GLU D O   1 
ATOM   12658 C  CB  . GLU D 2 313 ? 38.519  -36.159 -15.065 1.00 31.29  ? 313 GLU D CB  1 
ATOM   12659 C  CG  . GLU D 2 313 ? 39.022  -37.031 -16.196 1.00 38.79  ? 313 GLU D CG  1 
ATOM   12660 C  CD  . GLU D 2 313 ? 39.318  -38.491 -15.769 1.00 44.72  ? 313 GLU D CD  1 
ATOM   12661 O  OE1 . GLU D 2 313 ? 39.075  -38.881 -14.585 1.00 46.01  ? 313 GLU D OE1 1 
ATOM   12662 O  OE2 . GLU D 2 313 ? 39.773  -39.266 -16.653 1.00 48.87  ? 313 GLU D OE2 1 
ATOM   12663 N  N   . TYR D 2 314 ? 35.817  -34.729 -16.193 1.00 31.39  ? 314 TYR D N   1 
ATOM   12664 C  CA  . TYR D 2 314 ? 34.751  -34.726 -17.174 1.00 31.64  ? 314 TYR D CA  1 
ATOM   12665 C  C   . TYR D 2 314 ? 34.108  -33.353 -17.337 1.00 33.97  ? 314 TYR D C   1 
ATOM   12666 O  O   . TYR D 2 314 ? 33.063  -33.240 -17.988 1.00 33.21  ? 314 TYR D O   1 
ATOM   12667 C  CB  . TYR D 2 314 ? 33.711  -35.782 -16.809 1.00 28.67  ? 314 TYR D CB  1 
ATOM   12668 C  CG  . TYR D 2 314 ? 34.230  -37.167 -17.008 1.00 30.69  ? 314 TYR D CG  1 
ATOM   12669 C  CD1 . TYR D 2 314 ? 35.149  -37.748 -16.099 1.00 29.84  ? 314 TYR D CD1 1 
ATOM   12670 C  CD2 . TYR D 2 314 ? 33.840  -37.894 -18.130 1.00 28.42  ? 314 TYR D CD2 1 
ATOM   12671 C  CE1 . TYR D 2 314 ? 35.640  -39.103 -16.321 1.00 32.33  ? 314 TYR D CE1 1 
ATOM   12672 C  CE2 . TYR D 2 314 ? 34.337  -39.142 -18.380 1.00 30.64  ? 314 TYR D CE2 1 
ATOM   12673 C  CZ  . TYR D 2 314 ? 35.205  -39.760 -17.473 1.00 31.42  ? 314 TYR D CZ  1 
ATOM   12674 O  OH  . TYR D 2 314 ? 35.603  -41.022 -17.841 1.00 32.85  ? 314 TYR D OH  1 
ATOM   12675 N  N   A ASN D 2 315 ? 34.728  -32.308 -16.786 0.58 31.42  ? 315 ASN D N   1 
ATOM   12676 N  N   B ASN D 2 315 ? 34.716  -32.309 -16.777 0.42 31.45  ? 315 ASN D N   1 
ATOM   12677 C  CA  A ASN D 2 315 ? 34.319  -30.914 -17.017 0.58 33.65  ? 315 ASN D CA  1 
ATOM   12678 C  CA  B ASN D 2 315 ? 34.300  -30.925 -17.027 0.42 33.65  ? 315 ASN D CA  1 
ATOM   12679 C  C   A ASN D 2 315 ? 32.842  -30.699 -16.661 0.58 34.91  ? 315 ASN D C   1 
ATOM   12680 C  C   B ASN D 2 315 ? 32.826  -30.727 -16.669 0.42 34.89  ? 315 ASN D C   1 
ATOM   12681 O  O   A ASN D 2 315 ? 32.058  -30.132 -17.429 0.58 33.26  ? 315 ASN D O   1 
ATOM   12682 O  O   B ASN D 2 315 ? 32.024  -30.213 -17.454 0.42 33.27  ? 315 ASN D O   1 
ATOM   12683 C  CB  A ASN D 2 315 ? 34.628  -30.487 -18.465 0.58 35.78  ? 315 ASN D CB  1 
ATOM   12684 C  CB  B ASN D 2 315 ? 34.578  -30.530 -18.481 0.42 35.75  ? 315 ASN D CB  1 
ATOM   12685 C  CG  A ASN D 2 315 ? 36.093  -30.011 -18.657 0.58 36.90  ? 315 ASN D CG  1 
ATOM   12686 C  CG  B ASN D 2 315 ? 34.374  -29.052 -18.728 0.42 34.87  ? 315 ASN D CG  1 
ATOM   12687 O  OD1 A ASN D 2 315 ? 36.554  -29.060 -17.986 0.58 39.56  ? 315 ASN D OD1 1 
ATOM   12688 O  OD1 B ASN D 2 315 ? 34.536  -28.221 -17.815 0.42 34.98  ? 315 ASN D OD1 1 
ATOM   12689 N  ND2 A ASN D 2 315 ? 36.790  -30.612 -19.619 0.58 39.32  ? 315 ASN D ND2 1 
ATOM   12690 N  ND2 B ASN D 2 315 ? 33.987  -28.710 -19.953 0.42 37.26  ? 315 ASN D ND2 1 
ATOM   12691 N  N   . VAL D 2 316 ? 32.468  -31.180 -15.465 1.00 32.02  ? 316 VAL D N   1 
ATOM   12692 C  CA  . VAL D 2 316 ? 31.089  -31.086 -14.983 1.00 29.47  ? 316 VAL D CA  1 
ATOM   12693 C  C   . VAL D 2 316 ? 30.712  -29.650 -14.656 1.00 35.06  ? 316 VAL D C   1 
ATOM   12694 O  O   . VAL D 2 316 ? 31.477  -28.916 -14.018 1.00 31.93  ? 316 VAL D O   1 
ATOM   12695 C  CB  . VAL D 2 316 ? 30.946  -31.993 -13.756 1.00 33.02  ? 316 VAL D CB  1 
ATOM   12696 C  CG1 . VAL D 2 316 ? 29.658  -31.717 -12.998 1.00 31.64  ? 316 VAL D CG1 1 
ATOM   12697 C  CG2 . VAL D 2 316 ? 31.013  -33.418 -14.226 1.00 31.74  ? 316 VAL D CG2 1 
ATOM   12698 N  N   . GLU D 2 317 ? 29.510  -29.247 -15.060 1.00 30.33  ? 317 GLU D N   1 
ATOM   12699 C  CA  . GLU D 2 317 ? 29.062  -27.888 -14.711 1.00 31.96  ? 317 GLU D CA  1 
ATOM   12700 C  C   . GLU D 2 317 ? 28.147  -27.868 -13.498 1.00 34.46  ? 317 GLU D C   1 
ATOM   12701 O  O   . GLU D 2 317 ? 28.078  -26.840 -12.799 1.00 35.78  ? 317 GLU D O   1 
ATOM   12702 C  CB  . GLU D 2 317 ? 28.385  -27.230 -15.918 1.00 34.77  ? 317 GLU D CB  1 
ATOM   12703 C  CG  . GLU D 2 317 ? 29.437  -26.973 -17.044 1.00 39.51  ? 317 GLU D CG  1 
ATOM   12704 C  CD  . GLU D 2 317 ? 28.886  -26.751 -18.477 1.00 42.54  ? 317 GLU D CD  1 
ATOM   12705 O  OE1 . GLU D 2 317 ? 27.675  -26.959 -18.764 1.00 40.67  ? 317 GLU D OE1 1 
ATOM   12706 O  OE2 . GLU D 2 317 ? 29.711  -26.354 -19.328 1.00 46.49  ? 317 GLU D OE2 1 
ATOM   12707 N  N   . GLY D 2 318 ? 27.462  -28.979 -13.216 1.00 31.67  ? 318 GLY D N   1 
ATOM   12708 C  CA  . GLY D 2 318 ? 26.628  -29.057 -12.033 1.00 29.66  ? 318 GLY D CA  1 
ATOM   12709 C  C   . GLY D 2 318 ? 26.383  -30.497 -11.669 1.00 29.77  ? 318 GLY D C   1 
ATOM   12710 O  O   . GLY D 2 318 ? 26.345  -31.378 -12.535 1.00 31.16  ? 318 GLY D O   1 
ATOM   12711 N  N   . ALA D 2 319 ? 26.251  -30.750 -10.381 1.00 28.35  ? 319 ALA D N   1 
ATOM   12712 C  CA  . ALA D 2 319 ? 26.104  -32.132 -9.918  1.00 29.62  ? 319 ALA D CA  1 
ATOM   12713 C  C   . ALA D 2 319 ? 24.765  -32.313 -9.221  1.00 29.23  ? 319 ALA D C   1 
ATOM   12714 O  O   . ALA D 2 319 ? 24.352  -31.458 -8.427  1.00 30.24  ? 319 ALA D O   1 
ATOM   12715 C  CB  . ALA D 2 319 ? 27.227  -32.536 -8.965  1.00 29.33  ? 319 ALA D CB  1 
ATOM   12716 N  N   . ILE D 2 320 ? 24.102  -33.429 -9.519  1.00 26.41  ? 320 ILE D N   1 
ATOM   12717 C  CA  . ILE D 2 320 ? 22.779  -33.738 -9.025  1.00 27.47  ? 320 ILE D CA  1 
ATOM   12718 C  C   . ILE D 2 320 ? 22.927  -34.942 -8.091  1.00 28.14  ? 320 ILE D C   1 
ATOM   12719 O  O   . ILE D 2 320 ? 23.353  -36.036 -8.506  1.00 26.84  ? 320 ILE D O   1 
ATOM   12720 C  CB  . ILE D 2 320 ? 21.791  -34.031 -10.156 1.00 31.32  ? 320 ILE D CB  1 
ATOM   12721 C  CG1 . ILE D 2 320 ? 21.769  -32.862 -11.198 1.00 32.29  ? 320 ILE D CG1 1 
ATOM   12722 C  CG2 . ILE D 2 320 ? 20.405  -34.237 -9.577  1.00 33.01  ? 320 ILE D CG2 1 
ATOM   12723 C  CD1 . ILE D 2 320 ? 20.936  -33.130 -12.401 1.00 36.19  ? 320 ILE D CD1 1 
ATOM   12724 N  N   . PHE D 2 321 ? 22.645  -34.718 -6.812  1.00 25.24  ? 321 PHE D N   1 
ATOM   12725 C  CA  . PHE D 2 321 ? 22.563  -35.795 -5.824  1.00 25.88  ? 321 PHE D CA  1 
ATOM   12726 C  C   . PHE D 2 321 ? 21.175  -36.401 -5.903  1.00 29.15  ? 321 PHE D C   1 
ATOM   12727 O  O   . PHE D 2 321 ? 20.183  -35.713 -5.664  1.00 29.25  ? 321 PHE D O   1 
ATOM   12728 C  CB  . PHE D 2 321 ? 22.802  -35.294 -4.395  1.00 27.07  ? 321 PHE D CB  1 
ATOM   12729 C  CG  . PHE D 2 321 ? 24.198  -34.868 -4.100  1.00 29.72  ? 321 PHE D CG  1 
ATOM   12730 C  CD1 . PHE D 2 321 ? 24.615  -33.563 -4.357  1.00 32.99  ? 321 PHE D CD1 1 
ATOM   12731 C  CD2 . PHE D 2 321 ? 25.096  -35.761 -3.570  1.00 27.75  ? 321 PHE D CD2 1 
ATOM   12732 C  CE1 . PHE D 2 321 ? 25.938  -33.159 -4.077  1.00 34.97  ? 321 PHE D CE1 1 
ATOM   12733 C  CE2 . PHE D 2 321 ? 26.421  -35.391 -3.286  1.00 30.03  ? 321 PHE D CE2 1 
ATOM   12734 C  CZ  . PHE D 2 321 ? 26.851  -34.071 -3.539  1.00 30.52  ? 321 PHE D CZ  1 
ATOM   12735 N  N   . LEU D 2 322 ? 21.106  -37.703 -6.198  1.00 25.63  ? 322 LEU D N   1 
ATOM   12736 C  CA  . LEU D 2 322 ? 19.849  -38.428 -6.207  1.00 30.00  ? 322 LEU D CA  1 
ATOM   12737 C  C   . LEU D 2 322 ? 19.950  -39.304 -4.981  1.00 28.75  ? 322 LEU D C   1 
ATOM   12738 O  O   . LEU D 2 322 ? 20.873  -40.113 -4.868  1.00 29.50  ? 322 LEU D O   1 
ATOM   12739 C  CB  . LEU D 2 322 ? 19.659  -39.247 -7.490  1.00 28.98  ? 322 LEU D CB  1 
ATOM   12740 C  CG  . LEU D 2 322 ? 19.625  -38.602 -8.902  1.00 33.24  ? 322 LEU D CG  1 
ATOM   12741 C  CD1 . LEU D 2 322 ? 20.857  -37.882 -9.181  1.00 36.79  ? 322 LEU D CD1 1 
ATOM   12742 C  CD2 . LEU D 2 322 ? 19.520  -39.660 -9.971  1.00 38.27  ? 322 LEU D CD2 1 
ATOM   12743 N  N   A GLN D 2 323 ? 19.052  -39.111 -4.036  0.60 30.49  ? 323 GLN D N   1 
ATOM   12744 N  N   B GLN D 2 323 ? 19.058  -39.116 -4.019  0.40 30.50  ? 323 GLN D N   1 
ATOM   12745 C  CA  A GLN D 2 323 ? 19.145  -39.831 -2.778  0.60 31.17  ? 323 GLN D CA  1 
ATOM   12746 C  CA  B GLN D 2 323 ? 19.199  -39.830 -2.756  0.40 31.17  ? 323 GLN D CA  1 
ATOM   12747 C  C   A GLN D 2 323 ? 17.925  -40.718 -2.601  0.60 31.28  ? 323 GLN D C   1 
ATOM   12748 C  C   B GLN D 2 323 ? 17.958  -40.684 -2.521  0.40 31.30  ? 323 GLN D C   1 
ATOM   12749 O  O   A GLN D 2 323 ? 16.785  -40.267 -2.755  0.60 30.41  ? 323 GLN D O   1 
ATOM   12750 O  O   B GLN D 2 323 ? 16.829  -40.186 -2.602  0.40 30.61  ? 323 GLN D O   1 
ATOM   12751 C  CB  A GLN D 2 323 ? 19.243  -38.884 -1.598  0.60 32.20  ? 323 GLN D CB  1 
ATOM   12752 C  CB  B GLN D 2 323 ? 19.419  -38.862 -1.583  0.40 32.23  ? 323 GLN D CB  1 
ATOM   12753 C  CG  A GLN D 2 323 ? 19.839  -39.555 -0.384  0.60 33.98  ? 323 GLN D CG  1 
ATOM   12754 C  CG  B GLN D 2 323 ? 19.901  -39.576 -0.302  0.40 33.93  ? 323 GLN D CG  1 
ATOM   12755 C  CD  A GLN D 2 323 ? 19.737  -38.696 0.837   0.60 31.92  ? 323 GLN D CD  1 
ATOM   12756 C  CD  B GLN D 2 323 ? 21.203  -38.996 0.278   0.40 31.52  ? 323 GLN D CD  1 
ATOM   12757 O  OE1 A GLN D 2 323 ? 20.635  -37.929 1.144   0.60 34.75  ? 323 GLN D OE1 1 
ATOM   12758 O  OE1 B GLN D 2 323 ? 21.189  -38.383 1.331   0.40 32.96  ? 323 GLN D OE1 1 
ATOM   12759 N  NE2 A GLN D 2 323 ? 18.672  -38.889 1.600   0.60 35.94  ? 323 GLN D NE2 1 
ATOM   12760 N  NE2 B GLN D 2 323 ? 22.297  -39.119 -0.452  0.40 32.91  ? 323 GLN D NE2 1 
ATOM   12761 N  N   . GLN D 2 324 ? 18.161  -41.973 -2.248  1.00 29.65  ? 324 GLN D N   1 
ATOM   12762 C  CA  . GLN D 2 324 ? 17.062  -42.799 -1.792  1.00 32.13  ? 324 GLN D CA  1 
ATOM   12763 C  C   . GLN D 2 324 ? 16.616  -42.322 -0.415  1.00 28.34  ? 324 GLN D C   1 
ATOM   12764 O  O   . GLN D 2 324 ? 17.443  -42.030 0.452   1.00 29.11  ? 324 GLN D O   1 
ATOM   12765 C  CB  . GLN D 2 324 ? 17.483  -44.269 -1.723  1.00 31.92  ? 324 GLN D CB  1 
ATOM   12766 C  CG  . GLN D 2 324 ? 17.829  -44.895 -3.072  1.00 32.07  ? 324 GLN D CG  1 
ATOM   12767 C  CD  . GLN D 2 324 ? 16.552  -45.146 -3.885  1.00 36.41  ? 324 GLN D CD  1 
ATOM   12768 O  OE1 . GLN D 2 324 ? 15.685  -45.909 -3.453  1.00 36.62  ? 324 GLN D OE1 1 
ATOM   12769 N  NE2 . GLN D 2 324 ? 16.416  -44.476 -5.032  1.00 37.48  ? 324 GLN D NE2 1 
ATOM   12770 N  N   . LYS D 2 325 ? 15.306  -42.247 -0.220  1.00 28.11  ? 325 LYS D N   1 
ATOM   12771 C  CA  . LYS D 2 325 ? 14.773  -41.992 1.107   1.00 29.52  ? 325 LYS D CA  1 
ATOM   12772 C  C   . LYS D 2 325 ? 15.420  -42.968 2.092   1.00 27.09  ? 325 LYS D C   1 
ATOM   12773 O  O   . LYS D 2 325 ? 15.683  -44.120 1.759   1.00 27.32  ? 325 LYS D O   1 
ATOM   12774 C  CB  . LYS D 2 325 ? 13.242  -42.163 1.106   1.00 33.59  ? 325 LYS D CB  1 
ATOM   12775 C  CG  . LYS D 2 325 ? 12.564  -41.833 2.433   1.00 38.92  ? 325 LYS D CG  1 
ATOM   12776 C  CD  . LYS D 2 325 ? 11.210  -41.135 2.243   1.00 45.06  ? 325 LYS D CD  1 
ATOM   12777 C  CE  . LYS D 2 325 ? 10.865  -40.203 3.436   1.00 49.26  ? 325 LYS D CE  1 
ATOM   12778 N  NZ  . LYS D 2 325 ? 12.072  -39.527 4.095   1.00 40.50  ? 325 LYS D NZ  1 
ATOM   12779 N  N   . PHE D 2 326 ? 15.762  -42.470 3.263   1.00 27.50  ? 326 PHE D N   1 
ATOM   12780 C  CA  . PHE D 2 326 ? 16.282  -43.258 4.362   1.00 27.43  ? 326 PHE D CA  1 
ATOM   12781 C  C   . PHE D 2 326 ? 17.691  -43.798 4.146   1.00 28.37  ? 326 PHE D C   1 
ATOM   12782 O  O   . PHE D 2 326 ? 18.138  -44.586 4.955   1.00 26.83  ? 326 PHE D O   1 
ATOM   12783 C  CB  . PHE D 2 326 ? 15.335  -44.423 4.721   1.00 26.44  ? 326 PHE D CB  1 
ATOM   12784 C  CG  . PHE D 2 326 ? 13.923  -43.983 4.960   1.00 30.62  ? 326 PHE D CG  1 
ATOM   12785 C  CD1 . PHE D 2 326 ? 13.659  -43.009 5.905   1.00 30.47  ? 326 PHE D CD1 1 
ATOM   12786 C  CD2 . PHE D 2 326 ? 12.852  -44.574 4.300   1.00 33.49  ? 326 PHE D CD2 1 
ATOM   12787 C  CE1 . PHE D 2 326 ? 12.349  -42.567 6.166   1.00 35.18  ? 326 PHE D CE1 1 
ATOM   12788 C  CE2 . PHE D 2 326 ? 11.532  -44.157 4.568   1.00 32.77  ? 326 PHE D CE2 1 
ATOM   12789 C  CZ  . PHE D 2 326 ? 11.287  -43.145 5.491   1.00 36.31  ? 326 PHE D CZ  1 
ATOM   12790 N  N   . CYS D 2 327 ? 18.413  -43.412 3.081   1.00 24.60  ? 327 CYS D N   1 
ATOM   12791 C  CA  . CYS D 2 327 ? 19.717  -44.014 2.775   1.00 25.95  ? 327 CYS D CA  1 
ATOM   12792 C  C   . CYS D 2 327 ? 20.827  -43.520 3.709   1.00 26.24  ? 327 CYS D C   1 
ATOM   12793 O  O   . CYS D 2 327 ? 21.434  -42.479 3.460   1.00 24.57  ? 327 CYS D O   1 
ATOM   12794 C  CB  . CYS D 2 327 ? 20.077  -43.738 1.313   1.00 25.54  ? 327 CYS D CB  1 
ATOM   12795 S  SG  . CYS D 2 327 ? 21.670  -44.371 0.787   1.00 23.91  ? 327 CYS D SG  1 
ATOM   12796 N  N   . ASP D 2 328 ? 21.149  -44.292 4.781   1.00 26.13  ? 328 ASP D N   1 
ATOM   12797 C  CA  . ASP D 2 328 ? 22.072  -43.785 5.796   1.00 25.05  ? 328 ASP D CA  1 
ATOM   12798 C  C   . ASP D 2 328 ? 23.538  -43.607 5.360   1.00 23.53  ? 328 ASP D C   1 
ATOM   12799 O  O   . ASP D 2 328 ? 24.138  -42.569 5.681   1.00 23.00  ? 328 ASP D O   1 
ATOM   12800 C  CB  . ASP D 2 328 ? 22.029  -44.674 7.033   1.00 27.33  ? 328 ASP D CB  1 
ATOM   12801 C  CG  . ASP D 2 328 ? 20.684  -44.638 7.663   1.00 29.86  ? 328 ASP D CG  1 
ATOM   12802 O  OD1 . ASP D 2 328 ? 20.344  -43.636 8.328   1.00 32.22  ? 328 ASP D OD1 1 
ATOM   12803 O  OD2 . ASP D 2 328 ? 19.919  -45.588 7.450   1.00 29.38  ? 328 ASP D OD2 1 
ATOM   12804 N  N   . PRO D 2 329 ? 24.141  -44.517 4.585   1.00 25.06  ? 329 PRO D N   1 
ATOM   12805 C  CA  . PRO D 2 329 ? 25.547  -44.294 4.180   1.00 23.20  ? 329 PRO D CA  1 
ATOM   12806 C  C   . PRO D 2 329 ? 25.702  -43.024 3.362   1.00 21.96  ? 329 PRO D C   1 
ATOM   12807 O  O   . PRO D 2 329 ? 26.624  -42.245 3.602   1.00 24.06  ? 329 PRO D O   1 
ATOM   12808 C  CB  . PRO D 2 329 ? 25.905  -45.558 3.351   1.00 22.02  ? 329 PRO D CB  1 
ATOM   12809 C  CG  . PRO D 2 329 ? 24.942  -46.620 3.904   1.00 25.29  ? 329 PRO D CG  1 
ATOM   12810 C  CD  . PRO D 2 329 ? 23.638  -45.847 4.149   1.00 24.87  ? 329 PRO D CD  1 
ATOM   12811 N  N   . HIS D 2 330 ? 24.781  -42.775 2.447   1.00 22.97  ? 330 HIS D N   1 
ATOM   12812 C  CA  . HIS D 2 330 ? 24.936  -41.612 1.590   1.00 24.60  ? 330 HIS D CA  1 
ATOM   12813 C  C   . HIS D 2 330 ? 24.468  -40.365 2.320   1.00 23.46  ? 330 HIS D C   1 
ATOM   12814 O  O   . HIS D 2 330 ? 25.025  -39.281 2.104   1.00 25.06  ? 330 HIS D O   1 
ATOM   12815 C  CB  . HIS D 2 330 ? 24.196  -41.847 0.283   1.00 22.76  ? 330 HIS D CB  1 
ATOM   12816 C  CG  . HIS D 2 330 ? 24.842  -42.897 -0.562  1.00 22.53  ? 330 HIS D CG  1 
ATOM   12817 N  ND1 . HIS D 2 330 ? 25.622  -42.586 -1.658  1.00 25.05  ? 330 HIS D ND1 1 
ATOM   12818 C  CD2 . HIS D 2 330 ? 24.910  -44.241 -0.415  1.00 22.31  ? 330 HIS D CD2 1 
ATOM   12819 C  CE1 . HIS D 2 330 ? 26.084  -43.704 -2.193  1.00 23.10  ? 330 HIS D CE1 1 
ATOM   12820 N  NE2 . HIS D 2 330 ? 25.660  -44.725 -1.469  1.00 25.66  ? 330 HIS D NE2 1 
ATOM   12821 N  N   . GLU D 2 331 ? 23.462  -40.500 3.174   1.00 23.37  ? 331 GLU D N   1 
ATOM   12822 C  CA  . GLU D 2 331 ? 23.073  -39.353 4.025   1.00 24.46  ? 331 GLU D CA  1 
ATOM   12823 C  C   . GLU D 2 331 ? 24.225  -38.910 4.917   1.00 25.63  ? 331 GLU D C   1 
ATOM   12824 O  O   . GLU D 2 331 ? 24.374  -37.702 5.209   1.00 28.30  ? 331 GLU D O   1 
ATOM   12825 C  CB  . GLU D 2 331 ? 21.862  -39.737 4.854   1.00 25.36  ? 331 GLU D CB  1 
ATOM   12826 C  CG  . GLU D 2 331 ? 20.507  -39.712 4.079   1.00 25.26  ? 331 GLU D CG  1 
ATOM   12827 C  CD  . GLU D 2 331 ? 19.390  -40.277 4.928   1.00 28.07  ? 331 GLU D CD  1 
ATOM   12828 O  OE1 . GLU D 2 331 ? 19.680  -41.087 5.854   1.00 28.60  ? 331 GLU D OE1 1 
ATOM   12829 O  OE2 . GLU D 2 331 ? 18.204  -39.925 4.689   1.00 30.18  ? 331 GLU D OE2 1 
ATOM   12830 N  N   . GLY D 2 332 ? 25.018  -39.866 5.436   1.00 23.84  ? 332 GLY D N   1 
ATOM   12831 C  CA  . GLY D 2 332 ? 26.129  -39.467 6.306   1.00 27.22  ? 332 GLY D CA  1 
ATOM   12832 C  C   . GLY D 2 332 ? 27.229  -38.680 5.609   1.00 25.43  ? 332 GLY D C   1 
ATOM   12833 O  O   . GLY D 2 332 ? 27.876  -37.827 6.238   1.00 29.27  ? 332 GLY D O   1 
ATOM   12834 N  N   . ASP D 2 333 ? 27.507  -38.998 4.332   1.00 24.20  ? 333 ASP D N   1 
ATOM   12835 C  CA  . ASP D 2 333 ? 28.491  -38.303 3.513   1.00 25.50  ? 333 ASP D CA  1 
ATOM   12836 C  C   . ASP D 2 333 ? 27.979  -36.976 2.966   1.00 26.64  ? 333 ASP D C   1 
ATOM   12837 O  O   . ASP D 2 333 ? 28.791  -36.092 2.616   1.00 29.09  ? 333 ASP D O   1 
ATOM   12838 C  CB  . ASP D 2 333 ? 28.860  -39.190 2.317   1.00 25.77  ? 333 ASP D CB  1 
ATOM   12839 C  CG  . ASP D 2 333 ? 29.941  -40.198 2.631   1.00 26.03  ? 333 ASP D CG  1 
ATOM   12840 O  OD1 . ASP D 2 333 ? 30.275  -40.339 3.845   1.00 28.76  ? 333 ASP D OD1 1 
ATOM   12841 O  OD2 . ASP D 2 333 ? 30.412  -40.852 1.631   1.00 28.06  ? 333 ASP D OD2 1 
ATOM   12842 N  N   . TYR D 2 334 ? 26.653  -36.847 2.805   1.00 26.81  ? 334 TYR D N   1 
ATOM   12843 C  CA  . TYR D 2 334 ? 26.103  -35.826 1.893   1.00 25.89  ? 334 TYR D CA  1 
ATOM   12844 C  C   . TYR D 2 334 ? 26.463  -34.395 2.253   1.00 27.07  ? 334 TYR D C   1 
ATOM   12845 O  O   . TYR D 2 334 ? 26.890  -33.646 1.337   1.00 26.90  ? 334 TYR D O   1 
ATOM   12846 C  CB  . TYR D 2 334 ? 24.568  -35.959 1.822   1.00 29.31  ? 334 TYR D CB  1 
ATOM   12847 C  CG  . TYR D 2 334 ? 23.922  -34.763 1.167   1.00 28.30  ? 334 TYR D CG  1 
ATOM   12848 C  CD1 . TYR D 2 334 ? 24.048  -34.577 -0.210  1.00 28.81  ? 334 TYR D CD1 1 
ATOM   12849 C  CD2 . TYR D 2 334 ? 23.204  -33.826 1.909   1.00 24.95  ? 334 TYR D CD2 1 
ATOM   12850 C  CE1 . TYR D 2 334 ? 23.480  -33.494 -0.847  1.00 33.14  ? 334 TYR D CE1 1 
ATOM   12851 C  CE2 . TYR D 2 334 ? 22.624  -32.731 1.268   1.00 29.48  ? 334 TYR D CE2 1 
ATOM   12852 C  CZ  . TYR D 2 334 ? 22.781  -32.577 -0.107  1.00 31.19  ? 334 TYR D CZ  1 
ATOM   12853 O  OH  . TYR D 2 334 ? 22.182  -31.468 -0.683  1.00 35.89  ? 334 TYR D OH  1 
ATOM   12854 N  N   . PRO D 2 335 ? 26.254  -33.919 3.493   1.00 25.46  ? 335 PRO D N   1 
ATOM   12855 C  CA  . PRO D 2 335 ? 26.486  -32.484 3.759   1.00 25.08  ? 335 PRO D CA  1 
ATOM   12856 C  C   . PRO D 2 335 ? 27.901  -32.071 3.406   1.00 29.47  ? 335 PRO D C   1 
ATOM   12857 O  O   . PRO D 2 335 ? 28.097  -31.054 2.722   1.00 29.99  ? 335 PRO D O   1 
ATOM   12858 C  CB  . PRO D 2 335 ? 26.171  -32.344 5.244   1.00 25.86  ? 335 PRO D CB  1 
ATOM   12859 C  CG  . PRO D 2 335 ? 25.100  -33.406 5.456   1.00 26.15  ? 335 PRO D CG  1 
ATOM   12860 C  CD  . PRO D 2 335 ? 25.568  -34.561 4.648   1.00 25.46  ? 335 PRO D CD  1 
ATOM   12861 N  N   . ASP D 2 336 ? 28.896  -32.862 3.781   1.00 25.87  ? 336 ASP D N   1 
ATOM   12862 C  CA  . ASP D 2 336 ? 30.266  -32.461 3.461   1.00 27.63  ? 336 ASP D CA  1 
ATOM   12863 C  C   . ASP D 2 336 ? 30.670  -32.790 2.014   1.00 26.52  ? 336 ASP D C   1 
ATOM   12864 O  O   . ASP D 2 336 ? 31.443  -32.022 1.423   1.00 28.30  ? 336 ASP D O   1 
ATOM   12865 C  CB  . ASP D 2 336 ? 31.225  -33.061 4.485   1.00 27.46  ? 336 ASP D CB  1 
ATOM   12866 C  CG  . ASP D 2 336 ? 31.221  -32.281 5.826   1.00 32.38  ? 336 ASP D CG  1 
ATOM   12867 O  OD1 . ASP D 2 336 ? 30.354  -31.402 6.084   1.00 34.29  ? 336 ASP D OD1 1 
ATOM   12868 O  OD2 . ASP D 2 336 ? 32.120  -32.491 6.643   1.00 34.52  ? 336 ASP D OD2 1 
ATOM   12869 N  N   . LEU D 2 337 ? 30.153  -33.849 1.387   1.00 23.23  ? 337 LEU D N   1 
ATOM   12870 C  CA  . LEU D 2 337 ? 30.452  -34.010 -0.046  1.00 23.58  ? 337 LEU D CA  1 
ATOM   12871 C  C   . LEU D 2 337 ? 29.854  -32.869 -0.857  1.00 26.76  ? 337 LEU D C   1 
ATOM   12872 O  O   . LEU D 2 337 ? 30.512  -32.322 -1.758  1.00 26.90  ? 337 LEU D O   1 
ATOM   12873 C  CB  . LEU D 2 337 ? 29.926  -35.333 -0.548  1.00 24.92  ? 337 LEU D CB  1 
ATOM   12874 C  CG  . LEU D 2 337 ? 30.185  -35.599 -2.026  1.00 24.73  ? 337 LEU D CG  1 
ATOM   12875 C  CD1 . LEU D 2 337 ? 31.645  -35.477 -2.435  1.00 23.75  ? 337 LEU D CD1 1 
ATOM   12876 C  CD2 . LEU D 2 337 ? 29.698  -37.043 -2.325  1.00 27.62  ? 337 LEU D CD2 1 
ATOM   12877 N  N   . LYS D 2 338 ? 28.627  -32.459 -0.520  1.00 25.86  ? 338 LYS D N   1 
ATOM   12878 C  CA  . LYS D 2 338 ? 28.066  -31.271 -1.174  1.00 27.35  ? 338 LYS D CA  1 
ATOM   12879 C  C   . LYS D 2 338 ? 29.009  -30.091 -1.048  1.00 30.76  ? 338 LYS D C   1 
ATOM   12880 O  O   . LYS D 2 338 ? 29.332  -29.422 -2.047  1.00 32.52  ? 338 LYS D O   1 
ATOM   12881 C  CB  . LYS D 2 338 ? 26.702  -30.934 -0.572  1.00 32.03  ? 338 LYS D CB  1 
ATOM   12882 C  CG  . LYS D 2 338 ? 26.045  -29.664 -1.108  1.00 35.72  ? 338 LYS D CG  1 
ATOM   12883 C  CD  . LYS D 2 338 ? 25.100  -29.054 -0.070  1.00 35.09  ? 338 LYS D CD  1 
ATOM   12884 C  CE  . LYS D 2 338 ? 24.437  -27.766 -0.589  1.00 36.70  ? 338 LYS D CE  1 
ATOM   12885 N  NZ  . LYS D 2 338 ? 23.442  -27.291 0.404   1.00 49.61  ? 338 LYS D NZ  1 
ATOM   12886 N  N   . ARG D 2 339 ? 29.432  -29.789 0.179   1.00 27.35  ? 339 ARG D N   1 
ATOM   12887 C  CA  . ARG D 2 339 ? 30.296  -28.629 0.398   1.00 32.96  ? 339 ARG D CA  1 
ATOM   12888 C  C   . ARG D 2 339 ? 31.580  -28.749 -0.404  1.00 34.68  ? 339 ARG D C   1 
ATOM   12889 O  O   . ARG D 2 339 ? 32.041  -27.762 -0.998  1.00 30.92  ? 339 ARG D O   1 
ATOM   12890 C  CB  . ARG D 2 339 ? 30.636  -28.476 1.879   1.00 32.42  ? 339 ARG D CB  1 
ATOM   12891 C  CG  . ARG D 2 339 ? 29.472  -27.959 2.718   1.00 36.46  ? 339 ARG D CG  1 
ATOM   12892 C  CD  . ARG D 2 339 ? 29.782  -27.847 4.191   1.00 37.26  ? 339 ARG D CD  1 
ATOM   12893 N  NE  . ARG D 2 339 ? 30.877  -26.925 4.476   1.00 33.81  ? 339 ARG D NE  1 
ATOM   12894 C  CZ  . ARG D 2 339 ? 31.466  -26.796 5.654   1.00 33.68  ? 339 ARG D CZ  1 
ATOM   12895 N  NH1 . ARG D 2 339 ? 31.100  -27.528 6.701   1.00 36.09  ? 339 ARG D NH1 1 
ATOM   12896 N  NH2 . ARG D 2 339 ? 32.386  -25.845 5.814   1.00 41.63  ? 339 ARG D NH2 1 
ATOM   12897 N  N   . HIS D 2 340 ? 32.165  -29.962 -0.444  1.00 31.30  ? 340 HIS D N   1 
ATOM   12898 C  CA  . HIS D 2 340 ? 33.414  -30.176 -1.177  1.00 29.54  ? 340 HIS D CA  1 
ATOM   12899 C  C   . HIS D 2 340 ? 33.261  -29.804 -2.643  1.00 31.51  ? 340 HIS D C   1 
ATOM   12900 O  O   . HIS D 2 340 ? 34.141  -29.151 -3.240  1.00 31.44  ? 340 HIS D O   1 
ATOM   12901 C  CB  . HIS D 2 340 ? 33.847  -31.650 -1.013  1.00 30.20  ? 340 HIS D CB  1 
ATOM   12902 C  CG  . HIS D 2 340 ? 35.231  -31.946 -1.498  1.00 31.34  ? 340 HIS D CG  1 
ATOM   12903 N  ND1 . HIS D 2 340 ? 36.348  -31.274 -1.036  1.00 33.41  ? 340 HIS D ND1 1 
ATOM   12904 C  CD2 . HIS D 2 340 ? 35.686  -32.899 -2.350  1.00 30.19  ? 340 HIS D CD2 1 
ATOM   12905 C  CE1 . HIS D 2 340 ? 37.422  -31.767 -1.631  1.00 34.41  ? 340 HIS D CE1 1 
ATOM   12906 N  NE2 . HIS D 2 340 ? 37.052  -32.775 -2.401  1.00 31.77  ? 340 HIS D NE2 1 
ATOM   12907 N  N   . LEU D 2 341 ? 32.148  -30.212 -3.248  1.00 30.20  ? 341 LEU D N   1 
ATOM   12908 C  CA  . LEU D 2 341 ? 31.937  -29.883 -4.646  1.00 29.21  ? 341 LEU D CA  1 
ATOM   12909 C  C   . LEU D 2 341 ? 31.641  -28.396 -4.794  1.00 29.97  ? 341 LEU D C   1 
ATOM   12910 O  O   . LEU D 2 341 ? 32.137  -27.731 -5.729  1.00 29.29  ? 341 LEU D O   1 
ATOM   12911 C  CB  . LEU D 2 341 ? 30.783  -30.683 -5.199  1.00 27.77  ? 341 LEU D CB  1 
ATOM   12912 C  CG  . LEU D 2 341 ? 31.040  -32.203 -5.204  1.00 25.71  ? 341 LEU D CG  1 
ATOM   12913 C  CD1 . LEU D 2 341 ? 29.755  -32.877 -5.595  1.00 30.35  ? 341 LEU D CD1 1 
ATOM   12914 C  CD2 . LEU D 2 341 ? 32.177  -32.517 -6.125  1.00 32.20  ? 341 LEU D CD2 1 
ATOM   12915 N  N   . GLU D 2 342 ? 30.849  -27.844 -3.882  1.00 29.29  ? 342 GLU D N   1 
ATOM   12916 C  CA  . GLU D 2 342 ? 30.502  -26.421 -4.057  1.00 28.11  ? 342 GLU D CA  1 
ATOM   12917 C  C   . GLU D 2 342 ? 31.700  -25.524 -3.808  1.00 29.34  ? 342 GLU D C   1 
ATOM   12918 O  O   . GLU D 2 342 ? 31.858  -24.489 -4.470  1.00 31.94  ? 342 GLU D O   1 
ATOM   12919 C  CB  . GLU D 2 342 ? 29.326  -26.045 -3.165  1.00 34.28  ? 342 GLU D CB  1 
ATOM   12920 C  CG  . GLU D 2 342 ? 28.043  -26.610 -3.702  1.00 34.58  ? 342 GLU D CG  1 
ATOM   12921 C  CD  . GLU D 2 342 ? 26.795  -26.309 -2.856  1.00 45.56  ? 342 GLU D CD  1 
ATOM   12922 O  OE1 . GLU D 2 342 ? 26.900  -25.811 -1.712  1.00 47.44  ? 342 GLU D OE1 1 
ATOM   12923 O  OE2 . GLU D 2 342 ? 25.675  -26.553 -3.379  1.00 48.62  ? 342 GLU D OE2 1 
ATOM   12924 N  N   . GLU D 2 343 ? 32.555  -25.885 -2.857  1.00 33.75  ? 343 GLU D N   1 
ATOM   12925 C  CA  . GLU D 2 343 ? 33.760  -25.098 -2.617  1.00 32.99  ? 343 GLU D CA  1 
ATOM   12926 C  C   . GLU D 2 343 ? 34.724  -25.167 -3.789  1.00 32.23  ? 343 GLU D C   1 
ATOM   12927 O  O   . GLU D 2 343 ? 35.557  -24.275 -3.951  1.00 33.00  ? 343 GLU D O   1 
ATOM   12928 C  CB  . GLU D 2 343 ? 34.401  -25.573 -1.317  1.00 34.39  ? 343 GLU D CB  1 
ATOM   12929 C  CG  . GLU D 2 343 ? 33.480  -25.200 -0.149  1.00 33.01  ? 343 GLU D CG  1 
ATOM   12930 C  CD  . GLU D 2 343 ? 33.837  -25.837 1.171   1.00 38.84  ? 343 GLU D CD  1 
ATOM   12931 O  OE1 . GLU D 2 343 ? 34.820  -26.612 1.226   1.00 41.18  ? 343 GLU D OE1 1 
ATOM   12932 O  OE2 . GLU D 2 343 ? 33.176  -25.457 2.183   1.00 40.24  ? 343 GLU D OE2 1 
ATOM   12933 N  N   . ASN D 2 344 ? 34.608  -26.180 -4.621  1.00 30.81  ? 344 ASN D N   1 
ATOM   12934 C  CA  . ASN D 2 344 ? 35.476  -26.336 -5.769  1.00 33.72  ? 344 ASN D CA  1 
ATOM   12935 C  C   . ASN D 2 344 ? 34.783  -25.942 -7.061  1.00 35.65  ? 344 ASN D C   1 
ATOM   12936 O  O   . ASN D 2 344 ? 35.155  -26.432 -8.134  1.00 43.03  ? 344 ASN D O   1 
ATOM   12937 C  CB  . ASN D 2 344 ? 35.980  -27.779 -5.815  1.00 31.11  ? 344 ASN D CB  1 
ATOM   12938 C  CG  . ASN D 2 344 ? 37.097  -28.000 -4.822  1.00 34.01  ? 344 ASN D CG  1 
ATOM   12939 O  OD1 . ASN D 2 344 ? 38.252  -27.687 -5.101  1.00 37.05  ? 344 ASN D OD1 1 
ATOM   12940 N  ND2 . ASN D 2 344 ? 36.751  -28.469 -3.627  1.00 33.64  ? 344 ASN D ND2 1 
ATOM   12941 N  N   . GLY D 2 345 ? 33.753  -25.106 -6.979  1.00 33.38  ? 345 GLY D N   1 
ATOM   12942 C  CA  . GLY D 2 345 ? 33.167  -24.475 -8.138  1.00 38.85  ? 345 GLY D CA  1 
ATOM   12943 C  C   . GLY D 2 345 ? 32.080  -25.246 -8.858  1.00 40.19  ? 345 GLY D C   1 
ATOM   12944 O  O   . GLY D 2 345 ? 31.770  -24.903 -10.003 1.00 43.26  ? 345 GLY D O   1 
ATOM   12945 N  N   . ILE D 2 346 ? 31.489  -26.258 -8.243  1.00 36.41  ? 346 ILE D N   1 
ATOM   12946 C  CA  . ILE D 2 346 ? 30.432  -27.049 -8.864  1.00 38.10  ? 346 ILE D CA  1 
ATOM   12947 C  C   . ILE D 2 346 ? 29.158  -26.902 -8.052  1.00 34.06  ? 346 ILE D C   1 
ATOM   12948 O  O   . ILE D 2 346 ? 29.007  -27.526 -7.003  1.00 35.24  ? 346 ILE D O   1 
ATOM   12949 C  CB  . ILE D 2 346 ? 30.820  -28.532 -8.993  1.00 35.12  ? 346 ILE D CB  1 
ATOM   12950 C  CG1 . ILE D 2 346 ? 32.047  -28.706 -9.869  1.00 42.37  ? 346 ILE D CG1 1 
ATOM   12951 C  CG2 . ILE D 2 346 ? 29.619  -29.419 -9.418  1.00 33.73  ? 346 ILE D CG2 1 
ATOM   12952 C  CD1 . ILE D 2 346 ? 33.117  -29.471 -9.205  1.00 35.09  ? 346 ILE D CD1 1 
ATOM   12953 N  N   . PRO D 2 347 ? 28.184  -26.148 -8.552  1.00 34.03  ? 347 PRO D N   1 
ATOM   12954 C  CA  . PRO D 2 347 ? 26.882  -26.108 -7.889  1.00 34.08  ? 347 PRO D CA  1 
ATOM   12955 C  C   . PRO D 2 347 ? 26.199  -27.464 -7.904  1.00 34.66  ? 347 PRO D C   1 
ATOM   12956 O  O   . PRO D 2 347 ? 26.417  -28.288 -8.793  1.00 35.83  ? 347 PRO D O   1 
ATOM   12957 C  CB  . PRO D 2 347 ? 26.094  -25.069 -8.684  1.00 38.87  ? 347 PRO D CB  1 
ATOM   12958 C  CG  . PRO D 2 347 ? 27.012  -24.535 -9.708  1.00 42.53  ? 347 PRO D CG  1 
ATOM   12959 C  CD  . PRO D 2 347 ? 28.221  -25.346 -9.788  1.00 36.33  ? 347 PRO D CD  1 
ATOM   12960 N  N   . THR D 2 348 ? 25.379  -27.686 -6.882  1.00 33.46  ? 348 THR D N   1 
ATOM   12961 C  CA  . THR D 2 348 ? 24.729  -28.968 -6.661  1.00 28.99  ? 348 THR D CA  1 
ATOM   12962 C  C   . THR D 2 348 ? 23.213  -28.817 -6.454  1.00 30.34  ? 348 THR D C   1 
ATOM   12963 O  O   . THR D 2 348 ? 22.685  -27.765 -6.056  1.00 31.14  ? 348 THR D O   1 
ATOM   12964 C  CB  . THR D 2 348 ? 25.365  -29.711 -5.471  1.00 34.67  ? 348 THR D CB  1 
ATOM   12965 O  OG1 . THR D 2 348 ? 25.062  -29.018 -4.252  1.00 36.67  ? 348 THR D OG1 1 
ATOM   12966 C  CG2 . THR D 2 348 ? 26.893  -29.869 -5.658  1.00 33.04  ? 348 THR D CG2 1 
ATOM   12967 N  N   . LEU D 2 349 ? 22.517  -29.920 -6.724  1.00 31.97  ? 349 LEU D N   1 
ATOM   12968 C  CA  . LEU D 2 349 ? 21.076  -30.029 -6.583  1.00 31.95  ? 349 LEU D CA  1 
ATOM   12969 C  C   . LEU D 2 349 ? 20.806  -31.338 -5.837  1.00 30.40  ? 349 LEU D C   1 
ATOM   12970 O  O   . LEU D 2 349 ? 21.490  -32.316 -6.085  1.00 30.21  ? 349 LEU D O   1 
ATOM   12971 C  CB  . LEU D 2 349 ? 20.397  -30.076 -7.927  1.00 31.81  ? 349 LEU D CB  1 
ATOM   12972 C  CG  . LEU D 2 349 ? 18.886  -30.284 -7.901  1.00 34.65  ? 349 LEU D CG  1 
ATOM   12973 C  CD1 . LEU D 2 349 ? 18.202  -29.062 -7.328  1.00 36.80  ? 349 LEU D CD1 1 
ATOM   12974 C  CD2 . LEU D 2 349 ? 18.391  -30.555 -9.297  1.00 35.39  ? 349 LEU D CD2 1 
ATOM   12975 N  N   . PHE D 2 350 ? 19.802  -31.345 -4.946  1.00 30.20  ? 350 PHE D N   1 
ATOM   12976 C  CA  . PHE D 2 350 ? 19.437  -32.520 -4.142  1.00 29.19  ? 350 PHE D CA  1 
ATOM   12977 C  C   . PHE D 2 350 ? 18.023  -32.955 -4.475  1.00 32.54  ? 350 PHE D C   1 
ATOM   12978 O  O   . PHE D 2 350 ? 17.084  -32.166 -4.368  1.00 32.75  ? 350 PHE D O   1 
ATOM   12979 C  CB  . PHE D 2 350 ? 19.531  -32.201 -2.634  1.00 30.03  ? 350 PHE D CB  1 
ATOM   12980 C  CG  . PHE D 2 350 ? 19.132  -33.335 -1.745  1.00 32.54  ? 350 PHE D CG  1 
ATOM   12981 C  CD1 . PHE D 2 350 ? 20.074  -34.327 -1.436  1.00 34.29  ? 350 PHE D CD1 1 
ATOM   12982 C  CD2 . PHE D 2 350 ? 17.867  -33.392 -1.165  1.00 32.41  ? 350 PHE D CD2 1 
ATOM   12983 C  CE1 . PHE D 2 350 ? 19.723  -35.379 -0.596  1.00 35.01  ? 350 PHE D CE1 1 
ATOM   12984 C  CE2 . PHE D 2 350 ? 17.496  -34.446 -0.345  1.00 35.54  ? 350 PHE D CE2 1 
ATOM   12985 C  CZ  . PHE D 2 350 ? 18.425  -35.424 -0.036  1.00 35.42  ? 350 PHE D CZ  1 
ATOM   12986 N  N   . LEU D 2 351 ? 17.855  -34.209 -4.853  1.00 30.56  ? 351 LEU D N   1 
ATOM   12987 C  CA  . LEU D 2 351 ? 16.524  -34.740 -5.131  1.00 28.83  ? 351 LEU D CA  1 
ATOM   12988 C  C   . LEU D 2 351 ? 16.398  -36.054 -4.368  1.00 29.83  ? 351 LEU D C   1 
ATOM   12989 O  O   . LEU D 2 351 ? 17.353  -36.819 -4.299  1.00 30.38  ? 351 LEU D O   1 
ATOM   12990 C  CB  . LEU D 2 351 ? 16.322  -34.979 -6.631  1.00 29.37  ? 351 LEU D CB  1 
ATOM   12991 C  CG  . LEU D 2 351 ? 16.528  -33.763 -7.547  1.00 29.68  ? 351 LEU D CG  1 
ATOM   12992 C  CD1 . LEU D 2 351 ? 16.517  -34.228 -9.034  1.00 34.28  ? 351 LEU D CD1 1 
ATOM   12993 C  CD2 . LEU D 2 351 ? 15.421  -32.823 -7.255  1.00 34.58  ? 351 LEU D CD2 1 
ATOM   12994 N  N   . GLU D 2 352 ? 15.242  -36.282 -3.758  1.00 31.15  ? 352 GLU D N   1 
ATOM   12995 C  CA  . GLU D 2 352 ? 14.994  -37.466 -2.929  1.00 30.42  ? 352 GLU D CA  1 
ATOM   12996 C  C   . GLU D 2 352 ? 13.914  -38.343 -3.547  1.00 35.55  ? 352 GLU D C   1 
ATOM   12997 O  O   . GLU D 2 352 ? 12.893  -37.833 -4.020  1.00 33.81  ? 352 GLU D O   1 
ATOM   12998 C  CB  . GLU D 2 352 ? 14.541  -37.086 -1.520  1.00 35.86  ? 352 GLU D CB  1 
ATOM   12999 C  CG  . GLU D 2 352 ? 14.726  -38.237 -0.533  1.00 38.77  ? 352 GLU D CG  1 
ATOM   13000 C  CD  . GLU D 2 352 ? 14.308  -37.877 0.899   1.00 45.19  ? 352 GLU D CD  1 
ATOM   13001 O  OE1 . GLU D 2 352 ? 13.240  -37.247 1.078   1.00 44.34  ? 352 GLU D OE1 1 
ATOM   13002 O  OE2 . GLU D 2 352 ? 15.067  -38.262 1.836   1.00 46.25  ? 352 GLU D OE2 1 
ATOM   13003 N  N   . PHE D 2 353 ? 14.116  -39.664 -3.498  1.00 32.81  ? 353 PHE D N   1 
ATOM   13004 C  CA  . PHE D 2 353 ? 13.284  -40.609 -4.239  1.00 40.51  ? 353 PHE D CA  1 
ATOM   13005 C  C   . PHE D 2 353 ? 12.657  -41.671 -3.353  1.00 40.07  ? 353 PHE D C   1 
ATOM   13006 O  O   . PHE D 2 353 ? 13.292  -42.186 -2.423  1.00 38.75  ? 353 PHE D O   1 
ATOM   13007 C  CB  . PHE D 2 353 ? 14.090  -41.306 -5.346  1.00 37.63  ? 353 PHE D CB  1 
ATOM   13008 C  CG  . PHE D 2 353 ? 14.605  -40.353 -6.355  1.00 40.08  ? 353 PHE D CG  1 
ATOM   13009 C  CD1 . PHE D 2 353 ? 15.758  -39.631 -6.121  1.00 36.22  ? 353 PHE D CD1 1 
ATOM   13010 C  CD2 . PHE D 2 353 ? 13.863  -40.086 -7.495  1.00 40.67  ? 353 PHE D CD2 1 
ATOM   13011 C  CE1 . PHE D 2 353 ? 16.196  -38.696 -7.040  1.00 36.19  ? 353 PHE D CE1 1 
ATOM   13012 C  CE2 . PHE D 2 353 ? 14.294  -39.139 -8.432  1.00 42.97  ? 353 PHE D CE2 1 
ATOM   13013 C  CZ  . PHE D 2 353 ? 15.475  -38.454 -8.206  1.00 39.02  ? 353 PHE D CZ  1 
ATOM   13014 N  N   . ASP D 2 354 ? 11.418  -42.034 -3.692  1.00 42.76  ? 354 ASP D N   1 
ATOM   13015 C  CA  . ASP D 2 354 ? 10.777  -43.208 -3.127  1.00 42.50  ? 354 ASP D CA  1 
ATOM   13016 C  C   . ASP D 2 354 ? 10.781  -44.327 -4.179  1.00 46.93  ? 354 ASP D C   1 
ATOM   13017 O  O   . ASP D 2 354 ? 11.499  -44.247 -5.184  1.00 45.26  ? 354 ASP D O   1 
ATOM   13018 C  CB  . ASP D 2 354 ? 9.382   -42.852 -2.646  1.00 50.45  ? 354 ASP D CB  1 
ATOM   13019 C  CG  . ASP D 2 354 ? 9.019   -43.578 -1.369  1.00 56.77  ? 354 ASP D CG  1 
ATOM   13020 O  OD1 . ASP D 2 354 ? 9.144   -44.830 -1.334  1.00 53.64  ? 354 ASP D OD1 1 
ATOM   13021 O  OD2 . ASP D 2 354 ? 8.610   -42.892 -0.400  1.00 61.95  ? 354 ASP D OD2 1 
ATOM   13022 N  N   . ILE D 2 355 ? 9.988   -45.384 -3.948  1.00 48.74  ? 355 ILE D N   1 
ATOM   13023 C  CA  . ILE D 2 355 ? 9.955   -46.479 -4.917  1.00 49.59  ? 355 ILE D CA  1 
ATOM   13024 C  C   . ILE D 2 355 ? 9.477   -45.953 -6.262  1.00 51.62  ? 355 ILE D C   1 
ATOM   13025 O  O   . ILE D 2 355 ? 10.137  -46.141 -7.290  1.00 50.97  ? 355 ILE D O   1 
ATOM   13026 C  CB  . ILE D 2 355 ? 9.089   -47.655 -4.424  1.00 49.75  ? 355 ILE D CB  1 
ATOM   13027 C  CG1 . ILE D 2 355 ? 9.735   -48.380 -3.232  1.00 49.81  ? 355 ILE D CG1 1 
ATOM   13028 C  CG2 . ILE D 2 355 ? 8.917   -48.691 -5.544  1.00 50.32  ? 355 ILE D CG2 1 
ATOM   13029 C  CD1 . ILE D 2 355 ? 9.157   -49.806 -2.996  1.00 46.36  ? 355 ILE D CD1 1 
ATOM   13030 N  N   . THR D 2 356 ? 8.356   -45.235 -6.263  1.00 50.71  ? 356 THR D N   1 
ATOM   13031 C  CA  . THR D 2 356 ? 7.878   -44.512 -7.432  1.00 53.82  ? 356 THR D CA  1 
ATOM   13032 C  C   . THR D 2 356 ? 7.748   -43.024 -7.108  1.00 57.22  ? 356 THR D C   1 
ATOM   13033 O  O   . THR D 2 356 ? 7.416   -42.643 -5.979  1.00 57.41  ? 356 THR D O   1 
ATOM   13034 C  CB  . THR D 2 356 ? 6.519   -45.025 -7.894  1.00 56.55  ? 356 THR D CB  1 
ATOM   13035 O  OG1 . THR D 2 356 ? 5.550   -44.828 -6.858  1.00 59.90  ? 356 THR D OG1 1 
ATOM   13036 C  CG2 . THR D 2 356 ? 6.592   -46.493 -8.172  1.00 52.47  ? 356 THR D CG2 1 
ATOM   13037 N  N   . ASN D 2 357 ? 7.973   -42.171 -8.116  1.00 60.39  ? 357 ASN D N   1 
ATOM   13038 C  CA  . ASN D 2 357 ? 7.822   -40.706 -7.899  1.00 59.12  ? 357 ASN D CA  1 
ATOM   13039 C  C   . ASN D 2 357 ? 7.284   -40.064 -9.171  1.00 59.70  ? 357 ASN D C   1 
ATOM   13040 O  O   . ASN D 2 357 ? 7.844   -40.312 -10.253 1.00 58.36  ? 357 ASN D O   1 
ATOM   13041 C  CB  . ASN D 2 357 ? 9.149   -40.052 -7.535  1.00 56.46  ? 357 ASN D CB  1 
ATOM   13042 C  CG  . ASN D 2 357 ? 9.760   -40.637 -6.293  1.00 52.32  ? 357 ASN D CG  1 
ATOM   13043 O  OD1 . ASN D 2 357 ? 10.577  -41.523 -6.403  1.00 49.78  ? 357 ASN D OD1 1 
ATOM   13044 N  ND2 . ASN D 2 357 ? 9.387   -40.134 -5.112  1.00 52.17  ? 357 ASN D ND2 1 
ATOM   13045 N  N   . PRO D 2 358 ? 6.225   -39.259 -9.089  1.00 59.55  ? 358 PRO D N   1 
ATOM   13046 C  CA  . PRO D 2 358 ? 5.813   -38.467 -10.259 1.00 56.55  ? 358 PRO D CA  1 
ATOM   13047 C  C   . PRO D 2 358 ? 6.967   -37.608 -10.768 1.00 54.39  ? 358 PRO D C   1 
ATOM   13048 O  O   . PRO D 2 358 ? 7.601   -36.870 -10.009 1.00 54.23  ? 358 PRO D O   1 
ATOM   13049 C  CB  . PRO D 2 358 ? 4.657   -37.613 -9.724  1.00 57.05  ? 358 PRO D CB  1 
ATOM   13050 C  CG  . PRO D 2 358 ? 4.205   -38.281 -8.433  1.00 56.13  ? 358 PRO D CG  1 
ATOM   13051 C  CD  . PRO D 2 358 ? 5.130   -39.425 -8.121  1.00 57.22  ? 358 PRO D CD  1 
ATOM   13052 N  N   . ILE D 2 359 ? 7.228   -37.698 -12.076 1.00 54.91  ? 359 ILE D N   1 
ATOM   13053 C  CA  . ILE D 2 359 ? 8.417   -37.054 -12.627 1.00 57.50  ? 359 ILE D CA  1 
ATOM   13054 C  C   . ILE D 2 359 ? 8.270   -35.527 -12.769 1.00 53.49  ? 359 ILE D C   1 
ATOM   13055 O  O   . ILE D 2 359 ? 9.286   -34.819 -12.723 1.00 50.32  ? 359 ILE D O   1 
ATOM   13056 C  CB  . ILE D 2 359 ? 8.806   -37.756 -13.947 1.00 58.45  ? 359 ILE D CB  1 
ATOM   13057 C  CG1 . ILE D 2 359 ? 10.275  -37.456 -14.283 1.00 59.55  ? 359 ILE D CG1 1 
ATOM   13058 C  CG2 . ILE D 2 359 ? 7.850   -37.402 -15.085 1.00 53.39  ? 359 ILE D CG2 1 
ATOM   13059 C  CD1 . ILE D 2 359 ? 11.086  -38.659 -14.757 1.00 51.75  ? 359 ILE D CD1 1 
ATOM   13060 N  N   . GLY D 2 360 ? 7.040   -35.001 -12.870 1.00 51.11  ? 360 GLY D N   1 
ATOM   13061 C  CA  . GLY D 2 360 ? 6.778   -33.582 -12.999 1.00 52.27  ? 360 GLY D CA  1 
ATOM   13062 C  C   . GLY D 2 360 ? 7.531   -32.645 -12.057 1.00 54.02  ? 360 GLY D C   1 
ATOM   13063 O  O   . GLY D 2 360 ? 8.216   -31.722 -12.510 1.00 50.64  ? 360 GLY D O   1 
ATOM   13064 N  N   . PRO D 2 361 ? 7.394   -32.827 -10.732 1.00 53.82  ? 361 PRO D N   1 
ATOM   13065 C  CA  . PRO D 2 361 ? 8.068   -31.896 -9.811  1.00 49.79  ? 361 PRO D CA  1 
ATOM   13066 C  C   . PRO D 2 361 ? 9.576   -31.976 -9.885  1.00 49.43  ? 361 PRO D C   1 
ATOM   13067 O  O   . PRO D 2 361 ? 10.241  -30.958 -9.665  1.00 49.58  ? 361 PRO D O   1 
ATOM   13068 C  CB  . PRO D 2 361 ? 7.556   -32.321 -8.429  1.00 51.32  ? 361 PRO D CB  1 
ATOM   13069 C  CG  . PRO D 2 361 ? 6.298   -33.039 -8.694  1.00 52.51  ? 361 PRO D CG  1 
ATOM   13070 C  CD  . PRO D 2 361 ? 6.483   -33.733 -10.011 1.00 52.11  ? 361 PRO D CD  1 
ATOM   13071 N  N   . PHE D 2 362 ? 10.145  -33.153 -10.163 1.00 47.34  ? 362 PHE D N   1 
ATOM   13072 C  CA  . PHE D 2 362 ? 11.588  -33.227 -10.365 1.00 45.46  ? 362 PHE D CA  1 
ATOM   13073 C  C   . PHE D 2 362 ? 11.996  -32.480 -11.627 1.00 43.56  ? 362 PHE D C   1 
ATOM   13074 O  O   . PHE D 2 362 ? 13.013  -31.783 -11.635 1.00 41.49  ? 362 PHE D O   1 
ATOM   13075 C  CB  . PHE D 2 362 ? 12.051  -34.681 -10.431 1.00 44.83  ? 362 PHE D CB  1 
ATOM   13076 C  CG  . PHE D 2 362 ? 11.749  -35.474 -9.190  1.00 46.11  ? 362 PHE D CG  1 
ATOM   13077 C  CD1 . PHE D 2 362 ? 12.574  -35.408 -8.096  1.00 44.09  ? 362 PHE D CD1 1 
ATOM   13078 C  CD2 . PHE D 2 362 ? 10.610  -36.249 -9.109  1.00 52.64  ? 362 PHE D CD2 1 
ATOM   13079 C  CE1 . PHE D 2 362 ? 12.313  -36.149 -6.952  1.00 46.92  ? 362 PHE D CE1 1 
ATOM   13080 C  CE2 . PHE D 2 362 ? 10.330  -36.987 -7.962  1.00 55.06  ? 362 PHE D CE2 1 
ATOM   13081 C  CZ  . PHE D 2 362 ? 11.182  -36.939 -6.884  1.00 50.00  ? 362 PHE D CZ  1 
ATOM   13082 N  N   . ARG D 2 363 ? 11.205  -32.586 -12.690 1.00 41.86  ? 363 ARG D N   1 
ATOM   13083 C  CA  . ARG D 2 363 ? 11.532  -31.823 -13.890 1.00 44.82  ? 363 ARG D CA  1 
ATOM   13084 C  C   . ARG D 2 363 ? 11.532  -30.325 -13.608 1.00 45.95  ? 363 ARG D C   1 
ATOM   13085 O  O   . ARG D 2 363 ? 12.401  -29.599 -14.096 1.00 47.37  ? 363 ARG D O   1 
ATOM   13086 C  CB  . ARG D 2 363 ? 10.563  -32.127 -15.026 1.00 51.15  ? 363 ARG D CB  1 
ATOM   13087 C  CG  . ARG D 2 363 ? 11.054  -31.597 -16.366 1.00 51.29  ? 363 ARG D CG  1 
ATOM   13088 C  CD  . ARG D 2 363 ? 10.022  -31.792 -17.474 1.00 56.74  ? 363 ARG D CD  1 
ATOM   13089 N  NE  . ARG D 2 363 ? 9.406   -33.115 -17.420 1.00 66.87  ? 363 ARG D NE  1 
ATOM   13090 C  CZ  . ARG D 2 363 ? 8.139   -33.355 -17.083 1.00 70.55  ? 363 ARG D CZ  1 
ATOM   13091 N  NH1 . ARG D 2 363 ? 7.298   -32.373 -16.776 1.00 66.85  ? 363 ARG D NH1 1 
ATOM   13092 N  NH2 . ARG D 2 363 ? 7.704   -34.616 -17.056 1.00 69.04  ? 363 ARG D NH2 1 
ATOM   13093 N  N   . ILE D 2 364 ? 10.558  -29.831 -12.846 1.00 44.11  ? 364 ILE D N   1 
ATOM   13094 C  CA  . ILE D 2 364 ? 10.550  -28.396 -12.557 1.00 48.81  ? 364 ILE D CA  1 
ATOM   13095 C  C   . ILE D 2 364 ? 11.825  -28.026 -11.813 1.00 46.45  ? 364 ILE D C   1 
ATOM   13096 O  O   . ILE D 2 364 ? 12.461  -27.004 -12.099 1.00 45.93  ? 364 ILE D O   1 
ATOM   13097 C  CB  . ILE D 2 364 ? 9.294   -27.998 -11.754 1.00 46.74  ? 364 ILE D CB  1 
ATOM   13098 C  CG1 . ILE D 2 364 ? 8.021   -28.160 -12.593 1.00 45.46  ? 364 ILE D CG1 1 
ATOM   13099 C  CG2 . ILE D 2 364 ? 9.392   -26.575 -11.259 1.00 51.89  ? 364 ILE D CG2 1 
ATOM   13100 C  CD1 . ILE D 2 364 ? 6.722   -27.856 -11.815 1.00 47.64  ? 364 ILE D CD1 1 
ATOM   13101 N  N   . ARG D 2 365 ? 12.222  -28.869 -10.858 1.00 41.02  ? 365 ARG D N   1 
ATOM   13102 C  CA  . ARG D 2 365 ? 13.432  -28.621 -10.082 1.00 41.68  ? 365 ARG D CA  1 
ATOM   13103 C  C   . ARG D 2 365 ? 14.687  -28.612 -10.943 1.00 42.45  ? 365 ARG D C   1 
ATOM   13104 O  O   . ARG D 2 365 ? 15.574  -27.771 -10.736 1.00 41.12  ? 365 ARG D O   1 
ATOM   13105 C  CB  . ARG D 2 365 ? 13.555  -29.659 -8.967  1.00 42.58  ? 365 ARG D CB  1 
ATOM   13106 C  CG  . ARG D 2 365 ? 12.437  -29.517 -7.951  1.00 44.04  ? 365 ARG D CG  1 
ATOM   13107 C  CD  . ARG D 2 365 ? 12.764  -28.366 -7.016  1.00 46.49  ? 365 ARG D CD  1 
ATOM   13108 N  NE  . ARG D 2 365 ? 14.102  -28.481 -6.432  1.00 47.49  ? 365 ARG D NE  1 
ATOM   13109 C  CZ  . ARG D 2 365 ? 14.408  -29.299 -5.434  1.00 50.34  ? 365 ARG D CZ  1 
ATOM   13110 N  NH1 . ARG D 2 365 ? 13.506  -30.126 -4.918  1.00 54.89  ? 365 ARG D NH1 1 
ATOM   13111 N  NH2 . ARG D 2 365 ? 15.655  -29.309 -4.958  1.00 53.11  ? 365 ARG D NH2 1 
ATOM   13112 N  N   . ILE D 2 366 ? 14.804  -29.554 -11.886 1.00 42.02  ? 366 ILE D N   1 
ATOM   13113 C  CA  . ILE D 2 366 ? 15.984  -29.585 -12.751 1.00 39.09  ? 366 ILE D CA  1 
ATOM   13114 C  C   . ILE D 2 366 ? 16.025  -28.340 -13.650 1.00 39.48  ? 366 ILE D C   1 
ATOM   13115 O  O   . ILE D 2 366 ? 17.090  -27.753 -13.858 1.00 40.55  ? 366 ILE D O   1 
ATOM   13116 C  CB  . ILE D 2 366 ? 16.012  -30.876 -13.599 1.00 42.87  ? 366 ILE D CB  1 
ATOM   13117 C  CG1 . ILE D 2 366 ? 16.105  -32.166 -12.733 1.00 38.89  ? 366 ILE D CG1 1 
ATOM   13118 C  CG2 . ILE D 2 366 ? 17.162  -30.800 -14.601 1.00 40.84  ? 366 ILE D CG2 1 
ATOM   13119 C  CD1 . ILE D 2 366 ? 17.408  -32.409 -12.089 1.00 41.66  ? 366 ILE D CD1 1 
ATOM   13120 N  N   . GLU D 2 367 ? 14.883  -27.937 -14.221 1.00 40.60  ? 367 GLU D N   1 
ATOM   13121 C  CA  . GLU D 2 367 ? 14.854  -26.734 -15.063 1.00 42.49  ? 367 GLU D CA  1 
ATOM   13122 C  C   . GLU D 2 367 ? 15.278  -25.508 -14.283 1.00 43.18  ? 367 GLU D C   1 
ATOM   13123 O  O   . GLU D 2 367 ? 15.934  -24.617 -14.825 1.00 46.66  ? 367 GLU D O   1 
ATOM   13124 C  CB  . GLU D 2 367 ? 13.456  -26.540 -15.650 1.00 46.90  ? 367 GLU D CB  1 
ATOM   13125 C  CG  . GLU D 2 367 ? 12.939  -27.807 -16.305 1.00 52.81  ? 367 GLU D CG  1 
ATOM   13126 C  CD  . GLU D 2 367 ? 11.590  -27.662 -16.968 1.00 55.54  ? 367 GLU D CD  1 
ATOM   13127 O  OE1 . GLU D 2 367 ? 10.579  -27.541 -16.234 1.00 59.98  ? 367 GLU D OE1 1 
ATOM   13128 O  OE2 . GLU D 2 367 ? 11.536  -27.706 -18.209 1.00 59.26  ? 367 GLU D OE2 1 
ATOM   13129 N  N   . ALA D 2 368 ? 14.892  -25.433 -13.011 1.00 43.35  ? 368 ALA D N   1 
ATOM   13130 C  CA  . ALA D 2 368 ? 15.314  -24.304 -12.187 1.00 47.94  ? 368 ALA D CA  1 
ATOM   13131 C  C   . ALA D 2 368 ? 16.814  -24.367 -11.907 1.00 46.11  ? 368 ALA D C   1 
ATOM   13132 O  O   . ALA D 2 368 ? 17.496  -23.333 -11.912 1.00 43.34  ? 368 ALA D O   1 
ATOM   13133 C  CB  . ALA D 2 368 ? 14.518  -24.275 -10.879 1.00 49.37  ? 368 ALA D CB  1 
ATOM   13134 N  N   . PHE D 2 369 ? 17.347  -25.578 -11.693 1.00 41.32  ? 369 PHE D N   1 
ATOM   13135 C  CA  . PHE D 2 369 ? 18.785  -25.740 -11.471 1.00 40.66  ? 369 PHE D CA  1 
ATOM   13136 C  C   . PHE D 2 369 ? 19.579  -25.307 -12.700 1.00 45.26  ? 369 PHE D C   1 
ATOM   13137 O  O   . PHE D 2 369 ? 20.600  -24.624 -12.576 1.00 47.55  ? 369 PHE D O   1 
ATOM   13138 C  CB  . PHE D 2 369 ? 19.084  -27.197 -11.099 1.00 38.99  ? 369 PHE D CB  1 
ATOM   13139 C  CG  . PHE D 2 369 ? 20.534  -27.486 -10.778 1.00 38.25  ? 369 PHE D CG  1 
ATOM   13140 C  CD1 . PHE D 2 369 ? 21.242  -26.730 -9.858  1.00 35.61  ? 369 PHE D CD1 1 
ATOM   13141 C  CD2 . PHE D 2 369 ? 21.182  -28.536 -11.409 1.00 37.32  ? 369 PHE D CD2 1 
ATOM   13142 C  CE1 . PHE D 2 369 ? 22.584  -27.047 -9.578  1.00 33.56  ? 369 PHE D CE1 1 
ATOM   13143 C  CE2 . PHE D 2 369 ? 22.506  -28.852 -11.141 1.00 37.89  ? 369 PHE D CE2 1 
ATOM   13144 C  CZ  . PHE D 2 369 ? 23.207  -28.114 -10.235 1.00 34.93  ? 369 PHE D CZ  1 
ATOM   13145 N  N   . LEU D 2 370 ? 19.126  -25.705 -13.895 1.00 43.41  ? 370 LEU D N   1 
ATOM   13146 C  CA  . LEU D 2 370 ? 19.741  -25.252 -15.144 1.00 45.14  ? 370 LEU D CA  1 
ATOM   13147 C  C   . LEU D 2 370 ? 19.812  -23.733 -15.189 1.00 49.29  ? 370 LEU D C   1 
ATOM   13148 O  O   . LEU D 2 370 ? 20.836  -23.151 -15.558 1.00 53.68  ? 370 LEU D O   1 
ATOM   13149 C  CB  . LEU D 2 370 ? 18.937  -25.767 -16.344 1.00 47.42  ? 370 LEU D CB  1 
ATOM   13150 C  CG  . LEU D 2 370 ? 19.568  -26.209 -17.669 1.00 52.63  ? 370 LEU D CG  1 
ATOM   13151 C  CD1 . LEU D 2 370 ? 20.551  -27.346 -17.487 1.00 50.89  ? 370 LEU D CD1 1 
ATOM   13152 C  CD2 . LEU D 2 370 ? 18.469  -26.571 -18.665 1.00 49.11  ? 370 LEU D CD2 1 
ATOM   13153 N  N   . GLU D 2 371 ? 18.714  -23.073 -14.831 1.00 50.78  ? 371 GLU D N   1 
ATOM   13154 C  CA  . GLU D 2 371 ? 18.663  -21.619 -14.921 1.00 52.09  ? 371 GLU D CA  1 
ATOM   13155 C  C   . GLU D 2 371 ? 19.615  -20.985 -13.917 1.00 58.21  ? 371 GLU D C   1 
ATOM   13156 O  O   . GLU D 2 371 ? 20.174  -19.920 -14.181 1.00 64.75  ? 371 GLU D O   1 
ATOM   13157 C  CB  . GLU D 2 371 ? 17.215  -21.176 -14.722 1.00 54.06  ? 371 GLU D CB  1 
ATOM   13158 C  CG  . GLU D 2 371 ? 16.341  -21.668 -15.889 1.00 60.25  ? 371 GLU D CG  1 
ATOM   13159 C  CD  . GLU D 2 371 ? 14.848  -21.377 -15.739 1.00 64.90  ? 371 GLU D CD  1 
ATOM   13160 O  OE1 . GLU D 2 371 ? 14.232  -21.859 -14.752 1.00 62.68  ? 371 GLU D OE1 1 
ATOM   13161 O  OE2 . GLU D 2 371 ? 14.291  -20.689 -16.621 1.00 71.14  ? 371 GLU D OE2 1 
ATOM   13162 N  N   . THR D 2 372 ? 19.847  -21.653 -12.787 1.00 51.48  ? 372 THR D N   1 
ATOM   13163 C  CA  . THR D 2 372 ? 20.855  -21.203 -11.832 1.00 58.72  ? 372 THR D CA  1 
ATOM   13164 C  C   . THR D 2 372 ? 22.263  -21.234 -12.433 1.00 59.92  ? 372 THR D C   1 
ATOM   13165 O  O   . THR D 2 372 ? 23.048  -20.305 -12.226 1.00 63.07  ? 372 THR D O   1 
ATOM   13166 C  CB  . THR D 2 372 ? 20.758  -22.055 -10.558 1.00 56.95  ? 372 THR D CB  1 
ATOM   13167 O  OG1 . THR D 2 372 ? 19.588  -21.654 -9.833  1.00 58.29  ? 372 THR D OG1 1 
ATOM   13168 C  CG2 . THR D 2 372 ? 21.987  -21.893 -9.664  1.00 59.31  ? 372 THR D CG2 1 
ATOM   13169 N  N   . LEU D 2 373 ? 22.601  -22.287 -13.184 1.00 56.54  ? 373 LEU D N   1 
ATOM   13170 C  CA  . LEU D 2 373 ? 23.921  -22.353 -13.799 1.00 59.30  ? 373 LEU D CA  1 
ATOM   13171 C  C   . LEU D 2 373 ? 24.149  -21.171 -14.738 1.00 63.31  ? 373 LEU D C   1 
ATOM   13172 O  O   . LEU D 2 373 ? 25.289  -20.738 -14.923 1.00 68.85  ? 373 LEU D O   1 
ATOM   13173 C  CB  . LEU D 2 373 ? 24.105  -23.692 -14.540 1.00 50.13  ? 373 LEU D CB  1 
ATOM   13174 C  CG  . LEU D 2 373 ? 24.068  -24.950 -13.636 1.00 50.81  ? 373 LEU D CG  1 
ATOM   13175 C  CD1 . LEU D 2 373 ? 24.114  -26.308 -14.393 1.00 43.63  ? 373 LEU D CD1 1 
ATOM   13176 C  CD2 . LEU D 2 373 ? 25.128  -24.924 -12.556 1.00 46.59  ? 373 LEU D CD2 1 
ATOM   13177 N  N   . SER D 2 374 ? 23.080  -20.615 -15.312 1.00 67.92  ? 374 SER D N   1 
ATOM   13178 C  CA  . SER D 2 374 ? 23.233  -19.519 -16.271 1.00 72.70  ? 374 SER D CA  1 
ATOM   13179 C  C   . SER D 2 374 ? 23.656  -18.208 -15.622 1.00 75.98  ? 374 SER D C   1 
ATOM   13180 O  O   . SER D 2 374 ? 24.129  -17.318 -16.332 1.00 82.07  ? 374 SER D O   1 
ATOM   13181 C  CB  . SER D 2 374 ? 21.933  -19.288 -17.042 1.00 72.89  ? 374 SER D CB  1 
ATOM   13182 O  OG  . SER D 2 374 ? 21.738  -20.312 -17.998 1.00 73.44  ? 374 SER D OG  1 
ATOM   13183 N  N   . GLU D 2 375 ? 23.489  -18.059 -14.304 1.00 88.44  ? 375 GLU D N   1 
ATOM   13184 C  CA  . GLU D 2 375 ? 23.776  -16.807 -13.602 1.00 92.98  ? 375 GLU D CA  1 
ATOM   13185 C  C   . GLU D 2 375 ? 25.118  -16.801 -12.876 1.00 93.57  ? 375 GLU D C   1 
ATOM   13186 O  O   . GLU D 2 375 ? 25.423  -15.820 -12.187 1.00 96.80  ? 375 GLU D O   1 
ATOM   13187 C  CB  . GLU D 2 375 ? 22.665  -16.488 -12.593 1.00 88.87  ? 375 GLU D CB  1 
ATOM   13188 C  CG  . GLU D 2 375 ? 21.259  -16.711 -13.101 1.00 87.29  ? 375 GLU D CG  1 
ATOM   13189 C  CD  . GLU D 2 375 ? 20.282  -16.934 -11.969 1.00 92.15  ? 375 GLU D CD  1 
ATOM   13190 O  OE1 . GLU D 2 375 ? 20.708  -17.439 -10.901 1.00 86.81  ? 375 GLU D OE1 1 
ATOM   13191 O  OE2 . GLU D 2 375 ? 19.092  -16.603 -12.147 1.00 98.06  ? 375 GLU D OE2 1 
ATOM   13192 N  N   . GLU D 2 376 ? 25.916  -17.862 -12.996 1.00 85.30  ? 376 GLU D N   1 
ATOM   13193 C  CA  . GLU D 2 376 ? 27.268  -17.854 -12.438 1.00 86.92  ? 376 GLU D CA  1 
ATOM   13194 C  C   . GLU D 2 376 ? 28.302  -17.563 -13.525 1.00 89.30  ? 376 GLU D C   1 
ATOM   13195 O  O   . GLU D 2 376 ? 29.495  -17.440 -13.250 1.00 90.30  ? 376 GLU D O   1 
ATOM   13196 C  CB  . GLU D 2 376 ? 27.575  -19.181 -11.716 1.00 86.37  ? 376 GLU D CB  1 
ATOM   13197 C  CG  . GLU D 2 376 ? 27.272  -20.492 -12.480 1.00 86.34  ? 376 GLU D CG  1 
ATOM   13198 C  CD  . GLU D 2 376 ? 28.282  -20.843 -13.575 1.00 91.68  ? 376 GLU D CD  1 
ATOM   13199 O  OE1 . GLU D 2 376 ? 29.321  -20.155 -13.702 1.00 95.10  ? 376 GLU D OE1 1 
ATOM   13200 O  OE2 . GLU D 2 376 ? 28.037  -21.833 -14.303 1.00 84.32  ? 376 GLU D OE2 1 
HETATM 13201 N  N1A . BYC E 3 .   ? 27.431  -1.668  -12.478 0.50 40.84  ? 501 BYC A N1A 1 
HETATM 13202 O  O1A . BYC E 3 .   ? 24.685  -10.965 -7.644  0.50 38.46  ? 501 BYC A O1A 1 
HETATM 13203 P  P1A . BYC E 3 .   ? 25.112  -9.550  -7.292  0.50 41.60  ? 501 BYC A P1A 1 
HETATM 13204 C  C1B . BYC E 3 .   ? 25.693  -2.818  8.886   0.50 21.64  ? 501 BYC A C1B 1 
HETATM 13205 C  C1D . BYC E 3 .   ? 24.432  -5.523  -11.452 0.50 46.29  ? 501 BYC A C1D 1 
HETATM 13206 S  S1P . BYC E 3 .   ? 27.054  -3.323  7.876   0.50 28.11  ? 501 BYC A S1P 1 
HETATM 13207 C  C2A . BYC E 3 .   ? 26.608  -1.768  -11.434 0.50 41.43  ? 501 BYC A C2A 1 
HETATM 13208 O  O2A . BYC E 3 .   ? 26.343  -9.712  -6.430  0.50 38.35  ? 501 BYC A O2A 1 
HETATM 13209 P  P2A . BYC E 3 .   ? 24.089  -7.382  -5.743  0.50 41.25  ? 501 BYC A P2A 1 
HETATM 13210 C  C2B . BYC E 3 .   ? 25.942  -2.201  10.139  0.50 25.01  ? 501 BYC A C2B 1 
HETATM 13211 C  C2D . BYC E 3 .   ? 23.322  -6.291  -12.089 0.50 48.23  ? 501 BYC A C2D 1 
HETATM 13212 O  O2D . BYC E 3 .   ? 22.238  -5.360  -12.430 0.50 49.71  ? 501 BYC A O2D 1 
HETATM 13213 C  C2P . BYC E 3 .   ? 26.327  -4.405  6.611   0.50 25.35  ? 501 BYC A C2P 1 
HETATM 13214 N  N3A . BYC E 3 .   ? 25.872  -2.867  -11.309 0.50 39.97  ? 501 BYC A N3A 1 
HETATM 13215 O  O3A . BYC E 3 .   ? 23.959  -8.875  -6.376  0.50 45.01  ? 501 BYC A O3A 1 
HETATM 13216 C  C3B . BYC E 3 .   ? 24.877  -1.910  11.013  0.50 26.66  ? 501 BYC A C3B 1 
HETATM 13217 C  C3D . BYC E 3 .   ? 22.960  -7.295  -11.015 0.50 48.30  ? 501 BYC A C3D 1 
HETATM 13218 O  O3D . BYC E 3 .   ? 21.764  -6.930  -10.234 0.50 50.65  ? 501 BYC A O3D 1 
HETATM 13219 P  P3D . BYC E 3 .   ? 20.281  -7.065  -10.810 0.50 52.29  ? 501 BYC A P3D 1 
HETATM 13220 C  C3P . BYC E 3 .   ? 27.110  -4.143  5.341   0.50 26.25  ? 501 BYC A C3P 1 
HETATM 13221 C  C4A . BYC E 3 .   ? 25.943  -3.859  -12.208 0.50 45.14  ? 501 BYC A C4A 1 
HETATM 13222 O  O4A . BYC E 3 .   ? 24.903  -6.427  -6.598  0.50 43.43  ? 501 BYC A O4A 1 
HETATM 13223 C  C4B . BYC E 3 .   ? 25.156  -1.300  12.273  0.50 19.87  ? 501 BYC A C4B 1 
HETATM 13224 C  C4D . BYC E 3 .   ? 24.118  -7.259  -10.049 0.50 47.82  ? 501 BYC A C4D 1 
HETATM 13225 O  O4D . BYC E 3 .   ? 25.146  -6.429  -10.598 0.50 43.94  ? 501 BYC A O4D 1 
HETATM 13226 N  N4P . BYC E 3 .   ? 26.451  -4.655  4.158   0.50 24.36  ? 501 BYC A N4P 1 
HETATM 13227 O  O57 . BYC E 3 .   ? 24.563  -3.028  8.507   0.50 23.52  ? 501 BYC A O57 1 
HETATM 13228 O  O5A . BYC E 3 .   ? 22.710  -6.765  -5.788  0.50 43.94  ? 501 BYC A O5A 1 
HETATM 13229 C  C5B . BYC E 3 .   ? 26.451  -1.011  12.621  0.50 15.31  ? 501 BYC A C5B 1 
HETATM 13230 C  C5D . BYC E 3 .   ? 24.626  -8.682  -9.782  0.50 46.05  ? 501 BYC A C5D 1 
HETATM 13231 O  O5D . BYC E 3 .   ? 25.455  -8.647  -8.621  0.50 45.09  ? 501 BYC A O5D 1 
HETATM 13232 C  C5M . BYC E 3 .   ? 26.792  -3.783  -13.300 0.50 45.86  ? 501 BYC A C5M 1 
HETATM 13233 C  C5P . BYC E 3 .   ? 26.713  -5.860  3.352   0.50 28.35  ? 501 BYC A C5P 1 
HETATM 13234 O  O5P . BYC E 3 .   ? 27.546  -6.766  3.520   0.50 24.28  ? 501 BYC A O5P 1 
HETATM 13235 C  C6A . BYC E 3 .   ? 27.563  -2.631  -13.415 0.50 42.09  ? 501 BYC A C6A 1 
HETATM 13236 N  N6A . BYC E 3 .   ? 28.488  -2.517  -14.528 0.50 43.10  ? 501 BYC A N6A 1 
HETATM 13237 O  O6A . BYC E 3 .   ? 24.666  -7.383  -4.216  0.50 41.49  ? 501 BYC A O6A 1 
HETATM 13238 C  C6B . BYC E 3 .   ? 27.502  -1.349  11.749  0.50 21.20  ? 501 BYC A C6B 1 
HETATM 13239 C  C6P . BYC E 3 .   ? 25.770  -5.963  2.165   0.50 29.45  ? 501 BYC A C6P 1 
HETATM 13240 N  N7A . BYC E 3 .   ? 26.645  -4.985  -14.045 0.50 47.89  ? 501 BYC A N7A 1 
HETATM 13241 O  O7A . BYC E 3 .   ? 19.743  -8.480  -10.912 0.50 50.98  ? 501 BYC A O7A 1 
HETATM 13242 C  C7B . BYC E 3 .   ? 27.277  -1.940  10.500  0.50 22.70  ? 501 BYC A C7B 1 
HETATM 13243 C  C7P . BYC E 3 .   ? 26.297  -5.023  1.073   0.50 26.00  ? 501 BYC A C7P 1 
HETATM 13244 C  C8A . BYC E 3 .   ? 25.728  -5.789  -13.454 0.50 47.98  ? 501 BYC A C8A 1 
HETATM 13245 O  O8A . BYC E 3 .   ? 19.305  -6.317  -9.932  0.50 56.50  ? 501 BYC A O8A 1 
HETATM 13246 N  N8P . BYC E 3 .   ? 25.881  -5.555  -0.195  0.50 32.79  ? 501 BYC A N8P 1 
HETATM 13247 N  N9A . BYC E 3 .   ? 25.373  -5.047  -12.405 0.50 48.09  ? 501 BYC A N9A 1 
HETATM 13248 O  O9A . BYC E 3 .   ? 20.073  -6.456  -12.180 0.50 53.24  ? 501 BYC A O9A 1 
HETATM 13249 C  C9P . BYC E 3 .   ? 26.791  -6.260  -1.085  0.50 29.81  ? 501 BYC A C9P 1 
HETATM 13250 O  O9P . BYC E 3 .   ? 27.960  -6.397  -0.791  0.50 32.13  ? 501 BYC A O9P 1 
HETATM 13251 C  CAP . BYC E 3 .   ? 26.223  -6.766  -2.411  0.50 39.74  ? 501 BYC A CAP 1 
HETATM 13252 O  OAP . BYC E 3 .   ? 24.942  -6.096  -2.567  0.50 37.61  ? 501 BYC A OAP 1 
HETATM 13253 C  CBP . BYC E 3 .   ? 26.130  -8.312  -2.530  0.50 38.39  ? 501 BYC A CBP 1 
HETATM 13254 C  CCP . BYC E 3 .   ? 25.001  -8.597  -3.525  0.50 41.64  ? 501 BYC A CCP 1 
HETATM 13255 C  CDP . BYC E 3 .   ? 25.924  -9.061  -1.221  0.50 39.97  ? 501 BYC A CDP 1 
HETATM 13256 C  CEP . BYC E 3 .   ? 27.445  -8.925  -3.010  0.50 39.66  ? 501 BYC A CEP 1 
HETATM 13257 C  C1  . GOL F 4 .   ? 35.070  -23.327 23.715  1.00 36.26  ? 502 GOL A C1  1 
HETATM 13258 O  O1  . GOL F 4 .   ? 34.498  -24.138 24.738  1.00 37.65  ? 502 GOL A O1  1 
HETATM 13259 C  C2  . GOL F 4 .   ? 36.142  -24.071 22.948  1.00 40.69  ? 502 GOL A C2  1 
HETATM 13260 O  O2  . GOL F 4 .   ? 35.548  -25.006 22.049  1.00 44.03  ? 502 GOL A O2  1 
HETATM 13261 C  C3  . GOL F 4 .   ? 37.095  -23.160 22.203  1.00 37.19  ? 502 GOL A C3  1 
HETATM 13262 O  O3  . GOL F 4 .   ? 38.294  -23.839 21.841  1.00 37.91  ? 502 GOL A O3  1 
HETATM 13263 FE FE1 . SF4 G 5 .   ? 22.891  -3.278  17.413  1.00 19.94  ? 503 SF4 A FE1 1 
HETATM 13264 FE FE2 . SF4 G 5 .   ? 24.472  -3.465  15.227  1.00 21.77  ? 503 SF4 A FE2 1 
HETATM 13265 FE FE3 . SF4 G 5 .   ? 21.831  -3.132  14.822  1.00 20.75  ? 503 SF4 A FE3 1 
HETATM 13266 FE FE4 . SF4 G 5 .   ? 22.671  -5.446  15.777  1.00 19.16  ? 503 SF4 A FE4 1 
HETATM 13267 S  S1  . SF4 G 5 .   ? 23.183  -4.613  13.700  1.00 23.47  ? 503 SF4 A S1  1 
HETATM 13268 S  S2  . SF4 G 5 .   ? 20.964  -4.191  16.708  1.00 21.88  ? 503 SF4 A S2  1 
HETATM 13269 S  S3  . SF4 G 5 .   ? 24.448  -4.973  16.968  1.00 20.80  ? 503 SF4 A S3  1 
HETATM 13270 S  S4  . SF4 G 5 .   ? 23.286  -1.624  15.806  1.00 20.17  ? 503 SF4 A S4  1 
HETATM 13271 S  S1  . BJ8 H 6 .   ? 14.778  -3.195  26.782  1.00 24.50  ? 401 BJ8 B S1  1 
HETATM 13272 S  S2  . BJ8 H 6 .   ? 14.337  -0.274  28.955  1.00 24.72  ? 401 BJ8 B S2  1 
HETATM 13273 S  S3  . BJ8 H 6 .   ? 16.660  -3.061  29.863  1.00 22.57  ? 401 BJ8 B S3  1 
HETATM 13274 S  S4  . BJ8 H 6 .   ? 13.047  -3.543  30.007  1.00 24.91  ? 401 BJ8 B S4  1 
HETATM 13275 S  S5  . BJ8 H 6 .   ? 17.793  -2.847  33.977  1.00 22.23  ? 401 BJ8 B S5  1 
HETATM 13276 S  S6  . BJ8 H 6 .   ? 16.520  0.565   35.015  1.00 26.02  ? 401 BJ8 B S6  1 
HETATM 13277 S  S7  . BJ8 H 6 .   ? 18.225  0.188   31.864  1.00 25.01  ? 401 BJ8 B S7  1 
HETATM 13278 S  S8  . BJ8 H 6 .   ? 20.022  -0.243  34.971  1.00 24.56  ? 401 BJ8 B S8  1 
HETATM 13279 S  S9  . BJ8 H 6 .   ? 14.537  -1.271  32.684  1.00 27.68  ? 401 BJ8 B S9  1 
HETATM 13280 FE FE1 . BJ8 H 6 .   ? 14.681  -1.951  30.549  1.00 22.49  ? 401 BJ8 B FE1 1 
HETATM 13281 FE FE2 . BJ8 H 6 .   ? 14.946  -4.112  28.906  1.00 21.78  ? 401 BJ8 B FE2 1 
HETATM 13282 FE FE3 . BJ8 H 6 .   ? 13.274  -2.114  28.114  1.00 21.45  ? 401 BJ8 B FE3 1 
HETATM 13283 FE FE4 . BJ8 H 6 .   ? 15.892  -1.741  28.130  1.00 23.61  ? 401 BJ8 B FE4 1 
HETATM 13284 FE FE5 . BJ8 H 6 .   ? 18.458  1.123   33.955  1.00 22.90  ? 401 BJ8 B FE5 1 
HETATM 13285 FE FE6 . BJ8 H 6 .   ? 19.357  -1.410  33.106  1.00 24.30  ? 401 BJ8 B FE6 1 
HETATM 13286 FE FE7 . BJ8 H 6 .   ? 18.059  -1.093  35.502  1.00 24.02  ? 401 BJ8 B FE7 1 
HETATM 13287 FE FE8 . BJ8 H 6 .   ? 16.713  -0.891  33.175  1.00 25.52  ? 401 BJ8 B FE8 1 
HETATM 13288 C  C   . TRS I 7 .   ? 23.975  17.120  27.505  1.00 27.29  ? 402 TRS B C   1 
HETATM 13289 C  C1  . TRS I 7 .   ? 25.324  17.754  27.878  1.00 27.93  ? 402 TRS B C1  1 
HETATM 13290 C  C2  . TRS I 7 .   ? 23.004  17.153  28.689  1.00 26.58  ? 402 TRS B C2  1 
HETATM 13291 C  C3  . TRS I 7 .   ? 23.316  17.771  26.286  1.00 26.30  ? 402 TRS B C3  1 
HETATM 13292 N  N   . TRS I 7 .   ? 24.243  15.671  27.271  1.00 31.46  ? 402 TRS B N   1 
HETATM 13293 O  O1  . TRS I 7 .   ? 26.216  17.631  26.792  1.00 30.52  ? 402 TRS B O1  1 
HETATM 13294 O  O2  . TRS I 7 .   ? 21.697  16.869  28.233  1.00 29.12  ? 402 TRS B O2  1 
HETATM 13295 O  O3  . TRS I 7 .   ? 23.015  19.130  26.553  1.00 42.67  ? 402 TRS B O3  1 
HETATM 13296 N  N1A . BYC J 3 .   ? 15.034  -49.040 43.413  0.50 42.15  ? 501 BYC C N1A 1 
HETATM 13297 O  O1A . BYC J 3 .   ? 15.006  -39.740 37.816  0.50 61.35  ? 501 BYC C O1A 1 
HETATM 13298 P  P1A . BYC J 3 .   ? 15.294  -41.221 37.687  0.50 51.48  ? 501 BYC C P1A 1 
HETATM 13299 C  C1B . BYC J 3 .   ? 22.534  -47.950 23.142  0.50 22.36  ? 501 BYC C C1B 1 
HETATM 13300 C  C1D . BYC J 3 .   ? 12.874  -45.153 41.109  0.50 47.20  ? 501 BYC C C1D 1 
HETATM 13301 S  S1P . BYC J 3 .   ? 23.317  -47.342 24.590  0.50 29.79  ? 501 BYC C S1P 1 
HETATM 13302 C  C2A . BYC J 3 .   ? 14.639  -49.010 42.145  0.50 42.81  ? 501 BYC C C2A 1 
HETATM 13303 O  O2A . BYC J 3 .   ? 16.790  -41.177 37.454  0.50 50.74  ? 501 BYC C O2A 1 
HETATM 13304 P  P2A . BYC J 3 .   ? 14.655  -43.306 35.746  0.50 49.69  ? 501 BYC C P2A 1 
HETATM 13305 C  C2B . BYC J 3 .   ? 23.363  -48.542 22.149  0.50 24.12  ? 501 BYC C C2B 1 
HETATM 13306 C  C2D . BYC J 3 .   ? 11.612  -44.355 41.243  0.50 49.66  ? 501 BYC C C2D 1 
HETATM 13307 O  O2D . BYC J 3 .   ? 10.473  -45.273 41.231  0.50 49.35  ? 501 BYC C O2D 1 
HETATM 13308 C  C2P . BYC J 3 .   ? 21.961  -46.538 25.507  0.50 25.87  ? 501 BYC C C2P 1 
HETATM 13309 N  N3A . BYC J 3 .   ? 14.089  -47.890 41.682  0.50 42.79  ? 501 BYC C N3A 1 
HETATM 13310 O  O3A . BYC J 3 .   ? 14.472  -41.818 36.403  0.50 50.96  ? 501 BYC C O3A 1 
HETATM 13311 C  C3B . BYC J 3 .   ? 22.850  -48.880 20.891  0.50 28.01  ? 501 BYC C C3B 1 
HETATM 13312 C  C3D . BYC J 3 .   ? 11.644  -43.500 40.000  0.50 49.61  ? 501 BYC C C3D 1 
HETATM 13313 O  O3D . BYC J 3 .   ? 10.882  -44.131 38.906  0.50 51.80  ? 501 BYC C O3D 1 
HETATM 13314 P  P3D . BYC J 3 .   ? 9.388   -43.681 38.572  0.50 51.08  ? 501 BYC C P3D 1 
HETATM 13315 C  C3P . BYC J 3 .   ? 22.266  -46.678 26.975  0.50 28.28  ? 501 BYC C C3P 1 
HETATM 13316 C  C4A . BYC J 3 .   ? 13.916  -46.820 42.476  0.50 46.64  ? 501 BYC C C4A 1 
HETATM 13317 O  O4A . BYC J 3 .   ? 14.805  -44.380 36.806  0.50 49.55  ? 501 BYC C O4A 1 
HETATM 13318 C  C4B . BYC J 3 .   ? 23.703  -49.499 19.950  0.50 17.39  ? 501 BYC C C4B 1 
HETATM 13319 C  C4D . BYC J 3 .   ? 13.097  -43.490 39.586  0.50 49.69  ? 501 BYC C C4D 1 
HETATM 13320 O  O4D . BYC J 3 .   ? 13.839  -44.283 40.509  0.50 45.75  ? 501 BYC C O4D 1 
HETATM 13321 N  N4P . BYC J 3 .   ? 21.163  -46.167 27.753  0.50 24.51  ? 501 BYC C N4P 1 
HETATM 13322 O  O57 . BYC J 3 .   ? 21.313  -47.875 23.044  0.50 24.23  ? 501 BYC C O57 1 
HETATM 13323 O  O5A . BYC J 3 .   ? 13.355  -43.715 35.093  0.50 47.93  ? 501 BYC C O5A 1 
HETATM 13324 C  C5B . BYC J 3 .   ? 25.024  -49.712 20.278  0.50 18.95  ? 501 BYC C C5B 1 
HETATM 13325 C  C5D . BYC J 3 .   ? 13.655  -42.063 39.614  0.50 53.26  ? 501 BYC C C5D 1 
HETATM 13326 O  O5D . BYC J 3 .   ? 14.976  -42.051 39.070  0.50 52.68  ? 501 BYC C O5D 1 
HETATM 13327 C  C5M . BYC J 3 .   ? 14.323  -46.841 43.807  0.50 45.18  ? 501 BYC C C5M 1 
HETATM 13328 C  C5P . BYC J 3 .   ? 21.178  -44.988 28.600  0.50 31.04  ? 501 BYC C C5P 1 
HETATM 13329 O  O5P . BYC J 3 .   ? 22.120  -44.232 28.781  0.50 29.41  ? 501 BYC C O5P 1 
HETATM 13330 C  C6A . BYC J 3 .   ? 14.906  -48.013 44.275  0.50 42.72  ? 501 BYC C C6A 1 
HETATM 13331 N  N6A . BYC J 3 .   ? 15.366  -48.093 45.654  0.50 41.65  ? 501 BYC C N6A 1 
HETATM 13332 O  O6A . BYC J 3 .   ? 15.905  -43.408 34.691  0.50 48.08  ? 501 BYC C O6A 1 
HETATM 13333 C  C6B . BYC J 3 .   ? 25.537  -49.376 21.524  0.50 22.80  ? 501 BYC C C6B 1 
HETATM 13334 C  C6P . BYC J 3 .   ? 19.870  -44.745 29.321  0.50 32.88  ? 501 BYC C C6P 1 
HETATM 13335 N  N7A . BYC J 3 .   ? 14.022  -45.576 44.367  0.50 46.38  ? 501 BYC C N7A 1 
HETATM 13336 O  O7A . BYC J 3 .   ? 9.198   -42.181 38.570  0.50 49.53  ? 501 BYC C O7A 1 
HETATM 13337 C  C7B . BYC J 3 .   ? 24.710  -48.778 22.463  0.50 21.01  ? 501 BYC C C7B 1 
HETATM 13338 C  C7P . BYC J 3 .   ? 19.825  -45.790 30.460  0.50 31.96  ? 501 BYC C C7P 1 
HETATM 13339 C  C8A . BYC J 3 .   ? 13.436  -44.787 43.431  0.50 48.75  ? 501 BYC C C8A 1 
HETATM 13340 O  O8A . BYC J 3 .   ? 8.900   -44.126 37.213  0.50 52.06  ? 501 BYC C O8A 1 
HETATM 13341 N  N8P . BYC J 3 .   ? 18.792  -45.388 31.361  0.50 32.75  ? 501 BYC C N8P 1 
HETATM 13342 N  N9A . BYC J 3 .   ? 13.404  -45.589 42.365  0.50 47.37  ? 501 BYC C N9A 1 
HETATM 13343 O  O9A . BYC J 3 .   ? 8.345   -44.205 39.525  0.50 49.03  ? 501 BYC C O9A 1 
HETATM 13344 C  C9P . BYC J 3 .   ? 19.162  -44.629 32.560  0.50 34.53  ? 501 BYC C C9P 1 
HETATM 13345 O  O9P . BYC J 3 .   ? 20.346  -44.375 32.796  0.50 34.88  ? 501 BYC C O9P 1 
HETATM 13346 C  CAP . BYC J 3 .   ? 18.052  -44.211 33.544  0.50 43.40  ? 501 BYC C CAP 1 
HETATM 13347 O  OAP . BYC J 3 .   ? 16.786  -44.754 33.078  0.50 40.25  ? 501 BYC C OAP 1 
HETATM 13348 C  CBP . BYC J 3 .   ? 18.046  -42.685 33.824  0.50 43.95  ? 501 BYC C CBP 1 
HETATM 13349 C  CCP . BYC J 3 .   ? 16.621  -42.262 34.220  0.50 47.13  ? 501 BYC C CCP 1 
HETATM 13350 C  CDP . BYC J 3 .   ? 18.542  -41.830 32.657  0.50 42.83  ? 501 BYC C CDP 1 
HETATM 13351 C  CEP . BYC J 3 .   ? 19.034  -42.372 34.956  0.50 41.82  ? 501 BYC C CEP 1 
HETATM 13352 C  C1  . GOL K 4 .   ? 38.241  -27.570 16.013  1.00 44.19  ? 502 GOL C C1  1 
HETATM 13353 O  O1  . GOL K 4 .   ? 39.329  -27.060 16.755  1.00 45.64  ? 502 GOL C O1  1 
HETATM 13354 C  C2  . GOL K 4 .   ? 37.768  -26.517 14.880  1.00 44.82  ? 502 GOL C C2  1 
HETATM 13355 O  O2  . GOL K 4 .   ? 36.775  -25.678 15.349  1.00 51.44  ? 502 GOL C O2  1 
HETATM 13356 C  C3  . GOL K 4 .   ? 37.315  -27.391 13.583  1.00 41.24  ? 502 GOL C C3  1 
HETATM 13357 O  O3  . GOL K 4 .   ? 37.114  -26.507 12.471  1.00 43.18  ? 502 GOL C O3  1 
HETATM 13358 C  C1  A GOL L 4 .   ? 33.491  -25.930 19.273  0.55 34.78  ? 503 GOL C C1  1 
HETATM 13359 C  C1  B GOL L 4 .   ? 31.647  -24.942 17.609  0.45 29.69  ? 503 GOL C C1  1 
HETATM 13360 O  O1  A GOL L 4 .   ? 33.602  -25.817 20.689  0.55 30.98  ? 503 GOL C O1  1 
HETATM 13361 O  O1  B GOL L 4 .   ? 30.660  -25.329 18.529  0.45 25.01  ? 503 GOL C O1  1 
HETATM 13362 C  C2  A GOL L 4 .   ? 32.618  -24.837 18.694  0.55 31.67  ? 503 GOL C C2  1 
HETATM 13363 C  C2  B GOL L 4 .   ? 32.929  -25.908 17.708  0.45 31.19  ? 503 GOL C C2  1 
HETATM 13364 O  O2  A GOL L 4 .   ? 33.333  -24.110 17.696  0.55 28.45  ? 503 GOL C O2  1 
HETATM 13365 O  O2  B GOL L 4 .   ? 33.838  -25.585 16.660  0.45 34.88  ? 503 GOL C O2  1 
HETATM 13366 C  C3  A GOL L 4 .   ? 31.307  -25.344 18.133  0.55 28.38  ? 503 GOL C C3  1 
HETATM 13367 C  C3  B GOL L 4 .   ? 33.584  -25.620 19.139  0.45 34.77  ? 503 GOL C C3  1 
HETATM 13368 O  O3  A GOL L 4 .   ? 31.416  -25.659 16.748  0.55 27.42  ? 503 GOL C O3  1 
HETATM 13369 O  O3  B GOL L 4 .   ? 32.752  -24.730 19.899  0.45 32.94  ? 503 GOL C O3  1 
HETATM 13370 FE FE1 . SF4 M 5 .   ? 23.602  -47.445 14.271  1.00 21.88  ? 504 SF4 C FE1 1 
HETATM 13371 FE FE2 . SF4 M 5 .   ? 24.081  -47.228 16.876  1.00 21.91  ? 504 SF4 C FE2 1 
HETATM 13372 FE FE3 . SF4 M 5 .   ? 21.566  -47.560 16.127  1.00 23.41  ? 504 SF4 C FE3 1 
HETATM 13373 FE FE4 . SF4 M 5 .   ? 22.673  -45.271 15.674  1.00 21.77  ? 504 SF4 C FE4 1 
HETATM 13374 S  S1  . SF4 M 5 .   ? 22.311  -46.105 17.749  1.00 25.35  ? 504 SF4 C S1  1 
HETATM 13375 S  S2  . SF4 M 5 .   ? 21.590  -46.548 14.064  1.00 23.71  ? 504 SF4 C S2  1 
HETATM 13376 S  S3  . SF4 M 5 .   ? 24.842  -45.772 15.322  1.00 21.73  ? 504 SF4 C S3  1 
HETATM 13377 S  S4  . SF4 M 5 .   ? 23.289  -49.141 15.825  1.00 21.42  ? 504 SF4 C S4  1 
HETATM 13378 S  S1  . BJ8 N 6 .   ? 20.257  -47.564 2.350   1.00 27.34  ? 401 BJ8 D S1  1 
HETATM 13379 S  S2  . BJ8 N 6 .   ? 20.792  -50.471 0.189   1.00 24.42  ? 401 BJ8 D S2  1 
HETATM 13380 S  S3  . BJ8 N 6 .   ? 23.270  -47.694 0.292   1.00 25.26  ? 401 BJ8 D S3  1 
HETATM 13381 S  S4  . BJ8 N 6 .   ? 20.059  -47.273 -1.379  1.00 26.16  ? 401 BJ8 D S4  1 
HETATM 13382 S  S5  . BJ8 N 6 .   ? 26.052  -47.937 -2.819  1.00 24.20  ? 401 BJ8 D S5  1 
HETATM 13383 S  S6  . BJ8 N 6 .   ? 25.371  -51.296 -4.383  1.00 24.95  ? 401 BJ8 D S6  1 
HETATM 13384 S  S7  . BJ8 N 6 .   ? 25.611  -50.907 -0.770  1.00 26.08  ? 401 BJ8 D S7  1 
HETATM 13385 S  S8  . BJ8 N 6 .   ? 28.536  -50.540 -2.815  1.00 25.42  ? 401 BJ8 D S8  1 
HETATM 13386 S  S9  . BJ8 N 6 .   ? 22.543  -49.532 -3.083  1.00 28.64  ? 401 BJ8 D S9  1 
HETATM 13387 FE FE1 . BJ8 N 6 .   ? 21.770  -48.771 -1.112  1.00 23.36  ? 401 BJ8 D FE1 1 
HETATM 13388 FE FE2 . BJ8 N 6 .   ? 21.344  -46.618 0.522   1.00 24.62  ? 401 BJ8 D FE2 1 
HETATM 13389 FE FE3 . BJ8 N 6 .   ? 19.506  -48.623 0.463   1.00 23.50  ? 401 BJ8 D FE3 1 
HETATM 13390 FE FE4 . BJ8 N 6 .   ? 21.854  -48.977 1.567   1.00 24.87  ? 401 BJ8 D FE4 1 
HETATM 13391 FE FE5 . BJ8 N 6 .   ? 26.682  -51.837 -2.570  1.00 25.20  ? 401 BJ8 D FE5 1 
HETATM 13392 FE FE6 . BJ8 N 6 .   ? 27.117  -49.334 -1.446  1.00 24.62  ? 401 BJ8 D FE6 1 
HETATM 13393 FE FE7 . BJ8 N 6 .   ? 26.936  -49.612 -4.122  1.00 23.75  ? 401 BJ8 D FE7 1 
HETATM 13394 FE FE8 . BJ8 N 6 .   ? 24.763  -49.837 -2.632  1.00 27.60  ? 401 BJ8 D FE8 1 
HETATM 13395 C  C   . TRS O 7 .   ? 28.766  -67.910 5.591   1.00 28.89  ? 402 TRS D C   1 
HETATM 13396 C  C1  . TRS O 7 .   ? 30.163  -68.492 5.720   1.00 28.61  ? 402 TRS D C1  1 
HETATM 13397 C  C2  . TRS O 7 .   ? 28.780  -66.449 6.034   1.00 29.56  ? 402 TRS D C2  1 
HETATM 13398 C  C3  . TRS O 7 .   ? 28.350  -67.963 4.124   1.00 27.16  ? 402 TRS D C3  1 
HETATM 13399 N  N   . TRS O 7 .   ? 27.832  -68.563 6.478   1.00 29.04  ? 402 TRS D N   1 
HETATM 13400 O  O1  . TRS O 7 .   ? 30.559  -68.501 7.066   1.00 28.96  ? 402 TRS D O1  1 
HETATM 13401 O  O2  . TRS O 7 .   ? 29.945  -65.897 5.527   1.00 31.12  ? 402 TRS D O2  1 
HETATM 13402 O  O3  . TRS O 7 .   ? 27.003  -67.553 3.973   1.00 27.51  ? 402 TRS D O3  1 
HETATM 13403 O  O   A HOH P 8 .   ? 9.551   -12.887 3.801   0.54 27.79  ? 601 HOH A O   1 
HETATM 13404 O  O   B HOH P 8 .   ? 10.695  -12.477 2.373   0.46 32.31  ? 601 HOH A O   1 
HETATM 13405 O  O   . HOH P 8 .   ? 4.096   -0.210  11.311  1.00 33.65  ? 602 HOH A O   1 
HETATM 13406 O  O   . HOH P 8 .   ? 39.831  18.073  23.896  1.00 32.52  ? 603 HOH A O   1 
HETATM 13407 O  O   . HOH P 8 .   ? 42.408  1.462   -6.154  1.00 36.23  ? 604 HOH A O   1 
HETATM 13408 O  O   . HOH P 8 .   ? 13.968  1.153   11.815  1.00 34.97  ? 605 HOH A O   1 
HETATM 13409 O  O   . HOH P 8 .   ? 20.793  19.339  14.431  1.00 37.99  ? 606 HOH A O   1 
HETATM 13410 O  O   . HOH P 8 .   ? 35.811  -15.591 12.776  1.00 35.18  ? 607 HOH A O   1 
HETATM 13411 O  O   . HOH P 8 .   ? 21.927  22.784  3.561   1.00 37.87  ? 608 HOH A O   1 
HETATM 13412 O  O   . HOH P 8 .   ? 22.557  -3.620  6.248   1.00 41.10  ? 609 HOH A O   1 
HETATM 13413 O  O   . HOH P 8 .   ? 29.067  -18.160 9.416   1.00 25.78  ? 610 HOH A O   1 
HETATM 13414 O  O   . HOH P 8 .   ? 33.012  -10.380 13.298  1.00 28.49  ? 611 HOH A O   1 
HETATM 13415 O  O   . HOH P 8 .   ? 33.660  5.892   10.056  1.00 26.07  ? 612 HOH A O   1 
HETATM 13416 O  O   . HOH P 8 .   ? 49.063  1.616   25.318  1.00 30.30  ? 613 HOH A O   1 
HETATM 13417 O  O   . HOH P 8 .   ? 34.546  -14.320 15.320  1.00 37.05  ? 614 HOH A O   1 
HETATM 13418 O  O   . HOH P 8 .   ? -0.800  2.309   -8.157  1.00 35.03  ? 615 HOH A O   1 
HETATM 13419 O  O   . HOH P 8 .   ? 27.587  22.358  -2.452  1.00 35.14  ? 616 HOH A O   1 
HETATM 13420 O  O   . HOH P 8 .   ? 18.994  -2.395  24.416  1.00 23.27  ? 617 HOH A O   1 
HETATM 13421 O  O   . HOH P 8 .   ? 19.827  5.070   9.241   1.00 32.99  ? 618 HOH A O   1 
HETATM 13422 O  O   . HOH P 8 .   ? -1.983  18.976  -12.796 1.00 36.59  ? 619 HOH A O   1 
HETATM 13423 O  O   . HOH P 8 .   ? 44.017  -15.911 20.690  1.00 32.30  ? 620 HOH A O   1 
HETATM 13424 O  O   . HOH P 8 .   ? 40.636  17.304  2.768   1.00 26.93  ? 621 HOH A O   1 
HETATM 13425 O  O   . HOH P 8 .   ? 22.162  20.533  -3.254  1.00 32.64  ? 622 HOH A O   1 
HETATM 13426 O  O   . HOH P 8 .   ? 30.629  5.313   -15.446 1.00 28.34  ? 623 HOH A O   1 
HETATM 13427 O  O   . HOH P 8 .   ? 27.130  17.405  -5.736  1.00 32.76  ? 624 HOH A O   1 
HETATM 13428 O  O   . HOH P 8 .   ? 51.584  -13.071 7.144   1.00 29.00  ? 625 HOH A O   1 
HETATM 13429 O  O   . HOH P 8 .   ? 40.269  10.974  -6.630  1.00 35.30  ? 626 HOH A O   1 
HETATM 13430 O  O   . HOH P 8 .   ? 30.814  -23.220 4.760   1.00 31.68  ? 627 HOH A O   1 
HETATM 13431 O  O   . HOH P 8 .   ? 51.656  -11.454 24.428  1.00 39.13  ? 628 HOH A O   1 
HETATM 13432 O  O   . HOH P 8 .   ? 19.079  2.085   3.193   1.00 35.31  ? 629 HOH A O   1 
HETATM 13433 O  O   . HOH P 8 .   ? 6.782   -6.387  5.890   1.00 32.03  ? 630 HOH A O   1 
HETATM 13434 O  O   . HOH P 8 .   ? 30.216  7.410   9.679   1.00 33.49  ? 631 HOH A O   1 
HETATM 13435 O  O   . HOH P 8 .   ? 24.137  -24.781 7.435   1.00 26.02  ? 632 HOH A O   1 
HETATM 13436 O  O   . HOH P 8 .   ? 43.149  -17.776 14.767  1.00 36.18  ? 633 HOH A O   1 
HETATM 13437 O  O   . HOH P 8 .   ? 26.195  -2.893  14.851  1.00 23.79  ? 634 HOH A O   1 
HETATM 13438 O  O   . HOH P 8 .   ? 7.576   15.511  -3.368  1.00 35.81  ? 635 HOH A O   1 
HETATM 13439 O  O   . HOH P 8 .   ? 13.876  17.877  12.807  1.00 33.48  ? 636 HOH A O   1 
HETATM 13440 O  O   . HOH P 8 .   ? 17.992  -17.199 16.064  1.00 24.44  ? 637 HOH A O   1 
HETATM 13441 O  O   . HOH P 8 .   ? 33.284  -13.602 27.061  1.00 31.43  ? 638 HOH A O   1 
HETATM 13442 O  O   . HOH P 8 .   ? 39.966  -21.708 12.299  1.00 37.54  ? 639 HOH A O   1 
HETATM 13443 O  O   . HOH P 8 .   ? 40.613  -3.962  9.041   1.00 24.39  ? 640 HOH A O   1 
HETATM 13444 O  O   . HOH P 8 .   ? 33.826  -16.695 16.060  1.00 35.64  ? 641 HOH A O   1 
HETATM 13445 O  O   . HOH P 8 .   ? 35.189  -20.821 14.748  1.00 31.70  ? 642 HOH A O   1 
HETATM 13446 O  O   . HOH P 8 .   ? 42.041  -5.289  4.575   1.00 37.55  ? 643 HOH A O   1 
HETATM 13447 O  O   . HOH P 8 .   ? 17.583  -25.282 10.235  1.00 25.41  ? 644 HOH A O   1 
HETATM 13448 O  O   . HOH P 8 .   ? 35.993  6.470   11.032  1.00 26.15  ? 645 HOH A O   1 
HETATM 13449 O  O   . HOH P 8 .   ? 40.212  7.667   -0.089  1.00 29.98  ? 646 HOH A O   1 
HETATM 13450 O  O   . HOH P 8 .   ? 29.249  8.340   20.340  1.00 22.02  ? 647 HOH A O   1 
HETATM 13451 O  O   . HOH P 8 .   ? 51.967  -3.198  25.690  1.00 37.62  ? 648 HOH A O   1 
HETATM 13452 O  O   . HOH P 8 .   ? 44.776  -2.976  27.834  1.00 35.21  ? 649 HOH A O   1 
HETATM 13453 O  O   . HOH P 8 .   ? 32.392  -27.310 9.387   1.00 31.29  ? 650 HOH A O   1 
HETATM 13454 O  O   . HOH P 8 .   ? 3.128   11.159  2.709   1.00 28.44  ? 651 HOH A O   1 
HETATM 13455 O  O   . HOH P 8 .   ? 19.484  -27.549 6.843   1.00 29.12  ? 652 HOH A O   1 
HETATM 13456 O  O   . HOH P 8 .   ? 23.599  -2.008  -10.219 1.00 35.86  ? 653 HOH A O   1 
HETATM 13457 O  O   . HOH P 8 .   ? 9.950   18.860  11.044  1.00 32.31  ? 654 HOH A O   1 
HETATM 13458 O  O   . HOH P 8 .   ? 12.793  14.555  -9.309  1.00 36.51  ? 655 HOH A O   1 
HETATM 13459 O  O   . HOH P 8 .   ? 19.417  -7.237  19.614  1.00 23.14  ? 656 HOH A O   1 
HETATM 13460 O  O   . HOH P 8 .   ? 24.946  12.660  -13.290 1.00 27.25  ? 657 HOH A O   1 
HETATM 13461 O  O   . HOH P 8 .   ? 16.208  5.385   13.803  1.00 27.01  ? 658 HOH A O   1 
HETATM 13462 O  O   . HOH P 8 .   ? 37.913  13.672  1.148   1.00 25.16  ? 659 HOH A O   1 
HETATM 13463 O  O   . HOH P 8 .   ? 26.674  -16.459 25.998  1.00 26.66  ? 660 HOH A O   1 
HETATM 13464 O  O   . HOH P 8 .   ? 39.595  0.716   29.152  1.00 25.12  ? 661 HOH A O   1 
HETATM 13465 O  O   . HOH P 8 .   ? 16.605  -14.087 6.390   1.00 28.22  ? 662 HOH A O   1 
HETATM 13466 O  O   . HOH P 8 .   ? 26.512  -3.163  26.095  1.00 23.90  ? 663 HOH A O   1 
HETATM 13467 O  O   . HOH P 8 .   ? 35.798  16.926  0.965   1.00 30.86  ? 664 HOH A O   1 
HETATM 13468 O  O   . HOH P 8 .   ? 52.140  15.186  15.852  1.00 37.41  ? 665 HOH A O   1 
HETATM 13469 O  O   . HOH P 8 .   ? 28.690  19.274  26.953  1.00 25.51  ? 666 HOH A O   1 
HETATM 13470 O  O   . HOH P 8 .   ? 29.322  14.642  23.911  1.00 25.37  ? 667 HOH A O   1 
HETATM 13471 O  O   . HOH P 8 .   ? 21.585  -9.071  -4.939  1.00 48.41  ? 668 HOH A O   1 
HETATM 13472 O  O   . HOH P 8 .   ? 50.442  -5.163  26.341  1.00 37.13  ? 669 HOH A O   1 
HETATM 13473 O  O   . HOH P 8 .   ? 12.709  14.789  15.755  1.00 27.36  ? 670 HOH A O   1 
HETATM 13474 O  O   . HOH P 8 .   ? 29.410  -16.776 11.905  1.00 25.49  ? 671 HOH A O   1 
HETATM 13475 O  O   . HOH P 8 .   ? 11.866  17.601  4.173   1.00 31.80  ? 672 HOH A O   1 
HETATM 13476 O  O   . HOH P 8 .   ? 13.334  16.717  -6.787  1.00 31.60  ? 673 HOH A O   1 
HETATM 13477 O  O   . HOH P 8 .   ? -2.612  -6.652  4.050   1.00 36.30  ? 674 HOH A O   1 
HETATM 13478 O  O   . HOH P 8 .   ? 37.018  -21.069 5.984   1.00 29.04  ? 675 HOH A O   1 
HETATM 13479 O  O   . HOH P 8 .   ? 31.858  15.664  -3.380  1.00 29.46  ? 676 HOH A O   1 
HETATM 13480 O  O   . HOH P 8 .   ? 49.905  3.993   24.143  1.00 28.48  ? 677 HOH A O   1 
HETATM 13481 O  O   . HOH P 8 .   ? 5.610   9.217   13.970  1.00 30.90  ? 678 HOH A O   1 
HETATM 13482 O  O   . HOH P 8 .   ? 19.646  8.363   -11.924 1.00 29.25  ? 679 HOH A O   1 
HETATM 13483 O  O   . HOH P 8 .   ? 36.202  -2.980  -12.467 1.00 29.30  ? 680 HOH A O   1 
HETATM 13484 O  O   . HOH P 8 .   ? 22.988  -24.145 3.233   1.00 33.06  ? 681 HOH A O   1 
HETATM 13485 O  O   . HOH P 8 .   ? 32.630  -8.516  7.029   1.00 19.51  ? 682 HOH A O   1 
HETATM 13486 O  O   . HOH P 8 .   ? 14.342  2.704   4.573   1.00 28.21  ? 683 HOH A O   1 
HETATM 13487 O  O   . HOH P 8 .   ? 48.965  0.766   8.072   1.00 26.49  ? 684 HOH A O   1 
HETATM 13488 O  O   . HOH P 8 .   ? 39.839  14.350  14.020  1.00 25.25  ? 685 HOH A O   1 
HETATM 13489 O  O   . HOH P 8 .   ? 22.194  14.281  -18.852 1.00 35.17  ? 686 HOH A O   1 
HETATM 13490 O  O   . HOH P 8 .   ? 33.250  -22.620 15.194  1.00 31.52  ? 687 HOH A O   1 
HETATM 13491 O  O   . HOH P 8 .   ? 12.366  -7.330  17.028  1.00 28.00  ? 688 HOH A O   1 
HETATM 13492 O  O   . HOH P 8 .   ? 18.106  8.240   6.025   1.00 25.17  ? 689 HOH A O   1 
HETATM 13493 O  O   . HOH P 8 .   ? 38.855  17.455  10.276  1.00 28.66  ? 690 HOH A O   1 
HETATM 13494 O  O   . HOH P 8 .   ? 17.397  -12.823 4.003   1.00 27.55  ? 691 HOH A O   1 
HETATM 13495 O  O   . HOH P 8 .   ? 43.589  -1.865  7.764   1.00 27.05  ? 692 HOH A O   1 
HETATM 13496 O  O   . HOH P 8 .   ? 2.496   8.235   3.051   1.00 27.41  ? 693 HOH A O   1 
HETATM 13497 O  O   . HOH P 8 .   ? 30.796  -22.691 19.560  1.00 32.19  ? 694 HOH A O   1 
HETATM 13498 O  O   . HOH P 8 .   ? 8.933   16.843  -5.061  1.00 33.40  ? 695 HOH A O   1 
HETATM 13499 O  O   . HOH P 8 .   ? 2.040   11.360  10.476  1.00 36.99  ? 696 HOH A O   1 
HETATM 13500 O  O   . HOH P 8 .   ? 17.426  -10.046 4.049   1.00 29.17  ? 697 HOH A O   1 
HETATM 13501 O  O   . HOH P 8 .   ? 10.050  14.062  16.191  1.00 24.83  ? 698 HOH A O   1 
HETATM 13502 O  O   . HOH P 8 .   ? 42.423  -0.487  -4.139  1.00 28.90  ? 699 HOH A O   1 
HETATM 13503 O  O   . HOH P 8 .   ? 4.866   15.645  4.792   1.00 25.72  ? 700 HOH A O   1 
HETATM 13504 O  O   . HOH P 8 .   ? 16.046  -7.532  16.557  1.00 24.42  ? 701 HOH A O   1 
HETATM 13505 O  O   . HOH P 8 .   ? 46.715  1.391   6.271   1.00 28.05  ? 702 HOH A O   1 
HETATM 13506 O  O   . HOH P 8 .   ? 10.671  17.066  -0.582  1.00 33.28  ? 703 HOH A O   1 
HETATM 13507 O  O   . HOH P 8 .   ? 37.846  -3.755  9.835   1.00 25.00  ? 704 HOH A O   1 
HETATM 13508 O  O   . HOH P 8 .   ? 22.163  9.197   13.832  1.00 26.44  ? 705 HOH A O   1 
HETATM 13509 O  O   . HOH P 8 .   ? 41.009  9.135   31.998  1.00 35.49  ? 706 HOH A O   1 
HETATM 13510 O  O   . HOH P 8 .   ? 28.397  3.198   24.746  1.00 22.32  ? 707 HOH A O   1 
HETATM 13511 O  O   . HOH P 8 .   ? 31.627  -4.906  -3.175  1.00 26.86  ? 708 HOH A O   1 
HETATM 13512 O  O   . HOH P 8 .   ? 29.879  -7.970  2.663   1.00 26.03  ? 709 HOH A O   1 
HETATM 13513 O  O   . HOH P 8 .   ? 57.325  3.041   13.789  1.00 33.54  ? 710 HOH A O   1 
HETATM 13514 O  O   . HOH P 8 .   ? 14.400  2.464   -7.699  1.00 35.20  ? 711 HOH A O   1 
HETATM 13515 O  O   . HOH P 8 .   ? 54.712  8.164   18.294  1.00 36.26  ? 712 HOH A O   1 
HETATM 13516 O  O   . HOH P 8 .   ? 36.720  -23.304 13.354  1.00 39.18  ? 713 HOH A O   1 
HETATM 13517 O  O   . HOH P 8 .   ? 16.376  -20.348 26.023  1.00 36.73  ? 714 HOH A O   1 
HETATM 13518 O  O   . HOH P 8 .   ? 2.388   15.752  3.386   1.00 31.31  ? 715 HOH A O   1 
HETATM 13519 O  O   . HOH P 8 .   ? 38.075  0.295   26.893  1.00 25.10  ? 716 HOH A O   1 
HETATM 13520 O  O   . HOH P 8 .   ? 28.795  -5.833  16.223  1.00 20.87  ? 717 HOH A O   1 
HETATM 13521 O  O   . HOH P 8 .   ? 37.265  21.371  8.226   1.00 38.70  ? 718 HOH A O   1 
HETATM 13522 O  O   . HOH P 8 .   ? 13.087  -9.706  15.591  1.00 27.34  ? 719 HOH A O   1 
HETATM 13523 O  O   . HOH P 8 .   ? 48.739  -1.896  8.741   1.00 28.20  ? 720 HOH A O   1 
HETATM 13524 O  O   . HOH P 8 .   ? 26.784  0.481   -19.859 1.00 29.60  ? 721 HOH A O   1 
HETATM 13525 O  O   . HOH P 8 .   ? 46.102  10.310  22.960  1.00 26.46  ? 722 HOH A O   1 
HETATM 13526 O  O   . HOH P 8 .   ? 38.850  5.982   -11.856 1.00 33.07  ? 723 HOH A O   1 
HETATM 13527 O  O   . HOH P 8 .   ? 18.058  20.046  8.815   1.00 26.88  ? 724 HOH A O   1 
HETATM 13528 O  O   . HOH P 8 .   ? 32.181  16.637  -0.650  1.00 29.86  ? 725 HOH A O   1 
HETATM 13529 O  O   . HOH P 8 .   ? 20.307  -6.484  3.120   1.00 36.90  ? 726 HOH A O   1 
HETATM 13530 O  O   . HOH P 8 .   ? 25.782  -24.326 3.431   1.00 34.54  ? 727 HOH A O   1 
HETATM 13531 O  O   . HOH P 8 .   ? 33.187  2.230   1.055   1.00 29.00  ? 728 HOH A O   1 
HETATM 13532 O  O   . HOH P 8 .   ? 7.538   -12.156 1.962   1.00 44.15  ? 729 HOH A O   1 
HETATM 13533 O  O   . HOH P 8 .   ? 30.877  3.441   3.442   1.00 23.78  ? 730 HOH A O   1 
HETATM 13534 O  O   . HOH P 8 .   ? 16.369  -16.762 5.983   1.00 28.30  ? 731 HOH A O   1 
HETATM 13535 O  O   . HOH P 8 .   ? 22.589  -22.378 1.266   1.00 37.33  ? 732 HOH A O   1 
HETATM 13536 O  O   . HOH P 8 .   ? 35.201  22.836  4.505   1.00 34.92  ? 733 HOH A O   1 
HETATM 13537 O  O   . HOH P 8 .   ? 14.851  13.977  -11.133 1.00 34.39  ? 734 HOH A O   1 
HETATM 13538 O  O   . HOH P 8 .   ? 16.950  10.545  23.644  1.00 31.81  ? 735 HOH A O   1 
HETATM 13539 O  O   . HOH P 8 .   ? 5.311   14.334  -6.040  1.00 34.48  ? 736 HOH A O   1 
HETATM 13540 O  O   . HOH P 8 .   ? 11.753  -13.728 13.109  1.00 27.29  ? 737 HOH A O   1 
HETATM 13541 O  O   . HOH P 8 .   ? 26.096  15.815  17.418  1.00 23.17  ? 738 HOH A O   1 
HETATM 13542 O  O   . HOH P 8 .   ? -1.976  5.432   -3.256  1.00 26.43  ? 739 HOH A O   1 
HETATM 13543 O  O   . HOH P 8 .   ? 13.934  19.119  3.982   1.00 28.59  ? 740 HOH A O   1 
HETATM 13544 O  O   . HOH P 8 .   ? 29.441  10.737  19.203  1.00 26.29  ? 741 HOH A O   1 
HETATM 13545 O  O   . HOH P 8 .   ? 17.954  -5.768  17.793  1.00 22.77  ? 742 HOH A O   1 
HETATM 13546 O  O   . HOH P 8 .   ? 39.855  11.474  1.215   1.00 26.10  ? 743 HOH A O   1 
HETATM 13547 O  O   . HOH P 8 .   ? 24.614  -4.117  -4.656  1.00 36.40  ? 744 HOH A O   1 
HETATM 13548 O  O   . HOH P 8 .   ? 19.654  4.900   12.040  1.00 32.66  ? 745 HOH A O   1 
HETATM 13549 O  O   . HOH P 8 .   ? 25.166  15.233  -14.339 1.00 29.97  ? 746 HOH A O   1 
HETATM 13550 O  O   . HOH P 8 .   ? 16.498  8.326   15.521  1.00 26.59  ? 747 HOH A O   1 
HETATM 13551 O  O   . HOH P 8 .   ? 44.547  -1.748  -7.101  1.00 43.46  ? 748 HOH A O   1 
HETATM 13552 O  O   . HOH P 8 .   ? 36.076  -1.340  8.401   1.00 24.97  ? 749 HOH A O   1 
HETATM 13553 O  O   . HOH P 8 .   ? 36.878  -0.221  18.534  1.00 21.33  ? 750 HOH A O   1 
HETATM 13554 O  O   . HOH P 8 .   ? 27.046  -28.439 5.885   1.00 29.22  ? 751 HOH A O   1 
HETATM 13555 O  O   . HOH P 8 .   ? 30.532  13.616  10.411  1.00 23.47  ? 752 HOH A O   1 
HETATM 13556 O  O   . HOH P 8 .   ? 39.327  -6.031  27.729  1.00 29.53  ? 753 HOH A O   1 
HETATM 13557 O  O   . HOH P 8 .   ? 48.413  -15.968 5.060   1.00 32.27  ? 754 HOH A O   1 
HETATM 13558 O  O   . HOH P 8 .   ? 32.662  15.688  30.525  1.00 28.55  ? 755 HOH A O   1 
HETATM 13559 O  O   . HOH P 8 .   ? 44.248  -19.735 7.521   1.00 34.36  ? 756 HOH A O   1 
HETATM 13560 O  O   . HOH P 8 .   ? 12.049  -12.383 15.578  1.00 27.15  ? 757 HOH A O   1 
HETATM 13561 O  O   . HOH P 8 .   ? 45.036  7.653   -4.489  1.00 36.43  ? 758 HOH A O   1 
HETATM 13562 O  O   . HOH P 8 .   ? 40.131  -10.615 27.214  1.00 28.82  ? 759 HOH A O   1 
HETATM 13563 O  O   . HOH P 8 .   ? 37.154  -4.261  27.099  1.00 23.70  ? 760 HOH A O   1 
HETATM 13564 O  O   . HOH P 8 .   ? 37.139  12.405  -13.134 1.00 38.33  ? 761 HOH A O   1 
HETATM 13565 O  O   . HOH P 8 .   ? 39.492  13.500  31.842  1.00 27.72  ? 762 HOH A O   1 
HETATM 13566 O  O   . HOH P 8 .   ? 16.002  -23.982 16.225  1.00 25.30  ? 763 HOH A O   1 
HETATM 13567 O  O   . HOH P 8 .   ? 28.923  4.861   4.859   1.00 20.03  ? 764 HOH A O   1 
HETATM 13568 O  O   . HOH P 8 .   ? 0.738   18.575  -4.005  1.00 35.79  ? 765 HOH A O   1 
HETATM 13569 O  O   . HOH P 8 .   ? 54.697  -0.245  20.714  1.00 38.18  ? 766 HOH A O   1 
HETATM 13570 O  O   . HOH P 8 .   ? 15.420  -19.165 14.193  1.00 32.44  ? 767 HOH A O   1 
HETATM 13571 O  O   . HOH P 8 .   ? 18.538  18.570  16.929  1.00 32.20  ? 768 HOH A O   1 
HETATM 13572 O  O   . HOH P 8 .   ? 25.753  3.919   24.072  1.00 21.57  ? 769 HOH A O   1 
HETATM 13573 O  O   . HOH P 8 .   ? 18.632  -17.110 -1.031  1.00 36.86  ? 770 HOH A O   1 
HETATM 13574 O  O   . HOH P 8 .   ? 16.374  -17.300 18.128  1.00 29.29  ? 771 HOH A O   1 
HETATM 13575 O  O   . HOH P 8 .   ? 42.587  -3.924  11.221  1.00 32.53  ? 772 HOH A O   1 
HETATM 13576 O  O   . HOH P 8 .   ? 23.082  -4.442  -7.966  1.00 45.59  ? 773 HOH A O   1 
HETATM 13577 O  O   . HOH P 8 .   ? 16.833  3.067   -7.054  1.00 32.34  ? 774 HOH A O   1 
HETATM 13578 O  O   . HOH P 8 .   ? 40.068  -9.706  5.943   1.00 25.22  ? 775 HOH A O   1 
HETATM 13579 O  O   . HOH P 8 .   ? 23.733  17.274  8.924   1.00 26.48  ? 776 HOH A O   1 
HETATM 13580 O  O   . HOH P 8 .   ? 12.351  -16.470 20.941  1.00 35.55  ? 777 HOH A O   1 
HETATM 13581 O  O   . HOH P 8 .   ? 36.112  -2.091  11.355  1.00 26.27  ? 778 HOH A O   1 
HETATM 13582 O  O   . HOH P 8 .   ? 23.408  -27.002 5.161   1.00 32.84  ? 779 HOH A O   1 
HETATM 13583 O  O   . HOH P 8 .   ? 42.104  10.262  -0.348  1.00 34.37  ? 780 HOH A O   1 
HETATM 13584 O  O   . HOH P 8 .   ? 34.024  3.252   13.437  1.00 22.92  ? 781 HOH A O   1 
HETATM 13585 O  O   . HOH P 8 .   ? 31.850  -9.274  -3.866  1.00 32.94  ? 782 HOH A O   1 
HETATM 13586 O  O   . HOH P 8 .   ? 46.926  -0.787  4.627   1.00 33.30  ? 783 HOH A O   1 
HETATM 13587 O  O   . HOH P 8 .   ? 20.891  -7.956  5.118   1.00 33.08  ? 784 HOH A O   1 
HETATM 13588 O  O   . HOH P 8 .   ? 43.670  5.556   -6.253  1.00 31.59  ? 785 HOH A O   1 
HETATM 13589 O  O   . HOH P 8 .   ? 28.253  18.346  9.524   1.00 32.78  ? 786 HOH A O   1 
HETATM 13590 O  O   . HOH P 8 .   ? 17.592  -0.488  11.842  1.00 34.20  ? 787 HOH A O   1 
HETATM 13591 O  O   . HOH P 8 .   ? 4.311   0.433   8.664   1.00 37.34  ? 788 HOH A O   1 
HETATM 13592 O  O   . HOH P 8 .   ? 5.563   -3.360  5.067   1.00 35.15  ? 789 HOH A O   1 
HETATM 13593 O  O   . HOH P 8 .   ? 22.428  -22.348 26.502  1.00 30.41  ? 790 HOH A O   1 
HETATM 13594 O  O   . HOH P 8 .   ? 4.767   7.995   7.472   1.00 35.91  ? 791 HOH A O   1 
HETATM 13595 O  O   . HOH P 8 .   ? 33.249  -3.986  -14.004 1.00 35.61  ? 792 HOH A O   1 
HETATM 13596 O  O   . HOH P 8 .   ? 37.604  11.595  31.337  1.00 24.94  ? 793 HOH A O   1 
HETATM 13597 O  O   . HOH P 8 .   ? 15.535  -10.053 14.708  1.00 20.90  ? 794 HOH A O   1 
HETATM 13598 O  O   . HOH P 8 .   ? 40.557  -6.437  -0.270  1.00 33.59  ? 795 HOH A O   1 
HETATM 13599 O  O   . HOH P 8 .   ? 14.411  14.192  -13.700 1.00 39.55  ? 796 HOH A O   1 
HETATM 13600 O  O   . HOH P 8 .   ? 24.606  3.391   -10.773 1.00 34.72  ? 797 HOH A O   1 
HETATM 13601 O  O   . HOH P 8 .   ? 9.645   -15.392 13.440  1.00 30.74  ? 798 HOH A O   1 
HETATM 13602 O  O   . HOH P 8 .   ? 24.437  0.836   24.957  1.00 22.82  ? 799 HOH A O   1 
HETATM 13603 O  O   . HOH P 8 .   ? 10.796  -20.603 11.748  1.00 33.76  ? 800 HOH A O   1 
HETATM 13604 O  O   . HOH P 8 .   ? 45.555  -13.990 4.224   1.00 35.29  ? 801 HOH A O   1 
HETATM 13605 O  O   . HOH P 8 .   ? 44.748  12.215  24.387  1.00 27.45  ? 802 HOH A O   1 
HETATM 13606 O  O   . HOH P 8 .   ? 31.328  20.572  10.382  1.00 34.63  ? 803 HOH A O   1 
HETATM 13607 O  O   . HOH P 8 .   ? 35.797  20.618  28.018  1.00 33.35  ? 804 HOH A O   1 
HETATM 13608 O  O   . HOH P 8 .   ? 45.910  14.930  0.797   1.00 43.02  ? 805 HOH A O   1 
HETATM 13609 O  O   . HOH P 8 .   ? 44.275  -4.180  9.116   1.00 34.04  ? 806 HOH A O   1 
HETATM 13610 O  O   . HOH P 8 .   ? 56.965  -2.975  15.916  1.00 34.22  ? 807 HOH A O   1 
HETATM 13611 O  O   . HOH P 8 .   ? 22.996  6.234   -22.810 1.00 42.28  ? 808 HOH A O   1 
HETATM 13612 O  O   . HOH P 8 .   ? 22.629  15.502  7.030   1.00 26.53  ? 809 HOH A O   1 
HETATM 13613 O  O   . HOH P 8 .   ? 0.000   6.205   0.000   0.50 28.14  ? 810 HOH A O   1 
HETATM 13614 O  O   . HOH P 8 .   ? 35.913  18.488  30.116  1.00 25.55  ? 811 HOH A O   1 
HETATM 13615 O  O   . HOH P 8 .   ? 43.720  11.957  30.509  1.00 36.82  ? 812 HOH A O   1 
HETATM 13616 O  O   . HOH P 8 .   ? 41.465  -6.153  7.727   1.00 28.21  ? 813 HOH A O   1 
HETATM 13617 O  O   . HOH P 8 .   ? 49.419  -5.038  29.091  1.00 47.36  ? 814 HOH A O   1 
HETATM 13618 O  O   . HOH P 8 .   ? 27.448  13.933  13.381  1.00 28.52  ? 815 HOH A O   1 
HETATM 13619 O  O   . HOH P 8 .   ? 53.136  10.144  21.278  1.00 34.78  ? 816 HOH A O   1 
HETATM 13620 O  O   . HOH P 8 .   ? 21.760  17.343  12.976  1.00 29.21  ? 817 HOH A O   1 
HETATM 13621 O  O   . HOH P 8 .   ? 24.440  28.051  -0.227  1.00 34.18  ? 818 HOH A O   1 
HETATM 13622 O  O   . HOH P 8 .   ? 56.417  -8.711  21.124  1.00 40.97  ? 819 HOH A O   1 
HETATM 13623 O  O   . HOH P 8 .   ? 45.931  -2.315  1.824   1.00 31.65  ? 820 HOH A O   1 
HETATM 13624 O  O   . HOH P 8 .   ? 9.795   -7.683  16.431  1.00 41.85  ? 821 HOH A O   1 
HETATM 13625 O  O   . HOH P 8 .   ? 29.540  -6.587  -3.428  1.00 41.32  ? 822 HOH A O   1 
HETATM 13626 O  O   . HOH P 8 .   ? 20.536  19.389  -10.240 1.00 32.73  ? 823 HOH A O   1 
HETATM 13627 O  O   . HOH P 8 .   ? 38.388  -25.015 6.450   1.00 35.83  ? 824 HOH A O   1 
HETATM 13628 O  O   . HOH P 8 .   ? 56.388  -8.067  16.530  1.00 27.78  ? 825 HOH A O   1 
HETATM 13629 O  O   . HOH P 8 .   ? 8.526   16.367  15.521  1.00 31.46  ? 826 HOH A O   1 
HETATM 13630 O  O   . HOH P 8 .   ? 27.086  -12.395 -0.901  1.00 41.57  ? 827 HOH A O   1 
HETATM 13631 O  O   . HOH P 8 .   ? 2.508   4.725   0.653   1.00 30.80  ? 828 HOH A O   1 
HETATM 13632 O  O   . HOH P 8 .   ? 31.994  16.815  -12.521 1.00 43.85  ? 829 HOH A O   1 
HETATM 13633 O  O   . HOH P 8 .   ? 22.621  -2.156  -12.818 1.00 34.54  ? 830 HOH A O   1 
HETATM 13634 O  O   . HOH P 8 .   ? 49.261  -13.255 5.858   1.00 35.68  ? 831 HOH A O   1 
HETATM 13635 O  O   . HOH P 8 .   ? 0.511   -3.191  5.329   1.00 25.54  ? 832 HOH A O   1 
HETATM 13636 O  O   . HOH P 8 .   ? 24.591  19.717  14.622  1.00 38.59  ? 833 HOH A O   1 
HETATM 13637 O  O   . HOH P 8 .   ? 24.021  21.161  -1.345  1.00 35.11  ? 834 HOH A O   1 
HETATM 13638 O  O   . HOH P 8 .   ? 40.598  16.477  12.393  1.00 32.36  ? 835 HOH A O   1 
HETATM 13639 O  O   . HOH P 8 .   ? 10.734  -18.404 18.966  1.00 41.99  ? 836 HOH A O   1 
HETATM 13640 O  O   . HOH P 8 .   ? 3.889   -1.731  7.436   1.00 39.82  ? 837 HOH A O   1 
HETATM 13641 O  O   . HOH P 8 .   ? 16.954  -26.366 7.638   1.00 34.68  ? 838 HOH A O   1 
HETATM 13642 O  O   . HOH P 8 .   ? 25.799  17.135  10.823  1.00 34.59  ? 839 HOH A O   1 
HETATM 13643 O  O   . HOH P 8 .   ? 21.674  18.357  10.426  1.00 25.50  ? 840 HOH A O   1 
HETATM 13644 O  O   . HOH P 8 .   ? 2.033   -4.310  -5.625  1.00 36.74  ? 841 HOH A O   1 
HETATM 13645 O  O   . HOH P 8 .   ? 15.002  -25.273 14.023  1.00 31.89  ? 842 HOH A O   1 
HETATM 13646 O  O   . HOH P 8 .   ? 28.172  15.418  10.837  1.00 31.66  ? 843 HOH A O   1 
HETATM 13647 O  O   . HOH P 8 .   ? 17.567  21.187  6.375   1.00 33.55  ? 844 HOH A O   1 
HETATM 13648 O  O   . HOH P 8 .   ? 13.765  20.405  1.540   1.00 31.25  ? 845 HOH A O   1 
HETATM 13649 O  O   . HOH P 8 .   ? 41.926  12.272  32.311  1.00 41.93  ? 846 HOH A O   1 
HETATM 13650 O  O   . HOH P 8 .   ? 41.523  -8.067  4.388   1.00 35.79  ? 847 HOH A O   1 
HETATM 13651 O  O   . HOH P 8 .   ? 33.435  18.118  31.543  1.00 25.86  ? 848 HOH A O   1 
HETATM 13652 O  O   . HOH P 8 .   ? 29.155  18.814  29.675  1.00 21.92  ? 849 HOH A O   1 
HETATM 13653 O  O   . HOH P 8 .   ? 20.537  20.701  9.769   1.00 33.74  ? 850 HOH A O   1 
HETATM 13654 O  O   . HOH P 8 .   ? 14.556  21.489  5.734   1.00 39.40  ? 851 HOH A O   1 
HETATM 13655 O  O   . HOH P 8 .   ? 26.578  16.059  14.704  1.00 29.07  ? 852 HOH A O   1 
HETATM 13656 O  O   . HOH P 8 .   ? 12.854  17.471  15.330  1.00 32.92  ? 853 HOH A O   1 
HETATM 13657 O  O   . HOH P 8 .   ? 24.479  17.422  13.384  1.00 30.42  ? 854 HOH A O   1 
HETATM 13658 O  O   . HOH P 8 .   ? 42.739  -6.933  -1.810  1.00 36.91  ? 855 HOH A O   1 
HETATM 13659 O  O   . HOH P 8 .   ? 43.826  -2.617  -4.530  1.00 36.21  ? 856 HOH A O   1 
HETATM 13660 O  O   . HOH P 8 .   ? 31.491  20.140  30.773  1.00 27.22  ? 857 HOH A O   1 
HETATM 13661 O  O   . HOH Q 8 .   ? 6.302   -0.060  35.073  1.00 35.00  ? 501 HOH B O   1 
HETATM 13662 O  O   . HOH Q 8 .   ? 29.591  24.725  43.139  1.00 33.31  ? 502 HOH B O   1 
HETATM 13663 O  O   . HOH Q 8 .   ? 17.706  10.185  56.998  1.00 37.52  ? 503 HOH B O   1 
HETATM 13664 O  O   . HOH Q 8 .   ? 15.036  -7.725  21.243  1.00 18.62  ? 504 HOH B O   1 
HETATM 13665 O  O   . HOH Q 8 .   ? 22.039  14.312  55.851  1.00 41.55  ? 505 HOH B O   1 
HETATM 13666 O  O   . HOH Q 8 .   ? 29.559  -17.054 40.216  1.00 33.94  ? 506 HOH B O   1 
HETATM 13667 O  O   . HOH Q 8 .   ? 30.075  5.003   53.233  1.00 34.84  ? 507 HOH B O   1 
HETATM 13668 O  O   . HOH Q 8 .   ? 6.100   17.064  33.414  1.00 27.29  ? 508 HOH B O   1 
HETATM 13669 O  O   . HOH Q 8 .   ? 30.371  25.040  45.694  1.00 37.12  ? 509 HOH B O   1 
HETATM 13670 O  O   . HOH Q 8 .   ? 14.394  -20.902 28.620  1.00 38.87  ? 510 HOH B O   1 
HETATM 13671 O  O   . HOH Q 8 .   ? 12.132  -8.053  33.418  1.00 30.48  ? 511 HOH B O   1 
HETATM 13672 O  O   . HOH Q 8 .   ? 22.965  -9.139  51.664  1.00 35.67  ? 512 HOH B O   1 
HETATM 13673 O  O   . HOH Q 8 .   ? 15.433  -14.484 26.401  1.00 28.52  ? 513 HOH B O   1 
HETATM 13674 O  O   . HOH Q 8 .   ? 10.659  -11.052 23.348  1.00 30.26  ? 514 HOH B O   1 
HETATM 13675 O  O   . HOH Q 8 .   ? 32.679  -12.292 29.108  1.00 35.09  ? 515 HOH B O   1 
HETATM 13676 O  O   . HOH Q 8 .   ? -0.173  1.536   30.815  1.00 35.83  ? 516 HOH B O   1 
HETATM 13677 O  O   . HOH Q 8 .   ? 36.827  -6.525  33.703  1.00 36.63  ? 517 HOH B O   1 
HETATM 13678 O  O   . HOH Q 8 .   ? 12.834  -12.625 59.245  1.00 29.92  ? 518 HOH B O   1 
HETATM 13679 O  O   . HOH Q 8 .   ? 2.758   -11.710 49.646  1.00 37.53  ? 519 HOH B O   1 
HETATM 13680 O  O   . HOH Q 8 .   ? 3.638   16.782  20.431  1.00 36.97  ? 520 HOH B O   1 
HETATM 13681 O  O   . HOH Q 8 .   ? 14.973  10.700  57.934  1.00 36.57  ? 521 HOH B O   1 
HETATM 13682 O  O   . HOH Q 8 .   ? 21.493  18.475  50.836  1.00 32.45  ? 522 HOH B O   1 
HETATM 13683 O  O   . HOH Q 8 .   ? 26.305  -9.708  32.142  1.00 26.57  ? 523 HOH B O   1 
HETATM 13684 O  O   . HOH Q 8 .   ? 10.834  -22.662 53.060  1.00 36.29  ? 524 HOH B O   1 
HETATM 13685 O  O   . HOH Q 8 .   ? 11.012  6.665   17.997  1.00 33.72  ? 525 HOH B O   1 
HETATM 13686 O  O   . HOH Q 8 .   ? 26.806  15.185  32.587  1.00 22.21  ? 526 HOH B O   1 
HETATM 13687 O  O   . HOH Q 8 .   ? 12.762  -21.006 54.451  1.00 31.78  ? 527 HOH B O   1 
HETATM 13688 O  O   . HOH Q 8 .   ? 19.414  6.515   41.246  1.00 26.61  ? 528 HOH B O   1 
HETATM 13689 O  O   . HOH Q 8 .   ? 31.720  -2.637  32.258  1.00 21.09  ? 529 HOH B O   1 
HETATM 13690 O  O   . HOH Q 8 .   ? 20.874  -7.218  52.718  1.00 38.40  ? 530 HOH B O   1 
HETATM 13691 O  O   . HOH Q 8 .   ? 37.858  6.791   49.139  1.00 31.80  ? 531 HOH B O   1 
HETATM 13692 O  O   . HOH Q 8 .   ? 25.306  7.708   37.526  1.00 32.84  ? 532 HOH B O   1 
HETATM 13693 O  O   . HOH Q 8 .   ? 39.929  12.229  46.729  1.00 31.89  ? 533 HOH B O   1 
HETATM 13694 O  O   . HOH Q 8 .   ? 31.724  3.246   45.343  1.00 25.40  ? 534 HOH B O   1 
HETATM 13695 O  O   . HOH Q 8 .   ? 29.950  16.403  30.769  1.00 26.16  ? 535 HOH B O   1 
HETATM 13696 O  O   . HOH Q 8 .   ? 0.282   -26.146 36.926  1.00 39.57  ? 536 HOH B O   1 
HETATM 13697 O  O   . HOH Q 8 .   ? 5.761   22.430  34.444  1.00 37.83  ? 537 HOH B O   1 
HETATM 13698 O  O   . HOH Q 8 .   ? 31.020  8.648   50.951  1.00 25.32  ? 538 HOH B O   1 
HETATM 13699 O  O   . HOH Q 8 .   ? 7.125   -17.709 56.837  1.00 43.35  ? 539 HOH B O   1 
HETATM 13700 O  O   . HOH Q 8 .   ? 22.189  -7.433  37.867  1.00 26.08  ? 540 HOH B O   1 
HETATM 13701 O  O   . HOH Q 8 .   ? 1.177   20.727  43.978  1.00 36.09  ? 541 HOH B O   1 
HETATM 13702 O  O   . HOH Q 8 .   ? 19.664  11.143  35.276  1.00 23.55  ? 542 HOH B O   1 
HETATM 13703 O  O   . HOH Q 8 .   ? 30.236  13.154  51.722  1.00 34.23  ? 543 HOH B O   1 
HETATM 13704 O  O   . HOH Q 8 .   ? 32.012  10.808  29.629  1.00 29.76  ? 544 HOH B O   1 
HETATM 13705 O  O   . HOH Q 8 .   ? 30.193  -4.382  34.937  1.00 22.54  ? 545 HOH B O   1 
HETATM 13706 O  O   A HOH Q 8 .   ? 27.036  -19.694 32.112  0.51 28.14  ? 546 HOH B O   1 
HETATM 13707 O  O   B HOH Q 8 .   ? 28.002  -20.999 30.795  0.49 33.44  ? 546 HOH B O   1 
HETATM 13708 O  O   . HOH Q 8 .   ? 4.312   4.029   39.511  1.00 36.30  ? 547 HOH B O   1 
HETATM 13709 O  O   . HOH Q 8 .   ? 4.217   2.076   20.874  1.00 32.60  ? 548 HOH B O   1 
HETATM 13710 O  O   . HOH Q 8 .   ? 10.742  4.607   32.843  1.00 32.57  ? 549 HOH B O   1 
HETATM 13711 O  O   . HOH Q 8 .   ? 29.993  -9.616  40.741  1.00 34.79  ? 550 HOH B O   1 
HETATM 13712 O  O   . HOH Q 8 .   ? 28.985  -2.677  44.720  1.00 34.48  ? 551 HOH B O   1 
HETATM 13713 O  O   . HOH Q 8 .   ? 20.968  -6.654  41.812  1.00 24.12  ? 552 HOH B O   1 
HETATM 13714 O  O   . HOH Q 8 .   ? 40.465  9.085   47.003  1.00 36.82  ? 553 HOH B O   1 
HETATM 13715 O  O   . HOH Q 8 .   ? 35.554  3.133   42.919  1.00 29.33  ? 554 HOH B O   1 
HETATM 13716 O  O   . HOH Q 8 .   ? 20.213  3.854   45.722  1.00 27.86  ? 555 HOH B O   1 
HETATM 13717 O  O   . HOH Q 8 .   ? 30.700  8.386   29.105  1.00 26.29  ? 556 HOH B O   1 
HETATM 13718 O  O   . HOH Q 8 .   ? 39.181  6.455   36.101  1.00 24.36  ? 557 HOH B O   1 
HETATM 13719 O  O   . HOH Q 8 .   ? 8.042   19.146  25.836  1.00 30.60  ? 558 HOH B O   1 
HETATM 13720 O  O   . HOH Q 8 .   ? -0.988  12.228  38.049  1.00 31.82  ? 559 HOH B O   1 
HETATM 13721 O  O   . HOH Q 8 .   ? 20.416  24.520  43.774  1.00 30.70  ? 560 HOH B O   1 
HETATM 13722 O  O   . HOH Q 8 .   ? 37.288  3.404   36.342  1.00 24.12  ? 561 HOH B O   1 
HETATM 13723 O  O   . HOH Q 8 .   ? 15.461  -5.256  19.452  1.00 30.01  ? 562 HOH B O   1 
HETATM 13724 O  O   . HOH Q 8 .   ? 18.340  4.797   47.895  1.00 33.55  ? 563 HOH B O   1 
HETATM 13725 O  O   . HOH Q 8 .   ? 12.304  -5.482  46.577  1.00 33.85  ? 564 HOH B O   1 
HETATM 13726 O  O   . HOH Q 8 .   ? 21.162  2.853   41.501  1.00 21.28  ? 565 HOH B O   1 
HETATM 13727 O  O   . HOH Q 8 .   ? 31.717  11.419  50.484  1.00 36.57  ? 566 HOH B O   1 
HETATM 13728 O  O   . HOH Q 8 .   ? 35.780  19.013  37.348  1.00 37.66  ? 567 HOH B O   1 
HETATM 13729 O  O   . HOH Q 8 .   ? 20.608  -21.654 28.482  1.00 28.66  ? 568 HOH B O   1 
HETATM 13730 O  O   . HOH Q 8 .   ? 11.244  -12.079 51.526  1.00 33.87  ? 569 HOH B O   1 
HETATM 13731 O  O   . HOH Q 8 .   ? 19.317  4.579   28.813  1.00 23.82  ? 570 HOH B O   1 
HETATM 13732 O  O   . HOH Q 8 .   ? 27.393  9.136   53.001  1.00 31.58  ? 571 HOH B O   1 
HETATM 13733 O  O   . HOH Q 8 .   ? 27.551  21.595  32.844  1.00 22.85  ? 572 HOH B O   1 
HETATM 13734 O  O   . HOH Q 8 .   ? 2.097   16.526  31.491  1.00 30.61  ? 573 HOH B O   1 
HETATM 13735 O  O   . HOH Q 8 .   ? 1.430   6.654   36.328  1.00 39.14  ? 574 HOH B O   1 
HETATM 13736 O  O   . HOH Q 8 .   ? 16.915  13.069  23.591  1.00 34.88  ? 575 HOH B O   1 
HETATM 13737 O  O   . HOH Q 8 .   ? 27.324  -0.119  37.669  1.00 23.77  ? 576 HOH B O   1 
HETATM 13738 O  O   . HOH Q 8 .   ? 7.140   -15.484 55.741  1.00 39.01  ? 577 HOH B O   1 
HETATM 13739 O  O   . HOH Q 8 .   ? 1.671   15.373  28.901  1.00 32.10  ? 578 HOH B O   1 
HETATM 13740 O  O   . HOH Q 8 .   ? 27.788  11.872  52.863  1.00 28.65  ? 579 HOH B O   1 
HETATM 13741 O  O   . HOH Q 8 .   ? 30.115  -2.194  38.892  1.00 34.35  ? 580 HOH B O   1 
HETATM 13742 O  O   . HOH Q 8 .   ? 5.838   10.665  44.210  1.00 27.00  ? 581 HOH B O   1 
HETATM 13743 O  O   . HOH Q 8 .   ? 10.526  -5.711  34.106  1.00 34.08  ? 582 HOH B O   1 
HETATM 13744 O  O   . HOH Q 8 .   ? 12.951  10.386  45.844  1.00 30.59  ? 583 HOH B O   1 
HETATM 13745 O  O   . HOH Q 8 .   ? 27.979  -14.048 26.630  1.00 26.91  ? 584 HOH B O   1 
HETATM 13746 O  O   . HOH Q 8 .   ? 26.488  24.660  52.347  1.00 35.66  ? 585 HOH B O   1 
HETATM 13747 O  O   . HOH Q 8 .   ? 24.112  8.382   56.224  1.00 32.11  ? 586 HOH B O   1 
HETATM 13748 O  O   . HOH Q 8 .   ? 14.362  12.256  48.000  1.00 34.78  ? 587 HOH B O   1 
HETATM 13749 O  O   . HOH Q 8 .   ? 2.710   1.546   57.681  1.00 38.60  ? 588 HOH B O   1 
HETATM 13750 O  O   . HOH Q 8 .   ? 17.506  -10.834 33.518  1.00 23.98  ? 589 HOH B O   1 
HETATM 13751 O  O   . HOH Q 8 .   ? 24.824  -7.153  37.970  1.00 24.49  ? 590 HOH B O   1 
HETATM 13752 O  O   . HOH Q 8 .   ? 33.078  18.252  34.306  1.00 23.97  ? 591 HOH B O   1 
HETATM 13753 O  O   . HOH Q 8 .   ? 30.123  1.221   46.705  1.00 28.24  ? 592 HOH B O   1 
HETATM 13754 O  O   . HOH Q 8 .   ? 8.130   8.902   57.436  1.00 37.82  ? 593 HOH B O   1 
HETATM 13755 O  O   . HOH Q 8 .   ? 22.950  -2.159  56.027  1.00 32.02  ? 594 HOH B O   1 
HETATM 13756 O  O   . HOH Q 8 .   ? 3.549   14.405  50.382  1.00 35.35  ? 595 HOH B O   1 
HETATM 13757 O  O   . HOH Q 8 .   ? 10.919  3.800   17.936  1.00 32.09  ? 596 HOH B O   1 
HETATM 13758 O  O   . HOH Q 8 .   ? 17.755  -14.749 24.878  1.00 23.65  ? 597 HOH B O   1 
HETATM 13759 O  O   . HOH Q 8 .   ? 31.984  5.777   46.276  1.00 23.23  ? 598 HOH B O   1 
HETATM 13760 O  O   . HOH Q 8 .   ? 12.903  -2.586  68.519  1.00 42.41  ? 599 HOH B O   1 
HETATM 13761 O  O   . HOH Q 8 .   ? 4.273   -0.195  16.478  1.00 34.54  ? 600 HOH B O   1 
HETATM 13762 O  O   . HOH Q 8 .   ? 39.570  13.726  44.329  1.00 35.55  ? 601 HOH B O   1 
HETATM 13763 O  O   . HOH Q 8 .   ? -3.653  4.046   29.485  1.00 41.72  ? 602 HOH B O   1 
HETATM 13764 O  O   . HOH Q 8 .   ? 14.438  -20.503 32.777  1.00 34.53  ? 603 HOH B O   1 
HETATM 13765 O  O   . HOH Q 8 .   ? 5.629   10.160  41.440  1.00 27.94  ? 604 HOH B O   1 
HETATM 13766 O  O   . HOH Q 8 .   ? 26.727  19.671  30.791  1.00 26.82  ? 605 HOH B O   1 
HETATM 13767 O  O   . HOH Q 8 .   ? 38.532  9.015   31.443  1.00 24.37  ? 606 HOH B O   1 
HETATM 13768 O  O   . HOH Q 8 .   ? 10.539  -9.335  43.580  1.00 28.64  ? 607 HOH B O   1 
HETATM 13769 O  O   . HOH Q 8 .   ? 20.082  -23.924 29.715  1.00 35.52  ? 608 HOH B O   1 
HETATM 13770 O  O   . HOH Q 8 .   ? 27.678  -0.742  50.592  1.00 34.19  ? 609 HOH B O   1 
HETATM 13771 O  O   . HOH Q 8 .   ? 19.414  -12.129 31.811  1.00 22.98  ? 610 HOH B O   1 
HETATM 13772 O  O   . HOH Q 8 .   ? 14.186  8.637   41.429  1.00 32.82  ? 611 HOH B O   1 
HETATM 13773 O  O   . HOH Q 8 .   ? 33.798  17.138  48.833  1.00 29.59  ? 612 HOH B O   1 
HETATM 13774 O  O   . HOH Q 8 .   ? 31.426  23.266  41.522  1.00 33.34  ? 613 HOH B O   1 
HETATM 13775 O  O   . HOH Q 8 .   ? 2.840   -9.807  51.527  1.00 33.57  ? 614 HOH B O   1 
HETATM 13776 O  O   . HOH Q 8 .   ? 15.136  -11.871 33.081  1.00 29.49  ? 615 HOH B O   1 
HETATM 13777 O  O   . HOH Q 8 .   ? 33.329  12.957  31.126  1.00 25.59  ? 616 HOH B O   1 
HETATM 13778 O  O   . HOH Q 8 .   ? 28.047  -7.631  43.784  1.00 38.69  ? 617 HOH B O   1 
HETATM 13779 O  O   . HOH Q 8 .   ? 20.161  5.953   43.903  1.00 28.18  ? 618 HOH B O   1 
HETATM 13780 O  O   . HOH Q 8 .   ? 15.585  13.986  51.013  1.00 38.31  ? 619 HOH B O   1 
HETATM 13781 O  O   . HOH Q 8 .   ? 28.805  -23.151 31.647  1.00 41.78  ? 620 HOH B O   1 
HETATM 13782 O  O   . HOH Q 8 .   ? 32.279  17.233  51.289  1.00 37.63  ? 621 HOH B O   1 
HETATM 13783 O  O   . HOH Q 8 .   ? -1.464  3.913   31.137  1.00 36.99  ? 622 HOH B O   1 
HETATM 13784 O  O   . HOH Q 8 .   ? 2.912   14.095  32.307  1.00 25.19  ? 623 HOH B O   1 
HETATM 13785 O  O   . HOH Q 8 .   ? 32.582  -13.286 31.874  1.00 29.58  ? 624 HOH B O   1 
HETATM 13786 O  O   . HOH Q 8 .   ? 36.111  9.281   40.137  1.00 29.33  ? 625 HOH B O   1 
HETATM 13787 O  O   . HOH Q 8 .   ? 20.396  19.449  28.546  1.00 35.30  ? 626 HOH B O   1 
HETATM 13788 O  O   . HOH Q 8 .   ? 6.035   -16.612 29.173  1.00 40.19  ? 627 HOH B O   1 
HETATM 13789 O  O   . HOH Q 8 .   ? 27.502  -6.684  38.690  1.00 25.48  ? 628 HOH B O   1 
HETATM 13790 O  O   . HOH Q 8 .   ? 34.601  6.539   46.064  1.00 31.49  ? 629 HOH B O   1 
HETATM 13791 O  O   . HOH Q 8 .   ? 8.653   15.669  33.270  1.00 26.18  ? 630 HOH B O   1 
HETATM 13792 O  O   . HOH Q 8 .   ? -0.879  7.414   41.976  1.00 39.80  ? 631 HOH B O   1 
HETATM 13793 O  O   . HOH Q 8 .   ? 3.253   10.909  53.183  1.00 36.64  ? 632 HOH B O   1 
HETATM 13794 O  O   . HOH Q 8 .   ? 26.010  -12.529 25.408  1.00 25.38  ? 633 HOH B O   1 
HETATM 13795 O  O   . HOH Q 8 .   ? 16.880  21.773  29.546  1.00 26.87  ? 634 HOH B O   1 
HETATM 13796 O  O   . HOH Q 8 .   ? 33.115  10.124  53.484  1.00 29.71  ? 635 HOH B O   1 
HETATM 13797 O  O   . HOH Q 8 .   ? 30.378  23.261  51.422  1.00 30.79  ? 636 HOH B O   1 
HETATM 13798 O  O   . HOH Q 8 .   ? 13.177  -6.263  19.288  1.00 27.99  ? 637 HOH B O   1 
HETATM 13799 O  O   . HOH Q 8 .   ? 13.537  -7.772  30.860  1.00 27.97  ? 638 HOH B O   1 
HETATM 13800 O  O   . HOH Q 8 .   ? 10.766  -22.057 31.852  1.00 32.39  ? 639 HOH B O   1 
HETATM 13801 O  O   . HOH Q 8 .   ? 2.136   3.492   41.186  1.00 39.76  ? 640 HOH B O   1 
HETATM 13802 O  O   . HOH Q 8 .   ? 24.134  -15.635 27.277  1.00 26.22  ? 641 HOH B O   1 
HETATM 13803 O  O   . HOH Q 8 .   ? -3.806  5.115   26.237  1.00 42.46  ? 642 HOH B O   1 
HETATM 13804 O  O   . HOH Q 8 .   ? 11.272  -8.374  46.395  1.00 34.48  ? 643 HOH B O   1 
HETATM 13805 O  O   . HOH Q 8 .   ? 21.822  -8.189  23.319  1.00 27.87  ? 644 HOH B O   1 
HETATM 13806 O  O   . HOH Q 8 .   ? 39.129  15.997  33.198  1.00 32.54  ? 645 HOH B O   1 
HETATM 13807 O  O   . HOH Q 8 .   ? 33.116  22.279  36.812  1.00 26.82  ? 646 HOH B O   1 
HETATM 13808 O  O   . HOH Q 8 .   ? -2.058  9.409   43.120  1.00 40.64  ? 647 HOH B O   1 
HETATM 13809 O  O   . HOH Q 8 .   ? 12.278  8.154   20.532  1.00 30.46  ? 648 HOH B O   1 
HETATM 13810 O  O   . HOH Q 8 .   ? 39.488  3.228   38.101  1.00 31.96  ? 649 HOH B O   1 
HETATM 13811 O  O   . HOH Q 8 .   ? 36.930  5.289   47.078  1.00 36.36  ? 650 HOH B O   1 
HETATM 13812 O  O   . HOH Q 8 .   ? 30.514  -1.134  46.563  1.00 35.44  ? 651 HOH B O   1 
HETATM 13813 O  O   . HOH Q 8 .   ? 31.940  20.699  34.974  1.00 25.76  ? 652 HOH B O   1 
HETATM 13814 O  O   . HOH Q 8 .   ? 1.980   12.534  51.631  1.00 37.39  ? 653 HOH B O   1 
HETATM 13815 O  O   . HOH Q 8 .   ? 26.820  8.720   55.556  1.00 40.22  ? 654 HOH B O   1 
HETATM 13816 O  O   . HOH Q 8 .   ? 31.282  -3.861  37.393  1.00 25.63  ? 655 HOH B O   1 
HETATM 13817 O  O   . HOH Q 8 .   ? 2.850   0.198   19.202  1.00 41.73  ? 656 HOH B O   1 
HETATM 13818 O  O   . HOH Q 8 .   ? 17.807  -21.855 27.239  1.00 32.23  ? 657 HOH B O   1 
HETATM 13819 O  O   . HOH Q 8 .   ? 28.952  -6.641  41.032  1.00 31.28  ? 658 HOH B O   1 
HETATM 13820 O  O   . HOH Q 8 .   ? 35.585  21.402  36.980  1.00 37.77  ? 659 HOH B O   1 
HETATM 13821 O  O   . HOH Q 8 .   ? 13.677  -13.551 61.796  1.00 35.84  ? 660 HOH B O   1 
HETATM 13822 O  O   . HOH Q 8 .   ? 30.550  21.796  32.718  1.00 24.62  ? 661 HOH B O   1 
HETATM 13823 O  O   . HOH R 8 .   ? 5.535   -37.966 20.884  1.00 42.96  ? 601 HOH C O   1 
HETATM 13824 O  O   . HOH R 8 .   ? 33.354  -35.305 24.060  1.00 33.08  ? 602 HOH C O   1 
HETATM 13825 O  O   . HOH R 8 .   ? 33.168  -36.733 21.106  1.00 32.88  ? 603 HOH C O   1 
HETATM 13826 O  O   . HOH R 8 .   ? 1.879   -65.412 18.015  1.00 40.10  ? 604 HOH C O   1 
HETATM 13827 O  O   . HOH R 8 .   ? 17.446  -55.612 20.335  1.00 39.40  ? 605 HOH C O   1 
HETATM 13828 O  O   . HOH R 8 .   ? 12.865  -53.334 18.458  1.00 40.88  ? 606 HOH C O   1 
HETATM 13829 O  O   . HOH R 8 .   ? 44.919  -67.730 10.772  1.00 35.60  ? 607 HOH C O   1 
HETATM 13830 O  O   . HOH R 8 .   ? 31.549  -27.960 15.919  1.00 32.26  ? 608 HOH C O   1 
HETATM 13831 O  O   . HOH R 8 .   ? 53.360  -47.658 19.258  1.00 40.09  ? 609 HOH C O   1 
HETATM 13832 O  O   . HOH R 8 .   ? 31.095  -40.306 22.280  1.00 26.47  ? 610 HOH C O   1 
HETATM 13833 O  O   . HOH R 8 .   ? 11.764  -48.890 42.561  1.00 38.89  ? 611 HOH C O   1 
HETATM 13834 O  O   . HOH R 8 .   ? 31.346  -52.331 43.865  1.00 40.57  ? 612 HOH C O   1 
HETATM 13835 O  O   . HOH R 8 .   ? 29.018  -61.703 43.451  1.00 35.28  ? 613 HOH C O   1 
HETATM 13836 O  O   . HOH R 8 .   ? 7.458   -64.912 46.883  1.00 40.35  ? 614 HOH C O   1 
HETATM 13837 O  O   . HOH R 8 .   ? 25.734  -32.532 24.181  1.00 25.33  ? 615 HOH C O   1 
HETATM 13838 O  O   . HOH R 8 .   ? 33.473  -29.951 21.771  1.00 33.80  ? 616 HOH C O   1 
HETATM 13839 O  O   . HOH R 8 .   ? 25.282  -69.062 10.767  1.00 41.39  ? 617 HOH C O   1 
HETATM 13840 O  O   . HOH R 8 .   ? 11.202  -46.660 44.111  1.00 44.89  ? 618 HOH C O   1 
HETATM 13841 O  O   . HOH R 8 .   ? 30.531  -59.051 14.270  1.00 23.31  ? 619 HOH C O   1 
HETATM 13842 O  O   . HOH R 8 .   ? 32.627  -57.176 25.652  1.00 25.35  ? 620 HOH C O   1 
HETATM 13843 O  O   . HOH R 8 .   ? 41.033  -32.917 24.960  1.00 35.95  ? 621 HOH C O   1 
HETATM 13844 O  O   . HOH R 8 .   ? 7.779   -59.150 39.327  1.00 31.28  ? 622 HOH C O   1 
HETATM 13845 O  O   . HOH R 8 .   ? 16.083  -56.199 14.864  1.00 28.29  ? 623 HOH C O   1 
HETATM 13846 O  O   . HOH R 8 .   ? 21.305  -59.768 17.160  1.00 30.24  ? 624 HOH C O   1 
HETATM 13847 O  O   . HOH R 8 .   ? 37.155  -37.227 10.027  1.00 29.11  ? 625 HOH C O   1 
HETATM 13848 O  O   . HOH R 8 .   ? 13.990  -71.171 32.623  1.00 36.92  ? 626 HOH C O   1 
HETATM 13849 O  O   . HOH R 8 .   ? 12.769  -48.530 39.560  1.00 43.44  ? 627 HOH C O   1 
HETATM 13850 O  O   . HOH R 8 .   ? 16.452  -56.089 47.324  1.00 33.95  ? 628 HOH C O   1 
HETATM 13851 O  O   . HOH R 8 .   ? 4.594   -67.386 31.958  1.00 38.25  ? 629 HOH C O   1 
HETATM 13852 O  O   . HOH R 8 .   ? 26.902  -58.055 24.258  1.00 31.93  ? 630 HOH C O   1 
HETATM 13853 O  O   . HOH R 8 .   ? 16.700  -73.389 25.934  1.00 38.61  ? 631 HOH C O   1 
HETATM 13854 O  O   . HOH R 8 .   ? 12.996  -46.208 37.215  1.00 49.38  ? 632 HOH C O   1 
HETATM 13855 O  O   . HOH R 8 .   ? 20.281  -70.073 16.092  1.00 35.89  ? 633 HOH C O   1 
HETATM 13856 O  O   . HOH R 8 .   ? 28.851  -23.506 25.528  1.00 29.54  ? 634 HOH C O   1 
HETATM 13857 O  O   . HOH R 8 .   ? 30.168  -64.440 35.319  1.00 27.45  ? 635 HOH C O   1 
HETATM 13858 O  O   . HOH R 8 .   ? 30.246  -56.620 25.501  1.00 26.06  ? 636 HOH C O   1 
HETATM 13859 O  O   . HOH R 8 .   ? 30.577  -47.509 7.930   1.00 23.25  ? 637 HOH C O   1 
HETATM 13860 O  O   . HOH R 8 .   ? 46.311  -62.368 14.465  1.00 31.19  ? 638 HOH C O   1 
HETATM 13861 O  O   . HOH R 8 .   ? 43.709  -51.486 10.859  1.00 26.46  ? 639 HOH C O   1 
HETATM 13862 O  O   . HOH R 8 .   ? 22.865  -47.873 46.984  1.00 29.73  ? 640 HOH C O   1 
HETATM 13863 O  O   . HOH R 8 .   ? 18.467  -33.547 13.392  1.00 25.19  ? 641 HOH C O   1 
HETATM 13864 O  O   . HOH R 8 .   ? 22.863  -41.456 37.554  1.00 32.54  ? 642 HOH C O   1 
HETATM 13865 O  O   . HOH R 8 .   ? 41.578  -68.894 15.738  1.00 34.27  ? 643 HOH C O   1 
HETATM 13866 O  O   . HOH R 8 .   ? 50.704  -52.477 18.186  1.00 28.89  ? 644 HOH C O   1 
HETATM 13867 O  O   . HOH R 8 .   ? 28.025  -42.225 27.761  1.00 21.60  ? 645 HOH C O   1 
HETATM 13868 O  O   . HOH R 8 .   ? 11.275  -64.757 10.038  1.00 30.21  ? 646 HOH C O   1 
HETATM 13869 O  O   . HOH R 8 .   ? 23.172  -48.418 6.210   1.00 26.89  ? 647 HOH C O   1 
HETATM 13870 O  O   . HOH R 8 .   ? 15.933  -23.125 22.441  1.00 28.77  ? 648 HOH C O   1 
HETATM 13871 O  O   . HOH R 8 .   ? 10.454  -53.456 22.214  1.00 32.48  ? 649 HOH C O   1 
HETATM 13872 O  O   . HOH R 8 .   ? 17.592  -26.695 27.118  1.00 34.16  ? 650 HOH C O   1 
HETATM 13873 O  O   . HOH R 8 .   ? 27.055  -33.980 22.020  1.00 27.43  ? 651 HOH C O   1 
HETATM 13874 O  O   . HOH R 8 .   ? 3.295   -51.240 14.324  1.00 35.38  ? 652 HOH C O   1 
HETATM 13875 O  O   . HOH R 8 .   ? 45.154  -37.791 35.755  1.00 30.38  ? 653 HOH C O   1 
HETATM 13876 O  O   . HOH R 8 .   ? 42.736  -44.599 11.920  1.00 32.75  ? 654 HOH C O   1 
HETATM 13877 O  O   . HOH R 8 .   ? 9.674   -69.673 22.560  1.00 34.28  ? 655 HOH C O   1 
HETATM 13878 O  O   . HOH R 8 .   ? 12.889  -37.912 24.025  1.00 35.06  ? 656 HOH C O   1 
HETATM 13879 O  O   . HOH R 8 .   ? 15.111  -31.604 14.001  1.00 34.48  ? 657 HOH C O   1 
HETATM 13880 O  O   . HOH R 8 .   ? 49.200  -65.861 28.121  1.00 38.08  ? 658 HOH C O   1 
HETATM 13881 O  O   . HOH R 8 .   ? 31.606  -29.590 30.617  1.00 29.49  ? 659 HOH C O   1 
HETATM 13882 O  O   . HOH R 8 .   ? 27.451  -64.333 23.731  1.00 24.11  ? 660 HOH C O   1 
HETATM 13883 O  O   . DOD R 8 .   ? 25.484  -47.939 17.964  1.00 26.05  ? 661 DOD C O   1 
HETATM 13884 O  O   . HOH R 8 .   ? 15.724  -25.387 18.472  1.00 26.98  ? 662 HOH C O   1 
HETATM 13885 O  O   . HOH R 8 .   ? 32.040  -28.171 20.668  1.00 28.81  ? 663 HOH C O   1 
HETATM 13886 O  O   . HOH R 8 .   ? 32.175  -65.407 11.145  1.00 28.68  ? 664 HOH C O   1 
HETATM 13887 O  O   A HOH R 8 .   ? 29.084  -73.607 30.942  0.50 25.17  ? 665 HOH C O   1 
HETATM 13888 O  O   B HOH R 8 .   ? 28.377  -75.222 29.461  0.50 32.09  ? 665 HOH C O   1 
HETATM 13889 O  O   . HOH R 8 .   ? 21.553  -43.517 10.754  1.00 24.65  ? 666 HOH C O   1 
HETATM 13890 O  O   . HOH R 8 .   ? 32.887  -69.989 8.107   1.00 26.03  ? 667 HOH C O   1 
HETATM 13891 O  O   . HOH R 8 .   ? 15.734  -46.596 35.123  1.00 41.46  ? 668 HOH C O   1 
HETATM 13892 O  O   . HOH R 8 .   ? 22.761  -45.898 36.589  1.00 28.65  ? 669 HOH C O   1 
HETATM 13893 O  O   . HOH R 8 .   ? 33.876  -46.983 27.559  1.00 22.94  ? 670 HOH C O   1 
HETATM 13894 O  O   . HOH R 8 .   ? 14.252  -52.811 25.726  1.00 35.69  ? 671 HOH C O   1 
HETATM 13895 O  O   . HOH R 8 .   ? 14.317  -58.910 22.677  1.00 30.49  ? 672 HOH C O   1 
HETATM 13896 O  O   . HOH R 8 .   ? 3.664   -50.618 11.974  1.00 41.47  ? 673 HOH C O   1 
HETATM 13897 O  O   . HOH R 8 .   ? 20.512  -25.960 23.801  1.00 25.15  ? 674 HOH C O   1 
HETATM 13898 O  O   . HOH R 8 .   ? 40.368  -52.131 34.470  1.00 31.84  ? 675 HOH C O   1 
HETATM 13899 O  O   . HOH R 8 .   ? 13.608  -65.355 11.247  1.00 31.78  ? 676 HOH C O   1 
HETATM 13900 O  O   . HOH R 8 .   ? 23.736  -42.837 30.736  1.00 28.90  ? 677 HOH C O   1 
HETATM 13901 O  O   . HOH R 8 .   ? 12.869  -30.991 28.551  1.00 36.31  ? 678 HOH C O   1 
HETATM 13902 O  O   . HOH R 8 .   ? 41.432  -51.103 12.231  1.00 26.99  ? 679 HOH C O   1 
HETATM 13903 O  O   . HOH R 8 .   ? 44.865  -64.352 8.364   1.00 26.58  ? 680 HOH C O   1 
HETATM 13904 O  O   . HOH R 8 .   ? 38.002  -66.513 6.631   1.00 28.63  ? 681 HOH C O   1 
HETATM 13905 O  O   . HOH R 8 .   ? 13.918  -43.418 10.078  1.00 29.42  ? 682 HOH C O   1 
HETATM 13906 O  O   . HOH R 8 .   ? 17.046  -43.189 12.027  1.00 25.84  ? 683 HOH C O   1 
HETATM 13907 O  O   . HOH R 8 .   ? 15.448  -70.651 19.784  1.00 33.55  ? 684 HOH C O   1 
HETATM 13908 O  O   . HOH R 8 .   ? 31.740  -58.509 37.462  1.00 33.39  ? 685 HOH C O   1 
HETATM 13909 O  O   . HOH R 8 .   ? 28.469  -44.818 17.937  1.00 23.24  ? 686 HOH C O   1 
HETATM 13910 O  O   . HOH R 8 .   ? 37.198  -29.165 26.423  1.00 36.59  ? 687 HOH C O   1 
HETATM 13911 O  O   . HOH R 8 .   ? 52.878  -58.891 27.138  1.00 31.05  ? 688 HOH C O   1 
HETATM 13912 O  O   . HOH R 8 .   ? 37.501  -65.046 24.558  1.00 25.81  ? 689 HOH C O   1 
HETATM 13913 O  O   . HOH R 8 .   ? 17.055  -68.153 37.062  1.00 39.18  ? 690 HOH C O   1 
HETATM 13914 O  O   . HOH R 8 .   ? 13.359  -68.508 14.528  1.00 35.82  ? 691 HOH C O   1 
HETATM 13915 O  O   . HOH R 8 .   ? 34.790  -68.330 27.514  1.00 28.08  ? 692 HOH C O   1 
HETATM 13916 O  O   . HOH R 8 .   ? 11.709  -37.041 13.426  1.00 32.80  ? 693 HOH C O   1 
HETATM 13917 O  O   . HOH R 8 .   ? 36.108  -46.804 29.411  1.00 27.04  ? 694 HOH C O   1 
HETATM 13918 O  O   . HOH R 8 .   ? 7.882   -68.319 21.423  1.00 35.88  ? 695 HOH C O   1 
HETATM 13919 O  O   . HOH R 8 .   ? 25.331  -56.938 47.591  1.00 34.45  ? 696 HOH C O   1 
HETATM 13920 O  O   . HOH R 8 .   ? 40.815  -36.893 12.065  1.00 35.44  ? 697 HOH C O   1 
HETATM 13921 O  O   . HOH R 8 .   ? 22.569  -66.514 36.686  1.00 31.83  ? 698 HOH C O   1 
HETATM 13922 O  O   . HOH R 8 .   ? 43.333  -49.080 33.159  1.00 26.76  ? 699 HOH C O   1 
HETATM 13923 O  O   . HOH R 8 .   ? 31.746  -53.979 9.964   1.00 23.20  ? 700 HOH C O   1 
HETATM 13924 O  O   . HOH R 8 .   ? 52.467  -45.652 18.144  1.00 34.14  ? 701 HOH C O   1 
HETATM 13925 O  O   . HOH R 8 .   ? 13.967  -41.053 11.795  1.00 35.47  ? 702 HOH C O   1 
HETATM 13926 O  O   . HOH R 8 .   ? 9.086   -69.419 14.175  1.00 39.70  ? 703 HOH C O   1 
HETATM 13927 O  O   . HOH R 8 .   ? 14.537  -21.976 24.417  1.00 35.80  ? 704 HOH C O   1 
HETATM 13928 O  O   . HOH R 8 .   ? 19.893  -26.321 28.078  1.00 35.31  ? 705 HOH C O   1 
HETATM 13929 O  O   . HOH R 8 .   ? 46.977  -61.099 19.175  1.00 24.54  ? 706 HOH C O   1 
HETATM 13930 O  O   . HOH R 8 .   ? 29.894  -38.149 8.632   1.00 27.61  ? 707 HOH C O   1 
HETATM 13931 O  O   . HOH R 8 .   ? 32.050  -62.237 36.050  1.00 27.73  ? 708 HOH C O   1 
HETATM 13932 O  O   . HOH R 8 .   ? 32.052  -53.944 22.654  1.00 23.13  ? 709 HOH C O   1 
HETATM 13933 O  O   . HOH R 8 .   ? 10.047  -30.432 14.265  1.00 36.02  ? 710 HOH C O   1 
HETATM 13934 O  O   . HOH R 8 .   ? 43.190  -51.604 33.924  1.00 27.12  ? 711 HOH C O   1 
HETATM 13935 O  O   . HOH R 8 .   ? 31.966  -44.150 37.725  1.00 31.68  ? 712 HOH C O   1 
HETATM 13936 O  O   . HOH R 8 .   ? 36.750  -50.522 19.212  1.00 23.60  ? 713 HOH C O   1 
HETATM 13937 O  O   . HOH R 8 .   ? 18.430  -55.598 17.733  1.00 34.40  ? 714 HOH C O   1 
HETATM 13938 O  O   . HOH R 8 .   ? 31.667  -50.343 42.078  1.00 31.17  ? 715 HOH C O   1 
HETATM 13939 O  O   . HOH R 8 .   ? 51.004  -54.797 19.760  1.00 25.10  ? 716 HOH C O   1 
HETATM 13940 O  O   . HOH R 8 .   ? 38.425  -49.030 31.834  1.00 29.89  ? 717 HOH C O   1 
HETATM 13941 O  O   . HOH R 8 .   ? 13.121  -36.602 21.665  1.00 32.04  ? 718 HOH C O   1 
HETATM 13942 O  O   . HOH R 8 .   ? 17.598  -78.751 30.791  1.00 34.08  ? 719 HOH C O   1 
HETATM 13943 O  O   . HOH R 8 .   ? 35.344  -45.467 33.886  1.00 36.89  ? 720 HOH C O   1 
HETATM 13944 O  O   . HOH R 8 .   ? 31.643  -49.515 28.055  1.00 24.25  ? 721 HOH C O   1 
HETATM 13945 O  O   . HOH R 8 .   ? 33.401  -60.931 38.572  1.00 36.51  ? 722 HOH C O   1 
HETATM 13946 O  O   . HOH R 8 .   ? 42.759  -62.369 7.960   1.00 25.99  ? 723 HOH C O   1 
HETATM 13947 O  O   . HOH R 8 .   ? 28.201  -67.836 34.688  1.00 31.88  ? 724 HOH C O   1 
HETATM 13948 O  O   . HOH R 8 .   ? 25.906  -53.011 33.401  1.00 29.57  ? 725 HOH C O   1 
HETATM 13949 O  O   . HOH R 8 .   ? 12.094  -66.021 43.908  1.00 33.86  ? 726 HOH C O   1 
HETATM 13950 O  O   . HOH R 8 .   ? 17.014  -59.135 13.352  1.00 30.30  ? 727 HOH C O   1 
HETATM 13951 O  O   . HOH R 8 .   ? 12.117  -63.508 42.818  1.00 33.73  ? 728 HOH C O   1 
HETATM 13952 O  O   . HOH R 8 .   ? 18.571  -23.654 25.584  1.00 30.79  ? 729 HOH C O   1 
HETATM 13953 O  O   A HOH R 8 .   ? 16.326  -42.944 24.464  0.49 24.36  ? 730 HOH C O   1 
HETATM 13954 O  O   B HOH R 8 .   ? 15.101  -44.366 25.789  0.51 31.56  ? 730 HOH C O   1 
HETATM 13955 O  O   . HOH R 8 .   ? 12.967  -40.613 24.046  1.00 34.43  ? 731 HOH C O   1 
HETATM 13956 O  O   . HOH R 8 .   ? 47.768  -47.619 13.986  1.00 35.97  ? 732 HOH C O   1 
HETATM 13957 O  O   . HOH R 8 .   ? 4.491   -67.554 25.210  1.00 36.23  ? 733 HOH C O   1 
HETATM 13958 O  O   . HOH R 8 .   ? 39.850  -50.088 36.177  1.00 33.18  ? 734 HOH C O   1 
HETATM 13959 O  O   . HOH R 8 .   ? 12.744  -33.947 21.791  1.00 34.13  ? 735 HOH C O   1 
HETATM 13960 O  O   . HOH R 8 .   ? 30.290  -61.466 15.383  1.00 26.90  ? 736 HOH C O   1 
HETATM 13961 O  O   . HOH R 8 .   ? 28.981  -54.666 9.463   1.00 23.37  ? 737 HOH C O   1 
HETATM 13962 O  O   . HOH R 8 .   ? 24.280  -67.486 34.497  1.00 32.23  ? 738 HOH C O   1 
HETATM 13963 O  O   . HOH R 8 .   ? 16.875  -26.769 12.432  1.00 26.35  ? 739 HOH C O   1 
HETATM 13964 O  O   . HOH R 8 .   ? 6.690   -43.385 13.778  1.00 37.50  ? 740 HOH C O   1 
HETATM 13965 O  O   . HOH R 8 .   ? 19.597  -46.752 47.106  1.00 39.13  ? 741 HOH C O   1 
HETATM 13966 O  O   . HOH R 8 .   ? 38.777  -31.144 32.359  1.00 31.72  ? 742 HOH C O   1 
HETATM 13967 O  O   . HOH R 8 .   ? 17.950  -33.553 10.794  1.00 31.08  ? 743 HOH C O   1 
HETATM 13968 O  O   . HOH R 8 .   ? 15.812  -40.727 13.495  1.00 23.90  ? 744 HOH C O   1 
HETATM 13969 O  O   . HOH R 8 .   ? 22.111  -35.973 5.368   1.00 23.57  ? 745 HOH C O   1 
HETATM 13970 O  O   . HOH R 8 .   ? 34.334  -40.985 31.973  1.00 23.33  ? 746 HOH C O   1 
HETATM 13971 O  O   . HOH R 8 .   ? 26.423  -66.566 15.647  1.00 24.71  ? 747 HOH C O   1 
HETATM 13972 O  O   . HOH R 8 .   ? 34.350  -27.253 23.907  1.00 35.07  ? 748 HOH C O   1 
HETATM 13973 O  O   . HOH R 8 .   ? 42.385  -68.400 18.852  1.00 38.54  ? 749 HOH C O   1 
HETATM 13974 O  O   . HOH R 8 .   ? 12.874  -38.334 11.255  1.00 33.12  ? 750 HOH C O   1 
HETATM 13975 O  O   . HOH R 8 .   ? 26.136  -64.671 20.011  1.00 29.02  ? 751 HOH C O   1 
HETATM 13976 O  O   . HOH R 8 .   ? 19.476  -69.269 12.808  1.00 35.42  ? 752 HOH C O   1 
HETATM 13977 O  O   . HOH R 8 .   ? 24.666  -54.221 30.212  1.00 26.29  ? 753 HOH C O   1 
HETATM 13978 O  O   . HOH R 8 .   ? 23.607  -55.577 28.207  1.00 23.01  ? 754 HOH C O   1 
HETATM 13979 O  O   . HOH R 8 .   ? 15.645  -34.233 6.552   1.00 34.48  ? 755 HOH C O   1 
HETATM 13980 O  O   . HOH R 8 .   ? 52.455  -60.759 23.591  1.00 37.68  ? 756 HOH C O   1 
HETATM 13981 O  O   . HOH R 8 .   ? 32.681  -25.634 30.769  1.00 33.65  ? 757 HOH C O   1 
HETATM 13982 O  O   . HOH R 8 .   ? 52.826  -39.362 20.250  1.00 36.27  ? 758 HOH C O   1 
HETATM 13983 O  O   . HOH R 8 .   ? 41.437  -34.928 36.355  1.00 32.38  ? 759 HOH C O   1 
HETATM 13984 O  O   . HOH R 8 .   ? 28.055  -71.336 24.194  1.00 35.51  ? 760 HOH C O   1 
HETATM 13985 O  O   . HOH R 8 .   ? 32.344  -56.501 44.414  1.00 35.01  ? 761 HOH C O   1 
HETATM 13986 O  O   . HOH R 8 .   ? 20.585  -68.023 22.253  1.00 27.86  ? 762 HOH C O   1 
HETATM 13987 O  O   . HOH R 8 .   ? 7.814   -53.881 33.942  1.00 38.22  ? 763 HOH C O   1 
HETATM 13988 O  O   . HOH R 8 .   ? 20.412  -37.909 32.648  1.00 46.65  ? 764 HOH C O   1 
HETATM 13989 O  O   . HOH R 8 .   ? 19.174  -44.874 11.741  1.00 27.14  ? 765 HOH C O   1 
HETATM 13990 O  O   . HOH R 8 .   ? 6.886   -57.119 50.767  1.00 44.41  ? 766 HOH C O   1 
HETATM 13991 O  O   . HOH R 8 .   ? 9.949   -35.353 12.258  1.00 34.99  ? 767 HOH C O   1 
HETATM 13992 O  O   . HOH R 8 .   ? 33.319  -68.099 35.002  1.00 31.17  ? 768 HOH C O   1 
HETATM 13993 O  O   . HOH R 8 .   ? 9.601   -52.654 33.107  1.00 42.83  ? 769 HOH C O   1 
HETATM 13994 O  O   . HOH R 8 .   ? 16.387  -28.330 28.648  1.00 36.82  ? 770 HOH C O   1 
HETATM 13995 O  O   . HOH R 8 .   ? 33.054  -48.625 25.382  1.00 28.17  ? 771 HOH C O   1 
HETATM 13996 O  O   . HOH R 8 .   ? 38.954  -46.673 28.199  1.00 33.62  ? 772 HOH C O   1 
HETATM 13997 O  O   . HOH R 8 .   ? 45.823  -48.969 10.914  1.00 41.25  ? 773 HOH C O   1 
HETATM 13998 O  O   . HOH R 8 .   ? 43.487  -40.198 12.715  1.00 30.14  ? 774 HOH C O   1 
HETATM 13999 O  O   . HOH R 8 .   ? 8.408   -41.095 30.793  1.00 48.92  ? 775 HOH C O   1 
HETATM 14000 O  O   . HOH R 8 .   ? 39.590  -46.600 30.943  1.00 33.67  ? 776 HOH C O   1 
HETATM 14001 O  O   . HOH R 8 .   ? 36.383  -44.609 31.081  1.00 28.75  ? 777 HOH C O   1 
HETATM 14002 O  O   . HOH R 8 .   ? 3.279   -38.438 21.582  1.00 51.91  ? 778 HOH C O   1 
HETATM 14003 O  O   . HOH R 8 .   ? 28.195  -51.574 8.023   1.00 24.09  ? 779 HOH C O   1 
HETATM 14004 O  O   . HOH R 8 .   ? 18.822  -66.232 23.615  1.00 28.57  ? 780 HOH C O   1 
HETATM 14005 O  O   . HOH R 8 .   ? 2.714   -58.267 15.607  1.00 40.85  ? 781 HOH C O   1 
HETATM 14006 O  O   . HOH R 8 .   ? 20.614  -68.058 17.736  1.00 30.76  ? 782 HOH C O   1 
HETATM 14007 O  O   . HOH R 8 .   ? 46.352  -62.963 17.326  1.00 26.38  ? 783 HOH C O   1 
HETATM 14008 O  O   . HOH R 8 .   ? 40.816  -69.328 8.252   1.00 27.07  ? 784 HOH C O   1 
HETATM 14009 O  O   . HOH R 8 .   ? 37.671  -48.406 38.167  1.00 29.90  ? 785 HOH C O   1 
HETATM 14010 O  O   . HOH R 8 .   ? 2.295   -47.947 15.782  1.00 41.24  ? 786 HOH C O   1 
HETATM 14011 O  O   . HOH R 8 .   ? 53.231  -53.956 32.202  1.00 33.81  ? 787 HOH C O   1 
HETATM 14012 O  O   . HOH R 8 .   ? 48.019  -62.829 11.450  1.00 35.99  ? 788 HOH C O   1 
HETATM 14013 O  O   . HOH R 8 .   ? 9.685   -70.094 38.189  1.00 37.99  ? 789 HOH C O   1 
HETATM 14014 O  O   . HOH R 8 .   ? 53.633  -42.769 29.256  1.00 29.99  ? 790 HOH C O   1 
HETATM 14015 O  O   . HOH R 8 .   ? 9.391   -40.127 23.989  1.00 44.86  ? 791 HOH C O   1 
HETATM 14016 O  O   . HOH R 8 .   ? 39.768  -71.397 9.939   1.00 36.32  ? 792 HOH C O   1 
HETATM 14017 O  O   . HOH R 8 .   ? 18.894  -67.473 44.862  1.00 43.65  ? 793 HOH C O   1 
HETATM 14018 O  O   . HOH R 8 .   ? 47.232  -41.659 16.428  1.00 31.48  ? 794 HOH C O   1 
HETATM 14019 O  O   . HOH R 8 .   ? 11.199  -42.567 9.560   1.00 42.89  ? 795 HOH C O   1 
HETATM 14020 O  O   . HOH R 8 .   ? 14.142  -24.328 20.372  1.00 35.18  ? 796 HOH C O   1 
HETATM 14021 O  O   . HOH R 8 .   ? 24.047  -70.315 17.354  1.00 39.90  ? 797 HOH C O   1 
HETATM 14022 O  O   . HOH R 8 .   ? 9.540   -66.960 9.911   1.00 37.20  ? 798 HOH C O   1 
HETATM 14023 O  O   . HOH R 8 .   ? 42.526  -37.453 36.053  1.00 32.88  ? 799 HOH C O   1 
HETATM 14024 O  O   . HOH R 8 .   ? 20.495  -68.069 36.770  1.00 39.59  ? 800 HOH C O   1 
HETATM 14025 O  O   . HOH R 8 .   ? 19.381  -69.005 19.973  1.00 31.11  ? 801 HOH C O   1 
HETATM 14026 O  O   . HOH R 8 .   ? 37.612  -67.269 26.269  1.00 31.23  ? 802 HOH C O   1 
HETATM 14027 O  O   . HOH R 8 .   ? 23.092  -67.918 21.438  1.00 39.39  ? 803 HOH C O   1 
HETATM 14028 O  O   . HOH R 8 .   ? 43.574  -68.839 8.422   1.00 35.91  ? 804 HOH C O   1 
HETATM 14029 O  O   . HOH R 8 .   ? 35.189  -62.799 39.185  1.00 42.96  ? 805 HOH C O   1 
HETATM 14030 O  O   . HOH R 8 .   ? 46.914  -62.824 8.986   1.00 39.97  ? 806 HOH C O   1 
HETATM 14031 O  O   . HOH R 8 .   ? 25.386  -66.034 22.287  1.00 32.68  ? 807 HOH C O   1 
HETATM 14032 O  O   . HOH R 8 .   ? 34.983  -42.759 34.107  1.00 33.35  ? 808 HOH C O   1 
HETATM 14033 O  O   . HOH R 8 .   ? 12.329  -37.473 8.730   1.00 38.68  ? 809 HOH C O   1 
HETATM 14034 O  O   . HOH R 8 .   ? 18.038  -71.325 20.143  1.00 38.48  ? 810 HOH C O   1 
HETATM 14035 O  O   . HOH R 8 .   ? 39.149  -68.915 5.891   1.00 26.00  ? 811 HOH C O   1 
HETATM 14036 O  O   . HOH R 8 .   ? 34.444  -69.571 5.792   1.00 22.28  ? 812 HOH C O   1 
HETATM 14037 O  O   . HOH R 8 .   ? 11.062  -72.221 21.284  1.00 38.82  ? 813 HOH C O   1 
HETATM 14038 O  O   . HOH R 8 .   ? 31.367  -66.566 36.228  1.00 32.74  ? 814 HOH C O   1 
HETATM 14039 O  O   . HOH R 8 .   ? 25.731  -66.749 18.227  1.00 28.73  ? 815 HOH C O   1 
HETATM 14040 O  O   . HOH R 8 .   ? 13.385  -68.088 11.795  1.00 37.50  ? 816 HOH C O   1 
HETATM 14041 O  O   . HOH R 8 .   ? 23.171  -68.142 18.495  1.00 32.85  ? 817 HOH C O   1 
HETATM 14042 O  O   . HOH R 8 .   ? 37.050  -70.863 5.844   1.00 28.79  ? 818 HOH C O   1 
HETATM 14043 O  O   . HOH R 8 .   ? 37.536  -72.415 8.121   1.00 37.89  ? 819 HOH C O   1 
HETATM 14044 O  O   . HOH S 8 .   ? 16.153  -50.595 -8.836  1.00 37.85  ? 501 HOH D O   1 
HETATM 14045 O  O   . HOH S 8 .   ? 15.238  -39.721 3.666   1.00 34.61  ? 502 HOH D O   1 
HETATM 14046 O  O   . HOH S 8 .   ? 44.488  -70.452 -6.092  1.00 39.25  ? 503 HOH D O   1 
HETATM 14047 O  O   . HOH S 8 .   ? 44.999  -55.921 -15.050 1.00 35.81  ? 504 HOH D O   1 
HETATM 14048 O  O   . HOH S 8 .   ? 35.720  -60.985 -23.679 1.00 38.33  ? 505 HOH D O   1 
HETATM 14049 O  O   . HOH S 8 .   ? 20.777  -36.300 2.947   1.00 31.40  ? 506 HOH D O   1 
HETATM 14050 O  O   . HOH S 8 .   ? 19.272  -55.352 -4.853  1.00 35.99  ? 507 HOH D O   1 
HETATM 14051 O  O   . HOH S 8 .   ? 39.582  -33.643 -3.567  1.00 34.01  ? 508 HOH D O   1 
HETATM 14052 O  O   . HOH S 8 .   ? 32.388  -56.756 -10.928 1.00 29.72  ? 509 HOH D O   1 
HETATM 14053 O  O   . HOH S 8 .   ? 26.647  -45.207 -16.708 1.00 35.14  ? 510 HOH D O   1 
HETATM 14054 O  O   . HOH S 8 .   ? 40.660  -75.439 -6.048  1.00 34.78  ? 511 HOH D O   1 
HETATM 14055 O  O   . HOH S 8 .   ? 37.640  -38.466 7.908   1.00 37.07  ? 512 HOH D O   1 
HETATM 14056 O  O   . HOH S 8 .   ? 18.058  -42.989 7.487   1.00 22.04  ? 513 HOH D O   1 
HETATM 14057 O  O   . HOH S 8 .   ? 27.976  -27.972 -22.960 1.00 40.96  ? 514 HOH D O   1 
HETATM 14058 O  O   . HOH S 8 .   ? 13.185  -57.400 8.449   1.00 34.07  ? 515 HOH D O   1 
HETATM 14059 O  O   . HOH S 8 .   ? 45.966  -51.053 -6.134  1.00 44.29  ? 516 HOH D O   1 
HETATM 14060 O  O   . HOH S 8 .   ? 36.178  -50.580 -2.211  1.00 23.30  ? 517 HOH D O   1 
HETATM 14061 O  O   . HOH S 8 .   ? 31.284  -81.386 -3.927  1.00 38.87  ? 518 HOH D O   1 
HETATM 14062 O  O   . HOH S 8 .   ? 15.210  -67.822 -7.334  1.00 28.69  ? 519 HOH D O   1 
HETATM 14063 O  O   . HOH S 8 .   ? 43.929  -69.547 1.704   1.00 34.71  ? 520 HOH D O   1 
HETATM 14064 O  O   . HOH S 8 .   ? 33.530  -31.125 2.697   1.00 36.23  ? 521 HOH D O   1 
HETATM 14065 O  O   . HOH S 8 .   ? 51.446  -63.027 -4.929  1.00 31.07  ? 522 HOH D O   1 
HETATM 14066 O  O   . HOH S 8 .   ? 19.296  -38.955 -23.311 1.00 42.62  ? 523 HOH D O   1 
HETATM 14067 O  O   . HOH S 8 .   ? 8.450   -52.245 -7.501  1.00 41.22  ? 524 HOH D O   1 
HETATM 14068 O  O   . HOH S 8 .   ? 13.759  -69.763 0.252   1.00 34.77  ? 525 HOH D O   1 
HETATM 14069 O  O   . HOH S 8 .   ? 32.295  -53.553 -8.249  1.00 22.75  ? 526 HOH D O   1 
HETATM 14070 O  O   . HOH S 8 .   ? 37.113  -43.570 -18.683 1.00 34.45  ? 527 HOH D O   1 
HETATM 14071 O  O   . HOH S 8 .   ? 5.921   -59.543 9.686   1.00 39.40  ? 528 HOH D O   1 
HETATM 14072 O  O   . HOH S 8 .   ? 15.033  -56.348 -11.505 1.00 39.37  ? 529 HOH D O   1 
HETATM 14073 O  O   . HOH S 8 .   ? 42.347  -75.760 -8.169  1.00 36.02  ? 530 HOH D O   1 
HETATM 14074 O  O   . HOH S 8 .   ? 33.007  -41.105 2.490   1.00 28.37  ? 531 HOH D O   1 
HETATM 14075 O  O   . HOH S 8 .   ? 20.725  -42.728 -4.759  1.00 32.14  ? 532 HOH D O   1 
HETATM 14076 O  O   . HOH S 8 .   ? 30.204  -29.710 -23.618 1.00 34.90  ? 533 HOH D O   1 
HETATM 14077 O  O   . HOH S 8 .   ? 32.556  -38.174 -27.744 1.00 33.61  ? 534 HOH D O   1 
HETATM 14078 O  O   . HOH S 8 .   ? 39.357  -48.629 -2.198  1.00 34.40  ? 535 HOH D O   1 
HETATM 14079 O  O   . HOH S 8 .   ? 45.116  -59.467 -12.509 1.00 27.80  ? 536 HOH D O   1 
HETATM 14080 O  O   . HOH S 8 .   ? 44.894  -63.846 -13.792 1.00 35.55  ? 537 HOH D O   1 
HETATM 14081 O  O   . HOH S 8 .   ? 33.636  -65.887 2.212   1.00 22.83  ? 538 HOH D O   1 
HETATM 14082 O  O   . HOH S 8 .   ? 50.639  -57.548 -8.153  1.00 32.88  ? 539 HOH D O   1 
HETATM 14083 O  O   . HOH S 8 .   ? 41.546  -75.510 -15.645 1.00 35.04  ? 540 HOH D O   1 
HETATM 14084 O  O   . HOH S 8 .   ? 15.380  -71.496 -19.223 1.00 40.16  ? 541 HOH D O   1 
HETATM 14085 O  O   . HOH S 8 .   ? 33.228  -54.589 -12.565 1.00 25.77  ? 542 HOH D O   1 
HETATM 14086 O  O   . HOH S 8 .   ? 37.813  -78.407 -13.117 1.00 38.00  ? 543 HOH D O   1 
HETATM 14087 O  O   . HOH S 8 .   ? 30.586  -57.145 -8.727  1.00 27.51  ? 544 HOH D O   1 
HETATM 14088 O  O   . HOH S 8 .   ? 37.912  -48.093 4.639   1.00 22.71  ? 545 HOH D O   1 
HETATM 14089 O  O   . HOH S 8 .   ? 37.746  -46.286 1.621   1.00 21.02  ? 546 HOH D O   1 
HETATM 14090 O  O   . HOH S 8 .   ? 41.147  -59.077 -20.215 1.00 34.92  ? 547 HOH D O   1 
HETATM 14091 O  O   . HOH S 8 .   ? 25.822  -35.381 -27.076 1.00 41.65  ? 548 HOH D O   1 
HETATM 14092 O  O   . HOH S 8 .   ? 40.302  -48.023 -7.846  1.00 35.75  ? 549 HOH D O   1 
HETATM 14093 O  O   . HOH S 8 .   ? 34.490  -72.303 2.272   1.00 25.89  ? 550 HOH D O   1 
HETATM 14094 O  O   . HOH S 8 .   ? 34.423  -58.581 -3.047  1.00 32.85  ? 551 HOH D O   1 
HETATM 14095 O  O   . HOH S 8 .   ? 28.316  -61.844 -3.249  1.00 25.45  ? 552 HOH D O   1 
HETATM 14096 O  O   . HOH S 8 .   ? 25.409  -55.345 2.436   1.00 25.40  ? 553 HOH D O   1 
HETATM 14097 O  O   . HOH S 8 .   ? 30.239  -51.270 -35.136 1.00 33.63  ? 554 HOH D O   1 
HETATM 14098 O  O   . HOH S 8 .   ? 12.984  -54.632 8.824   1.00 31.90  ? 555 HOH D O   1 
HETATM 14099 O  O   . HOH S 8 .   ? 45.998  -53.966 -3.471  1.00 33.79  ? 556 HOH D O   1 
HETATM 14100 O  O   . HOH S 8 .   ? 19.765  -61.475 -17.149 1.00 28.16  ? 557 HOH D O   1 
HETATM 14101 O  O   . HOH S 8 .   ? 32.690  -75.344 -10.557 1.00 33.56  ? 558 HOH D O   1 
HETATM 14102 O  O   . HOH S 8 .   ? 46.296  -57.218 4.334   1.00 23.84  ? 559 HOH D O   1 
HETATM 14103 O  O   . HOH S 8 .   ? 20.077  -65.153 -23.873 1.00 40.46  ? 560 HOH D O   1 
HETATM 14104 O  O   . HOH S 8 .   ? 10.772  -67.442 -7.429  1.00 36.65  ? 561 HOH D O   1 
HETATM 14105 O  O   . HOH S 8 .   ? 44.693  -54.164 3.355   1.00 24.35  ? 562 HOH D O   1 
HETATM 14106 O  O   . HOH S 8 .   ? 9.214   -66.046 -5.169  1.00 33.31  ? 563 HOH D O   1 
HETATM 14107 O  O   . HOH S 8 .   ? 15.823  -26.548 -8.309  1.00 41.39  ? 564 HOH D O   1 
HETATM 14108 O  O   . HOH S 8 .   ? 37.138  -61.607 7.129   1.00 26.58  ? 565 HOH D O   1 
HETATM 14109 O  O   . HOH S 8 .   ? 25.169  -79.306 -4.688  1.00 35.22  ? 566 HOH D O   1 
HETATM 14110 O  O   . HOH S 8 .   ? 32.190  -36.652 8.070   1.00 28.18  ? 567 HOH D O   1 
HETATM 14111 O  O   . HOH S 8 .   ? 27.630  -38.645 -21.466 1.00 31.13  ? 568 HOH D O   1 
HETATM 14112 O  O   . HOH S 8 .   ? 45.580  -62.242 -11.903 1.00 36.90  ? 569 HOH D O   1 
HETATM 14113 O  O   . HOH S 8 .   ? 32.339  -44.039 -8.617  1.00 26.00  ? 570 HOH D O   1 
HETATM 14114 O  O   . HOH S 8 .   ? 15.459  -44.593 8.354   1.00 29.36  ? 571 HOH D O   1 
HETATM 14115 O  O   . HOH S 8 .   ? 31.768  -43.283 -4.455  1.00 27.16  ? 572 HOH D O   1 
HETATM 14116 O  O   . HOH S 8 .   ? 35.627  -67.149 5.170   1.00 28.28  ? 573 HOH D O   1 
HETATM 14117 O  O   . HOH S 8 .   ? 30.704  -34.380 8.086   1.00 27.79  ? 574 HOH D O   1 
HETATM 14118 O  O   . HOH S 8 .   ? 26.903  -61.041 -15.727 1.00 36.57  ? 575 HOH D O   1 
HETATM 14119 O  O   . HOH S 8 .   ? 8.199   -52.825 3.201   1.00 34.05  ? 576 HOH D O   1 
HETATM 14120 O  O   . HOH S 8 .   ? 23.618  -41.452 -14.617 1.00 29.10  ? 577 HOH D O   1 
HETATM 14121 O  O   . HOH S 8 .   ? 39.970  -68.975 3.275   1.00 22.96  ? 578 HOH D O   1 
HETATM 14122 O  O   . HOH S 8 .   ? 38.758  -50.062 -15.762 1.00 30.64  ? 579 HOH D O   1 
HETATM 14123 O  O   . HOH S 8 .   ? 20.403  -29.788 0.654   1.00 43.53  ? 580 HOH D O   1 
HETATM 14124 O  O   . HOH S 8 .   ? 18.347  -60.928 -14.783 1.00 28.75  ? 581 HOH D O   1 
HETATM 14125 O  O   . HOH S 8 .   ? 36.131  -48.344 -36.609 1.00 45.81  ? 582 HOH D O   1 
HETATM 14126 O  O   . HOH S 8 .   ? 43.472  -53.952 -7.306  1.00 24.13  ? 583 HOH D O   1 
HETATM 14127 O  O   . HOH S 8 .   ? 42.684  -51.993 -9.138  1.00 27.09  ? 584 HOH D O   1 
HETATM 14128 O  O   . HOH S 8 .   ? 32.832  -70.414 3.790   1.00 27.03  ? 585 HOH D O   1 
HETATM 14129 O  O   . HOH S 8 .   ? 4.764   -54.803 -7.885  1.00 44.06  ? 586 HOH D O   1 
HETATM 14130 O  O   . HOH S 8 .   ? 20.057  -40.971 -25.119 1.00 37.23  ? 587 HOH D O   1 
HETATM 14131 O  O   . HOH S 8 .   ? 25.654  -39.858 -2.457  1.00 25.44  ? 588 HOH D O   1 
HETATM 14132 O  O   . HOH S 8 .   ? 36.918  -43.983 -2.973  1.00 25.52  ? 589 HOH D O   1 
HETATM 14133 O  O   . HOH S 8 .   ? 22.575  -52.109 -30.824 1.00 39.32  ? 590 HOH D O   1 
HETATM 14134 O  O   . HOH S 8 .   ? 38.221  -41.602 -16.891 1.00 33.95  ? 591 HOH D O   1 
HETATM 14135 O  O   . HOH S 8 .   ? 20.809  -42.894 -1.958  1.00 25.74  ? 592 HOH D O   1 
HETATM 14136 O  O   . HOH S 8 .   ? 39.979  -41.263 -3.837  1.00 33.31  ? 593 HOH D O   1 
HETATM 14137 O  O   . HOH S 8 .   ? 40.772  -46.520 11.523  1.00 23.69  ? 594 HOH D O   1 
HETATM 14138 O  O   . HOH S 8 .   ? 38.628  -37.489 5.221   1.00 31.51  ? 595 HOH D O   1 
HETATM 14139 O  O   . HOH S 8 .   ? 34.188  -43.523 -3.484  1.00 26.72  ? 596 HOH D O   1 
HETATM 14140 O  O   . HOH S 8 .   ? 36.220  -52.235 -30.856 1.00 40.30  ? 597 HOH D O   1 
HETATM 14141 O  O   . HOH S 8 .   ? 35.722  -59.096 7.098   1.00 28.19  ? 598 HOH D O   1 
HETATM 14142 O  O   . HOH S 8 .   ? 11.839  -64.770 -7.743  1.00 32.49  ? 599 HOH D O   1 
HETATM 14143 O  O   . HOH S 8 .   ? 46.663  -67.938 -9.458  1.00 31.92  ? 600 HOH D O   1 
HETATM 14144 O  O   . HOH S 8 .   ? 44.097  -56.502 -7.973  1.00 22.61  ? 601 HOH D O   1 
HETATM 14145 O  O   . HOH S 8 .   ? 17.702  -45.463 9.220   1.00 31.63  ? 602 HOH D O   1 
HETATM 14146 O  O   . HOH S 8 .   ? 42.766  -59.952 -16.123 1.00 31.38  ? 603 HOH D O   1 
HETATM 14147 O  O   . HOH S 8 .   ? 26.132  -29.068 3.269   1.00 28.68  ? 604 HOH D O   1 
HETATM 14148 O  O   . HOH S 8 .   ? 46.405  -57.342 -6.562  1.00 33.01  ? 605 HOH D O   1 
HETATM 14149 O  O   . HOH S 8 .   ? 43.705  -59.739 8.276   1.00 22.85  ? 606 HOH D O   1 
HETATM 14150 O  O   . HOH S 8 .   ? 10.628  -63.079 -14.562 1.00 36.03  ? 607 HOH D O   1 
HETATM 14151 O  O   . HOH S 8 .   ? 12.469  -57.484 -11.996 1.00 38.50  ? 608 HOH D O   1 
HETATM 14152 O  O   . HOH S 8 .   ? 41.620  -74.028 -3.869  1.00 34.01  ? 609 HOH D O   1 
HETATM 14153 O  O   . HOH S 8 .   ? 13.638  -66.587 -22.760 1.00 38.85  ? 610 HOH D O   1 
HETATM 14154 O  O   . HOH S 8 .   ? 20.698  -61.210 6.225   1.00 33.83  ? 611 HOH D O   1 
HETATM 14155 O  O   . HOH S 8 .   ? 25.999  -59.467 -11.162 1.00 32.89  ? 612 HOH D O   1 
HETATM 14156 O  O   . HOH S 8 .   ? 32.539  -55.583 -15.212 1.00 34.60  ? 613 HOH D O   1 
HETATM 14157 O  O   . HOH S 8 .   ? 45.319  -60.043 -0.552  1.00 30.28  ? 614 HOH D O   1 
HETATM 14158 O  O   . HOH S 8 .   ? 17.531  -66.440 -6.109  1.00 27.26  ? 615 HOH D O   1 
HETATM 14159 O  O   . HOH S 8 .   ? 44.407  -74.475 -9.647  1.00 36.00  ? 616 HOH D O   1 
HETATM 14160 O  O   . HOH S 8 .   ? 36.379  -69.191 -16.553 1.00 32.81  ? 617 HOH D O   1 
HETATM 14161 O  O   . HOH S 8 .   ? 38.790  -63.703 6.329   1.00 27.03  ? 618 HOH D O   1 
HETATM 14162 O  O   . HOH S 8 .   ? 28.810  -35.103 5.837   1.00 29.72  ? 619 HOH D O   1 
HETATM 14163 O  O   . HOH S 8 .   ? 19.388  -45.200 -6.036  1.00 34.89  ? 620 HOH D O   1 
HETATM 14164 O  O   . HOH S 8 .   ? 23.208  -72.503 0.741   1.00 28.62  ? 621 HOH D O   1 
HETATM 14165 O  O   . HOH S 8 .   ? 28.940  -63.105 -17.006 1.00 35.84  ? 622 HOH D O   1 
HETATM 14166 O  O   . HOH S 8 .   ? 22.422  -30.146 -3.278  1.00 36.19  ? 623 HOH D O   1 
HETATM 14167 O  O   . HOH S 8 .   ? 43.281  -62.498 -15.670 1.00 30.38  ? 624 HOH D O   1 
HETATM 14168 O  O   . HOH S 8 .   ? 42.330  -50.046 -13.527 1.00 33.53  ? 625 HOH D O   1 
HETATM 14169 O  O   . HOH S 8 .   ? 7.415   -54.681 -8.428  1.00 41.42  ? 626 HOH D O   1 
HETATM 14170 O  O   . HOH S 8 .   ? 23.256  -38.889 -3.220  1.00 29.50  ? 627 HOH D O   1 
HETATM 14171 O  O   . HOH S 8 .   ? 44.907  -73.927 -13.310 1.00 34.43  ? 628 HOH D O   1 
HETATM 14172 O  O   . HOH S 8 .   ? 25.220  -42.682 8.412   1.00 28.63  ? 629 HOH D O   1 
HETATM 14173 O  O   . HOH S 8 .   ? 26.583  -38.563 -0.285  1.00 25.40  ? 630 HOH D O   1 
HETATM 14174 O  O   . HOH S 8 .   ? 15.065  -58.924 6.726   1.00 32.35  ? 631 HOH D O   1 
HETATM 14175 O  O   . HOH S 8 .   ? 27.168  -59.769 -28.315 1.00 35.12  ? 632 HOH D O   1 
HETATM 14176 O  O   . HOH S 8 .   ? 14.655  -54.439 -16.093 1.00 40.15  ? 633 HOH D O   1 
HETATM 14177 O  O   A HOH S 8 .   ? 21.016  -61.759 -26.401 0.51 29.56  ? 634 HOH D O   1 
HETATM 14178 O  O   B HOH S 8 .   ? 19.252  -63.350 -25.614 0.49 31.78  ? 634 HOH D O   1 
HETATM 14179 O  O   . HOH S 8 .   ? 23.343  -54.532 -32.074 1.00 46.68  ? 635 HOH D O   1 
HETATM 14180 O  O   . HOH S 8 .   ? 41.216  -73.083 0.994   1.00 28.52  ? 636 HOH D O   1 
HETATM 14181 O  O   . HOH S 8 .   ? 25.207  -42.409 -16.855 1.00 32.26  ? 637 HOH D O   1 
HETATM 14182 O  O   . HOH S 8 .   ? 48.057  -60.902 -14.134 1.00 29.85  ? 638 HOH D O   1 
HETATM 14183 O  O   . HOH S 8 .   ? 23.427  -28.827 3.079   1.00 35.15  ? 639 HOH D O   1 
HETATM 14184 O  O   . HOH S 8 .   ? 19.291  -28.603 -3.610  1.00 37.36  ? 640 HOH D O   1 
HETATM 14185 O  O   . HOH S 8 .   ? 11.168  -70.535 1.021   1.00 40.42  ? 641 HOH D O   1 
HETATM 14186 O  O   . HOH S 8 .   ? 44.947  -66.740 6.914   1.00 34.58  ? 642 HOH D O   1 
HETATM 14187 O  O   . HOH S 8 .   ? 49.045  -56.111 -6.665  1.00 35.97  ? 643 HOH D O   1 
HETATM 14188 O  O   . HOH S 8 .   ? 47.478  -54.036 2.603   1.00 33.09  ? 644 HOH D O   1 
HETATM 14189 O  O   . HOH S 8 .   ? 34.170  -37.280 -29.755 1.00 34.38  ? 645 HOH D O   1 
HETATM 14190 O  O   . HOH S 8 .   ? 13.980  -69.037 -22.789 1.00 50.16  ? 646 HOH D O   1 
HETATM 14191 O  O   . HOH S 8 .   ? 43.382  -59.311 -18.557 1.00 38.85  ? 647 HOH D O   1 
HETATM 14192 O  O   . HOH S 8 .   ? 39.159  -71.394 2.278   1.00 26.18  ? 648 HOH D O   1 
HETATM 14193 O  O   . HOH S 8 .   ? 43.060  -49.526 -8.899  1.00 33.66  ? 649 HOH D O   1 
HETATM 14194 O  O   . HOH S 8 .   ? 39.864  -46.807 -0.199  1.00 25.26  ? 650 HOH D O   1 
HETATM 14195 O  O   . HOH S 8 .   ? 40.590  -31.249 -3.199  1.00 35.94  ? 651 HOH D O   1 
HETATM 14196 O  O   . HOH S 8 .   ? 46.886  -61.300 0.727   1.00 40.87  ? 652 HOH D O   1 
HETATM 14197 O  O   . HOH S 8 .   ? 43.478  -72.286 1.987   1.00 41.75  ? 653 HOH D O   1 
HETATM 14198 O  O   . HOH S 8 .   ? 44.696  -62.461 -18.181 1.00 38.62  ? 654 HOH D O   1 
HETATM 14199 O  O   . HOH S 8 .   ? 36.907  -72.612 3.622   1.00 26.38  ? 655 HOH D O   1 
HETATM 14200 O  O   . HOH S 8 .   ? 37.129  -75.099 4.306   1.00 33.88  ? 656 HOH D 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   . ALA A 5   ? 0.7543 1.0138 0.7048 -0.0931 -0.2520 0.1509  5   ALA A N   
2     C CA  . ALA A 5   ? 0.8878 1.1529 0.8350 -0.0901 -0.2704 0.1593  5   ALA A CA  
3     C C   . ALA A 5   ? 0.9788 1.2321 0.8924 -0.0652 -0.2586 0.1574  5   ALA A C   
4     O O   . ALA A 5   ? 0.9705 1.2590 0.9112 -0.0471 -0.2538 0.1735  5   ALA A O   
5     C CB  . ALA A 5   ? 0.7970 1.1220 0.8107 -0.0919 -0.2769 0.1849  5   ALA A CB  
6     N N   . ASN A 6   ? 1.0364 1.2374 0.8896 -0.0635 -0.2518 0.1382  6   ASN A N   
7     C CA  . ASN A 6   ? 1.1163 1.2869 0.9208 -0.0480 -0.2482 0.1333  6   ASN A CA  
8     C C   . ASN A 6   ? 1.0032 1.1904 0.8154 -0.0229 -0.2269 0.1432  6   ASN A C   
9     O O   . ASN A 6   ? 1.1353 1.2979 0.9103 -0.0100 -0.2246 0.1420  6   ASN A O   
10    C CB  . ASN A 6   ? 1.1759 1.3432 0.9699 -0.0505 -0.2741 0.1378  6   ASN A CB  
11    C CG  . ASN A 6   ? 1.2654 1.4071 1.0439 -0.0740 -0.2982 0.1275  6   ASN A CG  
12    O OD1 . ASN A 6   ? 1.2615 1.4259 1.0813 -0.0914 -0.3098 0.1335  6   ASN A OD1 
13    N ND2 . ASN A 6   ? 1.1987 1.2910 0.9162 -0.0736 -0.3052 0.1132  6   ASN A ND2 
14    N N   . LYS A 7   ? 0.8077 1.0309 0.6627 -0.0136 -0.2105 0.1526  7   LYS A N   
15    C CA  . LYS A 7   ? 0.7453 0.9696 0.5958 0.0128  -0.1904 0.1585  7   LYS A CA  
16    C C   . LYS A 7   ? 0.6886 0.8709 0.4989 0.0149  -0.1689 0.1436  7   LYS A C   
17    O O   . LYS A 7   ? 0.7334 0.8849 0.5079 0.0269  -0.1604 0.1415  7   LYS A O   
18    C CB  . LYS A 7   ? 0.7491 1.0223 0.6550 0.0284  -0.1789 0.1737  7   LYS A CB  
19    C CG  . LYS A 7   ? 0.6889 0.9575 0.5899 0.0598  -0.1572 0.1782  7   LYS A CG  
20    C CD  . LYS A 7   ? 0.7573 0.9828 0.6094 0.0705  -0.1575 0.1738  7   LYS A CD  
21    C CE  . LYS A 7   ? 0.8374 1.0633 0.6932 0.1004  -0.1460 0.1826  7   LYS A CE  
22    N NZ  . LYS A 7   ? 0.8534 1.0251 0.6589 0.1088  -0.1388 0.1751  7   LYS A NZ  
23    N N   . TYR A 8   ? 0.6236 0.7972 0.4422 0.0024  -0.1575 0.1304  8   TYR A N   
24    C CA  . TYR A 8   ? 0.5835 0.7189 0.3778 0.0042  -0.1329 0.1144  8   TYR A CA  
25    C C   . TYR A 8   ? 0.5936 0.6989 0.3616 -0.0151 -0.1343 0.0977  8   TYR A C   
26    O O   . TYR A 8   ? 0.5797 0.6958 0.3609 -0.0308 -0.1499 0.0959  8   TYR A O   
27    C CB  . TYR A 8   ? 0.4976 0.6482 0.3252 0.0130  -0.1133 0.1139  8   TYR A CB  
28    C CG  . TYR A 8   ? 0.5416 0.7159 0.3885 0.0373  -0.1091 0.1291  8   TYR A CG  
29    C CD1 . TYR A 8   ? 0.5914 0.7378 0.4102 0.0546  -0.1007 0.1303  8   TYR A CD1 
30    C CD2 . TYR A 8   ? 0.5294 0.7535 0.4207 0.0443  -0.1144 0.1443  8   TYR A CD2 
31    C CE1 . TYR A 8   ? 0.5687 0.7300 0.3974 0.0806  -0.0983 0.1437  8   TYR A CE1 
32    C CE2 . TYR A 8   ? 0.5102 0.7559 0.4149 0.0718  -0.1087 0.1593  8   TYR A CE2 
33    C CZ  . TYR A 8   ? 0.5330 0.7443 0.4034 0.0911  -0.1011 0.1577  8   TYR A CZ  
34    O OH  . TYR A 8   ? 0.5832 0.8036 0.4635 0.1191  -0.0935 0.1672  8   TYR A OH  
35    N N   . PRO A 9   ? 0.6058 0.6732 0.3381 -0.0135 -0.1171 0.0867  9   PRO A N   
36    C CA  . PRO A 9   ? 0.6058 0.6468 0.3172 -0.0255 -0.1100 0.0708  9   PRO A CA  
37    C C   . PRO A 9   ? 0.5599 0.6158 0.3074 -0.0313 -0.1005 0.0648  9   PRO A C   
38    O O   . PRO A 9   ? 0.5114 0.5856 0.2902 -0.0228 -0.0880 0.0693  9   PRO A O   
39    C CB  . PRO A 9   ? 0.6526 0.6624 0.3312 -0.0181 -0.0879 0.0670  9   PRO A CB  
40    C CG  . PRO A 9   ? 0.6463 0.6667 0.3418 -0.0048 -0.0808 0.0786  9   PRO A CG  
41    C CD  . PRO A 9   ? 0.5907 0.6400 0.3046 0.0007  -0.1018 0.0908  9   PRO A CD  
42    N N   . THR A 10  ? 0.5474 0.5881 0.2832 -0.0441 -0.1059 0.0534  10  THR A N   
43    C CA  . THR A 10  ? 0.5348 0.5843 0.2992 -0.0508 -0.0984 0.0469  10  THR A CA  
44    C C   . THR A 10  ? 0.5337 0.5465 0.2645 -0.0536 -0.0857 0.0307  10  THR A C   
45    O O   . THR A 10  ? 0.6321 0.6141 0.3159 -0.0513 -0.0860 0.0251  10  THR A O   
46    C CB  . THR A 10  ? 0.5098 0.5836 0.3024 -0.0646 -0.1228 0.0534  10  THR A CB  
47    O OG1 . THR A 10  ? 0.6025 0.6999 0.4372 -0.0667 -0.1138 0.0552  10  THR A OG1 
48    C CG2 . THR A 10  ? 0.5692 0.6092 0.3237 -0.0795 -0.1433 0.0430  10  THR A CG2 
49    N N   . GLU A 11  ? 0.5513 0.5681 0.3046 -0.0562 -0.0740 0.0243  11  GLU A N   
50    C CA  . GLU A 11  ? 0.5709 0.5589 0.3000 -0.0560 -0.0599 0.0105  11  GLU A CA  
51    C C   . GLU A 11  ? 0.4987 0.4983 0.2620 -0.0603 -0.0531 0.0061  11  GLU A C   
52    O O   . GLU A 11  ? 0.4791 0.5054 0.2807 -0.0570 -0.0460 0.0131  11  GLU A O   
53    C CB  . GLU A 11  ? 0.6127 0.5895 0.3238 -0.0443 -0.0366 0.0113  11  GLU A CB  
54    C CG  . GLU A 11  ? 0.6243 0.5969 0.3446 -0.0408 -0.0143 0.0052  11  GLU A CG  
55    C CD  . GLU A 11  ? 0.7567 0.7230 0.4640 -0.0321 0.0065  0.0110  11  GLU A CD  
56    O OE1 . GLU A 11  ? 0.7469 0.7109 0.4383 -0.0288 0.0040  0.0201  11  GLU A OE1 
57    O OE2 . GLU A 11  ? 0.6529 0.6202 0.3719 -0.0295 0.0247  0.0089  11  GLU A OE2 
58    N N   . GLN A 12  ? 0.4952 0.4703 0.2392 -0.0660 -0.0562 -0.0055 12  GLN A N   
59    C CA  . GLN A 12  ? 0.5110 0.4925 0.2827 -0.0697 -0.0499 -0.0100 12  GLN A CA  
60    C C   . GLN A 12  ? 0.5527 0.5366 0.3341 -0.0583 -0.0225 -0.0127 12  GLN A C   
61    O O   . GLN A 12  ? 0.6204 0.5907 0.3769 -0.0495 -0.0084 -0.0141 12  GLN A O   
62    C CB  . GLN A 12  ? 0.4772 0.4246 0.2190 -0.0779 -0.0631 -0.0217 12  GLN A CB  
63    C CG  . GLN A 12  ? 0.5954 0.5534 0.3576 -0.0964 -0.0922 -0.0149 12  GLN A CG  
64    C CD  . GLN A 12  ? 0.7029 0.6154 0.4223 -0.1074 -0.1153 -0.0256 12  GLN A CD  
65    O OE1 . GLN A 12  ? 0.7081 0.6109 0.4111 -0.1194 -0.1436 -0.0216 12  GLN A OE1 
66    N NE2 . GLN A 12  ? 0.7594 0.6419 0.4608 -0.1039 -0.1060 -0.0385 12  GLN A NE2 
67    N N   . LEU A 13  ? 0.4750 0.4795 0.2951 -0.0585 -0.0159 -0.0102 13  LEU A N   
68    C CA  . LEU A 13  ? 0.4573 0.4655 0.2919 -0.0502 0.0052  -0.0113 13  LEU A CA  
69    C C   . LEU A 13  ? 0.5404 0.5258 0.3528 -0.0462 0.0176  -0.0216 13  LEU A C   
70    O O   . LEU A 13  ? 0.5706 0.5406 0.3737 -0.0500 0.0115  -0.0301 13  LEU A O   
71    C CB  . LEU A 13  ? 0.4275 0.4573 0.3017 -0.0509 0.0056  -0.0077 13  LEU A CB  
72    C CG  . LEU A 13  ? 0.5228 0.5684 0.4232 -0.0433 0.0141  -0.0012 13  LEU A CG  
73    C CD1 . LEU A 13  ? 0.4426 0.4890 0.3624 -0.0426 0.0217  -0.0062 13  LEU A CD1 
74    C CD2 . LEU A 13  ? 0.4520 0.4908 0.3430 -0.0373 0.0232  0.0025  13  LEU A CD2 
75    N N   . LYS A 14  ? 0.4978 0.4804 0.3011 -0.0379 0.0351  -0.0192 14  LYS A N   
76    C CA  . LYS A 14  ? 0.5297 0.4944 0.3097 -0.0298 0.0494  -0.0261 14  LYS A CA  
77    C C   . LYS A 14  ? 0.5060 0.4780 0.3134 -0.0278 0.0588  -0.0298 14  LYS A C   
78    O O   . LYS A 14  ? 0.5857 0.5401 0.3743 -0.0211 0.0652  -0.0381 14  LYS A O   
79    C CB  . LYS A 14  ? 0.5517 0.5178 0.3172 -0.0211 0.0669  -0.0178 14  LYS A CB  
80    C CG  . LYS A 14  ? 0.6200 0.5732 0.3491 -0.0203 0.0595  -0.0147 14  LYS A CG  
81    C CD  . LYS A 14  ? 0.6493 0.6107 0.3754 -0.0140 0.0778  -0.0015 14  LYS A CD  
82    C CE  . LYS A 14  ? 0.6872 0.6559 0.4190 -0.0199 0.0669  0.0079  14  LYS A CE  
83    N NZ  . LYS A 14  ? 0.7692 0.7223 0.4575 -0.0144 0.0680  0.0130  14  LYS A NZ  
84    N N   . LEU A 15  ? 0.4592 0.4528 0.3060 -0.0317 0.0586  -0.0241 15  LEU A N   
85    C CA  . LEU A 15  ? 0.4507 0.4516 0.3245 -0.0301 0.0652  -0.0265 15  LEU A CA  
86    C C   . LEU A 15  ? 0.4351 0.4324 0.3170 -0.0359 0.0526  -0.0329 15  LEU A C   
87    O O   . LEU A 15  ? 0.4415 0.4435 0.3443 -0.0345 0.0563  -0.0347 15  LEU A O   
88    C CB  . LEU A 15  ? 0.4004 0.4198 0.3063 -0.0306 0.0693  -0.0170 15  LEU A CB  
89    C CG  . LEU A 15  ? 0.4598 0.4858 0.3689 -0.0277 0.0826  -0.0072 15  LEU A CG  
90    C CD1 . LEU A 15  ? 0.4339 0.4681 0.3658 -0.0324 0.0770  0.0026  15  LEU A CD1 
91    C CD2 . LEU A 15  ? 0.4357 0.4670 0.3545 -0.0212 0.0979  -0.0071 15  LEU A CD2 
92    N N   . TRP A 16  ? 0.4572 0.4477 0.3248 -0.0433 0.0369  -0.0341 16  TRP A N   
93    C CA  . TRP A 16  ? 0.4892 0.4760 0.3640 -0.0519 0.0232  -0.0368 16  TRP A CA  
94    C C   . TRP A 16  ? 0.4281 0.3948 0.2947 -0.0487 0.0285  -0.0464 16  TRP A C   
95    O O   . TRP A 16  ? 0.4415 0.4148 0.3310 -0.0510 0.0279  -0.0458 16  TRP A O   
96    C CB  . TRP A 16  ? 0.5320 0.5061 0.3829 -0.0614 0.0042  -0.0371 16  TRP A CB  
97    C CG  . TRP A 16  ? 0.5939 0.5754 0.4636 -0.0748 -0.0135 -0.0324 16  TRP A CG  
98    C CD1 . TRP A 16  ? 0.6413 0.5975 0.4930 -0.0863 -0.0309 -0.0372 16  TRP A CD1 
99    C CD2 . TRP A 16  ? 0.5564 0.5726 0.4660 -0.0776 -0.0155 -0.0198 16  TRP A CD2 
100   N NE1 . TRP A 16  ? 0.6626 0.6415 0.5479 -0.0992 -0.0437 -0.0255 16  TRP A NE1 
101   C CE2 . TRP A 16  ? 0.5946 0.6127 0.5155 -0.0920 -0.0324 -0.0145 16  TRP A CE2 
102   C CE3 . TRP A 16  ? 0.5615 0.6047 0.4956 -0.0679 -0.0047 -0.0117 16  TRP A CE3 
103   C CZ2 . TRP A 16  ? 0.6014 0.6551 0.5612 -0.0956 -0.0354 0.0011  16  TRP A CZ2 
104   C CZ3 . TRP A 16  ? 0.4159 0.4875 0.3807 -0.0684 -0.0081 0.0007  16  TRP A CZ3 
105   C CH2 . TRP A 16  ? 0.4716 0.5520 0.4510 -0.0815 -0.0216 0.0080  16  TRP A CH2 
106   N N   . GLY A 17  ? 0.4779 0.4180 0.3082 -0.0411 0.0342  -0.0546 17  GLY A N   
107   C CA  . GLY A 17  ? 0.5033 0.4180 0.3177 -0.0348 0.0381  -0.0643 17  GLY A CA  
108   C C   . GLY A 17  ? 0.4995 0.4329 0.3458 -0.0266 0.0542  -0.0621 17  GLY A C   
109   O O   . GLY A 17  ? 0.4530 0.3782 0.3074 -0.0269 0.0521  -0.0660 17  GLY A O   
110   N N   . LYS A 18  ? 0.4363 0.3938 0.3009 -0.0203 0.0686  -0.0545 18  LYS A N   
111   C CA  . LYS A 18  ? 0.4289 0.4054 0.3264 -0.0149 0.0798  -0.0504 18  LYS A CA  
112   C C   . LYS A 18  ? 0.3909 0.3800 0.3188 -0.0233 0.0698  -0.0477 18  LYS A C   
113   O O   . LYS A 18  ? 0.3914 0.3815 0.3349 -0.0198 0.0725  -0.0494 18  LYS A O   
114   C CB  . LYS A 18  ? 0.4006 0.3990 0.3130 -0.0112 0.0921  -0.0399 18  LYS A CB  
115   C CG  . LYS A 18  ? 0.4204 0.4375 0.3674 -0.0070 0.1006  -0.0341 18  LYS A CG  
116   C CD  . LYS A 18  ? 0.4939 0.5305 0.4536 -0.0035 0.1137  -0.0215 18  LYS A CD  
117   C CE  . LYS A 18  ? 0.4676 0.5239 0.4630 -0.0004 0.1199  -0.0141 18  LYS A CE  
118   N NZ  . LYS A 18  ? 0.4769 0.5562 0.4902 -0.0011 0.1303  0.0028  18  LYS A NZ  
119   N N   . ALA A 19  ? 0.3754 0.3747 0.3106 -0.0319 0.0589  -0.0426 19  ALA A N   
120   C CA  . ALA A 19  ? 0.3758 0.3869 0.3348 -0.0357 0.0518  -0.0385 19  ALA A CA  
121   C C   . ALA A 19  ? 0.3514 0.3494 0.3076 -0.0399 0.0456  -0.0431 19  ALA A C   
122   O O   . ALA A 19  ? 0.3600 0.3623 0.3335 -0.0380 0.0466  -0.0417 19  ALA A O   
123   C CB  . ALA A 19  ? 0.3491 0.3741 0.3127 -0.0407 0.0425  -0.0307 19  ALA A CB  
124   N N   . LYS A 20  ? 0.3852 0.3631 0.3165 -0.0461 0.0373  -0.0480 20  LYS A N   
125   C CA  . LYS A 20  ? 0.4332 0.3914 0.3578 -0.0528 0.0277  -0.0515 20  LYS A CA  
126   C C   . LYS A 20  ? 0.3967 0.3378 0.3154 -0.0418 0.0381  -0.0595 20  LYS A C   
127   O O   . LYS A 20  ? 0.4038 0.3393 0.3324 -0.0439 0.0351  -0.0591 20  LYS A O   
128   C CB  . LYS A 20  ? 0.4911 0.4228 0.3833 -0.0623 0.0125  -0.0559 20  LYS A CB  
129   C CG  . LYS A 20  ? 0.5090 0.4593 0.4112 -0.0760 -0.0028 -0.0455 20  LYS A CG  
130   C CD  . LYS A 20  ? 0.5057 0.4825 0.4446 -0.0852 -0.0090 -0.0322 20  LYS A CD  
131   C CE  . LYS A 20  ? 0.6344 0.6169 0.5780 -0.1038 -0.0310 -0.0217 20  LYS A CE  
132   N NZ  . LYS A 20  ? 0.4836 0.5129 0.4668 -0.1059 -0.0311 -0.0027 20  LYS A NZ  
133   N N   . GLU A 21  ? 0.4246 0.3572 0.3256 -0.0292 0.0505  -0.0653 21  GLU A N   
134   C CA  . GLU A 21  ? 0.4358 0.3560 0.3318 -0.0152 0.0621  -0.0710 21  GLU A CA  
135   C C   . GLU A 21  ? 0.3976 0.3432 0.3314 -0.0114 0.0690  -0.0651 21  GLU A C   
136   O O   . GLU A 21  ? 0.3996 0.3353 0.3372 -0.0063 0.0701  -0.0679 21  GLU A O   
137   C CB  . GLU A 21  ? 0.4913 0.4060 0.3647 -0.0001 0.0769  -0.0739 21  GLU A CB  
138   C CG  . GLU A 21  ? 0.5804 0.4913 0.4543 0.0179  0.0917  -0.0763 21  GLU A CG  
139   C CD  . GLU A 21  ? 0.7692 0.6750 0.6161 0.0364  0.1089  -0.0767 21  GLU A CD  
140   O OE1 . GLU A 21  ? 0.8432 0.7189 0.6560 0.0533  0.1150  -0.0847 21  GLU A OE1 
141   O OE2 . GLU A 21  ? 0.7858 0.7160 0.6428 0.0350  0.1164  -0.0682 21  GLU A OE2 
142   N N   . LEU A 22  ? 0.3417 0.3154 0.3000 -0.0138 0.0715  -0.0570 22  LEU A N   
143   C CA  . LEU A 22  ? 0.2912 0.2821 0.2796 -0.0111 0.0732  -0.0520 22  LEU A CA  
144   C C   . LEU A 22  ? 0.3267 0.3120 0.3216 -0.0158 0.0643  -0.0517 22  LEU A C   
145   O O   . LEU A 22  ? 0.3258 0.3108 0.3328 -0.0101 0.0658  -0.0517 22  LEU A O   
146   C CB  . LEU A 22  ? 0.3077 0.3189 0.3124 -0.0143 0.0720  -0.0440 22  LEU A CB  
147   C CG  . LEU A 22  ? 0.2901 0.3116 0.2978 -0.0102 0.0819  -0.0398 22  LEU A CG  
148   C CD1 . LEU A 22  ? 0.3271 0.3594 0.3419 -0.0167 0.0762  -0.0323 22  LEU A CD1 
149   C CD2 . LEU A 22  ? 0.3013 0.3340 0.3289 -0.0022 0.0906  -0.0359 22  LEU A CD2 
150   N N   . ARG A 23  ? 0.2808 0.2652 0.2705 -0.0260 0.0550  -0.0490 23  ARG A N   
151   C CA  . ARG A 23  ? 0.2978 0.2822 0.2964 -0.0311 0.0482  -0.0442 23  ARG A CA  
152   C C   . ARG A 23  ? 0.3648 0.3237 0.3513 -0.0314 0.0460  -0.0500 23  ARG A C   
153   O O   . ARG A 23  ? 0.3399 0.2964 0.3358 -0.0290 0.0460  -0.0475 23  ARG A O   
154   C CB  . ARG A 23  ? 0.3085 0.3029 0.3081 -0.0425 0.0389  -0.0365 23  ARG A CB  
155   C CG  . ARG A 23  ? 0.3344 0.3348 0.3465 -0.0490 0.0331  -0.0269 23  ARG A CG  
156   C CD  . ARG A 23  ? 0.3439 0.3650 0.3652 -0.0591 0.0250  -0.0146 23  ARG A CD  
157   N NE  . ARG A 23  ? 0.3511 0.3805 0.3874 -0.0679 0.0195  -0.0016 23  ARG A NE  
158   C CZ  . ARG A 23  ? 0.3541 0.3676 0.3857 -0.0844 0.0067  0.0009  23  ARG A CZ  
159   N NH1 . ARG A 23  ? 0.4412 0.4236 0.4469 -0.0912 -0.0023 -0.0114 23  ARG A NH1 
160   N NH2 . ARG A 23  ? 0.4038 0.4293 0.4542 -0.0939 0.0020  0.0169  23  ARG A NH2 
161   N N   . GLU A 24  ? 0.3652 0.2998 0.3256 -0.0336 0.0430  -0.0576 24  GLU A N   
162   C CA  . GLU A 24  ? 0.4013 0.3018 0.3416 -0.0321 0.0393  -0.0644 24  GLU A CA  
163   C C   . GLU A 24  ? 0.4091 0.3084 0.3556 -0.0153 0.0513  -0.0683 24  GLU A C   
164   O O   . GLU A 24  ? 0.4174 0.3012 0.3637 -0.0133 0.0488  -0.0688 24  GLU A O   
165   C CB  . GLU A 24  ? 0.4693 0.3361 0.3702 -0.0322 0.0340  -0.0740 24  GLU A CB  
166   C CG  . GLU A 24  ? 0.5721 0.4302 0.4606 -0.0508 0.0162  -0.0710 24  GLU A CG  
167   C CD  . GLU A 24  ? 0.7421 0.5858 0.6350 -0.0692 -0.0019 -0.0640 24  GLU A CD  
168   O OE1 . GLU A 24  ? 0.7464 0.5712 0.6378 -0.0668 -0.0021 -0.0652 24  GLU A OE1 
169   O OE2 . GLU A 24  ? 0.7987 0.6506 0.6973 -0.0871 -0.0172 -0.0554 24  GLU A OE2 
170   N N   . GLN A 25  ? 0.3862 0.3030 0.3400 -0.0038 0.0635  -0.0692 25  GLN A N   
171   C CA  . GLN A 25  ? 0.4087 0.3323 0.3753 0.0117  0.0740  -0.0696 25  GLN A CA  
172   C C   . GLN A 25  ? 0.3749 0.3132 0.3685 0.0100  0.0702  -0.0634 25  GLN A C   
173   O O   . GLN A 25  ? 0.3932 0.3251 0.3918 0.0194  0.0721  -0.0643 25  GLN A O   
174   C CB  . GLN A 25  ? 0.3548 0.3028 0.3328 0.0201  0.0861  -0.0661 25  GLN A CB  
175   C CG  . GLN A 25  ? 0.4899 0.4449 0.4785 0.0383  0.0981  -0.0648 25  GLN A CG  
176   C CD  . GLN A 25  ? 0.6418 0.5633 0.5950 0.0536  0.1042  -0.0738 25  GLN A CD  
177   O OE1 . GLN A 25  ? 0.6818 0.5889 0.6329 0.0638  0.1044  -0.0764 25  GLN A OE1 
178   N NE2 . GLN A 25  ? 0.6433 0.5505 0.5654 0.0583  0.1097  -0.0781 25  GLN A NE2 
179   N N   . TYR A 26  ? 0.3085 0.2654 0.3167 0.0010  0.0651  -0.0570 26  TYR A N   
180   C CA  . TYR A 26  ? 0.2777 0.2428 0.3024 0.0023  0.0612  -0.0514 26  TYR A CA  
181   C C   . TYR A 26  ? 0.3293 0.2751 0.3464 0.0009  0.0569  -0.0512 26  TYR A C   
182   O O   . TYR A 26  ? 0.3056 0.2472 0.3287 0.0091  0.0573  -0.0508 26  TYR A O   
183   C CB  . TYR A 26  ? 0.2922 0.2739 0.3240 -0.0036 0.0572  -0.0448 26  TYR A CB  
184   C CG  . TYR A 26  ? 0.2893 0.2735 0.3270 -0.0003 0.0535  -0.0387 26  TYR A CG  
185   C CD1 . TYR A 26  ? 0.2609 0.2486 0.3066 0.0084  0.0512  -0.0376 26  TYR A CD1 
186   C CD2 . TYR A 26  ? 0.2602 0.2431 0.2948 -0.0056 0.0511  -0.0321 26  TYR A CD2 
187   C CE1 . TYR A 26  ? 0.2747 0.2591 0.3173 0.0148  0.0475  -0.0329 26  TYR A CE1 
188   C CE2 . TYR A 26  ? 0.2765 0.2635 0.3134 0.0012  0.0507  -0.0241 26  TYR A CE2 
189   C CZ  . TYR A 26  ? 0.2765 0.2615 0.3133 0.0131  0.0492  -0.0259 26  TYR A CZ  
190   O OH  . TYR A 26  ? 0.2903 0.2730 0.3204 0.0230  0.0486  -0.0191 26  TYR A OH  
191   N N   . TYR A 27  ? 0.3402 0.2731 0.3443 -0.0105 0.0512  -0.0503 27  TYR A N   
192   C CA  . TYR A 27  ? 0.3508 0.2644 0.3490 -0.0157 0.0453  -0.0468 27  TYR A CA  
193   C C   . TYR A 27  ? 0.3946 0.2777 0.3756 -0.0066 0.0465  -0.0558 27  TYR A C   
194   O O   . TYR A 27  ? 0.3827 0.2520 0.3632 -0.0032 0.0447  -0.0535 27  TYR A O   
195   C CB  . TYR A 27  ? 0.3161 0.2254 0.3087 -0.0338 0.0354  -0.0404 27  TYR A CB  
196   C CG  . TYR A 27  ? 0.3347 0.2780 0.3480 -0.0387 0.0359  -0.0274 27  TYR A CG  
197   C CD1 . TYR A 27  ? 0.3157 0.2722 0.3421 -0.0334 0.0394  -0.0168 27  TYR A CD1 
198   C CD2 . TYR A 27  ? 0.3364 0.2972 0.3525 -0.0448 0.0339  -0.0252 27  TYR A CD2 
199   C CE1 . TYR A 27  ? 0.2802 0.2660 0.3203 -0.0321 0.0423  -0.0040 27  TYR A CE1 
200   C CE2 . TYR A 27  ? 0.2858 0.2776 0.3191 -0.0449 0.0356  -0.0122 27  TYR A CE2 
201   C CZ  . TYR A 27  ? 0.2649 0.2687 0.3091 -0.0376 0.0404  -0.0015 27  TYR A CZ  
202   O OH  . TYR A 27  ? 0.2778 0.3095 0.3336 -0.0323 0.0445  0.0120  27  TYR A OH  
203   N N   A MET A 28  ? 0.3947 0.2649 0.3582 -0.0002 0.0503  -0.0653 28  MET A N   
204   N N   B MET A 28  ? 0.3950 0.2648 0.3581 -0.0003 0.0502  -0.0654 28  MET A N   
205   C CA  A MET A 28  ? 0.4294 0.2700 0.3731 0.0142  0.0538  -0.0734 28  MET A CA  
206   C CA  B MET A 28  ? 0.4296 0.2704 0.3730 0.0146  0.0541  -0.0736 28  MET A CA  
207   C C   A MET A 28  ? 0.4183 0.2779 0.3837 0.0308  0.0628  -0.0716 28  MET A C   
208   C C   B MET A 28  ? 0.4185 0.2781 0.3836 0.0312  0.0630  -0.0718 28  MET A C   
209   O O   A MET A 28  ? 0.4456 0.2865 0.4055 0.0402  0.0622  -0.0728 28  MET A O   
210   O O   B MET A 28  ? 0.4467 0.2867 0.4052 0.0412  0.0628  -0.0734 28  MET A O   
211   C CB  A MET A 28  ? 0.4920 0.3136 0.4063 0.0210  0.0576  -0.0828 28  MET A CB  
212   C CB  B MET A 28  ? 0.4910 0.3145 0.4061 0.0220  0.0585  -0.0829 28  MET A CB  
213   C CG  A MET A 28  ? 0.5730 0.3427 0.4454 0.0142  0.0446  -0.0899 28  MET A CG  
214   C CG  B MET A 28  ? 0.5732 0.3537 0.4535 0.0383  0.0603  -0.0922 28  MET A CG  
215   S SD  A MET A 28  ? 0.6598 0.4087 0.5313 -0.0141 0.0223  -0.0816 28  MET A SD  
216   S SD  B MET A 28  ? 0.6864 0.4617 0.5392 0.0592  0.0752  -0.1001 28  MET A SD  
217   C CE  A MET A 28  ? 0.5691 0.2992 0.4440 -0.0060 0.0226  -0.0789 28  MET A CE  
218   C CE  B MET A 28  ? 0.5995 0.4136 0.4856 0.0840  0.0953  -0.0939 28  MET A CE  
219   N N   . ASN A 29  ? 0.3866 0.2819 0.3772 0.0334  0.0686  -0.0674 29  ASN A N   
220   C CA  . ASN A 29  ? 0.3594 0.2736 0.3738 0.0456  0.0722  -0.0635 29  ASN A CA  
221   C C   . ASN A 29  ? 0.3766 0.2847 0.3971 0.0438  0.0641  -0.0593 29  ASN A C   
222   O O   . ASN A 29  ? 0.3793 0.2846 0.4064 0.0559  0.0642  -0.0585 29  ASN A O   
223   C CB  . ASN A 29  ? 0.3508 0.2996 0.3904 0.0430  0.0741  -0.0578 29  ASN A CB  
224   C CG  . ASN A 29  ? 0.3592 0.3200 0.3982 0.0488  0.0851  -0.0583 29  ASN A CG  
225   O OD1 . ASN A 29  ? 0.4546 0.4013 0.4766 0.0614  0.0937  -0.0628 29  ASN A OD1 
226   N ND2 . ASN A 29  ? 0.4645 0.4490 0.5185 0.0410  0.0852  -0.0529 29  ASN A ND2 
227   N N   . TYR A 30  ? 0.3544 0.2621 0.3727 0.0308  0.0579  -0.0549 30  TYR A N   
228   C CA  . TYR A 30  ? 0.3268 0.2280 0.3468 0.0317  0.0527  -0.0490 30  TYR A CA  
229   C C   . TYR A 30  ? 0.3758 0.2454 0.3792 0.0353  0.0512  -0.0512 30  TYR A C   
230   O O   . TYR A 30  ? 0.3976 0.2596 0.4028 0.0457  0.0498  -0.0496 30  TYR A O   
231   C CB  . TYR A 30  ? 0.3054 0.2146 0.3253 0.0199  0.0496  -0.0407 30  TYR A CB  
232   C CG  . TYR A 30  ? 0.3405 0.2463 0.3599 0.0235  0.0473  -0.0320 30  TYR A CG  
233   C CD1 . TYR A 30  ? 0.3399 0.2552 0.3644 0.0343  0.0456  -0.0302 30  TYR A CD1 
234   C CD2 . TYR A 30  ? 0.3496 0.2405 0.3609 0.0157  0.0456  -0.0244 30  TYR A CD2 
235   C CE1 . TYR A 30  ? 0.3378 0.2467 0.3547 0.0406  0.0441  -0.0221 30  TYR A CE1 
236   C CE2 . TYR A 30  ? 0.3855 0.2751 0.3949 0.0206  0.0459  -0.0137 30  TYR A CE2 
237   C CZ  . TYR A 30  ? 0.3742 0.2726 0.3843 0.0347  0.0461  -0.0135 30  TYR A CZ  
238   O OH  . TYR A 30  ? 0.4672 0.3605 0.4685 0.0430  0.0468  -0.0035 30  TYR A OH  
239   N N   . ALA A 31  ? 0.3838 0.2302 0.3676 0.0271  0.0493  -0.0551 31  ALA A N   
240   C CA  . ALA A 31  ? 0.4333 0.2403 0.3951 0.0292  0.0448  -0.0574 31  ALA A CA  
241   C C   . ALA A 31  ? 0.4535 0.2485 0.4089 0.0514  0.0508  -0.0650 31  ALA A C   
242   O O   . ALA A 31  ? 0.4784 0.2478 0.4230 0.0592  0.0479  -0.0646 31  ALA A O   
243   C CB  . ALA A 31  ? 0.4648 0.2432 0.4024 0.0146  0.0371  -0.0605 31  ALA A CB  
244   N N   . ARG A 32  ? 0.2931 0.2945 0.3916 0.0216  0.0205  -0.0844 32  ARG A N   
245   C CA  . ARG A 32  ? 0.3364 0.3409 0.4401 0.0225  0.0293  -0.0866 32  ARG A CA  
246   C C   . ARG A 32  ? 0.3143 0.3247 0.4164 0.0194  0.0364  -0.0734 32  ARG A C   
247   O O   . ARG A 32  ? 0.3482 0.3620 0.4542 0.0199  0.0443  -0.0754 32  ARG A O   
248   C CB  . ARG A 32  ? 0.4206 0.4212 0.4998 0.0265  0.0324  -0.1003 32  ARG A CB  
249   C CG  . ARG A 32  ? 0.4433 0.4384 0.5203 0.0310  0.0225  -0.1161 32  ARG A CG  
250   C CD  . ARG A 32  ? 0.4681 0.4590 0.5141 0.0367  0.0253  -0.1291 32  ARG A CD  
251   N NE  . ARG A 32  ? 0.6159 0.6099 0.6729 0.0383  0.0357  -0.1352 32  ARG A NE  
252   C CZ  . ARG A 32  ? 0.6323 0.6244 0.6651 0.0431  0.0438  -0.1445 32  ARG A CZ  
253   N NH1 . ARG A 32  ? 0.6981 0.6841 0.6906 0.0476  0.0426  -0.1483 32  ARG A NH1 
254   N NH2 . ARG A 32  ? 0.5883 0.5844 0.6374 0.0443  0.0540  -0.1497 32  ARG A NH2 
255   N N   . ALA A 33  ? 0.3219 0.3341 0.4212 0.0164  0.0336  -0.0610 33  ALA A N   
256   C CA  . ALA A 33  ? 0.3510 0.3688 0.4464 0.0139  0.0381  -0.0507 33  ALA A CA  
257   C C   . ALA A 33  ? 0.3436 0.3681 0.4625 0.0149  0.0424  -0.0484 33  ALA A C   
258   O O   . ALA A 33  ? 0.3516 0.3810 0.4690 0.0137  0.0476  -0.0464 33  ALA A O   
259   C CB  . ALA A 33  ? 0.3184 0.3373 0.4117 0.0121  0.0330  -0.0398 33  ALA A CB  
260   N N   . LYS A 34  ? 0.3030 0.3277 0.4466 0.0172  0.0400  -0.0478 34  LYS A N   
261   C CA  . LYS A 34  ? 0.3477 0.3785 0.5147 0.0191  0.0424  -0.0432 34  LYS A CA  
262   C C   . LYS A 34  ? 0.3548 0.3867 0.5330 0.0210  0.0484  -0.0544 34  LYS A C   
263   O O   . LYS A 34  ? 0.3513 0.3892 0.5483 0.0227  0.0509  -0.0516 34  LYS A O   
264   C CB  . LYS A 34  ? 0.3440 0.3733 0.5339 0.0215  0.0385  -0.0353 34  LYS A CB  
265   C CG  . LYS A 34  ? 0.3052 0.3351 0.4851 0.0206  0.0347  -0.0227 34  LYS A CG  
266   C CD  . LYS A 34  ? 0.3390 0.3762 0.5077 0.0204  0.0342  -0.0152 34  LYS A CD  
267   C CE  . LYS A 34  ? 0.3312 0.3693 0.4870 0.0205  0.0305  -0.0040 34  LYS A CE  
268   N NZ  . LYS A 34  ? 0.3099 0.3560 0.4578 0.0216  0.0280  0.0016  34  LYS A NZ  
269   N N   . GLU A 35  ? 0.3323 0.3588 0.4986 0.0217  0.0507  -0.0675 35  GLU A N   
270   C CA  . GLU A 35  ? 0.3749 0.4026 0.5493 0.0243  0.0580  -0.0794 35  GLU A CA  
271   C C   . GLU A 35  ? 0.3610 0.3962 0.5356 0.0231  0.0665  -0.0763 35  GLU A C   
272   O O   . GLU A 35  ? 0.3261 0.3658 0.5216 0.0254  0.0720  -0.0812 35  GLU A O   
273   C CB  . GLU A 35  ? 0.3777 0.3986 0.5294 0.0263  0.0592  -0.0938 35  GLU A CB  
274   C CG  . GLU A 35  ? 0.4252 0.4400 0.5870 0.0282  0.0498  -0.1011 35  GLU A CG  
275   C CD  . GLU A 35  ? 0.5057 0.5143 0.6444 0.0317  0.0478  -0.1175 35  GLU A CD  
276   O OE1 . GLU A 35  ? 0.5546 0.5630 0.6694 0.0337  0.0561  -0.1234 35  GLU A OE1 
277   O OE2 . GLU A 35  ? 0.4777 0.4817 0.6220 0.0329  0.0381  -0.1242 35  GLU A OE2 
278   N N   . LYS A 36  ? 0.3340 0.3708 0.4890 0.0195  0.0677  -0.0691 36  LYS A N   
279   C CA  . LYS A 36  ? 0.3147 0.3588 0.4742 0.0175  0.0756  -0.0666 36  LYS A CA  
280   C C   . LYS A 36  ? 0.3381 0.3883 0.5038 0.0151  0.0689  -0.0544 36  LYS A C   
281   O O   . LYS A 36  ? 0.3310 0.3859 0.4947 0.0121  0.0729  -0.0518 36  LYS A O   
282   C CB  . LYS A 36  ? 0.3525 0.3924 0.4842 0.0157  0.0853  -0.0706 36  LYS A CB  
283   C CG  . LYS A 36  ? 0.4067 0.4422 0.5296 0.0195  0.0944  -0.0835 36  LYS A CG  
284   C CD  . LYS A 36  ? 0.5151 0.5570 0.6694 0.0228  0.0994  -0.0912 36  LYS A CD  
285   C CE  . LYS A 36  ? 0.4363 0.4889 0.6138 0.0206  0.1080  -0.0873 36  LYS A CE  
286   N NZ  . LYS A 36  ? 0.4722 0.5304 0.6776 0.0245  0.1156  -0.0969 36  LYS A NZ  
287   N N   . GLY A 37  ? 0.3161 0.3661 0.4902 0.0169  0.0592  -0.0473 37  GLY A N   
288   C CA  . GLY A 37  ? 0.2772 0.3331 0.4557 0.0168  0.0521  -0.0366 37  GLY A CA  
289   C C   . GLY A 37  ? 0.2846 0.3383 0.4389 0.0130  0.0497  -0.0324 37  GLY A C   
290   O O   . GLY A 37  ? 0.2634 0.3233 0.4195 0.0123  0.0458  -0.0273 37  GLY A O   
291   N N   . GLY A 38  ? 0.2738 0.3189 0.4071 0.0114  0.0502  -0.0348 38  GLY A N   
292   C CA  . GLY A 38  ? 0.3110 0.3529 0.4228 0.0085  0.0472  -0.0306 38  GLY A CA  
293   C C   . GLY A 38  ? 0.3181 0.3612 0.4307 0.0100  0.0388  -0.0220 38  GLY A C   
294   O O   . GLY A 38  ? 0.2724 0.3177 0.4006 0.0134  0.0357  -0.0178 38  GLY A O   
295   N N   . ILE A 39  ? 0.2508 0.2920 0.3463 0.0077  0.0359  -0.0188 39  ILE A N   
296   C CA  . ILE A 39  ? 0.2675 0.3093 0.3590 0.0093  0.0295  -0.0112 39  ILE A CA  
297   C C   . ILE A 39  ? 0.2723 0.3060 0.3515 0.0084  0.0283  -0.0125 39  ILE A C   
298   O O   . ILE A 39  ? 0.3373 0.3653 0.4027 0.0062  0.0302  -0.0180 39  ILE A O   
299   C CB  . ILE A 39  ? 0.2982 0.3446 0.3818 0.0080  0.0265  -0.0086 39  ILE A CB  
300   C CG1 . ILE A 39  ? 0.3270 0.3830 0.4266 0.0099  0.0249  -0.0082 39  ILE A CG1 
301   C CG2 . ILE A 39  ? 0.3301 0.3763 0.4043 0.0102  0.0211  -0.0019 39  ILE A CG2 
302   C CD1 . ILE A 39  ? 0.3571 0.4184 0.4534 0.0087  0.0208  -0.0087 39  ILE A CD1 
303   N N   . ARG A 40  ? 0.2511 0.2841 0.3364 0.0107  0.0255  -0.0072 40  ARG A N   
304   C CA  . ARG A 40  ? 0.2892 0.3164 0.3688 0.0102  0.0234  -0.0079 40  ARG A CA  
305   C C   . ARG A 40  ? 0.2883 0.3180 0.3618 0.0112  0.0213  0.0002  40  ARG A C   
306   O O   . ARG A 40  ? 0.2719 0.3064 0.3524 0.0143  0.0216  0.0080  40  ARG A O   
307   C CB  . ARG A 40  ? 0.2842 0.3088 0.3833 0.0121  0.0235  -0.0085 40  ARG A CB  
308   C CG  . ARG A 40  ? 0.3166 0.3378 0.4228 0.0121  0.0243  -0.0186 40  ARG A CG  
309   C CD  . ARG A 40  ? 0.3106 0.3279 0.4364 0.0132  0.0224  -0.0212 40  ARG A CD  
310   N NE  . ARG A 40  ? 0.4328 0.4519 0.5830 0.0154  0.0255  -0.0157 40  ARG A NE  
311   C CZ  . ARG A 40  ? 0.3716 0.3888 0.5397 0.0167  0.0265  -0.0232 40  ARG A CZ  
312   N NH1 . ARG A 40  ? 0.3779 0.3923 0.5390 0.0164  0.0251  -0.0374 40  ARG A NH1 
313   N NH2 . ARG A 40  ? 0.3739 0.3918 0.5662 0.0190  0.0292  -0.0161 40  ARG A NH2 
314   N N   . TRP A 41  ? 0.2782 0.3044 0.3389 0.0096  0.0192  -0.0014 41  TRP A N   
315   C CA  . TRP A 41  ? 0.2529 0.2811 0.3100 0.0111  0.0183  0.0051  41  TRP A CA  
316   C C   . TRP A 41  ? 0.2467 0.2699 0.3030 0.0103  0.0166  0.0022  41  TRP A C   
317   O O   . TRP A 41  ? 0.2763 0.2941 0.3280 0.0086  0.0140  -0.0053 41  TRP A O   
318   C CB  . TRP A 41  ? 0.2764 0.3084 0.3194 0.0109  0.0166  0.0060  41  TRP A CB  
319   C CG  . TRP A 41  ? 0.2780 0.3053 0.3087 0.0072  0.0153  -0.0001 41  TRP A CG  
320   C CD1 . TRP A 41  ? 0.2826 0.3085 0.3104 0.0046  0.0171  -0.0045 41  TRP A CD1 
321   C CD2 . TRP A 41  ? 0.3061 0.3290 0.3262 0.0064  0.0131  -0.0014 41  TRP A CD2 
322   N NE1 . TRP A 41  ? 0.3000 0.3196 0.3145 0.0021  0.0165  -0.0071 41  TRP A NE1 
323   C CE2 . TRP A 41  ? 0.3041 0.3219 0.3142 0.0034  0.0132  -0.0055 41  TRP A CE2 
324   C CE3 . TRP A 41  ? 0.2750 0.2978 0.2949 0.0082  0.0119  0.0010  41  TRP A CE3 
325   C CZ2 . TRP A 41  ? 0.2853 0.2967 0.2844 0.0025  0.0109  -0.0069 41  TRP A CZ2 
326   C CZ3 . TRP A 41  ? 0.3436 0.3615 0.3543 0.0071  0.0092  -0.0018 41  TRP A CZ3 
327   C CH2 . TRP A 41  ? 0.3008 0.3127 0.3010 0.0045  0.0081  -0.0055 41  TRP A CH2 
328   N N   . SER A 42  ? 0.2290 0.2539 0.2891 0.0121  0.0180  0.0081  42  SER A N   
329   C CA  . SER A 42  ? 0.2129 0.2342 0.2769 0.0115  0.0161  0.0049  42  SER A CA  
330   C C   . SER A 42  ? 0.2648 0.2882 0.3184 0.0126  0.0165  0.0081  42  SER A C   
331   O O   . SER A 42  ? 0.2703 0.2985 0.3183 0.0151  0.0198  0.0146  42  SER A O   
332   C CB  . SER A 42  ? 0.3218 0.3427 0.4105 0.0124  0.0187  0.0067  42  SER A CB  
333   O OG  . SER A 42  ? 0.4383 0.4632 0.5346 0.0151  0.0256  0.0178  42  SER A OG  
334   N N   . GLY A 43  ? 0.2532 0.2730 0.3062 0.0117  0.0129  0.0032  43  GLY A N   
335   C CA  . GLY A 43  ? 0.2392 0.2601 0.2843 0.0128  0.0130  0.0043  43  GLY A CA  
336   C C   . GLY A 43  ? 0.2594 0.2747 0.3040 0.0119  0.0066  -0.0027 43  GLY A C   
337   O O   . GLY A 43  ? 0.2473 0.2580 0.2934 0.0110  0.0016  -0.0084 43  GLY A O   
338   N N   . SER A 44  ? 0.2526 0.2681 0.2929 0.0130  0.0060  -0.0028 44  SER A N   
339   C CA  . SER A 44  ? 0.2312 0.2416 0.2722 0.0134  -0.0007 -0.0085 44  SER A CA  
340   C C   . SER A 44  ? 0.2439 0.2465 0.2662 0.0121  -0.0067 -0.0121 44  SER A C   
341   O O   . SER A 44  ? 0.2494 0.2512 0.2586 0.0103  -0.0043 -0.0103 44  SER A O   
342   C CB  . SER A 44  ? 0.2426 0.2550 0.2829 0.0152  0.0009  -0.0078 44  SER A CB  
343   O OG  . SER A 44  ? 0.2448 0.2517 0.2846 0.0161  -0.0064 -0.0127 44  SER A OG  
344   N N   . ALA A 45  ? 0.2387 0.2356 0.2607 0.0136  -0.0143 -0.0170 45  ALA A N   
345   C CA  . ALA A 45  ? 0.2565 0.2443 0.2579 0.0139  -0.0191 -0.0183 45  ALA A CA  
346   C C   . ALA A 45  ? 0.3103 0.2963 0.3030 0.0130  -0.0167 -0.0151 45  ALA A C   
347   O O   . ALA A 45  ? 0.3156 0.2939 0.2928 0.0122  -0.0173 -0.0139 45  ALA A O   
348   C CB  . ALA A 45  ? 0.2740 0.2560 0.2756 0.0176  -0.0290 -0.0232 45  ALA A CB  
349   N N   . TRP A 46  ? 0.2555 0.2475 0.2581 0.0136  -0.0137 -0.0142 46  TRP A N   
350   C CA  . TRP A 46  ? 0.2786 0.2696 0.2747 0.0132  -0.0120 -0.0135 46  TRP A CA  
351   C C   . TRP A 46  ? 0.2921 0.2891 0.2844 0.0112  -0.0062 -0.0115 46  TRP A C   
352   O O   . TRP A 46  ? 0.2460 0.2441 0.2353 0.0113  -0.0054 -0.0128 46  TRP A O   
353   C CB  . TRP A 46  ? 0.2680 0.2628 0.2757 0.0161  -0.0119 -0.0152 46  TRP A CB  
354   C CG  . TRP A 46  ? 0.2573 0.2453 0.2683 0.0184  -0.0194 -0.0179 46  TRP A CG  
355   C CD1 . TRP A 46  ? 0.2692 0.2464 0.2683 0.0190  -0.0264 -0.0180 46  TRP A CD1 
356   C CD2 . TRP A 46  ? 0.2657 0.2571 0.2936 0.0216  -0.0209 -0.0207 46  TRP A CD2 
357   N NE1 . TRP A 46  ? 0.2895 0.2629 0.2961 0.0230  -0.0339 -0.0207 46  TRP A NE1 
358   C CE2 . TRP A 46  ? 0.2773 0.2598 0.3035 0.0242  -0.0307 -0.0231 46  TRP A CE2 
359   C CE3 . TRP A 46  ? 0.2457 0.2465 0.2891 0.0231  -0.0138 -0.0209 46  TRP A CE3 
360   C CZ2 . TRP A 46  ? 0.2873 0.2710 0.3307 0.0279  -0.0352 -0.0268 46  TRP A CZ2 
361   C CZ3 . TRP A 46  ? 0.2291 0.2313 0.2897 0.0262  -0.0160 -0.0244 46  TRP A CZ3 
362   C CH2 . TRP A 46  ? 0.2882 0.2824 0.3505 0.0284  -0.0273 -0.0279 46  TRP A CH2 
363   N N   . ALA A 47  ? 0.2283 0.2302 0.2231 0.0103  -0.0031 -0.0094 47  ALA A N   
364   C CA  . ALA A 47  ? 0.2325 0.2399 0.2239 0.0092  0.0004  -0.0079 47  ALA A CA  
365   C C   . ALA A 47  ? 0.2583 0.2600 0.2417 0.0061  -0.0007 -0.0097 47  ALA A C   
366   O O   . ALA A 47  ? 0.2842 0.2772 0.2619 0.0047  -0.0021 -0.0097 47  ALA A O   
367   C CB  . ALA A 47  ? 0.2584 0.2699 0.2551 0.0088  0.0032  -0.0052 47  ALA A CB  
368   N N   . LEU A 48  ? 0.2616 0.2683 0.2451 0.0056  0.0001  -0.0111 48  LEU A N   
369   C CA  . LEU A 48  ? 0.2741 0.2763 0.2564 0.0020  0.0001  -0.0131 48  LEU A CA  
370   C C   . LEU A 48  ? 0.2585 0.2630 0.2431 -0.0005 0.0034  -0.0116 48  LEU A C   
371   O O   . LEU A 48  ? 0.2540 0.2659 0.2447 -0.0009 0.0036  -0.0133 48  LEU A O   
372   C CB  . LEU A 48  ? 0.2751 0.2817 0.2605 0.0028  -0.0022 -0.0181 48  LEU A CB  
373   C CG  . LEU A 48  ? 0.2989 0.2972 0.2838 0.0027  -0.0044 -0.0207 48  LEU A CG  
374   C CD1 . LEU A 48  ? 0.2854 0.2827 0.2681 0.0065  -0.0054 -0.0194 48  LEU A CD1 
375   C CD2 . LEU A 48  ? 0.2903 0.2916 0.2805 0.0032  -0.0073 -0.0281 48  LEU A CD2 
376   N N   . ASP A 49  ? 0.2833 0.2810 0.2630 -0.0015 0.0055  -0.0094 49  ASP A N   
377   C CA  . ASP A 49  ? 0.2708 0.2706 0.2525 -0.0028 0.0094  -0.0086 49  ASP A CA  
378   C C   . ASP A 49  ? 0.2742 0.2737 0.2603 -0.0065 0.0142  -0.0091 49  ASP A C   
379   O O   . ASP A 49  ? 0.2836 0.2879 0.2757 -0.0072 0.0176  -0.0094 49  ASP A O   
380   C CB  . ASP A 49  ? 0.3291 0.3218 0.3026 -0.0014 0.0093  -0.0080 49  ASP A CB  
381   C CG  . ASP A 49  ? 0.3309 0.3120 0.2918 -0.0012 0.0083  -0.0069 49  ASP A CG  
382   O OD1 . ASP A 49  ? 0.3744 0.3527 0.3338 0.0010  0.0031  -0.0072 49  ASP A OD1 
383   O OD2 . ASP A 49  ? 0.3226 0.2968 0.2743 -0.0020 0.0128  -0.0054 49  ASP A OD2 
384   N N   . ALA A 50  ? 0.2638 0.2588 0.2515 -0.0090 0.0148  -0.0098 50  ALA A N   
385   C CA  . ALA A 50  ? 0.2506 0.2480 0.2502 -0.0129 0.0196  -0.0112 50  ALA A CA  
386   C C   . ALA A 50  ? 0.2358 0.2469 0.2495 -0.0121 0.0157  -0.0156 50  ALA A C   
387   O O   . ALA A 50  ? 0.2584 0.2739 0.2860 -0.0149 0.0193  -0.0175 50  ALA A O   
388   C CB  . ALA A 50  ? 0.2339 0.2238 0.2383 -0.0160 0.0207  -0.0117 50  ALA A CB  
389   N N   . ILE A 51  ? 0.2545 0.2724 0.2659 -0.0080 0.0088  -0.0173 51  ILE A N   
390   C CA  . ILE A 51  ? 0.2393 0.2696 0.2602 -0.0055 0.0040  -0.0208 51  ILE A CA  
391   C C   . ILE A 51  ? 0.2385 0.2736 0.2640 -0.0045 0.0069  -0.0177 51  ILE A C   
392   O O   . ILE A 51  ? 0.2666 0.3082 0.3063 -0.0057 0.0071  -0.0205 51  ILE A O   
393   C CB  . ILE A 51  ? 0.2265 0.2623 0.2394 0.0003  -0.0025 -0.0220 51  ILE A CB  
394   C CG1 . ILE A 51  ? 0.2771 0.3091 0.2888 -0.0003 -0.0058 -0.0275 51  ILE A CG1 
395   C CG2 . ILE A 51  ? 0.2743 0.3224 0.2926 0.0048  -0.0079 -0.0242 51  ILE A CG2 
396   C CD1 . ILE A 51  ? 0.2675 0.3046 0.2924 -0.0016 -0.0103 -0.0356 51  ILE A CD1 
397   N N   . PRO A 52  ? 0.2768 0.3095 0.2946 -0.0023 0.0089  -0.0130 52  PRO A N   
398   C CA  . PRO A 52  ? 0.2855 0.3213 0.3106 -0.0018 0.0123  -0.0112 52  PRO A CA  
399   C C   . PRO A 52  ? 0.2931 0.3254 0.3241 -0.0062 0.0193  -0.0131 52  PRO A C   
400   O O   . PRO A 52  ? 0.2916 0.3300 0.3354 -0.0061 0.0215  -0.0142 52  PRO A O   
401   C CB  . PRO A 52  ? 0.2991 0.3303 0.3167 0.0004  0.0132  -0.0076 52  PRO A CB  
402   C CG  . PRO A 52  ? 0.3195 0.3495 0.3291 0.0025  0.0097  -0.0063 52  PRO A CG  
403   C CD  . PRO A 52  ? 0.2556 0.2837 0.2624 0.0000  0.0078  -0.0101 52  PRO A CD  
404   N N   . ALA A 53  ? 0.2766 0.2993 0.2996 -0.0097 0.0237  -0.0131 53  ALA A N   
405   C CA  . ALA A 53  ? 0.2981 0.3166 0.3247 -0.0133 0.0330  -0.0133 53  ALA A CA  
406   C C   . ALA A 53  ? 0.2905 0.3172 0.3392 -0.0163 0.0349  -0.0167 53  ALA A C   
407   O O   . ALA A 53  ? 0.2967 0.3233 0.3547 -0.0188 0.0441  -0.0171 53  ALA A O   
408   C CB  . ALA A 53  ? 0.2671 0.2725 0.2788 -0.0151 0.0372  -0.0104 53  ALA A CB  
409   N N   . GLY A 54  ? 0.2435 0.2774 0.3015 -0.0155 0.0264  -0.0201 54  GLY A N   
410   C CA  . GLY A 54  ? 0.2378 0.2807 0.3203 -0.0178 0.0261  -0.0253 54  GLY A CA  
411   C C   . GLY A 54  ? 0.2456 0.2988 0.3413 -0.0151 0.0253  -0.0266 54  GLY A C   
412   O O   . GLY A 54  ? 0.2668 0.3284 0.3861 -0.0166 0.0249  -0.0314 54  GLY A O   
413   N N   . LEU A 55  ? 0.2483 0.3011 0.3323 -0.0110 0.0243  -0.0228 55  LEU A N   
414   C CA  . LEU A 55  ? 0.2515 0.3127 0.3481 -0.0077 0.0233  -0.0230 55  LEU A CA  
415   C C   . LEU A 55  ? 0.2959 0.3537 0.3976 -0.0100 0.0350  -0.0231 55  LEU A C   
416   O O   . LEU A 55  ? 0.2715 0.3356 0.3865 -0.0074 0.0355  -0.0240 55  LEU A O   
417   C CB  . LEU A 55  ? 0.2629 0.3244 0.3471 -0.0019 0.0172  -0.0182 55  LEU A CB  
418   C CG  . LEU A 55  ? 0.2827 0.3483 0.3585 0.0027  0.0070  -0.0169 55  LEU A CG  
419   C CD1 . LEU A 55  ? 0.2582 0.3230 0.3254 0.0082  0.0057  -0.0099 55  LEU A CD1 
420   C CD2 . LEU A 55  ? 0.2662 0.3431 0.3564 0.0055  -0.0014 -0.0216 55  LEU A CD2 
421   N N   . GLY A 56  ? 0.3013 0.3490 0.3921 -0.0140 0.0447  -0.0221 56  GLY A N   
422   C CA  . GLY A 56  ? 0.2716 0.3163 0.3645 -0.0152 0.0570  -0.0229 56  GLY A CA  
423   C C   . GLY A 56  ? 0.3263 0.3578 0.3923 -0.0149 0.0631  -0.0202 56  GLY A C   
424   O O   . GLY A 56  ? 0.3230 0.3486 0.3715 -0.0135 0.0561  -0.0178 56  GLY A O   
425   N N   . GLU A 57  ? 0.3400 0.3673 0.4027 -0.0155 0.0758  -0.0210 57  GLU A N   
426   C CA  . GLU A 57  ? 0.3918 0.4070 0.4265 -0.0133 0.0812  -0.0197 57  GLU A CA  
427   C C   . GLU A 57  ? 0.3973 0.4124 0.4242 -0.0084 0.0753  -0.0237 57  GLU A C   
428   O O   . GLU A 57  ? 0.4408 0.4465 0.4441 -0.0055 0.0755  -0.0245 57  GLU A O   
429   C CB  . GLU A 57  ? 0.3990 0.4098 0.4303 -0.0143 0.0983  -0.0195 57  GLU A CB  
430   C CG  . GLU A 57  ? 0.5106 0.5242 0.5622 -0.0197 0.1081  -0.0169 57  GLU A CG  
431   C CD  . GLU A 57  ? 0.5583 0.5609 0.5956 -0.0222 0.1092  -0.0101 57  GLU A CD  
432   O OE1 . GLU A 57  ? 0.6445 0.6438 0.6923 -0.0264 0.1218  -0.0060 57  GLU A OE1 
433   O OE2 . GLU A 57  ? 0.5732 0.5703 0.5916 -0.0198 0.0977  -0.0086 57  GLU A OE2 
434   N N   . ASP A 58  ? 0.3108 0.3354 0.3575 -0.0070 0.0695  -0.0262 58  ASP A N   
435   C CA  . ASP A 58  ? 0.3249 0.3495 0.3714 -0.0028 0.0647  -0.0298 58  ASP A CA  
436   C C   . ASP A 58  ? 0.3228 0.3496 0.3723 -0.0015 0.0524  -0.0263 58  ASP A C   
437   O O   . ASP A 58  ? 0.2993 0.3313 0.3639 0.0010  0.0482  -0.0264 58  ASP A O   
438   C CB  . ASP A 58  ? 0.3245 0.3568 0.3931 -0.0014 0.0696  -0.0343 58  ASP A CB  
439   C CG  . ASP A 58  ? 0.3273 0.3711 0.4217 -0.0023 0.0652  -0.0317 58  ASP A CG  
440   O OD1 . ASP A 58  ? 0.3194 0.3653 0.4144 -0.0052 0.0625  -0.0283 58  ASP A OD1 
441   O OD2 . ASP A 58  ? 0.3043 0.3548 0.4189 0.0004  0.0640  -0.0338 58  ASP A OD2 
442   N N   . VAL A 59  ? 0.2468 0.3096 0.4168 0.0033  0.0553  -0.0546 59  VAL A N   
443   C CA  . VAL A 59  ? 0.2334 0.2931 0.3930 0.0065  0.0425  -0.0469 59  VAL A CA  
444   C C   . VAL A 59  ? 0.2759 0.3248 0.4076 0.0043  0.0440  -0.0448 59  VAL A C   
445   O O   . VAL A 59  ? 0.2841 0.3285 0.3990 -0.0007 0.0485  -0.0443 59  VAL A O   
446   C CB  . VAL A 59  ? 0.2908 0.3545 0.4513 0.0053  0.0353  -0.0422 59  VAL A CB  
447   C CG1 . VAL A 59  ? 0.2665 0.3254 0.4137 0.0078  0.0233  -0.0347 59  VAL A CG1 
448   C CG2 . VAL A 59  ? 0.2395 0.3143 0.4296 0.0070  0.0331  -0.0447 59  VAL A CG2 
449   N N   . TYR A 60  ? 0.2370 0.2814 0.3642 0.0077  0.0398  -0.0433 60  TYR A N   
450   C CA  . TYR A 60  ? 0.2623 0.2971 0.3667 0.0058  0.0413  -0.0424 60  TYR A CA  
451   C C   . TYR A 60  ? 0.2959 0.3279 0.3907 0.0083  0.0308  -0.0358 60  TYR A C   
452   O O   . TYR A 60  ? 0.2723 0.3058 0.3768 0.0125  0.0243  -0.0340 60  TYR A O   
453   C CB  . TYR A 60  ? 0.2705 0.3016 0.3778 0.0068  0.0473  -0.0478 60  TYR A CB  
454   C CG  . TYR A 60  ? 0.2805 0.3149 0.4003 0.0043  0.0592  -0.0554 60  TYR A CG  
455   C CD1 . TYR A 60  ? 0.3394 0.3684 0.4441 -0.0023 0.0691  -0.0587 60  TYR A CD1 
456   C CD2 . TYR A 60  ? 0.3143 0.3566 0.4615 0.0083  0.0606  -0.0595 60  TYR A CD2 
457   C CE1 . TYR A 60  ? 0.3630 0.3946 0.4790 -0.0054 0.0816  -0.0664 60  TYR A CE1 
458   C CE2 . TYR A 60  ? 0.3397 0.3861 0.5015 0.0060  0.0727  -0.0675 60  TYR A CE2 
459   C CZ  . TYR A 60  ? 0.3654 0.4065 0.5111 -0.0012 0.0839  -0.0711 60  TYR A CZ  
460   O OH  . TYR A 60  ? 0.4160 0.4603 0.5753 -0.0043 0.0973  -0.0796 60  TYR A OH  
461   N N   . SER A 61  ? 0.2669 0.2937 0.3427 0.0055  0.0292  -0.0323 61  SER A N   
462   C CA  . SER A 61  ? 0.2591 0.2828 0.3252 0.0072  0.0211  -0.0270 61  SER A CA  
463   C C   . SER A 61  ? 0.2585 0.2755 0.3132 0.0071  0.0213  -0.0274 61  SER A C   
464   O O   . SER A 61  ? 0.2664 0.2791 0.3150 0.0046  0.0277  -0.0313 61  SER A O   
465   C CB  . SER A 61  ? 0.2731 0.2952 0.3274 0.0047  0.0189  -0.0231 61  SER A CB  
466   O OG  . SER A 61  ? 0.2836 0.2990 0.3224 0.0010  0.0232  -0.0241 61  SER A OG  
467   N N   . LEU A 62  ? 0.2266 0.2423 0.2783 0.0092  0.0146  -0.0236 62  LEU A N   
468   C CA  . LEU A 62  ? 0.2218 0.2315 0.2609 0.0084  0.0128  -0.0226 62  LEU A CA  
469   C C   . LEU A 62  ? 0.2622 0.2718 0.2948 0.0084  0.0073  -0.0178 62  LEU A C   
470   O O   . LEU A 62  ? 0.2557 0.2677 0.2937 0.0104  0.0027  -0.0151 62  LEU A O   
471   C CB  . LEU A 62  ? 0.2583 0.2665 0.3027 0.0110  0.0109  -0.0235 62  LEU A CB  
472   C CG  . LEU A 62  ? 0.2367 0.2392 0.2693 0.0097  0.0090  -0.0227 62  LEU A CG  
473   C CD1 . LEU A 62  ? 0.2625 0.2594 0.2852 0.0062  0.0147  -0.0268 62  LEU A CD1 
474   C CD2 . LEU A 62  ? 0.2488 0.2500 0.2866 0.0121  0.0057  -0.0223 62  LEU A CD2 
475   N N   . THR A 63  ? 0.2663 0.2725 0.2875 0.0058  0.0076  -0.0167 63  THR A N   
476   C CA  . THR A 63  ? 0.2610 0.2671 0.2780 0.0061  0.0029  -0.0128 63  THR A CA  
477   C C   . THR A 63  ? 0.2553 0.2592 0.2692 0.0068  -0.0009 -0.0116 63  THR A C   
478   O O   . THR A 63  ? 0.2504 0.2504 0.2588 0.0056  -0.0005 -0.0131 63  THR A O   
479   C CB  . THR A 63  ? 0.2596 0.2626 0.2675 0.0034  0.0040  -0.0119 63  THR A CB  
480   O OG1 . THR A 63  ? 0.2667 0.2635 0.2644 0.0006  0.0064  -0.0138 63  THR A OG1 
481   C CG2 . THR A 63  ? 0.2814 0.2877 0.2944 0.0025  0.0076  -0.0129 63  THR A CG2 
482   N N   . GLY A 64  ? 0.2521 0.2582 0.2696 0.0083  -0.0043 -0.0091 64  GLY A N   
483   C CA  . GLY A 64  ? 0.2430 0.2481 0.2609 0.0089  -0.0069 -0.0086 64  GLY A CA  
484   C C   . GLY A 64  ? 0.2535 0.2560 0.2657 0.0077  -0.0092 -0.0080 64  GLY A C   
485   O O   . GLY A 64  ? 0.2578 0.2584 0.2686 0.0071  -0.0104 -0.0090 64  GLY A O   
486   N N   . GLU A 65  ? 0.2235 0.2257 0.2329 0.0073  -0.0105 -0.0064 65  GLU A N   
487   C CA  . GLU A 65  ? 0.2502 0.2502 0.2567 0.0066  -0.0143 -0.0055 65  GLU A CA  
488   C C   . GLU A 65  ? 0.2711 0.2652 0.2678 0.0042  -0.0150 -0.0066 65  GLU A C   
489   O O   . GLU A 65  ? 0.2618 0.2537 0.2567 0.0033  -0.0185 -0.0068 65  GLU A O   
490   C CB  . GLU A 65  ? 0.2706 0.2708 0.2779 0.0073  -0.0161 -0.0034 65  GLU A CB  
491   C CG  . GLU A 65  ? 0.2431 0.2474 0.2573 0.0087  -0.0145 -0.0027 65  GLU A CG  
492   C CD  . GLU A 65  ? 0.2561 0.2611 0.2694 0.0086  -0.0114 -0.0027 65  GLU A CD  
493   O OE1 . GLU A 65  ? 0.2853 0.2889 0.2946 0.0076  -0.0096 -0.0036 65  GLU A OE1 
494   O OE2 . GLU A 65  ? 0.2517 0.2585 0.2684 0.0091  -0.0106 -0.0021 65  GLU A OE2 
495   N N   . PRO A 66  ? 0.2505 0.2412 0.2401 0.0024  -0.0117 -0.0075 66  PRO A N   
496   C CA  . PRO A 66  ? 0.2583 0.2415 0.2359 -0.0010 -0.0114 -0.0091 66  PRO A CA  
497   C C   . PRO A 66  ? 0.2771 0.2595 0.2553 -0.0014 -0.0094 -0.0121 66  PRO A C   
498   O O   . PRO A 66  ? 0.3000 0.2763 0.2693 -0.0041 -0.0118 -0.0128 66  PRO A O   
499   C CB  . PRO A 66  ? 0.3135 0.2939 0.2848 -0.0032 -0.0061 -0.0102 66  PRO A CB  
500   C CG  . PRO A 66  ? 0.2405 0.2261 0.2192 -0.0009 -0.0067 -0.0077 66  PRO A CG  
501   C CD  . PRO A 66  ? 0.2754 0.2681 0.2665 0.0026  -0.0078 -0.0075 66  PRO A CD  
502   N N   . TYR A 67  ? 0.2711 0.2587 0.2592 0.0009  -0.0058 -0.0137 67  TYR A N   
503   C CA  . TYR A 67  ? 0.2419 0.2280 0.2316 0.0010  -0.0042 -0.0165 67  TYR A CA  
504   C C   . TYR A 67  ? 0.2618 0.2476 0.2522 0.0010  -0.0096 -0.0152 67  TYR A C   
505   O O   . TYR A 67  ? 0.2764 0.2569 0.2602 -0.0013 -0.0107 -0.0169 67  TYR A O   
506   C CB  . TYR A 67  ? 0.2432 0.2344 0.2446 0.0039  -0.0007 -0.0178 67  TYR A CB  
507   C CG  . TYR A 67  ? 0.2429 0.2318 0.2470 0.0044  0.0003  -0.0204 67  TYR A CG  
508   C CD1 . TYR A 67  ? 0.2986 0.2818 0.2966 0.0022  0.0047  -0.0246 67  TYR A CD1 
509   C CD2 . TYR A 67  ? 0.2571 0.2480 0.2679 0.0064  -0.0029 -0.0188 67  TYR A CD2 
510   C CE1 . TYR A 67  ? 0.2689 0.2489 0.2692 0.0027  0.0058  -0.0273 67  TYR A CE1 
511   C CE2 . TYR A 67  ? 0.2592 0.2467 0.2719 0.0067  -0.0023 -0.0210 67  TYR A CE2 
512   C CZ  . TYR A 67  ? 0.2958 0.2780 0.3035 0.0051  0.0019  -0.0253 67  TYR A CZ  
513   O OH  . TYR A 67  ? 0.2958 0.2738 0.3049 0.0052  0.0025  -0.0278 67  TYR A OH  
514   N N   . ALA A 68  ? 0.2504 0.2414 0.2486 0.0030  -0.0128 -0.0124 68  ALA A N   
515   C CA  . ALA A 68  ? 0.2814 0.2733 0.2827 0.0027  -0.0172 -0.0115 68  ALA A CA  
516   C C   . ALA A 68  ? 0.2726 0.2602 0.2666 0.0002  -0.0221 -0.0109 68  ALA A C   
517   O O   . ALA A 68  ? 0.2972 0.2831 0.2909 -0.0013 -0.0254 -0.0116 68  ALA A O   
518   C CB  . ALA A 68  ? 0.2336 0.2314 0.2442 0.0047  -0.0182 -0.0092 68  ALA A CB  
519   N N   . ALA A 69  ? 0.2554 0.2406 0.2433 -0.0004 -0.0236 -0.0094 69  ALA A N   
520   C CA  . ALA A 69  ? 0.2661 0.2451 0.2453 -0.0032 -0.0299 -0.0083 69  ALA A CA  
521   C C   . ALA A 69  ? 0.2689 0.2395 0.2348 -0.0071 -0.0289 -0.0109 69  ALA A C   
522   O O   . ALA A 69  ? 0.3113 0.2770 0.2716 -0.0098 -0.0348 -0.0107 69  ALA A O   
523   C CB  . ALA A 69  ? 0.2865 0.2623 0.2596 -0.0035 -0.0317 -0.0059 69  ALA A CB  
524   N N   . ALA A 70  ? 0.2814 0.2501 0.2433 -0.0076 -0.0214 -0.0138 70  ALA A N   
525   C CA  . ALA A 70  ? 0.2966 0.2568 0.2464 -0.0115 -0.0185 -0.0174 70  ALA A CA  
526   C C   . ALA A 70  ? 0.3018 0.2628 0.2566 -0.0113 -0.0201 -0.0191 70  ALA A C   
527   O O   . ALA A 70  ? 0.3512 0.3044 0.2953 -0.0152 -0.0224 -0.0207 70  ALA A O   
528   C CB  . ALA A 70  ? 0.3152 0.2749 0.2640 -0.0115 -0.0089 -0.0208 70  ALA A CB  
529   N N   . VAL A 71  ? 0.3028 0.2720 0.2723 -0.0074 -0.0191 -0.0185 71  VAL A N   
530   C CA  . VAL A 71  ? 0.2727 0.2422 0.2470 -0.0076 -0.0210 -0.0197 71  VAL A CA  
531   C C   . VAL A 71  ? 0.2892 0.2590 0.2637 -0.0095 -0.0293 -0.0175 71  VAL A C   
532   O O   . VAL A 71  ? 0.3212 0.2865 0.2916 -0.0125 -0.0324 -0.0189 71  VAL A O   
533   C CB  . VAL A 71  ? 0.2479 0.2247 0.2359 -0.0038 -0.0185 -0.0189 71  VAL A CB  
534   C CG1 . VAL A 71  ? 0.2830 0.2596 0.2756 -0.0046 -0.0206 -0.0195 71  VAL A CG1 
535   C CG2 . VAL A 71  ? 0.3150 0.2914 0.3051 -0.0017 -0.0115 -0.0213 71  VAL A CG2 
536   N N   . ALA A 72  ? 0.3150 0.2902 0.2961 -0.0078 -0.0331 -0.0142 72  ALA A N   
537   C CA  . ALA A 72  ? 0.3059 0.2823 0.2908 -0.0090 -0.0415 -0.0123 72  ALA A CA  
538   C C   . ALA A 72  ? 0.3571 0.3238 0.3276 -0.0136 -0.0476 -0.0125 72  ALA A C   
539   O O   . ALA A 72  ? 0.3804 0.3470 0.3541 -0.0155 -0.0550 -0.0119 72  ALA A O   
540   C CB  . ALA A 72  ? 0.3200 0.3021 0.3136 -0.0062 -0.0440 -0.0092 72  ALA A CB  
541   N N   . HIS A 73  ? 0.3293 0.2872 0.2835 -0.0160 -0.0447 -0.0134 73  HIS A N   
542   C CA  . HIS A 73  ? 0.4124 0.3582 0.3486 -0.0216 -0.0500 -0.0139 73  HIS A CA  
543   C C   . HIS A 73  ? 0.4065 0.3482 0.3391 -0.0246 -0.0499 -0.0172 73  HIS A C   
544   O O   . HIS A 73  ? 0.4531 0.3868 0.3752 -0.0293 -0.0575 -0.0171 73  HIS A O   
545   C CB  . HIS A 73  ? 0.4826 0.4192 0.4013 -0.0242 -0.0441 -0.0152 73  HIS A CB  
546   C CG  . HIS A 73  ? 0.5058 0.4276 0.4020 -0.0310 -0.0494 -0.0152 73  HIS A CG  
547   N ND1 . HIS A 73  ? 0.5853 0.5010 0.4731 -0.0330 -0.0588 -0.0109 73  HIS A ND1 
548   C CD2 . HIS A 73  ? 0.5184 0.4287 0.3975 -0.0366 -0.0469 -0.0189 73  HIS A CD2 
549   C CE1 . HIS A 73  ? 0.5469 0.4475 0.4118 -0.0400 -0.0622 -0.0116 73  HIS A CE1 
550   N NE2 . HIS A 73  ? 0.5802 0.4772 0.4391 -0.0425 -0.0548 -0.0168 73  HIS A NE2 
551   N N   . ASP A 74  ? 0.4282 0.3741 0.3685 -0.0223 -0.0422 -0.0202 74  ASP A N   
552   C CA  . ASP A 74  ? 0.3773 0.3195 0.3161 -0.0247 -0.0414 -0.0235 74  ASP A CA  
553   C C   . ASP A 74  ? 0.3683 0.3203 0.3251 -0.0225 -0.0454 -0.0217 74  ASP A C   
554   O O   . ASP A 74  ? 0.3577 0.3165 0.3264 -0.0189 -0.0402 -0.0220 74  ASP A O   
555   C CB  . ASP A 74  ? 0.4168 0.3566 0.3540 -0.0234 -0.0307 -0.0276 74  ASP A CB  
556   C CG  . ASP A 74  ? 0.4114 0.3469 0.3484 -0.0252 -0.0291 -0.0312 74  ASP A CG  
557   O OD1 . ASP A 74  ? 0.4678 0.4036 0.4074 -0.0273 -0.0357 -0.0304 74  ASP A OD1 
558   O OD2 . ASP A 74  ? 0.5013 0.4328 0.4362 -0.0245 -0.0212 -0.0351 74  ASP A OD2 
559   N N   . ARG A 75  ? 0.3799 0.3320 0.3383 -0.0251 -0.0551 -0.0200 75  ARG A N   
560   C CA  . ARG A 75  ? 0.3651 0.3274 0.3423 -0.0236 -0.0589 -0.0185 75  ARG A CA  
561   C C   . ARG A 75  ? 0.3400 0.3042 0.3238 -0.0233 -0.0531 -0.0211 75  ARG A C   
562   O O   . ARG A 75  ? 0.3328 0.3056 0.3309 -0.0203 -0.0498 -0.0202 75  ARG A O   
563   C CB  . ARG A 75  ? 0.3961 0.3563 0.3732 -0.0275 -0.0705 -0.0173 75  ARG A CB  
564   C CG  . ARG A 75  ? 0.4602 0.4255 0.4456 -0.0253 -0.0779 -0.0135 75  ARG A CG  
565   C CD  . ARG A 75  ? 0.5327 0.4923 0.5052 -0.0242 -0.0768 -0.0116 75  ARG A CD  
566   N NE  . ARG A 75  ? 0.5684 0.5249 0.5391 -0.0251 -0.0879 -0.0080 75  ARG A NE  
567   C CZ  . ARG A 75  ? 0.6179 0.5623 0.5682 -0.0282 -0.0914 -0.0065 75  ARG A CZ  
568   N NH1 . ARG A 75  ? 0.5899 0.5250 0.5208 -0.0307 -0.0834 -0.0088 75  ARG A NH1 
569   N NH2 . ARG A 75  ? 0.6064 0.5473 0.5561 -0.0289 -0.1031 -0.0026 75  ARG A NH2 
570   N N   . LYS A 76  ? 0.3470 0.3019 0.3189 -0.0265 -0.0511 -0.0243 76  LYS A N   
571   C CA  . LYS A 76  ? 0.3389 0.2937 0.3159 -0.0265 -0.0465 -0.0266 76  LYS A CA  
572   C C   . LYS A 76  ? 0.3667 0.3247 0.3492 -0.0217 -0.0381 -0.0265 76  LYS A C   
573   O O   . LYS A 76  ? 0.3672 0.3299 0.3605 -0.0203 -0.0361 -0.0258 76  LYS A O   
574   C CB  . LYS A 76  ? 0.3582 0.3008 0.3205 -0.0310 -0.0461 -0.0305 76  LYS A CB  
575   C CG  . LYS A 76  ? 0.4549 0.3943 0.4194 -0.0300 -0.0392 -0.0333 76  LYS A CG  
576   C CD  . LYS A 76  ? 0.5299 0.4724 0.5043 -0.0319 -0.0420 -0.0330 76  LYS A CD  
577   C CE  . LYS A 76  ? 0.6106 0.5437 0.5802 -0.0333 -0.0372 -0.0368 76  LYS A CE  
578   N NZ  . LYS A 76  ? 0.6141 0.5389 0.5749 -0.0311 -0.0296 -0.0402 76  LYS A NZ  
579   N N   . PHE A 77  ? 0.3189 0.2738 0.2941 -0.0197 -0.0333 -0.0274 77  PHE A N   
580   C CA  . PHE A 77  ? 0.3129 0.2711 0.2947 -0.0151 -0.0266 -0.0272 77  PHE A CA  
581   C C   . PHE A 77  ? 0.3088 0.2769 0.3023 -0.0121 -0.0277 -0.0233 77  PHE A C   
582   O O   . PHE A 77  ? 0.2902 0.2616 0.2916 -0.0096 -0.0247 -0.0224 77  PHE A O   
583   C CB  . PHE A 77  ? 0.3372 0.2914 0.3113 -0.0139 -0.0212 -0.0291 77  PHE A CB  
584   C CG  . PHE A 77  ? 0.3512 0.3085 0.3334 -0.0093 -0.0152 -0.0294 77  PHE A CG  
585   C CD1 . PHE A 77  ? 0.3368 0.2930 0.3261 -0.0077 -0.0135 -0.0301 77  PHE A CD1 
586   C CD2 . PHE A 77  ? 0.3515 0.3115 0.3342 -0.0071 -0.0118 -0.0290 77  PHE A CD2 
587   C CE1 . PHE A 77  ? 0.3169 0.2750 0.3140 -0.0035 -0.0098 -0.0299 77  PHE A CE1 
588   C CE2 . PHE A 77  ? 0.3194 0.2826 0.3112 -0.0030 -0.0075 -0.0291 77  PHE A CE2 
589   C CZ  . PHE A 77  ? 0.3716 0.3336 0.3707 -0.0011 -0.0070 -0.0295 77  PHE A CZ  
590   N N   . ALA A 78  ? 0.2905 0.2625 0.2845 -0.0124 -0.0321 -0.0212 78  ALA A N   
591   C CA  . ALA A 78  ? 0.2968 0.2776 0.3021 -0.0097 -0.0323 -0.0182 78  ALA A CA  
592   C C   . ALA A 78  ? 0.2906 0.2757 0.3066 -0.0106 -0.0329 -0.0179 78  ALA A C   
593   O O   . ALA A 78  ? 0.2807 0.2702 0.3039 -0.0088 -0.0295 -0.0166 78  ALA A O   
594   C CB  . ALA A 78  ? 0.2792 0.2623 0.2839 -0.0098 -0.0374 -0.0162 78  ALA A CB  
595   N N   A LYS A 79  ? 0.2863 0.2699 0.3030 -0.0142 -0.0372 -0.0190 79  LYS A N   
596   N N   B LYS A 79  ? 0.2861 0.2698 0.3031 -0.0142 -0.0372 -0.0190 79  LYS A N   
597   C CA  A LYS A 79  ? 0.3087 0.2960 0.3357 -0.0161 -0.0371 -0.0192 79  LYS A CA  
598   C CA  B LYS A 79  ? 0.3086 0.2961 0.3359 -0.0160 -0.0369 -0.0192 79  LYS A CA  
599   C C   A LYS A 79  ? 0.3178 0.3013 0.3433 -0.0156 -0.0313 -0.0198 79  LYS A C   
600   C C   B LYS A 79  ? 0.3178 0.3013 0.3433 -0.0155 -0.0312 -0.0198 79  LYS A C   
601   O O   A LYS A 79  ? 0.2874 0.2742 0.3199 -0.0156 -0.0283 -0.0187 79  LYS A O   
602   O O   B LYS A 79  ? 0.2873 0.2741 0.3197 -0.0153 -0.0281 -0.0186 79  LYS A O   
603   C CB  A LYS A 79  ? 0.3276 0.3129 0.3549 -0.0205 -0.0430 -0.0208 79  LYS A CB  
604   C CB  B LYS A 79  ? 0.3271 0.3129 0.3552 -0.0204 -0.0428 -0.0207 79  LYS A CB  
605   C CG  A LYS A 79  ? 0.3673 0.3528 0.4010 -0.0235 -0.0413 -0.0220 79  LYS A CG  
606   C CG  B LYS A 79  ? 0.3670 0.3539 0.4027 -0.0232 -0.0407 -0.0217 79  LYS A CG  
607   C CD  A LYS A 79  ? 0.3917 0.3795 0.4320 -0.0280 -0.0481 -0.0231 79  LYS A CD  
608   C CD  B LYS A 79  ? 0.3934 0.3809 0.4339 -0.0280 -0.0468 -0.0232 79  LYS A CD  
609   C CE  A LYS A 79  ? 0.4170 0.4032 0.4615 -0.0319 -0.0458 -0.0248 79  LYS A CE  
610   C CE  B LYS A 79  ? 0.4079 0.3952 0.4545 -0.0312 -0.0430 -0.0244 79  LYS A CE  
611   N NZ  A LYS A 79  ? 0.3549 0.3307 0.3870 -0.0349 -0.0473 -0.0270 79  LYS A NZ  
612   N NZ  B LYS A 79  ? 0.3246 0.3190 0.3822 -0.0300 -0.0375 -0.0232 79  LYS A NZ  
613   N N   . GLU A 80  ? 0.3065 0.2819 0.3224 -0.0154 -0.0296 -0.0216 80  GLU A N   
614   C CA  . GLU A 80  ? 0.3146 0.2851 0.3297 -0.0142 -0.0252 -0.0220 80  GLU A CA  
615   C C   . GLU A 80  ? 0.2830 0.2567 0.3014 -0.0106 -0.0221 -0.0195 80  GLU A C   
616   O O   . GLU A 80  ? 0.2739 0.2467 0.2953 -0.0109 -0.0203 -0.0181 80  GLU A O   
617   C CB  . GLU A 80  ? 0.3043 0.2661 0.3105 -0.0139 -0.0236 -0.0250 80  GLU A CB  
618   C CG  . GLU A 80  ? 0.3517 0.3077 0.3522 -0.0183 -0.0264 -0.0278 80  GLU A CG  
619   C CD  . GLU A 80  ? 0.4302 0.3770 0.4199 -0.0184 -0.0238 -0.0316 80  GLU A CD  
620   O OE1 . GLU A 80  ? 0.3797 0.3265 0.3660 -0.0158 -0.0208 -0.0322 80  GLU A OE1 
621   O OE2 . GLU A 80  ? 0.4218 0.3611 0.4066 -0.0216 -0.0242 -0.0344 80  GLU A OE2 
622   N N   . CYS A 81  ? 0.2550 0.2319 0.2720 -0.0077 -0.0216 -0.0188 81  CYS A N   
623   C CA  . CYS A 81  ? 0.2607 0.2406 0.2806 -0.0047 -0.0192 -0.0166 81  CYS A CA  
624   C C   . CYS A 81  ? 0.2673 0.2523 0.2933 -0.0059 -0.0191 -0.0144 81  CYS A C   
625   O O   . CYS A 81  ? 0.2767 0.2599 0.3033 -0.0058 -0.0171 -0.0129 81  CYS A O   
626   C CB  . CYS A 81  ? 0.2902 0.2730 0.3077 -0.0024 -0.0189 -0.0165 81  CYS A CB  
627   S SG  . CYS A 81  ? 0.2879 0.2648 0.2995 -0.0008 -0.0160 -0.0195 81  CYS A SG  
628   N N   . MET A 82  ? 0.2746 0.2650 0.3052 -0.0074 -0.0213 -0.0146 82  MET A N   
629   C CA  . MET A 82  ? 0.2597 0.2555 0.2982 -0.0087 -0.0198 -0.0136 82  MET A CA  
630   C C   . MET A 82  ? 0.2638 0.2564 0.3037 -0.0123 -0.0178 -0.0140 82  MET A C   
631   O O   . MET A 82  ? 0.2589 0.2519 0.3007 -0.0138 -0.0142 -0.0130 82  MET A O   
632   C CB  . MET A 82  ? 0.2673 0.2695 0.3134 -0.0094 -0.0232 -0.0141 82  MET A CB  
633   C CG  . MET A 82  ? 0.2536 0.2582 0.2981 -0.0062 -0.0245 -0.0130 82  MET A CG  
634   S SD  . MET A 82  ? 0.2998 0.3107 0.3540 -0.0063 -0.0302 -0.0129 82  MET A SD  
635   C CE  . MET A 82  ? 0.3213 0.3270 0.3688 -0.0089 -0.0367 -0.0141 82  MET A CE  
636   N N   . ASP A 83  ? 0.2562 0.2443 0.2936 -0.0144 -0.0196 -0.0155 83  ASP A N   
637   C CA  . ASP A 83  ? 0.2858 0.2693 0.3233 -0.0182 -0.0177 -0.0158 83  ASP A CA  
638   C C   . ASP A 83  ? 0.3087 0.2847 0.3394 -0.0172 -0.0151 -0.0139 83  ASP A C   
639   O O   . ASP A 83  ? 0.2854 0.2583 0.3153 -0.0205 -0.0124 -0.0128 83  ASP A O   
640   C CB  . ASP A 83  ? 0.3044 0.2838 0.3401 -0.0207 -0.0206 -0.0180 83  ASP A CB  
641   C CG  . ASP A 83  ? 0.3345 0.3207 0.3788 -0.0236 -0.0240 -0.0196 83  ASP A CG  
642   O OD1 . ASP A 83  ? 0.3589 0.3536 0.4132 -0.0237 -0.0234 -0.0191 83  ASP A OD1 
643   O OD2 . ASP A 83  ? 0.3531 0.3362 0.3947 -0.0256 -0.0278 -0.0213 83  ASP A OD2 
644   N N   . ALA A 84  ? 0.2876 0.2604 0.3134 -0.0131 -0.0161 -0.0134 84  ALA A N   
645   C CA  . ALA A 84  ? 0.2915 0.2574 0.3127 -0.0116 -0.0154 -0.0112 84  ALA A CA  
646   C C   . ALA A 84  ? 0.2928 0.2611 0.3136 -0.0118 -0.0136 -0.0087 84  ALA A C   
647   O O   . ALA A 84  ? 0.3047 0.2663 0.3208 -0.0141 -0.0128 -0.0066 84  ALA A O   
648   C CB  . ALA A 84  ? 0.2840 0.2473 0.3037 -0.0071 -0.0166 -0.0120 84  ALA A CB  
649   N N   . ALA A 85  ? 0.2931 0.2695 0.3175 -0.0098 -0.0132 -0.0089 85  ALA A N   
650   C CA  . ALA A 85  ? 0.2557 0.2339 0.2794 -0.0105 -0.0109 -0.0072 85  ALA A CA  
651   C C   . ALA A 85  ? 0.2402 0.2181 0.2651 -0.0157 -0.0073 -0.0075 85  ALA A C   
652   O O   . ALA A 85  ? 0.2721 0.2455 0.2914 -0.0182 -0.0046 -0.0059 85  ALA A O   
653   C CB  . ALA A 85  ? 0.2497 0.2362 0.2777 -0.0076 -0.0110 -0.0077 85  ALA A CB  
654   N N   . GLU A 86  ? 0.2537 0.2359 0.2857 -0.0180 -0.0068 -0.0098 86  GLU A N   
655   C CA  . GLU A 86  ? 0.2779 0.2606 0.3133 -0.0234 -0.0023 -0.0108 86  GLU A CA  
656   C C   . GLU A 86  ? 0.2945 0.2659 0.3206 -0.0276 -0.0009 -0.0095 86  GLU A C   
657   O O   . GLU A 86  ? 0.3063 0.2734 0.3280 -0.0322 0.0038  -0.0090 86  GLU A O   
658   C CB  . GLU A 86  ? 0.2960 0.2863 0.3432 -0.0248 -0.0033 -0.0136 86  GLU A CB  
659   C CG  . GLU A 86  ? 0.2951 0.2877 0.3496 -0.0306 0.0019  -0.0156 86  GLU A CG  
660   C CD  . GLU A 86  ? 0.3469 0.3508 0.4179 -0.0305 0.0006  -0.0184 86  GLU A CD  
661   O OE1 . GLU A 86  ? 0.3405 0.3506 0.4165 -0.0259 -0.0030 -0.0182 86  GLU A OE1 
662   O OE2 . GLU A 86  ? 0.3867 0.3931 0.4662 -0.0350 0.0025  -0.0206 86  GLU A OE2 
663   N N   . ALA A 87  ? 0.2974 0.2628 0.3194 -0.0263 -0.0048 -0.0089 87  ALA A N   
664   C CA  . ALA A 87  ? 0.2967 0.2496 0.3092 -0.0295 -0.0048 -0.0071 87  ALA A CA  
665   C C   . ALA A 87  ? 0.3361 0.2808 0.3382 -0.0296 -0.0048 -0.0036 87  ALA A C   
666   O O   . ALA A 87  ? 0.3228 0.2573 0.3157 -0.0348 -0.0030 -0.0018 87  ALA A O   
667   C CB  . ALA A 87  ? 0.2902 0.2384 0.3017 -0.0265 -0.0093 -0.0075 87  ALA A CB  
668   N N   . TYR A 88  ? 0.3017 0.2498 0.3041 -0.0245 -0.0073 -0.0025 88  TYR A N   
669   C CA  . TYR A 88  ? 0.3102 0.2513 0.3034 -0.0247 -0.0084 0.0008  88  TYR A CA  
670   C C   . TYR A 88  ? 0.3360 0.2759 0.3241 -0.0306 -0.0025 0.0008  88  TYR A C   
671   O O   . TYR A 88  ? 0.3261 0.2546 0.3017 -0.0348 -0.0023 0.0035  88  TYR A O   
672   C CB  . TYR A 88  ? 0.2896 0.2363 0.2861 -0.0187 -0.0115 0.0014  88  TYR A CB  
673   C CG  . TYR A 88  ? 0.3261 0.2650 0.3134 -0.0190 -0.0143 0.0050  88  TYR A CG  
674   C CD1 . TYR A 88  ? 0.3140 0.2530 0.2957 -0.0220 -0.0112 0.0057  88  TYR A CD1 
675   C CD2 . TYR A 88  ? 0.3217 0.2519 0.3059 -0.0166 -0.0205 0.0078  88  TYR A CD2 
676   C CE1 . TYR A 88  ? 0.3492 0.2799 0.3209 -0.0229 -0.0149 0.0092  88  TYR A CE1 
677   C CE2 . TYR A 88  ? 0.3448 0.2675 0.3214 -0.0169 -0.0249 0.0115  88  TYR A CE2 
678   C CZ  . TYR A 88  ? 0.3656 0.2885 0.3350 -0.0204 -0.0223 0.0123  88  TYR A CZ  
679   O OH  . TYR A 88  ? 0.3731 0.2875 0.3330 -0.0216 -0.0273 0.0160  88  TYR A OH  
680   N N   . GLY A 89  ? 0.3246 0.2756 0.3223 -0.0311 0.0022  -0.0024 89  GLY A N   
681   C CA  . GLY A 89  ? 0.2848 0.2360 0.2816 -0.0370 0.0096  -0.0041 89  GLY A CA  
682   C C   . GLY A 89  ? 0.3204 0.2823 0.3257 -0.0345 0.0125  -0.0062 89  GLY A C   
683   O O   . GLY A 89  ? 0.3134 0.2752 0.3182 -0.0388 0.0194  -0.0080 89  GLY A O   
684   N N   . PHE A 90  ? 0.2860 0.2559 0.2986 -0.0280 0.0080  -0.0062 90  PHE A N   
685   C CA  . PHE A 90  ? 0.2706 0.2491 0.2904 -0.0255 0.0101  -0.0078 90  PHE A CA  
686   C C   . PHE A 90  ? 0.3035 0.2920 0.3387 -0.0263 0.0134  -0.0115 90  PHE A C   
687   O O   . PHE A 90  ? 0.2975 0.2893 0.3397 -0.0262 0.0109  -0.0125 90  PHE A O   
688   C CB  . PHE A 90  ? 0.2744 0.2568 0.2956 -0.0190 0.0043  -0.0064 90  PHE A CB  
689   C CG  . PHE A 90  ? 0.2816 0.2569 0.2916 -0.0180 0.0018  -0.0034 90  PHE A CG  
690   C CD1 . PHE A 90  ? 0.2995 0.2728 0.3040 -0.0197 0.0047  -0.0030 90  PHE A CD1 
691   C CD2 . PHE A 90  ? 0.3124 0.2830 0.3185 -0.0156 -0.0037 -0.0013 90  PHE A CD2 
692   C CE1 . PHE A 90  ? 0.3392 0.3057 0.3337 -0.0191 0.0011  0.0000  90  PHE A CE1 
693   C CE2 . PHE A 90  ? 0.3159 0.2808 0.3145 -0.0144 -0.0071 0.0015  90  PHE A CE2 
694   C CZ  . PHE A 90  ? 0.3218 0.2846 0.3143 -0.0164 -0.0052 0.0023  90  PHE A CZ  
695   N N   . ALA A 91  ? 0.2577 0.2511 0.2993 -0.0268 0.0185  -0.0137 91  ALA A N   
696   C CA  . ALA A 91  ? 0.2444 0.2481 0.3040 -0.0269 0.0212  -0.0174 91  ALA A CA  
697   C C   . ALA A 91  ? 0.2625 0.2742 0.3319 -0.0212 0.0135  -0.0170 91  ALA A C   
698   O O   . ALA A 91  ? 0.2664 0.2775 0.3304 -0.0167 0.0090  -0.0149 91  ALA A O   
699   C CB  . ALA A 91  ? 0.2388 0.2453 0.3031 -0.0272 0.0277  -0.0197 91  ALA A CB  
700   N N   . ARG A 92  ? 0.2580 0.2765 0.3415 -0.0219 0.0120  -0.0192 92  ARG A N   
701   C CA  . ARG A 92  ? 0.2314 0.2554 0.3217 -0.0176 0.0038  -0.0187 92  ARG A CA  
702   C C   . ARG A 92  ? 0.2512 0.2813 0.3505 -0.0134 0.0022  -0.0190 92  ARG A C   
703   O O   . ARG A 92  ? 0.2715 0.3035 0.3717 -0.0098 -0.0051 -0.0177 92  ARG A O   
704   C CB  . ARG A 92  ? 0.2628 0.2913 0.3648 -0.0202 0.0012  -0.0206 92  ARG A CB  
705   C CG  . ARG A 92  ? 0.3030 0.3330 0.4055 -0.0173 -0.0085 -0.0195 92  ARG A CG  
706   C CD  . ARG A 92  ? 0.2934 0.3287 0.4097 -0.0202 -0.0119 -0.0217 92  ARG A CD  
707   N NE  . ARG A 92  ? 0.2744 0.3044 0.3847 -0.0251 -0.0089 -0.0223 92  ARG A NE  
708   C CZ  . ARG A 92  ? 0.3308 0.3638 0.4507 -0.0289 -0.0107 -0.0243 92  ARG A CZ  
709   N NH1 . ARG A 92  ? 0.3000 0.3419 0.4373 -0.0285 -0.0159 -0.0259 92  ARG A NH1 
710   N NH2 . ARG A 92  ? 0.3029 0.3294 0.4153 -0.0335 -0.0078 -0.0246 92  ARG A NH2 
711   N N   . ASP A 93  ? 0.2429 0.2750 0.3478 -0.0140 0.0088  -0.0209 93  ASP A N   
712   C CA  . ASP A 93  ? 0.2058 0.2427 0.3196 -0.0097 0.0071  -0.0212 93  ASP A CA  
713   C C   . ASP A 93  ? 0.2042 0.2357 0.3042 -0.0072 0.0073  -0.0189 93  ASP A C   
714   O O   . ASP A 93  ? 0.2224 0.2564 0.3278 -0.0038 0.0063  -0.0190 93  ASP A O   
715   C CB  . ASP A 93  ? 0.2286 0.2714 0.3597 -0.0112 0.0140  -0.0253 93  ASP A CB  
716   C CG  . ASP A 93  ? 0.2859 0.3234 0.4091 -0.0163 0.0248  -0.0272 93  ASP A CG  
717   O OD1 . ASP A 93  ? 0.3267 0.3625 0.4493 -0.0216 0.0291  -0.0287 93  ASP A OD1 
718   O OD2 . ASP A 93  ? 0.3320 0.3656 0.4478 -0.0156 0.0287  -0.0272 93  ASP A OD2 
719   N N   . LEU A 94  ? 0.2348 0.2590 0.3180 -0.0086 0.0078  -0.0166 94  LEU A N   
720   C CA  . LEU A 94  ? 0.2055 0.2256 0.2772 -0.0059 0.0060  -0.0142 94  LEU A CA  
721   C C   . LEU A 94  ? 0.2144 0.2366 0.2863 -0.0017 -0.0018 -0.0124 94  LEU A C   
722   O O   . LEU A 94  ? 0.2449 0.2694 0.3214 -0.0015 -0.0065 -0.0125 94  LEU A O   
723   C CB  . LEU A 94  ? 0.2071 0.2192 0.2632 -0.0080 0.0066  -0.0120 94  LEU A CB  
724   C CG  . LEU A 94  ? 0.2398 0.2457 0.2881 -0.0125 0.0134  -0.0126 94  LEU A CG  
725   C CD1 . LEU A 94  ? 0.2574 0.2550 0.2922 -0.0146 0.0114  -0.0099 94  LEU A CD1 
726   C CD2 . LEU A 94  ? 0.2653 0.2699 0.3098 -0.0116 0.0160  -0.0126 94  LEU A CD2 
727   N N   . CYS A 95  ? 0.2243 0.2448 0.2902 0.0008  -0.0029 -0.0109 95  CYS A N   
728   C CA  . CYS A 95  ? 0.2268 0.2475 0.2902 0.0039  -0.0088 -0.0092 95  CYS A CA  
729   C C   . CYS A 95  ? 0.2519 0.2710 0.3110 0.0034  -0.0130 -0.0087 95  CYS A C   
730   O O   . CYS A 95  ? 0.2426 0.2581 0.2944 0.0022  -0.0118 -0.0083 95  CYS A O   
731   C CB  . CYS A 95  ? 0.2534 0.2704 0.3065 0.0051  -0.0080 -0.0076 95  CYS A CB  
732   S SG  . CYS A 95  ? 0.2357 0.2510 0.2818 0.0075  -0.0134 -0.0058 95  CYS A SG  
733   N N   . SER A 96  ? 0.2122 0.2330 0.2755 0.0042  -0.0184 -0.0087 96  SER A N   
734   C CA  . SER A 96  ? 0.2245 0.2427 0.2826 0.0028  -0.0219 -0.0088 96  SER A CA  
735   C C   . SER A 96  ? 0.2548 0.2679 0.3001 0.0036  -0.0219 -0.0079 96  SER A C   
736   O O   . SER A 96  ? 0.2323 0.2421 0.2725 0.0024  -0.0218 -0.0086 96  SER A O   
737   C CB  . SER A 96  ? 0.2473 0.2673 0.3114 0.0027  -0.0286 -0.0089 96  SER A CB  
738   O OG  . SER A 96  ? 0.2733 0.2917 0.3344 0.0047  -0.0324 -0.0073 96  SER A OG  
739   N N   . TYR A 97  ? 0.2366 0.2486 0.2772 0.0054  -0.0217 -0.0068 97  TYR A N   
740   C CA  . TYR A 97  ? 0.2548 0.2630 0.2859 0.0058  -0.0204 -0.0066 97  TYR A CA  
741   C C   . TYR A 97  ? 0.2349 0.2424 0.2653 0.0058  -0.0166 -0.0067 97  TYR A C   
742   O O   . TYR A 97  ? 0.2408 0.2454 0.2675 0.0057  -0.0161 -0.0074 97  TYR A O   
743   C CB  . TYR A 97  ? 0.2456 0.2531 0.2729 0.0071  -0.0204 -0.0054 97  TYR A CB  
744   C CG  . TYR A 97  ? 0.2547 0.2594 0.2778 0.0066  -0.0250 -0.0048 97  TYR A CG  
745   C CD1 . TYR A 97  ? 0.2840 0.2858 0.3039 0.0048  -0.0289 -0.0055 97  TYR A CD1 
746   C CD2 . TYR A 97  ? 0.2590 0.2624 0.2798 0.0075  -0.0259 -0.0033 97  TYR A CD2 
747   C CE1 . TYR A 97  ? 0.3317 0.3290 0.3453 0.0036  -0.0342 -0.0044 97  TYR A CE1 
748   C CE2 . TYR A 97  ? 0.2771 0.2758 0.2919 0.0065  -0.0310 -0.0021 97  TYR A CE2 
749   C CZ  . TYR A 97  ? 0.3654 0.3608 0.3761 0.0045  -0.0354 -0.0026 97  TYR A CZ  
750   O OH  . TYR A 97  ? 0.3848 0.3737 0.3875 0.0030  -0.0415 -0.0010 97  TYR A OH  
751   N N   . MET A 98  ? 0.2150 0.2240 0.2486 0.0056  -0.0141 -0.0060 98  MET A N   
752   C CA  . MET A 98  ? 0.2056 0.2122 0.2367 0.0050  -0.0119 -0.0055 98  MET A CA  
753   C C   . MET A 98  ? 0.2139 0.2179 0.2451 0.0033  -0.0122 -0.0061 98  MET A C   
754   O O   . MET A 98  ? 0.2442 0.2446 0.2723 0.0036  -0.0125 -0.0058 98  MET A O   
755   C CB  . MET A 98  ? 0.2016 0.2088 0.2343 0.0038  -0.0091 -0.0050 98  MET A CB  
756   C CG  . MET A 98  ? 0.2286 0.2316 0.2568 0.0018  -0.0072 -0.0041 98  MET A CG  
757   S SD  . MET A 98  ? 0.2605 0.2617 0.2850 0.0003  -0.0040 -0.0036 98  MET A SD  
758   C CE  . MET A 98  ? 0.2537 0.2565 0.2842 -0.0025 0.0003  -0.0058 98  MET A CE  
759   N N   . ARG A 99  ? 0.2275 0.2335 0.2636 0.0017  -0.0126 -0.0072 99  ARG A N   
760   C CA  . ARG A 99  ? 0.2202 0.2233 0.2563 -0.0005 -0.0126 -0.0079 99  ARG A CA  
761   C C   . ARG A 99  ? 0.2227 0.2229 0.2550 0.0004  -0.0150 -0.0088 99  ARG A C   
762   O O   . ARG A 99  ? 0.2405 0.2359 0.2700 -0.0002 -0.0148 -0.0089 99  ARG A O   
763   C CB  . ARG A 99  ? 0.2344 0.2413 0.2785 -0.0029 -0.0124 -0.0093 99  ARG A CB  
764   C CG  . ARG A 99  ? 0.2511 0.2602 0.2996 -0.0044 -0.0079 -0.0095 99  ARG A CG  
765   C CD  . ARG A 99  ? 0.2382 0.2519 0.2979 -0.0071 -0.0065 -0.0116 99  ARG A CD  
766   N NE  . ARG A 99  ? 0.2215 0.2412 0.2905 -0.0051 -0.0109 -0.0124 99  ARG A NE  
767   C CZ  . ARG A 99  ? 0.2459 0.2671 0.3191 -0.0057 -0.0159 -0.0130 99  ARG A CZ  
768   N NH1 . ARG A 99  ? 0.2535 0.2709 0.3220 -0.0080 -0.0168 -0.0134 99  ARG A NH1 
769   N NH2 . ARG A 99  ? 0.2446 0.2706 0.3269 -0.0041 -0.0205 -0.0133 99  ARG A NH2 
770   N N   . ILE A 100 ? 0.2279 0.2297 0.2594 0.0014  -0.0173 -0.0094 100 ILE A N   
771   C CA  . ILE A 100 ? 0.2422 0.2398 0.2680 0.0016  -0.0183 -0.0109 100 ILE A CA  
772   C C   . ILE A 100 ? 0.2336 0.2286 0.2569 0.0036  -0.0159 -0.0109 100 ILE A C   
773   O O   . ILE A 100 ? 0.2481 0.2388 0.2699 0.0036  -0.0153 -0.0123 100 ILE A O   
774   C CB  . ILE A 100 ? 0.2533 0.2512 0.2756 0.0015  -0.0209 -0.0112 100 ILE A CB  
775   C CG1 . ILE A 100 ? 0.2480 0.2475 0.2740 -0.0006 -0.0253 -0.0114 100 ILE A CG1 
776   C CG2 . ILE A 100 ? 0.2434 0.2360 0.2575 0.0013  -0.0198 -0.0132 100 ILE A CG2 
777   C CD1 . ILE A 100 ? 0.2721 0.2708 0.2943 -0.0009 -0.0299 -0.0107 100 ILE A CD1 
778   N N   . TYR A 101 ? 0.2095 0.2070 0.2334 0.0052  -0.0148 -0.0096 101 TYR A N   
779   C CA  . TYR A 101 ? 0.2035 0.1996 0.2275 0.0072  -0.0133 -0.0096 101 TYR A CA  
780   C C   . TYR A 101 ? 0.2644 0.2570 0.2902 0.0073  -0.0138 -0.0088 101 TYR A C   
781   O O   . TYR A 101 ? 0.2635 0.2528 0.2907 0.0087  -0.0136 -0.0099 101 TYR A O   
782   C CB  . TYR A 101 ? 0.2302 0.2297 0.2547 0.0082  -0.0127 -0.0081 101 TYR A CB  
783   C CG  . TYR A 101 ? 0.2219 0.2215 0.2484 0.0100  -0.0115 -0.0087 101 TYR A CG  
784   C CD1 . TYR A 101 ? 0.2544 0.2525 0.2843 0.0110  -0.0126 -0.0075 101 TYR A CD1 
785   C CD2 . TYR A 101 ? 0.2200 0.2206 0.2452 0.0103  -0.0094 -0.0104 101 TYR A CD2 
786   C CE1 . TYR A 101 ? 0.2464 0.2455 0.2813 0.0129  -0.0124 -0.0081 101 TYR A CE1 
787   C CE2 . TYR A 101 ? 0.2605 0.2622 0.2900 0.0117  -0.0076 -0.0114 101 TYR A CE2 
788   C CZ  . TYR A 101 ? 0.2730 0.2749 0.3086 0.0133  -0.0093 -0.0104 101 TYR A CZ  
789   O OH  . TYR A 101 ? 0.2836 0.2878 0.3264 0.0148  -0.0079 -0.0118 101 TYR A OH  
790   N N   . TRP A 102 ? 0.2442 0.2364 0.2697 0.0056  -0.0142 -0.0068 102 TRP A N   
791   C CA  . TRP A 102 ? 0.2269 0.2135 0.2513 0.0047  -0.0151 -0.0055 102 TRP A CA  
792   C C   . TRP A 102 ? 0.2521 0.2343 0.2764 0.0042  -0.0156 -0.0071 102 TRP A C   
793   O O   . TRP A 102 ? 0.2678 0.2447 0.2926 0.0053  -0.0169 -0.0069 102 TRP A O   
794   C CB  . TRP A 102 ? 0.2253 0.2114 0.2475 0.0015  -0.0140 -0.0040 102 TRP A CB  
795   C CG  . TRP A 102 ? 0.2538 0.2413 0.2742 0.0015  -0.0135 -0.0024 102 TRP A CG  
796   C CD1 . TRP A 102 ? 0.2342 0.2218 0.2543 0.0036  -0.0150 -0.0013 102 TRP A CD1 
797   C CD2 . TRP A 102 ? 0.2891 0.2770 0.3077 -0.0014 -0.0108 -0.0020 102 TRP A CD2 
798   N NE1 . TRP A 102 ? 0.2621 0.2497 0.2788 0.0020  -0.0140 0.0001  102 TRP A NE1 
799   C CE2 . TRP A 102 ? 0.2702 0.2578 0.2858 -0.0010 -0.0109 -0.0006 102 TRP A CE2 
800   C CE3 . TRP A 102 ? 0.2438 0.2329 0.2644 -0.0044 -0.0078 -0.0032 102 TRP A CE3 
801   C CZ2 . TRP A 102 ? 0.2350 0.2218 0.2473 -0.0038 -0.0077 -0.0005 102 TRP A CZ2 
802   C CZ3 . TRP A 102 ? 0.2373 0.2269 0.2570 -0.0069 -0.0040 -0.0035 102 TRP A CZ3 
803   C CH2 . TRP A 102 ? 0.2385 0.2263 0.2532 -0.0066 -0.0038 -0.0022 102 TRP A CH2 
804   N N   . GLY A 103 ? 0.2528 0.2368 0.2772 0.0022  -0.0152 -0.0088 103 GLY A N   
805   C CA  . GLY A 103 ? 0.2920 0.2710 0.3154 0.0009  -0.0157 -0.0105 103 GLY A CA  
806   C C   . GLY A 103 ? 0.2966 0.2726 0.3198 0.0034  -0.0153 -0.0128 103 GLY A C   
807   O O   . GLY A 103 ? 0.2899 0.2595 0.3131 0.0036  -0.0156 -0.0137 103 GLY A O   
808   N N   . GLY A 104 ? 0.2642 0.2438 0.2871 0.0049  -0.0141 -0.0142 104 GLY A N   
809   C CA  . GLY A 104 ? 0.2795 0.2564 0.3028 0.0068  -0.0120 -0.0173 104 GLY A CA  
810   C C   . GLY A 104 ? 0.3025 0.2777 0.3319 0.0100  -0.0120 -0.0166 104 GLY A C   
811   O O   . GLY A 104 ? 0.3029 0.2739 0.3355 0.0116  -0.0106 -0.0193 104 GLY A O   
812   N N   . MET A 105 ? 0.2622 0.2399 0.2937 0.0108  -0.0139 -0.0132 105 MET A N   
813   C CA  . MET A 105 ? 0.2331 0.2086 0.2707 0.0136  -0.0159 -0.0120 105 MET A CA  
814   C C   . MET A 105 ? 0.2730 0.2404 0.3103 0.0133  -0.0185 -0.0109 105 MET A C   
815   O O   . MET A 105 ? 0.2835 0.2466 0.3269 0.0160  -0.0194 -0.0121 105 MET A O   
816   C CB  . MET A 105 ? 0.2572 0.2362 0.2943 0.0134  -0.0180 -0.0084 105 MET A CB  
817   C CG  . MET A 105 ? 0.3155 0.2927 0.3590 0.0160  -0.0216 -0.0066 105 MET A CG  
818   S SD  . MET A 105 ? 0.3178 0.2947 0.3563 0.0140  -0.0256 -0.0016 105 MET A SD  
819   C CE  . MET A 105 ? 0.3320 0.3059 0.3596 0.0093  -0.0236 -0.0004 105 MET A CE  
820   N N   . HIS A 106 ? 0.2671 0.2317 0.2978 0.0097  -0.0195 -0.0088 106 HIS A N   
821   C CA  . HIS A 106 ? 0.2718 0.2274 0.3001 0.0083  -0.0217 -0.0075 106 HIS A CA  
822   C C   . HIS A 106 ? 0.2661 0.2177 0.2961 0.0090  -0.0200 -0.0114 106 HIS A C   
823   O O   . HIS A 106 ? 0.2700 0.2138 0.3022 0.0104  -0.0220 -0.0114 106 HIS A O   
824   C CB  . HIS A 106 ? 0.2622 0.2167 0.2835 0.0034  -0.0214 -0.0054 106 HIS A CB  
825   C CG  . HIS A 106 ? 0.2982 0.2517 0.3156 0.0021  -0.0230 -0.0016 106 HIS A CG  
826   N ND1 . HIS A 106 ? 0.2984 0.2424 0.3116 0.0012  -0.0269 0.0018  106 HIS A ND1 
827   C CD2 . HIS A 106 ? 0.2799 0.2395 0.2959 0.0011  -0.0215 -0.0007 106 HIS A CD2 
828   C CE1 . HIS A 106 ? 0.3164 0.2601 0.3242 -0.0009 -0.0276 0.0046  106 HIS A CE1 
829   N NE2 . HIS A 106 ? 0.2751 0.2286 0.2852 -0.0007 -0.0240 0.0029  106 HIS A NE2 
830   N N   . LEU A 107 ? 0.2759 0.2318 0.3041 0.0077  -0.0169 -0.0147 107 LEU A N   
831   C CA  . LEU A 107 ? 0.2853 0.2362 0.3131 0.0077  -0.0149 -0.0189 107 LEU A CA  
832   C C   . LEU A 107 ? 0.2820 0.2321 0.3168 0.0119  -0.0127 -0.0221 107 LEU A C   
833   O O   . LEU A 107 ? 0.3043 0.2482 0.3401 0.0125  -0.0106 -0.0259 107 LEU A O   
834   C CB  . LEU A 107 ? 0.2976 0.2518 0.3197 0.0044  -0.0133 -0.0213 107 LEU A CB  
835   C CG  . LEU A 107 ? 0.2741 0.2295 0.2928 0.0002  -0.0153 -0.0193 107 LEU A CG  
836   C CD1 . LEU A 107 ? 0.3297 0.2887 0.3447 -0.0025 -0.0154 -0.0213 107 LEU A CD1 
837   C CD2 . LEU A 107 ? 0.2595 0.2064 0.2767 -0.0020 -0.0163 -0.0193 107 LEU A CD2 
838   N N   . ASN A 108 ? 0.2742 0.2304 0.3145 0.0146  -0.0124 -0.0212 108 ASN A N   
839   C CA  . ASN A 108 ? 0.3083 0.2656 0.3583 0.0186  -0.0096 -0.0245 108 ASN A CA  
840   C C   . ASN A 108 ? 0.2845 0.2415 0.3311 0.0172  -0.0033 -0.0304 108 ASN A C   
841   O O   . ASN A 108 ? 0.2987 0.2514 0.3509 0.0190  0.0005  -0.0351 108 ASN A O   
842   C CB  . ASN A 108 ? 0.3203 0.2706 0.3794 0.0220  -0.0122 -0.0246 108 ASN A CB  
843   C CG  . ASN A 108 ? 0.3291 0.2827 0.4029 0.0267  -0.0103 -0.0274 108 ASN A CG  
844   O OD1 . ASN A 108 ? 0.3393 0.3010 0.4166 0.0272  -0.0083 -0.0278 108 ASN A OD1 
845   N ND2 . ASN A 108 ? 0.3469 0.2943 0.4308 0.0301  -0.0110 -0.0295 108 ASN A ND2 
846   N N   . LYS A 109 ? 0.3028 0.2634 0.3398 0.0138  -0.0021 -0.0302 109 LYS A N   
847   C CA  . LYS A 109 ? 0.2725 0.2307 0.3018 0.0111  0.0029  -0.0350 109 LYS A CA  
848   C C   . LYS A 109 ? 0.2789 0.2433 0.3048 0.0101  0.0045  -0.0344 109 LYS A C   
849   O O   . LYS A 109 ? 0.3085 0.2777 0.3320 0.0094  0.0007  -0.0301 109 LYS A O   
850   C CB  . LYS A 109 ? 0.2820 0.2351 0.2999 0.0067  0.0010  -0.0354 109 LYS A CB  
851   C CG  . LYS A 109 ? 0.2868 0.2322 0.3068 0.0070  -0.0001 -0.0365 109 LYS A CG  
852   C CD  . LYS A 109 ? 0.3404 0.2821 0.3506 0.0021  -0.0029 -0.0363 109 LYS A CD  
853   C CE  . LYS A 109 ? 0.3705 0.3080 0.3697 -0.0017 -0.0002 -0.0406 109 LYS A CE  
854   N NZ  . LYS A 109 ? 0.3864 0.3185 0.3771 -0.0067 -0.0038 -0.0411 109 LYS A NZ  
855   N N   . TYR A 110 ? 0.3000 0.2636 0.3259 0.0099  0.0108  -0.0390 110 TYR A N   
856   C CA  . TYR A 110 ? 0.2912 0.2586 0.3116 0.0079  0.0133  -0.0389 110 TYR A CA  
857   C C   . TYR A 110 ? 0.3249 0.2860 0.3285 0.0027  0.0140  -0.0406 110 TYR A C   
858   O O   . TYR A 110 ? 0.3536 0.3069 0.3512 0.0005  0.0169  -0.0448 110 TYR A O   
859   C CB  . TYR A 110 ? 0.2898 0.2593 0.3194 0.0097  0.0204  -0.0432 110 TYR A CB  
860   C CG  . TYR A 110 ? 0.2810 0.2553 0.3089 0.0084  0.0232  -0.0428 110 TYR A CG  
861   C CD1 . TYR A 110 ? 0.2798 0.2603 0.3081 0.0090  0.0179  -0.0372 110 TYR A CD1 
862   C CD2 . TYR A 110 ? 0.3308 0.3027 0.3567 0.0060  0.0322  -0.0485 110 TYR A CD2 
863   C CE1 . TYR A 110 ? 0.2850 0.2693 0.3120 0.0077  0.0208  -0.0371 110 TYR A CE1 
864   C CE2 . TYR A 110 ? 0.3123 0.2884 0.3372 0.0043  0.0355  -0.0483 110 TYR A CE2 
865   C CZ  . TYR A 110 ? 0.2902 0.2722 0.3155 0.0053  0.0292  -0.0424 110 TYR A CZ  
866   O OH  . TYR A 110 ? 0.3128 0.2978 0.3362 0.0033  0.0323  -0.0421 110 TYR A OH  
867   N N   . ALA A 111 ? 0.3313 0.2947 0.3268 0.0005  0.0112  -0.0374 111 ALA A N   
868   C CA  . ALA A 111 ? 0.3525 0.3091 0.3316 -0.0047 0.0096  -0.0381 111 ALA A CA  
869   C C   . ALA A 111 ? 0.3711 0.3197 0.3398 -0.0084 0.0173  -0.0438 111 ALA A C   
870   O O   . ALA A 111 ? 0.4153 0.3548 0.3689 -0.0133 0.0166  -0.0457 111 ALA A O   
871   C CB  . ALA A 111 ? 0.3629 0.3234 0.3376 -0.0057 0.0045  -0.0333 111 ALA A CB  
872   N N   . PHE A 112 ? 0.3689 0.3201 0.3452 -0.0067 0.0249  -0.0469 112 PHE A N   
873   C CA  . PHE A 112 ? 0.4039 0.3474 0.3710 -0.0108 0.0342  -0.0532 112 PHE A CA  
874   C C   . PHE A 112 ? 0.4610 0.4019 0.4381 -0.0088 0.0414  -0.0595 112 PHE A C   
875   O O   . PHE A 112 ? 0.4944 0.4311 0.4701 -0.0110 0.0514  -0.0658 112 PHE A O   
876   C CB  . PHE A 112 ? 0.4027 0.3507 0.3713 -0.0114 0.0387  -0.0529 112 PHE A CB  
877   C CG  . PHE A 112 ? 0.4224 0.3710 0.3799 -0.0136 0.0317  -0.0469 112 PHE A CG  
878   C CD1 . PHE A 112 ? 0.3551 0.3128 0.3228 -0.0094 0.0242  -0.0410 112 PHE A CD1 
879   C CD2 . PHE A 112 ? 0.4853 0.4239 0.4215 -0.0202 0.0327  -0.0474 112 PHE A CD2 
880   C CE1 . PHE A 112 ? 0.3954 0.3536 0.3555 -0.0107 0.0183  -0.0361 112 PHE A CE1 
881   C CE2 . PHE A 112 ? 0.4597 0.3983 0.3875 -0.0216 0.0254  -0.0417 112 PHE A CE2 
882   C CZ  . PHE A 112 ? 0.4560 0.4052 0.3975 -0.0163 0.0182  -0.0362 112 PHE A CZ  
883   N N   . GLY A 113 ? 0.4061 0.3484 0.3929 -0.0050 0.0367  -0.0582 113 GLY A N   
884   C CA  . GLY A 113 ? 0.4309 0.3690 0.4267 -0.0029 0.0424  -0.0640 113 GLY A CA  
885   C C   . GLY A 113 ? 0.4222 0.3689 0.4416 0.0042  0.0411  -0.0626 113 GLY A C   
886   O O   . GLY A 113 ? 0.4099 0.3650 0.4394 0.0066  0.0416  -0.0609 113 GLY A O   
887   N N   . GLY A 114 ? 0.3515 0.2949 0.3797 0.0075  0.0394  -0.0637 114 GLY A N   
888   C CA  . GLY A 114 ? 0.3454 0.2944 0.3959 0.0140  0.0381  -0.0630 114 GLY A CA  
889   C C   . GLY A 114 ? 0.3213 0.2756 0.3758 0.0168  0.0274  -0.0548 114 GLY A C   
890   O O   . GLY A 114 ? 0.3319 0.2860 0.3739 0.0139  0.0219  -0.0503 114 GLY A O   
891   N N   . GLU A 115 ? 0.2890 0.2473 0.3615 0.0222  0.0243  -0.0532 115 GLU A N   
892   C CA  . GLU A 115 ? 0.3109 0.2725 0.3862 0.0242  0.0146  -0.0457 115 GLU A CA  
893   C C   . GLU A 115 ? 0.3146 0.2841 0.3848 0.0225  0.0128  -0.0417 115 GLU A C   
894   O O   . GLU A 115 ? 0.2943 0.2677 0.3633 0.0209  0.0185  -0.0445 115 GLU A O   
895   C CB  . GLU A 115 ? 0.3388 0.3020 0.4340 0.0300  0.0111  -0.0448 115 GLU A CB  
896   C CG  . GLU A 115 ? 0.4056 0.3769 0.5160 0.0324  0.0157  -0.0480 115 GLU A CG  
897   C CD  . GLU A 115 ? 0.4750 0.4483 0.6080 0.0383  0.0111  -0.0474 115 GLU A CD  
898   O OE1 . GLU A 115 ? 0.4642 0.4302 0.6019 0.0410  0.0069  -0.0468 115 GLU A OE1 
899   O OE2 . GLU A 115 ? 0.4800 0.4616 0.6264 0.0401  0.0113  -0.0477 115 GLU A OE2 
900   N N   . PHE A 116 ? 0.2854 0.2567 0.3525 0.0225  0.0054  -0.0354 116 PHE A N   
901   C CA  . PHE A 116 ? 0.2859 0.2643 0.3501 0.0214  0.0036  -0.0317 116 PHE A CA  
902   C C   . PHE A 116 ? 0.2984 0.2827 0.3779 0.0249  0.0030  -0.0316 116 PHE A C   
903   O O   . PHE A 116 ? 0.3269 0.3099 0.4160 0.0280  -0.0024 -0.0292 116 PHE A O   
904   C CB  . PHE A 116 ? 0.2597 0.2381 0.3165 0.0200  -0.0029 -0.0258 116 PHE A CB  
905   C CG  . PHE A 116 ? 0.2843 0.2689 0.3367 0.0185  -0.0035 -0.0231 116 PHE A CG  
906   C CD1 . PHE A 116 ? 0.3155 0.3012 0.3593 0.0157  0.0002  -0.0250 116 PHE A CD1 
907   C CD2 . PHE A 116 ? 0.2949 0.2828 0.3510 0.0196  -0.0078 -0.0190 116 PHE A CD2 
908   C CE1 . PHE A 116 ? 0.3103 0.3007 0.3500 0.0144  -0.0003 -0.0227 116 PHE A CE1 
909   C CE2 . PHE A 116 ? 0.2912 0.2844 0.3428 0.0180  -0.0076 -0.0170 116 PHE A CE2 
910   C CZ  . PHE A 116 ? 0.3337 0.3281 0.3781 0.0158  -0.0039 -0.0189 116 PHE A CZ  
911   N N   . PRO A 117 ? 0.2910 0.2809 0.3736 0.0243  0.0081  -0.0341 117 PRO A N   
912   C CA  . PRO A 117 ? 0.3035 0.2993 0.4044 0.0277  0.0081  -0.0352 117 PRO A CA  
913   C C   . PRO A 117 ? 0.3430 0.3421 0.4463 0.0287  -0.0005 -0.0288 117 PRO A C   
914   O O   . PRO A 117 ? 0.3689 0.3694 0.4605 0.0260  -0.0023 -0.0253 117 PRO A O   
915   C CB  . PRO A 117 ? 0.2953 0.2956 0.3961 0.0252  0.0167  -0.0397 117 PRO A CB  
916   C CG  . PRO A 117 ? 0.3232 0.3174 0.4067 0.0212  0.0218  -0.0422 117 PRO A CG  
917   C CD  . PRO A 117 ? 0.3105 0.3006 0.3815 0.0202  0.0146  -0.0370 117 PRO A CD  
918   N N   . LYS A 118 ? 0.3246 0.3244 0.4434 0.0325  -0.0057 -0.0277 118 LYS A N   
919   C CA  . LYS A 118 ? 0.3698 0.3710 0.4891 0.0328  -0.0146 -0.0216 118 LYS A CA  
920   C C   . LYS A 118 ? 0.3142 0.3238 0.4384 0.0317  -0.0130 -0.0219 118 LYS A C   
921   O O   . LYS A 118 ? 0.3020 0.3174 0.4420 0.0334  -0.0089 -0.0262 118 LYS A O   
922   C CB  . LYS A 118 ? 0.3802 0.3778 0.5130 0.0367  -0.0226 -0.0196 118 LYS A CB  
923   C CG  . LYS A 118 ? 0.3909 0.3863 0.5180 0.0355  -0.0325 -0.0127 118 LYS A CG  
924   C CD  . LYS A 118 ? 0.4101 0.4003 0.5490 0.0389  -0.0422 -0.0099 118 LYS A CD  
925   C CE  . LYS A 118 ? 0.4366 0.4341 0.5970 0.0419  -0.0463 -0.0107 118 LYS A CE  
926   N NZ  . LYS A 118 ? 0.4336 0.4400 0.5938 0.0394  -0.0443 -0.0108 118 LYS A NZ  
927   N N   . PRO A 119 ? 0.3469 0.3573 0.4590 0.0289  -0.0157 -0.0177 119 PRO A N   
928   C CA  . PRO A 119 ? 0.2775 0.2950 0.3942 0.0277  -0.0155 -0.0174 119 PRO A CA  
929   C C   . PRO A 119 ? 0.2910 0.3102 0.4217 0.0299  -0.0238 -0.0149 119 PRO A C   
930   O O   . PRO A 119 ? 0.3200 0.3332 0.4507 0.0314  -0.0316 -0.0114 119 PRO A O   
931   C CB  . PRO A 119 ? 0.3158 0.3315 0.4143 0.0242  -0.0163 -0.0137 119 PRO A CB  
932   C CG  . PRO A 119 ? 0.3763 0.3847 0.4635 0.0237  -0.0192 -0.0110 119 PRO A CG  
933   C CD  . PRO A 119 ? 0.3621 0.3671 0.4559 0.0262  -0.0177 -0.0140 119 PRO A CD  
934   N N   . ASP A 120 ? 0.2349 0.2619 0.3775 0.0298  -0.0225 -0.0167 120 ASP A N   
935   C CA  . ASP A 120 ? 0.2450 0.2741 0.4012 0.0314  -0.0318 -0.0139 120 ASP A CA  
936   C C   . ASP A 120 ? 0.2637 0.2890 0.4047 0.0281  -0.0388 -0.0081 120 ASP A C   
937   O O   . ASP A 120 ? 0.2699 0.2919 0.4142 0.0285  -0.0491 -0.0040 120 ASP A O   
938   C CB  . ASP A 120 ? 0.2378 0.2772 0.4143 0.0320  -0.0281 -0.0183 120 ASP A CB  
939   C CG  . ASP A 120 ? 0.3146 0.3572 0.5088 0.0352  -0.0208 -0.0248 120 ASP A CG  
940   O OD1 . ASP A 120 ? 0.3031 0.3409 0.5038 0.0388  -0.0246 -0.0247 120 ASP A OD1 
941   O OD2 . ASP A 120 ? 0.2825 0.3316 0.4835 0.0337  -0.0108 -0.0303 120 ASP A OD2 
942   N N   . PHE A 121 ? 0.2294 0.2547 0.3541 0.0246  -0.0334 -0.0078 121 PHE A N   
943   C CA  . PHE A 121 ? 0.2564 0.2777 0.3658 0.0212  -0.0381 -0.0032 121 PHE A CA  
944   C C   . PHE A 121 ? 0.2496 0.2695 0.3422 0.0186  -0.0312 -0.0035 121 PHE A C   
945   O O   . PHE A 121 ? 0.2145 0.2374 0.3071 0.0188  -0.0235 -0.0071 121 PHE A O   
946   C CB  . PHE A 121 ? 0.2201 0.2461 0.3369 0.0196  -0.0421 -0.0023 121 PHE A CB  
947   C CG  . PHE A 121 ? 0.2222 0.2572 0.3479 0.0189  -0.0342 -0.0066 121 PHE A CG  
948   C CD1 . PHE A 121 ? 0.2527 0.2878 0.3647 0.0157  -0.0285 -0.0068 121 PHE A CD1 
949   C CD2 . PHE A 121 ? 0.2514 0.2941 0.3996 0.0213  -0.0330 -0.0105 121 PHE A CD2 
950   C CE1 . PHE A 121 ? 0.2480 0.2896 0.3662 0.0142  -0.0215 -0.0104 121 PHE A CE1 
951   C CE2 . PHE A 121 ? 0.2334 0.2837 0.3893 0.0196  -0.0248 -0.0148 121 PHE A CE2 
952   C CZ  . PHE A 121 ? 0.2311 0.2800 0.3698 0.0157  -0.0193 -0.0143 121 PHE A CZ  
953   N N   . VAL A 122 ? 0.2524 0.2671 0.3308 0.0158  -0.0342 0.0001  122 VAL A N   
954   C CA  . VAL A 122 ? 0.2251 0.2387 0.2895 0.0134  -0.0291 0.0001  122 VAL A CA  
955   C C   . VAL A 122 ? 0.2771 0.2937 0.3403 0.0111  -0.0286 0.0003  122 VAL A C   
956   O O   . VAL A 122 ? 0.2501 0.2656 0.3146 0.0098  -0.0344 0.0025  122 VAL A O   
957   C CB  . VAL A 122 ? 0.2683 0.2741 0.3192 0.0115  -0.0314 0.0031  122 VAL A CB  
958   C CG1 . VAL A 122 ? 0.2873 0.2924 0.3267 0.0089  -0.0272 0.0032  122 VAL A CG1 
959   C CG2 . VAL A 122 ? 0.2879 0.2907 0.3390 0.0132  -0.0306 0.0025  122 VAL A CG2 
960   N N   . PHE A 123 ? 0.2232 0.2429 0.2834 0.0103  -0.0222 -0.0017 123 PHE A N   
961   C CA  . PHE A 123 ? 0.2431 0.2639 0.2993 0.0078  -0.0211 -0.0014 123 PHE A CA  
962   C C   . PHE A 123 ? 0.2358 0.2539 0.2803 0.0069  -0.0167 -0.0014 123 PHE A C   
963   O O   . PHE A 123 ? 0.2593 0.2787 0.3034 0.0076  -0.0122 -0.0033 123 PHE A O   
964   C CB  . PHE A 123 ? 0.2551 0.2825 0.3223 0.0076  -0.0180 -0.0041 123 PHE A CB  
965   C CG  . PHE A 123 ? 0.2678 0.2962 0.3329 0.0046  -0.0182 -0.0036 123 PHE A CG  
966   C CD1 . PHE A 123 ? 0.2697 0.2992 0.3407 0.0034  -0.0243 -0.0021 123 PHE A CD1 
967   C CD2 . PHE A 123 ? 0.2929 0.3204 0.3501 0.0029  -0.0127 -0.0044 123 PHE A CD2 
968   C CE1 . PHE A 123 ? 0.2800 0.3100 0.3489 0.0002  -0.0244 -0.0019 123 PHE A CE1 
969   C CE2 . PHE A 123 ? 0.2690 0.2964 0.3237 0.0000  -0.0126 -0.0040 123 PHE A CE2 
970   C CZ  . PHE A 123 ? 0.2717 0.3007 0.3323 -0.0015 -0.0181 -0.0029 123 PHE A CZ  
971   N N   . GLN A 124 ? 0.2504 0.2642 0.2857 0.0051  -0.0181 0.0006  124 GLN A N   
972   C CA  . GLN A 124 ? 0.2105 0.2214 0.2375 0.0049  -0.0150 0.0006  124 GLN A CA  
973   C C   . GLN A 124 ? 0.2300 0.2386 0.2507 0.0028  -0.0137 0.0010  124 GLN A C   
974   O O   . GLN A 124 ? 0.2781 0.2853 0.2974 0.0007  -0.0161 0.0019  124 GLN A O   
975   C CB  . GLN A 124 ? 0.2483 0.2549 0.2711 0.0048  -0.0167 0.0018  124 GLN A CB  
976   C CG  . GLN A 124 ? 0.2164 0.2207 0.2333 0.0044  -0.0136 0.0015  124 GLN A CG  
977   C CD  . GLN A 124 ? 0.2440 0.2510 0.2631 0.0062  -0.0110 0.0001  124 GLN A CD  
978   O OE1 . GLN A 124 ? 0.2503 0.2599 0.2716 0.0068  -0.0099 -0.0007 124 GLN A OE1 
979   N NE2 . GLN A 124 ? 0.2330 0.2389 0.2511 0.0064  -0.0100 -0.0002 124 GLN A NE2 
980   N N   . THR A 125 ? 0.2196 0.2272 0.2367 0.0033  -0.0105 0.0005  125 THR A N   
981   C CA  . THR A 125 ? 0.2440 0.2484 0.2558 0.0019  -0.0089 0.0006  125 THR A CA  
982   C C   . THR A 125 ? 0.2768 0.2782 0.2855 0.0020  -0.0078 0.0005  125 THR A C   
983   O O   . THR A 125 ? 0.2528 0.2555 0.2640 0.0037  -0.0074 0.0002  125 THR A O   
984   C CB  . THR A 125 ? 0.2554 0.2602 0.2668 0.0026  -0.0068 0.0001  125 THR A CB  
985   O OG1 . THR A 125 ? 0.2486 0.2552 0.2618 0.0012  -0.0065 -0.0002 125 THR A OG1 
986   C CG2 . THR A 125 ? 0.2754 0.2761 0.2829 0.0024  -0.0052 0.0001  125 THR A CG2 
987   N N   . GLN A 126 ? 0.2569 0.2537 0.2602 -0.0002 -0.0067 0.0004  126 GLN A N   
988   C CA  . GLN A 126 ? 0.2671 0.2607 0.2678 -0.0010 -0.0040 -0.0005 126 GLN A CA  
989   C C   . GLN A 126 ? 0.2700 0.2618 0.2710 -0.0006 -0.0003 -0.0020 126 GLN A C   
990   O O   . GLN A 126 ? 0.2749 0.2628 0.2709 -0.0027 0.0007  -0.0024 126 GLN A O   
991   C CB  . GLN A 126 ? 0.2558 0.2436 0.2486 -0.0047 -0.0047 0.0001  126 GLN A CB  
992   C CG  . GLN A 126 ? 0.2546 0.2394 0.2452 -0.0061 -0.0010 -0.0011 126 GLN A CG  
993   C CD  . GLN A 126 ? 0.2582 0.2396 0.2468 -0.0075 0.0048  -0.0037 126 GLN A CD  
994   O OE1 . GLN A 126 ? 0.2737 0.2491 0.2540 -0.0108 0.0060  -0.0041 126 GLN A OE1 
995   N NE2 . GLN A 126 ? 0.2704 0.2554 0.2677 -0.0051 0.0084  -0.0056 126 GLN A NE2 
996   N N   . ILE A 127 ? 0.2212 0.2154 0.2284 0.0019  0.0011  -0.0029 127 ILE A N   
997   C CA  . ILE A 127 ? 0.2102 0.2024 0.2202 0.0027  0.0043  -0.0046 127 ILE A CA  
998   C C   . ILE A 127 ? 0.2955 0.2897 0.3129 0.0039  0.0066  -0.0063 127 ILE A C   
999   O O   . ILE A 127 ? 0.2549 0.2467 0.2743 0.0030  0.0113  -0.0088 127 ILE A O   
1000  C CB  . ILE A 127 ? 0.2361 0.2285 0.2482 0.0050  0.0022  -0.0037 127 ILE A CB  
1001  C CG1 . ILE A 127 ? 0.2737 0.2630 0.2899 0.0063  0.0048  -0.0054 127 ILE A CG1 
1002  C CG2 . ILE A 127 ? 0.2457 0.2418 0.2612 0.0072  -0.0013 -0.0023 127 ILE A CG2 
1003  C CD1 . ILE A 127 ? 0.2511 0.2373 0.2659 0.0074  0.0027  -0.0041 127 ILE A CD1 
1004  N N   . CYS A 128 ? 0.2076 0.2061 0.2292 0.0054  0.0038  -0.0053 128 CYS A N   
1005  C CA  . CYS A 128 ? 0.2182 0.2191 0.2468 0.0056  0.0057  -0.0069 128 CYS A CA  
1006  C C   . CYS A 128 ? 0.2275 0.2256 0.2494 0.0020  0.0082  -0.0072 128 CYS A C   
1007  O O   . CYS A 128 ? 0.2528 0.2492 0.2672 0.0008  0.0053  -0.0052 128 CYS A O   
1008  C CB  . CYS A 128 ? 0.2220 0.2273 0.2554 0.0079  0.0010  -0.0056 128 CYS A CB  
1009  S SG  . CYS A 128 ? 0.2512 0.2600 0.2939 0.0075  0.0027  -0.0075 128 CYS A SG  
1010  N N   . CYS A 129 ? 0.2335 0.2307 0.2584 0.0000  0.0131  -0.0096 129 CYS A N   
1011  C CA  . CYS A 129 ? 0.2483 0.2405 0.2640 -0.0045 0.0157  -0.0097 129 CYS A CA  
1012  C C   . CYS A 129 ? 0.2505 0.2442 0.2648 -0.0042 0.0110  -0.0073 129 CYS A C   
1013  O O   . CYS A 129 ? 0.3050 0.2936 0.3095 -0.0068 0.0092  -0.0055 129 CYS A O   
1014  C CB  . CYS A 129 ? 0.2381 0.2294 0.2583 -0.0072 0.0230  -0.0133 129 CYS A CB  
1015  S SG  . CYS A 129 ? 0.2773 0.2650 0.2987 -0.0083 0.0304  -0.0171 129 CYS A SG  
1016  N N   . SER A 130 ? 0.2429 0.2426 0.2665 -0.0009 0.0083  -0.0072 130 SER A N   
1017  C CA  . SER A 130 ? 0.2221 0.2226 0.2445 -0.0007 0.0046  -0.0056 130 SER A CA  
1018  C C   . SER A 130 ? 0.2512 0.2510 0.2688 0.0008  -0.0001 -0.0033 130 SER A C   
1019  O O   . SER A 130 ? 0.2281 0.2272 0.2441 0.0009  -0.0028 -0.0021 130 SER A O   
1020  C CB  . SER A 130 ? 0.2365 0.2425 0.2689 0.0015  0.0030  -0.0064 130 SER A CB  
1021  O OG  . SER A 130 ? 0.2559 0.2633 0.2953 -0.0001 0.0074  -0.0089 130 SER A OG  
1022  N N   . HIS A 131 ? 0.2620 0.2618 0.2778 0.0017  -0.0007 -0.0028 131 HIS A N   
1023  C CA  . HIS A 131 ? 0.2450 0.2453 0.2585 0.0028  -0.0044 -0.0012 131 HIS A CA  
1024  C C   . HIS A 131 ? 0.2590 0.2552 0.2669 0.0007  -0.0065 0.0003  131 HIS A C   
1025  O O   . HIS A 131 ? 0.2538 0.2511 0.2636 0.0021  -0.0098 0.0012  131 HIS A O   
1026  C CB  . HIS A 131 ? 0.2485 0.2489 0.2609 0.0032  -0.0041 -0.0012 131 HIS A CB  
1027  C CG  . HIS A 131 ? 0.2176 0.2211 0.2345 0.0056  -0.0043 -0.0016 131 HIS A CG  
1028  N ND1 . HIS A 131 ? 0.2344 0.2368 0.2510 0.0060  -0.0032 -0.0019 131 HIS A ND1 
1029  C CD2 . HIS A 131 ? 0.2197 0.2257 0.2399 0.0074  -0.0060 -0.0017 131 HIS A CD2 
1030  C CE1 . HIS A 131 ? 0.2306 0.2344 0.2503 0.0080  -0.0048 -0.0017 131 HIS A CE1 
1031  N NE2 . HIS A 131 ? 0.2555 0.2614 0.2766 0.0086  -0.0066 -0.0016 131 HIS A NE2 
1032  N N   . SER A 132 ? 0.2787 0.2691 0.2794 -0.0028 -0.0047 0.0004  132 SER A N   
1033  C CA  . SER A 132 ? 0.2493 0.2335 0.2425 -0.0054 -0.0082 0.0025  132 SER A CA  
1034  C C   . SER A 132 ? 0.2677 0.2500 0.2611 -0.0057 -0.0091 0.0031  132 SER A C   
1035  O O   . SER A 132 ? 0.2835 0.2646 0.2777 -0.0047 -0.0140 0.0048  132 SER A O   
1036  C CB  . SER A 132 ? 0.2426 0.2184 0.2241 -0.0104 -0.0061 0.0025  132 SER A CB  
1037  O OG  . SER A 132 ? 0.3009 0.2751 0.2814 -0.0125 0.0004  0.0002  132 SER A OG  
1038  N N   . LYS A 133 ? 0.2476 0.2298 0.2417 -0.0071 -0.0044 0.0014  133 LYS A N   
1039  C CA  . LYS A 133 ? 0.2573 0.2363 0.2501 -0.0086 -0.0047 0.0018  133 LYS A CA  
1040  C C   . LYS A 133 ? 0.2688 0.2524 0.2693 -0.0046 -0.0085 0.0022  133 LYS A C   
1041  O O   . LYS A 133 ? 0.2769 0.2563 0.2753 -0.0051 -0.0114 0.0036  133 LYS A O   
1042  C CB  . LYS A 133 ? 0.2972 0.2773 0.2926 -0.0108 0.0016  -0.0008 133 LYS A CB  
1043  C CG  . LYS A 133 ? 0.2693 0.2442 0.2575 -0.0151 0.0074  -0.0023 133 LYS A CG  
1044  C CD  . LYS A 133 ? 0.2971 0.2603 0.2696 -0.0204 0.0062  -0.0002 133 LYS A CD  
1045  C CE  . LYS A 133 ? 0.3241 0.2807 0.2862 -0.0249 0.0109  -0.0015 133 LYS A CE  
1046  N NZ  . LYS A 133 ? 0.3544 0.2984 0.2990 -0.0298 0.0061  0.0018  133 LYS A NZ  
1047  N N   . TRP A 134 ? 0.2363 0.2274 0.2448 -0.0011 -0.0082 0.0009  134 TRP A N   
1048  C CA  . TRP A 134 ? 0.2105 0.2048 0.2246 0.0019  -0.0107 0.0005  134 TRP A CA  
1049  C C   . TRP A 134 ? 0.2553 0.2468 0.2688 0.0030  -0.0148 0.0021  134 TRP A C   
1050  O O   . TRP A 134 ? 0.2648 0.2539 0.2797 0.0036  -0.0167 0.0023  134 TRP A O   
1051  C CB  . TRP A 134 ? 0.2185 0.2186 0.2371 0.0045  -0.0101 -0.0007 134 TRP A CB  
1052  C CG  . TRP A 134 ? 0.2348 0.2375 0.2571 0.0067  -0.0113 -0.0017 134 TRP A CG  
1053  C CD1 . TRP A 134 ? 0.2470 0.2484 0.2709 0.0079  -0.0129 -0.0019 134 TRP A CD1 
1054  C CD2 . TRP A 134 ? 0.2360 0.2417 0.2602 0.0077  -0.0108 -0.0029 134 TRP A CD2 
1055  N NE1 . TRP A 134 ? 0.2434 0.2469 0.2690 0.0092  -0.0123 -0.0038 134 TRP A NE1 
1056  C CE2 . TRP A 134 ? 0.2735 0.2790 0.2980 0.0088  -0.0115 -0.0041 134 TRP A CE2 
1057  C CE3 . TRP A 134 ? 0.2198 0.2274 0.2452 0.0077  -0.0103 -0.0032 134 TRP A CE3 
1058  C CZ2 . TRP A 134 ? 0.2447 0.2508 0.2679 0.0090  -0.0117 -0.0053 134 TRP A CZ2 
1059  C CZ3 . TRP A 134 ? 0.2195 0.2280 0.2450 0.0085  -0.0117 -0.0038 134 TRP A CZ3 
1060  C CH2 . TRP A 134 ? 0.2350 0.2421 0.2579 0.0087  -0.0125 -0.0047 134 TRP A CH2 
1061  N N   . TYR A 135 ? 0.2359 0.2280 0.2490 0.0033  -0.0165 0.0030  135 TYR A N   
1062  C CA  . TYR A 135 ? 0.2340 0.2252 0.2505 0.0049  -0.0210 0.0042  135 TYR A CA  
1063  C C   . TYR A 135 ? 0.2466 0.2298 0.2568 0.0025  -0.0257 0.0071  135 TYR A C   
1064  O O   . TYR A 135 ? 0.2779 0.2594 0.2929 0.0042  -0.0306 0.0082  135 TYR A O   
1065  C CB  . TYR A 135 ? 0.2187 0.2153 0.2404 0.0065  -0.0211 0.0034  135 TYR A CB  
1066  C CG  . TYR A 135 ? 0.2671 0.2693 0.2941 0.0088  -0.0177 0.0008  135 TYR A CG  
1067  C CD1 . TYR A 135 ? 0.2662 0.2696 0.2995 0.0109  -0.0178 -0.0007 135 TYR A CD1 
1068  C CD2 . TYR A 135 ? 0.2835 0.2882 0.3082 0.0084  -0.0144 -0.0001 135 TYR A CD2 
1069  C CE1 . TYR A 135 ? 0.2696 0.2761 0.3047 0.0119  -0.0143 -0.0033 135 TYR A CE1 
1070  C CE2 . TYR A 135 ? 0.2733 0.2808 0.3000 0.0096  -0.0122 -0.0020 135 TYR A CE2 
1071  C CZ  . TYR A 135 ? 0.2966 0.3047 0.3273 0.0109  -0.0119 -0.0036 135 TYR A CZ  
1072  O OH  . TYR A 135 ? 0.2956 0.3046 0.3250 0.0110  -0.0094 -0.0056 135 TYR A OH  
1073  N N   . GLN A 136 ? 0.2429 0.2200 0.2425 -0.0017 -0.0243 0.0081  136 GLN A N   
1074  C CA  . GLN A 136 ? 0.2767 0.2434 0.2669 -0.0051 -0.0286 0.0110  136 GLN A CA  
1075  C C   . GLN A 136 ? 0.2504 0.2137 0.2424 -0.0042 -0.0303 0.0116  136 GLN A C   
1076  O O   . GLN A 136 ? 0.3090 0.2657 0.2998 -0.0041 -0.0367 0.0142  136 GLN A O   
1077  C CB  . GLN A 136 ? 0.2755 0.2353 0.2525 -0.0106 -0.0246 0.0112  136 GLN A CB  
1078  C CG  . GLN A 136 ? 0.2948 0.2542 0.2671 -0.0123 -0.0250 0.0113  136 GLN A CG  
1079  C CD  . GLN A 136 ? 0.2915 0.2429 0.2500 -0.0183 -0.0198 0.0106  136 GLN A CD  
1080  O OE1 . GLN A 136 ? 0.3452 0.2999 0.3058 -0.0188 -0.0123 0.0077  136 GLN A OE1 
1081  N NE2 . GLN A 136 ? 0.2978 0.2380 0.2422 -0.0232 -0.0240 0.0131  136 GLN A NE2 
1082  N N   . HIS A 137 ? 0.2296 0.1963 0.2244 -0.0038 -0.0250 0.0093  137 HIS A N   
1083  C CA  . HIS A 137 ? 0.2547 0.2176 0.2509 -0.0033 -0.0265 0.0096  137 HIS A CA  
1084  C C   . HIS A 137 ? 0.2842 0.2506 0.2915 0.0018  -0.0303 0.0090  137 HIS A C   
1085  O O   . HIS A 137 ? 0.2899 0.2499 0.2980 0.0026  -0.0350 0.0107  137 HIS A O   
1086  C CB  . HIS A 137 ? 0.2472 0.2138 0.2451 -0.0043 -0.0204 0.0069  137 HIS A CB  
1087  C CG  . HIS A 137 ? 0.2569 0.2188 0.2551 -0.0047 -0.0214 0.0070  137 HIS A CG  
1088  N ND1 . HIS A 137 ? 0.2991 0.2498 0.2877 -0.0086 -0.0233 0.0095  137 HIS A ND1 
1089  C CD2 . HIS A 137 ? 0.2951 0.2604 0.3006 -0.0020 -0.0211 0.0049  137 HIS A CD2 
1090  C CE1 . HIS A 137 ? 0.3057 0.2536 0.2968 -0.0081 -0.0241 0.0090  137 HIS A CE1 
1091  N NE2 . HIS A 137 ? 0.2857 0.2425 0.2872 -0.0040 -0.0227 0.0061  137 HIS A NE2 
1092  N N   . VAL A 138 ? 0.2616 0.2374 0.2775 0.0051  -0.0279 0.0065  138 VAL A N   
1093  C CA  . VAL A 138 ? 0.2740 0.2536 0.3009 0.0093  -0.0295 0.0050  138 VAL A CA  
1094  C C   . VAL A 138 ? 0.2892 0.2657 0.3203 0.0106  -0.0362 0.0073  138 VAL A C   
1095  O O   . VAL A 138 ? 0.2606 0.2348 0.2994 0.0133  -0.0396 0.0072  138 VAL A O   
1096  C CB  . VAL A 138 ? 0.2518 0.2405 0.2841 0.0111  -0.0251 0.0020  138 VAL A CB  
1097  C CG1 . VAL A 138 ? 0.3076 0.2999 0.3512 0.0146  -0.0258 0.0000  138 VAL A CG1 
1098  C CG2 . VAL A 138 ? 0.2339 0.2250 0.2634 0.0102  -0.0204 -0.0002 138 VAL A CG2 
1099  N N   . ALA A 139 ? 0.2432 0.2192 0.2703 0.0087  -0.0388 0.0094  139 ALA A N   
1100  C CA  . ALA A 139 ? 0.2581 0.2321 0.2911 0.0100  -0.0464 0.0116  139 ALA A CA  
1101  C C   . ALA A 139 ? 0.3158 0.2780 0.3429 0.0086  -0.0535 0.0153  139 ALA A C   
1102  O O   . ALA A 139 ? 0.2982 0.2584 0.3349 0.0114  -0.0605 0.0166  139 ALA A O   
1103  C CB  . ALA A 139 ? 0.2875 0.2627 0.3156 0.0074  -0.0478 0.0129  139 ALA A CB  
1104  N N   . LYS A 140 ? 0.2979 0.2521 0.3100 0.0042  -0.0514 0.0168  140 LYS A N   
1105  C CA  . LYS A 140 ? 0.3242 0.2654 0.3276 0.0019  -0.0571 0.0203  140 LYS A CA  
1106  C C   . LYS A 140 ? 0.3355 0.2759 0.3482 0.0056  -0.0574 0.0190  140 LYS A C   
1107  O O   . LYS A 140 ? 0.3570 0.2894 0.3723 0.0070  -0.0652 0.0217  140 LYS A O   
1108  C CB  . LYS A 140 ? 0.3741 0.3080 0.3596 -0.0046 -0.0524 0.0212  140 LYS A CB  
1109  C CG  . LYS A 140 ? 0.4252 0.3434 0.3974 -0.0088 -0.0576 0.0253  140 LYS A CG  
1110  C CD  . LYS A 140 ? 0.4262 0.3418 0.3984 -0.0090 -0.0538 0.0240  140 LYS A CD  
1111  C CE  . LYS A 140 ? 0.4498 0.3705 0.4179 -0.0121 -0.0436 0.0208  140 LYS A CE  
1112  N NZ  . LYS A 140 ? 0.4585 0.3731 0.4234 -0.0141 -0.0414 0.0205  140 LYS A NZ  
1113  N N   . GLU A 141 ? 0.3176 0.2653 0.3348 0.0071  -0.0496 0.0150  141 GLU A N   
1114  C CA  . GLU A 141 ? 0.3069 0.2528 0.3319 0.0102  -0.0495 0.0133  141 GLU A CA  
1115  C C   . GLU A 141 ? 0.3377 0.2888 0.3804 0.0162  -0.0523 0.0113  141 GLU A C   
1116  O O   . GLU A 141 ? 0.3563 0.3024 0.4059 0.0190  -0.0550 0.0108  141 GLU A O   
1117  C CB  . GLU A 141 ? 0.3132 0.2646 0.3376 0.0097  -0.0414 0.0094  141 GLU A CB  
1118  C CG  . GLU A 141 ? 0.3304 0.2768 0.3415 0.0042  -0.0382 0.0106  141 GLU A CG  
1119  C CD  . GLU A 141 ? 0.3768 0.3104 0.3808 0.0017  -0.0418 0.0132  141 GLU A CD  
1120  O OE1 . GLU A 141 ? 0.3753 0.3064 0.3867 0.0051  -0.0441 0.0123  141 GLU A OE1 
1121  O OE2 . GLU A 141 ? 0.3891 0.3140 0.3796 -0.0038 -0.0424 0.0161  141 GLU A OE2 
1122  N N   . GLU A 142 ? 0.3194 0.2803 0.3705 0.0181  -0.0509 0.0095  142 GLU A N   
1123  C CA  . GLU A 142 ? 0.2805 0.2477 0.3503 0.0232  -0.0519 0.0068  142 GLU A CA  
1124  C C   . GLU A 142 ? 0.3273 0.2917 0.4043 0.0245  -0.0618 0.0102  142 GLU A C   
1125  O O   . GLU A 142 ? 0.3119 0.2807 0.4075 0.0290  -0.0639 0.0081  142 GLU A O   
1126  C CB  . GLU A 142 ? 0.2601 0.2394 0.3352 0.0238  -0.0441 0.0025  142 GLU A CB  
1127  C CG  . GLU A 142 ? 0.3039 0.2852 0.3722 0.0225  -0.0360 -0.0007 142 GLU A CG  
1128  C CD  . GLU A 142 ? 0.4042 0.3855 0.4816 0.0256  -0.0323 -0.0051 142 GLU A CD  
1129  O OE1 . GLU A 142 ? 0.3671 0.3438 0.4539 0.0285  -0.0367 -0.0048 142 GLU A OE1 
1130  O OE2 . GLU A 142 ? 0.3723 0.3572 0.4471 0.0248  -0.0253 -0.0089 142 GLU A OE2 
1131  N N   A LYS A 143 ? 0.3166 0.2742 0.3799 0.0202  -0.0676 0.0151  143 LYS A N   
1132  N N   B LYS A 143 ? 0.3182 0.2746 0.3812 0.0203  -0.0681 0.0154  143 LYS A N   
1133  C CA  A LYS A 143 ? 0.3166 0.2698 0.3831 0.0202  -0.0786 0.0192  143 LYS A CA  
1134  C CA  B LYS A 143 ? 0.3166 0.2699 0.3831 0.0202  -0.0785 0.0192  143 LYS A CA  
1135  C C   A LYS A 143 ? 0.3106 0.2762 0.3941 0.0229  -0.0784 0.0167  143 LYS A C   
1136  C C   B LYS A 143 ? 0.3100 0.2762 0.3941 0.0232  -0.0774 0.0161  143 LYS A C   
1137  O O   A LYS A 143 ? 0.2963 0.2640 0.3977 0.0266  -0.0854 0.0168  143 LYS A O   
1138  O O   B LYS A 143 ? 0.2955 0.2652 0.3994 0.0277  -0.0822 0.0151  143 LYS A O   
1139  C CB  A LYS A 143 ? 0.3493 0.2924 0.4222 0.0228  -0.0880 0.0221  143 LYS A CB  
1140  C CB  B LYS A 143 ? 0.3495 0.2924 0.4223 0.0226  -0.0892 0.0225  143 LYS A CB  
1141  C CG  A LYS A 143 ? 0.4089 0.3400 0.4659 0.0200  -0.0867 0.0239  143 LYS A CG  
1142  C CG  B LYS A 143 ? 0.4104 0.3394 0.4673 0.0197  -0.0903 0.0254  143 LYS A CG  
1143  C CD  A LYS A 143 ? 0.4290 0.3488 0.4922 0.0228  -0.0963 0.0268  143 LYS A CD  
1144  C CD  B LYS A 143 ? 0.4357 0.3531 0.4988 0.0222  -0.1027 0.0294  143 LYS A CD  
1145  C CE  A LYS A 143 ? 0.4812 0.3826 0.5211 0.0169  -0.1013 0.0324  143 LYS A CE  
1146  C CE  B LYS A 143 ? 0.4593 0.3701 0.5251 0.0246  -0.1010 0.0282  143 LYS A CE  
1147  N NZ  A LYS A 143 ? 0.4180 0.3130 0.4360 0.0096  -0.1028 0.0362  143 LYS A NZ  
1148  N NZ  B LYS A 143 ? 0.5232 0.4190 0.5892 0.0255  -0.1142 0.0336  143 LYS A NZ  
1149  N N   . ILE A 144 ? 0.2906 0.2639 0.3685 0.0206  -0.0707 0.0145  144 ILE A N   
1150  C CA  . ILE A 144 ? 0.2764 0.2613 0.3678 0.0221  -0.0687 0.0117  144 ILE A CA  
1151  C C   . ILE A 144 ? 0.2857 0.2700 0.3645 0.0174  -0.0702 0.0141  144 ILE A C   
1152  O O   . ILE A 144 ? 0.3112 0.2890 0.3708 0.0132  -0.0679 0.0160  144 ILE A O   
1153  C CB  . ILE A 144 ? 0.2870 0.2818 0.3857 0.0241  -0.0571 0.0058  144 ILE A CB  
1154  C CG1 . ILE A 144 ? 0.2599 0.2530 0.3408 0.0210  -0.0495 0.0053  144 ILE A CG1 
1155  C CG2 . ILE A 144 ? 0.2763 0.2721 0.3900 0.0287  -0.0553 0.0024  144 ILE A CG2 
1156  C CD1 . ILE A 144 ? 0.2966 0.2979 0.3821 0.0221  -0.0398 0.0003  144 ILE A CD1 
1157  N N   . PRO A 145 ? 0.2711 0.2625 0.3613 0.0178  -0.0728 0.0134  145 PRO A N   
1158  C CA  . PRO A 145 ? 0.2882 0.2798 0.3673 0.0133  -0.0729 0.0147  145 PRO A CA  
1159  C C   . PRO A 145 ? 0.2293 0.2245 0.2979 0.0116  -0.0617 0.0121  145 PRO A C   
1160  O O   . PRO A 145 ? 0.2466 0.2482 0.3215 0.0141  -0.0537 0.0083  145 PRO A O   
1161  C CB  . PRO A 145 ? 0.2751 0.2762 0.3738 0.0149  -0.0761 0.0131  145 PRO A CB  
1162  C CG  . PRO A 145 ? 0.3038 0.3075 0.4229 0.0199  -0.0803 0.0120  145 PRO A CG  
1163  C CD  . PRO A 145 ? 0.2653 0.2655 0.3809 0.0222  -0.0749 0.0106  145 PRO A CD  
1164  N N   . GLU A 146 ? 0.2520 0.2428 0.3048 0.0070  -0.0614 0.0138  146 GLU A N   
1165  C CA  . GLU A 146 ? 0.2756 0.2689 0.3191 0.0056  -0.0519 0.0116  146 GLU A CA  
1166  C C   . GLU A 146 ? 0.2704 0.2635 0.3066 0.0019  -0.0518 0.0121  146 GLU A C   
1167  O O   . GLU A 146 ? 0.2940 0.2795 0.3212 -0.0017 -0.0583 0.0150  146 GLU A O   
1168  C CB  . GLU A 146 ? 0.2789 0.2642 0.3075 0.0037  -0.0489 0.0127  146 GLU A CB  
1169  C CG  . GLU A 146 ? 0.2995 0.2725 0.3129 -0.0009 -0.0550 0.0166  146 GLU A CG  
1170  C CD  . GLU A 146 ? 0.3562 0.3215 0.3572 -0.0031 -0.0516 0.0172  146 GLU A CD  
1171  O OE1 . GLU A 146 ? 0.3187 0.2878 0.3184 -0.0027 -0.0435 0.0146  146 GLU A OE1 
1172  O OE2 . GLU A 146 ? 0.4261 0.3810 0.4193 -0.0053 -0.0575 0.0204  146 GLU A OE2 
1173  N N   . PHE A 147 ? 0.2419 0.2418 0.2805 0.0023  -0.0446 0.0092  147 PHE A N   
1174  C CA  . PHE A 147 ? 0.2786 0.2782 0.3107 -0.0009 -0.0434 0.0092  147 PHE A CA  
1175  C C   . PHE A 147 ? 0.2570 0.2568 0.2810 -0.0013 -0.0350 0.0074  147 PHE A C   
1176  O O   . PHE A 147 ? 0.2568 0.2613 0.2857 0.0014  -0.0299 0.0054  147 PHE A O   
1177  C CB  . PHE A 147 ? 0.2571 0.2648 0.3032 -0.0002 -0.0445 0.0077  147 PHE A CB  
1178  C CG  . PHE A 147 ? 0.2619 0.2689 0.3016 -0.0039 -0.0436 0.0076  147 PHE A CG  
1179  C CD1 . PHE A 147 ? 0.3099 0.3115 0.3441 -0.0076 -0.0509 0.0099  147 PHE A CD1 
1180  C CD2 . PHE A 147 ? 0.2989 0.3095 0.3372 -0.0038 -0.0358 0.0052  147 PHE A CD2 
1181  C CE1 . PHE A 147 ? 0.3145 0.3143 0.3416 -0.0114 -0.0498 0.0095  147 PHE A CE1 
1182  C CE2 . PHE A 147 ? 0.2984 0.3070 0.3301 -0.0072 -0.0347 0.0051  147 PHE A CE2 
1183  C CZ  . PHE A 147 ? 0.2839 0.2876 0.3107 -0.0110 -0.0415 0.0070  147 PHE A CZ  
1184  N N   . TYR A 148 ? 0.2512 0.2455 0.2631 -0.0048 -0.0337 0.0079  148 TYR A N   
1185  C CA  . TYR A 148 ? 0.2332 0.2270 0.2389 -0.0049 -0.0265 0.0062  148 TYR A CA  
1186  C C   . TYR A 148 ? 0.2556 0.2486 0.2575 -0.0073 -0.0252 0.0056  148 TYR A C   
1187  O O   . TYR A 148 ? 0.2704 0.2576 0.2650 -0.0110 -0.0288 0.0068  148 TYR A O   
1188  C CB  . TYR A 148 ? 0.2440 0.2302 0.2384 -0.0070 -0.0244 0.0067  148 TYR A CB  
1189  C CG  . TYR A 148 ? 0.2266 0.2124 0.2235 -0.0053 -0.0257 0.0074  148 TYR A CG  
1190  C CD1 . TYR A 148 ? 0.2776 0.2585 0.2726 -0.0065 -0.0324 0.0099  148 TYR A CD1 
1191  C CD2 . TYR A 148 ? 0.2316 0.2214 0.2329 -0.0026 -0.0212 0.0058  148 TYR A CD2 
1192  C CE1 . TYR A 148 ? 0.2660 0.2457 0.2635 -0.0048 -0.0337 0.0106  148 TYR A CE1 
1193  C CE2 . TYR A 148 ? 0.2733 0.2625 0.2770 -0.0012 -0.0223 0.0062  148 TYR A CE2 
1194  C CZ  . TYR A 148 ? 0.2634 0.2474 0.2650 -0.0023 -0.0281 0.0085  148 TYR A CZ  
1195  O OH  . TYR A 148 ? 0.2888 0.2714 0.2928 -0.0009 -0.0292 0.0089  148 TYR A OH  
1196  N N   . LEU A 149 ? 0.2314 0.2289 0.2373 -0.0056 -0.0205 0.0039  149 LEU A N   
1197  C CA  . LEU A 149 ? 0.2353 0.2311 0.2371 -0.0077 -0.0181 0.0031  149 LEU A CA  
1198  C C   . LEU A 149 ? 0.2426 0.2333 0.2366 -0.0080 -0.0133 0.0021  149 LEU A C   
1199  O O   . LEU A 149 ? 0.2540 0.2471 0.2510 -0.0052 -0.0100 0.0013  149 LEU A O   
1200  C CB  . LEU A 149 ? 0.2373 0.2393 0.2469 -0.0061 -0.0158 0.0020  149 LEU A CB  
1201  C CG  . LEU A 149 ? 0.2437 0.2434 0.2493 -0.0082 -0.0134 0.0013  149 LEU A CG  
1202  C CD1 . LEU A 149 ? 0.2540 0.2525 0.2590 -0.0119 -0.0176 0.0019  149 LEU A CD1 
1203  C CD2 . LEU A 149 ? 0.2583 0.2618 0.2684 -0.0069 -0.0100 0.0004  149 LEU A CD2 
1204  N N   . ASP A 150 ? 0.2786 0.2622 0.2630 -0.0116 -0.0128 0.0019  150 ASP A N   
1205  C CA  . ASP A 150 ? 0.2696 0.2483 0.2485 -0.0120 -0.0072 0.0000  150 ASP A CA  
1206  C C   . ASP A 150 ? 0.2786 0.2575 0.2591 -0.0113 -0.0043 -0.0012 150 ASP A C   
1207  O O   . ASP A 150 ? 0.2932 0.2687 0.2691 -0.0143 -0.0054 -0.0013 150 ASP A O   
1208  C CB  . ASP A 150 ? 0.2858 0.2552 0.2522 -0.0171 -0.0072 -0.0002 150 ASP A CB  
1209  C CG  . ASP A 150 ? 0.3150 0.2784 0.2757 -0.0186 0.0000  -0.0031 150 ASP A CG  
1210  O OD1 . ASP A 150 ? 0.3201 0.2873 0.2889 -0.0148 0.0043  -0.0047 150 ASP A OD1 
1211  O OD2 . ASP A 150 ? 0.3027 0.2567 0.2508 -0.0237 0.0012  -0.0039 150 ASP A OD2 
1212  N N   . VAL A 151 ? 0.2546 0.2368 0.2413 -0.0076 -0.0018 -0.0017 151 VAL A N   
1213  C CA  . VAL A 151 ? 0.2734 0.2542 0.2608 -0.0069 0.0000  -0.0023 151 VAL A CA  
1214  C C   . VAL A 151 ? 0.3384 0.3139 0.3246 -0.0064 0.0045  -0.0045 151 VAL A C   
1215  O O   . VAL A 151 ? 0.3134 0.2870 0.3016 -0.0048 0.0057  -0.0048 151 VAL A O   
1216  C CB  . VAL A 151 ? 0.2311 0.2168 0.2247 -0.0038 -0.0010 -0.0013 151 VAL A CB  
1217  C CG1 . VAL A 151 ? 0.2605 0.2514 0.2570 -0.0045 -0.0038 -0.0003 151 VAL A CG1 
1218  C CG2 . VAL A 151 ? 0.2544 0.2423 0.2527 -0.0005 -0.0003 -0.0016 151 VAL A CG2 
1219  N N   . GLY A 152 ? 0.3158 0.2881 0.2987 -0.0080 0.0074  -0.0061 152 GLY A N   
1220  C CA  . GLY A 152 ? 0.3131 0.2810 0.2972 -0.0075 0.0131  -0.0091 152 GLY A CA  
1221  C C   . GLY A 152 ? 0.2895 0.2493 0.2660 -0.0107 0.0160  -0.0110 152 GLY A C   
1222  O O   . GLY A 152 ? 0.3492 0.3023 0.3168 -0.0149 0.0195  -0.0131 152 GLY A O   
1223  N N   . VAL A 153 ? 0.2747 0.2338 0.2533 -0.0092 0.0147  -0.0104 153 VAL A N   
1224  C CA  . VAL A 153 ? 0.3047 0.2556 0.2762 -0.0121 0.0171  -0.0122 153 VAL A CA  
1225  C C   . VAL A 153 ? 0.2936 0.2414 0.2723 -0.0085 0.0205  -0.0141 153 VAL A C   
1226  O O   . VAL A 153 ? 0.3585 0.2990 0.3329 -0.0101 0.0227  -0.0157 153 VAL A O   
1227  C CB  . VAL A 153 ? 0.3286 0.2796 0.2951 -0.0149 0.0124  -0.0099 153 VAL A CB  
1228  C CG1 . VAL A 153 ? 0.3164 0.2689 0.2767 -0.0188 0.0085  -0.0084 153 VAL A CG1 
1229  C CG2 . VAL A 153 ? 0.3068 0.2635 0.2805 -0.0114 0.0091  -0.0072 153 VAL A CG2 
1230  N N   . GLY A 154 ? 0.3232 0.2756 0.3131 -0.0039 0.0211  -0.0144 154 GLY A N   
1231  C CA  . GLY A 154 ? 0.3101 0.2594 0.3092 -0.0001 0.0236  -0.0164 154 GLY A CA  
1232  C C   . GLY A 154 ? 0.3130 0.2623 0.3152 0.0030  0.0181  -0.0130 154 GLY A C   
1233  O O   . GLY A 154 ? 0.2972 0.2492 0.2942 0.0017  0.0136  -0.0097 154 GLY A O   
1234  N N   . PRO A 155 ? 0.3125 0.2577 0.3230 0.0067  0.0185  -0.0140 155 PRO A N   
1235  C CA  . PRO A 155 ? 0.3145 0.2580 0.3271 0.0097  0.0122  -0.0103 155 PRO A CA  
1236  C C   . PRO A 155 ? 0.3178 0.2563 0.3181 0.0059  0.0105  -0.0081 155 PRO A C   
1237  O O   . PRO A 155 ? 0.3068 0.2393 0.3006 0.0027  0.0140  -0.0101 155 PRO A O   
1238  C CB  . PRO A 155 ? 0.3586 0.2965 0.3826 0.0140  0.0133  -0.0124 155 PRO A CB  
1239  C CG  . PRO A 155 ? 0.3774 0.3190 0.4106 0.0147  0.0199  -0.0172 155 PRO A CG  
1240  C CD  . PRO A 155 ? 0.3301 0.2724 0.3501 0.0087  0.0245  -0.0187 155 PRO A CD  
1241  N N   . TYR A 156 ? 0.3010 0.2408 0.2985 0.0061  0.0053  -0.0042 156 TYR A N   
1242  C CA  . TYR A 156 ? 0.2728 0.2082 0.2601 0.0022  0.0040  -0.0021 156 TYR A CA  
1243  C C   . TYR A 156 ? 0.3055 0.2298 0.2902 0.0020  0.0052  -0.0029 156 TYR A C   
1244  O O   . TYR A 156 ? 0.3308 0.2511 0.3074 -0.0024 0.0069  -0.0033 156 TYR A O   
1245  C CB  . TYR A 156 ? 0.3215 0.2577 0.3062 0.0026  -0.0009 0.0017  156 TYR A CB  
1246  C CG  . TYR A 156 ? 0.2774 0.2102 0.2519 -0.0023 -0.0009 0.0035  156 TYR A CG  
1247  C CD1 . TYR A 156 ? 0.3190 0.2579 0.2905 -0.0064 0.0013  0.0025  156 TYR A CD1 
1248  C CD2 . TYR A 156 ? 0.3253 0.2483 0.2938 -0.0031 -0.0033 0.0059  156 TYR A CD2 
1249  C CE1 . TYR A 156 ? 0.3214 0.2585 0.2864 -0.0112 0.0019  0.0033  156 TYR A CE1 
1250  C CE2 . TYR A 156 ? 0.3769 0.2966 0.3358 -0.0086 -0.0022 0.0071  156 TYR A CE2 
1251  C CZ  . TYR A 156 ? 0.3559 0.2838 0.3145 -0.0125 0.0008  0.0055  156 TYR A CZ  
1252  O OH  . TYR A 156 ? 0.4067 0.3330 0.3591 -0.0180 0.0025  0.0059  156 TYR A OH  
1253  N N   A ARG A 157 ? 0.3238 0.2434 0.3169 0.0067  0.0040  -0.0032 157 ARG A N   
1254  N N   B ARG A 157 ? 0.3241 0.2436 0.3171 0.0067  0.0040  -0.0032 157 ARG A N   
1255  C CA  A ARG A 157 ? 0.3196 0.2276 0.3115 0.0072  0.0045  -0.0038 157 ARG A CA  
1256  C CA  B ARG A 157 ? 0.3203 0.2281 0.3120 0.0071  0.0045  -0.0038 157 ARG A CA  
1257  C C   A ARG A 157 ? 0.3343 0.2387 0.3239 0.0046  0.0114  -0.0086 157 ARG A C   
1258  C C   B ARG A 157 ? 0.3345 0.2389 0.3252 0.0051  0.0115  -0.0088 157 ARG A C   
1259  O O   A ARG A 157 ? 0.3685 0.2628 0.3534 0.0032  0.0127  -0.0093 157 ARG A O   
1260  O O   B ARG A 157 ? 0.3659 0.2599 0.3542 0.0047  0.0130  -0.0099 157 ARG A O   
1261  C CB  A ARG A 157 ? 0.3734 0.2777 0.3780 0.0136  0.0012  -0.0035 157 ARG A CB  
1262  C CB  B ARG A 157 ? 0.3741 0.2773 0.3773 0.0133  0.0005  -0.0029 157 ARG A CB  
1263  C CG  A ARG A 157 ? 0.3731 0.2849 0.3921 0.0172  0.0050  -0.0076 157 ARG A CG  
1264  C CG  B ARG A 157 ? 0.3739 0.2838 0.3927 0.0177  0.0035  -0.0067 157 ARG A CG  
1265  C CD  A ARG A 157 ? 0.4178 0.3246 0.4529 0.0231  0.0051  -0.0101 157 ARG A CD  
1266  C CD  B ARG A 157 ? 0.4016 0.3066 0.4363 0.0241  0.0005  -0.0074 157 ARG A CD  
1267  N NE  A ARG A 157 ? 0.4407 0.3464 0.4835 0.0276  -0.0042 -0.0058 157 ARG A NE  
1268  N NE  B ARG A 157 ? 0.3828 0.2960 0.4334 0.0272  0.0051  -0.0119 157 ARG A NE  
1269  C CZ  A ARG A 157 ? 0.4003 0.3085 0.4621 0.0335  -0.0070 -0.0069 157 ARG A CZ  
1270  C CZ  B ARG A 157 ? 0.3714 0.2850 0.4250 0.0259  0.0146  -0.0178 157 ARG A CZ  
1271  N NH1 A ARG A 157 ? 0.3695 0.2832 0.4464 0.0357  0.0001  -0.0127 157 ARG A NH1 
1272  N NH1 B ARG A 157 ? 0.4224 0.3272 0.4666 0.0227  0.0197  -0.0202 157 ARG A NH1 
1273  N NH2 A ARG A 157 ? 0.3784 0.2834 0.4439 0.0367  -0.0173 -0.0021 157 ARG A NH2 
1274  N NH2 B ARG A 157 ? 0.3784 0.3005 0.4430 0.0269  0.0193  -0.0215 157 ARG A NH2 
1275  N N   . ASP A 158 ? 0.3241 0.2353 0.3154 0.0035  0.0158  -0.0117 158 ASP A N   
1276  C CA  . ASP A 158 ? 0.3383 0.2451 0.3249 0.0000  0.0226  -0.0165 158 ASP A CA  
1277  C C   . ASP A 158 ? 0.3559 0.2650 0.3297 -0.0065 0.0226  -0.0159 158 ASP A C   
1278  O O   . ASP A 158 ? 0.3663 0.2721 0.3337 -0.0104 0.0271  -0.0194 158 ASP A O   
1279  C CB  . ASP A 158 ? 0.3326 0.2434 0.3282 0.0021  0.0279  -0.0206 158 ASP A CB  
1280  C CG  . ASP A 158 ? 0.3423 0.2520 0.3547 0.0089  0.0283  -0.0221 158 ASP A CG  
1281  O OD1 . ASP A 158 ? 0.4160 0.3179 0.4314 0.0115  0.0259  -0.0212 158 ASP A OD1 
1282  O OD2 . ASP A 158 ? 0.4365 0.3522 0.4594 0.0112  0.0313  -0.0247 158 ASP A OD2 
1283  N N   . MET A 159 ? 0.3312 0.2457 0.3017 -0.0080 0.0175  -0.0118 159 MET A N   
1284  C CA  . MET A 159 ? 0.3729 0.2922 0.3357 -0.0132 0.0162  -0.0111 159 MET A CA  
1285  C C   . MET A 159 ? 0.3796 0.2908 0.3325 -0.0189 0.0183  -0.0132 159 MET A C   
1286  O O   . MET A 159 ? 0.3969 0.2989 0.3471 -0.0195 0.0195  -0.0139 159 MET A O   
1287  C CB  . MET A 159 ? 0.4216 0.3459 0.3843 -0.0139 0.0117  -0.0071 159 MET A CB  
1288  C CG  . MET A 159 ? 0.4427 0.3757 0.4041 -0.0171 0.0094  -0.0058 159 MET A CG  
1289  S SD  . MET A 159 ? 0.4334 0.3744 0.3977 -0.0162 0.0094  -0.0068 159 MET A SD  
1290  C CE  . MET A 159 ? 0.3916 0.3352 0.3649 -0.0095 0.0097  -0.0063 159 MET A CE  
1291  N N   . THR A 160 ? 0.3373 0.2502 0.2838 -0.0235 0.0184  -0.0144 160 THR A N   
1292  C CA  . THR A 160 ? 0.3786 0.2844 0.3144 -0.0300 0.0186  -0.0160 160 THR A CA  
1293  C C   . THR A 160 ? 0.3728 0.2860 0.3071 -0.0340 0.0130  -0.0133 160 THR A C   
1294  O O   . THR A 160 ? 0.3255 0.2487 0.2662 -0.0318 0.0101  -0.0110 160 THR A O   
1295  C CB  . THR A 160 ? 0.3690 0.2682 0.2969 -0.0329 0.0230  -0.0199 160 THR A CB  
1296  O OG1 . THR A 160 ? 0.3496 0.2561 0.2772 -0.0336 0.0206  -0.0187 160 THR A OG1 
1297  C CG2 . THR A 160 ? 0.3788 0.2726 0.3118 -0.0285 0.0298  -0.0235 160 THR A CG2 
1298  N N   . ASP A 161 ? 0.3254 0.3008 0.3200 -0.0283 -0.0034 -0.0256 161 ASP A N   
1299  C CA  . ASP A 161 ? 0.3224 0.3081 0.3338 -0.0338 -0.0032 -0.0271 161 ASP A CA  
1300  C C   . ASP A 161 ? 0.3004 0.3020 0.3121 -0.0313 -0.0105 -0.0277 161 ASP A C   
1301  O O   . ASP A 161 ? 0.3015 0.3107 0.3196 -0.0320 -0.0092 -0.0251 161 ASP A O   
1302  C CB  . ASP A 161 ? 0.3652 0.3515 0.3929 -0.0403 -0.0045 -0.0353 161 ASP A CB  
1303  C CG  . ASP A 161 ? 0.4213 0.3897 0.4534 -0.0446 0.0060  -0.0346 161 ASP A CG  
1304  O OD1 . ASP A 161 ? 0.4525 0.4102 0.4798 -0.0436 0.0164  -0.0271 161 ASP A OD1 
1305  O OD2 . ASP A 161 ? 0.4706 0.4347 0.5107 -0.0484 0.0046  -0.0421 161 ASP A OD2 
1306  N N   . ALA A 162 ? 0.2877 0.2930 0.2919 -0.0278 -0.0171 -0.0309 162 ALA A N   
1307  C CA  . ALA A 162 ? 0.3090 0.3255 0.3107 -0.0241 -0.0218 -0.0305 162 ALA A CA  
1308  C C   . ALA A 162 ? 0.2843 0.3019 0.2807 -0.0214 -0.0178 -0.0242 162 ALA A C   
1309  O O   . ALA A 162 ? 0.2925 0.3176 0.2916 -0.0203 -0.0180 -0.0221 162 ALA A O   
1310  C CB  . ALA A 162 ? 0.3213 0.3381 0.3134 -0.0197 -0.0272 -0.0343 162 ALA A CB  
1311  N N   . ARG A 163 ? 0.2745 0.2850 0.2633 -0.0194 -0.0146 -0.0223 163 ARG A N   
1312  C CA  . ARG A 163 ? 0.2954 0.3083 0.2821 -0.0166 -0.0118 -0.0190 163 ARG A CA  
1313  C C   . ARG A 163 ? 0.2980 0.3124 0.2910 -0.0185 -0.0085 -0.0156 163 ARG A C   
1314  O O   . ARG A 163 ? 0.2723 0.2929 0.2679 -0.0175 -0.0077 -0.0137 163 ARG A O   
1315  C CB  . ARG A 163 ? 0.2857 0.2924 0.2644 -0.0125 -0.0107 -0.0200 163 ARG A CB  
1316  C CG  . ARG A 163 ? 0.3228 0.3306 0.2972 -0.0101 -0.0131 -0.0235 163 ARG A CG  
1317  C CD  . ARG A 163 ? 0.2866 0.2889 0.2540 -0.0050 -0.0133 -0.0262 163 ARG A CD  
1318  N NE  . ARG A 163 ? 0.3408 0.3462 0.3069 -0.0032 -0.0146 -0.0298 163 ARG A NE  
1319  C CZ  . ARG A 163 ? 0.3482 0.3516 0.3099 0.0016  -0.0156 -0.0337 163 ARG A CZ  
1320  N NH1 . ARG A 163 ? 0.3248 0.3228 0.2810 0.0065  -0.0164 -0.0346 163 ARG A NH1 
1321  N NH2 . ARG A 163 ? 0.2979 0.3045 0.2598 0.0026  -0.0156 -0.0367 163 ARG A NH2 
1322  N N   . LEU A 164 ? 0.2831 0.2906 0.2784 -0.0209 -0.0051 -0.0147 164 LEU A N   
1323  C CA  . LEU A 164 ? 0.2931 0.3011 0.2943 -0.0223 -0.0002 -0.0112 164 LEU A CA  
1324  C C   . LEU A 164 ? 0.3168 0.3364 0.3307 -0.0259 -0.0027 -0.0125 164 LEU A C   
1325  O O   . LEU A 164 ? 0.2781 0.3029 0.2956 -0.0253 -0.0009 -0.0098 164 LEU A O   
1326  C CB  . LEU A 164 ? 0.3147 0.3097 0.3151 -0.0238 0.0069  -0.0093 164 LEU A CB  
1327  C CG  . LEU A 164 ? 0.3100 0.3022 0.3154 -0.0249 0.0150  -0.0050 164 LEU A CG  
1328  C CD1 . LEU A 164 ? 0.3519 0.3459 0.3486 -0.0185 0.0157  -0.0015 164 LEU A CD1 
1329  C CD2 . LEU A 164 ? 0.3158 0.2905 0.3185 -0.0258 0.0250  -0.0025 164 LEU A CD2 
1330  N N   . ASP A 165 ? 0.2811 0.3050 0.3007 -0.0282 -0.0077 -0.0174 165 ASP A N   
1331  C CA  . ASP A 165 ? 0.2673 0.3036 0.2965 -0.0285 -0.0125 -0.0203 165 ASP A CA  
1332  C C   . ASP A 165 ? 0.2680 0.3093 0.2900 -0.0235 -0.0138 -0.0167 165 ASP A C   
1333  O O   . ASP A 165 ? 0.2762 0.3250 0.3043 -0.0226 -0.0141 -0.0156 165 ASP A O   
1334  C CB  . ASP A 165 ? 0.3014 0.3413 0.3324 -0.0282 -0.0199 -0.0275 165 ASP A CB  
1335  C CG  . ASP A 165 ? 0.3292 0.3670 0.3743 -0.0343 -0.0192 -0.0339 165 ASP A CG  
1336  O OD1 . ASP A 165 ? 0.3273 0.3602 0.3819 -0.0393 -0.0112 -0.0318 165 ASP A OD1 
1337  O OD2 . ASP A 165 ? 0.3135 0.3533 0.3600 -0.0338 -0.0259 -0.0414 165 ASP A OD2 
1338  N N   . TYR A 166 ? 0.2474 0.2843 0.2578 -0.0202 -0.0137 -0.0152 166 TYR A N   
1339  C CA  . TYR A 166 ? 0.2065 0.2460 0.2118 -0.0161 -0.0127 -0.0123 166 TYR A CA  
1340  C C   . TYR A 166 ? 0.2374 0.2778 0.2466 -0.0165 -0.0083 -0.0088 166 TYR A C   
1341  O O   . TYR A 166 ? 0.2536 0.2982 0.2647 -0.0145 -0.0077 -0.0067 166 TYR A O   
1342  C CB  . TYR A 166 ? 0.2426 0.2769 0.2392 -0.0139 -0.0112 -0.0126 166 TYR A CB  
1343  C CG  . TYR A 166 ? 0.2521 0.2866 0.2461 -0.0108 -0.0069 -0.0099 166 TYR A CG  
1344  C CD1 . TYR A 166 ? 0.2824 0.3186 0.2732 -0.0070 -0.0067 -0.0075 166 TYR A CD1 
1345  C CD2 . TYR A 166 ? 0.2555 0.2877 0.2505 -0.0110 -0.0027 -0.0108 166 TYR A CD2 
1346  C CE1 . TYR A 166 ? 0.2525 0.2852 0.2404 -0.0042 -0.0002 -0.0043 166 TYR A CE1 
1347  C CE2 . TYR A 166 ? 0.2498 0.2811 0.2463 -0.0094 0.0033  -0.0095 166 TYR A CE2 
1348  C CZ  . TYR A 166 ? 0.2587 0.2888 0.2511 -0.0064 0.0055  -0.0055 166 TYR A CZ  
1349  O OH  . TYR A 166 ? 0.2666 0.2926 0.2602 -0.0048 0.0138  -0.0033 166 TYR A OH  
1350  N N   . VAL A 167 ? 0.2344 0.2703 0.2436 -0.0178 -0.0054 -0.0083 167 VAL A N   
1351  C CA  . VAL A 167 ? 0.2214 0.2579 0.2326 -0.0168 -0.0018 -0.0058 167 VAL A CA  
1352  C C   . VAL A 167 ? 0.2451 0.2858 0.2646 -0.0187 -0.0004 -0.0040 167 VAL A C   
1353  O O   . VAL A 167 ? 0.2559 0.3005 0.2783 -0.0173 0.0011  -0.0020 167 VAL A O   
1354  C CB  . VAL A 167 ? 0.2570 0.2869 0.2622 -0.0145 0.0001  -0.0066 167 VAL A CB  
1355  C CG1 . VAL A 167 ? 0.2627 0.2932 0.2682 -0.0115 0.0029  -0.0052 167 VAL A CG1 
1356  C CG2 . VAL A 167 ? 0.2608 0.2900 0.2618 -0.0122 -0.0018 -0.0102 167 VAL A CG2 
1357  N N   . ALA A 168 ? 0.2250 0.2643 0.2500 -0.0223 0.0003  -0.0051 168 ALA A N   
1358  C CA  . ALA A 168 ? 0.2266 0.2716 0.2641 -0.0250 0.0026  -0.0050 168 ALA A CA  
1359  C C   . ALA A 168 ? 0.2429 0.2995 0.2869 -0.0235 -0.0027 -0.0069 168 ALA A C   
1360  O O   . ALA A 168 ? 0.2249 0.2874 0.2754 -0.0225 -0.0010 -0.0054 168 ALA A O   
1361  C CB  . ALA A 168 ? 0.2468 0.2880 0.2929 -0.0301 0.0054  -0.0076 168 ALA A CB  
1362  N N   . ASN A 169 ? 0.2317 0.2909 0.2719 -0.0215 -0.0091 -0.0102 169 ASN A N   
1363  C CA  . ASN A 169 ? 0.2313 0.2997 0.2736 -0.0169 -0.0144 -0.0120 169 ASN A CA  
1364  C C   . ASN A 169 ? 0.2420 0.3085 0.2760 -0.0122 -0.0117 -0.0066 169 ASN A C   
1365  O O   . ASN A 169 ? 0.2533 0.3263 0.2907 -0.0084 -0.0131 -0.0062 169 ASN A O   
1366  C CB  . ASN A 169 ? 0.2694 0.3390 0.3054 -0.0134 -0.0215 -0.0166 169 ASN A CB  
1367  C CG  . ASN A 169 ? 0.2791 0.3529 0.3281 -0.0183 -0.0253 -0.0245 169 ASN A CG  
1368  O OD1 . ASN A 169 ? 0.3021 0.3794 0.3673 -0.0240 -0.0219 -0.0265 169 ASN A OD1 
1369  N ND2 . ASN A 169 ? 0.3301 0.4028 0.3731 -0.0161 -0.0311 -0.0293 169 ASN A ND2 
1370  N N   . GLN A 170 ? 0.2332 0.2913 0.2582 -0.0121 -0.0077 -0.0035 170 GLN A N   
1371  C CA  . GLN A 170 ? 0.2401 0.2956 0.2612 -0.0089 -0.0035 0.0003  170 GLN A CA  
1372  C C   . GLN A 170 ? 0.2488 0.3074 0.2774 -0.0099 -0.0006 0.0019  170 GLN A C   
1373  O O   . GLN A 170 ? 0.2689 0.3291 0.2977 -0.0065 0.0008  0.0041  170 GLN A O   
1374  C CB  . GLN A 170 ? 0.2392 0.2873 0.2551 -0.0097 0.0004  0.0005  170 GLN A CB  
1375  C CG  . GLN A 170 ? 0.2253 0.2690 0.2332 -0.0077 0.0003  -0.0001 170 GLN A CG  
1376  C CD  . GLN A 170 ? 0.2679 0.3071 0.2763 -0.0091 0.0046  -0.0016 170 GLN A CD  
1377  O OE1 . GLN A 170 ? 0.2583 0.2954 0.2697 -0.0084 0.0097  -0.0010 170 GLN A OE1 
1378  N NE2 . GLN A 170 ? 0.2494 0.2874 0.2565 -0.0109 0.0026  -0.0047 170 GLN A NE2 
1379  N N   . LEU A 171 ? 0.2171 0.2749 0.2501 -0.0137 0.0013  0.0013  171 LEU A N   
1380  C CA  . LEU A 171 ? 0.2520 0.3116 0.2903 -0.0135 0.0053  0.0033  171 LEU A CA  
1381  C C   . LEU A 171 ? 0.2441 0.3135 0.2926 -0.0128 0.0038  0.0028  171 LEU A C   
1382  O O   . LEU A 171 ? 0.2562 0.3282 0.3071 -0.0103 0.0060  0.0049  171 LEU A O   
1383  C CB  . LEU A 171 ? 0.2129 0.2672 0.2512 -0.0160 0.0095  0.0037  171 LEU A CB  
1384  C CG  . LEU A 171 ? 0.2307 0.2766 0.2576 -0.0133 0.0105  0.0035  171 LEU A CG  
1385  C CD1 . LEU A 171 ? 0.2334 0.2711 0.2555 -0.0134 0.0142  0.0043  171 LEU A CD1 
1386  C CD2 . LEU A 171 ? 0.2338 0.2799 0.2589 -0.0091 0.0126  0.0042  171 LEU A CD2 
1387  N N   . HIS A 172 ? 0.2313 0.3070 0.2866 -0.0142 -0.0009 -0.0011 172 HIS A N   
1388  C CA  . HIS A 172 ? 0.2335 0.3212 0.3004 -0.0121 -0.0042 -0.0040 172 HIS A CA  
1389  C C   . HIS A 172 ? 0.2449 0.3336 0.3027 -0.0041 -0.0073 -0.0018 172 HIS A C   
1390  O O   . HIS A 172 ? 0.2691 0.3650 0.3329 -0.0005 -0.0076 -0.0017 172 HIS A O   
1391  C CB  . HIS A 172 ? 0.2392 0.3352 0.3172 -0.0142 -0.0104 -0.0116 172 HIS A CB  
1392  C CG  . HIS A 172 ? 0.2592 0.3552 0.3521 -0.0223 -0.0052 -0.0144 172 HIS A CG  
1393  N ND1 . HIS A 172 ? 0.2342 0.3373 0.3452 -0.0257 0.0001  -0.0160 172 HIS A ND1 
1394  C CD2 . HIS A 172 ? 0.2577 0.3455 0.3496 -0.0275 -0.0030 -0.0156 172 HIS A CD2 
1395  C CE1 . HIS A 172 ? 0.2623 0.3600 0.3829 -0.0329 0.0068  -0.0175 172 HIS A CE1 
1396  N NE2 . HIS A 172 ? 0.2696 0.3576 0.3782 -0.0338 0.0047  -0.0173 172 HIS A NE2 
1397  N N   . ASP A 173 ? 0.2365 0.3172 0.2798 -0.0008 -0.0083 0.0001  173 ASP A N   
1398  C CA  . ASP A 173 ? 0.2533 0.3294 0.2855 0.0069  -0.0072 0.0041  173 ASP A CA  
1399  C C   . ASP A 173 ? 0.2701 0.3417 0.3034 0.0061  -0.0005 0.0080  173 ASP A C   
1400  O O   . ASP A 173 ? 0.2705 0.3418 0.3014 0.0119  0.0009  0.0105  173 ASP A O   
1401  C CB  . ASP A 173 ? 0.2887 0.3539 0.3064 0.0094  -0.0053 0.0062  173 ASP A CB  
1402  C CG  . ASP A 173 ? 0.3412 0.4089 0.3526 0.0136  -0.0122 0.0027  173 ASP A CG  
1403  O OD1 . ASP A 173 ? 0.3436 0.4227 0.3630 0.0151  -0.0197 -0.0028 173 ASP A OD1 
1404  O OD2 . ASP A 173 ? 0.3808 0.4392 0.3798 0.0159  -0.0097 0.0047  173 ASP A OD2 
1405  N N   . GLY A 174 ? 0.2485 0.3162 0.2844 0.0002  0.0034  0.0080  174 GLY A N   
1406  C CA  . GLY A 174 ? 0.2707 0.3348 0.3075 0.0003  0.0086  0.0099  174 GLY A CA  
1407  C C   . GLY A 174 ? 0.2443 0.3158 0.2891 0.0018  0.0092  0.0105  174 GLY A C   
1408  O O   . GLY A 174 ? 0.2617 0.3311 0.3056 0.0052  0.0122  0.0124  174 GLY A O   
1409  N N   . ILE A 175 ? 0.2343 0.3140 0.2887 -0.0011 0.0076  0.0084  175 ILE A N   
1410  C CA  . ILE A 175 ? 0.2380 0.3269 0.3037 0.0001  0.0089  0.0081  175 ILE A CA  
1411  C C   . ILE A 175 ? 0.2606 0.3553 0.3259 0.0074  0.0048  0.0080  175 ILE A C   
1412  O O   . ILE A 175 ? 0.2483 0.3437 0.3140 0.0115  0.0073  0.0101  175 ILE A O   
1413  C CB  . ILE A 175 ? 0.2539 0.3508 0.3339 -0.0053 0.0088  0.0042  175 ILE A CB  
1414  C CG1 . ILE A 175 ? 0.2406 0.3282 0.3178 -0.0102 0.0157  0.0063  175 ILE A CG1 
1415  C CG2 . ILE A 175 ? 0.2375 0.3474 0.3335 -0.0039 0.0091  0.0017  175 ILE A CG2 
1416  C CD1 . ILE A 175 ? 0.2549 0.3450 0.3450 -0.0165 0.0187  0.0032  175 ILE A CD1 
1417  N N   . ALA A 176 ? 0.2367 0.3337 0.2980 0.0107  -0.0015 0.0058  176 ALA A N   
1418  C CA  . ALA A 176 ? 0.2611 0.3618 0.3177 0.0207  -0.0056 0.0059  176 ALA A CA  
1419  C C   . ALA A 176 ? 0.2850 0.3721 0.3279 0.0253  0.0002  0.0122  176 ALA A C   
1420  O O   . ALA A 176 ? 0.3059 0.3938 0.3468 0.0327  0.0007  0.0140  176 ALA A O   
1421  C CB  . ALA A 176 ? 0.3024 0.4058 0.3527 0.0257  -0.0135 0.0023  176 ALA A CB  
1422  N N   . PHE A 177 ? 0.2574 0.3322 0.2929 0.0208  0.0052  0.0146  177 PHE A N   
1423  C CA  . PHE A 177 ? 0.2828 0.3442 0.3095 0.0236  0.0120  0.0187  177 PHE A CA  
1424  C C   . PHE A 177 ? 0.2788 0.3411 0.3121 0.0231  0.0158  0.0192  177 PHE A C   
1425  O O   . PHE A 177 ? 0.2783 0.3345 0.3073 0.0289  0.0194  0.0219  177 PHE A O   
1426  C CB  . PHE A 177 ? 0.2870 0.3386 0.3103 0.0179  0.0161  0.0184  177 PHE A CB  
1427  C CG  . PHE A 177 ? 0.2678 0.3073 0.2897 0.0178  0.0243  0.0197  177 PHE A CG  
1428  C CD1 . PHE A 177 ? 0.2979 0.3385 0.3278 0.0138  0.0262  0.0167  177 PHE A CD1 
1429  C CD2 . PHE A 177 ? 0.3086 0.3354 0.3213 0.0227  0.0306  0.0234  177 PHE A CD2 
1430  C CE1 . PHE A 177 ? 0.2772 0.3081 0.3093 0.0137  0.0329  0.0154  177 PHE A CE1 
1431  C CE2 . PHE A 177 ? 0.2789 0.2938 0.2945 0.0215  0.0400  0.0235  177 PHE A CE2 
1432  C CZ  . PHE A 177 ? 0.2582 0.2766 0.2852 0.0165  0.0401  0.0184  177 PHE A CZ  
1433  N N   . VAL A 178 ? 0.2359 0.3035 0.2776 0.0170  0.0160  0.0168  178 VAL A N   
1434  C CA  . VAL A 178 ? 0.2220 0.2886 0.2669 0.0178  0.0200  0.0170  178 VAL A CA  
1435  C C   . VAL A 178 ? 0.2779 0.3535 0.3281 0.0232  0.0188  0.0180  178 VAL A C   
1436  O O   . VAL A 178 ? 0.2875 0.3602 0.3373 0.0270  0.0222  0.0191  178 VAL A O   
1437  C CB  . VAL A 178 ? 0.2436 0.3110 0.2916 0.0129  0.0215  0.0148  178 VAL A CB  
1438  C CG1 . VAL A 178 ? 0.2413 0.3007 0.2843 0.0094  0.0217  0.0124  178 VAL A CG1 
1439  C CG2 . VAL A 178 ? 0.2555 0.3324 0.3111 0.0099  0.0204  0.0144  178 VAL A CG2 
1440  N N   . GLU A 179 ? 0.2248 0.3123 0.2819 0.0239  0.0137  0.0162  179 GLU A N   
1441  C CA  . GLU A 179 ? 0.2324 0.3311 0.2971 0.0300  0.0116  0.0152  179 GLU A CA  
1442  C C   . GLU A 179 ? 0.2728 0.3640 0.3256 0.0401  0.0111  0.0183  179 GLU A C   
1443  O O   . GLU A 179 ? 0.3023 0.3943 0.3559 0.0459  0.0132  0.0196  179 GLU A O   
1444  C CB  . GLU A 179 ? 0.2769 0.3911 0.3539 0.0293  0.0049  0.0099  179 GLU A CB  
1445  C CG  . GLU A 179 ? 0.2556 0.3767 0.3480 0.0198  0.0083  0.0070  179 GLU A CG  
1446  C CD  . GLU A 179 ? 0.3130 0.4502 0.4230 0.0181  0.0029  -0.0002 179 GLU A CD  
1447  O OE1 . GLU A 179 ? 0.3373 0.4751 0.4432 0.0189  -0.0041 -0.0034 179 GLU A OE1 
1448  O OE2 . GLU A 179 ? 0.2978 0.4473 0.4268 0.0163  0.0057  -0.0037 179 GLU A OE2 
1449  N N   . LYS A 180 ? 0.2660 0.3497 0.3069 0.0434  0.0090  0.0197  180 LYS A N   
1450  C CA  . LYS A 180 ? 0.2946 0.3671 0.3201 0.0545  0.0106  0.0239  180 LYS A CA  
1451  C C   . LYS A 180 ? 0.3409 0.3982 0.3622 0.0538  0.0199  0.0278  180 LYS A C   
1452  O O   . LYS A 180 ? 0.3129 0.3656 0.3294 0.0622  0.0224  0.0305  180 LYS A O   
1453  C CB  . LYS A 180 ? 0.2851 0.3486 0.2967 0.0572  0.0096  0.0256  180 LYS A CB  
1454  C CG  . LYS A 180 ? 0.4148 0.4652 0.4065 0.0717  0.0118  0.0308  180 LYS A CG  
1455  C CD  . LYS A 180 ? 0.4695 0.5188 0.4476 0.0789  0.0063  0.0302  180 LYS A CD  
1456  C CE  . LYS A 180 ? 0.5877 0.6479 0.5594 0.0948  -0.0039 0.0272  180 LYS A CE  
1457  N NZ  . LYS A 180 ? 0.7030 0.7733 0.6714 0.0989  -0.0146 0.0211  180 LYS A NZ  
1458  N N   . ALA A 181 ? 0.2549 0.3048 0.2787 0.0444  0.0247  0.0271  181 ALA A N   
1459  C CA  . ALA A 181 ? 0.2941 0.3295 0.3163 0.0433  0.0332  0.0282  181 ALA A CA  
1460  C C   . ALA A 181 ? 0.3408 0.3810 0.3703 0.0443  0.0341  0.0267  181 ALA A C   
1461  O O   . ALA A 181 ? 0.3413 0.3705 0.3678 0.0483  0.0399  0.0282  181 ALA A O   
1462  C CB  . ALA A 181 ? 0.3218 0.3518 0.3480 0.0338  0.0362  0.0249  181 ALA A CB  
1463  N N   . SER A 182 ? 0.2711 0.3263 0.3098 0.0412  0.0296  0.0241  182 SER A N   
1464  C CA  . SER A 182 ? 0.2319 0.2913 0.2763 0.0426  0.0314  0.0228  182 SER A CA  
1465  C C   . SER A 182 ? 0.2288 0.2981 0.2763 0.0506  0.0291  0.0242  182 SER A C   
1466  O O   . SER A 182 ? 0.2874 0.3570 0.3372 0.0542  0.0319  0.0241  182 SER A O   
1467  C CB  . SER A 182 ? 0.2811 0.3486 0.3324 0.0360  0.0307  0.0199  182 SER A CB  
1468  O OG  . SER A 182 ? 0.2964 0.3776 0.3553 0.0347  0.0269  0.0197  182 SER A OG  
1469  N N   . GLY A 183 ? 0.2792 0.3574 0.3272 0.0545  0.0234  0.0242  183 GLY A N   
1470  C CA  . GLY A 183 ? 0.2788 0.3705 0.3335 0.0624  0.0197  0.0230  183 GLY A CA  
1471  C C   . GLY A 183 ? 0.3099 0.4192 0.3826 0.0571  0.0189  0.0189  183 GLY A C   
1472  O O   . GLY A 183 ? 0.3011 0.4239 0.3839 0.0628  0.0168  0.0165  183 GLY A O   
1473  N N   . ARG A 184 ? 0.2735 0.3826 0.3508 0.0470  0.0215  0.0179  184 ARG A N   
1474  C CA  . ARG A 184 ? 0.2638 0.3853 0.3568 0.0418  0.0244  0.0154  184 ARG A CA  
1475  C C   . ARG A 184 ? 0.2789 0.4108 0.3831 0.0359  0.0203  0.0114  184 ARG A C   
1476  O O   . ARG A 184 ? 0.2712 0.3983 0.3678 0.0347  0.0155  0.0111  184 ARG A O   
1477  C CB  . ARG A 184 ? 0.2263 0.3381 0.3143 0.0370  0.0317  0.0174  184 ARG A CB  
1478  C CG  . ARG A 184 ? 0.3078 0.4109 0.3874 0.0430  0.0356  0.0192  184 ARG A CG  
1479  C CD  . ARG A 184 ? 0.3241 0.4210 0.3994 0.0409  0.0417  0.0194  184 ARG A CD  
1480  N NE  . ARG A 184 ? 0.3193 0.4073 0.3861 0.0467  0.0442  0.0191  184 ARG A NE  
1481  C CZ  . ARG A 184 ? 0.2962 0.3785 0.3563 0.0480  0.0483  0.0181  184 ARG A CZ  
1482  N NH1 . ARG A 184 ? 0.2822 0.3651 0.3411 0.0450  0.0518  0.0190  184 ARG A NH1 
1483  N NH2 . ARG A 184 ? 0.2822 0.3572 0.3355 0.0538  0.0494  0.0160  184 ARG A NH2 
1484  N N   . LYS A 185 ? 0.2916 0.4376 0.4155 0.0325  0.0231  0.0077  185 LYS A N   
1485  C CA  . LYS A 185 ? 0.2742 0.4296 0.4133 0.0251  0.0215  0.0026  185 LYS A CA  
1486  C C   . LYS A 185 ? 0.3000 0.4438 0.4349 0.0166  0.0300  0.0061  185 LYS A C   
1487  O O   . LYS A 185 ? 0.3166 0.4559 0.4511 0.0160  0.0393  0.0093  185 LYS A O   
1488  C CB  . LYS A 185 ? 0.2774 0.4535 0.4440 0.0249  0.0224  -0.0044 185 LYS A CB  
1489  C CG  . LYS A 185 ? 0.3336 0.5208 0.5195 0.0175  0.0189  -0.0124 185 LYS A CG  
1490  C CD  . LYS A 185 ? 0.3779 0.5886 0.5964 0.0173  0.0189  -0.0224 185 LYS A CD  
1491  C CE  . LYS A 185 ? 0.4370 0.6633 0.6739 0.0155  0.0083  -0.0344 185 LYS A CE  
1492  N NZ  . LYS A 185 ? 0.4295 0.6442 0.6620 0.0057  0.0106  -0.0333 185 LYS A NZ  
1493  N N   . PHE A 186 ? 0.2677 0.4065 0.3984 0.0115  0.0268  0.0051  186 PHE A N   
1494  C CA  . PHE A 186 ? 0.2685 0.3952 0.3928 0.0050  0.0337  0.0081  186 PHE A CA  
1495  C C   . PHE A 186 ? 0.2820 0.4148 0.4258 -0.0010 0.0429  0.0061  186 PHE A C   
1496  O O   . PHE A 186 ? 0.3071 0.4549 0.4731 -0.0040 0.0402  -0.0008 186 PHE A O   
1497  C CB  . PHE A 186 ? 0.2643 0.3859 0.3807 0.0020  0.0268  0.0068  186 PHE A CB  
1498  C CG  . PHE A 186 ? 0.2584 0.3675 0.3665 -0.0032 0.0319  0.0091  186 PHE A CG  
1499  C CD1 . PHE A 186 ? 0.2644 0.3758 0.3855 -0.0101 0.0356  0.0064  186 PHE A CD1 
1500  C CD2 . PHE A 186 ? 0.2442 0.3397 0.3326 -0.0010 0.0318  0.0127  186 PHE A CD2 
1501  C CE1 . PHE A 186 ? 0.2423 0.3401 0.3529 -0.0135 0.0398  0.0089  186 PHE A CE1 
1502  C CE2 . PHE A 186 ? 0.2623 0.3471 0.3416 -0.0037 0.0346  0.0140  186 PHE A CE2 
1503  C CZ  . PHE A 186 ? 0.2642 0.3490 0.3524 -0.0095 0.0387  0.0129  186 PHE A CZ  
1504  N N   . ASP A 187 ? 0.2242 0.3451 0.3603 -0.0020 0.0542  0.0114  187 ASP A N   
1505  C CA  . ASP A 187 ? 0.2128 0.3351 0.3654 -0.0068 0.0674  0.0114  187 ASP A CA  
1506  C C   . ASP A 187 ? 0.2449 0.3531 0.3912 -0.0123 0.0739  0.0137  187 ASP A C   
1507  O O   . ASP A 187 ? 0.2279 0.3196 0.3498 -0.0085 0.0757  0.0192  187 ASP A O   
1508  C CB  . ASP A 187 ? 0.2529 0.3700 0.3996 -0.0014 0.0786  0.0167  187 ASP A CB  
1509  C CG  . ASP A 187 ? 0.3260 0.4452 0.4925 -0.0061 0.0945  0.0168  187 ASP A CG  
1510  O OD1 . ASP A 187 ? 0.3148 0.4519 0.5104 -0.0098 0.0959  0.0105  187 ASP A OD1 
1511  O OD2 . ASP A 187 ? 0.3400 0.4419 0.4934 -0.0062 0.1064  0.0228  187 ASP A OD2 
1512  N N   . ASP A 188 ? 0.3391 0.3603 0.3862 0.0087  0.0058  -0.0191 188 ASP A N   
1513  C CA  . ASP A 188 ? 0.2851 0.3003 0.3282 0.0042  0.0046  -0.0164 188 ASP A CA  
1514  C C   . ASP A 188 ? 0.3111 0.3342 0.3572 -0.0014 0.0092  -0.0132 188 ASP A C   
1515  O O   . ASP A 188 ? 0.3082 0.3241 0.3480 -0.0034 0.0101  -0.0113 188 ASP A O   
1516  C CB  . ASP A 188 ? 0.3053 0.3174 0.3529 0.0018  -0.0038 -0.0163 188 ASP A CB  
1517  C CG  . ASP A 188 ? 0.3680 0.3716 0.4082 0.0096  -0.0094 -0.0203 188 ASP A CG  
1518  O OD1 . ASP A 188 ? 0.3855 0.3870 0.4166 0.0152  -0.0060 -0.0201 188 ASP A OD1 
1519  O OD2 . ASP A 188 ? 0.4339 0.4346 0.4779 0.0101  -0.0181 -0.0225 188 ASP A OD2 
1520  N N   . GLU A 189 ? 0.2913 0.3322 0.3466 -0.0028 0.0121  -0.0121 189 GLU A N   
1521  C CA  . GLU A 189 ? 0.3197 0.3742 0.3772 -0.0069 0.0169  -0.0076 189 GLU A CA  
1522  C C   . GLU A 189 ? 0.3429 0.3917 0.3905 -0.0024 0.0214  -0.0114 189 GLU A C   
1523  O O   . GLU A 189 ? 0.3012 0.3483 0.3450 -0.0064 0.0233  -0.0077 189 GLU A O   
1524  C CB  . GLU A 189 ? 0.3555 0.4385 0.4242 -0.0064 0.0199  -0.0049 189 GLU A CB  
1525  C CG  . GLU A 189 ? 0.4000 0.5040 0.4712 -0.0104 0.0252  0.0027  189 GLU A CG  
1526  C CD  . GLU A 189 ? 0.5101 0.6520 0.5904 -0.0063 0.0301  0.0059  189 GLU A CD  
1527  O OE1 . GLU A 189 ? 0.5791 0.7463 0.6649 -0.0112 0.0340  0.0169  189 GLU A OE1 
1528  O OE2 . GLU A 189 ? 0.4863 0.6357 0.5689 0.0020  0.0298  -0.0013 189 GLU A OE2 
1529  N N   . LEU A 190 ? 0.2685 0.3139 0.3132 0.0055  0.0212  -0.0183 190 LEU A N   
1530  C CA  . LEU A 190 ? 0.3089 0.3456 0.3466 0.0087  0.0218  -0.0212 190 LEU A CA  
1531  C C   . LEU A 190 ? 0.2753 0.2957 0.3066 0.0045  0.0212  -0.0168 190 LEU A C   
1532  O O   . LEU A 190 ? 0.2870 0.3037 0.3135 0.0033  0.0229  -0.0158 190 LEU A O   
1533  C CB  . LEU A 190 ? 0.2860 0.3161 0.3245 0.0168  0.0167  -0.0279 190 LEU A CB  
1534  C CG  . LEU A 190 ? 0.3504 0.3966 0.3928 0.0258  0.0156  -0.0359 190 LEU A CG  
1535  C CD1 . LEU A 190 ? 0.3257 0.3585 0.3695 0.0340  0.0062  -0.0431 190 LEU A CD1 
1536  C CD2 . LEU A 190 ? 0.3558 0.4185 0.3945 0.0299  0.0196  -0.0388 190 LEU A CD2 
1537  N N   . PHE A 191 ? 0.2441 0.2564 0.2744 0.0040  0.0183  -0.0148 191 PHE A N   
1538  C CA  . PHE A 191 ? 0.2767 0.2794 0.2998 0.0034  0.0177  -0.0112 191 PHE A CA  
1539  C C   . PHE A 191 ? 0.2716 0.2731 0.2918 -0.0011 0.0184  -0.0094 191 PHE A C   
1540  O O   . PHE A 191 ? 0.3010 0.2980 0.3155 -0.0015 0.0199  -0.0076 191 PHE A O   
1541  C CB  . PHE A 191 ? 0.2601 0.2599 0.2812 0.0069  0.0139  -0.0106 191 PHE A CB  
1542  C CG  . PHE A 191 ? 0.2866 0.2828 0.2989 0.0096  0.0130  -0.0082 191 PHE A CG  
1543  C CD1 . PHE A 191 ? 0.3027 0.2996 0.3114 0.0104  0.0155  -0.0033 191 PHE A CD1 
1544  C CD2 . PHE A 191 ? 0.3062 0.2992 0.3141 0.0126  0.0078  -0.0111 191 PHE A CD2 
1545  C CE1 . PHE A 191 ? 0.2863 0.2855 0.2861 0.0153  0.0151  -0.0009 191 PHE A CE1 
1546  C CE2 . PHE A 191 ? 0.3163 0.3080 0.3137 0.0194  0.0054  -0.0115 191 PHE A CE2 
1547  C CZ  . PHE A 191 ? 0.3113 0.3085 0.3043 0.0212  0.0103  -0.0062 191 PHE A CZ  
1548  N N   . ILE A 192 ? 0.3271 0.3322 0.3525 -0.0049 0.0159  -0.0086 192 ILE A N   
1549  C CA  . ILE A 192 ? 0.3144 0.3161 0.3394 -0.0104 0.0134  -0.0049 192 ILE A CA  
1550  C C   . ILE A 192 ? 0.3090 0.3185 0.3337 -0.0137 0.0193  -0.0020 192 ILE A C   
1551  O O   . ILE A 192 ? 0.3173 0.3201 0.3368 -0.0155 0.0189  -0.0001 192 ILE A O   
1552  C CB  . ILE A 192 ? 0.2926 0.2973 0.3279 -0.0158 0.0065  -0.0018 192 ILE A CB  
1553  C CG1 . ILE A 192 ? 0.3068 0.3001 0.3393 -0.0105 -0.0017 -0.0068 192 ILE A CG1 
1554  C CG2 . ILE A 192 ? 0.3170 0.3182 0.3558 -0.0235 0.0012  0.0046  192 ILE A CG2 
1555  C CD1 . ILE A 192 ? 0.3278 0.3226 0.3726 -0.0159 -0.0108 -0.0041 192 ILE A CD1 
1556  N N   A LYS A 193 ? 0.2752 0.2997 0.3041 -0.0124 0.0241  -0.0029 193 LYS A N   
1557  N N   B LYS A 193 ? 0.2756 0.3002 0.3046 -0.0124 0.0241  -0.0029 193 LYS A N   
1558  C CA  A LYS A 193 ? 0.2950 0.3287 0.3212 -0.0121 0.0290  -0.0022 193 LYS A CA  
1559  C CA  B LYS A 193 ? 0.2951 0.3288 0.3212 -0.0121 0.0290  -0.0022 193 LYS A CA  
1560  C C   A LYS A 193 ? 0.2950 0.3147 0.3124 -0.0088 0.0294  -0.0055 193 LYS A C   
1561  C C   B LYS A 193 ? 0.2951 0.3149 0.3125 -0.0088 0.0294  -0.0056 193 LYS A C   
1562  O O   A LYS A 193 ? 0.2880 0.3071 0.3011 -0.0108 0.0311  -0.0034 193 LYS A O   
1563  O O   B LYS A 193 ? 0.2879 0.3070 0.3010 -0.0107 0.0311  -0.0035 193 LYS A O   
1564  C CB  A LYS A 193 ? 0.3130 0.3662 0.3428 -0.0061 0.0322  -0.0062 193 LYS A CB  
1565  C CB  B LYS A 193 ? 0.3129 0.3664 0.3427 -0.0062 0.0323  -0.0060 193 LYS A CB  
1566  C CG  A LYS A 193 ? 0.3412 0.4075 0.3663 -0.0022 0.0362  -0.0076 193 LYS A CG  
1567  C CG  B LYS A 193 ? 0.3182 0.3941 0.3586 -0.0099 0.0331  0.0004  193 LYS A CG  
1568  C CD  A LYS A 193 ? 0.3075 0.4029 0.3367 0.0051  0.0391  -0.0099 193 LYS A CD  
1569  C CD  B LYS A 193 ? 0.3255 0.4312 0.3669 -0.0038 0.0386  0.0002  193 LYS A CD  
1570  C CE  A LYS A 193 ? 0.3691 0.4593 0.3978 0.0159  0.0352  -0.0218 193 LYS A CE  
1571  C CE  B LYS A 193 ? 0.3887 0.5201 0.4405 -0.0013 0.0396  0.0021  193 LYS A CE  
1572  N NZ  A LYS A 193 ? 0.3549 0.4260 0.3762 0.0226  0.0302  -0.0309 193 LYS A NZ  
1573  N NZ  B LYS A 193 ? 0.3988 0.5345 0.4637 -0.0141 0.0362  0.0153  193 LYS A NZ  
1574  N N   . ALA A 194 ? 0.2879 0.2984 0.3041 -0.0044 0.0272  -0.0090 194 ALA A N   
1575  C CA  . ALA A 194 ? 0.3026 0.3033 0.3143 -0.0029 0.0264  -0.0087 194 ALA A CA  
1576  C C   . ALA A 194 ? 0.2760 0.2700 0.2822 -0.0053 0.0264  -0.0044 194 ALA A C   
1577  O O   . ALA A 194 ? 0.3030 0.2940 0.3055 -0.0059 0.0273  -0.0028 194 ALA A O   
1578  C CB  . ALA A 194 ? 0.2958 0.2913 0.3109 0.0007  0.0224  -0.0092 194 ALA A CB  
1579  N N   . VAL A 195 ? 0.2746 0.2661 0.2797 -0.0051 0.0239  -0.0038 195 VAL A N   
1580  C CA  . VAL A 195 ? 0.2857 0.2709 0.2844 -0.0042 0.0215  -0.0025 195 VAL A CA  
1581  C C   . VAL A 195 ? 0.2746 0.2583 0.2727 -0.0095 0.0217  -0.0007 195 VAL A C   
1582  O O   . VAL A 195 ? 0.2822 0.2622 0.2749 -0.0088 0.0221  0.0004  195 VAL A O   
1583  C CB  . VAL A 195 ? 0.2756 0.2568 0.2729 -0.0006 0.0152  -0.0050 195 VAL A CB  
1584  C CG1 . VAL A 195 ? 0.2814 0.2542 0.2716 0.0026  0.0090  -0.0067 195 VAL A CG1 
1585  C CG2 . VAL A 195 ? 0.2413 0.2270 0.2364 0.0063  0.0157  -0.0051 195 VAL A CG2 
1586  N N   . LYS A 196 ? 0.2795 0.2690 0.2841 -0.0149 0.0214  0.0014  196 LYS A N   
1587  C CA  . LYS A 196 ? 0.2937 0.2854 0.2992 -0.0209 0.0211  0.0065  196 LYS A CA  
1588  C C   . LYS A 196 ? 0.2890 0.2858 0.2899 -0.0198 0.0272  0.0061  196 LYS A C   
1589  O O   . LYS A 196 ? 0.3161 0.3089 0.3129 -0.0217 0.0268  0.0086  196 LYS A O   
1590  C CB  . LYS A 196 ? 0.2715 0.2765 0.2876 -0.0275 0.0202  0.0126  196 LYS A CB  
1591  C CG  . LYS A 196 ? 0.3279 0.3254 0.3510 -0.0300 0.0107  0.0137  196 LYS A CG  
1592  C CD  . LYS A 196 ? 0.3705 0.3817 0.4075 -0.0403 0.0072  0.0252  196 LYS A CD  
1593  C CE  . LYS A 196 ? 0.4043 0.4415 0.4467 -0.0395 0.0163  0.0271  196 LYS A CE  
1594  N NZ  . LYS A 196 ? 0.4347 0.4921 0.4931 -0.0502 0.0128  0.0423  196 LYS A NZ  
1595  N N   . ASN A 197 ? 0.3004 0.3042 0.3020 -0.0156 0.0310  0.0019  197 ASN A N   
1596  C CA  . ASN A 197 ? 0.2720 0.2778 0.2693 -0.0131 0.0335  -0.0003 197 ASN A CA  
1597  C C   . ASN A 197 ? 0.2857 0.2791 0.2786 -0.0120 0.0319  -0.0002 197 ASN A C   
1598  O O   . ASN A 197 ? 0.2881 0.2804 0.2772 -0.0124 0.0325  0.0003  197 ASN A O   
1599  C CB  . ASN A 197 ? 0.2945 0.3073 0.2941 -0.0068 0.0335  -0.0069 197 ASN A CB  
1600  C CG  . ASN A 197 ? 0.3030 0.3373 0.3052 -0.0052 0.0367  -0.0069 197 ASN A CG  
1601  O OD1 . ASN A 197 ? 0.3422 0.3879 0.3442 -0.0095 0.0395  -0.0003 197 ASN A OD1 
1602  N ND2 . ASN A 197 ? 0.3347 0.3773 0.3401 0.0015  0.0358  -0.0131 197 ASN A ND2 
1603  N N   . GLU A 198 ? 0.2761 0.2636 0.2696 -0.0102 0.0299  0.0004  198 GLU A N   
1604  C CA  . GLU A 198 ? 0.2504 0.2336 0.2409 -0.0086 0.0291  0.0032  198 GLU A CA  
1605  C C   . GLU A 198 ? 0.2939 0.2734 0.2785 -0.0092 0.0284  0.0045  198 GLU A C   
1606  O O   . GLU A 198 ? 0.2876 0.2660 0.2691 -0.0089 0.0287  0.0063  198 GLU A O   
1607  C CB  . GLU A 198 ? 0.2762 0.2612 0.2686 -0.0049 0.0276  0.0057  198 GLU A CB  
1608  C CG  . GLU A 198 ? 0.2786 0.2675 0.2690 -0.0025 0.0276  0.0114  198 GLU A CG  
1609  C CD  . GLU A 198 ? 0.3036 0.3014 0.2978 0.0006  0.0267  0.0178  198 GLU A CD  
1610  O OE1 . GLU A 198 ? 0.2990 0.2955 0.3000 -0.0011 0.0248  0.0183  198 GLU A OE1 
1611  O OE2 . GLU A 198 ? 0.3722 0.3807 0.3627 0.0058  0.0274  0.0227  198 GLU A OE2 
1612  N N   . MET A 199 ? 0.2847 0.2611 0.2686 -0.0101 0.0253  0.0037  199 MET A N   
1613  C CA  . MET A 199 ? 0.3145 0.2837 0.2941 -0.0105 0.0208  0.0045  199 MET A CA  
1614  C C   . MET A 199 ? 0.3058 0.2764 0.2853 -0.0161 0.0230  0.0078  199 MET A C   
1615  O O   . MET A 199 ? 0.3237 0.2902 0.2983 -0.0151 0.0221  0.0085  199 MET A O   
1616  C CB  . MET A 199 ? 0.3125 0.2751 0.2949 -0.0120 0.0131  0.0038  199 MET A CB  
1617  C CG  . MET A 199 ? 0.3613 0.3201 0.3391 -0.0025 0.0080  -0.0016 199 MET A CG  
1618  S SD  . MET A 199 ? 0.3395 0.2902 0.3237 -0.0047 -0.0029 -0.0034 199 MET A SD  
1619  C CE  . MET A 199 ? 0.3243 0.2731 0.2981 0.0114  -0.0089 -0.0124 199 MET A CE  
1620  N N   . ARG A 200 ? 0.2998 0.2797 0.2840 -0.0205 0.0264  0.0097  200 ARG A N   
1621  C CA  . ARG A 200 ? 0.3092 0.2967 0.2920 -0.0237 0.0294  0.0130  200 ARG A CA  
1622  C C   . ARG A 200 ? 0.3197 0.3050 0.2972 -0.0199 0.0317  0.0097  200 ARG A C   
1623  O O   . ARG A 200 ? 0.3153 0.2978 0.2887 -0.0212 0.0309  0.0120  200 ARG A O   
1624  C CB  . ARG A 200 ? 0.3169 0.3219 0.3039 -0.0245 0.0336  0.0141  200 ARG A CB  
1625  C CG  . ARG A 200 ? 0.3243 0.3383 0.3196 -0.0308 0.0314  0.0217  200 ARG A CG  
1626  C CD  . ARG A 200 ? 0.3753 0.4145 0.3743 -0.0285 0.0372  0.0223  200 ARG A CD  
1627  N NE  . ARG A 200 ? 0.3346 0.3889 0.3274 -0.0246 0.0417  0.0222  200 ARG A NE  
1628  C CZ  . ARG A 200 ? 0.3694 0.4420 0.3594 -0.0157 0.0456  0.0160  200 ARG A CZ  
1629  N NH1 . ARG A 200 ? 0.3604 0.4374 0.3539 -0.0102 0.0458  0.0094  200 ARG A NH1 
1630  N NH2 . ARG A 200 ? 0.3451 0.4331 0.3280 -0.0106 0.0483  0.0156  200 ARG A NH2 
1631  N N   . SER A 201 ? 0.3233 0.3089 0.3026 -0.0158 0.0325  0.0053  201 SER A N   
1632  C CA  . SER A 201 ? 0.3038 0.2874 0.2815 -0.0136 0.0317  0.0033  201 SER A CA  
1633  C C   . SER A 201 ? 0.3293 0.3067 0.3050 -0.0137 0.0304  0.0067  201 SER A C   
1634  O O   . SER A 201 ? 0.3123 0.2884 0.2854 -0.0140 0.0297  0.0072  201 SER A O   
1635  C CB  . SER A 201 ? 0.2848 0.2674 0.2679 -0.0102 0.0289  -0.0006 201 SER A CB  
1636  O OG  . SER A 201 ? 0.3201 0.2995 0.3077 -0.0105 0.0276  0.0031  201 SER A OG  
1637  N N   . THR A 202 ? 0.2820 0.2580 0.2582 -0.0119 0.0297  0.0087  202 THR A N   
1638  C CA  . THR A 202 ? 0.2689 0.2456 0.2429 -0.0089 0.0287  0.0117  202 THR A CA  
1639  C C   . THR A 202 ? 0.2785 0.2499 0.2457 -0.0085 0.0269  0.0111  202 THR A C   
1640  O O   . THR A 202 ? 0.2875 0.2597 0.2524 -0.0069 0.0263  0.0127  202 THR A O   
1641  C CB  . THR A 202 ? 0.3144 0.2969 0.2891 -0.0037 0.0283  0.0134  202 THR A CB  
1642  O OG1 . THR A 202 ? 0.2950 0.2729 0.2665 -0.0018 0.0262  0.0092  202 THR A OG1 
1643  C CG2 . THR A 202 ? 0.2642 0.2522 0.2477 -0.0052 0.0285  0.0172  202 THR A CG2 
1644  N N   . SER A 203 ? 0.2957 0.2616 0.2615 -0.0107 0.0245  0.0099  203 SER A N   
1645  C CA  . SER A 203 ? 0.2933 0.2515 0.2551 -0.0122 0.0198  0.0110  203 SER A CA  
1646  C C   . SER A 203 ? 0.2828 0.2437 0.2437 -0.0171 0.0226  0.0140  203 SER A C   
1647  O O   . SER A 203 ? 0.3190 0.2754 0.2759 -0.0168 0.0199  0.0153  203 SER A O   
1648  C CB  . SER A 203 ? 0.3132 0.2651 0.2780 -0.0159 0.0138  0.0121  203 SER A CB  
1649  O OG  . SER A 203 ? 0.3184 0.2608 0.2818 -0.0187 0.0063  0.0153  203 SER A OG  
1650  N N   . ARG A 204 ? 0.2790 0.2484 0.2427 -0.0201 0.0270  0.0143  204 ARG A N   
1651  C CA  . ARG A 204 ? 0.2842 0.2597 0.2450 -0.0220 0.0291  0.0160  204 ARG A CA  
1652  C C   . ARG A 204 ? 0.3201 0.2931 0.2785 -0.0186 0.0290  0.0131  204 ARG A C   
1653  O O   . ARG A 204 ? 0.3127 0.2856 0.2668 -0.0192 0.0283  0.0146  204 ARG A O   
1654  C CB  . ARG A 204 ? 0.3022 0.2913 0.2648 -0.0219 0.0328  0.0150  204 ARG A CB  
1655  C CG  . ARG A 204 ? 0.3252 0.3264 0.2829 -0.0218 0.0347  0.0175  204 ARG A CG  
1656  C CD  . ARG A 204 ? 0.3679 0.3690 0.3258 -0.0287 0.0325  0.0277  204 ARG A CD  
1657  N NE  . ARG A 204 ? 0.4356 0.4544 0.3988 -0.0332 0.0343  0.0362  204 ARG A NE  
1658  C CZ  . ARG A 204 ? 0.4711 0.4912 0.4399 -0.0419 0.0298  0.0489  204 ARG A CZ  
1659  N NH1 . ARG A 204 ? 0.4272 0.4297 0.3949 -0.0454 0.0227  0.0522  204 ARG A NH1 
1660  N NH2 . ARG A 204 ? 0.5331 0.5731 0.5102 -0.0472 0.0309  0.0593  204 ARG A NH2 
1661  N N   . TRP A 205 ? 0.2770 0.2492 0.2398 -0.0158 0.0287  0.0106  205 TRP A N   
1662  C CA  . TRP A 205 ? 0.2698 0.2407 0.2343 -0.0144 0.0264  0.0113  205 TRP A CA  
1663  C C   . TRP A 205 ? 0.3188 0.2876 0.2793 -0.0134 0.0256  0.0143  205 TRP A C   
1664  O O   . TRP A 205 ? 0.2919 0.2598 0.2503 -0.0136 0.0241  0.0150  205 TRP A O   
1665  C CB  . TRP A 205 ? 0.2776 0.2505 0.2511 -0.0136 0.0245  0.0131  205 TRP A CB  
1666  C CG  . TRP A 205 ? 0.3105 0.2846 0.2892 -0.0143 0.0206  0.0173  205 TRP A CG  
1667  C CD1 . TRP A 205 ? 0.2822 0.2643 0.2658 -0.0135 0.0205  0.0248  205 TRP A CD1 
1668  C CD2 . TRP A 205 ? 0.2990 0.2687 0.2781 -0.0150 0.0158  0.0146  205 TRP A CD2 
1669  N NE1 . TRP A 205 ? 0.2879 0.2715 0.2773 -0.0155 0.0161  0.0288  205 TRP A NE1 
1670  C CE2 . TRP A 205 ? 0.3037 0.2771 0.2907 -0.0166 0.0120  0.0219  205 TRP A CE2 
1671  C CE3 . TRP A 205 ? 0.3026 0.2686 0.2763 -0.0130 0.0135  0.0068  205 TRP A CE3 
1672  C CZ2 . TRP A 205 ? 0.3224 0.2913 0.3129 -0.0178 0.0049  0.0212  205 TRP A CZ2 
1673  C CZ3 . TRP A 205 ? 0.3054 0.2673 0.2798 -0.0119 0.0067  0.0043  205 TRP A CZ3 
1674  C CH2 . TRP A 205 ? 0.2870 0.2481 0.2706 -0.0151 0.0015  0.0113  205 TRP A CH2 
1675  N N   . ALA A 206 ? 0.2868 0.2541 0.2454 -0.0109 0.0250  0.0148  206 ALA A N   
1676  C CA  . ALA A 206 ? 0.3116 0.2759 0.2650 -0.0070 0.0218  0.0152  206 ALA A CA  
1677  C C   . ALA A 206 ? 0.3157 0.2726 0.2644 -0.0109 0.0194  0.0161  206 ALA A C   
1678  O O   . ALA A 206 ? 0.3202 0.2755 0.2657 -0.0091 0.0173  0.0168  206 ALA A O   
1679  C CB  . ALA A 206 ? 0.2789 0.2411 0.2296 -0.0007 0.0184  0.0126  206 ALA A CB  
1680  N N   . ASP A 207 ? 0.3087 0.2635 0.2576 -0.0162 0.0193  0.0177  207 ASP A N   
1681  C CA  . ASP A 207 ? 0.3363 0.2892 0.2824 -0.0211 0.0171  0.0225  207 ASP A CA  
1682  C C   . ASP A 207 ? 0.3174 0.2764 0.2602 -0.0208 0.0203  0.0221  207 ASP A C   
1683  O O   . ASP A 207 ? 0.3522 0.3080 0.2910 -0.0214 0.0175  0.0248  207 ASP A O   
1684  C CB  . ASP A 207 ? 0.3589 0.3184 0.3085 -0.0275 0.0183  0.0277  207 ASP A CB  
1685  C CG  . ASP A 207 ? 0.3874 0.3388 0.3418 -0.0300 0.0118  0.0301  207 ASP A CG  
1686  O OD1 . ASP A 207 ? 0.3954 0.3327 0.3484 -0.0261 0.0036  0.0271  207 ASP A OD1 
1687  O OD2 . ASP A 207 ? 0.3715 0.3322 0.3315 -0.0349 0.0139  0.0345  207 ASP A OD2 
1688  N N   . ILE A 208 ? 0.3116 0.2777 0.2564 -0.0192 0.0241  0.0182  208 ILE A N   
1689  C CA  . ILE A 208 ? 0.3087 0.2782 0.2509 -0.0172 0.0238  0.0156  208 ILE A CA  
1690  C C   . ILE A 208 ? 0.3157 0.2798 0.2586 -0.0155 0.0208  0.0160  208 ILE A C   
1691  O O   . ILE A 208 ? 0.3211 0.2846 0.2594 -0.0153 0.0190  0.0166  208 ILE A O   
1692  C CB  . ILE A 208 ? 0.3343 0.3077 0.2804 -0.0142 0.0239  0.0096  208 ILE A CB  
1693  C CG1 . ILE A 208 ? 0.3337 0.3178 0.2775 -0.0134 0.0272  0.0083  208 ILE A CG1 
1694  C CG2 . ILE A 208 ? 0.3317 0.3033 0.2774 -0.0111 0.0190  0.0053  208 ILE A CG2 
1695  C CD1 . ILE A 208 ? 0.3248 0.3099 0.2734 -0.0090 0.0255  0.0010  208 ILE A CD1 
1696  N N   . CYS A 209 ? 0.3294 0.2930 0.2780 -0.0137 0.0204  0.0166  209 CYS A N   
1697  C CA  . CYS A 209 ? 0.2943 0.2598 0.2451 -0.0111 0.0182  0.0189  209 CYS A CA  
1698  C C   . CYS A 209 ? 0.3191 0.2793 0.2624 -0.0093 0.0159  0.0196  209 CYS A C   
1699  O O   . CYS A 209 ? 0.3099 0.2712 0.2525 -0.0079 0.0137  0.0206  209 CYS A O   
1700  C CB  . CYS A 209 ? 0.2812 0.2546 0.2384 -0.0078 0.0191  0.0217  209 CYS A CB  
1701  S SG  . CYS A 209 ? 0.3170 0.2957 0.2870 -0.0115 0.0183  0.0244  209 CYS A SG  
1702  N N   . ALA A 210 ? 0.3408 0.2944 0.2801 -0.0097 0.0144  0.0194  210 ALA A N   
1703  C CA  . ALA A 210 ? 0.3543 0.2991 0.2882 -0.0078 0.0084  0.0202  210 ALA A CA  
1704  C C   . ALA A 210 ? 0.3536 0.2964 0.2835 -0.0127 0.0075  0.0239  210 ALA A C   
1705  O O   . ALA A 210 ? 0.3759 0.3119 0.3020 -0.0111 0.0019  0.0252  210 ALA A O   
1706  C CB  . ALA A 210 ? 0.3623 0.2973 0.2957 -0.0079 0.0029  0.0199  210 ALA A CB  
1707  N N   . LEU A 211 ? 0.3580 0.3081 0.2878 -0.0169 0.0121  0.0250  211 LEU A N   
1708  C CA  . LEU A 211 ? 0.3153 0.2690 0.2396 -0.0189 0.0118  0.0280  211 LEU A CA  
1709  C C   . LEU A 211 ? 0.3566 0.3098 0.2798 -0.0152 0.0101  0.0248  211 LEU A C   
1710  O O   . LEU A 211 ? 0.3677 0.3214 0.2853 -0.0155 0.0081  0.0268  211 LEU A O   
1711  C CB  . LEU A 211 ? 0.3504 0.3167 0.2732 -0.0200 0.0165  0.0276  211 LEU A CB  
1712  C CG  . LEU A 211 ? 0.3721 0.3437 0.2978 -0.0247 0.0184  0.0335  211 LEU A CG  
1713  C CD1 . LEU A 211 ? 0.3956 0.3859 0.3194 -0.0227 0.0238  0.0322  211 LEU A CD1 
1714  C CD2 . LEU A 211 ? 0.4219 0.3908 0.3471 -0.0310 0.0133  0.0451  211 LEU A CD2 
1715  N N   . ASN A 212 ? 0.3384 0.2928 0.2680 -0.0122 0.0103  0.0215  212 ASN A N   
1716  C CA  . ASN A 212 ? 0.3413 0.2980 0.2737 -0.0100 0.0076  0.0207  212 ASN A CA  
1717  C C   . ASN A 212 ? 0.3338 0.2879 0.2638 -0.0067 0.0044  0.0227  212 ASN A C   
1718  O O   . ASN A 212 ? 0.3628 0.3210 0.2960 -0.0048 0.0020  0.0232  212 ASN A O   
1719  C CB  . ASN A 212 ? 0.2944 0.2572 0.2382 -0.0098 0.0075  0.0207  212 ASN A CB  
1720  C CG  . ASN A 212 ? 0.3171 0.2797 0.2650 -0.0109 0.0026  0.0185  212 ASN A CG  
1721  O OD1 . ASN A 212 ? 0.3705 0.3301 0.3099 -0.0100 0.0011  0.0143  212 ASN A OD1 
1722  N ND2 . ASN A 212 ? 0.3032 0.2703 0.2642 -0.0123 -0.0015 0.0221  212 ASN A ND2 
1723  N N   . LYS A 213 ? 0.3439 0.2907 0.2692 -0.0054 0.0022  0.0235  213 LYS A N   
1724  C CA  . LYS A 213 ? 0.3649 0.3075 0.2872 0.0003  -0.0034 0.0231  213 LYS A CA  
1725  C C   . LYS A 213 ? 0.4015 0.3389 0.3182 -0.0018 -0.0072 0.0255  213 LYS A C   
1726  O O   . LYS A 213 ? 0.3766 0.3120 0.2915 0.0036  -0.0121 0.0247  213 LYS A O   
1727  C CB  . LYS A 213 ? 0.3571 0.2892 0.2767 0.0036  -0.0090 0.0216  213 LYS A CB  
1728  C CG  . LYS A 213 ? 0.3647 0.3027 0.2878 0.0083  -0.0064 0.0181  213 LYS A CG  
1729  C CD  . LYS A 213 ? 0.3527 0.2758 0.2721 0.0126  -0.0162 0.0149  213 LYS A CD  
1730  C CE  . LYS A 213 ? 0.4207 0.3484 0.3422 0.0172  -0.0144 0.0109  213 LYS A CE  
1731  N NZ  . LYS A 213 ? 0.4156 0.3273 0.3338 0.0235  -0.0270 0.0056  213 LYS A NZ  
1732  N N   . VAL A 214 ? 0.4383 0.3330 0.2992 0.0516  -0.0009 -0.0016 214 VAL A N   
1733  C CA  . VAL A 214 ? 0.4652 0.3545 0.3250 0.0454  -0.0048 0.0008  214 VAL A CA  
1734  C C   . VAL A 214 ? 0.4352 0.3438 0.3056 0.0434  0.0012  0.0060  214 VAL A C   
1735  O O   . VAL A 214 ? 0.4101 0.3354 0.2912 0.0422  0.0077  0.0088  214 VAL A O   
1736  C CB  . VAL A 214 ? 0.5253 0.4044 0.3859 0.0301  -0.0075 0.0018  214 VAL A CB  
1737  C CG1 . VAL A 214 ? 0.5538 0.4176 0.4088 0.0298  -0.0144 -0.0001 214 VAL A CG1 
1738  C CG2 . VAL A 214 ? 0.4430 0.3368 0.3142 0.0207  0.0019  0.0036  214 VAL A CG2 
1739  N N   . LYS A 215 ? 0.4399 0.3454 0.3074 0.0437  -0.0030 0.0083  215 LYS A N   
1740  C CA  . LYS A 215 ? 0.4519 0.3702 0.3283 0.0381  -0.0010 0.0142  215 LYS A CA  
1741  C C   . LYS A 215 ? 0.4791 0.3879 0.3533 0.0239  -0.0025 0.0136  215 LYS A C   
1742  O O   . LYS A 215 ? 0.4414 0.3364 0.3074 0.0210  -0.0077 0.0124  215 LYS A O   
1743  C CB  . LYS A 215 ? 0.4426 0.3654 0.3173 0.0482  -0.0045 0.0182  215 LYS A CB  
1744  C CG  . LYS A 215 ? 0.4606 0.4002 0.3375 0.0659  -0.0012 0.0216  215 LYS A CG  
1745  C CD  . LYS A 215 ? 0.4539 0.4022 0.3302 0.0775  -0.0038 0.0276  215 LYS A CD  
1746  C CE  . LYS A 215 ? 0.5570 0.5200 0.4288 0.1011  -0.0005 0.0300  215 LYS A CE  
1747  N NZ  . LYS A 215 ? 0.6309 0.6135 0.5077 0.1132  -0.0001 0.0400  215 LYS A NZ  
1748  N N   . PRO A 216 ? 0.4359 0.3510 0.3156 0.0155  0.0006  0.0150  216 PRO A N   
1749  C CA  . PRO A 216 ? 0.4562 0.3850 0.3465 0.0154  0.0035  0.0180  216 PRO A CA  
1750  C C   . PRO A 216 ? 0.3819 0.3123 0.2741 0.0168  0.0084  0.0143  216 PRO A C   
1751  O O   . PRO A 216 ? 0.3978 0.3179 0.2833 0.0144  0.0096  0.0096  216 PRO A O   
1752  C CB  . PRO A 216 ? 0.4474 0.3713 0.3358 0.0056  0.0007  0.0188  216 PRO A CB  
1753  C CG  . PRO A 216 ? 0.3918 0.3029 0.2680 0.0018  0.0021  0.0137  216 PRO A CG  
1754  C CD  . PRO A 216 ? 0.4368 0.3432 0.3098 0.0059  0.0001  0.0138  216 PRO A CD  
1755  N N   . ALA A 217 ? 0.4017 0.3462 0.3041 0.0203  0.0108  0.0179  217 ALA A N   
1756  C CA  . ALA A 217 ? 0.4035 0.3495 0.3082 0.0208  0.0153  0.0145  217 ALA A CA  
1757  C C   . ALA A 217 ? 0.3888 0.3269 0.2915 0.0114  0.0159  0.0109  217 ALA A C   
1758  O O   . ALA A 217 ? 0.3855 0.3237 0.2906 0.0060  0.0125  0.0133  217 ALA A O   
1759  C CB  . ALA A 217 ? 0.3517 0.3175 0.2688 0.0265  0.0175  0.0213  217 ALA A CB  
1760  N N   . PRO A 218 ? 0.3539 0.2847 0.2513 0.0101  0.0192  0.0058  218 PRO A N   
1761  C CA  . PRO A 218 ? 0.3683 0.2945 0.2624 0.0048  0.0212  0.0030  218 PRO A CA  
1762  C C   . PRO A 218 ? 0.3739 0.3051 0.2752 0.0041  0.0216  0.0030  218 PRO A C   
1763  O O   . PRO A 218 ? 0.3988 0.3235 0.2947 0.0016  0.0203  0.0005  218 PRO A O   
1764  C CB  . PRO A 218 ? 0.3970 0.3197 0.2877 0.0045  0.0247  0.0011  218 PRO A CB  
1765  C CG  . PRO A 218 ? 0.3639 0.2868 0.2573 0.0098  0.0229  0.0013  218 PRO A CG  
1766  C CD  . PRO A 218 ? 0.3610 0.2856 0.2537 0.0139  0.0192  0.0036  218 PRO A CD  
1767  N N   . LEU A 219 ? 0.3301 0.2720 0.2416 0.0075  0.0227  0.0060  219 LEU A N   
1768  C CA  . LEU A 219 ? 0.3457 0.2945 0.2667 0.0058  0.0219  0.0084  219 LEU A CA  
1769  C C   . LEU A 219 ? 0.3657 0.3301 0.2992 0.0071  0.0183  0.0183  219 LEU A C   
1770  O O   . LEU A 219 ? 0.3711 0.3449 0.3059 0.0139  0.0202  0.0218  219 LEU A O   
1771  C CB  . LEU A 219 ? 0.4093 0.3615 0.3331 0.0088  0.0276  0.0055  219 LEU A CB  
1772  C CG  . LEU A 219 ? 0.4329 0.3751 0.3488 0.0070  0.0313  -0.0007 219 LEU A CG  
1773  C CD1 . LEU A 219 ? 0.4287 0.3745 0.3487 0.0094  0.0353  -0.0021 219 LEU A CD1 
1774  C CD2 . LEU A 219 ? 0.4085 0.3440 0.3201 0.0041  0.0297  -0.0033 219 LEU A CD2 
1775  N N   . ASP A 220 ? 0.3400 0.3081 0.2828 0.0014  0.0123  0.0241  220 ASP A N   
1776  C CA  . ASP A 220 ? 0.3558 0.3445 0.3159 0.0007  0.0082  0.0379  220 ASP A CA  
1777  C C   . ASP A 220 ? 0.3365 0.3362 0.3066 0.0015  0.0109  0.0408  220 ASP A C   
1778  O O   . ASP A 220 ? 0.3512 0.3383 0.3155 -0.0004 0.0125  0.0322  220 ASP A O   
1779  C CB  . ASP A 220 ? 0.3802 0.3622 0.3444 -0.0091 -0.0051 0.0450  220 ASP A CB  
1780  C CG  . ASP A 220 ? 0.3782 0.3421 0.3378 -0.0155 -0.0126 0.0399  220 ASP A CG  
1781  O OD1 . ASP A 220 ? 0.5325 0.4751 0.4738 -0.0143 -0.0115 0.0273  220 ASP A OD1 
1782  O OD2 . ASP A 220 ? 0.5173 0.4890 0.4904 -0.0200 -0.0186 0.0482  220 ASP A OD2 
1783  N N   . GLU A 221 ? 0.3263 0.3523 0.3115 0.0057  0.0124  0.0541  221 GLU A N   
1784  C CA  . GLU A 221 ? 0.3458 0.3847 0.3391 0.0084  0.0167  0.0570  221 GLU A CA  
1785  C C   . GLU A 221 ? 0.3452 0.3775 0.3473 -0.0032 0.0073  0.0604  221 GLU A C   
1786  O O   . GLU A 221 ? 0.3500 0.3782 0.3512 -0.0031 0.0104  0.0549  221 GLU A O   
1787  C CB  . GLU A 221 ? 0.3119 0.3839 0.3169 0.0189  0.0217  0.0715  221 GLU A CB  
1788  C CG  . GLU A 221 ? 0.3332 0.4197 0.3438 0.0242  0.0273  0.0743  221 GLU A CG  
1789  C CD  . GLU A 221 ? 0.3460 0.4669 0.3638 0.0390  0.0341  0.0880  221 GLU A CD  
1790  O OE1 . GLU A 221 ? 0.3585 0.4821 0.3674 0.0504  0.0416  0.0823  221 GLU A OE1 
1791  O OE2 . GLU A 221 ? 0.3626 0.5056 0.3911 0.0417  0.0324  0.1029  221 GLU A OE2 
1792  N N   . LYS A 222 ? 0.3326 0.3594 0.3411 -0.0134 -0.0060 0.0684  222 LYS A N   
1793  C CA  . LYS A 222 ? 0.3713 0.3833 0.3834 -0.0237 -0.0187 0.0696  222 LYS A CA  
1794  C C   . LYS A 222 ? 0.3921 0.3755 0.3839 -0.0217 -0.0156 0.0500  222 LYS A C   
1795  O O   . LYS A 222 ? 0.4109 0.3891 0.4044 -0.0233 -0.0171 0.0475  222 LYS A O   
1796  C CB  . LYS A 222 ? 0.4478 0.4502 0.4648 -0.0346 -0.0372 0.0796  222 LYS A CB  
1797  C CG  . LYS A 222 ? 0.5442 0.5396 0.5724 -0.0458 -0.0547 0.0891  222 LYS A CG  
1798  C CD  . LYS A 222 ? 0.6352 0.6036 0.6576 -0.0563 -0.0777 0.0922  222 LYS A CD  
1799  C CE  . LYS A 222 ? 0.6863 0.6424 0.7187 -0.0682 -0.1000 0.1025  222 LYS A CE  
1800  N NZ  . LYS A 222 ? 0.6768 0.5913 0.6831 -0.0652 -0.1073 0.0822  222 LYS A NZ  
1801  N N   . THR A 223 ? 0.3763 0.3437 0.3497 -0.0174 -0.0107 0.0376  223 THR A N   
1802  C CA  . THR A 223 ? 0.4430 0.3908 0.3989 -0.0134 -0.0051 0.0221  223 THR A CA  
1803  C C   . THR A 223 ? 0.3828 0.3420 0.3421 -0.0080 0.0077  0.0185  223 THR A C   
1804  O O   . THR A 223 ? 0.3969 0.3482 0.3527 -0.0072 0.0093  0.0123  223 THR A O   
1805  C CB  . THR A 223 ? 0.4529 0.3877 0.3910 -0.0100 -0.0018 0.0136  223 THR A CB  
1806  O OG1 . THR A 223 ? 0.4579 0.3786 0.3902 -0.0147 -0.0154 0.0160  223 THR A OG1 
1807  C CG2 . THR A 223 ? 0.4244 0.3455 0.3464 -0.0048 0.0048  0.0013  223 THR A CG2 
1808  N N   . MET A 224 ? 0.3346 0.3108 0.2991 -0.0029 0.0157  0.0222  224 MET A N   
1809  C CA  . MET A 224 ? 0.3669 0.3503 0.3323 0.0026  0.0249  0.0188  224 MET A CA  
1810  C C   . MET A 224 ? 0.3437 0.3372 0.3217 0.0006  0.0236  0.0243  224 MET A C   
1811  O O   . MET A 224 ? 0.3548 0.3472 0.3308 0.0034  0.0295  0.0189  224 MET A O   
1812  C CB  . MET A 224 ? 0.3546 0.3500 0.3187 0.0111  0.0308  0.0210  224 MET A CB  
1813  C CG  . MET A 224 ? 0.3245 0.3097 0.2772 0.0128  0.0309  0.0165  224 MET A CG  
1814  S SD  . MET A 224 ? 0.4813 0.4773 0.4302 0.0249  0.0340  0.0197  224 MET A SD  
1815  C CE  . MET A 224 ? 0.4655 0.4501 0.4042 0.0297  0.0380  0.0104  224 MET A CE  
1816  N N   . TYR A 225 ? 0.3430 0.3462 0.3347 -0.0053 0.0148  0.0361  225 TYR A N   
1817  C CA  . TYR A 225 ? 0.3807 0.3935 0.3850 -0.0081 0.0127  0.0423  225 TYR A CA  
1818  C C   . TYR A 225 ? 0.3543 0.3456 0.3504 -0.0106 0.0108  0.0311  225 TYR A C   
1819  O O   . TYR A 225 ? 0.3235 0.3202 0.3257 -0.0104 0.0133  0.0316  225 TYR A O   
1820  C CB  . TYR A 225 ? 0.3635 0.3911 0.3870 -0.0164 0.0004  0.0604  225 TYR A CB  
1821  C CG  . TYR A 225 ? 0.3483 0.4085 0.3853 -0.0118 0.0042  0.0767  225 TYR A CG  
1822  C CD1 . TYR A 225 ? 0.3963 0.4743 0.4299 0.0014  0.0180  0.0756  225 TYR A CD1 
1823  C CD2 . TYR A 225 ? 0.3790 0.4512 0.4302 -0.0190 -0.0068 0.0934  225 TYR A CD2 
1824  C CE1 . TYR A 225 ? 0.3510 0.4600 0.3934 0.0101  0.0223  0.0903  225 TYR A CE1 
1825  C CE2 . TYR A 225 ? 0.3961 0.5018 0.4601 -0.0128 -0.0022 0.1099  225 TYR A CE2 
1826  C CZ  . TYR A 225 ? 0.3860 0.5110 0.4444 0.0034  0.0135  0.1077  225 TYR A CZ  
1827  O OH  . TYR A 225 ? 0.4099 0.5700 0.4781 0.0139  0.0190  0.1241  225 TYR A OH  
1828  N N   . SER A 226 ? 0.3238 0.2918 0.3049 -0.0114 0.0067  0.0214  226 SER A N   
1829  C CA  . SER A 226 ? 0.3115 0.2617 0.2823 -0.0097 0.0067  0.0109  226 SER A CA  
1830  C C   . SER A 226 ? 0.3456 0.2970 0.3086 -0.0033 0.0203  0.0023  226 SER A C   
1831  O O   . SER A 226 ? 0.3660 0.3084 0.3225 -0.0004 0.0226  -0.0044 226 SER A O   
1832  C CB  . SER A 226 ? 0.3999 0.3259 0.3546 -0.0096 -0.0033 0.0047  226 SER A CB  
1833  O OG  . SER A 226 ? 0.4637 0.3814 0.4250 -0.0166 -0.0204 0.0120  226 SER A OG  
1834  N N   . LEU A 227 ? 0.3328 0.2944 0.2960 -0.0006 0.0279  0.0032  227 LEU A N   
1835  C CA  . LEU A 227 ? 0.3157 0.2762 0.2722 0.0033  0.0368  -0.0024 227 LEU A CA  
1836  C C   . LEU A 227 ? 0.2937 0.2655 0.2571 0.0057  0.0415  0.0000  227 LEU A C   
1837  O O   . LEU A 227 ? 0.3502 0.3203 0.3133 0.0064  0.0454  -0.0030 227 LEU A O   
1838  C CB  . LEU A 227 ? 0.3407 0.2974 0.2879 0.0048  0.0383  -0.0039 227 LEU A CB  
1839  C CG  . LEU A 227 ? 0.3607 0.3059 0.2985 0.0036  0.0329  -0.0060 227 LEU A CG  
1840  C CD1 . LEU A 227 ? 0.3671 0.3107 0.2970 0.0046  0.0349  -0.0064 227 LEU A CD1 
1841  C CD2 . LEU A 227 ? 0.3897 0.3257 0.3185 0.0065  0.0348  -0.0118 227 LEU A CD2 
1842  N N   . TYR A 228 ? 0.3220 0.3060 0.2909 0.0080  0.0407  0.0063  228 TYR A N   
1843  C CA  . TYR A 228 ? 0.3178 0.3114 0.2887 0.0136  0.0443  0.0080  228 TYR A CA  
1844  C C   . TYR A 228 ? 0.3034 0.3025 0.2842 0.0107  0.0441  0.0104  228 TYR A C   
1845  O O   . TYR A 228 ? 0.2992 0.3018 0.2796 0.0145  0.0471  0.0097  228 TYR A O   
1846  C CB  . TYR A 228 ? 0.3186 0.3285 0.2919 0.0206  0.0445  0.0159  228 TYR A CB  
1847  C CG  . TYR A 228 ? 0.3110 0.3414 0.2997 0.0193  0.0428  0.0274  228 TYR A CG  
1848  C CD1 . TYR A 228 ? 0.3069 0.3376 0.3067 0.0094  0.0358  0.0332  228 TYR A CD1 
1849  C CD2 . TYR A 228 ? 0.2870 0.3358 0.2783 0.0284  0.0468  0.0336  228 TYR A CD2 
1850  C CE1 . TYR A 228 ? 0.3257 0.3752 0.3422 0.0059  0.0316  0.0465  228 TYR A CE1 
1851  C CE2 . TYR A 228 ? 0.3028 0.3753 0.3108 0.0266  0.0454  0.0476  228 TYR A CE2 
1852  C CZ  . TYR A 228 ? 0.3555 0.4283 0.3779 0.0138  0.0371  0.0548  228 TYR A CZ  
1853  O OH  . TYR A 228 ? 0.3565 0.4514 0.3981 0.0088  0.0323  0.0713  228 TYR A OH  
1854  N N   . VAL A 229 ? 0.2915 0.2883 0.2793 0.0043  0.0387  0.0127  229 VAL A N   
1855  C CA  . VAL A 229 ? 0.2925 0.2949 0.2907 0.0013  0.0367  0.0164  229 VAL A CA  
1856  C C   . VAL A 229 ? 0.2765 0.2694 0.2704 0.0021  0.0409  0.0085  229 VAL A C   
1857  O O   . VAL A 229 ? 0.2897 0.2886 0.2908 0.0016  0.0416  0.0107  229 VAL A O   
1858  C CB  . VAL A 229 ? 0.2888 0.2862 0.2939 -0.0059 0.0260  0.0211  229 VAL A CB  
1859  C CG1 . VAL A 229 ? 0.3057 0.2807 0.2982 -0.0063 0.0230  0.0111  229 VAL A CG1 
1860  C CG2 . VAL A 229 ? 0.2920 0.2966 0.3099 -0.0097 0.0220  0.0273  229 VAL A CG2 
1861  N N   . LEU A 230 ? 0.2643 0.2450 0.2481 0.0031  0.0438  0.0011  230 LEU A N   
1862  C CA  . LEU A 230 ? 0.3075 0.2835 0.2903 0.0036  0.0477  -0.0032 230 LEU A CA  
1863  C C   . LEU A 230 ? 0.3136 0.2958 0.2995 0.0050  0.0507  -0.0018 230 LEU A C   
1864  O O   . LEU A 230 ? 0.3027 0.2864 0.2944 0.0039  0.0515  -0.0016 230 LEU A O   
1865  C CB  . LEU A 230 ? 0.3055 0.2737 0.2786 0.0052  0.0509  -0.0074 230 LEU A CB  
1866  C CG  . LEU A 230 ? 0.3222 0.2811 0.2881 0.0063  0.0466  -0.0103 230 LEU A CG  
1867  C CD1 . LEU A 230 ? 0.4269 0.3808 0.3811 0.0102  0.0502  -0.0133 230 LEU A CD1 
1868  C CD2 . LEU A 230 ? 0.3309 0.2836 0.2993 0.0067  0.0412  -0.0117 230 LEU A CD2 
1869  N N   . CYS A 231 ? 0.2871 0.2703 0.2671 0.0084  0.0512  -0.0012 231 CYS A N   
1870  C CA  . CYS A 231 ? 0.2835 0.2675 0.2613 0.0119  0.0512  -0.0009 231 CYS A CA  
1871  C C   . CYS A 231 ? 0.2768 0.2737 0.2622 0.0141  0.0513  0.0037  231 CYS A C   
1872  O O   . CYS A 231 ? 0.2911 0.2881 0.2746 0.0170  0.0512  0.0036  231 CYS A O   
1873  C CB  . CYS A 231 ? 0.2845 0.2634 0.2500 0.0182  0.0492  -0.0021 231 CYS A CB  
1874  S SG  . CYS A 231 ? 0.3426 0.3056 0.2999 0.0146  0.0463  -0.0049 231 CYS A SG  
1875  N N   . THR A 232 ? 0.2720 0.2803 0.2654 0.0129  0.0502  0.0094  232 THR A N   
1876  C CA  . THR A 232 ? 0.2582 0.2826 0.2622 0.0133  0.0496  0.0173  232 THR A CA  
1877  C C   . THR A 232 ? 0.2472 0.2680 0.2610 0.0061  0.0474  0.0170  232 THR A C   
1878  O O   . THR A 232 ? 0.2522 0.2851 0.2753 0.0055  0.0464  0.0237  232 THR A O   
1879  C CB  . THR A 232 ? 0.2584 0.2997 0.2712 0.0131  0.0471  0.0280  232 THR A CB  
1880  O OG1 . THR A 232 ? 0.2665 0.3008 0.2874 0.0034  0.0405  0.0294  232 THR A OG1 
1881  C CG2 . THR A 232 ? 0.2607 0.3041 0.2636 0.0204  0.0491  0.0278  232 THR A CG2 
1882  N N   . LEU A 233 ? 0.2689 0.2748 0.2800 0.0023  0.0467  0.0103  233 LEU A N   
1883  C CA  . LEU A 233 ? 0.2741 0.2743 0.2912 -0.0014 0.0448  0.0085  233 LEU A CA  
1884  C C   . LEU A 233 ? 0.2837 0.2812 0.2992 -0.0001 0.0492  0.0050  233 LEU A C   
1885  O O   . LEU A 233 ? 0.2885 0.2910 0.3110 -0.0012 0.0488  0.0075  233 LEU A O   
1886  C CB  . LEU A 233 ? 0.2716 0.2582 0.2838 -0.0025 0.0414  0.0036  233 LEU A CB  
1887  C CG  . LEU A 233 ? 0.2665 0.2519 0.2789 -0.0050 0.0341  0.0075  233 LEU A CG  
1888  C CD1 . LEU A 233 ? 0.2912 0.2580 0.2938 -0.0038 0.0288  0.0009  233 LEU A CD1 
1889  C CD2 . LEU A 233 ? 0.2662 0.2619 0.2931 -0.0104 0.0260  0.0180  233 LEU A CD2 
1890  N N   . SER A 234 ? 0.2826 0.2734 0.2902 0.0014  0.0524  0.0011  234 SER A N   
1891  C CA  . SER A 234 ? 0.3072 0.2960 0.3155 0.0008  0.0540  0.0009  234 SER A CA  
1892  C C   . SER A 234 ? 0.2640 0.2464 0.2636 0.0014  0.0537  0.0002  234 SER A C   
1893  O O   . SER A 234 ? 0.2878 0.2682 0.2871 -0.0002 0.0554  0.0008  234 SER A O   
1894  C CB  . SER A 234 ? 0.2919 0.2802 0.3066 -0.0006 0.0558  0.0004  234 SER A CB  
1895  O OG  . SER A 234 ? 0.3283 0.3180 0.3478 -0.0024 0.0563  0.0030  234 SER A OG  
1896  N N   . LYS A 235 ? 0.2789 0.2589 0.2705 0.0050  0.0508  0.0000  235 LYS A N   
1897  C CA  . LYS A 235 ? 0.2787 0.2483 0.2602 0.0057  0.0472  -0.0009 235 LYS A CA  
1898  C C   . LYS A 235 ? 0.2969 0.2597 0.2809 0.0007  0.0432  0.0022  235 LYS A C   
1899  O O   . LYS A 235 ? 0.2924 0.2484 0.2732 -0.0024 0.0395  0.0046  235 LYS A O   
1900  C CB  . LYS A 235 ? 0.3067 0.2721 0.2752 0.0139  0.0435  -0.0027 235 LYS A CB  
1901  C CG  . LYS A 235 ? 0.3284 0.2970 0.2939 0.0198  0.0422  -0.0024 235 LYS A CG  
1902  C CD  . LYS A 235 ? 0.3166 0.2852 0.2663 0.0328  0.0404  -0.0037 235 LYS A CD  
1903  C CE  . LYS A 235 ? 0.3509 0.3300 0.2972 0.0420  0.0416  -0.0015 235 LYS A CE  
1904  N NZ  . LYS A 235 ? 0.3881 0.3595 0.3351 0.0387  0.0379  -0.0022 235 LYS A NZ  
1905  N N   . SER A 236 ? 0.2952 0.2606 0.2863 -0.0013 0.0428  0.0040  236 SER A N   
1906  C CA  . SER A 236 ? 0.3248 0.2854 0.3209 -0.0075 0.0375  0.0095  236 SER A CA  
1907  C C   . SER A 236 ? 0.2974 0.2704 0.3074 -0.0120 0.0437  0.0154  236 SER A C   
1908  O O   . SER A 236 ? 0.3106 0.2856 0.3291 -0.0176 0.0401  0.0234  236 SER A O   
1909  C CB  . SER A 236 ? 0.3252 0.2825 0.3221 -0.0073 0.0332  0.0098  236 SER A CB  
1910  O OG  . SER A 236 ? 0.3246 0.2948 0.3334 -0.0076 0.0402  0.0099  236 SER A OG  
1911  N N   . SER A 237 ? 0.2860 0.2676 0.2979 -0.0087 0.0518  0.0125  237 SER A N   
1912  C CA  . SER A 237 ? 0.3171 0.3103 0.3374 -0.0084 0.0579  0.0174  237 SER A CA  
1913  C C   . SER A 237 ? 0.3475 0.3449 0.3668 -0.0101 0.0586  0.0241  237 SER A C   
1914  O O   . SER A 237 ? 0.3526 0.3426 0.3630 -0.0105 0.0557  0.0219  237 SER A O   
1915  C CB  . SER A 237 ? 0.3274 0.3234 0.3457 -0.0021 0.0636  0.0110  237 SER A CB  
1916  O OG  . SER A 237 ? 0.3660 0.3566 0.3741 0.0002  0.0637  0.0064  237 SER A OG  
1917  N N   . GLN A 238 ? 0.3753 0.3700 0.3202 -0.0278 0.0347  -0.0178 238 GLN A N   
1918  C CA  . GLN A 238 ? 0.3890 0.3874 0.3367 -0.0315 0.0386  -0.0148 238 GLN A CA  
1919  C C   . GLN A 238 ? 0.3827 0.3773 0.3215 -0.0308 0.0412  -0.0127 238 GLN A C   
1920  O O   . GLN A 238 ? 0.3675 0.3604 0.3048 -0.0339 0.0431  -0.0091 238 GLN A O   
1921  C CB  . GLN A 238 ? 0.3805 0.3899 0.3361 -0.0311 0.0409  -0.0158 238 GLN A CB  
1922  C CG  . GLN A 238 ? 0.4583 0.4740 0.4187 -0.0348 0.0455  -0.0118 238 GLN A CG  
1923  C CD  . GLN A 238 ? 0.4993 0.5165 0.4709 -0.0400 0.0443  -0.0102 238 GLN A CD  
1924  O OE1 . GLN A 238 ? 0.4797 0.4988 0.4589 -0.0399 0.0403  -0.0139 238 GLN A OE1 
1925  N NE2 . GLN A 238 ? 0.4919 0.5092 0.4659 -0.0444 0.0475  -0.0046 238 GLN A NE2 
1926  N N   . TRP A 239 ? 0.3309 0.3238 0.2641 -0.0266 0.0409  -0.0150 239 TRP A N   
1927  C CA  . TRP A 239 ? 0.3812 0.3715 0.3067 -0.0252 0.0426  -0.0144 239 TRP A CA  
1928  C C   . TRP A 239 ? 0.3311 0.3129 0.2515 -0.0273 0.0412  -0.0121 239 TRP A C   
1929  O O   . TRP A 239 ? 0.3675 0.3487 0.2831 -0.0280 0.0431  -0.0101 239 TRP A O   
1930  C CB  . TRP A 239 ? 0.3568 0.3459 0.2795 -0.0203 0.0414  -0.0181 239 TRP A CB  
1931  C CG  . TRP A 239 ? 0.3619 0.3436 0.2839 -0.0187 0.0377  -0.0191 239 TRP A CG  
1932  C CD1 . TRP A 239 ? 0.3862 0.3687 0.3121 -0.0163 0.0357  -0.0205 239 TRP A CD1 
1933  C CD2 . TRP A 239 ? 0.3593 0.3325 0.2767 -0.0190 0.0358  -0.0182 239 TRP A CD2 
1934  N NE1 . TRP A 239 ? 0.4108 0.3859 0.3346 -0.0152 0.0332  -0.0196 239 TRP A NE1 
1935  C CE2 . TRP A 239 ? 0.3762 0.3459 0.2955 -0.0170 0.0333  -0.0184 239 TRP A CE2 
1936  C CE3 . TRP A 239 ? 0.3762 0.3453 0.2886 -0.0205 0.0361  -0.0170 239 TRP A CE3 
1937  C CZ2 . TRP A 239 ? 0.4010 0.3638 0.3181 -0.0170 0.0315  -0.0168 239 TRP A CZ2 
1938  C CZ3 . TRP A 239 ? 0.3919 0.3538 0.3022 -0.0205 0.0337  -0.0165 239 TRP A CZ3 
1939  C CH2 . TRP A 239 ? 0.4229 0.3820 0.3361 -0.0189 0.0317  -0.0162 239 TRP A CH2 
1940  N N   . CYS A 240 ? 0.3489 0.3252 0.2699 -0.0278 0.0379  -0.0125 240 CYS A N   
1941  C CA  . CYS A 240 ? 0.3556 0.3245 0.2720 -0.0291 0.0363  -0.0110 240 CYS A CA  
1942  C C   . CYS A 240 ? 0.3707 0.3393 0.2892 -0.0331 0.0371  -0.0080 240 CYS A C   
1943  O O   . CYS A 240 ? 0.3619 0.3271 0.2758 -0.0341 0.0379  -0.0057 240 CYS A O   
1944  C CB  . CYS A 240 ? 0.3650 0.3300 0.2816 -0.0278 0.0330  -0.0121 240 CYS A CB  
1945  S SG  . CYS A 240 ? 0.3912 0.3484 0.3022 -0.0284 0.0313  -0.0106 240 CYS A SG  
1946  N N   . ALA A 241 ? 0.3643 0.3364 0.2906 -0.0351 0.0365  -0.0082 241 ALA A N   
1947  C CA  . ALA A 241 ? 0.3430 0.3143 0.2742 -0.0394 0.0368  -0.0051 241 ALA A CA  
1948  C C   . ALA A 241 ? 0.3878 0.3630 0.3181 -0.0410 0.0416  -0.0005 241 ALA A C   
1949  O O   . ALA A 241 ? 0.3580 0.3294 0.2864 -0.0432 0.0423  0.0035  241 ALA A O   
1950  C CB  . ALA A 241 ? 0.3521 0.3274 0.2941 -0.0411 0.0347  -0.0071 241 ALA A CB  
1951  N N   . ASP A 242 ? 0.3563 0.3395 0.2872 -0.0394 0.0448  -0.0010 242 ASP A N   
1952  C CA  . ASP A 242 ? 0.3783 0.3674 0.3072 -0.0397 0.0498  0.0034  242 ASP A CA  
1953  C C   . ASP A 242 ? 0.3695 0.3541 0.2868 -0.0371 0.0502  0.0042  242 ASP A C   
1954  O O   . ASP A 242 ? 0.3831 0.3686 0.2972 -0.0381 0.0529  0.0092  242 ASP A O   
1955  C CB  . ASP A 242 ? 0.3950 0.3949 0.3267 -0.0373 0.0529  0.0016  242 ASP A CB  
1956  C CG  . ASP A 242 ? 0.4321 0.4389 0.3768 -0.0405 0.0535  0.0023  242 ASP A CG  
1957  O OD1 . ASP A 242 ? 0.4126 0.4161 0.3648 -0.0451 0.0520  0.0048  242 ASP A OD1 
1958  O OD2 . ASP A 242 ? 0.4020 0.4177 0.3503 -0.0382 0.0552  -0.0001 242 ASP A OD2 
1959  N N   . PHE A 243 ? 0.3608 0.3409 0.2721 -0.0335 0.0473  -0.0005 243 PHE A N   
1960  C CA  . PHE A 243 ? 0.3527 0.3287 0.2544 -0.0311 0.0468  -0.0007 243 PHE A CA  
1961  C C   . PHE A 243 ? 0.3793 0.3476 0.2788 -0.0336 0.0451  0.0026  243 PHE A C   
1962  O O   . PHE A 243 ? 0.3740 0.3418 0.2671 -0.0328 0.0463  0.0055  243 PHE A O   
1963  C CB  . PHE A 243 ? 0.4372 0.4094 0.3358 -0.0275 0.0437  -0.0063 243 PHE A CB  
1964  C CG  . PHE A 243 ? 0.4224 0.3917 0.3131 -0.0248 0.0426  -0.0075 243 PHE A CG  
1965  C CD1 . PHE A 243 ? 0.4319 0.4077 0.3175 -0.0214 0.0451  -0.0081 243 PHE A CD1 
1966  C CD2 . PHE A 243 ? 0.4596 0.4210 0.3480 -0.0252 0.0393  -0.0081 243 PHE A CD2 
1967  C CE1 . PHE A 243 ? 0.4829 0.4568 0.3609 -0.0182 0.0435  -0.0101 243 PHE A CE1 
1968  C CE2 . PHE A 243 ? 0.4402 0.3996 0.3222 -0.0225 0.0379  -0.0098 243 PHE A CE2 
1969  C CZ  . PHE A 243 ? 0.4555 0.4211 0.3322 -0.0190 0.0397  -0.0111 243 PHE A CZ  
1970  N N   . MET A 244 ? 0.3663 0.3293 0.2708 -0.0361 0.0420  0.0020  244 MET A N   
1971  C CA  . MET A 244 ? 0.3526 0.3085 0.2559 -0.0380 0.0399  0.0045  244 MET A CA  
1972  C C   . MET A 244 ? 0.3913 0.3487 0.2964 -0.0409 0.0429  0.0109  244 MET A C   
1973  O O   . MET A 244 ? 0.3725 0.3258 0.2724 -0.0407 0.0428  0.0142  244 MET A O   
1974  C CB  . MET A 244 ? 0.3366 0.2887 0.2459 -0.0393 0.0362  0.0019  244 MET A CB  
1975  C CG  . MET A 244 ? 0.3371 0.2874 0.2429 -0.0360 0.0338  -0.0025 244 MET A CG  
1976  S SD  . MET A 244 ? 0.4146 0.3592 0.3124 -0.0341 0.0323  -0.0027 244 MET A SD  
1977  C CE  . MET A 244 ? 0.4512 0.3990 0.3462 -0.0309 0.0334  -0.0056 244 MET A CE  
1978  N N   . ASP A 245 ? 0.3560 0.3198 0.2693 -0.0434 0.0457  0.0133  245 ASP A N   
1979  C CA  . ASP A 245 ? 0.3600 0.3262 0.2764 -0.0464 0.0492  0.0209  245 ASP A CA  
1980  C C   . ASP A 245 ? 0.3917 0.3623 0.2977 -0.0431 0.0531  0.0244  245 ASP A C   
1981  O O   . ASP A 245 ? 0.4349 0.4030 0.3376 -0.0438 0.0544  0.0306  245 ASP A O   
1982  C CB  . ASP A 245 ? 0.3659 0.3404 0.2940 -0.0495 0.0521  0.0229  245 ASP A CB  
1983  C CG  . ASP A 245 ? 0.3926 0.3629 0.3331 -0.0536 0.0481  0.0212  245 ASP A CG  
1984  O OD1 . ASP A 245 ? 0.4152 0.3761 0.3549 -0.0539 0.0435  0.0193  245 ASP A OD1 
1985  O OD2 . ASP A 245 ? 0.4132 0.3906 0.3644 -0.0558 0.0493  0.0208  245 ASP A OD2 
1986  N N   . GLU A 246 ? 0.3782 0.3558 0.2792 -0.0390 0.0549  0.0205  246 GLU A N   
1987  C CA  . GLU A 246 ? 0.4346 0.4176 0.3249 -0.0345 0.0578  0.0220  246 GLU A CA  
1988  C C   . GLU A 246 ? 0.3977 0.3725 0.2787 -0.0323 0.0544  0.0212  246 GLU A C   
1989  O O   . GLU A 246 ? 0.4191 0.3955 0.2928 -0.0304 0.0563  0.0261  246 GLU A O   
1990  C CB  . GLU A 246 ? 0.4213 0.4106 0.3083 -0.0297 0.0580  0.0151  246 GLU A CB  
1991  C CG  . GLU A 246 ? 0.4874 0.4884 0.3784 -0.0287 0.0623  0.0155  246 GLU A CG  
1992  C CD  . GLU A 246 ? 0.5181 0.5240 0.4016 -0.0218 0.0617  0.0084  246 GLU A CD  
1993  O OE1 . GLU A 246 ? 0.4991 0.5020 0.3856 -0.0206 0.0584  0.0017  246 GLU A OE1 
1994  O OE2 . GLU A 246 ? 0.5956 0.6082 0.4703 -0.0172 0.0643  0.0095  246 GLU A OE2 
1995  N N   . LEU A 247 ? 0.4013 0.3685 0.2826 -0.0321 0.0495  0.0153  247 LEU A N   
1996  C CA  . LEU A 247 ? 0.4171 0.3770 0.2914 -0.0301 0.0458  0.0135  247 LEU A CA  
1997  C C   . LEU A 247 ? 0.3918 0.3460 0.2662 -0.0327 0.0453  0.0196  247 LEU A C   
1998  O O   . LEU A 247 ? 0.4179 0.3704 0.2845 -0.0302 0.0448  0.0217  247 LEU A O   
1999  C CB  . LEU A 247 ? 0.3767 0.3308 0.2540 -0.0301 0.0413  0.0071  247 LEU A CB  
2000  C CG  . LEU A 247 ? 0.4036 0.3515 0.2756 -0.0281 0.0374  0.0046  247 LEU A CG  
2001  C CD1 . LEU A 247 ? 0.4053 0.3568 0.2688 -0.0234 0.0375  0.0026  247 LEU A CD1 
2002  C CD2 . LEU A 247 ? 0.4069 0.3511 0.2828 -0.0279 0.0341  -0.0007 247 LEU A CD2 
2003  N N   . TYR A 248 ? 0.3912 0.3423 0.2751 -0.0374 0.0450  0.0222  248 TYR A N   
2004  C CA  . TYR A 248 ? 0.3910 0.3357 0.2769 -0.0399 0.0442  0.0281  248 TYR A CA  
2005  C C   . TYR A 248 ? 0.4317 0.3809 0.3130 -0.0393 0.0487  0.0366  248 TYR A C   
2006  O O   . TYR A 248 ? 0.4494 0.3939 0.3251 -0.0380 0.0477  0.0406  248 TYR A O   
2007  C CB  . TYR A 248 ? 0.3915 0.3331 0.2900 -0.0448 0.0427  0.0285  248 TYR A CB  
2008  C CG  . TYR A 248 ? 0.4401 0.3743 0.3443 -0.0480 0.0412  0.0343  248 TYR A CG  
2009  C CD1 . TYR A 248 ? 0.4571 0.3819 0.3593 -0.0471 0.0362  0.0321  248 TYR A CD1 
2010  C CD2 . TYR A 248 ? 0.4901 0.4270 0.4023 -0.0519 0.0447  0.0422  248 TYR A CD2 
2011  C CE1 . TYR A 248 ? 0.3961 0.3132 0.3045 -0.0498 0.0341  0.0371  248 TYR A CE1 
2012  C CE2 . TYR A 248 ? 0.5340 0.4630 0.4531 -0.0551 0.0430  0.0481  248 TYR A CE2 
2013  C CZ  . TYR A 248 ? 0.5423 0.4609 0.4592 -0.0538 0.0373  0.0450  248 TYR A CZ  
2014  O OH  . TYR A 248 ? 0.5986 0.5085 0.5228 -0.0565 0.0349  0.0502  248 TYR A OH  
2015  N N   . GLU A 249 ? 0.4394 0.3988 0.3221 -0.0392 0.0539  0.0395  249 GLU A N   
2016  C CA  . GLU A 249 ? 0.4241 0.3899 0.3019 -0.0379 0.0590  0.0485  249 GLU A CA  
2017  C C   . GLU A 249 ? 0.4285 0.3949 0.2912 -0.0314 0.0580  0.0469  249 GLU A C   
2018  O O   . GLU A 249 ? 0.4538 0.4189 0.3107 -0.0301 0.0590  0.0539  249 GLU A O   
2019  C CB  . GLU A 249 ? 0.4589 0.4378 0.3399 -0.0377 0.0650  0.0506  249 GLU A CB  
2020  C CG  . GLU A 249 ? 0.4472 0.4273 0.3445 -0.0444 0.0668  0.0546  249 GLU A CG  
2021  C CD  . GLU A 249 ? 0.5658 0.5386 0.4713 -0.0496 0.0666  0.0637  249 GLU A CD  
2022  O OE1 . GLU A 249 ? 0.5512 0.5246 0.4506 -0.0482 0.0695  0.0724  249 GLU A OE1 
2023  O OE2 . GLU A 249 ? 0.5690 0.5345 0.4866 -0.0544 0.0627  0.0613  249 GLU A OE2 
2024  N N   . GLU A 250 ? 0.4124 0.3805 0.2694 -0.0273 0.0554  0.0375  250 GLU A N   
2025  C CA  . GLU A 250 ? 0.4180 0.3871 0.2624 -0.0210 0.0534  0.0344  250 GLU A CA  
2026  C C   . GLU A 250 ? 0.4370 0.3955 0.2789 -0.0213 0.0486  0.0348  250 GLU A C   
2027  O O   . GLU A 250 ? 0.4518 0.4109 0.2844 -0.0175 0.0485  0.0384  250 GLU A O   
2028  C CB  . GLU A 250 ? 0.4326 0.4048 0.2740 -0.0169 0.0508  0.0238  250 GLU A CB  
2029  C CG  . GLU A 250 ? 0.4445 0.4171 0.2745 -0.0106 0.0476  0.0199  250 GLU A CG  
2030  C CD  . GLU A 250 ? 0.5205 0.4978 0.3468 -0.0051 0.0451  0.0099  250 GLU A CD  
2031  O OE1 . GLU A 250 ? 0.5236 0.5026 0.3563 -0.0061 0.0453  0.0051  250 GLU A OE1 
2032  O OE2 . GLU A 250 ? 0.5336 0.5135 0.3503 0.0010  0.0426  0.0066  250 GLU A OE2 
2033  N N   . VAL A 251 ? 0.4238 0.3735 0.2734 -0.0251 0.0447  0.0313  251 VAL A N   
2034  C CA  . VAL A 251 ? 0.3949 0.3356 0.2424 -0.0247 0.0401  0.0308  251 VAL A CA  
2035  C C   . VAL A 251 ? 0.4468 0.3834 0.2948 -0.0265 0.0413  0.0404  251 VAL A C   
2036  O O   . VAL A 251 ? 0.4333 0.3664 0.2742 -0.0235 0.0391  0.0425  251 VAL A O   
2037  C CB  . VAL A 251 ? 0.3945 0.3286 0.2497 -0.0275 0.0359  0.0245  251 VAL A CB  
2038  C CG1 . VAL A 251 ? 0.3900 0.3163 0.2433 -0.0265 0.0314  0.0238  251 VAL A CG1 
2039  C CG2 . VAL A 251 ? 0.3947 0.3324 0.2487 -0.0250 0.0347  0.0165  251 VAL A CG2 
2040  N N   . LYS A 252 ? 0.4409 0.3783 0.2977 -0.0312 0.0448  0.0467  252 LYS A N   
2041  C CA  . LYS A 252 ? 0.4821 0.4160 0.3412 -0.0333 0.0466  0.0573  252 LYS A CA  
2042  C C   . LYS A 252 ? 0.4879 0.4285 0.3348 -0.0283 0.0501  0.0640  252 LYS A C   
2043  O O   . LYS A 252 ? 0.4956 0.4314 0.3386 -0.0270 0.0494  0.0709  252 LYS A O   
2044  C CB  . LYS A 252 ? 0.5398 0.4759 0.4123 -0.0394 0.0503  0.0626  252 LYS A CB  
2045  C CG  . LYS A 252 ? 0.6548 0.5841 0.5360 -0.0436 0.0506  0.0726  252 LYS A CG  
2046  C CD  . LYS A 252 ? 0.6569 0.5752 0.5493 -0.0474 0.0445  0.0669  252 LYS A CD  
2047  C CE  . LYS A 252 ? 0.7339 0.6409 0.6315 -0.0493 0.0414  0.0735  252 LYS A CE  
2048  N NZ  . LYS A 252 ? 0.7440 0.6432 0.6580 -0.0546 0.0374  0.0714  252 LYS A NZ  
2049  N N   . ASP A 253 ? 0.4669 0.4191 0.3073 -0.0246 0.0539  0.0620  253 ASP A N   
2050  C CA  . ASP A 253 ? 0.4922 0.4528 0.3195 -0.0184 0.0571  0.0673  253 ASP A CA  
2051  C C   . ASP A 253 ? 0.5034 0.4601 0.3193 -0.0125 0.0516  0.0618  253 ASP A C   
2052  O O   . ASP A 253 ? 0.4981 0.4556 0.3049 -0.0085 0.0521  0.0685  253 ASP A O   
2053  C CB  . ASP A 253 ? 0.5138 0.4882 0.3374 -0.0151 0.0616  0.0644  253 ASP A CB  
2054  C CG  . ASP A 253 ? 0.5706 0.5558 0.3797 -0.0075 0.0650  0.0691  253 ASP A CG  
2055  O OD1 . ASP A 253 ? 0.5597 0.5470 0.3673 -0.0078 0.0694  0.0817  253 ASP A OD1 
2056  O OD2 . ASP A 253 ? 0.6577 0.6495 0.4573 -0.0008 0.0632  0.0602  253 ASP A OD2 
2057  N N   . ARG A 254 ? 0.4547 0.4073 0.2719 -0.0120 0.0463  0.0504  254 ARG A N   
2058  C CA  . ARG A 254 ? 0.4517 0.4001 0.2613 -0.0075 0.0405  0.0450  254 ARG A CA  
2059  C C   . ARG A 254 ? 0.4864 0.4250 0.2968 -0.0088 0.0380  0.0514  254 ARG A C   
2060  O O   . ARG A 254 ? 0.4696 0.4082 0.2703 -0.0036 0.0359  0.0534  254 ARG A O   
2061  C CB  . ARG A 254 ? 0.4550 0.4001 0.2695 -0.0083 0.0357  0.0331  254 ARG A CB  
2062  C CG  . ARG A 254 ? 0.4736 0.4272 0.2868 -0.0057 0.0368  0.0258  254 ARG A CG  
2063  C CD  . ARG A 254 ? 0.4373 0.3867 0.2576 -0.0074 0.0324  0.0159  254 ARG A CD  
2064  N NE  . ARG A 254 ? 0.4419 0.3877 0.2595 -0.0044 0.0266  0.0101  254 ARG A NE  
2065  C CZ  . ARG A 254 ? 0.5101 0.4606 0.3222 0.0011  0.0236  0.0031  254 ARG A CZ  
2066  N NH1 . ARG A 254 ? 0.5043 0.4634 0.3112 0.0051  0.0258  0.0011  254 ARG A NH1 
2067  N NH2 . ARG A 254 ? 0.4897 0.4368 0.3023 0.0029  0.0179  -0.0025 254 ARG A NH2 
2068  N N   . VAL A 255 ? 0.4375 0.3677 0.2596 -0.0152 0.0375  0.0538  255 VAL A N   
2069  C CA  . VAL A 255 ? 0.4499 0.3700 0.2743 -0.0164 0.0345  0.0592  255 VAL A CA  
2070  C C   . VAL A 255 ? 0.4761 0.3981 0.2949 -0.0145 0.0384  0.0719  255 VAL A C   
2071  O O   . VAL A 255 ? 0.4997 0.4176 0.3116 -0.0107 0.0358  0.0756  255 VAL A O   
2072  C CB  . VAL A 255 ? 0.4089 0.3205 0.2476 -0.0230 0.0330  0.0585  255 VAL A CB  
2073  C CG1 . VAL A 255 ? 0.4789 0.3797 0.3212 -0.0240 0.0299  0.0648  255 VAL A CG1 
2074  C CG2 . VAL A 255 ? 0.4294 0.3398 0.2715 -0.0234 0.0289  0.0466  255 VAL A CG2 
2075  N N   . ALA A 256 ? 0.4812 0.4102 0.3030 -0.0170 0.0449  0.0793  256 ALA A N   
2076  C CA  . ALA A 256 ? 0.4768 0.4093 0.2942 -0.0155 0.0498  0.0932  256 ALA A CA  
2077  C C   . ALA A 256 ? 0.5102 0.4496 0.3099 -0.0064 0.0496  0.0942  256 ALA A C   
2078  O O   . ALA A 256 ? 0.5213 0.4599 0.3151 -0.0036 0.0511  0.1052  256 ALA A O   
2079  C CB  . ALA A 256 ? 0.4736 0.4163 0.2964 -0.0187 0.0575  0.0995  256 ALA A CB  
2080  N N   . ARG A 257 ? 0.4814 0.4280 0.2729 -0.0015 0.0477  0.0831  257 ARG A N   
2081  C CA  . ARG A 257 ? 0.5456 0.5010 0.3207 0.0078  0.0472  0.0821  257 ARG A CA  
2082  C C   . ARG A 257 ? 0.5129 0.4619 0.2825 0.0120  0.0392  0.0741  257 ARG A C   
2083  O O   . ARG A 257 ? 0.5443 0.5002 0.3005 0.0203  0.0373  0.0716  257 ARG A O   
2084  C CB  . ARG A 257 ? 0.5237 0.4920 0.2941 0.0113  0.0496  0.0742  257 ARG A CB  
2085  C CG  . ARG A 257 ? 0.5942 0.5732 0.3650 0.0105  0.0583  0.0846  257 ARG A CG  
2086  C CD  . ARG A 257 ? 0.6584 0.6516 0.4210 0.0167  0.0603  0.0773  257 ARG A CD  
2087  N NE  . ARG A 257 ? 0.6118 0.6028 0.3844 0.0125  0.0581  0.0658  257 ARG A NE  
2088  C CZ  . ARG A 257 ? 0.6890 0.6833 0.4572 0.0173  0.0536  0.0526  257 ARG A CZ  
2089  N NH1 . ARG A 257 ? 0.6893 0.6886 0.4442 0.0261  0.0501  0.0477  257 ARG A NH1 
2090  N NH2 . ARG A 257 ? 0.6472 0.6392 0.4252 0.0133  0.0522  0.0439  257 ARG A NH2 
2091  N N   . GLY A 258 ? 0.5166 0.4535 0.2962 0.0070  0.0346  0.0702  258 GLY A N   
2092  C CA  . GLY A 258 ? 0.4889 0.4199 0.2660 0.0102  0.0272  0.0629  258 GLY A CA  
2093  C C   . GLY A 258 ? 0.5341 0.4706 0.3089 0.0133  0.0235  0.0492  258 GLY A C   
2094  O O   . GLY A 258 ? 0.4978 0.4339 0.2672 0.0183  0.0178  0.0432  258 GLY A O   
2095  N N   . ILE A 259 ? 0.4650 0.4063 0.2447 0.0105  0.0263  0.0443  259 ILE A N   
2096  C CA  . ILE A 259 ? 0.4756 0.4215 0.2554 0.0128  0.0229  0.0317  259 ILE A CA  
2097  C C   . ILE A 259 ? 0.4743 0.4122 0.2639 0.0092  0.0176  0.0241  259 ILE A C   
2098  O O   . ILE A 259 ? 0.4665 0.3977 0.2662 0.0029  0.0186  0.0256  259 ILE A O   
2099  C CB  . ILE A 259 ? 0.4981 0.4510 0.2810 0.0109  0.0276  0.0299  259 ILE A CB  
2100  C CG1 . ILE A 259 ? 0.5466 0.5101 0.3195 0.0155  0.0332  0.0371  259 ILE A CG1 
2101  C CG2 . ILE A 259 ? 0.5307 0.4862 0.3163 0.0126  0.0236  0.0169  259 ILE A CG2 
2102  C CD1 . ILE A 259 ? 0.5709 0.5428 0.3303 0.0251  0.0302  0.0318  259 ILE A CD1 
2103  N N   . ALA A 260 ? 0.4854 0.4250 0.2726 0.0135  0.0120  0.0153  260 ALA A N   
2104  C CA  . ALA A 260 ? 0.4727 0.4072 0.2690 0.0110  0.0072  0.0078  260 ALA A CA  
2105  C C   . ALA A 260 ? 0.4655 0.4041 0.2673 0.0106  0.0059  -0.0017 260 ALA A C   
2106  O O   . ALA A 260 ? 0.4744 0.4200 0.2703 0.0157  0.0048  -0.0065 260 ALA A O   
2107  C CB  . ALA A 260 ? 0.4811 0.4148 0.2728 0.0160  0.0014  0.0051  260 ALA A CB  
2108  N N   . ALA A 261 ? 0.4314 0.3658 0.2446 0.0052  0.0057  -0.0046 261 ALA A N   
2109  C CA  . ALA A 261 ? 0.4334 0.3701 0.2541 0.0045  0.0035  -0.0132 261 ALA A CA  
2110  C C   . ALA A 261 ? 0.4707 0.4096 0.2911 0.0089  -0.0028 -0.0206 261 ALA A C   
2111  O O   . ALA A 261 ? 0.4891 0.4320 0.3114 0.0113  -0.0054 -0.0280 261 ALA A O   
2112  C CB  . ALA A 261 ? 0.4513 0.3832 0.2836 -0.0016 0.0045  -0.0132 261 ALA A CB  
2113  N N   . VAL A 262 ? 0.4618 0.3982 0.2805 0.0104  -0.0058 -0.0191 262 VAL A N   
2114  C CA  . VAL A 262 ? 0.4614 0.4000 0.2820 0.0141  -0.0123 -0.0262 262 VAL A CA  
2115  C C   . VAL A 262 ? 0.5072 0.4472 0.3156 0.0202  -0.0144 -0.0232 262 VAL A C   
2116  O O   . VAL A 262 ? 0.4792 0.4146 0.2856 0.0195  -0.0138 -0.0170 262 VAL A O   
2117  C CB  . VAL A 262 ? 0.4853 0.4205 0.3181 0.0100  -0.0143 -0.0278 262 VAL A CB  
2118  C CG1 . VAL A 262 ? 0.4728 0.4109 0.3086 0.0136  -0.0209 -0.0342 262 VAL A CG1 
2119  C CG2 . VAL A 262 ? 0.4639 0.3986 0.3080 0.0048  -0.0121 -0.0302 262 VAL A CG2 
2120  N N   . PRO A 263 ? 0.4901 0.4365 0.2898 0.0269  -0.0171 -0.0275 263 PRO A N   
2121  C CA  . PRO A 263 ? 0.5307 0.4796 0.3157 0.0333  -0.0173 -0.0222 263 PRO A CA  
2122  C C   . PRO A 263 ? 0.5853 0.5321 0.3696 0.0362  -0.0227 -0.0226 263 PRO A C   
2123  O O   . PRO A 263 ? 0.6136 0.5594 0.3876 0.0399  -0.0221 -0.0153 263 PRO A O   
2124  C CB  . PRO A 263 ? 0.5874 0.5454 0.3642 0.0405  -0.0195 -0.0289 263 PRO A CB  
2125  C CG  . PRO A 263 ? 0.5421 0.5009 0.3315 0.0384  -0.0237 -0.0400 263 PRO A CG  
2126  C CD  . PRO A 263 ? 0.5077 0.4596 0.3101 0.0291  -0.0197 -0.0368 263 PRO A CD  
2127  N N   . ASN A 264 ? 0.5201 0.4664 0.3159 0.0347  -0.0278 -0.0304 264 ASN A N   
2128  C CA  . ASN A 264 ? 0.5595 0.5043 0.3566 0.0369  -0.0327 -0.0310 264 ASN A CA  
2129  C C   . ASN A 264 ? 0.5160 0.4539 0.3230 0.0305  -0.0305 -0.0269 264 ASN A C   
2130  O O   . ASN A 264 ? 0.5139 0.4517 0.3278 0.0308  -0.0346 -0.0302 264 ASN A O   
2131  C CB  . ASN A 264 ? 0.5639 0.5144 0.3679 0.0402  -0.0403 -0.0425 264 ASN A CB  
2132  C CG  . ASN A 264 ? 0.5781 0.5285 0.3990 0.0339  -0.0405 -0.0488 264 ASN A CG  
2133  O OD1 . ASN A 264 ? 0.5770 0.5249 0.4015 0.0287  -0.0352 -0.0462 264 ASN A OD1 
2134  N ND2 . ASN A 264 ? 0.5614 0.5150 0.3935 0.0344  -0.0466 -0.0568 264 ASN A ND2 
2135  N N   . GLU A 265 ? 0.5009 0.4340 0.3088 0.0252  -0.0243 -0.0202 265 GLU A N   
2136  C CA  . GLU A 265 ? 0.5103 0.4375 0.3271 0.0199  -0.0225 -0.0171 265 GLU A CA  
2137  C C   . GLU A 265 ? 0.5319 0.4561 0.3473 0.0231  -0.0263 -0.0153 265 GLU A C   
2138  O O   . GLU A 265 ? 0.5158 0.4375 0.3210 0.0271  -0.0268 -0.0096 265 GLU A O   
2139  C CB  . GLU A 265 ? 0.5140 0.4362 0.3294 0.0154  -0.0162 -0.0094 265 GLU A CB  
2140  C CG  . GLU A 265 ? 0.4602 0.3765 0.2840 0.0110  -0.0151 -0.0071 265 GLU A CG  
2141  C CD  . GLU A 265 ? 0.4955 0.4066 0.3194 0.0066  -0.0100 -0.0003 265 GLU A CD  
2142  O OE1 . GLU A 265 ? 0.4704 0.3838 0.2934 0.0044  -0.0061 0.0008  265 GLU A OE1 
2143  O OE2 . GLU A 265 ? 0.4792 0.3842 0.3051 0.0057  -0.0103 0.0036  265 GLU A OE2 
2144  N N   . ALA A 266 ? 0.4723 0.3974 0.2982 0.0216  -0.0291 -0.0199 266 ALA A N   
2145  C CA  . ALA A 266 ? 0.4964 0.4186 0.3224 0.0244  -0.0324 -0.0184 266 ALA A CA  
2146  C C   . ALA A 266 ? 0.4876 0.4080 0.3245 0.0204  -0.0311 -0.0191 266 ALA A C   
2147  O O   . ALA A 266 ? 0.5022 0.4187 0.3392 0.0222  -0.0329 -0.0170 266 ALA A O   
2148  C CB  . ALA A 266 ? 0.4803 0.4085 0.3064 0.0300  -0.0389 -0.0248 266 ALA A CB  
2149  N N   . ILE A 267 ? 0.4718 0.3954 0.3179 0.0156  -0.0284 -0.0220 267 ILE A N   
2150  C CA  . ILE A 267 ? 0.4450 0.3694 0.3015 0.0124  -0.0268 -0.0229 267 ILE A CA  
2151  C C   . ILE A 267 ? 0.4432 0.3655 0.3017 0.0071  -0.0213 -0.0203 267 ILE A C   
2152  O O   . ILE A 267 ? 0.4579 0.3824 0.3169 0.0051  -0.0195 -0.0214 267 ILE A O   
2153  C CB  . ILE A 267 ? 0.4399 0.3726 0.3078 0.0122  -0.0293 -0.0290 267 ILE A CB  
2154  C CG1 . ILE A 267 ? 0.5037 0.4393 0.3705 0.0177  -0.0353 -0.0322 267 ILE A CG1 
2155  C CG2 . ILE A 267 ? 0.4234 0.3589 0.3017 0.0086  -0.0261 -0.0288 267 ILE A CG2 
2156  C CD1 . ILE A 267 ? 0.5278 0.4723 0.4068 0.0173  -0.0383 -0.0387 267 ILE A CD1 
2157  N N   . ARG A 268 ? 0.4234 0.3419 0.2835 0.0055  -0.0193 -0.0175 268 ARG A N   
2158  C CA  . ARG A 268 ? 0.4197 0.3365 0.2819 0.0012  -0.0147 -0.0154 268 ARG A CA  
2159  C C   . ARG A 268 ? 0.3997 0.3215 0.2715 -0.0004 -0.0135 -0.0178 268 ARG A C   
2160  O O   . ARG A 268 ? 0.4002 0.3225 0.2746 0.0018  -0.0152 -0.0187 268 ARG A O   
2161  C CB  . ARG A 268 ? 0.4031 0.3120 0.2600 0.0007  -0.0135 -0.0103 268 ARG A CB  
2162  C CG  . ARG A 268 ? 0.4029 0.3082 0.2502 0.0018  -0.0132 -0.0059 268 ARG A CG  
2163  C CD  . ARG A 268 ? 0.4464 0.3431 0.2904 0.0018  -0.0131 0.0002  268 ARG A CD  
2164  N NE  . ARG A 268 ? 0.3999 0.2939 0.2481 -0.0027 -0.0095 0.0023  268 ARG A NE  
2165  C CZ  . ARG A 268 ? 0.4027 0.2963 0.2485 -0.0055 -0.0057 0.0062  268 ARG A CZ  
2166  N NH1 . ARG A 268 ? 0.4145 0.3106 0.2531 -0.0040 -0.0044 0.0088  268 ARG A NH1 
2167  N NH2 . ARG A 268 ? 0.4090 0.3005 0.2599 -0.0094 -0.0033 0.0073  268 ARG A NH2 
2168  N N   . LEU A 269 ? 0.3940 0.3196 0.2709 -0.0036 -0.0106 -0.0185 269 LEU A N   
2169  C CA  . LEU A 269 ? 0.3455 0.2770 0.2314 -0.0051 -0.0087 -0.0195 269 LEU A CA  
2170  C C   . LEU A 269 ? 0.4055 0.3353 0.2912 -0.0077 -0.0048 -0.0172 269 LEU A C   
2171  O O   . LEU A 269 ? 0.4123 0.3381 0.2937 -0.0097 -0.0031 -0.0155 269 LEU A O   
2172  C CB  . LEU A 269 ? 0.3478 0.2857 0.2421 -0.0067 -0.0085 -0.0218 269 LEU A CB  
2173  C CG  . LEU A 269 ? 0.3590 0.2999 0.2556 -0.0042 -0.0131 -0.0253 269 LEU A CG  
2174  C CD1 . LEU A 269 ? 0.4037 0.3499 0.3108 -0.0064 -0.0138 -0.0281 269 LEU A CD1 
2175  C CD2 . LEU A 269 ? 0.3832 0.3274 0.2823 -0.0011 -0.0153 -0.0262 269 LEU A CD2 
2176  N N   . MET A 270 ? 0.3844 0.3187 0.2750 -0.0072 -0.0034 -0.0173 270 MET A N   
2177  C CA  . MET A 270 ? 0.3882 0.3234 0.2799 -0.0089 0.0000  -0.0158 270 MET A CA  
2178  C C   . MET A 270 ? 0.3725 0.3164 0.2725 -0.0097 0.0025  -0.0153 270 MET A C   
2179  O O   . MET A 270 ? 0.3925 0.3427 0.2980 -0.0079 0.0017  -0.0162 270 MET A O   
2180  C CB  . MET A 270 ? 0.3591 0.2921 0.2482 -0.0065 -0.0009 -0.0163 270 MET A CB  
2181  C CG  . MET A 270 ? 0.4036 0.3357 0.2921 -0.0078 0.0013  -0.0155 270 MET A CG  
2182  S SD  . MET A 270 ? 0.4243 0.3577 0.3127 -0.0033 -0.0008 -0.0184 270 MET A SD  
2183  C CE  . MET A 270 ? 0.4096 0.3544 0.3026 0.0007  -0.0004 -0.0198 270 MET A CE  
2184  N N   . THR A 271 ? 0.3774 0.3219 0.2793 -0.0124 0.0056  -0.0135 271 THR A N   
2185  C CA  . THR A 271 ? 0.3546 0.3068 0.2646 -0.0132 0.0085  -0.0114 271 THR A CA  
2186  C C   . THR A 271 ? 0.3803 0.3353 0.2883 -0.0118 0.0111  -0.0097 271 THR A C   
2187  O O   . THR A 271 ? 0.3776 0.3292 0.2796 -0.0100 0.0099  -0.0113 271 THR A O   
2188  C CB  . THR A 271 ? 0.3651 0.3162 0.2799 -0.0167 0.0095  -0.0105 271 THR A CB  
2189  O OG1 . THR A 271 ? 0.4013 0.3471 0.3106 -0.0180 0.0107  -0.0100 271 THR A OG1 
2190  C CG2 . THR A 271 ? 0.4105 0.3591 0.3263 -0.0171 0.0061  -0.0134 271 THR A CG2 
2191  N N   . ASP A 272 ? 0.3624 0.3243 0.2764 -0.0123 0.0145  -0.0065 272 ASP A N   
2192  C CA  . ASP A 272 ? 0.3927 0.3584 0.3040 -0.0100 0.0167  -0.0050 272 ASP A CA  
2193  C C   . ASP A 272 ? 0.4090 0.3747 0.3235 -0.0127 0.0196  -0.0015 272 ASP A C   
2194  O O   . ASP A 272 ? 0.4530 0.4115 0.3658 -0.0156 0.0188  -0.0025 272 ASP A O   
2195  C CB  . ASP A 272 ? 0.4159 0.3921 0.3294 -0.0057 0.0180  -0.0042 272 ASP A CB  
2196  C CG  . ASP A 272 ? 0.4236 0.4038 0.3318 -0.0017 0.0191  -0.0045 272 ASP A CG  
2197  O OD1 . ASP A 272 ? 0.4855 0.4588 0.3875 -0.0012 0.0165  -0.0081 272 ASP A OD1 
2198  O OD2 . ASP A 272 ? 0.4398 0.4309 0.3505 0.0014  0.0223  -0.0013 272 ASP A OD2 
2199  N N   . THR A 273 ? 0.3860 0.3597 0.3055 -0.0118 0.0230  0.0029  273 THR A N   
2200  C CA  . THR A 273 ? 0.4414 0.4143 0.3636 -0.0138 0.0254  0.0066  273 THR A CA  
2201  C C   . THR A 273 ? 0.5209 0.4880 0.4498 -0.0183 0.0245  0.0067  273 THR A C   
2202  O O   . THR A 273 ? 0.5416 0.5090 0.4765 -0.0197 0.0230  0.0057  273 THR A O   
2203  C CB  . THR A 273 ? 0.5001 0.4834 0.4271 -0.0115 0.0295  0.0128  273 THR A CB  
2204  O OG1 . THR A 273 ? 0.5071 0.4944 0.4451 -0.0138 0.0307  0.0161  273 THR A OG1 
2205  C CG2 . THR A 273 ? 0.5198 0.5112 0.4410 -0.0060 0.0300  0.0117  273 THR A CG2 
2206  N N   . GLN A 274 ? 0.5450 0.5070 0.4727 -0.0199 0.0247  0.0068  274 GLN A N   
2207  C CA  . GLN A 274 ? 0.5475 0.5076 0.4836 -0.0226 0.0255  0.0095  274 GLN A CA  
2208  C C   . GLN A 274 ? 0.4201 0.3822 0.3683 -0.0249 0.0250  0.0110  274 GLN A C   
2209  O O   . GLN A 274 ? 0.4298 0.3989 0.3857 -0.0247 0.0277  0.0165  274 GLN A O   
2210  C CB  . GLN A 274 ? 0.5287 0.4933 0.4639 -0.0206 0.0290  0.0146  274 GLN A CB  
2211  C CG  . GLN A 274 ? 0.4789 0.4503 0.4229 -0.0202 0.0325  0.0224  274 GLN A CG  
2212  C CD  . GLN A 274 ? 0.5223 0.5016 0.4594 -0.0155 0.0355  0.0260  274 GLN A CD  
2213  O OE1 . GLN A 274 ? 0.5802 0.5663 0.5134 -0.0123 0.0360  0.0253  274 GLN A OE1 
2214  N NE2 . GLN A 274 ? 0.4309 0.4100 0.3663 -0.0142 0.0370  0.0292  274 GLN A NE2 
2215  N N   . PRO A 275 ? 0.4708 0.4279 0.4217 -0.0268 0.0213  0.0062  275 PRO A N   
2216  C CA  . PRO A 275 ? 0.4134 0.3728 0.3777 -0.0289 0.0200  0.0068  275 PRO A CA  
2217  C C   . PRO A 275 ? 0.3874 0.3438 0.3632 -0.0316 0.0200  0.0092  275 PRO A C   
2218  O O   . PRO A 275 ? 0.4292 0.3809 0.4008 -0.0314 0.0204  0.0091  275 PRO A O   
2219  C CB  . PRO A 275 ? 0.5473 0.5024 0.5076 -0.0288 0.0152  -0.0005 275 PRO A CB  
2220  C CG  . PRO A 275 ? 0.5006 0.4489 0.4509 -0.0282 0.0145  -0.0036 275 PRO A CG  
2221  C CD  . PRO A 275 ? 0.5629 0.5128 0.5057 -0.0268 0.0182  0.0002  275 PRO A CD  
2222  N N   . PRO A 276 ? 0.4290 0.3881 0.4204 -0.0341 0.0194  0.0117  276 PRO A N   
2223  C CA  . PRO A 276 ? 0.3812 0.3352 0.3851 -0.0368 0.0179  0.0125  276 PRO A CA  
2224  C C   . PRO A 276 ? 0.3890 0.3351 0.3908 -0.0368 0.0120  0.0030  276 PRO A C   
2225  O O   . PRO A 276 ? 0.4288 0.3745 0.4231 -0.0354 0.0090  -0.0033 276 PRO A O   
2226  C CB  . PRO A 276 ? 0.4249 0.3843 0.4479 -0.0398 0.0183  0.0173  276 PRO A CB  
2227  C CG  . PRO A 276 ? 0.4673 0.4361 0.4870 -0.0383 0.0207  0.0192  276 PRO A CG  
2228  C CD  . PRO A 276 ? 0.4342 0.4015 0.4338 -0.0345 0.0202  0.0141  276 PRO A CD  
2229  N N   . TRP A 277 ? 0.4728 0.4049 0.4746 -0.1192 -0.0540 -0.0366 277 TRP A N   
2230  C CA  . TRP A 277 ? 0.4463 0.3613 0.4314 -0.1111 -0.0609 -0.0482 277 TRP A CA  
2231  C C   . TRP A 277 ? 0.4505 0.3763 0.4398 -0.1172 -0.0714 -0.0537 277 TRP A C   
2232  O O   . TRP A 277 ? 0.5119 0.4396 0.4910 -0.1069 -0.0739 -0.0615 277 TRP A O   
2233  C CB  . TRP A 277 ? 0.4909 0.3710 0.4618 -0.1116 -0.0665 -0.0531 277 TRP A CB  
2234  C CG  . TRP A 277 ? 0.5165 0.3852 0.4781 -0.1005 -0.0575 -0.0515 277 TRP A CG  
2235  C CD1 . TRP A 277 ? 0.5144 0.3810 0.4816 -0.1030 -0.0501 -0.0429 277 TRP A CD1 
2236  C CD2 . TRP A 277 ? 0.5125 0.3807 0.4617 -0.0841 -0.0521 -0.0561 277 TRP A CD2 
2237  N NE1 . TRP A 277 ? 0.5405 0.3999 0.4972 -0.0893 -0.0425 -0.0439 277 TRP A NE1 
2238  C CE2 . TRP A 277 ? 0.6054 0.4675 0.5521 -0.0779 -0.0430 -0.0512 277 TRP A CE2 
2239  C CE3 . TRP A 277 ? 0.6620 0.5345 0.6016 -0.0739 -0.0541 -0.0635 277 TRP A CE3 
2240  C CZ2 . TRP A 277 ? 0.6320 0.4933 0.5686 -0.0629 -0.0363 -0.0534 277 TRP A CZ2 
2241  C CZ3 . TRP A 277 ? 0.6521 0.5230 0.5808 -0.0587 -0.0468 -0.0651 277 TRP A CZ3 
2242  C CH2 . TRP A 277 ? 0.6678 0.5340 0.5959 -0.0539 -0.0381 -0.0599 277 TRP A CH2 
2243  N N   . SER A 278 ? 0.3916 0.3262 0.3961 -0.1336 -0.0776 -0.0491 278 SER A N   
2244  C CA  . SER A 278 ? 0.4774 0.4251 0.4893 -0.1419 -0.0885 -0.0534 278 SER A CA  
2245  C C   . SER A 278 ? 0.5031 0.4818 0.5198 -0.1333 -0.0846 -0.0536 278 SER A C   
2246  O O   . SER A 278 ? 0.5586 0.5464 0.5765 -0.1354 -0.0939 -0.0598 278 SER A O   
2247  C CB  . SER A 278 ? 0.5169 0.4736 0.5483 -0.1625 -0.0936 -0.0451 278 SER A CB  
2248  O OG  . SER A 278 ? 0.6042 0.5292 0.6291 -0.1729 -0.1043 -0.0489 278 SER A OG  
2249  N N   . PHE A 279 ? 0.4460 0.4401 0.4650 -0.1236 -0.0718 -0.0474 279 PHE A N   
2250  C CA  . PHE A 279 ? 0.4989 0.5189 0.5200 -0.1141 -0.0683 -0.0477 279 PHE A CA  
2251  C C   . PHE A 279 ? 0.5089 0.5175 0.5114 -0.0998 -0.0700 -0.0575 279 PHE A C   
2252  O O   . PHE A 279 ? 0.5141 0.5400 0.5160 -0.0937 -0.0718 -0.0605 279 PHE A O   
2253  C CB  . PHE A 279 ? 0.4167 0.4525 0.4436 -0.1075 -0.0553 -0.0386 279 PHE A CB  
2254  C CG  . PHE A 279 ? 0.4310 0.4959 0.4630 -0.1002 -0.0522 -0.0368 279 PHE A CG  
2255  C CD1 . PHE A 279 ? 0.4535 0.5173 0.4726 -0.0852 -0.0488 -0.0413 279 PHE A CD1 
2256  C CD2 . PHE A 279 ? 0.3957 0.4893 0.4449 -0.1078 -0.0527 -0.0302 279 PHE A CD2 
2257  C CE1 . PHE A 279 ? 0.4241 0.5119 0.4460 -0.0777 -0.0463 -0.0396 279 PHE A CE1 
2258  C CE2 . PHE A 279 ? 0.3691 0.4890 0.4212 -0.0991 -0.0502 -0.0290 279 PHE A CE2 
2259  C CZ  . PHE A 279 ? 0.3930 0.5084 0.4308 -0.0842 -0.0473 -0.0340 279 PHE A CZ  
2260  N N   . LEU A 280 ? 0.5440 0.5246 0.5308 -0.0936 -0.0694 -0.0622 280 LEU A N   
2261  C CA  . LEU A 280 ? 0.5798 0.5519 0.5487 -0.0782 -0.0688 -0.0697 280 LEU A CA  
2262  C C   . LEU A 280 ? 0.5948 0.5714 0.5590 -0.0777 -0.0799 -0.0784 280 LEU A C   
2263  O O   . LEU A 280 ? 0.5606 0.5459 0.5162 -0.0655 -0.0781 -0.0816 280 LEU A O   
2264  C CB  . LEU A 280 ? 0.6451 0.5875 0.5984 -0.0725 -0.0680 -0.0736 280 LEU A CB  
2265  C CG  . LEU A 280 ? 0.5590 0.4982 0.5110 -0.0654 -0.0555 -0.0671 280 LEU A CG  
2266  C CD1 . LEU A 280 ? 0.5578 0.5118 0.5266 -0.0727 -0.0477 -0.0563 280 LEU A CD1 
2267  C CD2 . LEU A 280 ? 0.6639 0.5751 0.6021 -0.0618 -0.0572 -0.0715 280 LEU A CD2 
2268  N N   . LYS A 281 ? 0.5372 0.5074 0.5066 -0.0909 -0.0920 -0.0821 281 LYS A N   
2269  C CA  . LYS A 281 ? 0.5863 0.5624 0.5533 -0.0922 -0.1042 -0.0905 281 LYS A CA  
2270  C C   . LYS A 281 ? 0.5341 0.5454 0.5142 -0.0918 -0.1025 -0.0866 281 LYS A C   
2271  O O   . LYS A 281 ? 0.5234 0.5430 0.4980 -0.0866 -0.1097 -0.0937 281 LYS A O   
2272  C CB  . LYS A 281 ? 0.5879 0.5494 0.5603 -0.1091 -0.1181 -0.0940 281 LYS A CB  
2273  C CG  . LYS A 281 ? 0.6135 0.6023 0.6091 -0.1249 -0.1233 -0.0886 281 LYS A CG  
2274  C CD  . LYS A 281 ? 0.6570 0.6326 0.6575 -0.1421 -0.1398 -0.0934 281 LYS A CD  
2275  C CE  . LYS A 281 ? 0.7007 0.6478 0.7003 -0.1522 -0.1403 -0.0899 281 LYS A CE  
2276  N NZ  . LYS A 281 ? 0.8087 0.7449 0.8160 -0.1717 -0.1570 -0.0929 281 LYS A NZ  
2277  N N   . ILE A 282 ? 0.4832 0.5156 0.4800 -0.0967 -0.0937 -0.0759 282 ILE A N   
2278  C CA  . ILE A 282 ? 0.4632 0.5287 0.4701 -0.0931 -0.0908 -0.0720 282 ILE A CA  
2279  C C   . ILE A 282 ? 0.4475 0.5148 0.4397 -0.0743 -0.0828 -0.0735 282 ILE A C   
2280  O O   . ILE A 282 ? 0.4650 0.5499 0.4556 -0.0673 -0.0852 -0.0761 282 ILE A O   
2281  C CB  . ILE A 282 ? 0.4394 0.5258 0.4656 -0.1013 -0.0832 -0.0601 282 ILE A CB  
2282  C CG1 . ILE A 282 ? 0.4687 0.5560 0.5108 -0.1212 -0.0912 -0.0571 282 ILE A CG1 
2283  C CG2 . ILE A 282 ? 0.4239 0.5433 0.4572 -0.0940 -0.0792 -0.0563 282 ILE A CG2 
2284  C CD1 . ILE A 282 ? 0.4275 0.5425 0.4905 -0.1297 -0.0850 -0.0448 282 ILE A CD1 
2285  N N   . PHE A 283 ? 0.4747 0.5248 0.4567 -0.0660 -0.0733 -0.0714 283 PHE A N   
2286  C CA  . PHE A 283 ? 0.4776 0.5263 0.4448 -0.0492 -0.0666 -0.0727 283 PHE A CA  
2287  C C   . PHE A 283 ? 0.5046 0.5474 0.4571 -0.0415 -0.0749 -0.0825 283 PHE A C   
2288  O O   . PHE A 283 ? 0.4767 0.5311 0.4225 -0.0305 -0.0732 -0.0834 283 PHE A O   
2289  C CB  . PHE A 283 ? 0.4544 0.4833 0.4123 -0.0426 -0.0572 -0.0700 283 PHE A CB  
2290  C CG  . PHE A 283 ? 0.5116 0.5462 0.4800 -0.0453 -0.0473 -0.0604 283 PHE A CG  
2291  C CD1 . PHE A 283 ? 0.5479 0.6024 0.5221 -0.0405 -0.0413 -0.0545 283 PHE A CD1 
2292  C CD2 . PHE A 283 ? 0.4559 0.4746 0.4262 -0.0508 -0.0443 -0.0578 283 PHE A CD2 
2293  C CE1 . PHE A 283 ? 0.4971 0.5551 0.4787 -0.0415 -0.0330 -0.0466 283 PHE A CE1 
2294  C CE2 . PHE A 283 ? 0.4735 0.4969 0.4521 -0.0523 -0.0359 -0.0496 283 PHE A CE2 
2295  C CZ  . PHE A 283 ? 0.4522 0.4950 0.4363 -0.0475 -0.0303 -0.0441 283 PHE A CZ  
2296  N N   . ARG A 284 ? 0.4799 0.5034 0.4260 -0.0464 -0.0843 -0.0901 284 ARG A N   
2297  C CA  . ARG A 284 ? 0.4831 0.4998 0.4135 -0.0383 -0.0932 -0.1004 284 ARG A CA  
2298  C C   . ARG A 284 ? 0.5242 0.5642 0.4626 -0.0415 -0.1020 -0.1032 284 ARG A C   
2299  O O   . ARG A 284 ? 0.5107 0.5577 0.4378 -0.0294 -0.1036 -0.1076 284 ARG A O   
2300  C CB  . ARG A 284 ? 0.5742 0.5635 0.4956 -0.0433 -0.1029 -0.1083 284 ARG A CB  
2301  C CG  . ARG A 284 ? 0.6871 0.6540 0.5905 -0.0308 -0.0959 -0.1097 284 ARG A CG  
2302  C CD  . ARG A 284 ? 0.7924 0.7302 0.6827 -0.0325 -0.1063 -0.1189 284 ARG A CD  
2303  N NE  . ARG A 284 ? 0.8460 0.7678 0.7410 -0.0399 -0.1019 -0.1140 284 ARG A NE  
2304  C CZ  . ARG A 284 ? 0.8199 0.7281 0.7219 -0.0547 -0.1106 -0.1153 284 ARG A CZ  
2305  N NH1 . ARG A 284 ? 0.7910 0.6975 0.6958 -0.0646 -0.1252 -0.1219 284 ARG A NH1 
2306  N NH2 . ARG A 284 ? 0.7933 0.6886 0.6991 -0.0599 -0.1048 -0.1095 284 ARG A NH2 
2307  N N   . TYR A 285 ? 0.4896 0.5436 0.4477 -0.0574 -0.1073 -0.1001 285 TYR A N   
2308  C CA  . TYR A 285 ? 0.4840 0.5650 0.4527 -0.0609 -0.1151 -0.1016 285 TYR A CA  
2309  C C   . TYR A 285 ? 0.4362 0.5408 0.4055 -0.0488 -0.1054 -0.0958 285 TYR A C   
2310  O O   . TYR A 285 ? 0.4516 0.5726 0.4177 -0.0417 -0.1103 -0.0996 285 TYR A O   
2311  C CB  . TYR A 285 ? 0.5305 0.6249 0.5227 -0.0808 -0.1203 -0.0966 285 TYR A CB  
2312  C CG  . TYR A 285 ? 0.5185 0.6462 0.5257 -0.0857 -0.1271 -0.0959 285 TYR A CG  
2313  C CD1 . TYR A 285 ? 0.5518 0.6820 0.5574 -0.0894 -0.1423 -0.1056 285 TYR A CD1 
2314  C CD2 . TYR A 285 ? 0.5114 0.6691 0.5340 -0.0859 -0.1187 -0.0859 285 TYR A CD2 
2315  C CE1 . TYR A 285 ? 0.5826 0.7457 0.6030 -0.0939 -0.1491 -0.1051 285 TYR A CE1 
2316  C CE2 . TYR A 285 ? 0.4921 0.6835 0.5289 -0.0893 -0.1248 -0.0851 285 TYR A CE2 
2317  C CZ  . TYR A 285 ? 0.5649 0.7596 0.6012 -0.0937 -0.1400 -0.0946 285 TYR A CZ  
2318  O OH  . TYR A 285 ? 0.5099 0.7397 0.5609 -0.0973 -0.1471 -0.0942 285 TYR A OH  
2319  N N   . LEU A 286 ? 0.4336 0.5392 0.4064 -0.0460 -0.0925 -0.0867 286 LEU A N   
2320  C CA  . LEU A 286 ? 0.4472 0.5714 0.4195 -0.0347 -0.0837 -0.0809 286 LEU A CA  
2321  C C   . LEU A 286 ? 0.4596 0.5762 0.4113 -0.0177 -0.0821 -0.0855 286 LEU A C   
2322  O O   . LEU A 286 ? 0.4834 0.6166 0.4320 -0.0078 -0.0802 -0.0840 286 LEU A O   
2323  C CB  . LEU A 286 ? 0.4110 0.5320 0.3887 -0.0351 -0.0713 -0.0713 286 LEU A CB  
2324  C CG  . LEU A 286 ? 0.4448 0.5850 0.4435 -0.0471 -0.0701 -0.0638 286 LEU A CG  
2325  C CD1 . LEU A 286 ? 0.4157 0.5474 0.4170 -0.0473 -0.0589 -0.0558 286 LEU A CD1 
2326  C CD2 . LEU A 286 ? 0.4505 0.6213 0.4561 -0.0422 -0.0706 -0.0612 286 LEU A CD2 
2327  N N   . GLU A 287 ? 0.5297 0.6218 0.4663 -0.0135 -0.0833 -0.0911 287 GLU A N   
2328  C CA  . GLU A 287 ? 0.5011 0.5864 0.4176 0.0030  -0.0808 -0.0943 287 GLU A CA  
2329  C C   . GLU A 287 ? 0.5056 0.6041 0.4167 0.0081  -0.0911 -0.1017 287 GLU A C   
2330  O O   . GLU A 287 ? 0.5343 0.6366 0.4319 0.0226  -0.0880 -0.1018 287 GLU A O   
2331  C CB  . GLU A 287 ? 0.5406 0.5992 0.4426 0.0067  -0.0801 -0.0985 287 GLU A CB  
2332  C CG  . GLU A 287 ? 0.4658 0.5137 0.3707 0.0055  -0.0685 -0.0907 287 GLU A CG  
2333  C CD  . GLU A 287 ? 0.6839 0.7077 0.5749 0.0100  -0.0677 -0.0947 287 GLU A CD  
2334  O OE1 . GLU A 287 ? 0.6821 0.6961 0.5746 0.0094  -0.0590 -0.0891 287 GLU A OE1 
2335  O OE2 . GLU A 287 ? 0.7268 0.7418 0.6048 0.0148  -0.0764 -0.1038 287 GLU A OE2 
2336  N N   . THR A 288 ? 0.5035 0.6096 0.4252 -0.0037 -0.1037 -0.1075 288 THR A N   
2337  C CA  . THR A 288 ? 0.5284 0.6501 0.4468 0.0008  -0.1145 -0.1146 288 THR A CA  
2338  C C   . THR A 288 ? 0.5084 0.6589 0.4345 0.0061  -0.1105 -0.1087 288 THR A C   
2339  O O   . THR A 288 ? 0.5555 0.7186 0.4740 0.0155  -0.1162 -0.1134 288 THR A O   
2340  C CB  . THR A 288 ? 0.5530 0.6760 0.4822 -0.0147 -0.1303 -0.1222 288 THR A CB  
2341  O OG1 . THR A 288 ? 0.5534 0.7026 0.5071 -0.0282 -0.1318 -0.1161 288 THR A OG1 
2342  C CG2 . THR A 288 ? 0.5792 0.6724 0.5039 -0.0227 -0.1333 -0.1260 288 THR A CG2 
2343  N N   . TYR A 289 ? 0.5005 0.6610 0.4398 0.0019  -0.1010 -0.0988 289 TYR A N   
2344  C CA  . TYR A 289 ? 0.4218 0.6040 0.3633 0.0110  -0.0949 -0.0925 289 TYR A CA  
2345  C C   . TYR A 289 ? 0.4663 0.6353 0.3905 0.0264  -0.0834 -0.0880 289 TYR A C   
2346  O O   . TYR A 289 ? 0.4752 0.6575 0.3985 0.0351  -0.0780 -0.0825 289 TYR A O   
2347  C CB  . TYR A 289 ? 0.4398 0.6388 0.4020 0.0010  -0.0898 -0.0837 289 TYR A CB  
2348  C CG  . TYR A 289 ? 0.4742 0.6963 0.4562 -0.0130 -0.1001 -0.0853 289 TYR A CG  
2349  C CD1 . TYR A 289 ? 0.4551 0.7079 0.4436 -0.0088 -0.1048 -0.0854 289 TYR A CD1 
2350  C CD2 . TYR A 289 ? 0.4375 0.6515 0.4322 -0.0306 -0.1051 -0.0860 289 TYR A CD2 
2351  C CE1 . TYR A 289 ? 0.4992 0.7767 0.5079 -0.0224 -0.1145 -0.0862 289 TYR A CE1 
2352  C CE2 . TYR A 289 ? 0.4692 0.7054 0.4837 -0.0451 -0.1149 -0.0863 289 TYR A CE2 
2353  C CZ  . TYR A 289 ? 0.4764 0.7457 0.4987 -0.0413 -0.1194 -0.0862 289 TYR A CZ  
2354  O OH  . TYR A 289 ? 0.4837 0.7787 0.5273 -0.0559 -0.1291 -0.0857 289 TYR A OH  
2355  N N   . GLY A 290 ? 0.4190 0.5624 0.3303 0.0296  -0.0792 -0.0892 290 GLY A N   
2356  C CA  . GLY A 290 ? 0.4454 0.5776 0.3442 0.0413  -0.0675 -0.0827 290 GLY A CA  
2357  C C   . GLY A 290 ? 0.4271 0.5570 0.3360 0.0363  -0.0577 -0.0736 290 GLY A C   
2358  O O   . GLY A 290 ? 0.4241 0.5500 0.3257 0.0452  -0.0490 -0.0672 290 GLY A O   
2359  N N   . ALA A 291 ? 0.3743 0.5060 0.2994 0.0223  -0.0592 -0.0726 291 ALA A N   
2360  C CA  . ALA A 291 ? 0.3946 0.5243 0.3289 0.0178  -0.0506 -0.0645 291 ALA A CA  
2361  C C   . ALA A 291 ? 0.4190 0.5244 0.3485 0.0152  -0.0456 -0.0639 291 ALA A C   
2362  O O   . ALA A 291 ? 0.4021 0.4961 0.3300 0.0096  -0.0510 -0.0697 291 ALA A O   
2363  C CB  . ALA A 291 ? 0.3423 0.4893 0.2968 0.0050  -0.0539 -0.0623 291 ALA A CB  
2364  N N   . VAL A 292 ? 0.3395 0.4366 0.2653 0.0202  -0.0360 -0.0572 292 VAL A N   
2365  C CA  . VAL A 292 ? 0.3649 0.4427 0.2885 0.0180  -0.0300 -0.0550 292 VAL A CA  
2366  C C   . VAL A 292 ? 0.3700 0.4495 0.3049 0.0127  -0.0239 -0.0478 292 VAL A C   
2367  O O   . VAL A 292 ? 0.3359 0.4243 0.2718 0.0176  -0.0203 -0.0429 292 VAL A O   
2368  C CB  . VAL A 292 ? 0.3894 0.4554 0.2971 0.0296  -0.0243 -0.0533 292 VAL A CB  
2369  C CG1 . VAL A 292 ? 0.3841 0.4569 0.2876 0.0383  -0.0192 -0.0470 292 VAL A CG1 
2370  C CG2 . VAL A 292 ? 0.3849 0.4343 0.2923 0.0271  -0.0178 -0.0502 292 VAL A CG2 
2371  N N   . SER A 293 ? 0.3487 0.4183 0.2906 0.0038  -0.0228 -0.0474 293 SER A N   
2372  C CA  . SER A 293 ? 0.3138 0.3809 0.2627 0.0012  -0.0161 -0.0407 293 SER A CA  
2373  C C   . SER A 293 ? 0.3226 0.3751 0.2623 0.0080  -0.0089 -0.0373 293 SER A C   
2374  O O   . SER A 293 ? 0.3313 0.3706 0.2649 0.0086  -0.0080 -0.0396 293 SER A O   
2375  C CB  . SER A 293 ? 0.3388 0.4014 0.2985 -0.0105 -0.0173 -0.0405 293 SER A CB  
2376  O OG  . SER A 293 ? 0.3608 0.4250 0.3264 -0.0108 -0.0111 -0.0341 293 SER A OG  
2377  N N   . ILE A 294 ? 0.3048 0.3597 0.2437 0.0132  -0.0039 -0.0316 294 ILE A N   
2378  C CA  . ILE A 294 ? 0.3026 0.3445 0.2348 0.0179  0.0024  -0.0275 294 ILE A CA  
2379  C C   . ILE A 294 ? 0.3109 0.3446 0.2505 0.0122  0.0062  -0.0243 294 ILE A C   
2380  O O   . ILE A 294 ? 0.3091 0.3329 0.2453 0.0146  0.0111  -0.0207 294 ILE A O   
2381  C CB  . ILE A 294 ? 0.3389 0.3830 0.2644 0.0264  0.0048  -0.0230 294 ILE A CB  
2382  C CG1 . ILE A 294 ? 0.3373 0.3914 0.2692 0.0262  0.0040  -0.0206 294 ILE A CG1 
2383  C CG2 . ILE A 294 ? 0.3854 0.4353 0.3010 0.0334  0.0015  -0.0262 294 ILE A CG2 
2384  C CD1 . ILE A 294 ? 0.3003 0.3486 0.2397 0.0216  0.0074  -0.0169 294 ILE A CD1 
2385  N N   . GLY A 295 ? 0.3128 0.3511 0.2628 0.0044  0.0042  -0.0251 295 GLY A N   
2386  C CA  . GLY A 295 ? 0.2936 0.3247 0.2495 0.0002  0.0080  -0.0217 295 GLY A CA  
2387  C C   . GLY A 295 ? 0.2861 0.3276 0.2515 -0.0034 0.0076  -0.0190 295 GLY A C   
2388  O O   . GLY A 295 ? 0.3158 0.3719 0.2853 -0.0046 0.0040  -0.0199 295 GLY A O   
2389  N N   . SER A 296 ? 0.2652 0.3004 0.2340 -0.0047 0.0113  -0.0155 296 SER A N   
2390  C CA  . SER A 296 ? 0.2487 0.2918 0.2256 -0.0074 0.0120  -0.0122 296 SER A CA  
2391  C C   . SER A 296 ? 0.2470 0.2795 0.2231 -0.0053 0.0160  -0.0090 296 SER A C   
2392  O O   . SER A 296 ? 0.3016 0.3216 0.2742 -0.0051 0.0179  -0.0094 296 SER A O   
2393  C CB  . SER A 296 ? 0.2702 0.3166 0.2556 -0.0168 0.0098  -0.0131 296 SER A CB  
2394  O OG  . SER A 296 ? 0.2958 0.3263 0.2795 -0.0206 0.0107  -0.0148 296 SER A OG  
2395  N N   . LEU A 297 ? 0.2738 0.3125 0.2535 -0.0039 0.0170  -0.0058 297 LEU A N   
2396  C CA  . LEU A 297 ? 0.2750 0.3038 0.2546 -0.0027 0.0196  -0.0035 297 LEU A CA  
2397  C C   . LEU A 297 ? 0.2787 0.2987 0.2621 -0.0091 0.0209  -0.0041 297 LEU A C   
2398  O O   . LEU A 297 ? 0.3018 0.3107 0.2835 -0.0082 0.0229  -0.0035 297 LEU A O   
2399  C CB  . LEU A 297 ? 0.2660 0.3038 0.2479 0.0007  0.0199  -0.0005 297 LEU A CB  
2400  C CG  . LEU A 297 ? 0.3061 0.3335 0.2862 0.0035  0.0215  0.0012  297 LEU A CG  
2401  C CD1 . LEU A 297 ? 0.2999 0.3165 0.2721 0.0091  0.0206  0.0008  297 LEU A CD1 
2402  C CD2 . LEU A 297 ? 0.3376 0.3748 0.3193 0.0074  0.0219  0.0039  297 LEU A CD2 
2403  N N   . TYR A 298 ? 0.2728 0.2974 0.2612 -0.0157 0.0194  -0.0052 298 TYR A N   
2404  C CA  . TYR A 298 ? 0.3060 0.3198 0.2961 -0.0210 0.0201  -0.0059 298 TYR A CA  
2405  C C   . TYR A 298 ? 0.2754 0.2769 0.2591 -0.0193 0.0203  -0.0092 298 TYR A C   
2406  O O   . TYR A 298 ? 0.2999 0.2916 0.2822 -0.0182 0.0227  -0.0086 298 TYR A O   
2407  C CB  . TYR A 298 ? 0.2821 0.3019 0.2782 -0.0289 0.0173  -0.0061 298 TYR A CB  
2408  C CG  . TYR A 298 ? 0.2976 0.3035 0.2932 -0.0345 0.0166  -0.0077 298 TYR A CG  
2409  C CD1 . TYR A 298 ? 0.3537 0.3502 0.3436 -0.0353 0.0136  -0.0128 298 TYR A CD1 
2410  C CD2 . TYR A 298 ? 0.3572 0.3595 0.3569 -0.0382 0.0184  -0.0040 298 TYR A CD2 
2411  C CE1 . TYR A 298 ? 0.3294 0.3113 0.3168 -0.0390 0.0122  -0.0148 298 TYR A CE1 
2412  C CE2 . TYR A 298 ? 0.3430 0.3306 0.3408 -0.0427 0.0172  -0.0054 298 TYR A CE2 
2413  C CZ  . TYR A 298 ? 0.3702 0.3471 0.3615 -0.0428 0.0140  -0.0111 298 TYR A CZ  
2414  O OH  . TYR A 298 ? 0.3951 0.3552 0.3824 -0.0460 0.0121  -0.0130 298 TYR A OH  
2415  N N   . THR A 299 ? 0.2888 0.2920 0.2680 -0.0182 0.0179  -0.0126 299 THR A N   
2416  C CA  . THR A 299 ? 0.2983 0.2920 0.2705 -0.0150 0.0187  -0.0152 299 THR A CA  
2417  C C   . THR A 299 ? 0.2882 0.2792 0.2579 -0.0095 0.0226  -0.0120 299 THR A C   
2418  O O   . THR A 299 ? 0.2906 0.2741 0.2585 -0.0081 0.0251  -0.0115 299 THR A O   
2419  C CB  . THR A 299 ? 0.3258 0.3234 0.2928 -0.0136 0.0151  -0.0192 299 THR A CB  
2420  O OG1 . THR A 299 ? 0.3454 0.3431 0.3154 -0.0203 0.0104  -0.0225 299 THR A OG1 
2421  C CG2 . THR A 299 ? 0.3519 0.3421 0.3101 -0.0082 0.0166  -0.0211 299 THR A CG2 
2422  N N   . PHE A 300 ? 0.2788 0.2757 0.2486 -0.0065 0.0228  -0.0093 300 PHE A N   
2423  C CA  . PHE A 300 ? 0.3019 0.2944 0.2691 -0.0025 0.0253  -0.0060 300 PHE A CA  
2424  C C   . PHE A 300 ? 0.2618 0.2489 0.2336 -0.0038 0.0271  -0.0036 300 PHE A C   
2425  O O   . PHE A 300 ? 0.2891 0.2712 0.2604 -0.0026 0.0291  -0.0012 300 PHE A O   
2426  C CB  . PHE A 300 ? 0.2972 0.2947 0.2619 0.0014  0.0239  -0.0043 300 PHE A CB  
2427  C CG  . PHE A 300 ? 0.3110 0.3139 0.2698 0.0046  0.0222  -0.0060 300 PHE A CG  
2428  C CD1 . PHE A 300 ? 0.2776 0.2808 0.2332 0.0042  0.0216  -0.0092 300 PHE A CD1 
2429  C CD2 . PHE A 300 ? 0.3035 0.3102 0.2584 0.0095  0.0207  -0.0044 300 PHE A CD2 
2430  C CE1 . PHE A 300 ? 0.3017 0.3103 0.2510 0.0082  0.0196  -0.0109 300 PHE A CE1 
2431  C CE2 . PHE A 300 ? 0.2894 0.3014 0.2382 0.0135  0.0191  -0.0057 300 PHE A CE2 
2432  C CZ  . PHE A 300 ? 0.3013 0.3147 0.2476 0.0127  0.0186  -0.0089 300 PHE A CZ  
2433  N N   . ALA A 301 ? 0.2761 0.2655 0.2526 -0.0062 0.0263  -0.0034 301 ALA A N   
2434  C CA  . ALA A 301 ? 0.2974 0.2828 0.2768 -0.0056 0.0272  -0.0011 301 ALA A CA  
2435  C C   . ALA A 301 ? 0.2750 0.2589 0.2586 -0.0088 0.0280  -0.0014 301 ALA A C   
2436  O O   . ALA A 301 ? 0.2857 0.2681 0.2712 -0.0076 0.0282  0.0004  301 ALA A O   
2437  C CB  . ALA A 301 ? 0.3042 0.2932 0.2822 -0.0018 0.0255  0.0004  301 ALA A CB  
2438  N N   . LEU A 302 ? 0.2699 0.2529 0.2540 -0.0126 0.0278  -0.0034 302 LEU A N   
2439  C CA  . LEU A 302 ? 0.2881 0.2659 0.2746 -0.0153 0.0286  -0.0030 302 LEU A CA  
2440  C C   . LEU A 302 ? 0.2888 0.2594 0.2746 -0.0126 0.0305  -0.0026 302 LEU A C   
2441  O O   . LEU A 302 ? 0.3150 0.2827 0.3029 -0.0122 0.0314  -0.0011 302 LEU A O   
2442  C CB  . LEU A 302 ? 0.2978 0.2718 0.2832 -0.0198 0.0270  -0.0057 302 LEU A CB  
2443  C CG  . LEU A 302 ? 0.3311 0.2981 0.3181 -0.0233 0.0273  -0.0047 302 LEU A CG  
2444  C CD1 . LEU A 302 ? 0.3151 0.2903 0.3075 -0.0261 0.0275  -0.0009 302 LEU A CD1 
2445  C CD2 . LEU A 302 ? 0.3579 0.3165 0.3411 -0.0271 0.0244  -0.0086 302 LEU A CD2 
2446  N N   . GLU A 303 ? 0.3122 0.2815 0.2953 -0.0103 0.0314  -0.0034 303 GLU A N   
2447  C CA  . GLU A 303 ? 0.2701 0.2366 0.2541 -0.0079 0.0333  -0.0020 303 GLU A CA  
2448  C C   . GLU A 303 ? 0.2820 0.2516 0.2661 -0.0062 0.0336  0.0004  303 GLU A C   
2449  O O   . GLU A 303 ? 0.2968 0.2661 0.2842 -0.0055 0.0344  0.0028  303 GLU A O   
2450  C CB  . GLU A 303 ? 0.2804 0.2428 0.2610 -0.0063 0.0348  -0.0040 303 GLU A CB  
2451  C CG  . GLU A 303 ? 0.2822 0.2376 0.2609 -0.0082 0.0337  -0.0065 303 GLU A CG  
2452  C CD  . GLU A 303 ? 0.3290 0.2809 0.3106 -0.0080 0.0344  -0.0048 303 GLU A CD  
2453  O OE1 . GLU A 303 ? 0.3456 0.3014 0.3315 -0.0071 0.0349  -0.0023 303 GLU A OE1 
2454  O OE2 . GLU A 303 ? 0.3045 0.2482 0.2828 -0.0085 0.0340  -0.0064 303 GLU A OE2 
2455  N N   . GLY A 304 ? 0.2694 0.2419 0.2501 -0.0056 0.0329  0.0001  304 GLY A N   
2456  C CA  . GLY A 304 ? 0.2419 0.2153 0.2217 -0.0042 0.0332  0.0033  304 GLY A CA  
2457  C C   . GLY A 304 ? 0.2597 0.2307 0.2422 -0.0043 0.0310  0.0055  304 GLY A C   
2458  O O   . GLY A 304 ? 0.2963 0.2676 0.2787 -0.0038 0.0290  0.0042  304 GLY A O   
2459  N N   . ILE A 305 ? 0.2827 0.2516 0.2674 -0.0049 0.0311  0.0090  305 ILE A N   
2460  C CA  . ILE A 305 ? 0.2378 0.2016 0.2242 -0.0051 0.0275  0.0106  305 ILE A CA  
2461  C C   . ILE A 305 ? 0.2723 0.2321 0.2549 -0.0049 0.0258  0.0139  305 ILE A C   
2462  O O   . ILE A 305 ? 0.2806 0.2419 0.2641 -0.0065 0.0282  0.0175  305 ILE A O   
2463  C CB  . ILE A 305 ? 0.2651 0.2287 0.2584 -0.0072 0.0276  0.0120  305 ILE A CB  
2464  C CG1 . ILE A 305 ? 0.3064 0.2718 0.3012 -0.0062 0.0288  0.0088  305 ILE A CG1 
2465  C CG2 . ILE A 305 ? 0.3107 0.2678 0.3054 -0.0079 0.0226  0.0132  305 ILE A CG2 
2466  C CD1 . ILE A 305 ? 0.2852 0.2483 0.2778 -0.0043 0.0260  0.0068  305 ILE A CD1 
2467  N N   . TRP A 306 ? 0.2912 0.2456 0.2688 -0.0023 0.0218  0.0130  306 TRP A N   
2468  C CA  . TRP A 306 ? 0.2708 0.2199 0.2414 -0.0002 0.0199  0.0151  306 TRP A CA  
2469  C C   . TRP A 306 ? 0.2868 0.2239 0.2552 -0.0001 0.0143  0.0167  306 TRP A C   
2470  O O   . TRP A 306 ? 0.3258 0.2594 0.2966 0.0000  0.0110  0.0148  306 TRP A O   
2471  C CB  . TRP A 306 ? 0.3087 0.2623 0.2727 0.0048  0.0194  0.0118  306 TRP A CB  
2472  C CG  . TRP A 306 ? 0.3185 0.2823 0.2839 0.0040  0.0233  0.0098  306 TRP A CG  
2473  C CD1 . TRP A 306 ? 0.2898 0.2595 0.2602 0.0019  0.0252  0.0070  306 TRP A CD1 
2474  C CD2 . TRP A 306 ? 0.2965 0.2636 0.2571 0.0056  0.0249  0.0102  306 TRP A CD2 
2475  N NE1 . TRP A 306 ? 0.2905 0.2659 0.2593 0.0016  0.0271  0.0053  306 TRP A NE1 
2476  C CE2 . TRP A 306 ? 0.3251 0.2999 0.2879 0.0043  0.0270  0.0070  306 TRP A CE2 
2477  C CE3 . TRP A 306 ? 0.3148 0.2780 0.2684 0.0084  0.0242  0.0131  306 TRP A CE3 
2478  C CZ2 . TRP A 306 ? 0.3099 0.2892 0.2680 0.0061  0.0280  0.0058  306 TRP A CZ2 
2479  C CZ3 . TRP A 306 ? 0.2901 0.2590 0.2391 0.0106  0.0261  0.0125  306 TRP A CZ3 
2480  C CH2 . TRP A 306 ? 0.3130 0.2901 0.2643 0.0095  0.0278  0.0086  306 TRP A CH2 
2481  N N   . GLU A 307 ? 0.2872 0.2165 0.2495 0.0005  0.0125  0.0200  307 GLU A N   
2482  C CA  . GLU A 307 ? 0.3563 0.2704 0.3134 0.0014  0.0057  0.0209  307 GLU A CA  
2483  C C   . GLU A 307 ? 0.3481 0.2548 0.2936 0.0061  0.0040  0.0224  307 GLU A C   
2484  O O   . GLU A 307 ? 0.3310 0.2447 0.2744 0.0072  0.0084  0.0239  307 GLU A O   
2485  C CB  . GLU A 307 ? 0.3421 0.2500 0.3068 -0.0065 0.0038  0.0258  307 GLU A CB  
2486  C CG  . GLU A 307 ? 0.3512 0.2568 0.3155 -0.0105 0.0063  0.0330  307 GLU A CG  
2487  C CD  . GLU A 307 ? 0.4086 0.3136 0.3836 -0.0196 0.0058  0.0393  307 GLU A CD  
2488  O OE1 . GLU A 307 ? 0.3923 0.2983 0.3753 -0.0228 0.0029  0.0374  307 GLU A OE1 
2489  O OE2 . GLU A 307 ? 0.4179 0.3226 0.3935 -0.0234 0.0084  0.0466  307 GLU A OE2 
2490  N N   . ASP A 308 ? 0.3443 0.2356 0.2809 0.0100  -0.0029 0.0216  308 ASP A N   
2491  C CA  . ASP A 308 ? 0.3817 0.2613 0.3061 0.0144  -0.0057 0.0240  308 ASP A CA  
2492  C C   . ASP A 308 ? 0.4342 0.3045 0.3610 0.0065  -0.0055 0.0317  308 ASP A C   
2493  O O   . ASP A 308 ? 0.3783 0.2395 0.3109 -0.0004 -0.0093 0.0344  308 ASP A O   
2494  C CB  . ASP A 308 ? 0.3920 0.2553 0.3044 0.0219  -0.0141 0.0204  308 ASP A CB  
2495  C CG  . ASP A 308 ? 0.4975 0.3723 0.4068 0.0309  -0.0138 0.0140  308 ASP A CG  
2496  O OD1 . ASP A 308 ? 0.4533 0.3464 0.3668 0.0320  -0.0077 0.0129  308 ASP A OD1 
2497  O OD2 . ASP A 308 ? 0.5181 0.3843 0.4213 0.0366  -0.0197 0.0103  308 ASP A OD2 
2498  N N   . LYS A 309 ? 0.3916 0.2647 0.3141 0.0077  -0.0013 0.0357  309 LYS A N   
2499  C CA  . LYS A 309 ? 0.3845 0.2512 0.3087 0.0009  0.0002  0.0446  309 LYS A CA  
2500  C C   . LYS A 309 ? 0.4319 0.2749 0.3434 0.0028  -0.0070 0.0477  309 LYS A C   
2501  O O   . LYS A 309 ? 0.4593 0.2916 0.3588 0.0114  -0.0127 0.0424  309 LYS A O   
2502  C CB  . LYS A 309 ? 0.4175 0.2984 0.3410 0.0028  0.0081  0.0473  309 LYS A CB  
2503  C CG  . LYS A 309 ? 0.3935 0.2948 0.3286 0.0005  0.0145  0.0446  309 LYS A CG  
2504  C CD  . LYS A 309 ? 0.4358 0.3401 0.3844 -0.0093 0.0163  0.0502  309 LYS A CD  
2505  C CE  . LYS A 309 ? 0.4197 0.3427 0.3782 -0.0105 0.0225  0.0478  309 LYS A CE  
2506  N NZ  . LYS A 309 ? 0.3864 0.3141 0.3577 -0.0187 0.0240  0.0534  309 LYS A NZ  
2507  N N   . PRO A 310 ? 0.4676 0.3015 0.3802 -0.0044 -0.0066 0.0570  310 PRO A N   
2508  C CA  . PRO A 310 ? 0.4769 0.2843 0.3768 -0.0037 -0.0144 0.0609  310 PRO A CA  
2509  C C   . PRO A 310 ? 0.4919 0.2911 0.3728 0.0087  -0.0156 0.0587  310 PRO A C   
2510  O O   . PRO A 310 ? 0.5031 0.2779 0.3699 0.0130  -0.0239 0.0585  310 PRO A O   
2511  C CB  . PRO A 310 ? 0.4994 0.3047 0.4070 -0.0152 -0.0113 0.0731  310 PRO A CB  
2512  C CG  . PRO A 310 ? 0.4834 0.3093 0.4104 -0.0234 -0.0064 0.0735  310 PRO A CG  
2513  C CD  . PRO A 310 ? 0.4469 0.2929 0.3747 -0.0151 -0.0008 0.0647  310 PRO A CD  
2514  N N   . ASP A 311 ? 0.4394 0.2572 0.3187 0.0151  -0.0083 0.0571  311 ASP A N   
2515  C CA  . ASP A 311 ? 0.4575 0.2717 0.3200 0.0277  -0.0094 0.0543  311 ASP A CA  
2516  C C   . ASP A 311 ? 0.4278 0.2520 0.2871 0.0376  -0.0115 0.0438  311 ASP A C   
2517  O O   . ASP A 311 ? 0.4656 0.2940 0.3136 0.0486  -0.0115 0.0408  311 ASP A O   
2518  C CB  . ASP A 311 ? 0.4630 0.2914 0.3242 0.0298  -0.0016 0.0583  311 ASP A CB  
2519  C CG  . ASP A 311 ? 0.4295 0.2853 0.3024 0.0295  0.0051  0.0531  311 ASP A CG  
2520  O OD1 . ASP A 311 ? 0.4371 0.2996 0.3213 0.0249  0.0048  0.0488  311 ASP A OD1 
2521  O OD2 . ASP A 311 ? 0.5204 0.3888 0.3904 0.0336  0.0103  0.0538  311 ASP A OD2 
2522  N N   . GLY A 312 ? 0.4500 0.2788 0.3187 0.0345  -0.0132 0.0389  312 GLY A N   
2523  C CA  . GLY A 312 ? 0.4076 0.2481 0.2747 0.0431  -0.0143 0.0304  312 GLY A CA  
2524  C C   . GLY A 312 ? 0.4395 0.3069 0.3172 0.0424  -0.0070 0.0273  312 GLY A C   
2525  O O   . GLY A 312 ? 0.4326 0.3119 0.3118 0.0475  -0.0073 0.0214  312 GLY A O   
2526  N N   . SER A 313 ? 0.3778 0.2547 0.2624 0.0364  -0.0008 0.0313  313 SER A N   
2527  C CA  . SER A 313 ? 0.4033 0.3030 0.2962 0.0359  0.0051  0.0278  313 SER A CA  
2528  C C   . SER A 313 ? 0.4061 0.3140 0.3134 0.0282  0.0072  0.0259  313 SER A C   
2529  O O   . SER A 313 ? 0.3432 0.2416 0.2559 0.0221  0.0054  0.0283  313 SER A O   
2530  C CB  . SER A 313 ? 0.4003 0.3061 0.2923 0.0346  0.0103  0.0322  313 SER A CB  
2531  O OG  . SER A 313 ? 0.4077 0.3093 0.3073 0.0257  0.0132  0.0385  313 SER A OG  
2532  N N   . TRP A 314 ? 0.3455 0.2713 0.2593 0.0280  0.0111  0.0218  314 TRP A N   
2533  C CA  . TRP A 314 ? 0.3641 0.2974 0.2901 0.0219  0.0133  0.0197  314 TRP A CA  
2534  C C   . TRP A 314 ? 0.3218 0.2603 0.2544 0.0159  0.0185  0.0230  314 TRP A C   
2535  O O   . TRP A 314 ? 0.3731 0.3178 0.3017 0.0181  0.0214  0.0237  314 TRP A O   
2536  C CB  . TRP A 314 ? 0.3727 0.3209 0.3017 0.0244  0.0141  0.0141  314 TRP A CB  
2537  C CG  . TRP A 314 ? 0.3184 0.2685 0.2549 0.0218  0.0135  0.0117  314 TRP A CG  
2538  C CD1 . TRP A 314 ? 0.3447 0.2839 0.2824 0.0204  0.0104  0.0125  314 TRP A CD1 
2539  C CD2 . TRP A 314 ? 0.3497 0.3131 0.2929 0.0206  0.0153  0.0081  314 TRP A CD2 
2540  N NE1 . TRP A 314 ? 0.3290 0.2746 0.2725 0.0199  0.0106  0.0095  314 TRP A NE1 
2541  C CE2 . TRP A 314 ? 0.3658 0.3260 0.3132 0.0194  0.0141  0.0074  314 TRP A CE2 
2542  C CE3 . TRP A 314 ? 0.3771 0.3539 0.3230 0.0198  0.0175  0.0057  314 TRP A CE3 
2543  C CZ2 . TRP A 314 ? 0.3653 0.3351 0.3190 0.0177  0.0157  0.0053  314 TRP A CZ2 
2544  C CZ3 . TRP A 314 ? 0.3510 0.3367 0.3042 0.0168  0.0185  0.0035  314 TRP A CZ3 
2545  C CH2 . TRP A 314 ? 0.3717 0.3539 0.3286 0.0159  0.0181  0.0037  314 TRP A CH2 
2546  N N   . GLY A 315 ? 0.3414 0.2770 0.2825 0.0094  0.0194  0.0255  315 GLY A N   
2547  C CA  . GLY A 315 ? 0.3582 0.3009 0.3058 0.0050  0.0247  0.0288  315 GLY A CA  
2548  C C   . GLY A 315 ? 0.3072 0.2534 0.2658 -0.0002 0.0257  0.0279  315 GLY A C   
2549  O O   . GLY A 315 ? 0.3088 0.2517 0.2700 -0.0005 0.0222  0.0247  315 GLY A O   
2550  N N   . GLY A 316 ? 0.3237 0.2778 0.2878 -0.0027 0.0305  0.0306  316 GLY A N   
2551  C CA  . GLY A 316 ? 0.3445 0.3028 0.3187 -0.0067 0.0316  0.0303  316 GLY A CA  
2552  C C   . GLY A 316 ? 0.3302 0.2807 0.3102 -0.0116 0.0275  0.0335  316 GLY A C   
2553  O O   . GLY A 316 ? 0.3142 0.2574 0.2932 -0.0144 0.0256  0.0393  316 GLY A O   
2554  N N   . ARG A 317 ? 0.3151 0.2662 0.3008 -0.0127 0.0255  0.0298  317 ARG A N   
2555  C CA  . ARG A 317 ? 0.3123 0.2557 0.3030 -0.0167 0.0202  0.0313  317 ARG A CA  
2556  C C   . ARG A 317 ? 0.3308 0.2791 0.3308 -0.0230 0.0220  0.0385  317 ARG A C   
2557  O O   . ARG A 317 ? 0.3278 0.2886 0.3324 -0.0229 0.0280  0.0404  317 ARG A O   
2558  C CB  . ARG A 317 ? 0.3323 0.2773 0.3265 -0.0154 0.0183  0.0258  317 ARG A CB  
2559  C CG  . ARG A 317 ? 0.2959 0.2322 0.2937 -0.0185 0.0115  0.0263  317 ARG A CG  
2560  C CD  . ARG A 317 ? 0.3334 0.2700 0.3317 -0.0151 0.0092  0.0206  317 ARG A CD  
2561  N NE  . ARG A 317 ? 0.3502 0.2793 0.3523 -0.0180 0.0023  0.0209  317 ARG A NE  
2562  C CZ  . ARG A 317 ? 0.3583 0.2837 0.3587 -0.0145 -0.0021 0.0162  317 ARG A CZ  
2563  N NH1 . ARG A 317 ? 0.3407 0.2700 0.3363 -0.0084 0.0005  0.0120  317 ARG A NH1 
2564  N NH2 . ARG A 317 ? 0.3598 0.2773 0.3631 -0.0173 -0.0096 0.0162  317 ARG A NH2 
2565  N N   . THR A 318 ? 0.3272 0.2658 0.3294 -0.0282 0.0168  0.0429  318 THR A N   
2566  C CA  . THR A 318 ? 0.3206 0.2655 0.3334 -0.0357 0.0183  0.0514  318 THR A CA  
2567  C C   . THR A 318 ? 0.3247 0.2813 0.3498 -0.0382 0.0189  0.0504  318 THR A C   
2568  O O   . THR A 318 ? 0.3238 0.2751 0.3499 -0.0376 0.0135  0.0449  318 THR A O   
2569  C CB  . THR A 318 ? 0.3728 0.3020 0.3850 -0.0421 0.0112  0.0566  318 THR A CB  
2570  O OG1 . THR A 318 ? 0.3772 0.2968 0.3776 -0.0392 0.0118  0.0592  318 THR A OG1 
2571  C CG2 . THR A 318 ? 0.3576 0.2952 0.3832 -0.0517 0.0125  0.0667  318 THR A CG2 
2572  N N   . LEU A 319 ? 0.3267 0.2997 0.3602 -0.0401 0.0252  0.0560  319 LEU A N   
2573  C CA  . LEU A 319 ? 0.3534 0.3396 0.3987 -0.0417 0.0261  0.0559  319 LEU A CA  
2574  C C   . LEU A 319 ? 0.3635 0.3458 0.4193 -0.0506 0.0186  0.0596  319 LEU A C   
2575  O O   . LEU A 319 ? 0.3573 0.3334 0.4154 -0.0576 0.0157  0.0666  319 LEU A O   
2576  C CB  . LEU A 319 ? 0.3323 0.3379 0.3827 -0.0400 0.0349  0.0615  319 LEU A CB  
2577  C CG  . LEU A 319 ? 0.2907 0.2979 0.3292 -0.0315 0.0411  0.0580  319 LEU A CG  
2578  C CD1 . LEU A 319 ? 0.3252 0.3498 0.3672 -0.0296 0.0488  0.0650  319 LEU A CD1 
2579  C CD2 . LEU A 319 ? 0.3346 0.3409 0.3691 -0.0253 0.0410  0.0486  319 LEU A CD2 
2580  N N   . PRO A 320 ? 0.3383 0.3223 0.3998 -0.0505 0.0143  0.0548  320 PRO A N   
2581  C CA  . PRO A 320 ? 0.3909 0.3681 0.4607 -0.0586 0.0049  0.0565  320 PRO A CA  
2582  C C   . PRO A 320 ? 0.4037 0.3937 0.4885 -0.0686 0.0057  0.0674  320 PRO A C   
2583  O O   . PRO A 320 ? 0.3809 0.3601 0.4696 -0.0776 -0.0018 0.0718  320 PRO A O   
2584  C CB  . PRO A 320 ? 0.4168 0.3982 0.4897 -0.0546 0.0019  0.0493  320 PRO A CB  
2585  C CG  . PRO A 320 ? 0.3551 0.3372 0.4170 -0.0441 0.0081  0.0424  320 PRO A CG  
2586  C CD  . PRO A 320 ? 0.3141 0.3022 0.3719 -0.0424 0.0166  0.0467  320 PRO A CD  
2587  N N   . TRP A 321 ? 0.3531 0.3656 0.4458 -0.0672 0.0146  0.0725  321 TRP A N   
2588  C CA  . TRP A 321 ? 0.3481 0.3766 0.4560 -0.0765 0.0165  0.0844  321 TRP A CA  
2589  C C   . TRP A 321 ? 0.3664 0.3877 0.4703 -0.0814 0.0186  0.0932  321 TRP A C   
2590  O O   . TRP A 321 ? 0.4365 0.4669 0.5532 -0.0916 0.0184  0.1044  321 TRP A O   
2591  C CB  . TRP A 321 ? 0.3643 0.4210 0.4808 -0.0717 0.0259  0.0879  321 TRP A CB  
2592  C CG  . TRP A 321 ? 0.3403 0.4009 0.4438 -0.0600 0.0356  0.0849  321 TRP A CG  
2593  C CD1 . TRP A 321 ? 0.3713 0.4396 0.4709 -0.0579 0.0435  0.0919  321 TRP A CD1 
2594  C CD2 . TRP A 321 ? 0.3043 0.3605 0.3968 -0.0493 0.0374  0.0742  321 TRP A CD2 
2595  N NE1 . TRP A 321 ? 0.3451 0.4135 0.4315 -0.0460 0.0494  0.0850  321 TRP A NE1 
2596  C CE2 . TRP A 321 ? 0.2762 0.3368 0.3587 -0.0414 0.0456  0.0745  321 TRP A CE2 
2597  C CE3 . TRP A 321 ? 0.3233 0.3718 0.4132 -0.0456 0.0326  0.0648  321 TRP A CE3 
2598  C CZ2 . TRP A 321 ? 0.2855 0.3417 0.3560 -0.0313 0.0483  0.0654  321 TRP A CZ2 
2599  C CZ3 . TRP A 321 ? 0.3041 0.3490 0.3826 -0.0357 0.0362  0.0569  321 TRP A CZ3 
2600  C CH2 . TRP A 321 ? 0.3177 0.3658 0.3870 -0.0293 0.0435  0.0571  321 TRP A CH2 
2601  N N   . ASP A 322 ? 0.3544 0.3596 0.4414 -0.0751 0.0201  0.0890  322 ASP A N   
2602  C CA  . ASP A 322 ? 0.4216 0.4159 0.5023 -0.0789 0.0207  0.0967  322 ASP A CA  
2603  C C   . ASP A 322 ? 0.4479 0.4154 0.5234 -0.0851 0.0094  0.0953  322 ASP A C   
2604  O O   . ASP A 322 ? 0.4690 0.4236 0.5378 -0.0882 0.0085  0.1014  322 ASP A O   
2605  C CB  . ASP A 322 ? 0.4024 0.3931 0.4667 -0.0682 0.0274  0.0928  322 ASP A CB  
2606  C CG  . ASP A 322 ? 0.4237 0.4377 0.4901 -0.0621 0.0385  0.0962  322 ASP A CG  
2607  O OD1 . ASP A 322 ? 0.5004 0.5335 0.5805 -0.0672 0.0423  0.1054  322 ASP A OD1 
2608  O OD2 . ASP A 322 ? 0.4157 0.4294 0.4702 -0.0522 0.0429  0.0899  322 ASP A OD2 
2609  N N   . LYS A 323 ? 0.4027 0.3612 0.4795 -0.0854 0.0006  0.0871  323 LYS A N   
2610  C CA  . LYS A 323 ? 0.4491 0.3815 0.5191 -0.0885 -0.0117 0.0827  323 LYS A CA  
2611  C C   . LYS A 323 ? 0.4512 0.3852 0.5366 -0.0996 -0.0205 0.0854  323 LYS A C   
2612  O O   . LYS A 323 ? 0.4916 0.4058 0.5720 -0.1005 -0.0320 0.0790  323 LYS A O   
2613  C CB  . LYS A 323 ? 0.5223 0.4447 0.5797 -0.0773 -0.0148 0.0692  323 LYS A CB  
2614  C CG  . LYS A 323 ? 0.5488 0.4642 0.5896 -0.0667 -0.0104 0.0640  323 LYS A CG  
2615  C CD  . LYS A 323 ? 0.5465 0.4418 0.5747 -0.0605 -0.0193 0.0545  323 LYS A CD  
2616  C CE  . LYS A 323 ? 0.5500 0.4536 0.5753 -0.0513 -0.0165 0.0453  323 LYS A CE  
2617  N NZ  . LYS A 323 ? 0.5306 0.4216 0.5390 -0.0411 -0.0182 0.0382  323 LYS A NZ  
2618  N N   . GLY A 324 ? 0.3917 0.3512 0.4954 -0.1060 -0.0154 0.0931  324 GLY A N   
2619  C CA  . GLY A 324 ? 0.4206 0.3865 0.5415 -0.1168 -0.0237 0.0958  324 GLY A CA  
2620  C C   . GLY A 324 ? 0.4316 0.4014 0.5547 -0.1113 -0.0286 0.0850  324 GLY A C   
2621  O O   . GLY A 324 ? 0.4686 0.4378 0.6029 -0.1197 -0.0386 0.0851  324 GLY A O   
2622  N N   . ILE A 325 ? 0.4059 0.3799 0.5189 -0.0980 -0.0224 0.0761  325 ILE A N   
2623  C CA  . ILE A 325 ? 0.4228 0.3992 0.5358 -0.0916 -0.0265 0.0661  325 ILE A CA  
2624  C C   . ILE A 325 ? 0.4562 0.4624 0.5819 -0.0890 -0.0178 0.0687  325 ILE A C   
2625  O O   . ILE A 325 ? 0.4347 0.4514 0.5554 -0.0813 -0.0069 0.0691  325 ILE A O   
2626  C CB  . ILE A 325 ? 0.4208 0.3815 0.5142 -0.0787 -0.0258 0.0553  325 ILE A CB  
2627  C CG1 . ILE A 325 ? 0.4670 0.3992 0.5467 -0.0793 -0.0346 0.0525  325 ILE A CG1 
2628  C CG2 . ILE A 325 ? 0.3933 0.3576 0.4860 -0.0714 -0.0287 0.0462  325 ILE A CG2 
2629  C CD1 . ILE A 325 ? 0.5084 0.4293 0.5692 -0.0668 -0.0314 0.0447  325 ILE A CD1 
2630  N N   . GLU A 326 ? 0.4428 0.4624 0.5838 -0.0944 -0.0231 0.0698  326 GLU A N   
2631  C CA  . GLU A 326 ? 0.4569 0.5062 0.6100 -0.0911 -0.0151 0.0729  326 GLU A CA  
2632  C C   . GLU A 326 ? 0.4339 0.4832 0.5777 -0.0780 -0.0133 0.0621  326 GLU A C   
2633  O O   . GLU A 326 ? 0.4041 0.4345 0.5376 -0.0740 -0.0206 0.0532  326 GLU A O   
2634  C CB  . GLU A 326 ? 0.5201 0.5876 0.6952 -0.1025 -0.0210 0.0798  326 GLU A CB  
2635  C CG  . GLU A 326 ? 0.5655 0.6459 0.7542 -0.1147 -0.0175 0.0943  326 GLU A CG  
2636  C CD  . GLU A 326 ? 0.6571 0.7647 0.8706 -0.1251 -0.0206 0.1026  326 GLU A CD  
2637  O OE1 . GLU A 326 ? 0.6970 0.8065 0.9165 -0.1253 -0.0294 0.0962  326 GLU A OE1 
2638  O OE2 . GLU A 326 ? 0.6939 0.8220 0.9212 -0.1331 -0.0145 0.1159  326 GLU A OE2 
2639  N N   . ILE A 327 ? 0.4116 0.4809 0.5573 -0.0703 -0.0033 0.0631  327 ILE A N   
2640  C CA  . ILE A 327 ? 0.3283 0.3978 0.4653 -0.0580 -0.0011 0.0541  327 ILE A CA  
2641  C C   . ILE A 327 ? 0.3500 0.4470 0.5005 -0.0557 0.0023  0.0574  327 ILE A C   
2642  O O   . ILE A 327 ? 0.3962 0.5084 0.5461 -0.0493 0.0121  0.0603  327 ILE A O   
2643  C CB  . ILE A 327 ? 0.3852 0.4462 0.5056 -0.0483 0.0075  0.0502  327 ILE A CB  
2644  C CG1 . ILE A 327 ? 0.4208 0.4611 0.5301 -0.0510 0.0061  0.0497  327 ILE A CG1 
2645  C CG2 . ILE A 327 ? 0.3393 0.3940 0.4497 -0.0379 0.0074  0.0410  327 ILE A CG2 
2646  C CD1 . ILE A 327 ? 0.4564 0.4880 0.5495 -0.0416 0.0130  0.0446  327 ILE A CD1 
2647  N N   . ASN A 328 ? 0.3481 0.4513 0.5097 -0.0597 -0.0061 0.0563  328 ASN A N   
2648  C CA  . ASN A 328 ? 0.3571 0.4897 0.5348 -0.0594 -0.0040 0.0611  328 ASN A CA  
2649  C C   . ASN A 328 ? 0.3569 0.4927 0.5322 -0.0500 -0.0071 0.0532  328 ASN A C   
2650  O O   . ASN A 328 ? 0.3814 0.5421 0.5704 -0.0491 -0.0070 0.0563  328 ASN A O   
2651  C CB  . ASN A 328 ? 0.3717 0.5167 0.5701 -0.0747 -0.0113 0.0696  328 ASN A CB  
2652  C CG  . ASN A 328 ? 0.4875 0.6354 0.6907 -0.0838 -0.0062 0.0803  328 ASN A CG  
2653  O OD1 . ASN A 328 ? 0.5195 0.6618 0.7321 -0.0975 -0.0136 0.0859  328 ASN A OD1 
2654  N ND2 . ASN A 328 ? 0.5280 0.6858 0.7249 -0.0759 0.0062  0.0837  328 ASN A ND2 
2655  N N   . ASP A 329 ? 0.3145 0.4272 0.4735 -0.0432 -0.0103 0.0438  329 ASP A N   
2656  C CA  . ASP A 329 ? 0.2794 0.3931 0.4349 -0.0341 -0.0138 0.0367  329 ASP A CA  
2657  C C   . ASP A 329 ? 0.2813 0.3725 0.4158 -0.0241 -0.0111 0.0289  329 ASP A C   
2658  O O   . ASP A 329 ? 0.2907 0.3639 0.4148 -0.0258 -0.0096 0.0279  329 ASP A O   
2659  C CB  . ASP A 329 ? 0.3466 0.4590 0.5113 -0.0406 -0.0271 0.0342  329 ASP A CB  
2660  C CG  . ASP A 329 ? 0.3946 0.4783 0.5491 -0.0453 -0.0357 0.0296  329 ASP A CG  
2661  O OD1 . ASP A 329 ? 0.4806 0.5584 0.6408 -0.0568 -0.0392 0.0345  329 ASP A OD1 
2662  O OD2 . ASP A 329 ? 0.3990 0.4657 0.5385 -0.0368 -0.0383 0.0216  329 ASP A OD2 
2663  N N   . ARG A 330 ? 0.2748 0.3688 0.4039 -0.0136 -0.0103 0.0240  330 ARG A N   
2664  C CA  . ARG A 330 ? 0.2809 0.3567 0.3914 -0.0038 -0.0069 0.0178  330 ARG A CA  
2665  C C   . ARG A 330 ? 0.2863 0.3396 0.3872 -0.0060 -0.0135 0.0133  330 ARG A C   
2666  O O   . ARG A 330 ? 0.2619 0.3005 0.3504 -0.0040 -0.0093 0.0117  330 ARG A O   
2667  C CB  . ARG A 330 ? 0.2620 0.3441 0.3692 0.0072  -0.0068 0.0142  330 ARG A CB  
2668  C CG  . ARG A 330 ? 0.2999 0.3639 0.3885 0.0165  -0.0027 0.0094  330 ARG A CG  
2669  C CD  . ARG A 330 ? 0.3024 0.3690 0.3865 0.0271  -0.0043 0.0058  330 ARG A CD  
2670  N NE  . ARG A 330 ? 0.3052 0.3895 0.3939 0.0333  0.0007  0.0082  330 ARG A NE  
2671  C CZ  . ARG A 330 ? 0.3379 0.4239 0.4197 0.0446  0.0020  0.0058  330 ARG A CZ  
2672  N NH1 . ARG A 330 ? 0.2791 0.3498 0.3489 0.0507  -0.0007 0.0015  330 ARG A NH1 
2673  N NH2 . ARG A 330 ? 0.3272 0.4313 0.4139 0.0506  0.0059  0.0081  330 ARG A NH2 
2674  N N   . ASP A 331 ? 0.3065 0.3572 0.4121 -0.0092 -0.0243 0.0106  331 ASP A N   
2675  C CA  . ASP A 331 ? 0.2867 0.3157 0.3801 -0.0079 -0.0307 0.0053  331 ASP A CA  
2676  C C   . ASP A 331 ? 0.3025 0.3190 0.3928 -0.0151 -0.0304 0.0076  331 ASP A C   
2677  O O   . ASP A 331 ? 0.3088 0.3097 0.3852 -0.0110 -0.0286 0.0046  331 ASP A O   
2678  C CB  . ASP A 331 ? 0.3737 0.4014 0.4719 -0.0095 -0.0435 0.0016  331 ASP A CB  
2679  C CG  . ASP A 331 ? 0.4129 0.4498 0.5103 0.0001  -0.0445 -0.0020 331 ASP A CG  
2680  O OD1 . ASP A 331 ? 0.3634 0.4057 0.4556 0.0080  -0.0353 -0.0013 331 ASP A OD1 
2681  O OD2 . ASP A 331 ? 0.4707 0.5100 0.5733 -0.0006 -0.0552 -0.0051 331 ASP A OD2 
2682  N N   . THR A 332 ? 0.2868 0.3113 0.3899 -0.0257 -0.0314 0.0136  332 THR A N   
2683  C CA  . THR A 332 ? 0.2936 0.3068 0.3935 -0.0323 -0.0304 0.0168  332 THR A CA  
2684  C C   . THR A 332 ? 0.2673 0.2793 0.3578 -0.0274 -0.0189 0.0179  332 THR A C   
2685  O O   . THR A 332 ? 0.2729 0.2697 0.3519 -0.0260 -0.0180 0.0160  332 THR A O   
2686  C CB  . THR A 332 ? 0.3132 0.3376 0.4298 -0.0450 -0.0327 0.0247  332 THR A CB  
2687  O OG1 . THR A 332 ? 0.3233 0.3498 0.4505 -0.0510 -0.0446 0.0238  332 THR A OG1 
2688  C CG2 . THR A 332 ? 0.3235 0.3330 0.4354 -0.0515 -0.0335 0.0279  332 THR A CG2 
2689  N N   . ALA A 333 ? 0.2620 0.2902 0.3569 -0.0239 -0.0103 0.0205  333 ALA A N   
2690  C CA  . ALA A 333 ? 0.2768 0.3033 0.3623 -0.0188 -0.0004 0.0208  333 ALA A CA  
2691  C C   . ALA A 333 ? 0.2457 0.2569 0.3160 -0.0111 0.0001  0.0145  333 ALA A C   
2692  O O   . ALA A 333 ? 0.2670 0.2685 0.3282 -0.0105 0.0036  0.0139  333 ALA A O   
2693  C CB  . ALA A 333 ? 0.2581 0.3029 0.3488 -0.0142 0.0069  0.0234  333 ALA A CB  
2694  N N   . VAL A 334 ? 0.2644 0.2740 0.3322 -0.0053 -0.0037 0.0103  334 VAL A N   
2695  C CA  . VAL A 334 ? 0.2519 0.2492 0.3059 0.0020  -0.0023 0.0058  334 VAL A CA  
2696  C C   . VAL A 334 ? 0.2834 0.2665 0.3300 0.0002  -0.0064 0.0040  334 VAL A C   
2697  O O   . VAL A 334 ? 0.2940 0.2700 0.3315 0.0024  -0.0021 0.0034  334 VAL A O   
2698  C CB  . VAL A 334 ? 0.2585 0.2575 0.3107 0.0092  -0.0055 0.0024  334 VAL A CB  
2699  C CG1 . VAL A 334 ? 0.2731 0.2586 0.3113 0.0162  -0.0062 -0.0014 334 VAL A CG1 
2700  C CG2 . VAL A 334 ? 0.2228 0.2340 0.2783 0.0137  0.0006  0.0040  334 VAL A CG2 
2701  N N   . ARG A 335 ? 0.2939 0.2727 0.3442 -0.0039 -0.0155 0.0033  335 ARG A N   
2702  C CA  . ARG A 335 ? 0.3022 0.2660 0.3432 -0.0035 -0.0202 0.0009  335 ARG A CA  
2703  C C   . ARG A 335 ? 0.3057 0.2662 0.3449 -0.0080 -0.0157 0.0042  335 ARG A C   
2704  O O   . ARG A 335 ? 0.2954 0.2478 0.3241 -0.0042 -0.0138 0.0025  335 ARG A O   
2705  C CB  . ARG A 335 ? 0.3370 0.2942 0.3808 -0.0066 -0.0320 -0.0012 335 ARG A CB  
2706  C CG  . ARG A 335 ? 0.3095 0.2499 0.3392 -0.0009 -0.0381 -0.0058 335 ARG A CG  
2707  C CD  . ARG A 335 ? 0.3673 0.2977 0.3980 -0.0036 -0.0516 -0.0089 335 ARG A CD  
2708  N NE  . ARG A 335 ? 0.3524 0.2668 0.3670 0.0049  -0.0578 -0.0143 335 ARG A NE  
2709  C CZ  . ARG A 335 ? 0.3554 0.2683 0.3594 0.0163  -0.0584 -0.0189 335 ARG A CZ  
2710  N NH1 . ARG A 335 ? 0.3429 0.2675 0.3501 0.0204  -0.0538 -0.0190 335 ARG A NH1 
2711  N NH2 . ARG A 335 ? 0.4021 0.3008 0.3912 0.0243  -0.0647 -0.0234 335 ARG A NH2 
2712  N N   . LEU A 336 ? 0.2878 0.2565 0.3373 -0.0157 -0.0135 0.0094  336 LEU A N   
2713  C CA  . LEU A 336 ? 0.2933 0.2596 0.3405 -0.0192 -0.0088 0.0129  336 LEU A CA  
2714  C C   . LEU A 336 ? 0.2884 0.2572 0.3285 -0.0140 0.0001  0.0119  336 LEU A C   
2715  O O   . LEU A 336 ? 0.2871 0.2492 0.3195 -0.0132 0.0020  0.0117  336 LEU A O   
2716  C CB  . LEU A 336 ? 0.3153 0.2922 0.3746 -0.0274 -0.0068 0.0197  336 LEU A CB  
2717  C CG  . LEU A 336 ? 0.3869 0.3587 0.4533 -0.0356 -0.0159 0.0223  336 LEU A CG  
2718  C CD1 . LEU A 336 ? 0.4008 0.3902 0.4836 -0.0438 -0.0135 0.0301  336 LEU A CD1 
2719  C CD2 . LEU A 336 ? 0.3833 0.3386 0.4406 -0.0375 -0.0188 0.0228  336 LEU A CD2 
2720  N N   . TYR A 337 ? 0.2534 0.2309 0.2955 -0.0102 0.0047  0.0112  337 TYR A N   
2721  C CA  . TYR A 337 ? 0.2758 0.2536 0.3109 -0.0058 0.0120  0.0101  337 TYR A CA  
2722  C C   . TYR A 337 ? 0.3126 0.2806 0.3373 -0.0014 0.0110  0.0065  337 TYR A C   
2723  O O   . TYR A 337 ? 0.2812 0.2461 0.3000 -0.0011 0.0145  0.0064  337 TYR A O   
2724  C CB  . TYR A 337 ? 0.2627 0.2492 0.3009 -0.0021 0.0156  0.0100  337 TYR A CB  
2725  C CG  . TYR A 337 ? 0.2765 0.2618 0.3077 0.0017  0.0224  0.0091  337 TYR A CG  
2726  C CD1 . TYR A 337 ? 0.2930 0.2782 0.3215 -0.0003 0.0264  0.0104  337 TYR A CD1 
2727  C CD2 . TYR A 337 ? 0.2702 0.2539 0.2972 0.0072  0.0240  0.0069  337 TYR A CD2 
2728  C CE1 . TYR A 337 ? 0.3241 0.3070 0.3460 0.0028  0.0311  0.0089  337 TYR A CE1 
2729  C CE2 . TYR A 337 ? 0.2766 0.2563 0.2966 0.0100  0.0289  0.0059  337 TYR A CE2 
2730  C CZ  . TYR A 337 ? 0.2953 0.2746 0.3129 0.0076  0.0321  0.0066  337 TYR A CZ  
2731  O OH  . TYR A 337 ? 0.2991 0.2731 0.3092 0.0103  0.0356  0.0049  337 TYR A OH  
2732  N N   . ALA A 338 ? 0.2874 0.2516 0.3100 0.0023  0.0060  0.0039  338 ALA A N   
2733  C CA  . ALA A 338 ? 0.2993 0.2562 0.3121 0.0073  0.0050  0.0014  338 ALA A CA  
2734  C C   . ALA A 338 ? 0.3337 0.2845 0.3418 0.0059  0.0028  0.0014  338 ALA A C   
2735  O O   . ALA A 338 ? 0.2806 0.2305 0.2826 0.0079  0.0062  0.0013  338 ALA A O   
2736  C CB  . ALA A 338 ? 0.3137 0.2679 0.3242 0.0125  -0.0009 -0.0014 338 ALA A CB  
2737  N N   . ASP A 339 ? 0.3055 0.2520 0.3165 0.0022  -0.0031 0.0019  339 ASP A N   
2738  C CA  . ASP A 339 ? 0.3541 0.2925 0.3591 0.0017  -0.0059 0.0020  339 ASP A CA  
2739  C C   . ASP A 339 ? 0.3219 0.2641 0.3265 -0.0010 0.0007  0.0046  339 ASP A C   
2740  O O   . ASP A 339 ? 0.3233 0.2625 0.3202 0.0020  0.0014  0.0038  339 ASP A O   
2741  C CB  . ASP A 339 ? 0.2974 0.2286 0.3061 -0.0033 -0.0137 0.0029  339 ASP A CB  
2742  C CG  . ASP A 339 ? 0.4120 0.3336 0.4141 -0.0043 -0.0160 0.0039  339 ASP A CG  
2743  O OD1 . ASP A 339 ? 0.3604 0.2725 0.3519 0.0019  -0.0206 0.0007  339 ASP A OD1 
2744  O OD2 . ASP A 339 ? 0.3794 0.3031 0.3859 -0.0102 -0.0130 0.0082  339 ASP A OD2 
2745  N N   . TRP A 340 ? 0.2723 0.2222 0.2845 -0.0057 0.0054  0.0076  340 TRP A N   
2746  C CA  . TRP A 340 ? 0.3006 0.2541 0.3115 -0.0074 0.0112  0.0096  340 TRP A CA  
2747  C C   . TRP A 340 ? 0.2676 0.2224 0.2724 -0.0034 0.0151  0.0072  340 TRP A C   
2748  O O   . TRP A 340 ? 0.2735 0.2267 0.2727 -0.0024 0.0158  0.0069  340 TRP A O   
2749  C CB  . TRP A 340 ? 0.2857 0.2484 0.3045 -0.0107 0.0157  0.0127  340 TRP A CB  
2750  C CG  . TRP A 340 ? 0.2656 0.2318 0.2830 -0.0122 0.0207  0.0152  340 TRP A CG  
2751  C CD1 . TRP A 340 ? 0.2886 0.2581 0.3021 -0.0099 0.0259  0.0137  340 TRP A CD1 
2752  C CD2 . TRP A 340 ? 0.2645 0.2307 0.2837 -0.0163 0.0205  0.0197  340 TRP A CD2 
2753  N NE1 . TRP A 340 ? 0.2896 0.2621 0.3020 -0.0112 0.0289  0.0164  340 TRP A NE1 
2754  C CE2 . TRP A 340 ? 0.2783 0.2493 0.2940 -0.0149 0.0263  0.0206  340 TRP A CE2 
2755  C CE3 . TRP A 340 ? 0.2728 0.2347 0.2957 -0.0210 0.0158  0.0234  340 TRP A CE3 
2756  C CZ2 . TRP A 340 ? 0.3208 0.2936 0.3362 -0.0172 0.0282  0.0254  340 TRP A CZ2 
2757  C CZ3 . TRP A 340 ? 0.3192 0.2818 0.3424 -0.0244 0.0177  0.0288  340 TRP A CZ3 
2758  C CH2 . TRP A 340 ? 0.3197 0.2886 0.3391 -0.0220 0.0244  0.0299  340 TRP A CH2 
2759  N N   . ASN A 341 ? 0.2778 0.2352 0.2833 -0.0010 0.0170  0.0057  341 ASN A N   
2760  C CA  . ASN A 341 ? 0.2850 0.2434 0.2859 0.0011  0.0206  0.0045  341 ASN A CA  
2761  C C   . ASN A 341 ? 0.2964 0.2527 0.2912 0.0048  0.0181  0.0035  341 ASN A C   
2762  O O   . ASN A 341 ? 0.2865 0.2456 0.2783 0.0050  0.0205  0.0036  341 ASN A O   
2763  C CB  . ASN A 341 ? 0.3026 0.2622 0.3048 0.0029  0.0228  0.0040  341 ASN A CB  
2764  C CG  . ASN A 341 ? 0.3007 0.2631 0.3054 0.0010  0.0268  0.0046  341 ASN A CG  
2765  O OD1 . ASN A 341 ? 0.3067 0.2684 0.3082 0.0001  0.0297  0.0041  341 ASN A OD1 
2766  N ND2 . ASN A 341 ? 0.3062 0.2724 0.3164 0.0008  0.0265  0.0056  341 ASN A ND2 
2767  N N   . LEU A 342 ? 0.2676 0.2197 0.2605 0.0082  0.0130  0.0024  342 LEU A N   
2768  C CA  . LEU A 342 ? 0.3284 0.2793 0.3138 0.0139  0.0107  0.0014  342 LEU A CA  
2769  C C   . LEU A 342 ? 0.3180 0.2678 0.2993 0.0140  0.0098  0.0016  342 LEU A C   
2770  O O   . LEU A 342 ? 0.3379 0.2903 0.3132 0.0190  0.0096  0.0012  342 LEU A O   
2771  C CB  . LEU A 342 ? 0.3146 0.2591 0.2967 0.0188  0.0041  -0.0007 342 LEU A CB  
2772  C CG  . LEU A 342 ? 0.2989 0.2463 0.2823 0.0216  0.0056  -0.0010 342 LEU A CG  
2773  C CD1 . LEU A 342 ? 0.3450 0.2866 0.3268 0.0254  -0.0016 -0.0036 342 LEU A CD1 
2774  C CD2 . LEU A 342 ? 0.2845 0.2379 0.2631 0.0263  0.0101  0.0004  342 LEU A CD2 
2775  N N   . SER A 343 ? 0.2889 0.2360 0.2729 0.0092  0.0095  0.0027  343 SER A N   
2776  C CA  . SER A 343 ? 0.3210 0.2663 0.3000 0.0100  0.0087  0.0032  343 SER A CA  
2777  C C   . SER A 343 ? 0.3276 0.2817 0.3072 0.0085  0.0141  0.0038  343 SER A C   
2778  O O   . SER A 343 ? 0.3313 0.2859 0.3067 0.0096  0.0138  0.0041  343 SER A O   
2779  C CB  . SER A 343 ? 0.3259 0.2641 0.3069 0.0055  0.0060  0.0051  343 SER A CB  
2780  O OG  . SER A 343 ? 0.3030 0.2468 0.2908 -0.0001 0.0109  0.0075  343 SER A OG  
2781  N N   . LYS A 344 ? 0.2154 0.2574 0.2472 0.0137  -0.0001 -0.0064 344 LYS A N   
2782  C CA  . LYS A 344 ? 0.2434 0.2816 0.2705 0.0150  0.0015  -0.0063 344 LYS A CA  
2783  C C   . LYS A 344 ? 0.2311 0.2627 0.2574 0.0138  0.0004  -0.0073 344 LYS A C   
2784  O O   . LYS A 344 ? 0.2231 0.2518 0.2492 0.0144  -0.0004 -0.0094 344 LYS A O   
2785  C CB  . LYS A 344 ? 0.2746 0.3120 0.2974 0.0190  0.0031  -0.0076 344 LYS A CB  
2786  C CG  . LYS A 344 ? 0.3146 0.3483 0.3321 0.0205  0.0047  -0.0077 344 LYS A CG  
2787  C CD  . LYS A 344 ? 0.3878 0.4188 0.4004 0.0244  0.0057  -0.0091 344 LYS A CD  
2788  C CE  . LYS A 344 ? 0.3137 0.3506 0.3268 0.0277  0.0066  -0.0089 344 LYS A CE  
2789  N NZ  . LYS A 344 ? 0.3156 0.3558 0.3270 0.0295  0.0086  -0.0083 344 LYS A NZ  
2790  N N   . PRO A 345 ? 0.2240 0.2535 0.2497 0.0123  0.0001  -0.0059 345 PRO A N   
2791  C CA  . PRO A 345 ? 0.2506 0.2749 0.2766 0.0116  -0.0014 -0.0070 345 PRO A CA  
2792  C C   . PRO A 345 ? 0.2688 0.2901 0.2914 0.0134  -0.0003 -0.0092 345 PRO A C   
2793  O O   . PRO A 345 ? 0.2599 0.2790 0.2839 0.0133  -0.0012 -0.0109 345 PRO A O   
2794  C CB  . PRO A 345 ? 0.2501 0.2732 0.2751 0.0100  -0.0019 -0.0047 345 PRO A CB  
2795  C CG  . PRO A 345 ? 0.2821 0.3105 0.3085 0.0084  -0.0013 -0.0020 345 PRO A CG  
2796  C CD  . PRO A 345 ? 0.2690 0.3016 0.2945 0.0108  0.0008  -0.0031 345 PRO A CD  
2797  N N   . GLN A 346 ? 0.2360 0.2570 0.2540 0.0152  0.0015  -0.0091 346 GLN A N   
2798  C CA  . GLN A 346 ? 0.2928 0.3098 0.3069 0.0163  0.0023  -0.0108 346 GLN A CA  
2799  C C   . GLN A 346 ? 0.2998 0.3166 0.3134 0.0174  0.0027  -0.0122 346 GLN A C   
2800  O O   . GLN A 346 ? 0.2924 0.3056 0.3022 0.0179  0.0034  -0.0131 346 GLN A O   
2801  C CB  . GLN A 346 ? 0.2624 0.2776 0.2710 0.0178  0.0037  -0.0104 346 GLN A CB  
2802  C CG  . GLN A 346 ? 0.2882 0.3012 0.2953 0.0163  0.0031  -0.0099 346 GLN A CG  
2803  C CD  . GLN A 346 ? 0.3407 0.3499 0.3474 0.0150  0.0024  -0.0112 346 GLN A CD  
2804  O OE1 . GLN A 346 ? 0.4052 0.4140 0.4135 0.0147  0.0024  -0.0125 346 GLN A OE1 
2805  N NE2 . GLN A 346 ? 0.3171 0.3245 0.3220 0.0139  0.0016  -0.0110 346 GLN A NE2 
2806  N N   . TRP A 347 ? 0.2708 0.2909 0.2877 0.0175  0.0019  -0.0123 347 TRP A N   
2807  C CA  . TRP A 347 ? 0.2563 0.2760 0.2723 0.0183  0.0019  -0.0138 347 TRP A CA  
2808  C C   . TRP A 347 ? 0.2623 0.2817 0.2814 0.0168  0.0008  -0.0155 347 TRP A C   
2809  O O   . TRP A 347 ? 0.2644 0.2833 0.2820 0.0172  0.0010  -0.0171 347 TRP A O   
2810  C CB  . TRP A 347 ? 0.2540 0.2778 0.2710 0.0196  0.0014  -0.0134 347 TRP A CB  
2811  C CG  . TRP A 347 ? 0.2531 0.2777 0.2666 0.0225  0.0025  -0.0124 347 TRP A CG  
2812  C CD1 . TRP A 347 ? 0.2837 0.3041 0.2923 0.0239  0.0038  -0.0122 347 TRP A CD1 
2813  C CD2 . TRP A 347 ? 0.2321 0.2617 0.2469 0.0246  0.0021  -0.0119 347 TRP A CD2 
2814  N NE1 . TRP A 347 ? 0.3067 0.3286 0.3131 0.0272  0.0043  -0.0117 347 TRP A NE1 
2815  C CE2 . TRP A 347 ? 0.2339 0.2620 0.2442 0.0279  0.0034  -0.0114 347 TRP A CE2 
2816  C CE3 . TRP A 347 ? 0.2543 0.2894 0.2734 0.0240  0.0006  -0.0118 347 TRP A CE3 
2817  C CZ2 . TRP A 347 ? 0.2528 0.2858 0.2638 0.0311  0.0033  -0.0110 347 TRP A CZ2 
2818  C CZ3 . TRP A 347 ? 0.2389 0.2795 0.2588 0.0267  0.0005  -0.0112 347 TRP A CZ3 
2819  C CH2 . TRP A 347 ? 0.2487 0.2883 0.2647 0.0306  0.0019  -0.0108 347 TRP A CH2 
2820  N N   . GLN A 348 ? 0.2640 0.2836 0.2872 0.0153  -0.0005 -0.0154 348 GLN A N   
2821  C CA  . GLN A 348 ? 0.2287 0.2481 0.2554 0.0147  -0.0019 -0.0175 348 GLN A CA  
2822  C C   . GLN A 348 ? 0.2472 0.2653 0.2729 0.0149  -0.0009 -0.0195 348 GLN A C   
2823  O O   . GLN A 348 ? 0.2513 0.2700 0.2780 0.0152  -0.0011 -0.0219 348 GLN A O   
2824  C CB  . GLN A 348 ? 0.2390 0.2579 0.2700 0.0133  -0.0040 -0.0165 348 GLN A CB  
2825  C CG  . GLN A 348 ? 0.2450 0.2662 0.2769 0.0123  -0.0045 -0.0140 348 GLN A CG  
2826  C CD  . GLN A 348 ? 0.2731 0.2971 0.3055 0.0125  -0.0050 -0.0148 348 GLN A CD  
2827  O OE1 . GLN A 348 ? 0.2688 0.2919 0.3030 0.0122  -0.0065 -0.0170 348 GLN A OE1 
2828  N NE2 . GLN A 348 ? 0.2608 0.2884 0.2918 0.0132  -0.0038 -0.0132 348 GLN A NE2 
2829  N N   . HIS A 349 ? 0.2395 0.2563 0.2633 0.0145  0.0002  -0.0187 349 HIS A N   
2830  C CA  . HIS A 349 ? 0.2402 0.2572 0.2645 0.0141  0.0010  -0.0204 349 HIS A CA  
2831  C C   . HIS A 349 ? 0.2545 0.2714 0.2744 0.0142  0.0030  -0.0212 349 HIS A C   
2832  O O   . HIS A 349 ? 0.2525 0.2707 0.2726 0.0135  0.0041  -0.0228 349 HIS A O   
2833  C CB  . HIS A 349 ? 0.2841 0.2998 0.3076 0.0132  0.0011  -0.0192 349 HIS A CB  
2834  C CG  . HIS A 349 ? 0.2643 0.2774 0.2818 0.0130  0.0025  -0.0179 349 HIS A CG  
2835  N ND1 . HIS A 349 ? 0.2830 0.2949 0.2979 0.0140  0.0025  -0.0162 349 HIS A ND1 
2836  C CD2 . HIS A 349 ? 0.2959 0.3071 0.3095 0.0121  0.0040  -0.0181 349 HIS A CD2 
2837  C CE1 . HIS A 349 ? 0.3158 0.3246 0.3252 0.0144  0.0037  -0.0157 349 HIS A CE1 
2838  N NE2 . HIS A 349 ? 0.2861 0.2937 0.2943 0.0129  0.0045  -0.0166 349 HIS A NE2 
2839  N N   . PHE A 350 ? 0.2540 0.2699 0.2700 0.0151  0.0033  -0.0201 350 PHE A N   
2840  C CA  . PHE A 350 ? 0.2219 0.2370 0.2331 0.0153  0.0046  -0.0205 350 PHE A CA  
2841  C C   . PHE A 350 ? 0.2552 0.2729 0.2679 0.0154  0.0046  -0.0230 350 PHE A C   
2842  O O   . PHE A 350 ? 0.2872 0.3052 0.2961 0.0149  0.0061  -0.0237 350 PHE A O   
2843  C CB  . PHE A 350 ? 0.2313 0.2449 0.2384 0.0169  0.0044  -0.0188 350 PHE A CB  
2844  C CG  . PHE A 350 ? 0.2410 0.2507 0.2439 0.0173  0.0050  -0.0170 350 PHE A CG  
2845  C CD1 . PHE A 350 ? 0.2401 0.2455 0.2372 0.0167  0.0062  -0.0164 350 PHE A CD1 
2846  C CD2 . PHE A 350 ? 0.2519 0.2619 0.2563 0.0182  0.0045  -0.0159 350 PHE A CD2 
2847  C CE1 . PHE A 350 ? 0.2879 0.2884 0.2808 0.0172  0.0064  -0.0151 350 PHE A CE1 
2848  C CE2 . PHE A 350 ? 0.2639 0.2700 0.2639 0.0190  0.0051  -0.0148 350 PHE A CE2 
2849  C CZ  . PHE A 350 ? 0.2776 0.2782 0.2716 0.0187  0.0058  -0.0146 350 PHE A CZ  
2850  N N   . TYR A 351 ? 0.2470 0.2665 0.2648 0.0158  0.0028  -0.0244 351 TYR A N   
2851  C CA  . TYR A 351 ? 0.2710 0.2923 0.2904 0.0163  0.0023  -0.0274 351 TYR A CA  
2852  C C   . TYR A 351 ? 0.3290 0.3517 0.3535 0.0164  0.0021  -0.0297 351 TYR A C   
2853  O O   . TYR A 351 ? 0.3096 0.3345 0.3342 0.0169  0.0031  -0.0326 351 TYR A O   
2854  C CB  . TYR A 351 ? 0.3010 0.3224 0.3222 0.0168  -0.0001 -0.0276 351 TYR A CB  
2855  C CG  . TYR A 351 ? 0.2799 0.3013 0.2980 0.0171  -0.0004 -0.0251 351 TYR A CG  
2856  C CD1 . TYR A 351 ? 0.2705 0.2919 0.2831 0.0178  0.0004  -0.0251 351 TYR A CD1 
2857  C CD2 . TYR A 351 ? 0.2637 0.2854 0.2841 0.0169  -0.0014 -0.0228 351 TYR A CD2 
2858  C CE1 . TYR A 351 ? 0.2485 0.2699 0.2584 0.0189  -0.0001 -0.0229 351 TYR A CE1 
2859  C CE2 . TYR A 351 ? 0.2880 0.3109 0.3063 0.0178  -0.0015 -0.0209 351 TYR A CE2 
2860  C CZ  . TYR A 351 ? 0.2991 0.3217 0.3123 0.0191  -0.0010 -0.0210 351 TYR A CZ  
2861  O OH  . TYR A 351 ? 0.3236 0.3475 0.3348 0.0207  -0.0015 -0.0194 351 TYR A OH  
2862  N N   . ASP A 352 ? 0.2714 0.2932 0.3001 0.0162  0.0007  -0.0286 352 ASP A N   
2863  C CA  . ASP A 352 ? 0.2836 0.3060 0.3177 0.0170  -0.0006 -0.0308 352 ASP A CA  
2864  C C   . ASP A 352 ? 0.2748 0.2967 0.3111 0.0163  -0.0011 -0.0286 352 ASP A C   
2865  O O   . ASP A 352 ? 0.2674 0.2869 0.3044 0.0158  -0.0030 -0.0262 352 ASP A O   
2866  C CB  . ASP A 352 ? 0.2934 0.3137 0.3304 0.0177  -0.0035 -0.0318 352 ASP A CB  
2867  C CG  . ASP A 352 ? 0.3269 0.3465 0.3691 0.0192  -0.0054 -0.0341 352 ASP A CG  
2868  O OD1 . ASP A 352 ? 0.3071 0.3290 0.3516 0.0198  -0.0045 -0.0346 352 ASP A OD1 
2869  O OD2 . ASP A 352 ? 0.3602 0.3769 0.4044 0.0199  -0.0080 -0.0357 352 ASP A OD2 
2870  N N   . PRO A 353 ? 0.2990 0.3235 0.3364 0.0160  0.0003  -0.0293 353 PRO A N   
2871  C CA  . PRO A 353 ? 0.3155 0.3395 0.3543 0.0151  -0.0006 -0.0273 353 PRO A CA  
2872  C C   . PRO A 353 ? 0.2607 0.2832 0.3044 0.0162  -0.0039 -0.0271 353 PRO A C   
2873  O O   . PRO A 353 ? 0.2657 0.2864 0.3092 0.0154  -0.0052 -0.0246 353 PRO A O   
2874  C CB  . PRO A 353 ? 0.3019 0.3302 0.3423 0.0144  0.0012  -0.0288 353 PRO A CB  
2875  C CG  . PRO A 353 ? 0.3609 0.3929 0.4031 0.0159  0.0025  -0.0325 353 PRO A CG  
2876  C CD  . PRO A 353 ? 0.3615 0.3904 0.4001 0.0166  0.0022  -0.0326 353 PRO A CD  
2877  N N   . THR A 354 ? 0.2699 0.2925 0.3173 0.0181  -0.0053 -0.0297 354 THR A N   
2878  C CA  . THR A 354 ? 0.2797 0.2995 0.3313 0.0193  -0.0088 -0.0294 354 THR A CA  
2879  C C   . THR A 354 ? 0.2975 0.3126 0.3470 0.0177  -0.0107 -0.0259 354 THR A C   
2880  O O   . THR A 354 ? 0.2681 0.2804 0.3192 0.0176  -0.0135 -0.0239 354 THR A O   
2881  C CB  . THR A 354 ? 0.2905 0.3101 0.3460 0.0220  -0.0103 -0.0334 354 THR A CB  
2882  O OG1 . THR A 354 ? 0.2978 0.3145 0.3511 0.0217  -0.0107 -0.0340 354 THR A OG1 
2883  C CG2 . THR A 354 ? 0.3067 0.3327 0.3645 0.0236  -0.0077 -0.0371 354 THR A CG2 
2884  N N   . ILE A 355 ? 0.2675 0.2823 0.3131 0.0165  -0.0092 -0.0250 355 ILE A N   
2885  C CA  . ILE A 355 ? 0.3042 0.3165 0.3482 0.0148  -0.0104 -0.0216 355 ILE A CA  
2886  C C   . ILE A 355 ? 0.2707 0.2832 0.3124 0.0137  -0.0099 -0.0184 355 ILE A C   
2887  O O   . ILE A 355 ? 0.2760 0.2864 0.3179 0.0126  -0.0117 -0.0156 355 ILE A O   
2888  C CB  . ILE A 355 ? 0.2823 0.2958 0.3235 0.0141  -0.0090 -0.0214 355 ILE A CB  
2889  C CG1 . ILE A 355 ? 0.2819 0.2950 0.3246 0.0151  -0.0099 -0.0249 355 ILE A CG1 
2890  C CG2 . ILE A 355 ? 0.2569 0.2696 0.2974 0.0122  -0.0100 -0.0179 355 ILE A CG2 
2891  C CD1 . ILE A 355 ? 0.2997 0.3143 0.3395 0.0144  -0.0090 -0.0247 355 ILE A CD1 
2892  N N   . LYS A 356 ? 0.2680 0.2826 0.3071 0.0137  -0.0074 -0.0189 356 LYS A N   
2893  C CA  . LYS A 356 ? 0.2649 0.2790 0.3013 0.0128  -0.0072 -0.0166 356 LYS A CA  
2894  C C   . LYS A 356 ? 0.2963 0.3099 0.3360 0.0130  -0.0097 -0.0165 356 LYS A C   
2895  O O   . LYS A 356 ? 0.2912 0.3033 0.3294 0.0121  -0.0111 -0.0140 356 LYS A O   
2896  C CB  . LYS A 356 ? 0.2603 0.2755 0.2929 0.0125  -0.0045 -0.0174 356 LYS A CB  
2897  C CG  . LYS A 356 ? 0.2443 0.2585 0.2742 0.0115  -0.0047 -0.0159 356 LYS A CG  
2898  C CD  . LYS A 356 ? 0.2769 0.2900 0.3013 0.0109  -0.0022 -0.0160 356 LYS A CD  
2899  C CE  . LYS A 356 ? 0.3919 0.4033 0.4132 0.0098  -0.0027 -0.0151 356 LYS A CE  
2900  N NZ  . LYS A 356 ? 0.3886 0.3995 0.4080 0.0085  -0.0016 -0.0163 356 LYS A NZ  
2901  N N   . SER A 357 ? 0.2628 0.2782 0.3071 0.0144  -0.0104 -0.0193 357 SER A N   
2902  C CA  . SER A 357 ? 0.2767 0.2923 0.3250 0.0153  -0.0132 -0.0193 357 SER A CA  
2903  C C   . SER A 357 ? 0.2425 0.2536 0.2915 0.0153  -0.0166 -0.0168 357 SER A C   
2904  O O   . SER A 357 ? 0.2558 0.2653 0.3041 0.0148  -0.0189 -0.0144 357 SER A O   
2905  C CB  . SER A 357 ? 0.2902 0.3093 0.3443 0.0176  -0.0135 -0.0231 357 SER A CB  
2906  O OG  . SER A 357 ? 0.2964 0.3204 0.3502 0.0170  -0.0104 -0.0250 357 SER A OG  
2907  N N   . ASP A 358 ? 0.2673 0.2759 0.3169 0.0155  -0.0172 -0.0172 358 ASP A N   
2908  C CA  . ASP A 358 ? 0.2713 0.2748 0.3213 0.0148  -0.0206 -0.0144 358 ASP A CA  
2909  C C   . ASP A 358 ? 0.2675 0.2704 0.3126 0.0120  -0.0199 -0.0101 358 ASP A C   
2910  O O   . ASP A 358 ? 0.2726 0.2724 0.3168 0.0111  -0.0225 -0.0070 358 ASP A O   
2911  C CB  . ASP A 358 ? 0.2995 0.3003 0.3510 0.0149  -0.0214 -0.0158 358 ASP A CB  
2912  C CG  . ASP A 358 ? 0.3738 0.3743 0.4299 0.0181  -0.0227 -0.0203 358 ASP A CG  
2913  O OD1 . ASP A 358 ? 0.3768 0.3784 0.4361 0.0204  -0.0240 -0.0216 358 ASP A OD1 
2914  O OD2 . ASP A 358 ? 0.3663 0.3657 0.4229 0.0185  -0.0225 -0.0227 358 ASP A OD2 
2915  N N   . MET A 359 ? 0.2628 0.2686 0.3044 0.0111  -0.0164 -0.0100 359 MET A N   
2916  C CA  . MET A 359 ? 0.2634 0.2697 0.3003 0.0091  -0.0152 -0.0066 359 MET A CA  
2917  C C   . MET A 359 ? 0.2596 0.2656 0.2939 0.0090  -0.0160 -0.0052 359 MET A C   
2918  O O   . MET A 359 ? 0.2665 0.2709 0.2980 0.0075  -0.0173 -0.0019 359 MET A O   
2919  C CB  . MET A 359 ? 0.3017 0.3112 0.3360 0.0094  -0.0115 -0.0079 359 MET A CB  
2920  C CG  . MET A 359 ? 0.2701 0.2805 0.3053 0.0084  -0.0112 -0.0072 359 MET A CG  
2921  S SD  . MET A 359 ? 0.3073 0.3214 0.3394 0.0095  -0.0075 -0.0086 359 MET A SD  
2922  C CE  . MET A 359 ? 0.3114 0.3274 0.3460 0.0085  -0.0079 -0.0083 359 MET A CE  
2923  N N   . MET A 360 ? 0.2781 0.2857 0.3132 0.0102  -0.0155 -0.0077 360 MET A N   
2924  C CA  . MET A 360 ? 0.2763 0.2839 0.3096 0.0099  -0.0168 -0.0069 360 MET A CA  
2925  C C   . MET A 360 ? 0.2629 0.2681 0.2988 0.0103  -0.0211 -0.0053 360 MET A C   
2926  O O   . MET A 360 ? 0.2743 0.2780 0.3066 0.0092  -0.0227 -0.0024 360 MET A O   
2927  C CB  . MET A 360 ? 0.3018 0.3122 0.3358 0.0103  -0.0154 -0.0098 360 MET A CB  
2928  C CG  . MET A 360 ? 0.3119 0.3233 0.3431 0.0101  -0.0116 -0.0112 360 MET A CG  
2929  S SD  . MET A 360 ? 0.3285 0.3425 0.3607 0.0098  -0.0102 -0.0140 360 MET A SD  
2930  C CE  . MET A 360 ? 0.3560 0.3683 0.3826 0.0080  -0.0108 -0.0129 360 MET A CE  
2931  N N   . LEU A 361 ? 0.2436 0.2478 0.2851 0.0119  -0.0231 -0.0067 361 LEU A N   
2932  C CA  . LEU A 361 ? 0.3145 0.3152 0.3584 0.0128  -0.0278 -0.0050 361 LEU A CA  
2933  C C   . LEU A 361 ? 0.2748 0.2709 0.3147 0.0106  -0.0293 -0.0005 361 LEU A C   
2934  O O   . LEU A 361 ? 0.2787 0.2720 0.3167 0.0100  -0.0325 0.0026  361 LEU A O   
2935  C CB  . LEU A 361 ? 0.3084 0.3083 0.3590 0.0157  -0.0297 -0.0081 361 LEU A CB  
2936  C CG  . LEU A 361 ? 0.2672 0.2729 0.3224 0.0179  -0.0284 -0.0123 361 LEU A CG  
2937  C CD1 . LEU A 361 ? 0.3171 0.3222 0.3778 0.0208  -0.0293 -0.0158 361 LEU A CD1 
2938  C CD2 . LEU A 361 ? 0.2803 0.2882 0.3376 0.0188  -0.0313 -0.0119 361 LEU A CD2 
2939  N N   . ARG A 362 ? 0.2648 0.2607 0.3031 0.0089  -0.0268 0.0002  362 ARG A N   
2940  C CA  . ARG A 362 ? 0.2729 0.2659 0.3076 0.0060  -0.0277 0.0047  362 ARG A CA  
2941  C C   . ARG A 362 ? 0.2602 0.2552 0.2884 0.0042  -0.0260 0.0075  362 ARG A C   
2942  O O   . ARG A 362 ? 0.2995 0.2919 0.3241 0.0022  -0.0280 0.0117  362 ARG A O   
2943  C CB  . ARG A 362 ? 0.2579 0.2519 0.2934 0.0045  -0.0254 0.0044  362 ARG A CB  
2944  C CG  . ARG A 362 ? 0.2949 0.2866 0.3280 0.0009  -0.0262 0.0090  362 ARG A CG  
2945  C CD  . ARG A 362 ? 0.3015 0.2964 0.3359 -0.0005 -0.0237 0.0083  362 ARG A CD  
2946  N NE  . ARG A 362 ? 0.3125 0.3058 0.3461 -0.0045 -0.0246 0.0125  362 ARG A NE  
2947  C CZ  . ARG A 362 ? 0.3438 0.3393 0.3795 -0.0065 -0.0235 0.0124  362 ARG A CZ  
2948  N NH1 . ARG A 362 ? 0.2928 0.2916 0.3311 -0.0046 -0.0217 0.0083  362 ARG A NH1 
2949  N NH2 . ARG A 362 ? 0.3046 0.2991 0.3398 -0.0110 -0.0246 0.0167  362 ARG A NH2 
2950  N N   . ILE A 363 ? 0.2502 0.2495 0.2760 0.0048  -0.0225 0.0054  363 ILE A N   
2951  C CA  . ILE A 363 ? 0.2546 0.2552 0.2736 0.0037  -0.0212 0.0073  363 ILE A CA  
2952  C C   . ILE A 363 ? 0.2519 0.2501 0.2694 0.0039  -0.0250 0.0085  363 ILE A C   
2953  O O   . ILE A 363 ? 0.2811 0.2781 0.2931 0.0023  -0.0260 0.0120  363 ILE A O   
2954  C CB  . ILE A 363 ? 0.2360 0.2399 0.2526 0.0047  -0.0173 0.0043  363 ILE A CB  
2955  C CG1 . ILE A 363 ? 0.2280 0.2346 0.2448 0.0045  -0.0139 0.0040  363 ILE A CG1 
2956  C CG2 . ILE A 363 ? 0.2562 0.2602 0.2656 0.0041  -0.0169 0.0055  363 ILE A CG2 
2957  C CD1 . ILE A 363 ? 0.2628 0.2715 0.2784 0.0063  -0.0105 0.0004  363 ILE A CD1 
2958  N N   . ILE A 364 ? 0.2652 0.2635 0.2877 0.0060  -0.0271 0.0058  364 ILE A N   
2959  C CA  . ILE A 364 ? 0.2649 0.2619 0.2873 0.0066  -0.0314 0.0067  364 ILE A CA  
2960  C C   . ILE A 364 ? 0.3310 0.3230 0.3521 0.0057  -0.0353 0.0112  364 ILE A C   
2961  O O   . ILE A 364 ? 0.3069 0.2974 0.3227 0.0047  -0.0376 0.0141  364 ILE A O   
2962  C CB  . ILE A 364 ? 0.2731 0.2723 0.3029 0.0092  -0.0331 0.0030  364 ILE A CB  
2963  C CG1 . ILE A 364 ? 0.2663 0.2699 0.2957 0.0091  -0.0297 -0.0004 364 ILE A CG1 
2964  C CG2 . ILE A 364 ? 0.2973 0.2953 0.3284 0.0103  -0.0385 0.0044  364 ILE A CG2 
2965  C CD1 . ILE A 364 ? 0.2646 0.2719 0.3020 0.0111  -0.0298 -0.0043 364 ILE A CD1 
2966  N N   . LYS A 365 ? 0.2781 0.2670 0.3031 0.0059  -0.0363 0.0118  365 LYS A N   
2967  C CA  . LYS A 365 ? 0.3036 0.2864 0.3271 0.0046  -0.0403 0.0163  365 LYS A CA  
2968  C C   . LYS A 365 ? 0.3016 0.2841 0.3173 0.0006  -0.0384 0.0210  365 LYS A C   
2969  O O   . LYS A 365 ? 0.3529 0.3326 0.3631 -0.0008 -0.0411 0.0250  365 LYS A O   
2970  C CB  . LYS A 365 ? 0.2974 0.2763 0.3268 0.0055  -0.0417 0.0152  365 LYS A CB  
2971  C CG  . LYS A 365 ? 0.3683 0.3402 0.3954 0.0026  -0.0445 0.0201  365 LYS A CG  
2972  C CD  . LYS A 365 ? 0.4024 0.3692 0.4359 0.0047  -0.0472 0.0178  365 LYS A CD  
2973  C CE  . LYS A 365 ? 0.5000 0.4623 0.5324 0.0008  -0.0472 0.0208  365 LYS A CE  
2974  N NZ  . LYS A 365 ? 0.5823 0.5378 0.6094 -0.0026 -0.0509 0.0273  365 LYS A NZ  
2975  N N   . GLU A 366 ? 0.2898 0.2758 0.3047 -0.0011 -0.0338 0.0206  366 GLU A N   
2976  C CA  . GLU A 366 ? 0.2757 0.2624 0.2847 -0.0049 -0.0318 0.0251  366 GLU A CA  
2977  C C   . GLU A 366 ? 0.3300 0.3200 0.3311 -0.0055 -0.0298 0.0262  366 GLU A C   
2978  O O   . GLU A 366 ? 0.2960 0.2853 0.2910 -0.0085 -0.0300 0.0308  366 GLU A O   
2979  C CB  . GLU A 366 ? 0.3006 0.2911 0.3122 -0.0061 -0.0278 0.0240  366 GLU A CB  
2980  C CG  . GLU A 366 ? 0.3263 0.3123 0.3440 -0.0067 -0.0304 0.0239  366 GLU A CG  
2981  C CD  . GLU A 366 ? 0.3164 0.3063 0.3364 -0.0087 -0.0271 0.0235  366 GLU A CD  
2982  O OE1 . GLU A 366 ? 0.3177 0.3138 0.3344 -0.0105 -0.0231 0.0248  366 GLU A OE1 
2983  O OE2 . GLU A 366 ? 0.3161 0.3030 0.3414 -0.0084 -0.0288 0.0217  366 GLU A OE2 
2984  N N   . TRP A 367 ? 0.2807 0.2739 0.2815 -0.0031 -0.0282 0.0221  367 TRP A N   
2985  C CA  . TRP A 367 ? 0.2820 0.2774 0.2748 -0.0034 -0.0266 0.0223  367 TRP A CA  
2986  C C   . TRP A 367 ? 0.3159 0.3083 0.3064 -0.0026 -0.0313 0.0229  367 TRP A C   
2987  O O   . TRP A 367 ? 0.3147 0.3083 0.2986 -0.0027 -0.0309 0.0224  367 TRP A O   
2988  C CB  . TRP A 367 ? 0.2788 0.2785 0.2714 -0.0015 -0.0222 0.0176  367 TRP A CB  
2989  C CG  . TRP A 367 ? 0.2937 0.2977 0.2848 -0.0022 -0.0172 0.0178  367 TRP A CG  
2990  C CD1 . TRP A 367 ? 0.2825 0.2899 0.2664 -0.0026 -0.0137 0.0183  367 TRP A CD1 
2991  C CD2 . TRP A 367 ? 0.2678 0.2738 0.2648 -0.0024 -0.0153 0.0173  367 TRP A CD2 
2992  N NE1 . TRP A 367 ? 0.2783 0.2903 0.2641 -0.0026 -0.0098 0.0180  367 TRP A NE1 
2993  C CE2 . TRP A 367 ? 0.2759 0.2871 0.2697 -0.0027 -0.0108 0.0175  367 TRP A CE2 
2994  C CE3 . TRP A 367 ? 0.2958 0.2999 0.3005 -0.0019 -0.0170 0.0161  367 TRP A CE3 
2995  C CZ2 . TRP A 367 ? 0.2869 0.3020 0.2853 -0.0030 -0.0084 0.0171  367 TRP A CZ2 
2996  C CZ3 . TRP A 367 ? 0.2880 0.2952 0.2965 -0.0024 -0.0146 0.0155  367 TRP A CZ3 
2997  C CH2 . TRP A 367 ? 0.2654 0.2782 0.2710 -0.0030 -0.0105 0.0162  367 TRP A CH2 
2998  N N   . GLN A 368 ? 0.2924 0.2808 0.2882 -0.0017 -0.0361 0.0238  368 GLN A N   
2999  C CA  . GLN A 368 ? 0.2922 0.2779 0.2869 -0.0007 -0.0415 0.0249  368 GLN A CA  
3000  C C   . GLN A 368 ? 0.3216 0.3108 0.3163 0.0009  -0.0414 0.0207  368 GLN A C   
3001  O O   . GLN A 368 ? 0.3138 0.3031 0.3018 0.0002  -0.0430 0.0216  368 GLN A O   
3002  C CB  . GLN A 368 ? 0.3294 0.3122 0.3149 -0.0034 -0.0434 0.0305  368 GLN A CB  
3003  C CG  . GLN A 368 ? 0.4003 0.3803 0.3845 -0.0064 -0.0426 0.0352  368 GLN A CG  
3004  C CD  . GLN A 368 ? 0.4642 0.4409 0.4387 -0.0094 -0.0451 0.0414  368 GLN A CD  
3005  O OE1 . GLN A 368 ? 0.4415 0.4129 0.4152 -0.0088 -0.0509 0.0441  368 GLN A OE1 
3006  N NE2 . GLN A 368 ? 0.4474 0.4279 0.4144 -0.0123 -0.0405 0.0435  368 GLN A NE2 
3007  N N   . VAL A 369 ? 0.2915 0.2835 0.2935 0.0028  -0.0396 0.0162  369 VAL A N   
3008  C CA  . VAL A 369 ? 0.2908 0.2863 0.2934 0.0036  -0.0387 0.0121  369 VAL A CA  
3009  C C   . VAL A 369 ? 0.3327 0.3290 0.3408 0.0053  -0.0439 0.0111  369 VAL A C   
3010  O O   . VAL A 369 ? 0.3047 0.3006 0.3206 0.0074  -0.0463 0.0107  369 VAL A O   
3011  C CB  . VAL A 369 ? 0.2670 0.2653 0.2741 0.0044  -0.0342 0.0083  369 VAL A CB  
3012  C CG1 . VAL A 369 ? 0.2613 0.2627 0.2701 0.0047  -0.0338 0.0043  369 VAL A CG1 
3013  C CG2 . VAL A 369 ? 0.2807 0.2792 0.2816 0.0031  -0.0293 0.0090  369 VAL A CG2 
3014  N N   . ASP A 370 ? 0.2722 0.2702 0.2767 0.0046  -0.0455 0.0101  370 ASP A N   
3015  C CA  . ASP A 370 ? 0.2798 0.2803 0.2895 0.0059  -0.0505 0.0088  370 ASP A CA  
3016  C C   . ASP A 370 ? 0.3259 0.3319 0.3429 0.0064  -0.0487 0.0040  370 ASP A C   
3017  O O   . ASP A 370 ? 0.3051 0.3150 0.3298 0.0079  -0.0523 0.0026  370 ASP A O   
3018  C CB  . ASP A 370 ? 0.3122 0.3118 0.3136 0.0042  -0.0538 0.0105  370 ASP A CB  
3019  C CG  . ASP A 370 ? 0.3675 0.3621 0.3606 0.0033  -0.0555 0.0156  370 ASP A CG  
3020  O OD1 . ASP A 370 ? 0.3951 0.3870 0.3920 0.0046  -0.0583 0.0184  370 ASP A OD1 
3021  O OD2 . ASP A 370 ? 0.3780 0.3711 0.3606 0.0012  -0.0543 0.0170  370 ASP A OD2 
3022  N N   . GLY A 371 ? 0.2855 0.2922 0.3001 0.0050  -0.0437 0.0016  371 GLY A N   
3023  C CA  . GLY A 371 ? 0.2981 0.3095 0.3181 0.0045  -0.0422 -0.0023 371 GLY A CA  
3024  C C   . GLY A 371 ? 0.3000 0.3102 0.3171 0.0036  -0.0364 -0.0041 371 GLY A C   
3025  O O   . GLY A 371 ? 0.3003 0.3068 0.3097 0.0030  -0.0340 -0.0026 371 GLY A O   
3026  N N   . VAL A 372 ? 0.2672 0.2811 0.2906 0.0037  -0.0341 -0.0070 372 VAL A N   
3027  C CA  . VAL A 372 ? 0.2449 0.2576 0.2663 0.0032  -0.0290 -0.0085 372 VAL A CA  
3028  C C   . VAL A 372 ? 0.2964 0.3107 0.3174 0.0009  -0.0278 -0.0111 372 VAL A C   
3029  O O   . VAL A 372 ? 0.2769 0.2963 0.3045 0.0002  -0.0297 -0.0126 372 VAL A O   
3030  C CB  . VAL A 372 ? 0.2507 0.2655 0.2791 0.0052  -0.0270 -0.0094 372 VAL A CB  
3031  C CG1 . VAL A 372 ? 0.2798 0.2930 0.3048 0.0047  -0.0222 -0.0105 372 VAL A CG1 
3032  C CG2 . VAL A 372 ? 0.2730 0.2853 0.3022 0.0071  -0.0289 -0.0067 372 VAL A CG2 
3033  N N   . MET A 373 ? 0.2734 0.2835 0.2869 -0.0003 -0.0249 -0.0117 373 MET A N   
3034  C CA  . MET A 373 ? 0.2715 0.2811 0.2832 -0.0030 -0.0239 -0.0138 373 MET A CA  
3035  C C   . MET A 373 ? 0.2915 0.2993 0.3024 -0.0025 -0.0194 -0.0147 373 MET A C   
3036  O O   . MET A 373 ? 0.3107 0.3142 0.3155 -0.0011 -0.0173 -0.0139 373 MET A O   
3037  C CB  . MET A 373 ? 0.3108 0.3148 0.3126 -0.0045 -0.0250 -0.0139 373 MET A CB  
3038  C CG  . MET A 373 ? 0.3281 0.3331 0.3287 -0.0051 -0.0298 -0.0128 373 MET A CG  
3039  S SD  . MET A 373 ? 0.3496 0.3478 0.3380 -0.0075 -0.0310 -0.0142 373 MET A SD  
3040  C CE  . MET A 373 ? 0.3656 0.3586 0.3449 -0.0046 -0.0272 -0.0131 373 MET A CE  
3041  N N   . LEU A 374 ? 0.2644 0.2763 0.2816 -0.0034 -0.0180 -0.0161 374 LEU A N   
3042  C CA  . LEU A 374 ? 0.2754 0.2860 0.2918 -0.0028 -0.0141 -0.0166 374 LEU A CA  
3043  C C   . LEU A 374 ? 0.2817 0.2886 0.2933 -0.0058 -0.0126 -0.0177 374 LEU A C   
3044  O O   . LEU A 374 ? 0.2782 0.2884 0.2934 -0.0089 -0.0133 -0.0186 374 LEU A O   
3045  C CB  . LEU A 374 ? 0.2860 0.3031 0.3113 -0.0018 -0.0131 -0.0175 374 LEU A CB  
3046  C CG  . LEU A 374 ? 0.3186 0.3381 0.3490 0.0014  -0.0145 -0.0168 374 LEU A CG  
3047  C CD1 . LEU A 374 ? 0.3308 0.3565 0.3693 0.0025  -0.0133 -0.0186 374 LEU A CD1 
3048  C CD2 . LEU A 374 ? 0.3832 0.3981 0.4089 0.0034  -0.0132 -0.0152 374 LEU A CD2 
3049  N N   . HIS A 375 ? 0.2821 0.2825 0.2864 -0.0049 -0.0104 -0.0174 375 HIS A N   
3050  C CA  . HIS A 375 ? 0.2774 0.2722 0.2761 -0.0072 -0.0090 -0.0182 375 HIS A CA  
3051  C C   . HIS A 375 ? 0.2828 0.2806 0.2854 -0.0078 -0.0063 -0.0183 375 HIS A C   
3052  O O   . HIS A 375 ? 0.3421 0.3408 0.3456 -0.0049 -0.0044 -0.0179 375 HIS A O   
3053  C CB  . HIS A 375 ? 0.2870 0.2740 0.2766 -0.0047 -0.0079 -0.0179 375 HIS A CB  
3054  C CG  . HIS A 375 ? 0.3306 0.3095 0.3131 -0.0063 -0.0069 -0.0186 375 HIS A CG  
3055  N ND1 . HIS A 375 ? 0.3410 0.3136 0.3167 -0.0032 -0.0053 -0.0186 375 HIS A ND1 
3056  C CD2 . HIS A 375 ? 0.3513 0.3273 0.3324 -0.0106 -0.0076 -0.0192 375 HIS A CD2 
3057  C CE1 . HIS A 375 ? 0.3400 0.3049 0.3099 -0.0051 -0.0053 -0.0192 375 HIS A CE1 
3058  N NE2 . HIS A 375 ? 0.3347 0.3012 0.3076 -0.0100 -0.0066 -0.0194 375 HIS A NE2 
3059  N N   . LEU A 376 ? 0.2827 0.2829 0.2879 -0.0117 -0.0062 -0.0188 376 LEU A N   
3060  C CA  . LEU A 376 ? 0.2654 0.2678 0.2723 -0.0128 -0.0033 -0.0188 376 LEU A CA  
3061  C C   . LEU A 376 ? 0.3038 0.2960 0.3011 -0.0140 -0.0023 -0.0181 376 LEU A C   
3062  O O   . LEU A 376 ? 0.3508 0.3388 0.3446 -0.0182 -0.0033 -0.0182 376 LEU A O   
3063  C CB  . LEU A 376 ? 0.2779 0.2885 0.2920 -0.0168 -0.0033 -0.0195 376 LEU A CB  
3064  C CG  . LEU A 376 ? 0.2991 0.3192 0.3228 -0.0148 -0.0050 -0.0204 376 LEU A CG  
3065  C CD1 . LEU A 376 ? 0.2977 0.3271 0.3290 -0.0183 -0.0049 -0.0214 376 LEU A CD1 
3066  C CD2 . LEU A 376 ? 0.3453 0.3682 0.3722 -0.0101 -0.0034 -0.0207 376 LEU A CD2 
3067  N N   . ASN A 377 ? 0.2860 0.2738 0.2789 -0.0103 -0.0008 -0.0176 377 ASN A N   
3068  C CA  . ASN A 377 ? 0.2840 0.2611 0.2672 -0.0096 -0.0006 -0.0172 377 ASN A CA  
3069  C C   . ASN A 377 ? 0.2949 0.2689 0.2753 -0.0114 0.0013  -0.0162 377 ASN A C   
3070  O O   . ASN A 377 ? 0.3075 0.2831 0.2883 -0.0087 0.0031  -0.0156 377 ASN A O   
3071  C CB  . ASN A 377 ? 0.3124 0.2877 0.2931 -0.0043 -0.0004 -0.0171 377 ASN A CB  
3072  C CG  . ASN A 377 ? 0.3086 0.2740 0.2803 -0.0023 -0.0001 -0.0171 377 ASN A CG  
3073  O OD1 . ASN A 377 ? 0.3175 0.2751 0.2834 -0.0050 -0.0008 -0.0171 377 ASN A OD1 
3074  N ND2 . ASN A 377 ? 0.3396 0.3051 0.3099 0.0025  0.0006  -0.0170 377 ASN A ND2 
3075  N N   . ARG A 378 ? 0.2773 0.2471 0.2546 -0.0164 0.0008  -0.0158 378 ARG A N   
3076  C CA  . ARG A 378 ? 0.3075 0.2736 0.2811 -0.0190 0.0025  -0.0144 378 ARG A CA  
3077  C C   . ARG A 378 ? 0.3232 0.2786 0.2878 -0.0155 0.0027  -0.0135 378 ARG A C   
3078  O O   . ARG A 378 ? 0.3218 0.2733 0.2824 -0.0170 0.0038  -0.0118 378 ARG A O   
3079  C CB  . ARG A 378 ? 0.3271 0.2898 0.2987 -0.0258 0.0015  -0.0139 378 ARG A CB  
3080  C CG  . ARG A 378 ? 0.3532 0.3274 0.3342 -0.0297 0.0012  -0.0147 378 ARG A CG  
3081  C CD  . ARG A 378 ? 0.4086 0.3794 0.3875 -0.0370 0.0001  -0.0141 378 ARG A CD  
3082  N NE  . ARG A 378 ? 0.4202 0.4041 0.4091 -0.0410 0.0004  -0.0147 378 ARG A NE  
3083  C CZ  . ARG A 378 ? 0.4296 0.4232 0.4242 -0.0435 0.0033  -0.0140 378 ARG A CZ  
3084  N NH1 . ARG A 378 ? 0.4459 0.4369 0.4362 -0.0433 0.0061  -0.0124 378 ARG A NH1 
3085  N NH2 . ARG A 378 ? 0.4649 0.4716 0.4697 -0.0460 0.0032  -0.0151 378 ARG A NH2 
3086  N N   . GLY A 379 ? 0.3014 0.2522 0.2626 -0.0110 0.0014  -0.0144 379 GLY A N   
3087  C CA  . GLY A 379 ? 0.3249 0.2658 0.2779 -0.0069 0.0012  -0.0140 379 GLY A CA  
3088  C C   . GLY A 379 ? 0.3197 0.2653 0.2749 -0.0016 0.0027  -0.0136 379 GLY A C   
3089  O O   . GLY A 379 ? 0.3301 0.2691 0.2795 0.0022  0.0025  -0.0132 379 GLY A O   
3090  N N   . CYS A 380 ? 0.3276 0.2845 0.2912 -0.0013 0.0039  -0.0138 380 CYS A N   
3091  C CA  . CYS A 380 ? 0.2865 0.2481 0.2527 0.0035  0.0048  -0.0137 380 CYS A CA  
3092  C C   . CYS A 380 ? 0.2868 0.2577 0.2599 0.0021  0.0062  -0.0136 380 CYS A C   
3093  O O   . CYS A 380 ? 0.3074 0.2858 0.2875 0.0017  0.0060  -0.0146 380 CYS A O   
3094  C CB  . CYS A 380 ? 0.3171 0.2819 0.2858 0.0067  0.0041  -0.0148 380 CYS A CB  
3095  S SG  . CYS A 380 ? 0.2892 0.2612 0.2624 0.0115  0.0050  -0.0146 380 CYS A SG  
3096  N N   . GLU A 381 ? 0.2750 0.2451 0.2458 0.0015  0.0073  -0.0126 381 GLU A N   
3097  C CA  . GLU A 381 ? 0.2857 0.2648 0.2625 0.0009  0.0087  -0.0131 381 GLU A CA  
3098  C C   . GLU A 381 ? 0.2789 0.2640 0.2611 0.0049  0.0084  -0.0141 381 GLU A C   
3099  O O   . GLU A 381 ? 0.2814 0.2740 0.2705 0.0044  0.0087  -0.0153 381 GLU A O   
3100  C CB  . GLU A 381 ? 0.2966 0.2736 0.2686 -0.0002 0.0100  -0.0117 381 GLU A CB  
3101  C CG  . GLU A 381 ? 0.3262 0.2974 0.2920 0.0041  0.0092  -0.0105 381 GLU A CG  
3102  C CD  . GLU A 381 ? 0.3519 0.3236 0.3144 0.0039  0.0101  -0.0094 381 GLU A CD  
3103  O OE1 . GLU A 381 ? 0.3425 0.3073 0.2982 0.0065  0.0090  -0.0078 381 GLU A OE1 
3104  O OE2 . GLU A 381 ? 0.3477 0.3266 0.3139 0.0015  0.0118  -0.0102 381 GLU A OE2 
3105  N N   . GLY A 382 ? 0.3130 0.2952 0.2924 0.0087  0.0076  -0.0136 382 GLY A N   
3106  C CA  . GLY A 382 ? 0.2927 0.2808 0.2770 0.0118  0.0073  -0.0142 382 GLY A CA  
3107  C C   . GLY A 382 ? 0.3097 0.3030 0.3006 0.0115  0.0067  -0.0151 382 GLY A C   
3108  O O   . GLY A 382 ? 0.2682 0.2673 0.2648 0.0118  0.0066  -0.0159 382 GLY A O   
3109  N N   . LEU A 383 ? 0.3016 0.2922 0.2913 0.0108  0.0060  -0.0150 383 LEU A N   
3110  C CA  . LEU A 383 ? 0.2727 0.2675 0.2675 0.0106  0.0050  -0.0154 383 LEU A CA  
3111  C C   . LEU A 383 ? 0.2990 0.2966 0.2980 0.0075  0.0046  -0.0162 383 LEU A C   
3112  O O   . LEU A 383 ? 0.2973 0.2986 0.3013 0.0075  0.0034  -0.0164 383 LEU A O   
3113  C CB  . LEU A 383 ? 0.2811 0.2725 0.2722 0.0119  0.0044  -0.0150 383 LEU A CB  
3114  C CG  . LEU A 383 ? 0.2921 0.2829 0.2805 0.0156  0.0050  -0.0144 383 LEU A CG  
3115  C CD1 . LEU A 383 ? 0.3190 0.3082 0.3042 0.0172  0.0048  -0.0144 383 LEU A CD1 
3116  C CD2 . LEU A 383 ? 0.3119 0.3094 0.3061 0.0168  0.0050  -0.0140 383 LEU A CD2 
3117  N N   . SER A 384 ? 0.2699 0.2662 0.2672 0.0048  0.0055  -0.0164 384 SER A N   
3118  C CA  . SER A 384 ? 0.2664 0.2671 0.2685 0.0018  0.0053  -0.0173 384 SER A CA  
3119  C C   . SER A 384 ? 0.3073 0.3146 0.3148 0.0018  0.0066  -0.0185 384 SER A C   
3120  O O   . SER A 384 ? 0.2992 0.3122 0.3125 0.0004  0.0064  -0.0196 384 SER A O   
3121  C CB  . SER A 384 ? 0.2990 0.2953 0.2966 -0.0020 0.0056  -0.0168 384 SER A CB  
3122  O OG  . SER A 384 ? 0.3031 0.2936 0.2964 -0.0021 0.0040  -0.0165 384 SER A OG  
3123  N N   . VAL A 385 ? 0.2809 0.2881 0.2866 0.0036  0.0077  -0.0184 385 VAL A N   
3124  C CA  . VAL A 385 ? 0.2820 0.2954 0.2921 0.0037  0.0089  -0.0201 385 VAL A CA  
3125  C C   . VAL A 385 ? 0.2954 0.3135 0.3131 0.0054  0.0073  -0.0216 385 VAL A C   
3126  O O   . VAL A 385 ? 0.2888 0.3050 0.3071 0.0072  0.0055  -0.0208 385 VAL A O   
3127  C CB  . VAL A 385 ? 0.3103 0.3229 0.3171 0.0056  0.0098  -0.0201 385 VAL A CB  
3128  C CG1 . VAL A 385 ? 0.3278 0.3364 0.3272 0.0035  0.0114  -0.0187 385 VAL A CG1 
3129  C CG2 . VAL A 385 ? 0.3077 0.3176 0.3134 0.0085  0.0083  -0.0193 385 VAL A CG2 
3130  N N   . GLY A 386 ? 0.2964 0.3207 0.3197 0.0048  0.0078  -0.0235 386 GLY A N   
3131  C CA  . GLY A 386 ? 0.2628 0.2910 0.2935 0.0069  0.0059  -0.0251 386 GLY A CA  
3132  C C   . GLY A 386 ? 0.2973 0.3259 0.3312 0.0061  0.0037  -0.0244 386 GLY A C   
3133  O O   . GLY A 386 ? 0.2666 0.2979 0.3064 0.0079  0.0017  -0.0254 386 GLY A O   
3134  N N   . ILE A 387 ? 0.2758 0.3012 0.3056 0.0036  0.0036  -0.0228 387 ILE A N   
3135  C CA  . ILE A 387 ? 0.3019 0.3267 0.3333 0.0031  0.0010  -0.0220 387 ILE A CA  
3136  C C   . ILE A 387 ? 0.2793 0.3114 0.3188 0.0030  -0.0002 -0.0237 387 ILE A C   
3137  O O   . ILE A 387 ? 0.2922 0.3248 0.3351 0.0043  -0.0031 -0.0234 387 ILE A O   
3138  C CB  . ILE A 387 ? 0.2289 0.2487 0.2539 0.0002  0.0012  -0.0206 387 ILE A CB  
3139  C CG1 . ILE A 387 ? 0.3330 0.3513 0.3581 -0.0001 -0.0017 -0.0198 387 ILE A CG1 
3140  C CG2 . ILE A 387 ? 0.3068 0.3293 0.3320 -0.0035 0.0028  -0.0211 387 ILE A CG2 
3141  C CD1 . ILE A 387 ? 0.3826 0.3988 0.4073 0.0028  -0.0033 -0.0187 387 ILE A CD1 
3142  N N   . MET A 388 ? 0.2679 0.3061 0.3107 0.0016  0.0020  -0.0253 388 MET A N   
3143  C CA  . MET A 388 ? 0.2772 0.3237 0.3286 0.0019  0.0009  -0.0272 388 MET A CA  
3144  C C   . MET A 388 ? 0.2556 0.3047 0.3130 0.0065  -0.0005 -0.0291 388 MET A C   
3145  O O   . MET A 388 ? 0.3005 0.3533 0.3642 0.0082  -0.0032 -0.0299 388 MET A O   
3146  C CB  . MET A 388 ? 0.3268 0.3810 0.3809 -0.0010 0.0038  -0.0285 388 MET A CB  
3147  C CG  . MET A 388 ? 0.3217 0.3724 0.3698 -0.0062 0.0049  -0.0265 388 MET A CG  
3148  S SD  . MET A 388 ? 0.3997 0.4485 0.4486 -0.0083 0.0008  -0.0253 388 MET A SD  
3149  C CE  . MET A 388 ? 0.3742 0.4359 0.4357 -0.0069 -0.0009 -0.0277 388 MET A CE  
3150  N N   . GLU A 389 ? 0.2835 0.3295 0.3383 0.0086  0.0007  -0.0297 389 GLU A N   
3151  C CA  . GLU A 389 ? 0.2737 0.3200 0.3331 0.0126  -0.0013 -0.0314 389 GLU A CA  
3152  C C   . GLU A 389 ? 0.2535 0.2938 0.3122 0.0136  -0.0051 -0.0290 389 GLU A C   
3153  O O   . GLU A 389 ? 0.2637 0.3045 0.3275 0.0163  -0.0080 -0.0298 389 GLU A O   
3154  C CB  . GLU A 389 ? 0.2807 0.3251 0.3372 0.0141  0.0007  -0.0328 389 GLU A CB  
3155  C CG  . GLU A 389 ? 0.2999 0.3509 0.3568 0.0134  0.0045  -0.0354 389 GLU A CG  
3156  C CD  . GLU A 389 ? 0.3054 0.3648 0.3706 0.0162  0.0046  -0.0392 389 GLU A CD  
3157  O OE1 . GLU A 389 ? 0.2933 0.3524 0.3642 0.0196  0.0012  -0.0404 389 GLU A OE1 
3158  O OE2 . GLU A 389 ? 0.2965 0.3630 0.3627 0.0152  0.0080  -0.0411 389 GLU A OE2 
3159  N N   . ASN A 390 ? 0.2716 0.3062 0.3237 0.0116  -0.0050 -0.0262 390 ASN A N   
3160  C CA  . ASN A 390 ? 0.2751 0.3051 0.3258 0.0120  -0.0081 -0.0236 390 ASN A CA  
3161  C C   . ASN A 390 ? 0.2731 0.3058 0.3276 0.0117  -0.0110 -0.0233 390 ASN A C   
3162  O O   . ASN A 390 ? 0.2680 0.2993 0.3252 0.0135  -0.0144 -0.0225 390 ASN A O   
3163  C CB  . ASN A 390 ? 0.2834 0.3082 0.3261 0.0100  -0.0069 -0.0211 390 ASN A CB  
3164  C CG  . ASN A 390 ? 0.2994 0.3219 0.3384 0.0105  -0.0046 -0.0211 390 ASN A CG  
3165  O OD1 . ASN A 390 ? 0.2997 0.3197 0.3330 0.0093  -0.0027 -0.0202 390 ASN A OD1 
3166  N ND2 . ASN A 390 ? 0.2563 0.2792 0.2983 0.0125  -0.0050 -0.0223 390 ASN A ND2 
3167  N N   A ARG A 391 ? 0.2762 0.3127 0.3310 0.0092  -0.0099 -0.0239 391 ARG A N   
3168  N N   B ARG A 391 ? 0.2762 0.3128 0.3311 0.0092  -0.0100 -0.0239 391 ARG A N   
3169  C CA  A ARG A 391 ? 0.2831 0.3236 0.3423 0.0088  -0.0129 -0.0239 391 ARG A CA  
3170  C CA  B ARG A 391 ? 0.2829 0.3234 0.3422 0.0088  -0.0130 -0.0239 391 ARG A CA  
3171  C C   A ARG A 391 ? 0.2930 0.3390 0.3612 0.0123  -0.0150 -0.0260 391 ARG A C   
3172  C C   B ARG A 391 ? 0.2930 0.3390 0.3612 0.0123  -0.0150 -0.0260 391 ARG A C   
3173  O O   A ARG A 391 ? 0.2655 0.3114 0.3367 0.0139  -0.0191 -0.0252 391 ARG A O   
3174  O O   B ARG A 391 ? 0.2653 0.3113 0.3367 0.0139  -0.0191 -0.0252 391 ARG A O   
3175  C CB  A ARG A 391 ? 0.3149 0.3597 0.3740 0.0050  -0.0111 -0.0246 391 ARG A CB  
3176  C CB  B ARG A 391 ? 0.3152 0.3597 0.3741 0.0050  -0.0114 -0.0244 391 ARG A CB  
3177  C CG  A ARG A 391 ? 0.3264 0.3745 0.3885 0.0035  -0.0145 -0.0242 391 ARG A CG  
3178  C CG  B ARG A 391 ? 0.3256 0.3748 0.3892 0.0041  -0.0149 -0.0245 391 ARG A CG  
3179  C CD  A ARG A 391 ? 0.3419 0.3975 0.4077 0.0002  -0.0127 -0.0257 391 ARG A CD  
3180  C CD  B ARG A 391 ? 0.3429 0.3981 0.4084 0.0000  -0.0134 -0.0254 391 ARG A CD  
3181  N NE  A ARG A 391 ? 0.3456 0.4101 0.4201 0.0027  -0.0114 -0.0284 391 ARG A NE  
3182  N NE  B ARG A 391 ? 0.3429 0.4082 0.4169 0.0006  -0.0114 -0.0281 391 ARG A NE  
3183  C CZ  A ARG A 391 ? 0.3426 0.4136 0.4258 0.0058  -0.0143 -0.0298 391 ARG A CZ  
3184  C CZ  B ARG A 391 ? 0.3335 0.4071 0.4120 -0.0028 -0.0105 -0.0291 391 ARG A CZ  
3185  N NH1 A ARG A 391 ? 0.3111 0.3814 0.3955 0.0061  -0.0189 -0.0285 391 ARG A NH1 
3186  N NH1 B ARG A 391 ? 0.3394 0.4116 0.4148 -0.0075 -0.0118 -0.0278 391 ARG A NH1 
3187  N NH2 A ARG A 391 ? 0.3222 0.4005 0.4125 0.0090  -0.0128 -0.0327 391 ARG A NH2 
3188  N NH2 B ARG A 391 ? 0.3786 0.4624 0.4648 -0.0017 -0.0081 -0.0316 391 ARG A NH2 
3189  N N   . LEU A 392 ? 0.2774 0.3283 0.3497 0.0138  -0.0123 -0.0289 392 LEU A N   
3190  C CA  . LEU A 392 ? 0.2656 0.3217 0.3462 0.0179  -0.0140 -0.0317 392 LEU A CA  
3191  C C   . LEU A 392 ? 0.2593 0.3083 0.3399 0.0213  -0.0177 -0.0306 392 LEU A C   
3192  O O   . LEU A 392 ? 0.2798 0.3301 0.3659 0.0243  -0.0216 -0.0311 392 LEU A O   
3193  C CB  . LEU A 392 ? 0.2604 0.3219 0.3433 0.0189  -0.0100 -0.0351 392 LEU A CB  
3194  C CG  . LEU A 392 ? 0.3011 0.3696 0.3932 0.0236  -0.0110 -0.0390 392 LEU A CG  
3195  C CD1 . LEU A 392 ? 0.3235 0.4017 0.4237 0.0238  -0.0128 -0.0398 392 LEU A CD1 
3196  C CD2 . LEU A 392 ? 0.3197 0.3927 0.4122 0.0248  -0.0066 -0.0426 392 LEU A CD2 
3197  N N   . ALA A 393 ? 0.2405 0.2819 0.3148 0.0207  -0.0168 -0.0291 393 ALA A N   
3198  C CA  . ALA A 393 ? 0.2373 0.2720 0.3115 0.0231  -0.0202 -0.0279 393 ALA A CA  
3199  C C   . ALA A 393 ? 0.2962 0.3271 0.3689 0.0224  -0.0243 -0.0243 393 ALA A C   
3200  O O   . ALA A 393 ? 0.2876 0.3154 0.3632 0.0251  -0.0285 -0.0237 393 ALA A O   
3201  C CB  . ALA A 393 ? 0.2727 0.3014 0.3408 0.0219  -0.0182 -0.0269 393 ALA A CB  
3202  N N   . ILE A 394 ? 0.2490 0.2797 0.3167 0.0190  -0.0234 -0.0220 394 ILE A N   
3203  C CA  . ILE A 394 ? 0.2310 0.2587 0.2963 0.0183  -0.0272 -0.0188 394 ILE A CA  
3204  C C   . ILE A 394 ? 0.2298 0.2633 0.3022 0.0201  -0.0305 -0.0201 394 ILE A C   
3205  O O   . ILE A 394 ? 0.2745 0.3054 0.3482 0.0219  -0.0352 -0.0183 394 ILE A O   
3206  C CB  . ILE A 394 ? 0.2670 0.2929 0.3245 0.0145  -0.0253 -0.0167 394 ILE A CB  
3207  C CG1 . ILE A 394 ? 0.2789 0.2998 0.3301 0.0134  -0.0223 -0.0154 394 ILE A CG1 
3208  C CG2 . ILE A 394 ? 0.2724 0.2961 0.3270 0.0136  -0.0295 -0.0138 394 ILE A CG2 
3209  C CD1 . ILE A 394 ? 0.2835 0.3029 0.3272 0.0104  -0.0199 -0.0143 394 ILE A CD1 
3210  N N   . ALA A 395 ? 0.2709 0.3127 0.3483 0.0198  -0.0284 -0.0231 395 ALA A N   
3211  C CA  . ALA A 395 ? 0.2640 0.3133 0.3493 0.0216  -0.0315 -0.0246 395 ALA A CA  
3212  C C   . ALA A 395 ? 0.3203 0.3691 0.4122 0.0270  -0.0349 -0.0260 395 ALA A C   
3213  O O   . ALA A 395 ? 0.3197 0.3693 0.4153 0.0293  -0.0398 -0.0252 395 ALA A O   
3214  C CB  . ALA A 395 ? 0.2711 0.3304 0.3611 0.0199  -0.0278 -0.0277 395 ALA A CB  
3215  N N   . LYS A 396 ? 0.2863 0.3330 0.3790 0.0292  -0.0327 -0.0281 396 LYS A N   
3216  C CA  . LYS A 396 ? 0.2985 0.3437 0.3970 0.0347  -0.0361 -0.0300 396 LYS A CA  
3217  C C   . LYS A 396 ? 0.3106 0.3452 0.4052 0.0355  -0.0412 -0.0261 396 LYS A C   
3218  O O   . LYS A 396 ? 0.3029 0.3355 0.4022 0.0400  -0.0458 -0.0266 396 LYS A O   
3219  C CB  . LYS A 396 ? 0.3153 0.3595 0.4144 0.0367  -0.0328 -0.0335 396 LYS A CB  
3220  C CG  . LYS A 396 ? 0.3577 0.4128 0.4611 0.0366  -0.0280 -0.0377 396 LYS A CG  
3221  C CD  . LYS A 396 ? 0.3627 0.4158 0.4656 0.0390  -0.0254 -0.0411 396 LYS A CD  
3222  C CE  . LYS A 396 ? 0.4287 0.4929 0.5351 0.0389  -0.0203 -0.0452 396 LYS A CE  
3223  N NZ  . LYS A 396 ? 0.4283 0.4908 0.5329 0.0409  -0.0175 -0.0487 396 LYS A NZ  
3224  N N   . SER A 397 ? 0.3375 0.3651 0.4234 0.0315  -0.0403 -0.0222 397 SER A N   
3225  C CA  . SER A 397 ? 0.3380 0.3557 0.4192 0.0313  -0.0443 -0.0180 397 SER A CA  
3226  C C   . SER A 397 ? 0.3467 0.3641 0.4281 0.0318  -0.0494 -0.0151 397 SER A C   
3227  O O   . SER A 397 ? 0.3380 0.3473 0.4168 0.0326  -0.0538 -0.0117 397 SER A O   
3228  C CB  . SER A 397 ? 0.3032 0.3159 0.3755 0.0267  -0.0412 -0.0149 397 SER A CB  
3229  O OG  . SER A 397 ? 0.3369 0.3520 0.4045 0.0234  -0.0404 -0.0127 397 SER A OG  
3230  N N   . GLY A 398 ? 0.3802 0.3147 0.4379 0.0361  -0.0423 -0.0592 398 GLY A N   
3231  C CA  . GLY A 398 ? 0.3607 0.3109 0.4327 0.0338  -0.0381 -0.0468 398 GLY A CA  
3232  C C   . GLY A 398 ? 0.3350 0.3054 0.4140 0.0217  -0.0369 -0.0374 398 GLY A C   
3233  O O   . GLY A 398 ? 0.3475 0.3320 0.4353 0.0201  -0.0341 -0.0277 398 GLY A O   
3234  N N   . THR A 399 ? 0.3254 0.2979 0.3997 0.0144  -0.0390 -0.0403 399 THR A N   
3235  C CA  . THR A 399 ? 0.3146 0.3062 0.3918 0.0060  -0.0362 -0.0333 399 THR A CA  
3236  C C   . THR A 399 ? 0.3068 0.3130 0.3769 0.0090  -0.0287 -0.0352 399 THR A C   
3237  O O   . THR A 399 ? 0.2935 0.2964 0.3543 0.0143  -0.0259 -0.0430 399 THR A O   
3238  C CB  . THR A 399 ? 0.3056 0.2947 0.3818 -0.0013 -0.0407 -0.0352 399 THR A CB  
3239  O OG1 . THR A 399 ? 0.3316 0.3103 0.4196 -0.0063 -0.0485 -0.0295 399 THR A OG1 
3240  C CG2 . THR A 399 ? 0.2774 0.2856 0.3529 -0.0071 -0.0362 -0.0301 399 THR A CG2 
3241  N N   . PRO A 400 ? 0.2666 0.2884 0.3408 0.0058  -0.0262 -0.0279 400 PRO A N   
3242  C CA  . PRO A 400 ? 0.2682 0.3024 0.3382 0.0067  -0.0214 -0.0290 400 PRO A CA  
3243  C C   . PRO A 400 ? 0.2894 0.3241 0.3507 0.0039  -0.0203 -0.0351 400 PRO A C   
3244  O O   . PRO A 400 ? 0.2598 0.2938 0.3198 -0.0014 -0.0226 -0.0349 400 PRO A O   
3245  C CB  . PRO A 400 ? 0.3160 0.3630 0.3902 0.0021  -0.0226 -0.0209 400 PRO A CB  
3246  C CG  . PRO A 400 ? 0.3134 0.3557 0.3960 0.0021  -0.0260 -0.0137 400 PRO A CG  
3247  C CD  . PRO A 400 ? 0.2975 0.3255 0.3801 0.0014  -0.0286 -0.0177 400 PRO A CD  
3248  N N   . VAL A 401 ? 0.2777 0.3156 0.3348 0.0078  -0.0163 -0.0386 401 VAL A N   
3249  C CA  . VAL A 401 ? 0.2841 0.3226 0.3336 0.0059  -0.0150 -0.0434 401 VAL A CA  
3250  C C   . VAL A 401 ? 0.2556 0.3038 0.3056 0.0073  -0.0109 -0.0419 401 VAL A C   
3251  O O   . VAL A 401 ? 0.2894 0.3420 0.3440 0.0126  -0.0076 -0.0390 401 VAL A O   
3252  C CB  . VAL A 401 ? 0.2792 0.3052 0.3211 0.0097  -0.0164 -0.0504 401 VAL A CB  
3253  C CG1 . VAL A 401 ? 0.3077 0.3278 0.3462 0.0196  -0.0136 -0.0533 401 VAL A CG1 
3254  C CG2 . VAL A 401 ? 0.2844 0.3126 0.3184 0.0082  -0.0153 -0.0543 401 VAL A CG2 
3255  N N   A MET A 402 ? 0.2548 0.3072 0.3021 0.0024  -0.0113 -0.0426 402 MET A N   
3256  N N   B MET A 402 ? 0.2542 0.3065 0.3015 0.0025  -0.0113 -0.0426 402 MET A N   
3257  C CA  A MET A 402 ? 0.2698 0.3296 0.3194 0.0020  -0.0090 -0.0405 402 MET A CA  
3258  C CA  B MET A 402 ? 0.2696 0.3292 0.3191 0.0022  -0.0089 -0.0406 402 MET A CA  
3259  C C   A MET A 402 ? 0.2714 0.3287 0.3141 0.0010  -0.0081 -0.0443 402 MET A C   
3260  C C   B MET A 402 ? 0.2716 0.3286 0.3141 0.0014  -0.0079 -0.0445 402 MET A C   
3261  O O   A MET A 402 ? 0.2726 0.3247 0.3100 -0.0008 -0.0100 -0.0480 402 MET A O   
3262  O O   B MET A 402 ? 0.2716 0.3230 0.3085 0.0000  -0.0097 -0.0483 402 MET A O   
3263  C CB  A MET A 402 ? 0.2768 0.3429 0.3319 -0.0034 -0.0128 -0.0365 402 MET A CB  
3264  C CB  B MET A 402 ? 0.2773 0.3432 0.3321 -0.0034 -0.0127 -0.0368 402 MET A CB  
3265  C CG  A MET A 402 ? 0.2763 0.3398 0.3249 -0.0078 -0.0165 -0.0390 402 MET A CG  
3266  C CG  B MET A 402 ? 0.2770 0.3398 0.3246 -0.0077 -0.0160 -0.0398 402 MET A CG  
3267  S SD  A MET A 402 ? 0.3616 0.4254 0.4066 -0.0120 -0.0200 -0.0410 402 MET A SD  
3268  S SD  B MET A 402 ? 0.2528 0.3133 0.2951 -0.0096 -0.0157 -0.0438 402 MET A SD  
3269  C CE  A MET A 402 ? 0.2857 0.3445 0.3245 -0.0107 -0.0165 -0.0457 402 MET A CE  
3270  C CE  B MET A 402 ? 0.2490 0.3131 0.2982 -0.0132 -0.0200 -0.0405 402 MET A CE  
3271  N N   . THR A 403 ? 0.2696 0.3321 0.3147 0.0024  -0.0052 -0.0417 403 THR A N   
3272  C CA  . THR A 403 ? 0.2493 0.3104 0.2895 0.0015  -0.0044 -0.0435 403 THR A CA  
3273  C C   . THR A 403 ? 0.2560 0.3205 0.3028 -0.0036 -0.0066 -0.0400 403 THR A C   
3274  O O   . THR A 403 ? 0.2660 0.3359 0.3221 -0.0058 -0.0082 -0.0352 403 THR A O   
3275  C CB  . THR A 403 ? 0.2688 0.3321 0.3050 0.0081  0.0007  -0.0424 403 THR A CB  
3276  O OG1 . THR A 403 ? 0.2779 0.3512 0.3237 0.0107  0.0047  -0.0347 403 THR A OG1 
3277  C CG2 . THR A 403 ? 0.2852 0.3405 0.3116 0.0137  0.0006  -0.0483 403 THR A CG2 
3278  N N   . PHE A 404 ? 0.2465 0.3074 0.2893 -0.0054 -0.0075 -0.0423 404 PHE A N   
3279  C CA  . PHE A 404 ? 0.2755 0.3362 0.3239 -0.0092 -0.0100 -0.0396 404 PHE A CA  
3280  C C   . PHE A 404 ? 0.3035 0.3626 0.3485 -0.0073 -0.0076 -0.0394 404 PHE A C   
3281  O O   . PHE A 404 ? 0.2811 0.3374 0.3177 -0.0049 -0.0065 -0.0437 404 PHE A O   
3282  C CB  . PHE A 404 ? 0.3033 0.3578 0.3487 -0.0130 -0.0158 -0.0440 404 PHE A CB  
3283  C CG  . PHE A 404 ? 0.3240 0.3738 0.3594 -0.0112 -0.0151 -0.0497 404 PHE A CG  
3284  C CD1 . PHE A 404 ? 0.3243 0.3755 0.3554 -0.0099 -0.0141 -0.0515 404 PHE A CD1 
3285  C CD2 . PHE A 404 ? 0.3237 0.3685 0.3562 -0.0106 -0.0155 -0.0518 404 PHE A CD2 
3286  C CE1 . PHE A 404 ? 0.3558 0.4060 0.3815 -0.0085 -0.0132 -0.0540 404 PHE A CE1 
3287  C CE2 . PHE A 404 ? 0.3201 0.3636 0.3460 -0.0080 -0.0141 -0.0553 404 PHE A CE2 
3288  C CZ  . PHE A 404 ? 0.3436 0.3909 0.3666 -0.0072 -0.0128 -0.0559 404 PHE A CZ  
3289  N N   . GLU A 405 ? 0.2847 0.3462 0.3378 -0.0089 -0.0075 -0.0332 405 GLU A N   
3290  C CA  . GLU A 405 ? 0.3042 0.3648 0.3550 -0.0071 -0.0055 -0.0313 405 GLU A CA  
3291  C C   . GLU A 405 ? 0.2840 0.3350 0.3335 -0.0098 -0.0101 -0.0353 405 GLU A C   
3292  O O   . GLU A 405 ? 0.3083 0.3532 0.3612 -0.0136 -0.0155 -0.0374 405 GLU A O   
3293  C CB  . GLU A 405 ? 0.3233 0.3924 0.3850 -0.0068 -0.0024 -0.0201 405 GLU A CB  
3294  C CG  . GLU A 405 ? 0.3640 0.4438 0.4235 -0.0004 0.0046  -0.0161 405 GLU A CG  
3295  C CD  . GLU A 405 ? 0.4520 0.5440 0.5210 0.0022  0.0101  -0.0030 405 GLU A CD  
3296  O OE1 . GLU A 405 ? 0.4191 0.5107 0.4933 -0.0002 0.0093  0.0029  405 GLU A OE1 
3297  O OE2 . GLU A 405 ? 0.3950 0.4977 0.4665 0.0075  0.0160  0.0024  405 GLU A OE2 
3298  N N   . GLY A 406 ? 0.2908 0.3398 0.3341 -0.0069 -0.0085 -0.0371 406 GLY A N   
3299  C CA  . GLY A 406 ? 0.2874 0.3279 0.3308 -0.0075 -0.0117 -0.0396 406 GLY A CA  
3300  C C   . GLY A 406 ? 0.2516 0.2933 0.2925 -0.0041 -0.0095 -0.0373 406 GLY A C   
3301  O O   . GLY A 406 ? 0.2695 0.3184 0.3093 -0.0020 -0.0062 -0.0323 406 GLY A O   
3302  N N   . ASN A 407 ? 0.2761 0.3105 0.3159 -0.0027 -0.0115 -0.0405 407 ASN A N   
3303  C CA  . ASN A 407 ? 0.2531 0.2889 0.2916 0.0010  -0.0101 -0.0385 407 ASN A CA  
3304  C C   . ASN A 407 ? 0.2837 0.3145 0.3189 0.0041  -0.0108 -0.0445 407 ASN A C   
3305  O O   . ASN A 407 ? 0.2642 0.2846 0.2998 0.0047  -0.0134 -0.0478 407 ASN A O   
3306  C CB  . ASN A 407 ? 0.2389 0.2715 0.2857 0.0004  -0.0109 -0.0304 407 ASN A CB  
3307  C CG  . ASN A 407 ? 0.2469 0.2827 0.2928 0.0043  -0.0097 -0.0264 407 ASN A CG  
3308  O OD1 . ASN A 407 ? 0.2506 0.2850 0.2936 0.0076  -0.0100 -0.0305 407 ASN A OD1 
3309  N ND2 . ASN A 407 ? 0.2299 0.2715 0.2793 0.0046  -0.0080 -0.0167 407 ASN A ND2 
3310  N N   . MET A 408 ? 0.2704 0.3082 0.3024 0.0066  -0.0091 -0.0455 408 MET A N   
3311  C CA  . MET A 408 ? 0.2596 0.2971 0.2898 0.0105  -0.0080 -0.0493 408 MET A CA  
3312  C C   . MET A 408 ? 0.2712 0.3016 0.3036 0.0157  -0.0080 -0.0488 408 MET A C   
3313  O O   . MET A 408 ? 0.3015 0.3267 0.3303 0.0206  -0.0071 -0.0534 408 MET A O   
3314  C CB  . MET A 408 ? 0.2807 0.3296 0.3120 0.0111  -0.0070 -0.0473 408 MET A CB  
3315  C CG  . MET A 408 ? 0.2986 0.3533 0.3342 0.0130  -0.0079 -0.0422 408 MET A CG  
3316  S SD  . MET A 408 ? 0.2612 0.3164 0.2945 0.0109  -0.0101 -0.0381 408 MET A SD  
3317  C CE  . MET A 408 ? 0.2488 0.3119 0.2867 0.0141  -0.0121 -0.0329 408 MET A CE  
3318  N N   . GLY A 409 ? 0.2660 0.2959 0.3034 0.0157  -0.0089 -0.0432 409 GLY A N   
3319  C CA  . GLY A 409 ? 0.2908 0.3131 0.3317 0.0212  -0.0091 -0.0421 409 GLY A CA  
3320  C C   . GLY A 409 ? 0.3140 0.3213 0.3587 0.0196  -0.0129 -0.0412 409 GLY A C   
3321  O O   . GLY A 409 ? 0.3330 0.3283 0.3787 0.0250  -0.0142 -0.0435 409 GLY A O   
3322  N N   . ASP A 410 ? 0.2723 0.2797 0.3204 0.0129  -0.0149 -0.0376 410 ASP A N   
3323  C CA  . ASP A 410 ? 0.2702 0.2661 0.3271 0.0095  -0.0193 -0.0329 410 ASP A CA  
3324  C C   . ASP A 410 ? 0.2901 0.2803 0.3474 0.0036  -0.0234 -0.0366 410 ASP A C   
3325  O O   . ASP A 410 ? 0.2888 0.2892 0.3494 -0.0013 -0.0220 -0.0317 410 ASP A O   
3326  C CB  . ASP A 410 ? 0.2741 0.2800 0.3388 0.0072  -0.0175 -0.0204 410 ASP A CB  
3327  C CG  . ASP A 410 ? 0.3121 0.3078 0.3898 0.0041  -0.0217 -0.0121 410 ASP A CG  
3328  O OD1 . ASP A 410 ? 0.3135 0.2929 0.3945 0.0017  -0.0280 -0.0173 410 ASP A OD1 
3329  O OD2 . ASP A 410 ? 0.2918 0.2962 0.3758 0.0040  -0.0194 0.0001  410 ASP A OD2 
3330  N N   A GLU A 411 ? 0.3205 0.2941 0.3741 0.0048  -0.0289 -0.0452 411 GLU A N   
3331  N N   B GLU A 411 ? 0.3206 0.2941 0.3740 0.0050  -0.0289 -0.0453 411 GLU A N   
3332  C CA  A GLU A 411 ? 0.3521 0.3216 0.4049 -0.0011 -0.0341 -0.0491 411 GLU A CA  
3333  C CA  B GLU A 411 ? 0.3537 0.3206 0.4063 -0.0006 -0.0349 -0.0498 411 GLU A CA  
3334  C C   A GLU A 411 ? 0.3274 0.2938 0.3965 -0.0096 -0.0401 -0.0397 411 GLU A C   
3335  C C   B GLU A 411 ? 0.3273 0.2942 0.3962 -0.0095 -0.0398 -0.0396 411 GLU A C   
3336  O O   A GLU A 411 ? 0.3226 0.2869 0.3951 -0.0157 -0.0459 -0.0407 411 GLU A O   
3337  O O   B GLU A 411 ? 0.3231 0.2908 0.3952 -0.0155 -0.0443 -0.0400 411 GLU A O   
3338  C CB  A GLU A 411 ? 0.3933 0.3460 0.4334 0.0037  -0.0392 -0.0620 411 GLU A CB  
3339  C CB  B GLU A 411 ? 0.3789 0.3250 0.4213 0.0040  -0.0414 -0.0618 411 GLU A CB  
3340  C CG  A GLU A 411 ? 0.3996 0.3624 0.4262 0.0113  -0.0315 -0.0678 411 GLU A CG  
3341  C CG  B GLU A 411 ? 0.4166 0.3411 0.4665 0.0034  -0.0501 -0.0616 411 GLU A CG  
3342  C CD  A GLU A 411 ? 0.4232 0.3859 0.4373 0.0117  -0.0330 -0.0759 411 GLU A CD  
3343  C CD  B GLU A 411 ? 0.4699 0.3706 0.5070 0.0065  -0.0599 -0.0756 411 GLU A CD  
3344  O OE1 A GLU A 411 ? 0.4452 0.3993 0.4599 0.0060  -0.0410 -0.0782 411 GLU A OE1 
3345  O OE1 B GLU A 411 ? 0.5033 0.4048 0.5223 0.0133  -0.0573 -0.0859 411 GLU A OE1 
3346  O OE2 A GLU A 411 ? 0.3927 0.3655 0.3979 0.0174  -0.0264 -0.0783 411 GLU A OE2 
3347  O OE2 B GLU A 411 ? 0.4562 0.3371 0.5013 0.0023  -0.0710 -0.0758 411 GLU A OE2 
3348  N N   . ARG A 412 ? 0.3288 0.2968 0.4099 -0.0105 -0.0391 -0.0287 412 ARG A N   
3349  C CA  . ARG A 412 ? 0.3231 0.2948 0.4226 -0.0188 -0.0426 -0.0157 412 ARG A CA  
3350  C C   . ARG A 412 ? 0.3223 0.3148 0.4232 -0.0214 -0.0365 -0.0100 412 ARG A C   
3351  O O   . ARG A 412 ? 0.3029 0.3006 0.4186 -0.0282 -0.0395 -0.0008 412 ARG A O   
3352  C CB  . ARG A 412 ? 0.3262 0.3005 0.4379 -0.0182 -0.0404 -0.0021 412 ARG A CB  
3353  C CG  . ARG A 412 ? 0.3606 0.3109 0.4773 -0.0174 -0.0490 -0.0049 412 ARG A CG  
3354  C CD  . ARG A 412 ? 0.3428 0.2964 0.4716 -0.0159 -0.0464 0.0096  412 ARG A CD  
3355  N NE  . ARG A 412 ? 0.3197 0.2844 0.4358 -0.0071 -0.0374 0.0079  412 ARG A NE  
3356  C CZ  . ARG A 412 ? 0.3317 0.2972 0.4526 -0.0029 -0.0354 0.0167  412 ARG A CZ  
3357  N NH1 . ARG A 412 ? 0.3230 0.2781 0.4612 -0.0063 -0.0409 0.0280  412 ARG A NH1 
3358  N NH2 . ARG A 412 ? 0.3290 0.3062 0.4387 0.0044  -0.0287 0.0148  412 ARG A NH2 
3359  N N   . GLU A 413 ? 0.2927 0.2971 0.3798 -0.0159 -0.0283 -0.0146 413 GLU A N   
3360  C CA  . GLU A 413 ? 0.3007 0.3225 0.3860 -0.0161 -0.0223 -0.0111 413 GLU A CA  
3361  C C   . GLU A 413 ? 0.3224 0.3431 0.3975 -0.0161 -0.0233 -0.0222 413 GLU A C   
3362  O O   . GLU A 413 ? 0.3033 0.3354 0.3729 -0.0142 -0.0180 -0.0226 413 GLU A O   
3363  C CB  . GLU A 413 ? 0.2777 0.3121 0.3550 -0.0102 -0.0141 -0.0075 413 GLU A CB  
3364  C CG  . GLU A 413 ? 0.2976 0.3381 0.3856 -0.0102 -0.0119 0.0072  413 GLU A CG  
3365  C CD  . GLU A 413 ? 0.3693 0.4236 0.4465 -0.0037 -0.0046 0.0113  413 GLU A CD  
3366  O OE1 . GLU A 413 ? 0.3272 0.3811 0.3904 0.0003  -0.0037 0.0019  413 GLU A OE1 
3367  O OE2 . GLU A 413 ? 0.4090 0.4743 0.4922 -0.0023 -0.0004 0.0249  413 GLU A OE2 
3368  N N   . PHE A 414 ? 0.2709 0.2775 0.3432 -0.0178 -0.0305 -0.0307 414 PHE A N   
3369  C CA  . PHE A 414 ? 0.3003 0.3070 0.3636 -0.0181 -0.0321 -0.0391 414 PHE A CA  
3370  C C   . PHE A 414 ? 0.3835 0.3803 0.4535 -0.0243 -0.0425 -0.0404 414 PHE A C   
3371  O O   . PHE A 414 ? 0.3617 0.3414 0.4322 -0.0254 -0.0506 -0.0444 414 PHE A O   
3372  C CB  . PHE A 414 ? 0.3179 0.3193 0.3654 -0.0116 -0.0301 -0.0497 414 PHE A CB  
3373  C CG  . PHE A 414 ? 0.3447 0.3468 0.3824 -0.0113 -0.0314 -0.0570 414 PHE A CG  
3374  C CD1 . PHE A 414 ? 0.3385 0.3536 0.3764 -0.0125 -0.0273 -0.0544 414 PHE A CD1 
3375  C CD2 . PHE A 414 ? 0.3836 0.3728 0.4108 -0.0088 -0.0369 -0.0660 414 PHE A CD2 
3376  C CE1 . PHE A 414 ? 0.3541 0.3704 0.3843 -0.0122 -0.0286 -0.0592 414 PHE A CE1 
3377  C CE2 . PHE A 414 ? 0.4008 0.3922 0.4177 -0.0078 -0.0379 -0.0712 414 PHE A CE2 
3378  C CZ  . PHE A 414 ? 0.3747 0.3806 0.3945 -0.0100 -0.0336 -0.0669 414 PHE A CZ  
3379  N N   . ASP A 415 ? 0.3197 0.3258 0.3948 -0.0283 -0.0434 -0.0373 415 ASP A N   
3380  C CA  . ASP A 415 ? 0.3894 0.3892 0.4730 -0.0353 -0.0546 -0.0368 415 ASP A CA  
3381  C C   . ASP A 415 ? 0.3995 0.3946 0.4660 -0.0328 -0.0576 -0.0483 415 ASP A C   
3382  O O   . ASP A 415 ? 0.3571 0.3649 0.4213 -0.0318 -0.0528 -0.0472 415 ASP A O   
3383  C CB  . ASP A 415 ? 0.4041 0.4207 0.5073 -0.0406 -0.0531 -0.0231 415 ASP A CB  
3384  C CG  . ASP A 415 ? 0.3688 0.3804 0.4873 -0.0497 -0.0665 -0.0191 415 ASP A CG  
3385  O OD1 . ASP A 415 ? 0.3587 0.3564 0.4670 -0.0515 -0.0770 -0.0297 415 ASP A OD1 
3386  O OD2 . ASP A 415 ? 0.4331 0.4554 0.5745 -0.0553 -0.0672 -0.0044 415 ASP A OD2 
3387  N N   . GLU A 416 ? 0.4165 0.3934 0.4704 -0.0308 -0.0653 -0.0591 416 GLU A N   
3388  C CA  . GLU A 416 ? 0.3845 0.3576 0.4195 -0.0268 -0.0676 -0.0694 416 GLU A CA  
3389  C C   . GLU A 416 ? 0.3874 0.3658 0.4280 -0.0333 -0.0755 -0.0668 416 GLU A C   
3390  O O   . GLU A 416 ? 0.3863 0.3734 0.4175 -0.0307 -0.0723 -0.0688 416 GLU A O   
3391  C CB  . GLU A 416 ? 0.4948 0.4457 0.5137 -0.0219 -0.0753 -0.0816 416 GLU A CB  
3392  C CG  . GLU A 416 ? 0.5493 0.4968 0.5620 -0.0137 -0.0668 -0.0842 416 GLU A CG  
3393  C CD  . GLU A 416 ? 0.6586 0.5849 0.6523 -0.0057 -0.0724 -0.0971 416 GLU A CD  
3394  O OE1 . GLU A 416 ? 0.6882 0.6002 0.6860 -0.0039 -0.0751 -0.0982 416 GLU A OE1 
3395  O OE2 . GLU A 416 ? 0.6165 0.5403 0.5911 -0.0005 -0.0742 -0.1056 416 GLU A OE2 
3396  N N   . VAL A 417 ? 0.3551 0.3286 0.4125 -0.0419 -0.0865 -0.0612 417 VAL A N   
3397  C CA  . VAL A 417 ? 0.3954 0.3734 0.4604 -0.0487 -0.0967 -0.0581 417 VAL A CA  
3398  C C   . VAL A 417 ? 0.3537 0.3557 0.4302 -0.0491 -0.0866 -0.0474 417 VAL A C   
3399  O O   . VAL A 417 ? 0.3489 0.3578 0.4193 -0.0484 -0.0877 -0.0488 417 VAL A O   
3400  C CB  . VAL A 417 ? 0.4194 0.3879 0.5046 -0.0590 -0.1116 -0.0523 417 VAL A CB  
3401  C CG1 . VAL A 417 ? 0.3929 0.3708 0.4912 -0.0670 -0.1219 -0.0459 417 VAL A CG1 
3402  C CG2 . VAL A 417 ? 0.4608 0.4006 0.5298 -0.0574 -0.1241 -0.0662 417 VAL A CG2 
3403  N N   . ARG A 418 ? 0.2904 0.3048 0.3828 -0.0493 -0.0770 -0.0366 418 ARG A N   
3404  C CA  . ARG A 418 ? 0.3163 0.3515 0.4181 -0.0475 -0.0671 -0.0272 418 ARG A CA  
3405  C C   . ARG A 418 ? 0.3097 0.3480 0.3926 -0.0397 -0.0577 -0.0346 418 ARG A C   
3406  O O   . ARG A 418 ? 0.2848 0.3335 0.3689 -0.0385 -0.0553 -0.0321 418 ARG A O   
3407  C CB  . ARG A 418 ? 0.3163 0.3628 0.4340 -0.0469 -0.0580 -0.0153 418 ARG A CB  
3408  C CG  . ARG A 418 ? 0.3601 0.4115 0.5046 -0.0557 -0.0659 -0.0017 418 ARG A CG  
3409  C CD  . ARG A 418 ? 0.3772 0.4443 0.5371 -0.0534 -0.0547 0.0130  418 ARG A CD  
3410  N NE  . ARG A 418 ? 0.4472 0.5241 0.6369 -0.0618 -0.0611 0.0296  418 ARG A NE  
3411  C CZ  . ARG A 418 ? 0.4781 0.5435 0.6814 -0.0700 -0.0720 0.0339  418 ARG A CZ  
3412  N NH1 . ARG A 418 ? 0.4786 0.5218 0.6668 -0.0694 -0.0766 0.0222  418 ARG A NH1 
3413  N NH2 . ARG A 418 ? 0.3923 0.4686 0.6264 -0.0788 -0.0787 0.0512  418 ARG A NH2 
3414  N N   . THR A 419 ? 0.2928 0.3230 0.3607 -0.0344 -0.0526 -0.0424 419 THR A N   
3415  C CA  . THR A 419 ? 0.3317 0.3656 0.3854 -0.0281 -0.0446 -0.0474 419 THR A CA  
3416  C C   . THR A 419 ? 0.2972 0.3288 0.3394 -0.0276 -0.0499 -0.0529 419 THR A C   
3417  O O   . THR A 419 ? 0.2914 0.3318 0.3318 -0.0255 -0.0455 -0.0510 419 THR A O   
3418  C CB  . THR A 419 ? 0.3384 0.3655 0.3813 -0.0232 -0.0396 -0.0531 419 THR A CB  
3419  O OG1 . THR A 419 ? 0.3606 0.3920 0.4128 -0.0229 -0.0343 -0.0469 419 THR A OG1 
3420  C CG2 . THR A 419 ? 0.3025 0.3344 0.3338 -0.0178 -0.0326 -0.0566 419 THR A CG2 
3421  N N   . GLN A 420 ? 0.2999 0.3190 0.3333 -0.0290 -0.0598 -0.0596 420 GLN A N   
3422  C CA  . GLN A 420 ? 0.3398 0.3579 0.3593 -0.0274 -0.0648 -0.0643 420 GLN A CA  
3423  C C   . GLN A 420 ? 0.3561 0.3850 0.3882 -0.0324 -0.0693 -0.0567 420 GLN A C   
3424  O O   . GLN A 420 ? 0.3351 0.3710 0.3606 -0.0300 -0.0677 -0.0559 420 GLN A O   
3425  C CB  . GLN A 420 ? 0.4270 0.4275 0.4306 -0.0262 -0.0755 -0.0747 420 GLN A CB  
3426  C CG  . GLN A 420 ? 0.4979 0.4976 0.4866 -0.0249 -0.0830 -0.0787 420 GLN A CG  
3427  C CD  . GLN A 420 ? 0.6098 0.5935 0.5717 -0.0174 -0.0878 -0.0915 420 GLN A CD  
3428  O OE1 . GLN A 420 ? 0.6463 0.6205 0.6014 -0.0120 -0.0834 -0.0971 420 GLN A OE1 
3429  N NE2 . GLN A 420 ? 0.6547 0.6348 0.6009 -0.0163 -0.0973 -0.0961 420 GLN A NE2 
3430  N N   . ALA A 421 ? 0.3270 0.3591 0.3792 -0.0391 -0.0745 -0.0492 421 ALA A N   
3431  C CA  . ALA A 421 ? 0.2929 0.3382 0.3604 -0.0430 -0.0778 -0.0399 421 ALA A CA  
3432  C C   . ALA A 421 ? 0.3377 0.3969 0.4094 -0.0378 -0.0647 -0.0343 421 ALA A C   
3433  O O   . ALA A 421 ? 0.3147 0.3821 0.3879 -0.0369 -0.0652 -0.0307 421 ALA A O   
3434  C CB  . ALA A 421 ? 0.3087 0.3582 0.4007 -0.0507 -0.0845 -0.0303 421 ALA A CB  
3435  N N   . ARG A 422 ? 0.2569 0.3175 0.3298 -0.0340 -0.0538 -0.0336 422 ARG A N   
3436  C CA  . ARG A 422 ? 0.2704 0.3401 0.3445 -0.0284 -0.0432 -0.0304 422 ARG A CA  
3437  C C   . ARG A 422 ? 0.3166 0.3836 0.3755 -0.0249 -0.0416 -0.0358 422 ARG A C   
3438  O O   . ARG A 422 ? 0.2771 0.3504 0.3391 -0.0222 -0.0380 -0.0321 422 ARG A O   
3439  C CB  . ARG A 422 ? 0.2903 0.3601 0.3646 -0.0246 -0.0339 -0.0301 422 ARG A CB  
3440  C CG  . ARG A 422 ? 0.2468 0.3233 0.3378 -0.0267 -0.0328 -0.0213 422 ARG A CG  
3441  C CD  . ARG A 422 ? 0.2796 0.3562 0.3664 -0.0216 -0.0235 -0.0214 422 ARG A CD  
3442  N NE  . ARG A 422 ? 0.2771 0.3590 0.3595 -0.0144 -0.0151 -0.0214 422 ARG A NE  
3443  C CZ  . ARG A 422 ? 0.2657 0.3588 0.3577 -0.0099 -0.0093 -0.0135 422 ARG A CZ  
3444  N NH1 . ARG A 422 ? 0.2574 0.3613 0.3672 -0.0127 -0.0102 -0.0025 422 ARG A NH1 
3445  N NH2 . ARG A 422 ? 0.2913 0.3848 0.3757 -0.0021 -0.0029 -0.0160 422 ARG A NH2 
3446  N N   . VAL A 423 ? 0.2910 0.3489 0.3345 -0.0239 -0.0431 -0.0435 423 VAL A N   
3447  C CA  . VAL A 423 ? 0.3252 0.3834 0.3562 -0.0201 -0.0401 -0.0461 423 VAL A CA  
3448  C C   . VAL A 423 ? 0.2978 0.3592 0.3251 -0.0213 -0.0470 -0.0442 423 VAL A C   
3449  O O   . VAL A 423 ? 0.3109 0.3779 0.3366 -0.0191 -0.0442 -0.0406 423 VAL A O   
3450  C CB  . VAL A 423 ? 0.3663 0.4170 0.3831 -0.0170 -0.0382 -0.0532 423 VAL A CB  
3451  C CG1 . VAL A 423 ? 0.3814 0.4351 0.3860 -0.0131 -0.0360 -0.0536 423 VAL A CG1 
3452  C CG2 . VAL A 423 ? 0.3500 0.4000 0.3711 -0.0155 -0.0312 -0.0534 423 VAL A CG2 
3453  N N   . ASP A 424 ? 0.2996 0.3573 0.3269 -0.0252 -0.0572 -0.0457 424 ASP A N   
3454  C CA  . ASP A 424 ? 0.3456 0.4074 0.3701 -0.0267 -0.0654 -0.0431 424 ASP A CA  
3455  C C   . ASP A 424 ? 0.3107 0.3846 0.3535 -0.0280 -0.0638 -0.0330 424 ASP A C   
3456  O O   . ASP A 424 ? 0.3125 0.3925 0.3530 -0.0266 -0.0652 -0.0288 424 ASP A O   
3457  C CB  . ASP A 424 ? 0.3647 0.4184 0.3855 -0.0313 -0.0794 -0.0474 424 ASP A CB  
3458  C CG  . ASP A 424 ? 0.4408 0.4968 0.4503 -0.0311 -0.0886 -0.0472 424 ASP A CG  
3459  O OD1 . ASP A 424 ? 0.4552 0.5067 0.4418 -0.0255 -0.0880 -0.0533 424 ASP A OD1 
3460  O OD2 . ASP A 424 ? 0.4397 0.5035 0.4634 -0.0360 -0.0963 -0.0399 424 ASP A OD2 
3461  N N   . ALA A 425 ? 0.2993 0.3776 0.3600 -0.0297 -0.0604 -0.0281 425 ALA A N   
3462  C CA  . ALA A 425 ? 0.2930 0.3830 0.3702 -0.0282 -0.0569 -0.0186 425 ALA A CA  
3463  C C   . ALA A 425 ? 0.2627 0.3529 0.3345 -0.0222 -0.0479 -0.0186 425 ALA A C   
3464  O O   . ALA A 425 ? 0.2699 0.3666 0.3486 -0.0201 -0.0475 -0.0124 425 ALA A O   
3465  C CB  . ALA A 425 ? 0.2820 0.3781 0.3775 -0.0287 -0.0526 -0.0128 425 ALA A CB  
3466  N N   . PHE A 426 ? 0.2657 0.3487 0.3273 -0.0198 -0.0416 -0.0248 426 PHE A N   
3467  C CA  . PHE A 426 ? 0.2714 0.3530 0.3296 -0.0156 -0.0352 -0.0245 426 PHE A CA  
3468  C C   . PHE A 426 ? 0.2596 0.3432 0.3102 -0.0156 -0.0385 -0.0220 426 PHE A C   
3469  O O   . PHE A 426 ? 0.3042 0.3900 0.3598 -0.0133 -0.0364 -0.0168 426 PHE A O   
3470  C CB  . PHE A 426 ? 0.2591 0.3337 0.3093 -0.0144 -0.0300 -0.0307 426 PHE A CB  
3471  C CG  . PHE A 426 ? 0.2612 0.3331 0.3125 -0.0112 -0.0249 -0.0300 426 PHE A CG  
3472  C CD1 . PHE A 426 ? 0.2770 0.3490 0.3370 -0.0078 -0.0223 -0.0273 426 PHE A CD1 
3473  C CD2 . PHE A 426 ? 0.2968 0.3656 0.3408 -0.0112 -0.0232 -0.0320 426 PHE A CD2 
3474  C CE1 . PHE A 426 ? 0.2806 0.3461 0.3408 -0.0048 -0.0198 -0.0282 426 PHE A CE1 
3475  C CE2 . PHE A 426 ? 0.2918 0.3567 0.3393 -0.0098 -0.0210 -0.0310 426 PHE A CE2 
3476  C CZ  . PHE A 426 ? 0.2757 0.3371 0.3304 -0.0069 -0.0202 -0.0299 426 PHE A CZ  
3477  N N   . MET A 427 ? 0.2531 0.3356 0.2911 -0.0172 -0.0440 -0.0253 427 MET A N   
3478  C CA  . MET A 427 ? 0.2699 0.3561 0.2978 -0.0157 -0.0462 -0.0221 427 MET A CA  
3479  C C   . MET A 427 ? 0.2838 0.3775 0.3213 -0.0167 -0.0517 -0.0141 427 MET A C   
3480  O O   . MET A 427 ? 0.2747 0.3731 0.3136 -0.0147 -0.0504 -0.0071 427 MET A O   
3481  C CB  . MET A 427 ? 0.3109 0.3931 0.3199 -0.0153 -0.0514 -0.0289 427 MET A CB  
3482  C CG  . MET A 427 ? 0.3599 0.4382 0.3565 -0.0116 -0.0449 -0.0340 427 MET A CG  
3483  S SD  . MET A 427 ? 0.4456 0.5290 0.4469 -0.0088 -0.0344 -0.0280 427 MET A SD  
3484  C CE  . MET A 427 ? 0.3282 0.4058 0.3445 -0.0111 -0.0301 -0.0307 427 MET A CE  
3485  N N   . GLU A 428 ? 0.2562 0.3519 0.3032 -0.0201 -0.0580 -0.0135 428 GLU A N   
3486  C CA  . GLU A 428 ? 0.2688 0.3737 0.3289 -0.0209 -0.0632 -0.0046 428 GLU A CA  
3487  C C   . GLU A 428 ? 0.2556 0.3634 0.3298 -0.0167 -0.0549 0.0018  428 GLU A C   
3488  O O   . GLU A 428 ? 0.2575 0.3706 0.3364 -0.0147 -0.0561 0.0094  428 GLU A O   
3489  C CB  . GLU A 428 ? 0.2654 0.3738 0.3384 -0.0257 -0.0707 -0.0032 428 GLU A CB  
3490  C CG  . GLU A 428 ? 0.2476 0.3683 0.3381 -0.0264 -0.0756 0.0078  428 GLU A CG  
3491  C CD  . GLU A 428 ? 0.2483 0.3749 0.3541 -0.0327 -0.0854 0.0114  428 GLU A CD  
3492  O OE1 . GLU A 428 ? 0.2388 0.3658 0.3566 -0.0338 -0.0810 0.0117  428 GLU A OE1 
3493  O OE2 . GLU A 428 ? 0.2764 0.4075 0.3824 -0.0367 -0.0981 0.0148  428 GLU A OE2 
3494  N N   . GLN A 429 ? 0.2570 0.3604 0.3370 -0.0146 -0.0472 -0.0015 429 GLN A N   
3495  C CA  . GLN A 429 ? 0.2748 0.3769 0.3646 -0.0089 -0.0399 0.0018  429 GLN A CA  
3496  C C   . GLN A 429 ? 0.2655 0.3628 0.3495 -0.0072 -0.0384 0.0036  429 GLN A C   
3497  O O   . GLN A 429 ? 0.2617 0.3597 0.3551 -0.0036 -0.0376 0.0101  429 GLN A O   
3498  C CB  . GLN A 429 ? 0.2500 0.3460 0.3399 -0.0064 -0.0328 -0.0043 429 GLN A CB  
3499  C CG  . GLN A 429 ? 0.2395 0.3295 0.3338 0.0005  -0.0267 -0.0038 429 GLN A CG  
3500  C CD  . GLN A 429 ? 0.3139 0.3959 0.4030 0.0037  -0.0207 -0.0111 429 GLN A CD  
3501  O OE1 . GLN A 429 ? 0.3189 0.3911 0.4057 0.0083  -0.0180 -0.0141 429 GLN A OE1 
3502  N NE2 . GLN A 429 ? 0.2871 0.3723 0.3743 0.0014  -0.0197 -0.0139 429 GLN A NE2 
3503  N N   . LEU A 430 ? 0.2545 0.3477 0.3251 -0.0094 -0.0378 -0.0009 430 LEU A N   
3504  C CA  . LEU A 430 ? 0.2638 0.3550 0.3320 -0.0086 -0.0362 0.0035  430 LEU A CA  
3505  C C   . LEU A 430 ? 0.3221 0.4217 0.3909 -0.0086 -0.0409 0.0131  430 LEU A C   
3506  O O   . LEU A 430 ? 0.3130 0.4120 0.3895 -0.0069 -0.0401 0.0210  430 LEU A O   
3507  C CB  . LEU A 430 ? 0.2859 0.3751 0.3417 -0.0102 -0.0338 -0.0009 430 LEU A CB  
3508  C CG  . LEU A 430 ? 0.2588 0.3399 0.3153 -0.0100 -0.0296 -0.0088 430 LEU A CG  
3509  C CD1 . LEU A 430 ? 0.2894 0.3708 0.3362 -0.0110 -0.0274 -0.0110 430 LEU A CD1 
3510  C CD2 . LEU A 430 ? 0.2891 0.3616 0.3562 -0.0077 -0.0273 -0.0085 430 LEU A CD2 
3511  N N   . GLY A 431 ? 0.2988 0.4051 0.3593 -0.0104 -0.0470 0.0127  431 GLY A N   
3512  C CA  . GLY A 431 ? 0.3309 0.4461 0.3916 -0.0101 -0.0530 0.0221  431 GLY A CA  
3513  C C   . GLY A 431 ? 0.3271 0.4457 0.4073 -0.0081 -0.0540 0.0302  431 GLY A C   
3514  O O   . GLY A 431 ? 0.3059 0.4283 0.3915 -0.0061 -0.0551 0.0403  431 GLY A O   
3515  N N   . VAL A 432 ? 0.2403 0.3589 0.3321 -0.0077 -0.0535 0.0274  432 VAL A N   
3516  C CA  . VAL A 432 ? 0.2824 0.4061 0.3935 -0.0037 -0.0533 0.0357  432 VAL A CA  
3517  C C   . VAL A 432 ? 0.2771 0.3916 0.3945 0.0016  -0.0471 0.0384  432 VAL A C   
3518  O O   . VAL A 432 ? 0.2604 0.3777 0.3888 0.0052  -0.0484 0.0480  432 VAL A O   
3519  C CB  . VAL A 432 ? 0.2936 0.4205 0.4161 -0.0028 -0.0513 0.0330  432 VAL A CB  
3520  C CG1 . VAL A 432 ? 0.2474 0.3785 0.3889 0.0045  -0.0473 0.0408  432 VAL A CG1 
3521  C CG2 . VAL A 432 ? 0.2174 0.3537 0.3399 -0.0093 -0.0608 0.0337  432 VAL A CG2 
3522  N N   . ARG A 433 ? 0.2585 0.3612 0.3700 0.0021  -0.0413 0.0300  433 ARG A N   
3523  C CA  . ARG A 433 ? 0.2762 0.3665 0.3930 0.0062  -0.0377 0.0307  433 ARG A CA  
3524  C C   . ARG A 433 ? 0.2991 0.3901 0.4163 0.0042  -0.0408 0.0403  433 ARG A C   
3525  O O   . ARG A 433 ? 0.2908 0.3755 0.4193 0.0078  -0.0412 0.0469  433 ARG A O   
3526  C CB  . ARG A 433 ? 0.2990 0.3777 0.4074 0.0052  -0.0336 0.0198  433 ARG A CB  
3527  C CG  . ARG A 433 ? 0.3178 0.3926 0.4282 0.0104  -0.0291 0.0122  433 ARG A CG  
3528  C CD  . ARG A 433 ? 0.3505 0.4154 0.4509 0.0089  -0.0264 0.0023  433 ARG A CD  
3529  N NE  . ARG A 433 ? 0.4037 0.4665 0.5026 0.0140  -0.0217 -0.0045 433 ARG A NE  
3530  C CZ  . ARG A 433 ? 0.4178 0.4683 0.5160 0.0214  -0.0189 -0.0095 433 ARG A CZ  
3531  N NH1 . ARG A 433 ? 0.3569 0.3946 0.4584 0.0240  -0.0216 -0.0084 433 ARG A NH1 
3532  N NH2 . ARG A 433 ? 0.3884 0.4380 0.4812 0.0264  -0.0139 -0.0157 433 ARG A NH2 
3533  N N   . ARG A 434 ? 0.2676 0.3668 0.3728 -0.0007 -0.0430 0.0422  434 ARG A N   
3534  C CA  . ARG A 434 ? 0.2945 0.3982 0.3995 -0.0018 -0.0449 0.0540  434 ARG A CA  
3535  C C   . ARG A 434 ? 0.3459 0.4581 0.4599 0.0006  -0.0496 0.0655  434 ARG A C   
3536  O O   . ARG A 434 ? 0.3100 0.4206 0.4339 0.0021  -0.0503 0.0768  434 ARG A O   
3537  C CB  . ARG A 434 ? 0.3546 0.4669 0.4414 -0.0050 -0.0448 0.0529  434 ARG A CB  
3538  C CG  . ARG A 434 ? 0.4504 0.5717 0.5341 -0.0052 -0.0451 0.0669  434 ARG A CG  
3539  C CD  . ARG A 434 ? 0.5845 0.7180 0.6457 -0.0047 -0.0467 0.0661  434 ARG A CD  
3540  N NE  . ARG A 434 ? 0.6228 0.7606 0.6772 -0.0045 -0.0540 0.0618  434 ARG A NE  
3541  C CZ  . ARG A 434 ? 0.6222 0.7586 0.6628 -0.0056 -0.0570 0.0497  434 ARG A CZ  
3542  N NH1 . ARG A 434 ? 0.6057 0.7369 0.6352 -0.0058 -0.0523 0.0399  434 ARG A NH1 
3543  N NH2 . ARG A 434 ? 0.5742 0.7142 0.6142 -0.0068 -0.0657 0.0479  434 ARG A NH2 
3544  N N   . GLN A 435 ? 0.3195 0.4411 0.4321 0.0007  -0.0538 0.0642  435 GLN A N   
3545  C CA  . GLN A 435 ? 0.3330 0.4646 0.4559 0.0030  -0.0593 0.0758  435 GLN A CA  
3546  C C   . GLN A 435 ? 0.3424 0.4667 0.4859 0.0092  -0.0563 0.0804  435 GLN A C   
3547  O O   . GLN A 435 ? 0.3101 0.4364 0.4639 0.0120  -0.0586 0.0927  435 GLN A O   
3548  C CB  . GLN A 435 ? 0.3066 0.4491 0.4271 0.0008  -0.0657 0.0730  435 GLN A CB  
3549  C CG  . GLN A 435 ? 0.3887 0.5353 0.4867 -0.0039 -0.0705 0.0677  435 GLN A CG  
3550  C CD  . GLN A 435 ? 0.4294 0.5861 0.5172 -0.0037 -0.0767 0.0781  435 GLN A CD  
3551  O OE1 . GLN A 435 ? 0.4553 0.6168 0.5548 -0.0009 -0.0776 0.0912  435 GLN A OE1 
3552  N NE2 . GLN A 435 ? 0.5267 0.6860 0.5908 -0.0056 -0.0809 0.0725  435 GLN A NE2 
3553  N N   . ALA A 436 ? 0.2854 0.4011 0.4342 0.0125  -0.0512 0.0707  436 ALA A N   
3554  C CA  . ALA A 436 ? 0.2805 0.3867 0.4450 0.0210  -0.0476 0.0729  436 ALA A CA  
3555  C C   . ALA A 436 ? 0.3558 0.4463 0.5230 0.0219  -0.0472 0.0762  436 ALA A C   
3556  O O   . ALA A 436 ? 0.4120 0.4982 0.5926 0.0272  -0.0486 0.0854  436 ALA A O   
3557  C CB  . ALA A 436 ? 0.2776 0.3771 0.4421 0.0256  -0.0413 0.0611  436 ALA A CB  
3558  N N   . ALA A 437 ? 0.2863 0.3683 0.4429 0.0165  -0.0460 0.0700  437 ALA A N   
3559  C CA  . ALA A 437 ? 0.3908 0.4576 0.5537 0.0159  -0.0471 0.0743  437 ALA A CA  
3560  C C   . ALA A 437 ? 0.4254 0.5009 0.5955 0.0139  -0.0511 0.0917  437 ALA A C   
3561  O O   . ALA A 437 ? 0.4764 0.5410 0.6607 0.0169  -0.0534 0.1002  437 ALA A O   
3562  C CB  . ALA A 437 ? 0.3429 0.4034 0.4958 0.0095  -0.0457 0.0669  437 ALA A CB  
3563  N N   . SER A 438 ? 0.4161 0.5104 0.5755 0.0095  -0.0526 0.0973  438 SER A N   
3564  C CA  . SER A 438 ? 0.4102 0.5156 0.5735 0.0087  -0.0562 0.1148  438 SER A CA  
3565  C C   . SER A 438 ? 0.5101 0.6175 0.6888 0.0149  -0.0595 0.1238  438 SER A C   
3566  O O   . SER A 438 ? 0.5486 0.6538 0.7398 0.0164  -0.0619 0.1382  438 SER A O   
3567  C CB  . SER A 438 ? 0.4117 0.5361 0.5556 0.0049  -0.0575 0.1164  438 SER A CB  
3568  O OG  . SER A 438 ? 0.5091 0.6458 0.6548 0.0056  -0.0613 0.1339  438 SER A OG  
3569  N N   . ALA A 439 ? 0.4293 0.5414 0.6099 0.0188  -0.0596 0.1170  439 ALA A N   
3570  C CA  . ALA A 439 ? 0.4780 0.5951 0.6753 0.0256  -0.0622 0.1266  439 ALA A CA  
3571  C C   . ALA A 439 ? 0.5246 0.6214 0.7384 0.0333  -0.0597 0.1278  439 ALA A C   
3572  O O   . ALA A 439 ? 0.5978 0.6952 0.8267 0.0384  -0.0625 0.1409  439 ALA A O   
3573  C CB  . ALA A 439 ? 0.4231 0.5514 0.6221 0.0280  -0.0621 0.1203  439 ALA A CB  
3574  N N   . TRP A 440 ? 0.5515 0.6291 0.7617 0.0347  -0.0554 0.1138  440 TRP A N   
3575  C CA  . TRP A 440 ? 0.6748 0.7283 0.8969 0.0428  -0.0546 0.1117  440 TRP A CA  
3576  C C   . TRP A 440 ? 0.6952 0.7367 0.9255 0.0385  -0.0594 0.1229  440 TRP A C   
3577  O O   . TRP A 440 ? 0.7772 0.8066 1.0231 0.0448  -0.0621 0.1313  440 TRP A O   
3578  C CB  . TRP A 440 ? 0.7116 0.7475 0.9241 0.0455  -0.0502 0.0927  440 TRP A CB  
3579  C CG  . TRP A 440 ? 0.8662 0.8736 1.0869 0.0553  -0.0508 0.0875  440 TRP A CG  
3580  C CD1 . TRP A 440 ? 0.8622 0.8452 1.0846 0.0520  -0.0557 0.0852  440 TRP A CD1 
3581  C CD2 . TRP A 440 ? 0.9060 0.9057 1.1339 0.0705  -0.0471 0.0844  440 TRP A CD2 
3582  N NE1 . TRP A 440 ? 0.9246 0.8820 1.1527 0.0641  -0.0567 0.0788  440 TRP A NE1 
3583  C CE2 . TRP A 440 ? 0.9508 0.9182 1.1812 0.0767  -0.0504 0.0780  440 TRP A CE2 
3584  C CE3 . TRP A 440 ? 0.9349 0.9524 1.1684 0.0798  -0.0416 0.0870  440 TRP A CE3 
3585  C CZ2 . TRP A 440 ? 0.9701 0.9209 1.2049 0.0939  -0.0476 0.0724  440 TRP A CZ2 
3586  C CZ3 . TRP A 440 ? 0.9491 0.9539 1.1897 0.0967  -0.0374 0.0836  440 TRP A CZ3 
3587  C CH2 . TRP A 440 ? 0.9770 0.9479 1.2164 0.1044  -0.0399 0.0756  440 TRP A CH2 
3588  N N   . SER A 441 ? 0.6668 0.7114 0.8883 0.0282  -0.0603 0.1241  441 SER A N   
3589  C CA  . SER A 441 ? 0.7286 0.7664 0.9600 0.0225  -0.0644 0.1378  441 SER A CA  
3590  C C   . SER A 441 ? 0.7825 0.8429 1.0166 0.0197  -0.0665 0.1583  441 SER A C   
3591  O O   . SER A 441 ? 0.8367 0.8962 1.0798 0.0149  -0.0691 0.1735  441 SER A O   
3592  C CB  . SER A 441 ? 0.6786 0.7121 0.9014 0.0136  -0.0635 0.1313  441 SER A CB  
3593  O OG  . SER A 441 ? 0.6958 0.7538 0.9052 0.0075  -0.0609 0.1367  441 SER A OG  
3594  N N   . HIS A 442 ? 0.7580 0.8386 0.9849 0.0225  -0.0661 0.1599  442 HIS A N   
3595  C CA  . HIS A 442 ? 0.7832 0.8872 1.0068 0.0204  -0.0691 0.1771  442 HIS A CA  
3596  C C   . HIS A 442 ? 0.8429 0.9579 1.0536 0.0127  -0.0677 0.1838  442 HIS A C   
3597  O O   . HIS A 442 ? 0.7970 0.9215 0.9877 0.0094  -0.0651 0.1733  442 HIS A O   
3598  C CB  . HIS A 442 ? 0.8489 0.9501 1.0932 0.0253  -0.0733 0.1954  442 HIS A CB  
3599  C CG  . HIS A 442 ? 0.8672 0.9583 1.1255 0.0352  -0.0735 0.1904  442 HIS A CG  
3600  N ND1 . HIS A 442 ? 0.8592 0.9634 1.1128 0.0392  -0.0726 0.1827  442 HIS A ND1 
3601  C CD2 . HIS A 442 ? 0.8595 0.9291 1.1368 0.0428  -0.0745 0.1929  442 HIS A CD2 
3602  C CE1 . HIS A 442 ? 0.8723 0.9662 1.1420 0.0495  -0.0715 0.1816  442 HIS A CE1 
3603  N NE2 . HIS A 442 ? 0.8904 0.9620 1.1731 0.0526  -0.0726 0.1866  442 HIS A NE2 
3604  N N   . SER B 2   ? 0.7949 0.9160 0.8470 -0.1240 0.1029  0.1389  2   SER B N   
3605  C CA  . SER B 2   ? 0.7683 0.9211 0.8442 -0.1172 0.1314  0.1612  2   SER B CA  
3606  C C   . SER B 2   ? 0.7911 0.9494 0.8388 -0.0875 0.1541  0.1522  2   SER B C   
3607  O O   . SER B 2   ? 0.8209 1.0144 0.8954 -0.0766 0.1712  0.1620  2   SER B O   
3608  C CB  . SER B 2   ? 0.9222 1.0588 0.9914 -0.1278 0.1400  0.1789  2   SER B CB  
3609  O OG  . SER B 2   ? 1.0220 1.1956 1.1279 -0.1267 0.1657  0.2067  2   SER B OG  
3610  N N   . ASP B 3   ? 0.7376 0.8606 0.7312 -0.0738 0.1536  0.1342  3   ASP B N   
3611  C CA  . ASP B 3   ? 0.6662 0.7896 0.6298 -0.0468 0.1734  0.1270  3   ASP B CA  
3612  C C   . ASP B 3   ? 0.6466 0.7828 0.6144 -0.0346 0.1678  0.1108  3   ASP B C   
3613  O O   . ASP B 3   ? 0.6109 0.7518 0.5618 -0.0127 0.1843  0.1071  3   ASP B O   
3614  C CB  . ASP B 3   ? 0.6248 0.7075 0.5318 -0.0370 0.1733  0.1155  3   ASP B CB  
3615  C CG  . ASP B 3   ? 0.6064 0.6615 0.4858 -0.0367 0.1491  0.0906  3   ASP B CG  
3616  O OD1 . ASP B 3   ? 0.5479 0.6133 0.4450 -0.0401 0.1350  0.0802  3   ASP B OD1 
3617  O OD2 . ASP B 3   ? 0.6276 0.6512 0.4681 -0.0325 0.1445  0.0828  3   ASP B OD2 
3618  N N   . GLY B 4   ? 0.5835 0.7235 0.5719 -0.0475 0.1453  0.1018  4   GLY B N   
3619  C CA  . GLY B 4   ? 0.5032 0.6579 0.5006 -0.0372 0.1408  0.0898  4   GLY B CA  
3620  C C   . GLY B 4   ? 0.5132 0.6422 0.4670 -0.0206 0.1354  0.0667  4   GLY B C   
3621  O O   . GLY B 4   ? 0.4377 0.5773 0.3957 -0.0093 0.1352  0.0579  4   GLY B O   
3622  N N   . LEU B 5   ? 0.4691 0.5650 0.3834 -0.0193 0.1300  0.0578  5   LEU B N   
3623  C CA  . LEU B 5   ? 0.4685 0.5415 0.3442 -0.0044 0.1241  0.0383  5   LEU B CA  
3624  C C   . LEU B 5   ? 0.4639 0.5394 0.3491 -0.0063 0.1060  0.0240  5   LEU B C   
3625  O O   . LEU B 5   ? 0.4496 0.5207 0.3198 0.0072  0.1049  0.0120  5   LEU B O   
3626  C CB  . LEU B 5   ? 0.4522 0.4928 0.2921 -0.0058 0.1175  0.0333  5   LEU B CB  
3627  C CG  . LEU B 5   ? 0.5057 0.5224 0.3079 0.0073  0.1088  0.0158  5   LEU B CG  
3628  C CD1 . LEU B 5   ? 0.5342 0.5510 0.3168 0.0271  0.1217  0.0120  5   LEU B CD1 
3629  C CD2 . LEU B 5   ? 0.5119 0.4999 0.2825 0.0062  0.1042  0.0151  5   LEU B CD2 
3630  N N   . PHE B 6   ? 0.4006 0.4796 0.3074 -0.0228 0.0907  0.0251  6   PHE B N   
3631  C CA  . PHE B 6   ? 0.4144 0.4938 0.3269 -0.0240 0.0743  0.0129  6   PHE B CA  
3632  C C   . PHE B 6   ? 0.4207 0.5304 0.3703 -0.0256 0.0746  0.0177  6   PHE B C   
3633  O O   . PHE B 6   ? 0.4308 0.5420 0.3883 -0.0286 0.0603  0.0100  6   PHE B O   
3634  C CB  . PHE B 6   ? 0.3907 0.4501 0.2959 -0.0373 0.0565  0.0093  6   PHE B CB  
3635  C CG  . PHE B 6   ? 0.4170 0.4471 0.2849 -0.0309 0.0530  0.0004  6   PHE B CG  
3636  C CD1 . PHE B 6   ? 0.4362 0.4512 0.2861 -0.0318 0.0608  0.0071  6   PHE B CD1 
3637  C CD2 . PHE B 6   ? 0.4358 0.4551 0.2884 -0.0235 0.0427  -0.0128 6   PHE B CD2 
3638  C CE1 . PHE B 6   ? 0.4560 0.4455 0.2727 -0.0248 0.0572  -0.0001 6   PHE B CE1 
3639  C CE2 . PHE B 6   ? 0.4751 0.4717 0.2980 -0.0168 0.0397  -0.0189 6   PHE B CE2 
3640  C CZ  . PHE B 6   ? 0.4905 0.4719 0.2950 -0.0173 0.0463  -0.0130 6   PHE B CZ  
3641  N N   . ASP B 7   ? 0.4041 0.5380 0.3753 -0.0215 0.0916  0.0308  7   ASP B N   
3642  C CA  . ASP B 7   ? 0.3947 0.5603 0.4052 -0.0227 0.0924  0.0381  7   ASP B CA  
3643  C C   . ASP B 7   ? 0.3830 0.5494 0.3875 -0.0094 0.0884  0.0245  7   ASP B C   
3644  O O   . ASP B 7   ? 0.3807 0.5646 0.4119 -0.0135 0.0794  0.0254  7   ASP B O   
3645  C CB  . ASP B 7   ? 0.3915 0.5835 0.4249 -0.0173 0.1153  0.0569  7   ASP B CB  
3646  C CG  . ASP B 7   ? 0.4801 0.6841 0.5422 -0.0370 0.1146  0.0758  7   ASP B CG  
3647  O OD1 . ASP B 7   ? 0.4759 0.6594 0.5301 -0.0533 0.0960  0.0714  7   ASP B OD1 
3648  O OD2 . ASP B 7   ? 0.4972 0.7304 0.5906 -0.0363 0.1317  0.0956  7   ASP B OD2 
3649  N N   . GLN B 8   ? 0.3969 0.5435 0.3670 0.0058  0.0931  0.0123  8   GLN B N   
3650  C CA  . GLN B 8   ? 0.3843 0.5294 0.3502 0.0164  0.0874  0.0004  8   GLN B CA  
3651  C C   . GLN B 8   ? 0.3773 0.5147 0.3450 0.0067  0.0669  -0.0084 8   GLN B C   
3652  O O   . GLN B 8   ? 0.3817 0.5297 0.3647 0.0086  0.0602  -0.0114 8   GLN B O   
3653  C CB  . GLN B 8   ? 0.4439 0.5660 0.3723 0.0326  0.0930  -0.0104 8   GLN B CB  
3654  C CG  . GLN B 8   ? 0.3787 0.4966 0.3042 0.0417  0.0850  -0.0220 8   GLN B CG  
3655  C CD  . GLN B 8   ? 0.4154 0.5566 0.3662 0.0505  0.0944  -0.0160 8   GLN B CD  
3656  O OE1 . GLN B 8   ? 0.4158 0.5727 0.3928 0.0449  0.0855  -0.0149 8   GLN B OE1 
3657  N NE2 . GLN B 8   ? 0.4531 0.5951 0.3942 0.0658  0.1123  -0.0118 8   GLN B NE2 
3658  N N   . PHE B 9   ? 0.3550 0.4731 0.3054 -0.0021 0.0574  -0.0119 9   PHE B N   
3659  C CA  . PHE B 9   ? 0.3839 0.4933 0.3330 -0.0091 0.0400  -0.0188 9   PHE B CA  
3660  C C   . PHE B 9   ? 0.3631 0.4889 0.3415 -0.0214 0.0311  -0.0114 9   PHE B C   
3661  O O   . PHE B 9   ? 0.3572 0.4845 0.3410 -0.0221 0.0195  -0.0160 9   PHE B O   
3662  C CB  . PHE B 9   ? 0.3846 0.4686 0.3074 -0.0136 0.0337  -0.0228 9   PHE B CB  
3663  C CG  . PHE B 9   ? 0.4065 0.4744 0.3019 -0.0028 0.0385  -0.0296 9   PHE B CG  
3664  C CD1 . PHE B 9   ? 0.4002 0.4620 0.2862 0.0054  0.0325  -0.0389 9   PHE B CD1 
3665  C CD2 . PHE B 9   ? 0.4121 0.4702 0.2912 -0.0014 0.0479  -0.0255 9   PHE B CD2 
3666  C CE1 . PHE B 9   ? 0.4130 0.4598 0.2759 0.0137  0.0333  -0.0444 9   PHE B CE1 
3667  C CE2 . PHE B 9   ? 0.5091 0.5505 0.3604 0.0091  0.0496  -0.0321 9   PHE B CE2 
3668  C CZ  . PHE B 9   ? 0.4436 0.4795 0.2878 0.0160  0.0411  -0.0417 9   PHE B CZ  
3669  N N   . LYS B 10  ? 0.3698 0.5082 0.3679 -0.0313 0.0356  0.0014  10  LYS B N   
3670  C CA  . LYS B 10  ? 0.3277 0.4814 0.3561 -0.0452 0.0240  0.0101  10  LYS B CA  
3671  C C   . LYS B 10  ? 0.3579 0.5404 0.4158 -0.0387 0.0265  0.0136  10  LYS B C   
3672  O O   . LYS B 10  ? 0.3279 0.5159 0.3990 -0.0442 0.0115  0.0127  10  LYS B O   
3673  C CB  . LYS B 10  ? 0.3505 0.5112 0.3958 -0.0586 0.0282  0.0252  10  LYS B CB  
3674  C CG  . LYS B 10  ? 0.4603 0.6421 0.5449 -0.0747 0.0168  0.0381  10  LYS B CG  
3675  C CD  . LYS B 10  ? 0.5325 0.7081 0.6251 -0.0923 0.0146  0.0511  10  LYS B CD  
3676  C CE  . LYS B 10  ? 0.5389 0.7229 0.6627 -0.1129 -0.0069 0.0606  10  LYS B CE  
3677  N NZ  . LYS B 10  ? 0.5465 0.7751 0.7211 -0.1137 -0.0022 0.0758  10  LYS B NZ  
3678  N N   . THR B 11  ? 0.3049 0.5026 0.3689 -0.0249 0.0450  0.0170  11  THR B N   
3679  C CA  . THR B 11  ? 0.3085 0.5290 0.3944 -0.0145 0.0490  0.0189  11  THR B CA  
3680  C C   . THR B 11  ? 0.3210 0.5273 0.3904 -0.0082 0.0374  0.0047  11  THR B C   
3681  O O   . THR B 11  ? 0.3155 0.5356 0.4047 -0.0089 0.0285  0.0062  11  THR B O   
3682  C CB  . THR B 11  ? 0.2683 0.4969 0.3505 0.0030  0.0719  0.0222  11  THR B CB  
3683  O OG1 . THR B 11  ? 0.3512 0.5949 0.4498 -0.0017 0.0852  0.0379  11  THR B OG1 
3684  C CG2 . THR B 11  ? 0.3439 0.5952 0.4495 0.0149  0.0769  0.0255  11  THR B CG2 
3685  N N   . TRP B 12  ? 0.2973 0.4778 0.3323 -0.0013 0.0380  -0.0077 12  TRP B N   
3686  C CA  . TRP B 12  ? 0.3549 0.5233 0.3770 0.0039  0.0280  -0.0186 12  TRP B CA  
3687  C C   . TRP B 12  ? 0.3468 0.5123 0.3734 -0.0072 0.0104  -0.0191 12  TRP B C   
3688  O O   . TRP B 12  ? 0.3612 0.5299 0.3931 -0.0039 0.0027  -0.0218 12  TRP B O   
3689  C CB  . TRP B 12  ? 0.3306 0.4735 0.3195 0.0096  0.0292  -0.0288 12  TRP B CB  
3690  C CG  . TRP B 12  ? 0.3604 0.4985 0.3370 0.0236  0.0408  -0.0327 12  TRP B CG  
3691  C CD1 . TRP B 12  ? 0.3318 0.4818 0.3198 0.0347  0.0496  -0.0307 12  TRP B CD1 
3692  C CD2 . TRP B 12  ? 0.3897 0.5057 0.3367 0.0292  0.0433  -0.0397 12  TRP B CD2 
3693  N NE1 . TRP B 12  ? 0.3921 0.5244 0.3548 0.0470  0.0569  -0.0372 12  TRP B NE1 
3694  C CE2 . TRP B 12  ? 0.4127 0.5249 0.3511 0.0430  0.0521  -0.0427 12  TRP B CE2 
3695  C CE3 . TRP B 12  ? 0.3655 0.4633 0.2913 0.0246  0.0378  -0.0437 12  TRP B CE3 
3696  C CZ2 . TRP B 12  ? 0.3824 0.4716 0.2905 0.0508  0.0534  -0.0499 12  TRP B CZ2 
3697  C CZ3 . TRP B 12  ? 0.3914 0.4712 0.2921 0.0323  0.0398  -0.0495 12  TRP B CZ3 
3698  C CH2 . TRP B 12  ? 0.3757 0.4504 0.2669 0.0445  0.0465  -0.0529 12  TRP B CH2 
3699  N N   . TYR B 13  ? 0.3425 0.4981 0.3633 -0.0195 0.0033  -0.0167 13  TYR B N   
3700  C CA  . TYR B 13  ? 0.3632 0.5085 0.3799 -0.0285 -0.0145 -0.0184 13  TYR B CA  
3701  C C   . TYR B 13  ? 0.3645 0.5329 0.4136 -0.0349 -0.0230 -0.0097 13  TYR B C   
3702  O O   . TYR B 13  ? 0.3657 0.5342 0.4155 -0.0327 -0.0336 -0.0126 13  TYR B O   
3703  C CB  . TYR B 13  ? 0.3535 0.4772 0.3521 -0.0393 -0.0207 -0.0182 13  TYR B CB  
3704  C CG  . TYR B 13  ? 0.4030 0.5118 0.3950 -0.0500 -0.0405 -0.0187 13  TYR B CG  
3705  C CD1 . TYR B 13  ? 0.4718 0.5575 0.4349 -0.0441 -0.0491 -0.0278 13  TYR B CD1 
3706  C CD2 . TYR B 13  ? 0.4098 0.5259 0.4230 -0.0655 -0.0511 -0.0093 13  TYR B CD2 
3707  C CE1 . TYR B 13  ? 0.4972 0.5630 0.4459 -0.0514 -0.0674 -0.0292 13  TYR B CE1 
3708  C CE2 . TYR B 13  ? 0.5213 0.6175 0.5232 -0.0756 -0.0724 -0.0108 13  TYR B CE2 
3709  C CZ  . TYR B 13  ? 0.5389 0.6079 0.5053 -0.0675 -0.0805 -0.0216 13  TYR B CZ  
3710  O OH  . TYR B 13  ? 0.5840 0.6281 0.5325 -0.0756 -0.1019 -0.0237 13  TYR B OH  
3711  N N   . GLU B 14  ? 0.2891 0.4793 0.3671 -0.0419 -0.0173 0.0024  14  GLU B N   
3712  C CA  . GLU B 14  ? 0.3073 0.5243 0.4231 -0.0493 -0.0260 0.0137  14  GLU B CA  
3713  C C   . GLU B 14  ? 0.2897 0.5260 0.4207 -0.0355 -0.0213 0.0133  14  GLU B C   
3714  O O   . GLU B 14  ? 0.3786 0.6267 0.5278 -0.0388 -0.0350 0.0171  14  GLU B O   
3715  C CB  . GLU B 14  ? 0.3540 0.5944 0.5009 -0.0570 -0.0159 0.0292  14  GLU B CB  
3716  C CG  . GLU B 14  ? 0.4386 0.6599 0.5758 -0.0742 -0.0256 0.0319  14  GLU B CG  
3717  C CD  . GLU B 14  ? 0.5243 0.7713 0.6991 -0.0854 -0.0188 0.0509  14  GLU B CD  
3718  O OE1 . GLU B 14  ? 0.5530 0.8361 0.7697 -0.0848 -0.0159 0.0638  14  GLU B OE1 
3719  O OE2 . GLU B 14  ? 0.6316 0.8638 0.7954 -0.0942 -0.0157 0.0542  14  GLU B OE2 
3720  N N   . LYS B 15  ? 0.2942 0.5310 0.4157 -0.0199 -0.0035 0.0088  15  LYS B N   
3721  C CA  . LYS B 15  ? 0.2912 0.5424 0.4243 -0.0050 0.0036  0.0086  15  LYS B CA  
3722  C C   . LYS B 15  ? 0.3106 0.5379 0.4129 0.0050  0.0020  -0.0052 15  LYS B C   
3723  O O   . LYS B 15  ? 0.3004 0.5272 0.3983 0.0190  0.0126  -0.0087 15  LYS B O   
3724  C CB  . LYS B 15  ? 0.3047 0.5733 0.4507 0.0068  0.0257  0.0157  15  LYS B CB  
3725  C CG  . LYS B 15  ? 0.3063 0.6041 0.4886 -0.0020 0.0311  0.0332  15  LYS B CG  
3726  C CD  . LYS B 15  ? 0.4377 0.7705 0.6618 0.0024  0.0317  0.0461  15  LYS B CD  
3727  C CE  . LYS B 15  ? 0.4260 0.7639 0.6670 -0.0123 0.0058  0.0481  15  LYS B CE  
3728  N NZ  . LYS B 15  ? 0.4470 0.8261 0.7405 -0.0161 0.0030  0.0670  15  LYS B NZ  
3729  N N   . ARG B 16  ? 0.3178 0.5238 0.3984 -0.0017 -0.0116 -0.0123 16  ARG B N   
3730  C CA  . ARG B 16  ? 0.3331 0.5187 0.3876 0.0070  -0.0113 -0.0226 16  ARG B CA  
3731  C C   . ARG B 16  ? 0.2934 0.4869 0.3579 0.0174  -0.0117 -0.0228 16  ARG B C   
3732  O O   . ARG B 16  ? 0.3168 0.5001 0.3693 0.0271  -0.0055 -0.0285 16  ARG B O   
3733  C CB  . ARG B 16  ? 0.3334 0.4974 0.3646 0.0002  -0.0238 -0.0276 16  ARG B CB  
3734  C CG  . ARG B 16  ? 0.3252 0.4922 0.3636 -0.0066 -0.0400 -0.0240 16  ARG B CG  
3735  C CD  . ARG B 16  ? 0.3381 0.4781 0.3444 -0.0073 -0.0498 -0.0302 16  ARG B CD  
3736  N NE  . ARG B 16  ? 0.3181 0.4498 0.3104 0.0041  -0.0435 -0.0349 16  ARG B NE  
3737  C CZ  . ARG B 16  ? 0.3797 0.4914 0.3459 0.0076  -0.0457 -0.0386 16  ARG B CZ  
3738  N NH1 . ARG B 16  ? 0.3702 0.4636 0.3153 0.0028  -0.0545 -0.0400 16  ARG B NH1 
3739  N NH2 . ARG B 16  ? 0.3363 0.4453 0.2973 0.0167  -0.0387 -0.0402 16  ARG B NH2 
3740  N N   . HIS B 17  ? 0.3002 0.5110 0.3871 0.0152  -0.0200 -0.0160 17  HIS B N   
3741  C CA  . HIS B 17  ? 0.2923 0.5080 0.3863 0.0253  -0.0218 -0.0158 17  HIS B CA  
3742  C C   . HIS B 17  ? 0.2876 0.5165 0.3965 0.0378  -0.0074 -0.0131 17  HIS B C   
3743  O O   . HIS B 17  ? 0.3074 0.5271 0.4085 0.0490  -0.0039 -0.0172 17  HIS B O   
3744  C CB  . HIS B 17  ? 0.2671 0.4954 0.3778 0.0202  -0.0369 -0.0093 17  HIS B CB  
3745  C CG  . HIS B 17  ? 0.3179 0.5272 0.4068 0.0109  -0.0523 -0.0128 17  HIS B CG  
3746  N ND1 . HIS B 17  ? 0.3070 0.4922 0.3656 0.0149  -0.0526 -0.0203 17  HIS B ND1 
3747  C CD2 . HIS B 17  ? 0.3139 0.5230 0.4054 -0.0009 -0.0684 -0.0092 17  HIS B CD2 
3748  C CE1 . HIS B 17  ? 0.3301 0.5001 0.3704 0.0081  -0.0659 -0.0215 17  HIS B CE1 
3749  N NE2 . HIS B 17  ? 0.3394 0.5211 0.3971 -0.0018 -0.0772 -0.0158 17  HIS B NE2 
3750  N N   . ASP B 18  ? 0.2842 0.5326 0.4129 0.0367  0.0016  -0.0054 18  ASP B N   
3751  C CA  . ASP B 18  ? 0.3120 0.5694 0.4483 0.0515  0.0190  -0.0028 18  ASP B CA  
3752  C C   . ASP B 18  ? 0.3234 0.5529 0.4265 0.0596  0.0273  -0.0141 18  ASP B C   
3753  O O   . ASP B 18  ? 0.3275 0.5482 0.4228 0.0741  0.0343  -0.0177 18  ASP B O   
3754  C CB  . ASP B 18  ? 0.2988 0.5810 0.4593 0.0487  0.0296  0.0091  18  ASP B CB  
3755  C CG  . ASP B 18  ? 0.3436 0.6596 0.5458 0.0451  0.0237  0.0233  18  ASP B CG  
3756  O OD1 . ASP B 18  ? 0.3392 0.6597 0.5501 0.0495  0.0142  0.0235  18  ASP B OD1 
3757  O OD2 . ASP B 18  ? 0.4091 0.7481 0.6371 0.0377  0.0283  0.0357  18  ASP B OD2 
3758  N N   . TYR B 19  ? 0.2960 0.5091 0.3784 0.0505  0.0251  -0.0196 19  TYR B N   
3759  C CA  . TYR B 19  ? 0.3528 0.5398 0.4048 0.0563  0.0298  -0.0296 19  TYR B CA  
3760  C C   . TYR B 19  ? 0.3120 0.4818 0.3524 0.0612  0.0220  -0.0366 19  TYR B C   
3761  O O   . TYR B 19  ? 0.3352 0.4884 0.3606 0.0715  0.0263  -0.0423 19  TYR B O   
3762  C CB  . TYR B 19  ? 0.3103 0.4847 0.3452 0.0451  0.0262  -0.0329 19  TYR B CB  
3763  C CG  . TYR B 19  ? 0.3479 0.4962 0.3537 0.0501  0.0270  -0.0426 19  TYR B CG  
3764  C CD1 . TYR B 19  ? 0.3428 0.4768 0.3385 0.0479  0.0166  -0.0480 19  TYR B CD1 
3765  C CD2 . TYR B 19  ? 0.3444 0.4827 0.3334 0.0573  0.0379  -0.0450 19  TYR B CD2 
3766  C CE1 . TYR B 19  ? 0.3706 0.4833 0.3451 0.0511  0.0150  -0.0550 19  TYR B CE1 
3767  C CE2 . TYR B 19  ? 0.3289 0.4417 0.2910 0.0611  0.0349  -0.0538 19  TYR B CE2 
3768  C CZ  . TYR B 19  ? 0.3712 0.4730 0.3290 0.0570  0.0228  -0.0583 19  TYR B CZ  
3769  O OH  . TYR B 19  ? 0.4148 0.4944 0.3516 0.0592  0.0179  -0.0650 19  TYR B OH  
3770  N N   . ALA B 20  ? 0.3083 0.4796 0.3537 0.0540  0.0099  -0.0357 20  ALA B N   
3771  C CA  . ALA B 20  ? 0.3077 0.4648 0.3450 0.0576  0.0032  -0.0394 20  ALA B CA  
3772  C C   . ALA B 20  ? 0.2947 0.4541 0.3413 0.0699  0.0067  -0.0381 20  ALA B C   
3773  O O   . ALA B 20  ? 0.3138 0.4542 0.3479 0.0765  0.0067  -0.0430 20  ALA B O   
3774  C CB  . ALA B 20  ? 0.2681 0.4281 0.3079 0.0496  -0.0082 -0.0365 20  ALA B CB  
3775  N N   A ARG B 21  ? 0.2880 0.4699 0.3574 0.0731  0.0086  -0.0306 21  ARG B N   
3776  N N   B ARG B 21  ? 0.2872 0.4690 0.3566 0.0729  0.0084  -0.0306 21  ARG B N   
3777  C CA  A ARG B 21  ? 0.3180 0.5022 0.3965 0.0868  0.0123  -0.0284 21  ARG B CA  
3778  C CA  B ARG B 21  ? 0.3180 0.5026 0.3967 0.0867  0.0124  -0.0283 21  ARG B CA  
3779  C C   A ARG B 21  ? 0.3348 0.5059 0.3997 0.1002  0.0253  -0.0329 21  ARG B C   
3780  C C   B ARG B 21  ? 0.3359 0.5054 0.3992 0.0997  0.0248  -0.0334 21  ARG B C   
3781  O O   A ARG B 21  ? 0.3597 0.5150 0.4165 0.1120  0.0264  -0.0360 21  ARG B O   
3782  O O   B ARG B 21  ? 0.3614 0.5119 0.4137 0.1102  0.0249  -0.0376 21  ARG B O   
3783  C CB  A ARG B 21  ? 0.3059 0.5206 0.4152 0.0880  0.0115  -0.0177 21  ARG B CB  
3784  C CB  B ARG B 21  ? 0.3065 0.5222 0.4160 0.0880  0.0128  -0.0176 21  ARG B CB  
3785  C CG  A ARG B 21  ? 0.2828 0.5070 0.4015 0.0760  -0.0039 -0.0135 21  ARG B CG  
3786  C CG  B ARG B 21  ? 0.2811 0.5061 0.4017 0.0789  -0.0025 -0.0131 21  ARG B CG  
3787  C CD  A ARG B 21  ? 0.2692 0.5218 0.4196 0.0793  -0.0077 -0.0025 21  ARG B CD  
3788  C CD  B ARG B 21  ? 0.2662 0.5229 0.4203 0.0805  -0.0043 -0.0015 21  ARG B CD  
3789  N NE  A ARG B 21  ? 0.2666 0.5289 0.4253 0.0658  -0.0238 0.0020  21  ARG B NE  
3790  N NE  B ARG B 21  ? 0.2915 0.5670 0.4611 0.0687  -0.0046 0.0044  21  ARG B NE  
3791  C CZ  A ARG B 21  ? 0.2775 0.5343 0.4317 0.0648  -0.0374 0.0028  21  ARG B CZ  
3792  C CZ  B ARG B 21  ? 0.2714 0.5505 0.4443 0.0536  -0.0197 0.0066  21  ARG B CZ  
3793  N NH1 A ARG B 21  ? 0.2422 0.4871 0.3881 0.0755  -0.0365 0.0012  21  ARG B NH1 
3794  N NH1 B ARG B 21  ? 0.2749 0.5411 0.4348 0.0501  -0.0344 0.0037  21  ARG B NH1 
3795  N NH2 A ARG B 21  ? 0.3106 0.5708 0.4656 0.0529  -0.0529 0.0056  21  ARG B NH2 
3796  N NH2 B ARG B 21  ? 0.2766 0.5706 0.4647 0.0423  -0.0204 0.0127  21  ARG B NH2 
3797  N N   . ASP B 22  ? 0.3340 0.5079 0.3928 0.0993  0.0348  -0.0333 22  ASP B N   
3798  C CA  . ASP B 22  ? 0.3727 0.5292 0.4107 0.1138  0.0472  -0.0381 22  ASP B CA  
3799  C C   . ASP B 22  ? 0.4115 0.5321 0.4171 0.1123  0.0400  -0.0498 22  ASP B C   
3800  O O   . ASP B 22  ? 0.4012 0.4968 0.3856 0.1252  0.0429  -0.0561 22  ASP B O   
3801  C CB  . ASP B 22  ? 0.3900 0.5613 0.4311 0.1140  0.0607  -0.0328 22  ASP B CB  
3802  C CG  . ASP B 22  ? 0.4813 0.6300 0.4926 0.1301  0.0740  -0.0384 22  ASP B CG  
3803  O OD1 . ASP B 22  ? 0.5046 0.6506 0.5139 0.1488  0.0841  -0.0368 22  ASP B OD1 
3804  O OD2 . ASP B 22  ? 0.5259 0.6565 0.5125 0.1254  0.0736  -0.0445 22  ASP B OD2 
3805  N N   . TRP B 23  ? 0.3623 0.4790 0.3643 0.0972  0.0295  -0.0523 23  TRP B N   
3806  C CA  . TRP B 23  ? 0.3543 0.4420 0.3333 0.0940  0.0204  -0.0606 23  TRP B CA  
3807  C C   . TRP B 23  ? 0.4267 0.4987 0.4052 0.0989  0.0126  -0.0624 23  TRP B C   
3808  O O   . TRP B 23  ? 0.4530 0.4961 0.4109 0.1031  0.0077  -0.0693 23  TRP B O   
3809  C CB  . TRP B 23  ? 0.3819 0.4743 0.3632 0.0787  0.0120  -0.0598 23  TRP B CB  
3810  C CG  . TRP B 23  ? 0.4009 0.4703 0.3655 0.0742  0.0027  -0.0653 23  TRP B CG  
3811  C CD1 . TRP B 23  ? 0.3881 0.4437 0.3338 0.0725  0.0022  -0.0702 23  TRP B CD1 
3812  C CD2 . TRP B 23  ? 0.3566 0.4161 0.3252 0.0706  -0.0081 -0.0646 23  TRP B CD2 
3813  N NE1 . TRP B 23  ? 0.4032 0.4419 0.3425 0.0676  -0.0096 -0.0727 23  TRP B NE1 
3814  C CE2 . TRP B 23  ? 0.3345 0.3767 0.2895 0.0657  -0.0154 -0.0685 23  TRP B CE2 
3815  C CE3 . TRP B 23  ? 0.3633 0.4281 0.3469 0.0707  -0.0123 -0.0595 23  TRP B CE3 
3816  C CZ2 . TRP B 23  ? 0.3704 0.4025 0.3302 0.0600  -0.0267 -0.0662 23  TRP B CZ2 
3817  C CZ3 . TRP B 23  ? 0.3942 0.4467 0.3793 0.0659  -0.0219 -0.0576 23  TRP B CZ3 
3818  C CH2 . TRP B 23  ? 0.3577 0.3954 0.3331 0.0601  -0.0290 -0.0604 23  TRP B CH2 
3819  N N   . LYS B 24  ? 0.3630 0.4517 0.3630 0.0979  0.0098  -0.0559 24  LYS B N   
3820  C CA  . LYS B 24  ? 0.4003 0.4741 0.4008 0.1026  0.0029  -0.0559 24  LYS B CA  
3821  C C   . LYS B 24  ? 0.4531 0.5091 0.4412 0.1197  0.0094  -0.0598 24  LYS B C   
3822  O O   . LYS B 24  ? 0.4741 0.5001 0.4467 0.1237  0.0026  -0.0648 24  LYS B O   
3823  C CB  . LYS B 24  ? 0.3839 0.4801 0.4077 0.1001  -0.0001 -0.0473 24  LYS B CB  
3824  C CG  . LYS B 24  ? 0.3827 0.4871 0.4109 0.0863  -0.0077 -0.0441 24  LYS B CG  
3825  C CD  . LYS B 24  ? 0.3623 0.4828 0.4069 0.0863  -0.0120 -0.0362 24  LYS B CD  
3826  C CE  . LYS B 24  ? 0.4193 0.5252 0.4639 0.0908  -0.0172 -0.0336 24  LYS B CE  
3827  N NZ  . LYS B 24  ? 0.4387 0.5612 0.4967 0.0919  -0.0212 -0.0256 24  LYS B NZ  
3828  N N   . VAL B 25  ? 0.4323 0.5058 0.4271 0.1305  0.0228  -0.0566 25  VAL B N   
3829  C CA  . VAL B 25  ? 0.4966 0.5529 0.4759 0.1507  0.0325  -0.0598 25  VAL B CA  
3830  C C   . VAL B 25  ? 0.5370 0.5554 0.4785 0.1546  0.0311  -0.0710 25  VAL B C   
3831  O O   . VAL B 25  ? 0.5482 0.5317 0.4661 0.1659  0.0275  -0.0777 25  VAL B O   
3832  C CB  . VAL B 25  ? 0.4414 0.5296 0.4393 0.1614  0.0494  -0.0511 25  VAL B CB  
3833  C CG1 . VAL B 25  ? 0.5246 0.5940 0.5031 0.1862  0.0626  -0.0535 25  VAL B CG1 
3834  C CG2 . VAL B 25  ? 0.4684 0.5895 0.5027 0.1583  0.0464  -0.0403 25  VAL B CG2 
3835  N N   . ARG B 26  ? 0.4932 0.5144 0.4262 0.1452  0.0318  -0.0733 26  ARG B N   
3836  C CA  . ARG B 26  ? 0.5835 0.5704 0.4789 0.1499  0.0305  -0.0833 26  ARG B CA  
3837  C C   . ARG B 26  ? 0.5826 0.5363 0.4626 0.1406  0.0106  -0.0907 26  ARG B C   
3838  O O   . ARG B 26  ? 0.5935 0.5080 0.4397 0.1488  0.0050  -0.0999 26  ARG B O   
3839  C CB  . ARG B 26  ? 0.5863 0.5874 0.4789 0.1416  0.0362  -0.0821 26  ARG B CB  
3840  C CG  . ARG B 26  ? 0.5628 0.5914 0.4663 0.1511  0.0566  -0.0741 26  ARG B CG  
3841  C CD  . ARG B 26  ? 0.5715 0.6052 0.4647 0.1446  0.0625  -0.0734 26  ARG B CD  
3842  N NE  . ARG B 26  ? 0.5093 0.5656 0.4254 0.1239  0.0545  -0.0690 26  ARG B NE  
3843  C CZ  . ARG B 26  ? 0.5658 0.6083 0.4681 0.1122  0.0435  -0.0742 26  ARG B CZ  
3844  N NH1 . ARG B 26  ? 0.5904 0.5991 0.4605 0.1163  0.0363  -0.0836 26  ARG B NH1 
3845  N NH2 . ARG B 26  ? 0.4603 0.5222 0.3807 0.0966  0.0387  -0.0697 26  ARG B NH2 
3846  N N   . THR B 27  ? 0.5272 0.4950 0.4306 0.1239  -0.0006 -0.0860 27  THR B N   
3847  C CA  . THR B 27  ? 0.5257 0.4702 0.4229 0.1121  -0.0189 -0.0891 27  THR B CA  
3848  C C   . THR B 27  ? 0.5273 0.4626 0.4370 0.1106  -0.0282 -0.0856 27  THR B C   
3849  O O   . THR B 27  ? 0.5760 0.4851 0.4785 0.1035  -0.0436 -0.0878 27  THR B O   
3850  C CB  . THR B 27  ? 0.5189 0.4855 0.4329 0.0948  -0.0236 -0.0842 27  THR B CB  
3851  O OG1 . THR B 27  ? 0.5010 0.4978 0.4442 0.0894  -0.0206 -0.0749 27  THR B OG1 
3852  C CG2 . THR B 27  ? 0.4930 0.4694 0.3965 0.0947  -0.0149 -0.0863 27  THR B CG2 
3853  N N   . GLY B 28  ? 0.4857 0.4761 0.5748 0.0911  0.0260  -0.1354 28  GLY B N   
3854  C CA  . GLY B 28  ? 0.5026 0.4723 0.5966 0.0962  0.0117  -0.1291 28  GLY B CA  
3855  C C   . GLY B 28  ? 0.4912 0.4499 0.5715 0.0889  0.0045  -0.1113 28  GLY B C   
3856  O O   . GLY B 28  ? 0.5029 0.4442 0.5845 0.0912  -0.0076 -0.1047 28  GLY B O   
3857  N N   . GLY B 29  ? 0.4209 0.3897 0.4881 0.0798  0.0114  -0.1032 29  GLY B N   
3858  C CA  . GLY B 29  ? 0.4771 0.4365 0.5300 0.0727  0.0062  -0.0879 29  GLY B CA  
3859  C C   . GLY B 29  ? 0.4094 0.3728 0.4706 0.0736  0.0003  -0.0793 29  GLY B C   
3860  O O   . GLY B 29  ? 0.4318 0.4069 0.5099 0.0791  0.0008  -0.0846 29  GLY B O   
3861  N N   . GLN B 30  ? 0.3695 0.3237 0.4186 0.0680  -0.0053 -0.0664 30  GLN B N   
3862  C CA  . GLN B 30  ? 0.3947 0.3523 0.4476 0.0670  -0.0104 -0.0578 30  GLN B CA  
3863  C C   . GLN B 30  ? 0.3671 0.3378 0.4125 0.0608  -0.0015 -0.0547 30  GLN B C   
3864  O O   . GLN B 30  ? 0.3584 0.3313 0.3921 0.0559  0.0064  -0.0552 30  GLN B O   
3865  C CB  . GLN B 30  ? 0.4414 0.3843 0.4852 0.0637  -0.0209 -0.0459 30  GLN B CB  
3866  C CG  . GLN B 30  ? 0.5358 0.4614 0.5832 0.0675  -0.0319 -0.0456 30  GLN B CG  
3867  C CD  . GLN B 30  ? 0.5999 0.5139 0.6361 0.0616  -0.0416 -0.0318 30  GLN B CD  
3868  O OE1 . GLN B 30  ? 0.5686 0.4883 0.6020 0.0581  -0.0431 -0.0241 30  GLN B OE1 
3869  N NE2 . GLN B 30  ? 0.6651 0.5631 0.6949 0.0601  -0.0484 -0.0289 30  GLN B NE2 
3870  N N   . VAL B 31  ? 0.3302 0.3090 0.3830 0.0609  -0.0035 -0.0516 31  VAL B N   
3871  C CA  . VAL B 31  ? 0.3014 0.2903 0.3479 0.0549  0.0030  -0.0480 31  VAL B CA  
3872  C C   . VAL B 31  ? 0.3378 0.3196 0.3751 0.0509  -0.0034 -0.0372 31  VAL B C   
3873  O O   . VAL B 31  ? 0.3284 0.3041 0.3706 0.0533  -0.0132 -0.0332 31  VAL B O   
3874  C CB  . VAL B 31  ? 0.2804 0.2859 0.3424 0.0572  0.0065  -0.0541 31  VAL B CB  
3875  C CG1 . VAL B 31  ? 0.2808 0.2940 0.3356 0.0503  0.0115  -0.0495 31  VAL B CG1 
3876  C CG2 . VAL B 31  ? 0.3164 0.3316 0.3861 0.0603  0.0148  -0.0659 31  VAL B CG2 
3877  N N   . VAL B 32  ? 0.3041 0.2869 0.3281 0.0447  0.0019  -0.0324 32  VAL B N   
3878  C CA  . VAL B 32  ? 0.2849 0.2620 0.2986 0.0407  -0.0025 -0.0234 32  VAL B CA  
3879  C C   . VAL B 32  ? 0.2799 0.2653 0.2913 0.0369  0.0026  -0.0227 32  VAL B C   
3880  O O   . VAL B 32  ? 0.3087 0.2983 0.3160 0.0344  0.0106  -0.0248 32  VAL B O   
3881  C CB  . VAL B 32  ? 0.3084 0.2767 0.3077 0.0373  -0.0015 -0.0184 32  VAL B CB  
3882  C CG1 . VAL B 32  ? 0.3189 0.2834 0.3082 0.0332  -0.0059 -0.0095 32  VAL B CG1 
3883  C CG2 . VAL B 32  ? 0.4253 0.3851 0.4269 0.0404  -0.0058 -0.0203 32  VAL B CG2 
3884  N N   . ALA B 33  ? 0.2643 0.2518 0.2784 0.0360  -0.0026 -0.0198 33  ALA B N   
3885  C CA  . ALA B 33  ? 0.2934 0.2866 0.3039 0.0318  0.0011  -0.0190 33  ALA B CA  
3886  C C   . ALA B 33  ? 0.3128 0.2996 0.3077 0.0277  0.0033  -0.0138 33  ALA B C   
3887  O O   . ALA B 33  ? 0.3088 0.2897 0.2973 0.0270  -0.0019 -0.0088 33  ALA B O   
3888  C CB  . ALA B 33  ? 0.2867 0.2837 0.3043 0.0318  -0.0060 -0.0178 33  ALA B CB  
3889  N N   . THR B 34  ? 0.2838 0.2722 0.2732 0.0250  0.0107  -0.0148 34  THR B N   
3890  C CA  . THR B 34  ? 0.3036 0.2868 0.2805 0.0224  0.0134  -0.0108 34  THR B CA  
3891  C C   . THR B 34  ? 0.3087 0.2933 0.2821 0.0193  0.0149  -0.0109 34  THR B C   
3892  O O   . THR B 34  ? 0.3063 0.2957 0.2858 0.0182  0.0158  -0.0140 34  THR B O   
3893  C CB  . THR B 34  ? 0.2995 0.2815 0.2726 0.0219  0.0197  -0.0111 34  THR B CB  
3894  O OG1 . THR B 34  ? 0.2996 0.2868 0.2764 0.0201  0.0248  -0.0145 34  THR B OG1 
3895  C CG2 . THR B 34  ? 0.2974 0.2774 0.2732 0.0245  0.0183  -0.0122 34  THR B CG2 
3896  N N   . MET B 35  ? 0.3222 0.3027 0.2857 0.0178  0.0151  -0.0078 35  MET B N   
3897  C CA  . MET B 35  ? 0.3064 0.2866 0.2651 0.0152  0.0158  -0.0087 35  MET B CA  
3898  C C   . MET B 35  ? 0.3693 0.3457 0.3203 0.0152  0.0209  -0.0076 35  MET B C   
3899  O O   . MET B 35  ? 0.3693 0.3445 0.3157 0.0161  0.0209  -0.0043 35  MET B O   
3900  C CB  . MET B 35  ? 0.2968 0.2773 0.2515 0.0138  0.0098  -0.0068 35  MET B CB  
3901  C CG  . MET B 35  ? 0.3169 0.3012 0.2815 0.0145  0.0031  -0.0072 35  MET B CG  
3902  S SD  . MET B 35  ? 0.3437 0.3287 0.3030 0.0110  -0.0050 -0.0043 35  MET B SD  
3903  C CE  . MET B 35  ? 0.3399 0.3306 0.3150 0.0126  -0.0119 -0.0055 35  MET B CE  
3904  N N   . CYS B 36  ? 0.3484 0.3230 0.2986 0.0138  0.0245  -0.0099 36  CYS B N   
3905  C CA  . CYS B 36  ? 0.3763 0.3466 0.3217 0.0144  0.0290  -0.0093 36  CYS B CA  
3906  C C   . CYS B 36  ? 0.3718 0.3418 0.3189 0.0156  0.0319  -0.0066 36  CYS B C   
3907  O O   . CYS B 36  ? 0.4073 0.3795 0.3559 0.0165  0.0306  -0.0047 36  CYS B O   
3908  C CB  . CYS B 36  ? 0.3624 0.3323 0.3004 0.0154  0.0289  -0.0086 36  CYS B CB  
3909  S SG  . CYS B 36  ? 0.3384 0.3042 0.2737 0.0177  0.0343  -0.0088 36  CYS B SG  
3910  N N   . THR B 37  ? 0.3411 0.3074 0.2877 0.0151  0.0351  -0.0063 37  THR B N   
3911  C CA  . THR B 37  ? 0.3289 0.2951 0.2767 0.0148  0.0374  -0.0034 37  THR B CA  
3912  C C   . THR B 37  ? 0.3152 0.2815 0.2598 0.0170  0.0377  0.0004  37  THR B C   
3913  O O   . THR B 37  ? 0.3028 0.2695 0.2475 0.0164  0.0388  0.0032  37  THR B O   
3914  C CB  . THR B 37  ? 0.3796 0.3410 0.3279 0.0127  0.0394  -0.0030 37  THR B CB  
3915  O OG1 . THR B 37  ? 0.3283 0.2846 0.2740 0.0151  0.0396  -0.0038 37  THR B OG1 
3916  C CG2 . THR B 37  ? 0.3653 0.3279 0.3170 0.0090  0.0390  -0.0060 37  THR B CG2 
3917  N N   . TYR B 38  ? 0.3297 0.2974 0.2712 0.0188  0.0365  0.0006  38  TYR B N   
3918  C CA  . TYR B 38  ? 0.2983 0.2682 0.2373 0.0201  0.0366  0.0045  38  TYR B CA  
3919  C C   . TYR B 38  ? 0.3250 0.2971 0.2636 0.0192  0.0335  0.0066  38  TYR B C   
3920  O O   . TYR B 38  ? 0.3388 0.3126 0.2751 0.0192  0.0329  0.0104  38  TYR B O   
3921  C CB  . TYR B 38  ? 0.2916 0.2636 0.2273 0.0217  0.0374  0.0038  38  TYR B CB  
3922  C CG  . TYR B 38  ? 0.2685 0.2378 0.2057 0.0242  0.0407  0.0025  38  TYR B CG  
3923  C CD1 . TYR B 38  ? 0.2959 0.2653 0.2359 0.0258  0.0421  0.0064  38  TYR B CD1 
3924  C CD2 . TYR B 38  ? 0.3486 0.3149 0.2846 0.0252  0.0418  -0.0027 38  TYR B CD2 
3925  C CE1 . TYR B 38  ? 0.3238 0.2899 0.2669 0.0289  0.0441  0.0055  38  TYR B CE1 
3926  C CE2 . TYR B 38  ? 0.3376 0.2998 0.2760 0.0282  0.0442  -0.0046 38  TYR B CE2 
3927  C CZ  . TYR B 38  ? 0.3321 0.2943 0.2746 0.0304  0.0452  -0.0005 38  TYR B CZ  
3928  O OH  . TYR B 38  ? 0.3539 0.3117 0.3003 0.0343  0.0468  -0.0023 38  TYR B OH  
3929  N N   . THR B 39  ? 0.3309 0.3028 0.2723 0.0185  0.0311  0.0041  39  THR B N   
3930  C CA  . THR B 39  ? 0.3567 0.3287 0.2989 0.0184  0.0275  0.0053  39  THR B CA  
3931  C C   . THR B 39  ? 0.3309 0.3021 0.2720 0.0178  0.0290  0.0076  39  THR B C   
3932  O O   . THR B 39  ? 0.3129 0.2841 0.2553 0.0171  0.0323  0.0066  39  THR B O   
3933  C CB  . THR B 39  ? 0.3561 0.3286 0.3044 0.0189  0.0256  0.0011  39  THR B CB  
3934  O OG1 . THR B 39  ? 0.3501 0.3235 0.2991 0.0188  0.0223  0.0001  39  THR B OG1 
3935  C CG2 . THR B 39  ? 0.3429 0.3139 0.2935 0.0197  0.0226  0.0011  39  THR B CG2 
3936  N N   . PRO B 40  ? 0.3595 0.3301 0.2975 0.0172  0.0264  0.0114  40  PRO B N   
3937  C CA  . PRO B 40  ? 0.3752 0.3449 0.3115 0.0158  0.0273  0.0134  40  PRO B CA  
3938  C C   . PRO B 40  ? 0.3262 0.2934 0.2648 0.0157  0.0261  0.0095  40  PRO B C   
3939  O O   . PRO B 40  ? 0.3300 0.2939 0.2680 0.0156  0.0221  0.0096  40  PRO B O   
3940  C CB  . PRO B 40  ? 0.3574 0.3281 0.2896 0.0145  0.0247  0.0190  40  PRO B CB  
3941  C CG  . PRO B 40  ? 0.3858 0.3558 0.3178 0.0147  0.0204  0.0188  40  PRO B CG  
3942  C CD  . PRO B 40  ? 0.3809 0.3522 0.3156 0.0165  0.0226  0.0147  40  PRO B CD  
3943  N N   . GLU B 41  ? 0.3191 0.2882 0.2607 0.0157  0.0297  0.0055  41  GLU B N   
3944  C CA  . GLU B 41  ? 0.3551 0.3248 0.3004 0.0161  0.0302  -0.0002 41  GLU B CA  
3945  C C   . GLU B 41  ? 0.3173 0.2842 0.2588 0.0146  0.0293  -0.0004 41  GLU B C   
3946  O O   . GLU B 41  ? 0.3594 0.3247 0.3041 0.0162  0.0278  -0.0056 41  GLU B O   
3947  C CB  . GLU B 41  ? 0.4098 0.3840 0.3571 0.0143  0.0352  -0.0031 41  GLU B CB  
3948  C CG  . GLU B 41  ? 0.5057 0.4828 0.4584 0.0152  0.0359  -0.0056 41  GLU B CG  
3949  C CD  . GLU B 41  ? 0.4466 0.4285 0.4004 0.0118  0.0407  -0.0077 41  GLU B CD  
3950  O OE1 . GLU B 41  ? 0.4837 0.4643 0.4327 0.0087  0.0428  -0.0037 41  GLU B OE1 
3951  O OE2 . GLU B 41  ? 0.5582 0.5457 0.5181 0.0121  0.0420  -0.0133 41  GLU B OE2 
3952  N N   . GLU B 42  ? 0.3057 0.2720 0.2410 0.0118  0.0299  0.0050  42  GLU B N   
3953  C CA  . GLU B 42  ? 0.3307 0.2943 0.2611 0.0093  0.0288  0.0050  42  GLU B CA  
3954  C C   . GLU B 42  ? 0.3391 0.2966 0.2701 0.0108  0.0231  0.0038  42  GLU B C   
3955  O O   . GLU B 42  ? 0.3393 0.2931 0.2692 0.0103  0.0220  -0.0006 42  GLU B O   
3956  C CB  . GLU B 42  ? 0.3456 0.3101 0.2704 0.0060  0.0287  0.0125  42  GLU B CB  
3957  C CG  . GLU B 42  ? 0.3349 0.3032 0.2586 0.0039  0.0328  0.0143  42  GLU B CG  
3958  C CD  . GLU B 42  ? 0.3404 0.3105 0.2683 0.0065  0.0342  0.0166  42  GLU B CD  
3959  O OE1 . GLU B 42  ? 0.3497 0.3193 0.2806 0.0097  0.0328  0.0157  42  GLU B OE1 
3960  O OE2 . GLU B 42  ? 0.3866 0.3581 0.3139 0.0048  0.0362  0.0197  42  GLU B OE2 
3961  N N   . LEU B 43  ? 0.3217 0.2779 0.2542 0.0122  0.0193  0.0077  43  LEU B N   
3962  C CA  . LEU B 43  ? 0.3187 0.2680 0.2514 0.0127  0.0125  0.0084  43  LEU B CA  
3963  C C   . LEU B 43  ? 0.3359 0.2821 0.2760 0.0168  0.0106  0.0009  43  LEU B C   
3964  O O   . LEU B 43  ? 0.3768 0.3155 0.3178 0.0175  0.0060  -0.0018 43  LEU B O   
3965  C CB  . LEU B 43  ? 0.3709 0.3212 0.3024 0.0120  0.0090  0.0150  43  LEU B CB  
3966  C CG  . LEU B 43  ? 0.3611 0.3136 0.2862 0.0078  0.0082  0.0228  43  LEU B CG  
3967  C CD1 . LEU B 43  ? 0.4186 0.3775 0.3420 0.0068  0.0141  0.0245  43  LEU B CD1 
3968  C CD2 . LEU B 43  ? 0.3326 0.2882 0.2566 0.0069  0.0055  0.0279  43  LEU B CD2 
3969  N N   . LEU B 44  ? 0.3134 0.2649 0.2599 0.0196  0.0132  -0.0024 44  LEU B N   
3970  C CA  . LEU B 44  ? 0.3354 0.2865 0.2914 0.0239  0.0117  -0.0097 44  LEU B CA  
3971  C C   . LEU B 44  ? 0.3461 0.2980 0.3036 0.0247  0.0155  -0.0177 44  LEU B C   
3972  O O   . LEU B 44  ? 0.3534 0.3008 0.3167 0.0282  0.0122  -0.0236 44  LEU B O   
3973  C CB  . LEU B 44  ? 0.3125 0.2710 0.2745 0.0255  0.0143  -0.0112 44  LEU B CB  
3974  C CG  . LEU B 44  ? 0.3604 0.3186 0.3197 0.0244  0.0107  -0.0045 44  LEU B CG  
3975  C CD1 . LEU B 44  ? 0.3573 0.3221 0.3210 0.0250  0.0134  -0.0063 44  LEU B CD1 
3976  C CD2 . LEU B 44  ? 0.3460 0.2975 0.3079 0.0259  0.0018  -0.0023 44  LEU B CD2 
3977  N N   . ILE B 45  ? 0.2994 0.2570 0.2516 0.0212  0.0223  -0.0181 45  ILE B N   
3978  C CA  . ILE B 45  ? 0.3512 0.3111 0.3025 0.0204  0.0266  -0.0255 45  ILE B CA  
3979  C C   . ILE B 45  ? 0.3448 0.2951 0.2906 0.0195  0.0224  -0.0264 45  ILE B C   
3980  O O   . ILE B 45  ? 0.3498 0.2979 0.2990 0.0220  0.0224  -0.0351 45  ILE B O   
3981  C CB  . ILE B 45  ? 0.3593 0.3265 0.3041 0.0152  0.0333  -0.0233 45  ILE B CB  
3982  C CG1 . ILE B 45  ? 0.3313 0.3065 0.2828 0.0161  0.0367  -0.0238 45  ILE B CG1 
3983  C CG2 . ILE B 45  ? 0.3657 0.3354 0.3049 0.0117  0.0376  -0.0292 45  ILE B CG2 
3984  C CD1 . ILE B 45  ? 0.3627 0.3427 0.3081 0.0106  0.0414  -0.0186 45  ILE B CD1 
3985  N N   . ALA B 46  ? 0.3685 0.3134 0.3063 0.0159  0.0187  -0.0178 46  ALA B N   
3986  C CA  . ALA B 46  ? 0.3940 0.3296 0.3258 0.0137  0.0140  -0.0175 46  ALA B CA  
3987  C C   . ALA B 46  ? 0.4172 0.3429 0.3557 0.0182  0.0067  -0.0210 46  ALA B C   
3988  O O   . ALA B 46  ? 0.4603 0.3773 0.3972 0.0184  0.0036  -0.0262 46  ALA B O   
3989  C CB  . ALA B 46  ? 0.3678 0.3023 0.2915 0.0086  0.0115  -0.0066 46  ALA B CB  
3990  N N   . ALA B 47  ? 0.3760 0.3027 0.3223 0.0220  0.0038  -0.0190 47  ALA B N   
3991  C CA  . ALA B 47  ? 0.3945 0.3117 0.3485 0.0265  -0.0044 -0.0211 47  ALA B CA  
3992  C C   . ALA B 47  ? 0.4408 0.3600 0.4066 0.0332  -0.0025 -0.0330 47  ALA B C   
3993  O O   . ALA B 47  ? 0.4247 0.3368 0.3998 0.0381  -0.0097 -0.0350 47  ALA B O   
3994  C CB  . ALA B 47  ? 0.4136 0.3314 0.3704 0.0267  -0.0095 -0.0130 47  ALA B CB  
3995  N N   . GLY B 48  ? 0.4211 0.3506 0.3872 0.0331  0.0067  -0.0403 48  GLY B N   
3996  C CA  . GLY B 48  ? 0.3885 0.3233 0.3659 0.0390  0.0102  -0.0527 48  GLY B CA  
3997  C C   . GLY B 48  ? 0.3378 0.2834 0.3277 0.0431  0.0119  -0.0540 48  GLY B C   
3998  O O   . GLY B 48  ? 0.3654 0.3150 0.3684 0.0494  0.0123  -0.0634 48  GLY B O   
3999  N N   . MET B 49  ? 0.3238 0.2752 0.3105 0.0397  0.0132  -0.0456 49  MET B N   
4000  C CA  . MET B 49  ? 0.3176 0.2764 0.3147 0.0426  0.0122  -0.0447 49  MET B CA  
4001  C C   . MET B 49  ? 0.3337 0.3061 0.3296 0.0392  0.0214  -0.0459 49  MET B C   
4002  O O   . MET B 49  ? 0.3686 0.3424 0.3536 0.0338  0.0267  -0.0437 49  MET B O   
4003  C CB  . MET B 49  ? 0.3262 0.2787 0.3189 0.0406  0.0052  -0.0337 49  MET B CB  
4004  C CG  . MET B 49  ? 0.3787 0.3186 0.3749 0.0436  -0.0054 -0.0317 49  MET B CG  
4005  S SD  . MET B 49  ? 0.4282 0.3648 0.4171 0.0393  -0.0120 -0.0187 49  MET B SD  
4006  C CE  . MET B 49  ? 0.3674 0.2875 0.3556 0.0395  -0.0246 -0.0139 49  MET B CE  
4007  N N   . LEU B 50  ? 0.3038 0.2862 0.3117 0.0420  0.0226  -0.0494 50  LEU B N   
4008  C CA  . LEU B 50  ? 0.2780 0.2729 0.2857 0.0380  0.0300  -0.0495 50  LEU B CA  
4009  C C   . LEU B 50  ? 0.2942 0.2874 0.2990 0.0357  0.0267  -0.0409 50  LEU B C   
4010  O O   . LEU B 50  ? 0.2979 0.2928 0.3121 0.0388  0.0217  -0.0406 50  LEU B O   
4011  C CB  . LEU B 50  ? 0.2786 0.2871 0.3014 0.0416  0.0336  -0.0589 50  LEU B CB  
4012  C CG  . LEU B 50  ? 0.3311 0.3532 0.3545 0.0363  0.0405  -0.0585 50  LEU B CG  
4013  C CD1 . LEU B 50  ? 0.3579 0.3828 0.3691 0.0297  0.0481  -0.0586 50  LEU B CD1 
4014  C CD2 . LEU B 50  ? 0.3130 0.3510 0.3538 0.0396  0.0430  -0.0668 50  LEU B CD2 
4015  N N   . PRO B 51  ? 0.2977 0.2887 0.2908 0.0304  0.0293  -0.0344 51  PRO B N   
4016  C CA  . PRO B 51  ? 0.3002 0.2909 0.2912 0.0285  0.0275  -0.0284 51  PRO B CA  
4017  C C   . PRO B 51  ? 0.3192 0.3205 0.3171 0.0267  0.0314  -0.0315 51  PRO B C   
4018  O O   . PRO B 51  ? 0.3213 0.3293 0.3182 0.0234  0.0379  -0.0341 51  PRO B O   
4019  C CB  . PRO B 51  ? 0.3545 0.3399 0.3324 0.0242  0.0298  -0.0220 51  PRO B CB  
4020  C CG  . PRO B 51  ? 0.3588 0.3432 0.3319 0.0228  0.0331  -0.0239 51  PRO B CG  
4021  C CD  . PRO B 51  ? 0.3520 0.3417 0.3341 0.0259  0.0344  -0.0329 51  PRO B CD  
4022  N N   . VAL B 52  ? 0.3051 0.3085 0.3093 0.0279  0.0273  -0.0306 52  VAL B N   
4023  C CA  . VAL B 52  ? 0.2744 0.2876 0.2844 0.0251  0.0303  -0.0325 52  VAL B CA  
4024  C C   . VAL B 52  ? 0.2973 0.3060 0.3021 0.0226  0.0269  -0.0273 52  VAL B C   
4025  O O   . VAL B 52  ? 0.2846 0.2901 0.2911 0.0248  0.0204  -0.0254 52  VAL B O   
4026  C CB  . VAL B 52  ? 0.2932 0.3173 0.3195 0.0288  0.0290  -0.0389 52  VAL B CB  
4027  C CG1 . VAL B 52  ? 0.2629 0.2923 0.2941 0.0315  0.0337  -0.0460 52  VAL B CG1 
4028  C CG2 . VAL B 52  ? 0.3240 0.3438 0.3574 0.0340  0.0199  -0.0377 52  VAL B CG2 
4029  N N   . ARG B 53  ? 0.3022 0.3103 0.3002 0.0177  0.0311  -0.0252 53  ARG B N   
4030  C CA  . ARG B 53  ? 0.3089 0.3119 0.3011 0.0153  0.0289  -0.0217 53  ARG B CA  
4031  C C   . ARG B 53  ? 0.2957 0.3052 0.2962 0.0144  0.0256  -0.0237 53  ARG B C   
4032  O O   . ARG B 53  ? 0.3121 0.3306 0.3201 0.0119  0.0283  -0.0267 53  ARG B O   
4033  C CB  . ARG B 53  ? 0.3048 0.3045 0.2893 0.0108  0.0337  -0.0196 53  ARG B CB  
4034  C CG  . ARG B 53  ? 0.4126 0.4069 0.3923 0.0086  0.0319  -0.0179 53  ARG B CG  
4035  C CD  . ARG B 53  ? 0.4019 0.3874 0.3722 0.0102  0.0315  -0.0146 53  ARG B CD  
4036  N NE  . ARG B 53  ? 0.5181 0.4984 0.4834 0.0084  0.0305  -0.0146 53  ARG B NE  
4037  C CZ  . ARG B 53  ? 0.4314 0.4076 0.3947 0.0052  0.0325  -0.0149 53  ARG B CZ  
4038  N NH1 . ARG B 53  ? 0.5002 0.4767 0.4648 0.0024  0.0358  -0.0137 53  ARG B NH1 
4039  N NH2 . ARG B 53  ? 0.4890 0.4600 0.4480 0.0042  0.0308  -0.0163 53  ARG B NH2 
4040  N N   . VAL B 54  ? 0.2991 0.3047 0.2975 0.0152  0.0196  -0.0216 54  VAL B N   
4041  C CA  . VAL B 54  ? 0.3078 0.3190 0.3127 0.0134  0.0154  -0.0228 54  VAL B CA  
4042  C C   . VAL B 54  ? 0.3471 0.3572 0.3471 0.0077  0.0186  -0.0230 54  VAL B C   
4043  O O   . VAL B 54  ? 0.3407 0.3418 0.3296 0.0061  0.0203  -0.0211 54  VAL B O   
4044  C CB  . VAL B 54  ? 0.3229 0.3294 0.3237 0.0143  0.0080  -0.0197 54  VAL B CB  
4045  C CG1 . VAL B 54  ? 0.3239 0.3359 0.3295 0.0110  0.0035  -0.0205 54  VAL B CG1 
4046  C CG2 . VAL B 54  ? 0.3371 0.3430 0.3436 0.0196  0.0032  -0.0187 54  VAL B CG2 
4047  N N   . LEU B 55  ? 0.3292 0.3486 0.3383 0.0046  0.0192  -0.0254 55  LEU B N   
4048  C CA  . LEU B 55  ? 0.3704 0.3876 0.3751 -0.0018 0.0205  -0.0252 55  LEU B CA  
4049  C C   . LEU B 55  ? 0.4203 0.4453 0.4331 -0.0046 0.0152  -0.0265 55  LEU B C   
4050  O O   . LEU B 55  ? 0.3594 0.3938 0.3837 -0.0013 0.0116  -0.0275 55  LEU B O   
4051  C CB  . LEU B 55  ? 0.3902 0.4115 0.3967 -0.0057 0.0269  -0.0257 55  LEU B CB  
4052  C CG  . LEU B 55  ? 0.4355 0.4490 0.4336 -0.0036 0.0312  -0.0238 55  LEU B CG  
4053  C CD1 . LEU B 55  ? 0.4180 0.4376 0.4180 -0.0078 0.0370  -0.0238 55  LEU B CD1 
4054  C CD2 . LEU B 55  ? 0.4261 0.4253 0.4120 -0.0039 0.0303  -0.0212 55  LEU B CD2 
4055  N N   . GLY B 56  ? 0.4106 0.4312 0.4179 -0.0106 0.0143  -0.0264 56  GLY B N   
4056  C CA  . GLY B 56  ? 0.4153 0.4435 0.4295 -0.0146 0.0090  -0.0272 56  GLY B CA  
4057  C C   . GLY B 56  ? 0.4225 0.4653 0.4500 -0.0183 0.0113  -0.0287 56  GLY B C   
4058  O O   . GLY B 56  ? 0.4629 0.5089 0.4920 -0.0193 0.0176  -0.0290 56  GLY B O   
4059  N N   . ALA B 57  ? 0.3827 0.4359 0.4201 -0.0209 0.0060  -0.0293 57  ALA B N   
4060  C CA  . ALA B 57  ? 0.3566 0.4269 0.4084 -0.0251 0.0078  -0.0307 57  ALA B CA  
4061  C C   . ALA B 57  ? 0.3998 0.4684 0.4475 -0.0355 0.0070  -0.0298 57  ALA B C   
4062  O O   . ALA B 57  ? 0.3883 0.4711 0.4463 -0.0410 0.0093  -0.0303 57  ALA B O   
4063  C CB  . ALA B 57  ? 0.3865 0.4724 0.4557 -0.0212 0.0021  -0.0318 57  ALA B CB  
4064  N N   . HIS B 58  ? 0.4093 0.4615 0.4425 -0.0387 0.0037  -0.0289 58  HIS B N   
4065  C CA  . HIS B 58  ? 0.3913 0.4385 0.4194 -0.0486 0.0019  -0.0286 58  HIS B CA  
4066  C C   . HIS B 58  ? 0.4293 0.4938 0.4713 -0.0543 -0.0029 -0.0286 58  HIS B C   
4067  O O   . HIS B 58  ? 0.4253 0.4968 0.4720 -0.0626 -0.0016 -0.0279 58  HIS B O   
4068  C CB  . HIS B 58  ? 0.4083 0.4509 0.4324 -0.0534 0.0082  -0.0273 58  HIS B CB  
4069  C CG  . HIS B 58  ? 0.4647 0.4912 0.4765 -0.0482 0.0121  -0.0266 58  HIS B CG  
4070  N ND1 . HIS B 58  ? 0.4761 0.4830 0.4738 -0.0484 0.0104  -0.0271 58  HIS B ND1 
4071  C CD2 . HIS B 58  ? 0.4682 0.4960 0.4804 -0.0426 0.0177  -0.0259 58  HIS B CD2 
4072  C CE1 . HIS B 58  ? 0.4173 0.4152 0.4084 -0.0428 0.0147  -0.0262 58  HIS B CE1 
4073  N NE2 . HIS B 58  ? 0.4557 0.4656 0.4548 -0.0396 0.0188  -0.0251 58  HIS B NE2 
4074  N N   . GLU B 59  ? 0.4358 0.5079 0.4849 -0.0501 -0.0089 -0.0289 59  GLU B N   
4075  C CA  . GLU B 59  ? 0.4291 0.5177 0.4921 -0.0547 -0.0152 -0.0285 59  GLU B CA  
4076  C C   . GLU B 59  ? 0.4403 0.5224 0.4968 -0.0547 -0.0244 -0.0276 59  GLU B C   
4077  O O   . GLU B 59  ? 0.3875 0.4571 0.4326 -0.0491 -0.0253 -0.0274 59  GLU B O   
4078  C CB  . GLU B 59  ? 0.4645 0.5758 0.5498 -0.0488 -0.0136 -0.0293 59  GLU B CB  
4079  C CG  . GLU B 59  ? 0.4730 0.5825 0.5612 -0.0373 -0.0147 -0.0297 59  GLU B CG  
4080  C CD  . GLU B 59  ? 0.5585 0.6874 0.6675 -0.0304 -0.0111 -0.0324 59  GLU B CD  
4081  O OE1 . GLU B 59  ? 0.5659 0.7043 0.6797 -0.0330 -0.0030 -0.0344 59  GLU B OE1 
4082  O OE2 . GLU B 59  ? 0.5662 0.6998 0.6857 -0.0222 -0.0164 -0.0325 59  GLU B OE2 
4083  N N   . PRO B 60  ? 0.4266 0.5180 0.4896 -0.0617 -0.0316 -0.0268 60  PRO B N   
4084  C CA  . PRO B 60  ? 0.4081 0.4936 0.4631 -0.0632 -0.0410 -0.0256 60  PRO B CA  
4085  C C   . PRO B 60  ? 0.4378 0.5285 0.5002 -0.0534 -0.0449 -0.0236 60  PRO B C   
4086  O O   . PRO B 60  ? 0.4046 0.5095 0.4853 -0.0466 -0.0432 -0.0235 60  PRO B O   
4087  C CB  . PRO B 60  ? 0.4810 0.5798 0.5458 -0.0727 -0.0480 -0.0245 60  PRO B CB  
4088  C CG  . PRO B 60  ? 0.4587 0.5667 0.5327 -0.0778 -0.0414 -0.0253 60  PRO B CG  
4089  C CD  . PRO B 60  ? 0.4127 0.5223 0.4912 -0.0691 -0.0319 -0.0264 60  PRO B CD  
4090  N N   . GLN B 61  ? 0.4255 0.5035 0.4725 -0.0527 -0.0498 -0.0224 61  GLN B N   
4091  C CA  . GLN B 61  ? 0.4256 0.5052 0.4766 -0.0446 -0.0544 -0.0195 61  GLN B CA  
4092  C C   . GLN B 61  ? 0.4850 0.5566 0.5207 -0.0494 -0.0632 -0.0171 61  GLN B C   
4093  O O   . GLN B 61  ? 0.4351 0.4937 0.4512 -0.0555 -0.0615 -0.0196 61  GLN B O   
4094  C CB  . GLN B 61  ? 0.4304 0.5006 0.4758 -0.0360 -0.0466 -0.0203 61  GLN B CB  
4095  C CG  . GLN B 61  ? 0.4141 0.4655 0.4358 -0.0380 -0.0421 -0.0218 61  GLN B CG  
4096  C CD  . GLN B 61  ? 0.4384 0.4821 0.4468 -0.0373 -0.0482 -0.0190 61  GLN B CD  
4097  O OE1 . GLN B 61  ? 0.4216 0.4723 0.4382 -0.0349 -0.0564 -0.0148 61  GLN B OE1 
4098  N NE2 . GLN B 61  ? 0.4421 0.4722 0.4302 -0.0402 -0.0449 -0.0213 61  GLN B NE2 
4099  N N   . ASN B 62  ? 0.4629 0.5421 0.5076 -0.0467 -0.0727 -0.0124 62  ASN B N   
4100  C CA  . ASN B 62  ? 0.4811 0.5548 0.5115 -0.0521 -0.0823 -0.0090 62  ASN B CA  
4101  C C   . ASN B 62  ? 0.4449 0.5177 0.4778 -0.0453 -0.0881 -0.0036 62  ASN B C   
4102  O O   . ASN B 62  ? 0.5593 0.6358 0.5928 -0.0482 -0.0997 0.0019  62  ASN B O   
4103  C CB  . ASN B 62  ? 0.5766 0.6616 0.6144 -0.0604 -0.0926 -0.0068 62  ASN B CB  
4104  C CG  . ASN B 62  ? 0.7103 0.7853 0.7242 -0.0712 -0.0971 -0.0076 62  ASN B CG  
4105  O OD1 . ASN B 62  ? 0.7059 0.7712 0.7022 -0.0717 -0.0991 -0.0061 62  ASN B OD1 
4106  N ND2 . ASN B 62  ? 0.7520 0.8298 0.7648 -0.0805 -0.0990 -0.0102 62  ASN B ND2 
4107  N N   . VAL B 63  ? 0.4277 0.4953 0.4620 -0.0368 -0.0809 -0.0045 63  VAL B N   
4108  C CA  . VAL B 63  ? 0.4126 0.4769 0.4477 -0.0310 -0.0865 0.0008  63  VAL B CA  
4109  C C   . VAL B 63  ? 0.3968 0.4465 0.4077 -0.0326 -0.0830 0.0015  63  VAL B C   
4110  O O   . VAL B 63  ? 0.3885 0.4347 0.3962 -0.0305 -0.0891 0.0072  63  VAL B O   
4111  C CB  . VAL B 63  ? 0.3695 0.4386 0.4245 -0.0200 -0.0826 -0.0002 63  VAL B CB  
4112  C CG1 . VAL B 63  ? 0.4569 0.5432 0.5377 -0.0178 -0.0866 -0.0011 63  VAL B CG1 
4113  C CG2 . VAL B 63  ? 0.3821 0.4450 0.4310 -0.0171 -0.0685 -0.0060 63  VAL B CG2 
4114  N N   . THR B 64  ? 0.3115 0.4143 0.4016 0.0115  -0.0169 -0.0296 64  THR B N   
4115  C CA  . THR B 64  ? 0.3082 0.3971 0.3858 0.0123  -0.0167 -0.0288 64  THR B CA  
4116  C C   . THR B 64  ? 0.3025 0.3878 0.3753 0.0116  -0.0220 -0.0313 64  THR B C   
4117  O O   . THR B 64  ? 0.3056 0.3805 0.3679 0.0131  -0.0221 -0.0305 64  THR B O   
4118  C CB  . THR B 64  ? 0.3275 0.4083 0.4027 0.0080  -0.0119 -0.0271 64  THR B CB  
4119  O OG1 . THR B 64  ? 0.3552 0.4380 0.4368 0.0015  -0.0124 -0.0287 64  THR B OG1 
4120  C CG2 . THR B 64  ? 0.3045 0.3880 0.3823 0.0094  -0.0065 -0.0245 64  THR B CG2 
4121  N N   . GLU B 65  ? 0.3328 0.4264 0.4129 0.0094  -0.0263 -0.0343 65  GLU B N   
4122  C CA  . GLU B 65  ? 0.3883 0.4777 0.4629 0.0086  -0.0313 -0.0371 65  GLU B CA  
4123  C C   . GLU B 65  ? 0.3750 0.4596 0.4386 0.0149  -0.0339 -0.0363 65  GLU B C   
4124  O O   . GLU B 65  ? 0.3814 0.4572 0.4357 0.0149  -0.0350 -0.0369 65  GLU B O   
4125  C CB  . GLU B 65  ? 0.4157 0.5160 0.5005 0.0054  -0.0362 -0.0408 65  GLU B CB  
4126  C CG  . GLU B 65  ? 0.4823 0.5786 0.5618 0.0041  -0.0419 -0.0448 65  GLU B CG  
4127  C CD  . GLU B 65  ? 0.5333 0.6295 0.6039 0.0108  -0.0467 -0.0454 65  GLU B CD  
4128  O OE1 . GLU B 65  ? 0.5204 0.6232 0.5928 0.0158  -0.0473 -0.0437 65  GLU B OE1 
4129  O OE2 . GLU B 65  ? 0.5025 0.5926 0.5646 0.0112  -0.0500 -0.0476 65  GLU B OE2 
4130  N N   . PRO B 66  ? 0.3354 0.4245 0.3991 0.0206  -0.0345 -0.0347 66  PRO B N   
4131  C CA  . PRO B 66  ? 0.3690 0.4518 0.4216 0.0263  -0.0365 -0.0331 66  PRO B CA  
4132  C C   . PRO B 66  ? 0.3528 0.4234 0.3957 0.0270  -0.0321 -0.0299 66  PRO B C   
4133  O O   . PRO B 66  ? 0.3380 0.4025 0.3715 0.0308  -0.0333 -0.0282 66  PRO B O   
4134  C CB  . PRO B 66  ? 0.3707 0.4615 0.4275 0.0319  -0.0380 -0.0321 66  PRO B CB  
4135  C CG  . PRO B 66  ? 0.3985 0.5015 0.4685 0.0293  -0.0381 -0.0340 66  PRO B CG  
4136  C CD  . PRO B 66  ? 0.3733 0.4742 0.4476 0.0223  -0.0341 -0.0345 66  PRO B CD  
4137  N N   . HIS B 67  ? 0.3240 0.3910 0.3690 0.0236  -0.0272 -0.0288 67  HIS B N   
4138  C CA  . HIS B 67  ? 0.2897 0.3465 0.3269 0.0244  -0.0233 -0.0259 67  HIS B CA  
4139  C C   . HIS B 67  ? 0.3280 0.3774 0.3613 0.0201  -0.0211 -0.0262 67  HIS B C   
4140  O O   . HIS B 67  ? 0.3196 0.3607 0.3448 0.0212  -0.0194 -0.0242 67  HIS B O   
4141  C CB  . HIS B 67  ? 0.3052 0.3632 0.3462 0.0255  -0.0192 -0.0239 67  HIS B CB  
4142  C CG  . HIS B 67  ? 0.3229 0.3870 0.3669 0.0306  -0.0209 -0.0235 67  HIS B CG  
4143  N ND1 . HIS B 67  ? 0.3261 0.3847 0.3628 0.0357  -0.0221 -0.0215 67  HIS B ND1 
4144  C CD2 . HIS B 67  ? 0.3291 0.4045 0.3823 0.0318  -0.0223 -0.0249 67  HIS B CD2 
4145  C CE1 . HIS B 67  ? 0.3538 0.4191 0.3946 0.0401  -0.0240 -0.0217 67  HIS B CE1 
4146  N NE2 . HIS B 67  ? 0.3209 0.3971 0.3719 0.0381  -0.0241 -0.0239 67  HIS B NE2 
4147  N N   . ILE B 68  ? 0.3249 0.3768 0.3643 0.0152  -0.0207 -0.0283 68  ILE B N   
4148  C CA  . ILE B 68  ? 0.3061 0.3504 0.3423 0.0114  -0.0184 -0.0286 68  ILE B CA  
4149  C C   . ILE B 68  ? 0.3465 0.3929 0.3861 0.0076  -0.0219 -0.0323 68  ILE B C   
4150  O O   . ILE B 68  ? 0.3390 0.3933 0.3882 0.0049  -0.0231 -0.0339 68  ILE B O   
4151  C CB  . ILE B 68  ? 0.2989 0.3416 0.3388 0.0087  -0.0133 -0.0266 68  ILE B CB  
4152  C CG1 . ILE B 68  ? 0.3238 0.3637 0.3596 0.0125  -0.0105 -0.0235 68  ILE B CG1 
4153  C CG2 . ILE B 68  ? 0.3310 0.3660 0.3681 0.0048  -0.0116 -0.0271 68  ILE B CG2 
4154  C CD1 . ILE B 68  ? 0.3142 0.3527 0.3522 0.0110  -0.0057 -0.0216 68  ILE B CD1 
4155  N N   . PHE B 69  ? 0.3125 0.3522 0.3445 0.0076  -0.0235 -0.0339 69  PHE B N   
4156  C CA  . PHE B 69  ? 0.3120 0.3521 0.3456 0.0045  -0.0273 -0.0380 69  PHE B CA  
4157  C C   . PHE B 69  ? 0.3214 0.3596 0.3617 -0.0013 -0.0250 -0.0387 69  PHE B C   
4158  O O   . PHE B 69  ? 0.3101 0.3430 0.3492 -0.0023 -0.0203 -0.0360 69  PHE B O   
4159  C CB  . PHE B 69  ? 0.3135 0.3462 0.3359 0.0068  -0.0288 -0.0393 69  PHE B CB  
4160  C CG  . PHE B 69  ? 0.3113 0.3427 0.3331 0.0045  -0.0331 -0.0442 69  PHE B CG  
4161  C CD1 . PHE B 69  ? 0.3334 0.3726 0.3626 0.0026  -0.0379 -0.0476 69  PHE B CD1 
4162  C CD2 . PHE B 69  ? 0.3276 0.3502 0.3415 0.0046  -0.0326 -0.0457 69  PHE B CD2 
4163  C CE1 . PHE B 69  ? 0.3625 0.4000 0.3908 0.0005  -0.0425 -0.0527 69  PHE B CE1 
4164  C CE2 . PHE B 69  ? 0.3464 0.3669 0.3589 0.0029  -0.0370 -0.0508 69  PHE B CE2 
4165  C CZ  . PHE B 69  ? 0.3552 0.3830 0.3749 0.0006  -0.0421 -0.0544 69  PHE B CZ  
4166  N N   . GLY B 70  ? 0.3276 0.3707 0.3755 -0.0053 -0.0284 -0.0420 70  GLY B N   
4167  C CA  . GLY B 70  ? 0.3176 0.3599 0.3736 -0.0115 -0.0264 -0.0423 70  GLY B CA  
4168  C C   . GLY B 70  ? 0.3665 0.3970 0.4170 -0.0139 -0.0249 -0.0429 70  GLY B C   
4169  O O   . GLY B 70  ? 0.3552 0.3833 0.4116 -0.0192 -0.0230 -0.0426 70  GLY B O   
4170  N N   . MET B 71  ? 0.3292 0.3520 0.3685 -0.0102 -0.0253 -0.0435 71  MET B N   
4171  C CA  . MET B 71  ? 0.3572 0.3690 0.3910 -0.0115 -0.0232 -0.0436 71  MET B CA  
4172  C C   . MET B 71  ? 0.3514 0.3598 0.3845 -0.0112 -0.0173 -0.0389 71  MET B C   
4173  O O   . MET B 71  ? 0.3025 0.3021 0.3318 -0.0121 -0.0152 -0.0384 71  MET B O   
4174  C CB  . MET B 71  ? 0.3297 0.3350 0.3518 -0.0071 -0.0248 -0.0454 71  MET B CB  
4175  C CG  . MET B 71  ? 0.3372 0.3432 0.3527 -0.0019 -0.0221 -0.0417 71  MET B CG  
4176  S SD  . MET B 71  ? 0.3350 0.3362 0.3375 0.0033  -0.0240 -0.0436 71  MET B SD  
4177  C CE  . MET B 71  ? 0.2966 0.2876 0.2944 0.0030  -0.0196 -0.0422 71  MET B CE  
4178  N N   . PHE B 72  ? 0.2790 0.2936 0.3149 -0.0093 -0.0147 -0.0355 72  PHE B N   
4179  C CA  . PHE B 72  ? 0.3097 0.3210 0.3437 -0.0084 -0.0095 -0.0314 72  PHE B CA  
4180  C C   . PHE B 72  ? 0.2937 0.3086 0.3366 -0.0125 -0.0065 -0.0294 72  PHE B C   
4181  O O   . PHE B 72  ? 0.2594 0.2811 0.3109 -0.0158 -0.0083 -0.0308 72  PHE B O   
4182  C CB  . PHE B 72  ? 0.2876 0.3019 0.3176 -0.0034 -0.0085 -0.0291 72  PHE B CB  
4183  C CG  . PHE B 72  ? 0.3170 0.3271 0.3377 0.0004  -0.0104 -0.0299 72  PHE B CG  
4184  C CD1 . PHE B 72  ? 0.3270 0.3289 0.3408 0.0011  -0.0085 -0.0294 72  PHE B CD1 
4185  C CD2 . PHE B 72  ? 0.3478 0.3624 0.3666 0.0032  -0.0140 -0.0312 72  PHE B CD2 
4186  C CE1 . PHE B 72  ? 0.3301 0.3290 0.3356 0.0046  -0.0097 -0.0299 72  PHE B CE1 
4187  C CE2 . PHE B 72  ? 0.3243 0.3352 0.3342 0.0066  -0.0153 -0.0316 72  PHE B CE2 
4188  C CZ  . PHE B 72  ? 0.3264 0.3298 0.3299 0.0071  -0.0129 -0.0309 72  PHE B CZ  
4189  N N   . CYS B 73  ? 0.2859 0.2967 0.3266 -0.0122 -0.0020 -0.0260 73  CYS B N   
4190  C CA  . CYS B 73  ? 0.2875 0.2989 0.3344 -0.0165 0.0014  -0.0238 73  CYS B CA  
4191  C C   . CYS B 73  ? 0.3013 0.3244 0.3573 -0.0173 0.0025  -0.0226 73  CYS B C   
4192  O O   . CYS B 73  ? 0.2731 0.3025 0.3290 -0.0133 0.0018  -0.0226 73  CYS B O   
4193  C CB  . CYS B 73  ? 0.2805 0.2850 0.3217 -0.0150 0.0057  -0.0204 73  CYS B CB  
4194  S SG  . CYS B 73  ? 0.2672 0.2758 0.3052 -0.0099 0.0087  -0.0174 73  CYS B SG  
4195  N N   . PRO B 74  ? 0.2745 0.3006 0.3386 -0.0223 0.0044  -0.0215 74  PRO B N   
4196  C CA  . PRO B 74  ? 0.3220 0.3602 0.3953 -0.0229 0.0063  -0.0199 74  PRO B CA  
4197  C C   . PRO B 74  ? 0.3060 0.3464 0.3758 -0.0184 0.0104  -0.0169 74  PRO B C   
4198  O O   . PRO B 74  ? 0.3238 0.3739 0.3980 -0.0158 0.0105  -0.0168 74  PRO B O   
4199  C CB  . PRO B 74  ? 0.3451 0.3838 0.4264 -0.0298 0.0086  -0.0184 74  PRO B CB  
4200  C CG  . PRO B 74  ? 0.3713 0.3999 0.4498 -0.0330 0.0052  -0.0211 74  PRO B CG  
4201  C CD  . PRO B 74  ? 0.2705 0.2894 0.3365 -0.0278 0.0043  -0.0219 74  PRO B CD  
4202  N N   . PHE B 75  ? 0.2892 0.3208 0.3511 -0.0168 0.0133  -0.0146 75  PHE B N   
4203  C CA  . PHE B 75  ? 0.3325 0.3659 0.3911 -0.0127 0.0169  -0.0120 75  PHE B CA  
4204  C C   . PHE B 75  ? 0.2881 0.3232 0.3424 -0.0072 0.0144  -0.0136 75  PHE B C   
4205  O O   . PHE B 75  ? 0.3105 0.3520 0.3665 -0.0040 0.0159  -0.0128 75  PHE B O   
4206  C CB  . PHE B 75  ? 0.3114 0.3349 0.3623 -0.0124 0.0199  -0.0096 75  PHE B CB  
4207  C CG  . PHE B 75  ? 0.3356 0.3602 0.3822 -0.0082 0.0232  -0.0073 75  PHE B CG  
4208  C CD1 . PHE B 75  ? 0.3362 0.3693 0.3880 -0.0080 0.0266  -0.0055 75  PHE B CD1 
4209  C CD2 . PHE B 75  ? 0.3290 0.3465 0.3668 -0.0046 0.0230  -0.0071 75  PHE B CD2 
4210  C CE1 . PHE B 75  ? 0.3530 0.3867 0.4000 -0.0037 0.0295  -0.0039 75  PHE B CE1 
4211  C CE2 . PHE B 75  ? 0.3796 0.3977 0.4134 -0.0009 0.0255  -0.0055 75  PHE B CE2 
4212  C CZ  . PHE B 75  ? 0.3390 0.3647 0.3769 -0.0003 0.0287  -0.0040 75  PHE B CZ  
4213  N N   . CYS B 76  ? 0.2976 0.3270 0.3463 -0.0058 0.0108  -0.0156 76  CYS B N   
4214  C CA  . CYS B 76  ? 0.2459 0.2756 0.2897 -0.0006 0.0090  -0.0161 76  CYS B CA  
4215  C C   . CYS B 76  ? 0.2681 0.3075 0.3182 0.0007  0.0065  -0.0177 76  CYS B C   
4216  O O   . CYS B 76  ? 0.2875 0.3297 0.3362 0.0052  0.0060  -0.0174 76  CYS B O   
4217  C CB  . CYS B 76  ? 0.3204 0.3430 0.3567 0.0010  0.0061  -0.0174 76  CYS B CB  
4218  S SG  . CYS B 76  ? 0.3017 0.3240 0.3385 -0.0008 0.0013  -0.0208 76  CYS B SG  
4219  N N   . ARG B 77  ? 0.2413 0.2861 0.2989 -0.0031 0.0047  -0.0193 77  ARG B N   
4220  C CA  . ARG B 77  ? 0.2770 0.3322 0.3417 -0.0020 0.0018  -0.0211 77  ARG B CA  
4221  C C   . ARG B 77  ? 0.3222 0.3871 0.3946 -0.0017 0.0053  -0.0194 77  ARG B C   
4222  O O   . ARG B 77  ? 0.2801 0.3512 0.3538 0.0029  0.0047  -0.0196 77  ARG B O   
4223  C CB  . ARG B 77  ? 0.3238 0.3813 0.3936 -0.0064 -0.0022 -0.0240 77  ARG B CB  
4224  C CG  . ARG B 77  ? 0.2834 0.3336 0.3447 -0.0045 -0.0065 -0.0263 77  ARG B CG  
4225  C CD  . ARG B 77  ? 0.3303 0.3760 0.3922 -0.0094 -0.0090 -0.0290 77  ARG B CD  
4226  N NE  . ARG B 77  ? 0.4066 0.4617 0.4795 -0.0132 -0.0113 -0.0309 77  ARG B NE  
4227  C CZ  . ARG B 77  ? 0.4305 0.4845 0.5092 -0.0193 -0.0113 -0.0319 77  ARG B CZ  
4228  N NH1 . ARG B 77  ? 0.4404 0.4832 0.5141 -0.0219 -0.0098 -0.0316 77  ARG B NH1 
4229  N NH2 . ARG B 77  ? 0.4474 0.5116 0.5375 -0.0230 -0.0132 -0.0333 77  ARG B NH2 
4230  N N   . ASP B 78  ? 0.2437 0.3095 0.3205 -0.0060 0.0093  -0.0175 78  ASP B N   
4231  C CA  . ASP B 78  ? 0.2959 0.3707 0.3790 -0.0056 0.0136  -0.0154 78  ASP B CA  
4232  C C   . ASP B 78  ? 0.2718 0.3451 0.3484 0.0008  0.0157  -0.0143 78  ASP B C   
4233  O O   . ASP B 78  ? 0.2835 0.3657 0.3641 0.0044  0.0165  -0.0144 78  ASP B O   
4234  C CB  . ASP B 78  ? 0.2865 0.3586 0.3717 -0.0109 0.0180  -0.0127 78  ASP B CB  
4235  C CG  . ASP B 78  ? 0.3306 0.4142 0.4248 -0.0123 0.0225  -0.0104 78  ASP B CG  
4236  O OD1 . ASP B 78  ? 0.3432 0.4376 0.4426 -0.0088 0.0222  -0.0113 78  ASP B OD1 
4237  O OD2 . ASP B 78  ? 0.3399 0.4218 0.4362 -0.0169 0.0265  -0.0076 78  ASP B OD2 
4238  N N   . SER B 79  ? 0.2488 0.3109 0.3153 0.0024  0.0164  -0.0134 79  SER B N   
4239  C CA  . SER B 79  ? 0.2597 0.3191 0.3196 0.0079  0.0178  -0.0127 79  SER B CA  
4240  C C   . SER B 79  ? 0.2359 0.2981 0.2953 0.0128  0.0141  -0.0146 79  SER B C   
4241  O O   . SER B 79  ? 0.2557 0.3222 0.3156 0.0173  0.0152  -0.0145 79  SER B O   
4242  C CB  . SER B 79  ? 0.2910 0.3381 0.3411 0.0080  0.0181  -0.0118 79  SER B CB  
4243  O OG  . SER B 79  ? 0.2964 0.3404 0.3460 0.0045  0.0218  -0.0097 79  SER B OG  
4244  N N   . LEU B 80  ? 0.2541 0.3133 0.3117 0.0125  0.0096  -0.0162 80  LEU B N   
4245  C CA  . LEU B 80  ? 0.2730 0.3341 0.3293 0.0172  0.0060  -0.0174 80  LEU B CA  
4246  C C   . LEU B 80  ? 0.2906 0.3643 0.3562 0.0190  0.0055  -0.0184 80  LEU B C   
4247  O O   . LEU B 80  ? 0.2737 0.3500 0.3386 0.0245  0.0048  -0.0186 80  LEU B O   
4248  C CB  . LEU B 80  ? 0.2552 0.3118 0.3079 0.0163  0.0014  -0.0188 80  LEU B CB  
4249  C CG  . LEU B 80  ? 0.2497 0.3083 0.3009 0.0212  -0.0026 -0.0196 80  LEU B CG  
4250  C CD1 . LEU B 80  ? 0.2738 0.3265 0.3185 0.0261  -0.0016 -0.0182 80  LEU B CD1 
4251  C CD2 . LEU B 80  ? 0.2387 0.2937 0.2858 0.0204  -0.0069 -0.0208 80  LEU B CD2 
4252  N N   . ALA B 81  ? 0.2596 0.3415 0.3342 0.0145  0.0059  -0.0189 81  ALA B N   
4253  C CA  . ALA B 81  ? 0.2556 0.3513 0.3404 0.0158  0.0054  -0.0198 81  ALA B CA  
4254  C C   . ALA B 81  ? 0.2569 0.3572 0.3425 0.0203  0.0096  -0.0185 81  ALA B C   
4255  O O   . ALA B 81  ? 0.3055 0.4139 0.3950 0.0251  0.0084  -0.0194 81  ALA B O   
4256  C CB  . ALA B 81  ? 0.2238 0.3277 0.3192 0.0092  0.0060  -0.0201 81  ALA B CB  
4257  N N   . GLN B 82  ? 0.2585 0.3537 0.3401 0.0191  0.0143  -0.0165 82  GLN B N   
4258  C CA  . GLN B 82  ? 0.2596 0.3589 0.3409 0.0236  0.0185  -0.0156 82  GLN B CA  
4259  C C   . GLN B 82  ? 0.2380 0.3329 0.3127 0.0309  0.0161  -0.0168 82  GLN B C   
4260  O O   . GLN B 82  ? 0.3008 0.4029 0.3782 0.0362  0.0172  -0.0175 82  GLN B O   
4261  C CB  . GLN B 82  ? 0.2763 0.3690 0.3521 0.0216  0.0233  -0.0133 82  GLN B CB  
4262  C CG  . GLN B 82  ? 0.2416 0.3363 0.3226 0.0141  0.0262  -0.0113 82  GLN B CG  
4263  C CD  . GLN B 82  ? 0.3164 0.4251 0.4100 0.0116  0.0269  -0.0114 82  GLN B CD  
4264  O OE1 . GLN B 82  ? 0.3000 0.4190 0.3984 0.0145  0.0301  -0.0108 82  GLN B OE1 
4265  N NE2 . GLN B 82  ? 0.3395 0.4495 0.4390 0.0059  0.0239  -0.0122 82  GLN B NE2 
4266  N N   . GLY B 83  ? 0.2899 0.3730 0.3560 0.0314  0.0129  -0.0171 83  GLY B N   
4267  C CA  . GLY B 83  ? 0.2617 0.3398 0.3220 0.0377  0.0101  -0.0180 83  GLY B CA  
4268  C C   . GLY B 83  ? 0.2842 0.3702 0.3500 0.0410  0.0062  -0.0195 83  GLY B C   
4269  O O   . GLY B 83  ? 0.2847 0.3736 0.3506 0.0472  0.0057  -0.0202 83  GLY B O   
4270  N N   . LEU B 84  ? 0.2610 0.3501 0.3307 0.0373  0.0030  -0.0200 84  LEU B N   
4271  C CA  . LEU B 84  ? 0.2931 0.3894 0.3672 0.0406  -0.0014 -0.0214 84  LEU B CA  
4272  C C   . LEU B 84  ? 0.3062 0.4174 0.3907 0.0433  0.0001  -0.0223 84  LEU B C   
4273  O O   . LEU B 84  ? 0.3007 0.4170 0.3871 0.0491  -0.0028 -0.0233 84  LEU B O   
4274  C CB  . LEU B 84  ? 0.2796 0.3771 0.3561 0.0357  -0.0050 -0.0223 84  LEU B CB  
4275  C CG  . LEU B 84  ? 0.3211 0.4049 0.3871 0.0340  -0.0065 -0.0216 84  LEU B CG  
4276  C CD1 . LEU B 84  ? 0.2822 0.3675 0.3504 0.0293  -0.0098 -0.0230 84  LEU B CD1 
4277  C CD2 . LEU B 84  ? 0.2972 0.3742 0.3554 0.0400  -0.0095 -0.0211 84  LEU B CD2 
4278  N N   . LEU B 85  ? 0.2792 0.3976 0.3703 0.0395  0.0047  -0.0216 85  LEU B N   
4279  C CA  . LEU B 85  ? 0.2814 0.4158 0.3836 0.0412  0.0067  -0.0220 85  LEU B CA  
4280  C C   . LEU B 85  ? 0.2753 0.4106 0.3747 0.0483  0.0099  -0.0219 85  LEU B C   
4281  O O   . LEU B 85  ? 0.3154 0.4644 0.4234 0.0510  0.0120  -0.0224 85  LEU B O   
4282  C CB  . LEU B 85  ? 0.2796 0.4217 0.3903 0.0339  0.0108  -0.0208 85  LEU B CB  
4283  C CG  . LEU B 85  ? 0.3011 0.4452 0.4175 0.0268  0.0074  -0.0215 85  LEU B CG  
4284  C CD1 . LEU B 85  ? 0.3316 0.4800 0.4547 0.0194  0.0121  -0.0197 85  LEU B CD1 
4285  C CD2 . LEU B 85  ? 0.3441 0.5012 0.4700 0.0287  0.0028  -0.0237 85  LEU B CD2 
4286  N N   . GLY B 86  ? 0.2700 0.3913 0.3576 0.0514  0.0102  -0.0216 86  GLY B N   
4287  C CA  . GLY B 86  ? 0.2978 0.4177 0.3812 0.0585  0.0125  -0.0222 86  GLY B CA  
4288  C C   . GLY B 86  ? 0.2991 0.4197 0.3811 0.0573  0.0187  -0.0211 86  GLY B C   
4289  O O   . GLY B 86  ? 0.3041 0.4254 0.3831 0.0635  0.0210  -0.0219 86  GLY B O   
4290  N N   . ARG B 87  ? 0.2734 0.3933 0.3567 0.0499  0.0214  -0.0192 87  ARG B N   
4291  C CA  . ARG B 87  ? 0.2949 0.4174 0.3776 0.0489  0.0276  -0.0177 87  ARG B CA  
4292  C C   . ARG B 87  ? 0.3186 0.4269 0.3886 0.0512  0.0286  -0.0176 87  ARG B C   
4293  O O   . ARG B 87  ? 0.3569 0.4667 0.4243 0.0525  0.0333  -0.0168 87  ARG B O   
4294  C CB  . ARG B 87  ? 0.2968 0.4232 0.3857 0.0403  0.0299  -0.0154 87  ARG B CB  
4295  C CG  . ARG B 87  ? 0.2843 0.4273 0.3873 0.0382  0.0299  -0.0156 87  ARG B CG  
4296  C CD  . ARG B 87  ? 0.3309 0.4751 0.4395 0.0290  0.0310  -0.0137 87  ARG B CD  
4297  N NE  . ARG B 87  ? 0.3534 0.5133 0.4761 0.0263  0.0303  -0.0140 87  ARG B NE  
4298  C CZ  . ARG B 87  ? 0.4024 0.5659 0.5330 0.0180  0.0305  -0.0129 87  ARG B CZ  
4299  N NH1 . ARG B 87  ? 0.4027 0.5548 0.5280 0.0122  0.0314  -0.0112 87  ARG B NH1 
4300  N NH2 . ARG B 87  ? 0.4255 0.6044 0.5698 0.0157  0.0296  -0.0135 87  ARG B NH2 
4301  N N   . PHE B 88  ? 0.3109 0.4063 0.3730 0.0522  0.0242  -0.0185 88  PHE B N   
4302  C CA  . PHE B 88  ? 0.3233 0.4061 0.3743 0.0547  0.0244  -0.0189 88  PHE B CA  
4303  C C   . PHE B 88  ? 0.3382 0.4156 0.3847 0.0618  0.0207  -0.0212 88  PHE B C   
4304  O O   . PHE B 88  ? 0.3382 0.4028 0.3761 0.0628  0.0184  -0.0216 88  PHE B O   
4305  C CB  . PHE B 88  ? 0.3298 0.4011 0.3751 0.0490  0.0229  -0.0176 88  PHE B CB  
4306  C CG  . PHE B 88  ? 0.3092 0.3821 0.3558 0.0432  0.0269  -0.0154 88  PHE B CG  
4307  C CD1 . PHE B 88  ? 0.2766 0.3555 0.3308 0.0373  0.0273  -0.0141 88  PHE B CD1 
4308  C CD2 . PHE B 88  ? 0.3292 0.3965 0.3688 0.0435  0.0299  -0.0146 88  PHE B CD2 
4309  C CE1 . PHE B 88  ? 0.2861 0.3650 0.3412 0.0318  0.0309  -0.0117 88  PHE B CE1 
4310  C CE2 . PHE B 88  ? 0.3398 0.4076 0.3798 0.0385  0.0335  -0.0121 88  PHE B CE2 
4311  C CZ  . PHE B 88  ? 0.3633 0.4365 0.4111 0.0326  0.0341  -0.0105 88  PHE B CZ  
4312  N N   . ASP B 89  ? 0.3075 0.3947 0.3601 0.0668  0.0201  -0.0225 89  ASP B N   
4313  C CA  . ASP B 89  ? 0.3144 0.3960 0.3629 0.0739  0.0164  -0.0245 89  ASP B CA  
4314  C C   . ASP B 89  ? 0.3706 0.4434 0.4101 0.0791  0.0176  -0.0262 89  ASP B C   
4315  O O   . ASP B 89  ? 0.4004 0.4630 0.4338 0.0835  0.0140  -0.0276 89  ASP B O   
4316  C CB  . ASP B 89  ? 0.3442 0.4394 0.4018 0.0786  0.0155  -0.0256 89  ASP B CB  
4317  C CG  . ASP B 89  ? 0.4081 0.5173 0.4717 0.0818  0.0208  -0.0262 89  ASP B CG  
4318  O OD1 . ASP B 89  ? 0.3881 0.4975 0.4491 0.0802  0.0254  -0.0255 89  ASP B OD1 
4319  O OD2 . ASP B 89  ? 0.4948 0.6160 0.5661 0.0864  0.0202  -0.0272 89  ASP B OD2 
4320  N N   . TYR B 90  ? 0.3048 0.3801 0.3425 0.0783  0.0224  -0.0260 90  TYR B N   
4321  C CA  . TYR B 90  ? 0.3474 0.4139 0.3757 0.0831  0.0231  -0.0280 90  TYR B CA  
4322  C C   . TYR B 90  ? 0.3415 0.3926 0.3610 0.0792  0.0207  -0.0275 90  TYR B C   
4323  O O   . TYR B 90  ? 0.3382 0.3804 0.3496 0.0828  0.0201  -0.0296 90  TYR B O   
4324  C CB  . TYR B 90  ? 0.3369 0.4121 0.3655 0.0842  0.0291  -0.0279 90  TYR B CB  
4325  C CG  . TYR B 90  ? 0.3331 0.4122 0.3650 0.0760  0.0323  -0.0245 90  TYR B CG  
4326  C CD1 . TYR B 90  ? 0.3091 0.3774 0.3337 0.0714  0.0321  -0.0233 90  TYR B CD1 
4327  C CD2 . TYR B 90  ? 0.3775 0.4707 0.4199 0.0727  0.0354  -0.0225 90  TYR B CD2 
4328  C CE1 . TYR B 90  ? 0.3338 0.4046 0.3610 0.0643  0.0349  -0.0202 90  TYR B CE1 
4329  C CE2 . TYR B 90  ? 0.3268 0.4221 0.3720 0.0651  0.0380  -0.0194 90  TYR B CE2 
4330  C CZ  . TYR B 90  ? 0.3346 0.4185 0.3719 0.0612  0.0379  -0.0182 90  TYR B CZ  
4331  O OH  . TYR B 90  ? 0.3021 0.3877 0.3423 0.0542  0.0405  -0.0151 90  TYR B OH  
4332  N N   . ALA B 91  ? 0.3211 0.3690 0.3421 0.0724  0.0190  -0.0252 91  ALA B N   
4333  C CA  . ALA B 91  ? 0.3032 0.3384 0.3170 0.0685  0.0173  -0.0245 91  ALA B CA  
4334  C C   . ALA B 91  ? 0.3674 0.3919 0.3775 0.0701  0.0121  -0.0251 91  ALA B C   
4335  O O   . ALA B 91  ? 0.4276 0.4537 0.4415 0.0687  0.0096  -0.0239 91  ALA B O   
4336  C CB  . ALA B 91  ? 0.3282 0.3650 0.3448 0.0609  0.0184  -0.0217 91  ALA B CB  
4337  N N   . GLU B 92  ? 0.3641 0.3773 0.3665 0.0723  0.0103  -0.0266 92  GLU B N   
4338  C CA  . GLU B 92  ? 0.3405 0.3425 0.3393 0.0729  0.0056  -0.0266 92  GLU B CA  
4339  C C   . GLU B 92  ? 0.3339 0.3304 0.3316 0.0662  0.0042  -0.0240 92  GLU B C   
4340  O O   . GLU B 92  ? 0.3517 0.3435 0.3492 0.0655  0.0010  -0.0226 92  GLU B O   
4341  C CB  . GLU B 92  ? 0.3708 0.3622 0.3622 0.0772  0.0039  -0.0293 92  GLU B CB  
4342  C CG  . GLU B 92  ? 0.4439 0.4380 0.4350 0.0856  0.0041  -0.0325 92  GLU B CG  
4343  C CD  . GLU B 92  ? 0.5034 0.5053 0.4937 0.0884  0.0086  -0.0345 92  GLU B CD  
4344  O OE1 . GLU B 92  ? 0.4203 0.4281 0.4119 0.0838  0.0121  -0.0329 92  GLU B OE1 
4345  O OE2 . GLU B 92  ? 0.4570 0.4582 0.4444 0.0956  0.0086  -0.0378 92  GLU B OE2 
4346  N N   . GLY B 93  ? 0.3396 0.3365 0.3362 0.0615  0.0065  -0.0231 93  GLY B N   
4347  C CA  . GLY B 93  ? 0.3138 0.3052 0.3089 0.0558  0.0053  -0.0209 93  GLY B CA  
4348  C C   . GLY B 93  ? 0.2790 0.2784 0.2790 0.0512  0.0076  -0.0189 93  GLY B C   
4349  O O   . GLY B 93  ? 0.2951 0.3036 0.2993 0.0514  0.0106  -0.0191 93  GLY B O   
4350  N N   . VAL B 94  ? 0.2691 0.2647 0.2684 0.0468  0.0062  -0.0171 94  VAL B N   
4351  C CA  . VAL B 94  ? 0.3013 0.3017 0.3036 0.0421  0.0081  -0.0155 94  VAL B CA  
4352  C C   . VAL B 94  ? 0.2928 0.2863 0.2913 0.0384  0.0073  -0.0142 94  VAL B C   
4353  O O   . VAL B 94  ? 0.2928 0.2797 0.2884 0.0384  0.0047  -0.0137 94  VAL B O   
4354  C CB  . VAL B 94  ? 0.2404 0.2470 0.2480 0.0412  0.0070  -0.0149 94  VAL B CB  
4355  C CG1 . VAL B 94  ? 0.2806 0.2818 0.2860 0.0415  0.0034  -0.0140 94  VAL B CG1 
4356  C CG2 . VAL B 94  ? 0.2657 0.2768 0.2765 0.0362  0.0090  -0.0139 94  VAL B CG2 
4357  N N   . THR B 95  ? 0.2495 0.2447 0.2481 0.0352  0.0097  -0.0135 95  THR B N   
4358  C CA  . THR B 95  ? 0.2367 0.2262 0.2319 0.0322  0.0091  -0.0124 95  THR B CA  
4359  C C   . THR B 95  ? 0.2614 0.2541 0.2585 0.0287  0.0112  -0.0112 95  THR B C   
4360  O O   . THR B 95  ? 0.2855 0.2828 0.2847 0.0284  0.0138  -0.0112 95  THR B O   
4361  C CB  . THR B 95  ? 0.2822 0.2666 0.2729 0.0335  0.0090  -0.0133 95  THR B CB  
4362  O OG1 . THR B 95  ? 0.2983 0.2784 0.2868 0.0306  0.0081  -0.0122 95  THR B OG1 
4363  C CG2 . THR B 95  ? 0.2879 0.2761 0.2779 0.0348  0.0121  -0.0140 95  THR B CG2 
4364  N N   . LEU B 96  ? 0.2866 0.2766 0.2827 0.0261  0.0101  -0.0101 96  LEU B N   
4365  C CA  . LEU B 96  ? 0.2522 0.2433 0.2491 0.0230  0.0116  -0.0092 96  LEU B CA  
4366  C C   . LEU B 96  ? 0.2985 0.2848 0.2917 0.0219  0.0112  -0.0084 96  LEU B C   
4367  O O   . LEU B 96  ? 0.2819 0.2649 0.2734 0.0221  0.0093  -0.0080 96  LEU B O   
4368  C CB  . LEU B 96  ? 0.2351 0.2282 0.2343 0.0216  0.0103  -0.0091 96  LEU B CB  
4369  C CG  . LEU B 96  ? 0.2579 0.2500 0.2567 0.0188  0.0111  -0.0086 96  LEU B CG  
4370  C CD1 . LEU B 96  ? 0.3009 0.2953 0.3019 0.0173  0.0135  -0.0086 96  LEU B CD1 
4371  C CD2 . LEU B 96  ? 0.3023 0.2958 0.3021 0.0180  0.0091  -0.0089 96  LEU B CD2 
4372  N N   . THR B 97  ? 0.2897 0.2758 0.2820 0.0206  0.0131  -0.0079 97  THR B N   
4373  C CA  . THR B 97  ? 0.2372 0.2200 0.2269 0.0196  0.0127  -0.0071 97  THR B CA  
4374  C C   . THR B 97  ? 0.2857 0.2692 0.2765 0.0176  0.0133  -0.0065 97  THR B C   
4375  O O   . THR B 97  ? 0.3029 0.2881 0.2955 0.0167  0.0148  -0.0066 97  THR B O   
4376  C CB  . THR B 97  ? 0.2728 0.2543 0.2598 0.0204  0.0138  -0.0070 97  THR B CB  
4377  O OG1 . THR B 97  ? 0.3045 0.2846 0.2899 0.0224  0.0125  -0.0081 97  THR B OG1 
4378  C CG2 . THR B 97  ? 0.2896 0.2690 0.2747 0.0195  0.0133  -0.0061 97  THR B CG2 
4379  N N   . GLN B 98  ? 0.2822 0.2643 0.2719 0.0170  0.0120  -0.0060 98  GLN B N   
4380  C CA  . GLN B 98  ? 0.2540 0.2364 0.2439 0.0158  0.0120  -0.0060 98  GLN B CA  
4381  C C   . GLN B 98  ? 0.2621 0.2436 0.2518 0.0150  0.0137  -0.0060 98  GLN B C   
4382  O O   . GLN B 98  ? 0.2867 0.2665 0.2745 0.0155  0.0145  -0.0053 98  GLN B O   
4383  C CB  . GLN B 98  ? 0.3098 0.2913 0.2979 0.0159  0.0111  -0.0051 98  GLN B CB  
4384  C CG  . GLN B 98  ? 0.2866 0.2683 0.2738 0.0155  0.0113  -0.0050 98  GLN B CG  
4385  C CD  . GLN B 98  ? 0.2870 0.2691 0.2729 0.0156  0.0106  -0.0037 98  GLN B CD  
4386  O OE1 . GLN B 98  ? 0.3262 0.3089 0.3119 0.0157  0.0096  -0.0031 98  GLN B OE1 
4387  N NE2 . GLN B 98  ? 0.2855 0.2677 0.2709 0.0156  0.0113  -0.0029 98  GLN B NE2 
4388  N N   A SER B 99  ? 0.2786 0.2607 0.2698 0.0139  0.0138  -0.0068 99  SER B N   
4389  N N   B SER B 99  ? 0.2787 0.2609 0.2702 0.0139  0.0139  -0.0068 99  SER B N   
4390  C CA  A SER B 99  ? 0.2689 0.2488 0.2599 0.0128  0.0151  -0.0068 99  SER B CA  
4391  C CA  B SER B 99  ? 0.2688 0.2486 0.2596 0.0129  0.0149  -0.0069 99  SER B CA  
4392  C C   A SER B 99  ? 0.2912 0.2711 0.2832 0.0117  0.0139  -0.0084 99  SER B C   
4393  C C   B SER B 99  ? 0.2913 0.2718 0.2837 0.0117  0.0137  -0.0085 99  SER B C   
4394  O O   A SER B 99  ? 0.3071 0.2871 0.2973 0.0125  0.0126  -0.0090 99  SER B O   
4395  O O   B SER B 99  ? 0.2810 0.2625 0.2723 0.0124  0.0121  -0.0091 99  SER B O   
4396  C CB  A SER B 99  ? 0.2865 0.2666 0.2791 0.0121  0.0170  -0.0061 99  SER B CB  
4397  C CB  B SER B 99  ? 0.2818 0.2605 0.2732 0.0123  0.0171  -0.0059 99  SER B CB  
4398  O OG  A SER B 99  ? 0.3250 0.3092 0.3214 0.0114  0.0168  -0.0068 99  SER B OG  
4399  O OG  B SER B 99  ? 0.3043 0.2790 0.2936 0.0121  0.0180  -0.0054 99  SER B OG  
4400  N N   . CYS B 100 ? 0.2797 0.2599 0.2747 0.0097  0.0144  -0.0091 100 CYS B N   
4401  C CA  . CYS B 100 ? 0.2836 0.2641 0.2802 0.0083  0.0127  -0.0111 100 CYS B CA  
4402  C C   . CYS B 100 ? 0.2584 0.2429 0.2556 0.0092  0.0104  -0.0122 100 CYS B C   
4403  O O   . CYS B 100 ? 0.2718 0.2600 0.2712 0.0099  0.0102  -0.0116 100 CYS B O   
4404  C CB  . CYS B 100 ? 0.3360 0.3175 0.3373 0.0055  0.0136  -0.0113 100 CYS B CB  
4405  S SG  . CYS B 100 ? 0.3137 0.2966 0.3185 0.0031  0.0108  -0.0143 100 CYS B SG  
4406  N N   . ILE B 101 ? 0.2715 0.2552 0.2664 0.0096  0.0085  -0.0138 101 ILE B N   
4407  C CA  . ILE B 101 ? 0.2434 0.2305 0.2377 0.0110  0.0063  -0.0143 101 ILE B CA  
4408  C C   . ILE B 101 ? 0.2467 0.2383 0.2459 0.0099  0.0046  -0.0156 101 ILE B C   
4409  O O   . ILE B 101 ? 0.2765 0.2715 0.2761 0.0114  0.0031  -0.0154 101 ILE B O   
4410  C CB  . ILE B 101 ? 0.2430 0.2288 0.2325 0.0124  0.0049  -0.0154 101 ILE B CB  
4411  C CG1 . ILE B 101 ? 0.2809 0.2650 0.2705 0.0111  0.0035  -0.0184 101 ILE B CG1 
4412  C CG2 . ILE B 101 ? 0.2527 0.2361 0.2383 0.0139  0.0067  -0.0137 101 ILE B CG2 
4413  C CD1 . ILE B 101 ? 0.3190 0.3025 0.3034 0.0130  0.0017  -0.0202 101 ILE B CD1 
4414  N N   . GLN B 102 ? 0.2421 0.2339 0.2453 0.0072  0.0047  -0.0170 102 GLN B N   
4415  C CA  . GLN B 102 ? 0.2491 0.2466 0.2583 0.0058  0.0032  -0.0183 102 GLN B CA  
4416  C C   . GLN B 102 ? 0.2981 0.2999 0.3104 0.0069  0.0046  -0.0165 102 GLN B C   
4417  O O   . GLN B 102 ? 0.3048 0.3120 0.3200 0.0081  0.0028  -0.0171 102 GLN B O   
4418  C CB  . GLN B 102 ? 0.2562 0.2530 0.2700 0.0019  0.0035  -0.0195 102 GLN B CB  
4419  C CG  . GLN B 102 ? 0.2594 0.2507 0.2696 0.0011  0.0016  -0.0220 102 GLN B CG  
4420  C CD  . GLN B 102 ? 0.2919 0.2829 0.3074 -0.0031 0.0005  -0.0241 102 GLN B CD  
4421  O OE1 . GLN B 102 ? 0.2963 0.2934 0.3191 -0.0054 0.0001  -0.0242 102 GLN B OE1 
4422  N NE2 . GLN B 102 ? 0.3020 0.2860 0.3143 -0.0040 -0.0003 -0.0259 102 GLN B NE2 
4423  N N   . TYR B 103 ? 0.2854 0.2851 0.2970 0.0070  0.0077  -0.0144 103 TYR B N   
4424  C CA  . TYR B 103 ? 0.2618 0.2650 0.2756 0.0085  0.0092  -0.0131 103 TYR B CA  
4425  C C   . TYR B 103 ? 0.3161 0.3196 0.3269 0.0119  0.0076  -0.0127 103 TYR B C   
4426  O O   . TYR B 103 ? 0.3071 0.3142 0.3202 0.0137  0.0076  -0.0125 103 TYR B O   
4427  C CB  . TYR B 103 ? 0.3557 0.3553 0.3673 0.0084  0.0124  -0.0112 103 TYR B CB  
4428  C CG  . TYR B 103 ? 0.3126 0.3158 0.3272 0.0086  0.0150  -0.0101 103 TYR B CG  
4429  C CD1 . TYR B 103 ? 0.3559 0.3647 0.3734 0.0107  0.0148  -0.0104 103 TYR B CD1 
4430  C CD2 . TYR B 103 ? 0.4139 0.4145 0.4277 0.0071  0.0180  -0.0085 103 TYR B CD2 
4431  C CE1 . TYR B 103 ? 0.3475 0.3600 0.3672 0.0114  0.0177  -0.0094 103 TYR B CE1 
4432  C CE2 . TYR B 103 ? 0.3722 0.3761 0.3878 0.0075  0.0209  -0.0071 103 TYR B CE2 
4433  C CZ  . TYR B 103 ? 0.4279 0.4380 0.4464 0.0097  0.0209  -0.0076 103 TYR B CZ  
4434  O OH  . TYR B 103 ? 0.4601 0.4741 0.4798 0.0107  0.0242  -0.0064 103 TYR B OH  
4435  N N   . ARG B 104 ? 0.3070 0.3064 0.3127 0.0128  0.0065  -0.0125 104 ARG B N   
4436  C CA  . ARG B 104 ? 0.3109 0.3098 0.3137 0.0155  0.0049  -0.0116 104 ARG B CA  
4437  C C   . ARG B 104 ? 0.3098 0.3132 0.3149 0.0169  0.0022  -0.0126 104 ARG B C   
4438  O O   . ARG B 104 ? 0.2821 0.2858 0.2863 0.0195  0.0012  -0.0117 104 ARG B O   
4439  C CB  . ARG B 104 ? 0.3116 0.3063 0.3091 0.0157  0.0046  -0.0108 104 ARG B CB  
4440  C CG  . ARG B 104 ? 0.3089 0.3000 0.3046 0.0148  0.0069  -0.0098 104 ARG B CG  
4441  C CD  . ARG B 104 ? 0.3163 0.3047 0.3076 0.0152  0.0068  -0.0090 104 ARG B CD  
4442  N NE  . ARG B 104 ? 0.2751 0.2609 0.2652 0.0145  0.0087  -0.0088 104 ARG B NE  
4443  C CZ  . ARG B 104 ? 0.2742 0.2587 0.2612 0.0150  0.0091  -0.0080 104 ARG B CZ  
4444  N NH1 . ARG B 104 ? 0.2652 0.2505 0.2500 0.0160  0.0082  -0.0070 104 ARG B NH1 
4445  N NH2 . ARG B 104 ? 0.2856 0.2681 0.2718 0.0149  0.0105  -0.0079 104 ARG B NH2 
4446  N N   . GLN B 105 ? 0.2964 0.3033 0.3046 0.0153  0.0008  -0.0145 105 GLN B N   
4447  C CA  . GLN B 105 ? 0.3263 0.3388 0.3377 0.0166  -0.0020 -0.0156 105 GLN B CA  
4448  C C   . GLN B 105 ? 0.3282 0.3460 0.3453 0.0177  -0.0011 -0.0155 105 GLN B C   
4449  O O   . GLN B 105 ? 0.2943 0.3153 0.3123 0.0208  -0.0031 -0.0155 105 GLN B O   
4450  C CB  . GLN B 105 ? 0.3319 0.3471 0.3458 0.0142  -0.0040 -0.0181 105 GLN B CB  
4451  C CG  . GLN B 105 ? 0.2898 0.3002 0.2977 0.0140  -0.0049 -0.0187 105 GLN B CG  
4452  C CD  . GLN B 105 ? 0.2897 0.3020 0.3000 0.0116  -0.0073 -0.0218 105 GLN B CD  
4453  O OE1 . GLN B 105 ? 0.3053 0.3196 0.3137 0.0129  -0.0106 -0.0234 105 GLN B OE1 
4454  N NE2 . GLN B 105 ? 0.2805 0.2924 0.2953 0.0081  -0.0057 -0.0227 105 GLN B NE2 
4455  N N   . THR B 106 ? 0.2552 0.2743 0.2760 0.0156  0.0018  -0.0154 106 THR B N   
4456  C CA  . THR B 106 ? 0.2566 0.2812 0.2823 0.0171  0.0033  -0.0152 106 THR B CA  
4457  C C   . THR B 106 ? 0.2803 0.3020 0.3019 0.0213  0.0031  -0.0141 106 THR B C   
4458  O O   . THR B 106 ? 0.2895 0.3154 0.3135 0.0244  0.0017  -0.0146 106 THR B O   
4459  C CB  . THR B 106 ? 0.2809 0.3059 0.3090 0.0146  0.0071  -0.0144 106 THR B CB  
4460  O OG1 . THR B 106 ? 0.2977 0.3236 0.3292 0.0103  0.0071  -0.0152 106 THR B OG1 
4461  C CG2 . THR B 106 ? 0.2654 0.2977 0.2990 0.0161  0.0092  -0.0142 106 THR B CG2 
4462  N N   . PHE B 107 ? 0.2673 0.2817 0.2831 0.0213  0.0042  -0.0129 107 PHE B N   
4463  C CA  . PHE B 107 ? 0.2528 0.2629 0.2645 0.0246  0.0038  -0.0119 107 PHE B CA  
4464  C C   . PHE B 107 ? 0.2619 0.2713 0.2718 0.0271  0.0005  -0.0117 107 PHE B C   
4465  O O   . PHE B 107 ? 0.2756 0.2850 0.2854 0.0306  -0.0006 -0.0116 107 PHE B O   
4466  C CB  . PHE B 107 ? 0.2313 0.2345 0.2380 0.0233  0.0051  -0.0107 107 PHE B CB  
4467  C CG  . PHE B 107 ? 0.2611 0.2590 0.2637 0.0257  0.0042  -0.0098 107 PHE B CG  
4468  C CD1 . PHE B 107 ? 0.2564 0.2536 0.2589 0.0278  0.0052  -0.0103 107 PHE B CD1 
4469  C CD2 . PHE B 107 ? 0.2747 0.2681 0.2735 0.0257  0.0023  -0.0085 107 PHE B CD2 
4470  C CE1 . PHE B 107 ? 0.2649 0.2561 0.2637 0.0299  0.0039  -0.0099 107 PHE B CE1 
4471  C CE2 . PHE B 107 ? 0.2896 0.2777 0.2854 0.0272  0.0014  -0.0074 107 PHE B CE2 
4472  C CZ  . PHE B 107 ? 0.3078 0.2942 0.3036 0.0292  0.0020  -0.0084 107 PHE B CZ  
4473  N N   . GLY B 108 ? 0.2860 0.2945 0.2937 0.0258  -0.0013 -0.0115 108 GLY B N   
4474  C CA  . GLY B 108 ? 0.2538 0.2607 0.2583 0.0283  -0.0042 -0.0106 108 GLY B CA  
4475  C C   . GLY B 108 ? 0.2967 0.3101 0.3054 0.0310  -0.0066 -0.0117 108 GLY B C   
4476  O O   . GLY B 108 ? 0.3290 0.3409 0.3360 0.0347  -0.0084 -0.0108 108 GLY B O   
4477  N N   . SER B 109 ? 0.2522 0.2728 0.2666 0.0293  -0.0068 -0.0137 109 SER B N   
4478  C CA  . SER B 109 ? 0.2552 0.2835 0.2749 0.0318  -0.0090 -0.0150 109 SER B CA  
4479  C C   . SER B 109 ? 0.2852 0.3158 0.3081 0.0349  -0.0075 -0.0150 109 SER B C   
4480  O O   . SER B 109 ? 0.2686 0.3023 0.2929 0.0391  -0.0096 -0.0152 109 SER B O   
4481  C CB  . SER B 109 ? 0.3423 0.3782 0.3685 0.0284  -0.0096 -0.0172 109 SER B CB  
4482  O OG  . SER B 109 ? 0.2990 0.3329 0.3217 0.0266  -0.0119 -0.0179 109 SER B OG  
4483  N N   . TRP B 110 ? 0.2559 0.2853 0.2796 0.0332  -0.0038 -0.0148 110 TRP B N   
4484  C CA  . TRP B 110 ? 0.2539 0.2855 0.2798 0.0365  -0.0020 -0.0151 110 TRP B CA  
4485  C C   . TRP B 110 ? 0.2538 0.2782 0.2741 0.0411  -0.0036 -0.0143 110 TRP B C   
4486  O O   . TRP B 110 ? 0.2843 0.3114 0.3063 0.0457  -0.0046 -0.0149 110 TRP B O   
4487  C CB  . TRP B 110 ? 0.2644 0.2948 0.2904 0.0339  0.0021  -0.0149 110 TRP B CB  
4488  C CG  . TRP B 110 ? 0.2391 0.2724 0.2668 0.0368  0.0046  -0.0154 110 TRP B CG  
4489  C CD1 . TRP B 110 ? 0.2807 0.3094 0.3045 0.0414  0.0043  -0.0156 110 TRP B CD1 
4490  C CD2 . TRP B 110 ? 0.2542 0.2952 0.2875 0.0353  0.0081  -0.0157 110 TRP B CD2 
4491  N NE1 . TRP B 110 ? 0.3065 0.3400 0.3326 0.0433  0.0074  -0.0164 110 TRP B NE1 
4492  C CE2 . TRP B 110 ? 0.2902 0.3316 0.3222 0.0396  0.0100  -0.0162 110 TRP B CE2 
4493  C CE3 . TRP B 110 ? 0.2515 0.2986 0.2907 0.0306  0.0099  -0.0154 110 TRP B CE3 
4494  C CZ2 . TRP B 110 ? 0.2770 0.3258 0.3131 0.0397  0.0141  -0.0162 110 TRP B CZ2 
4495  C CZ3 . TRP B 110 ? 0.2607 0.3144 0.3043 0.0301  0.0139  -0.0150 110 TRP B CZ3 
4496  C CH2 . TRP B 110 ? 0.2864 0.3414 0.3284 0.0347  0.0161  -0.0153 110 TRP B CH2 
4497  N N   . ARG B 111 ? 0.2807 0.2956 0.2944 0.0398  -0.0037 -0.0128 111 ARG B N   
4498  C CA  . ARG B 111 ? 0.3094 0.3166 0.3181 0.0433  -0.0053 -0.0118 111 ARG B CA  
4499  C C   . ARG B 111 ? 0.3223 0.3298 0.3302 0.0466  -0.0089 -0.0110 111 ARG B C   
4500  O O   . ARG B 111 ? 0.3170 0.3203 0.3228 0.0509  -0.0105 -0.0107 111 ARG B O   
4501  C CB  . ARG B 111 ? 0.3352 0.3332 0.3382 0.0406  -0.0047 -0.0101 111 ARG B CB  
4502  C CG  . ARG B 111 ? 0.3541 0.3494 0.3538 0.0383  -0.0061 -0.0082 111 ARG B CG  
4503  C CD  . ARG B 111 ? 0.3756 0.3634 0.3709 0.0354  -0.0048 -0.0066 111 ARG B CD  
4504  N NE  . ARG B 111 ? 0.4747 0.4608 0.4668 0.0336  -0.0057 -0.0045 111 ARG B NE  
4505  C CZ  . ARG B 111 ? 0.5336 0.5164 0.5224 0.0353  -0.0079 -0.0024 111 ARG B CZ  
4506  N NH1 . ARG B 111 ? 0.5828 0.5631 0.5711 0.0391  -0.0099 -0.0020 111 ARG B NH1 
4507  N NH2 . ARG B 111 ? 0.6014 0.5835 0.5868 0.0337  -0.0081 -0.0005 111 ARG B NH2 
4508  N N   . LEU B 112 ? 0.2897 0.3018 0.2988 0.0450  -0.0105 -0.0109 112 LEU B N   
4509  C CA  . LEU B 112 ? 0.2982 0.3106 0.3056 0.0485  -0.0142 -0.0100 112 LEU B CA  
4510  C C   . LEU B 112 ? 0.3465 0.3681 0.3602 0.0526  -0.0158 -0.0118 112 LEU B C   
4511  O O   . LEU B 112 ? 0.3573 0.3778 0.3693 0.0574  -0.0187 -0.0111 112 LEU B O   
4512  C CB  . LEU B 112 ? 0.3141 0.3283 0.3197 0.0459  -0.0158 -0.0095 112 LEU B CB  
4513  C CG  . LEU B 112 ? 0.4033 0.4095 0.4017 0.0437  -0.0156 -0.0070 112 LEU B CG  
4514  C CD1 . LEU B 112 ? 0.3665 0.3768 0.3643 0.0410  -0.0166 -0.0078 112 LEU B CD1 
4515  C CD2 . LEU B 112 ? 0.3970 0.3957 0.3894 0.0472  -0.0176 -0.0039 112 LEU B CD2 
4516  N N   . HIS B 113 ? 0.2745 0.3053 0.2955 0.0507  -0.0139 -0.0140 113 HIS B N   
4517  C CA  . HIS B 113 ? 0.2715 0.3138 0.3001 0.0536  -0.0155 -0.0158 113 HIS B CA  
4518  C C   . HIS B 113 ? 0.3117 0.3603 0.3462 0.0559  -0.0127 -0.0173 113 HIS B C   
4519  O O   . HIS B 113 ? 0.3072 0.3657 0.3481 0.0592  -0.0140 -0.0186 113 HIS B O   
4520  C CB  . HIS B 113 ? 0.2737 0.3242 0.3074 0.0493  -0.0164 -0.0172 113 HIS B CB  
4521  C CG  . HIS B 113 ? 0.3041 0.3505 0.3321 0.0485  -0.0197 -0.0163 113 HIS B CG  
4522  N ND1 . HIS B 113 ? 0.3514 0.3988 0.3772 0.0529  -0.0239 -0.0158 113 HIS B ND1 
4523  C CD2 . HIS B 113 ? 0.3161 0.3576 0.3397 0.0442  -0.0193 -0.0159 113 HIS B CD2 
4524  C CE1 . HIS B 113 ? 0.3489 0.3924 0.3689 0.0513  -0.0259 -0.0150 113 HIS B CE1 
4525  N NE2 . HIS B 113 ? 0.2927 0.3326 0.3114 0.0461  -0.0230 -0.0151 113 HIS B NE2 
4526  N N   . VAL B 114 ? 0.3087 0.3527 0.3411 0.0546  -0.0090 -0.0172 114 VAL B N   
4527  C CA  . VAL B 114 ? 0.2816 0.3312 0.3183 0.0575  -0.0061 -0.0185 114 VAL B CA  
4528  C C   . VAL B 114 ? 0.3003 0.3426 0.3318 0.0641  -0.0076 -0.0185 114 VAL B C   
4529  O O   . VAL B 114 ? 0.3112 0.3418 0.3354 0.0637  -0.0074 -0.0176 114 VAL B O   
4530  C CB  . VAL B 114 ? 0.2932 0.3416 0.3296 0.0534  -0.0016 -0.0184 114 VAL B CB  
4531  C CG1 . VAL B 114 ? 0.3024 0.3563 0.3416 0.0572  0.0016  -0.0196 114 VAL B CG1 
4532  C CG2 . VAL B 114 ? 0.2644 0.3194 0.3062 0.0471  -0.0004 -0.0183 114 VAL B CG2 
4533  N N   . PRO B 115 ? 0.3126 0.3612 0.3478 0.0700  -0.0093 -0.0196 115 PRO B N   
4534  C CA  . PRO B 115 ? 0.3349 0.3743 0.3641 0.0764  -0.0119 -0.0194 115 PRO B CA  
4535  C C   . PRO B 115 ? 0.3673 0.4010 0.3931 0.0795  -0.0094 -0.0208 115 PRO B C   
4536  O O   . PRO B 115 ? 0.3585 0.3814 0.3781 0.0837  -0.0116 -0.0206 115 PRO B O   
4537  C CB  . PRO B 115 ? 0.3527 0.4021 0.3877 0.0820  -0.0146 -0.0203 115 PRO B CB  
4538  C CG  . PRO B 115 ? 0.3793 0.4445 0.4244 0.0799  -0.0117 -0.0219 115 PRO B CG  
4539  C CD  . PRO B 115 ? 0.2964 0.3604 0.3414 0.0712  -0.0094 -0.0210 115 PRO B CD  
4540  N N   . THR B 116 ? 0.3262 0.3659 0.3551 0.0775  -0.0051 -0.0220 116 THR B N   
4541  C CA  . THR B 116 ? 0.3046 0.3388 0.3292 0.0800  -0.0027 -0.0235 116 THR B CA  
4542  C C   . THR B 116 ? 0.3219 0.3439 0.3392 0.0754  -0.0021 -0.0225 116 THR B C   
4543  O O   . THR B 116 ? 0.3275 0.3437 0.3403 0.0774  -0.0008 -0.0239 116 THR B O   
4544  C CB  . THR B 116 ? 0.3242 0.3713 0.3551 0.0804  0.0019  -0.0248 116 THR B CB  
4545  O OG1 . THR B 116 ? 0.3351 0.3889 0.3709 0.0731  0.0039  -0.0233 116 THR B OG1 
4546  C CG2 . THR B 116 ? 0.3306 0.3896 0.3685 0.0866  0.0014  -0.0262 116 THR B CG2 
4547  N N   . VAL B 117 ? 0.3444 0.3624 0.3603 0.0696  -0.0033 -0.0203 117 VAL B N   
4548  C CA  . VAL B 117 ? 0.3147 0.3218 0.3243 0.0655  -0.0031 -0.0192 117 VAL B CA  
4549  C C   . VAL B 117 ? 0.3367 0.3310 0.3397 0.0688  -0.0062 -0.0191 117 VAL B C   
4550  O O   . VAL B 117 ? 0.3642 0.3553 0.3663 0.0705  -0.0094 -0.0176 117 VAL B O   
4551  C CB  . VAL B 117 ? 0.3279 0.3350 0.3379 0.0592  -0.0034 -0.0170 117 VAL B CB  
4552  C CG1 . VAL B 117 ? 0.3276 0.3240 0.3315 0.0554  -0.0033 -0.0157 117 VAL B CG1 
4553  C CG2 . VAL B 117 ? 0.3207 0.3391 0.3371 0.0555  -0.0005 -0.0172 117 VAL B CG2 
4554  N N   . LYS B 118 ? 0.3389 0.3256 0.3373 0.0695  -0.0055 -0.0205 118 LYS B N   
4555  C CA  . LYS B 118 ? 0.3381 0.3109 0.3302 0.0713  -0.0085 -0.0205 118 LYS B CA  
4556  C C   . LYS B 118 ? 0.3887 0.3534 0.3773 0.0651  -0.0089 -0.0185 118 LYS B C   
4557  O O   . LYS B 118 ? 0.3647 0.3189 0.3494 0.0646  -0.0117 -0.0170 118 LYS B O   
4558  C CB  . LYS B 118 ? 0.3299 0.2993 0.3192 0.0766  -0.0082 -0.0240 118 LYS B CB  
4559  C CG  . LYS B 118 ? 0.4088 0.3866 0.4015 0.0836  -0.0074 -0.0262 118 LYS B CG  
4560  C CD  . LYS B 118 ? 0.5109 0.4907 0.5064 0.0867  -0.0103 -0.0246 118 LYS B CD  
4561  C CE  . LYS B 118 ? 0.5915 0.5859 0.5939 0.0916  -0.0087 -0.0262 118 LYS B CE  
4562  N NZ  . LYS B 118 ? 0.5437 0.5412 0.5490 0.0947  -0.0120 -0.0247 118 LYS B NZ  
4563  N N   . TRP B 119 ? 0.3065 0.2759 0.2965 0.0602  -0.0062 -0.0181 119 TRP B N   
4564  C CA  . TRP B 119 ? 0.3188 0.2818 0.3061 0.0547  -0.0067 -0.0160 119 TRP B CA  
4565  C C   . TRP B 119 ? 0.3525 0.3232 0.3426 0.0501  -0.0040 -0.0150 119 TRP B C   
4566  O O   . TRP B 119 ? 0.3492 0.3286 0.3428 0.0507  -0.0014 -0.0162 119 TRP B O   
4567  C CB  . TRP B 119 ? 0.3259 0.2803 0.3088 0.0546  -0.0074 -0.0177 119 TRP B CB  
4568  C CG  . TRP B 119 ? 0.3330 0.2921 0.3157 0.0559  -0.0047 -0.0205 119 TRP B CG  
4569  C CD1 . TRP B 119 ? 0.3869 0.3472 0.3685 0.0614  -0.0042 -0.0237 119 TRP B CD1 
4570  C CD2 . TRP B 119 ? 0.3919 0.3547 0.3748 0.0519  -0.0022 -0.0202 119 TRP B CD2 
4571  N NE1 . TRP B 119 ? 0.4145 0.3792 0.3953 0.0609  -0.0013 -0.0251 119 TRP B NE1 
4572  C CE2 . TRP B 119 ? 0.3800 0.3460 0.3616 0.0551  -0.0002 -0.0229 119 TRP B CE2 
4573  C CE3 . TRP B 119 ? 0.3276 0.2913 0.3114 0.0464  -0.0015 -0.0179 119 TRP B CE3 
4574  C CZ2 . TRP B 119 ? 0.3764 0.3460 0.3572 0.0527  0.0025  -0.0229 119 TRP B CZ2 
4575  C CZ3 . TRP B 119 ? 0.4056 0.3727 0.3889 0.0443  0.0010  -0.0182 119 TRP B CZ3 
4576  C CH2 . TRP B 119 ? 0.3891 0.3589 0.3708 0.0474  0.0029  -0.0206 119 TRP B CH2 
4577  N N   . ASP B 120 ? 0.3270 0.2946 0.3160 0.0455  -0.0044 -0.0127 120 ASP B N   
4578  C CA  . ASP B 120 ? 0.2848 0.2582 0.2758 0.0413  -0.0020 -0.0118 120 ASP B CA  
4579  C C   . ASP B 120 ? 0.3209 0.2888 0.3091 0.0373  -0.0021 -0.0105 120 ASP B C   
4580  O O   . ASP B 120 ? 0.3377 0.2983 0.3235 0.0369  -0.0041 -0.0094 120 ASP B O   
4581  C CB  . ASP B 120 ? 0.3102 0.2890 0.3039 0.0401  -0.0024 -0.0104 120 ASP B CB  
4582  C CG  . ASP B 120 ? 0.3564 0.3298 0.3473 0.0390  -0.0046 -0.0078 120 ASP B CG  
4583  O OD1 . ASP B 120 ? 0.3725 0.3440 0.3619 0.0352  -0.0040 -0.0062 120 ASP B OD1 
4584  O OD2 . ASP B 120 ? 0.4221 0.3934 0.4123 0.0422  -0.0068 -0.0073 120 ASP B OD2 
4585  N N   . TYR B 121 ? 0.2997 0.2713 0.2889 0.0344  0.0002  -0.0105 121 TYR B N   
4586  C CA  . TYR B 121 ? 0.2665 0.2345 0.2538 0.0308  0.0002  -0.0092 121 TYR B CA  
4587  C C   . TYR B 121 ? 0.3128 0.2859 0.3017 0.0280  0.0024  -0.0085 121 TYR B C   
4588  O O   . TYR B 121 ? 0.3060 0.2835 0.2963 0.0282  0.0045  -0.0096 121 TYR B O   
4589  C CB  . TYR B 121 ? 0.2955 0.2593 0.2804 0.0313  -0.0001 -0.0108 121 TYR B CB  
4590  C CG  . TYR B 121 ? 0.3091 0.2688 0.2928 0.0279  -0.0011 -0.0095 121 TYR B CG  
4591  C CD1 . TYR B 121 ? 0.3077 0.2705 0.2917 0.0254  0.0005  -0.0089 121 TYR B CD1 
4592  C CD2 . TYR B 121 ? 0.3390 0.2918 0.3215 0.0273  -0.0037 -0.0086 121 TYR B CD2 
4593  C CE1 . TYR B 121 ? 0.2982 0.2587 0.2820 0.0224  -0.0003 -0.0077 121 TYR B CE1 
4594  C CE2 . TYR B 121 ? 0.3040 0.2541 0.2865 0.0236  -0.0045 -0.0072 121 TYR B CE2 
4595  C CZ  . TYR B 121 ? 0.2982 0.2529 0.2816 0.0214  -0.0028 -0.0069 121 TYR B CZ  
4596  O OH  . TYR B 121 ? 0.3046 0.2581 0.2888 0.0181  -0.0036 -0.0056 121 TYR B OH  
4597  N N   . TYR B 122 ? 0.2796 0.2519 0.2680 0.0254  0.0021  -0.0065 122 TYR B N   
4598  C CA  . TYR B 122 ? 0.2687 0.2445 0.2578 0.0230  0.0039  -0.0060 122 TYR B CA  
4599  C C   . TYR B 122 ? 0.2959 0.2692 0.2835 0.0211  0.0042  -0.0054 122 TYR B C   
4600  O O   . TYR B 122 ? 0.2952 0.2655 0.2820 0.0199  0.0029  -0.0039 122 TYR B O   
4601  C CB  . TYR B 122 ? 0.2683 0.2455 0.2574 0.0221  0.0032  -0.0046 122 TYR B CB  
4602  C CG  . TYR B 122 ? 0.2601 0.2400 0.2494 0.0201  0.0047  -0.0043 122 TYR B CG  
4603  C CD1 . TYR B 122 ? 0.2578 0.2363 0.2456 0.0184  0.0052  -0.0030 122 TYR B CD1 
4604  C CD2 . TYR B 122 ? 0.3695 0.3533 0.3607 0.0200  0.0052  -0.0055 122 TYR B CD2 
4605  C CE1 . TYR B 122 ? 0.2609 0.2417 0.2485 0.0173  0.0065  -0.0030 122 TYR B CE1 
4606  C CE2 . TYR B 122 ? 0.3573 0.3424 0.3482 0.0184  0.0062  -0.0057 122 TYR B CE2 
4607  C CZ  . TYR B 122 ? 0.3254 0.3087 0.3141 0.0174  0.0069  -0.0045 122 TYR B CZ  
4608  O OH  . TYR B 122 ? 0.3353 0.3194 0.3233 0.0165  0.0078  -0.0050 122 TYR B OH  
4609  N N   . VAL B 123 ? 0.2771 0.2522 0.2648 0.0206  0.0059  -0.0061 123 VAL B N   
4610  C CA  . VAL B 123 ? 0.2837 0.2575 0.2703 0.0193  0.0060  -0.0058 123 VAL B CA  
4611  C C   . VAL B 123 ? 0.2817 0.2578 0.2687 0.0177  0.0073  -0.0046 123 VAL B C   
4612  O O   . VAL B 123 ? 0.2823 0.2604 0.2696 0.0177  0.0089  -0.0051 123 VAL B O   
4613  C CB  . VAL B 123 ? 0.2829 0.2568 0.2681 0.0205  0.0069  -0.0072 123 VAL B CB  
4614  C CG1 . VAL B 123 ? 0.3009 0.2737 0.2849 0.0195  0.0064  -0.0069 123 VAL B CG1 
4615  C CG2 . VAL B 123 ? 0.3281 0.3005 0.3125 0.0230  0.0062  -0.0089 123 VAL B CG2 
4616  N N   . PRO B 124 ? 0.2978 0.2736 0.2847 0.0162  0.0067  -0.0031 124 PRO B N   
4617  C CA  . PRO B 124 ? 0.2825 0.2609 0.2695 0.0154  0.0080  -0.0023 124 PRO B CA  
4618  C C   . PRO B 124 ? 0.2730 0.2519 0.2597 0.0153  0.0087  -0.0025 124 PRO B C   
4619  O O   . PRO B 124 ? 0.3115 0.2916 0.2987 0.0145  0.0086  -0.0015 124 PRO B O   
4620  C CB  . PRO B 124 ? 0.3330 0.3116 0.3199 0.0144  0.0074  -0.0004 124 PRO B CB  
4621  C CG  . PRO B 124 ? 0.3724 0.3479 0.3596 0.0139  0.0057  0.0003  124 PRO B CG  
4622  C CD  . PRO B 124 ? 0.2912 0.2645 0.2782 0.0154  0.0050  -0.0018 124 PRO B CD  
4623  N N   . MET B 125 ? 0.2961 0.2747 0.2821 0.0163  0.0096  -0.0036 125 MET B N   
4624  C CA  . MET B 125 ? 0.2724 0.2513 0.2574 0.0168  0.0104  -0.0036 125 MET B CA  
4625  C C   . MET B 125 ? 0.2800 0.2603 0.2652 0.0165  0.0113  -0.0029 125 MET B C   
4626  O O   . MET B 125 ? 0.2980 0.2782 0.2832 0.0164  0.0122  -0.0032 125 MET B O   
4627  C CB  . MET B 125 ? 0.3022 0.2805 0.2862 0.0177  0.0119  -0.0042 125 MET B CB  
4628  C CG  . MET B 125 ? 0.3219 0.2997 0.3040 0.0186  0.0125  -0.0038 125 MET B CG  
4629  S SD  . MET B 125 ? 0.2968 0.2735 0.2769 0.0196  0.0146  -0.0037 125 MET B SD  
4630  C CE  . MET B 125 ? 0.3068 0.2825 0.2844 0.0208  0.0151  -0.0025 125 MET B CE  
4631  N N   . PRO B 126 ? 0.2585 0.2403 0.2438 0.0168  0.0112  -0.0023 126 PRO B N   
4632  C CA  . PRO B 126 ? 0.2533 0.2364 0.2383 0.0175  0.0123  -0.0019 126 PRO B CA  
4633  C C   . PRO B 126 ? 0.2488 0.2293 0.2321 0.0183  0.0136  -0.0026 126 PRO B C   
4634  O O   . PRO B 126 ? 0.2741 0.2527 0.2565 0.0186  0.0141  -0.0028 126 PRO B O   
4635  C CB  . PRO B 126 ? 0.2921 0.2773 0.2776 0.0182  0.0117  -0.0013 126 PRO B CB  
4636  C CG  . PRO B 126 ? 0.3080 0.2936 0.2950 0.0168  0.0099  -0.0012 126 PRO B CG  
4637  C CD  . PRO B 126 ? 0.3207 0.3031 0.3067 0.0165  0.0096  -0.0021 126 PRO B CD  
4638  N N   . ASN B 127 ? 0.2636 0.2441 0.2465 0.0185  0.0143  -0.0030 127 ASN B N   
4639  C CA  . ASN B 127 ? 0.2588 0.2361 0.2404 0.0190  0.0152  -0.0038 127 ASN B CA  
4640  C C   . ASN B 127 ? 0.2374 0.2139 0.2175 0.0211  0.0158  -0.0033 127 ASN B C   
4641  O O   . ASN B 127 ? 0.2721 0.2449 0.2507 0.0217  0.0165  -0.0031 127 ASN B O   
4642  C CB  . ASN B 127 ? 0.2476 0.2243 0.2287 0.0188  0.0152  -0.0051 127 ASN B CB  
4643  C CG  . ASN B 127 ? 0.2842 0.2609 0.2668 0.0170  0.0146  -0.0059 127 ASN B CG  
4644  O OD1 . ASN B 127 ? 0.2958 0.2724 0.2797 0.0161  0.0147  -0.0055 127 ASN B OD1 
4645  N ND2 . ASN B 127 ? 0.3205 0.2980 0.3026 0.0169  0.0139  -0.0070 127 ASN B ND2 
4646  N N   . GLU B 128 ? 0.2617 0.2416 0.2423 0.0223  0.0155  -0.0029 128 GLU B N   
4647  C CA  . GLU B 128 ? 0.2816 0.2613 0.2610 0.0250  0.0159  -0.0026 128 GLU B CA  
4648  C C   . GLU B 128 ? 0.2729 0.2538 0.2526 0.0256  0.0152  -0.0016 128 GLU B C   
4649  O O   . GLU B 128 ? 0.2857 0.2712 0.2671 0.0264  0.0144  -0.0010 128 GLU B O   
4650  C CB  . GLU B 128 ? 0.2818 0.2657 0.2618 0.0265  0.0163  -0.0027 128 GLU B CB  
4651  C CG  . GLU B 128 ? 0.3074 0.2905 0.2859 0.0300  0.0167  -0.0029 128 GLU B CG  
4652  C CD  . GLU B 128 ? 0.3201 0.3073 0.2987 0.0322  0.0176  -0.0035 128 GLU B CD  
4653  O OE1 . GLU B 128 ? 0.2988 0.2893 0.2781 0.0309  0.0179  -0.0035 128 GLU B OE1 
4654  O OE2 . GLU B 128 ? 0.3336 0.3211 0.3113 0.0357  0.0179  -0.0037 128 GLU B OE2 
4655  N N   . VAL B 129 ? 0.2490 0.2261 0.2270 0.0252  0.0154  -0.0013 129 VAL B N   
4656  C CA  . VAL B 129 ? 0.2683 0.2458 0.2451 0.0264  0.0146  -0.0005 129 VAL B CA  
4657  C C   . VAL B 129 ? 0.3165 0.2946 0.2921 0.0295  0.0143  0.0001  129 VAL B C   
4658  O O   . VAL B 129 ? 0.2901 0.2707 0.2656 0.0308  0.0129  0.0005  129 VAL B O   
4659  C CB  . VAL B 129 ? 0.2992 0.2727 0.2736 0.0258  0.0155  -0.0001 129 VAL B CB  
4660  C CG1 . VAL B 129 ? 0.2978 0.2723 0.2741 0.0232  0.0154  -0.0009 129 VAL B CG1 
4661  C CG2 . VAL B 129 ? 0.3165 0.2845 0.2886 0.0264  0.0172  0.0007  129 VAL B CG2 
4662  N N   . GLN B 130 ? 0.2673 0.2435 0.2422 0.0311  0.0153  -0.0002 130 GLN B N   
4663  C CA  . GLN B 130 ? 0.2652 0.2425 0.2392 0.0348  0.0149  0.0003  130 GLN B CA  
4664  C C   . GLN B 130 ? 0.2927 0.2781 0.2705 0.0355  0.0139  0.0001  130 GLN B C   
4665  O O   . GLN B 130 ? 0.3097 0.2979 0.2877 0.0387  0.0132  0.0005  130 GLN B O   
4666  C CB  . GLN B 130 ? 0.2800 0.2517 0.2516 0.0368  0.0161  -0.0002 130 GLN B CB  
4667  C CG  . GLN B 130 ? 0.2991 0.2626 0.2671 0.0365  0.0169  0.0008  130 GLN B CG  
4668  C CD  . GLN B 130 ? 0.3103 0.2670 0.2764 0.0373  0.0178  -0.0001 130 GLN B CD  
4669  O OE1 . GLN B 130 ? 0.2897 0.2466 0.2552 0.0405  0.0176  -0.0011 130 GLN B OE1 
4670  N NE2 . GLN B 130 ? 0.3322 0.2831 0.2976 0.0344  0.0187  -0.0001 130 GLN B NE2 
4671  N N   . SER B 131 ? 0.2736 0.2632 0.2546 0.0326  0.0138  -0.0002 131 SER B N   
4672  C CA  . SER B 131 ? 0.2694 0.2670 0.2546 0.0326  0.0133  0.0001  131 SER B CA  
4673  C C   . SER B 131 ? 0.2879 0.2895 0.2755 0.0320  0.0111  0.0006  131 SER B C   
4674  O O   . SER B 131 ? 0.2767 0.2755 0.2633 0.0300  0.0100  0.0003  131 SER B O   
4675  C CB  . SER B 131 ? 0.2886 0.2886 0.2762 0.0294  0.0139  0.0002  131 SER B CB  
4676  O OG  . SER B 131 ? 0.2982 0.3059 0.2904 0.0282  0.0133  0.0012  131 SER B OG  
4677  N N   . PRO B 132 ? 0.3048 0.3137 0.2959 0.0336  0.0102  0.0010  132 PRO B N   
4678  C CA  . PRO B 132 ? 0.2707 0.2843 0.2650 0.0325  0.0075  0.0010  132 PRO B CA  
4679  C C   . PRO B 132 ? 0.3138 0.3290 0.3115 0.0278  0.0065  0.0011  132 PRO B C   
4680  O O   . PRO B 132 ? 0.3159 0.3331 0.3155 0.0264  0.0038  0.0006  132 PRO B O   
4681  C CB  . PRO B 132 ? 0.3230 0.3453 0.3215 0.0351  0.0072  0.0015  132 PRO B CB  
4682  C CG  . PRO B 132 ? 0.3903 0.4128 0.3879 0.0374  0.0102  0.0017  132 PRO B CG  
4683  C CD  . PRO B 132 ? 0.3059 0.3184 0.2977 0.0373  0.0116  0.0011  132 PRO B CD  
4684  N N   . HIS B 133 ? 0.2989 0.3128 0.2970 0.0255  0.0083  0.0015  133 HIS B N   
4685  C CA  . HIS B 133 ? 0.2599 0.2740 0.2607 0.0211  0.0073  0.0019  133 HIS B CA  
4686  C C   . HIS B 133 ? 0.2952 0.3016 0.2922 0.0198  0.0072  0.0010  133 HIS B C   
4687  O O   . HIS B 133 ? 0.2789 0.2841 0.2775 0.0167  0.0061  0.0012  133 HIS B O   
4688  C CB  . HIS B 133 ? 0.2453 0.2640 0.2492 0.0198  0.0094  0.0034  133 HIS B CB  
4689  C CG  . HIS B 133 ? 0.2883 0.3159 0.2964 0.0214  0.0100  0.0043  133 HIS B CG  
4690  N ND1 . HIS B 133 ? 0.2964 0.3306 0.3101 0.0201  0.0078  0.0047  133 HIS B ND1 
4691  C CD2 . HIS B 133 ? 0.3069 0.3381 0.3146 0.0248  0.0123  0.0046  133 HIS B CD2 
4692  C CE1 . HIS B 133 ? 0.2987 0.3412 0.3159 0.0224  0.0090  0.0055  133 HIS B CE1 
4693  N NE2 . HIS B 133 ? 0.2991 0.3397 0.3123 0.0257  0.0118  0.0053  133 HIS B NE2 
4694  N N   . ALA B 134 ? 0.2173 0.2998 0.2770 0.0155  -0.0174 -0.0019 134 ALA B N   
4695  C CA  . ALA B 134 ? 0.2127 0.2850 0.2589 0.0133  -0.0181 -0.0048 134 ALA B CA  
4696  C C   . ALA B 134 ? 0.2072 0.2713 0.2492 0.0046  -0.0214 -0.0008 134 ALA B C   
4697  O O   . ALA B 134 ? 0.2518 0.3109 0.2842 0.0027  -0.0193 -0.0008 134 ALA B O   
4698  C CB  . ALA B 134 ? 0.2193 0.2845 0.2632 0.0165  -0.0221 -0.0112 134 ALA B CB  
4699  N N   . ARG B 135 ? 0.2060 0.2682 0.2540 0.0000  -0.0268 0.0023  135 ARG B N   
4700  C CA  . ARG B 135 ? 0.2107 0.2633 0.2505 -0.0074 -0.0306 0.0045  135 ARG B CA  
4701  C C   . ARG B 135 ? 0.2312 0.2844 0.2706 -0.0116 -0.0289 0.0080  135 ARG B C   
4702  O O   . ARG B 135 ? 0.2580 0.3015 0.2865 -0.0152 -0.0294 0.0074  135 ARG B O   
4703  C CB  . ARG B 135 ? 0.2435 0.2928 0.2866 -0.0109 -0.0380 0.0067  135 ARG B CB  
4704  C CG  . ARG B 135 ? 0.2471 0.2914 0.2878 -0.0083 -0.0397 0.0043  135 ARG B CG  
4705  C CD  . ARG B 135 ? 0.2755 0.3199 0.3241 -0.0090 -0.0465 0.0074  135 ARG B CD  
4706  N NE  . ARG B 135 ? 0.2785 0.3172 0.3262 -0.0068 -0.0478 0.0061  135 ARG B NE  
4707  C CZ  . ARG B 135 ? 0.2703 0.3108 0.3247 -0.0011 -0.0460 0.0019  135 ARG B CZ  
4708  N NH1 . ARG B 135 ? 0.2415 0.2901 0.3015 0.0044  -0.0418 -0.0017 135 ARG B NH1 
4709  N NH2 . ARG B 135 ? 0.2945 0.3281 0.3491 -0.0008 -0.0483 0.0015  135 ARG B NH2 
4710  N N   . LYS B 136 ? 0.2305 0.2948 0.2824 -0.0110 -0.0266 0.0119  136 LYS B N   
4711  C CA  . LYS B 136 ? 0.2270 0.2921 0.2807 -0.0152 -0.0243 0.0165  136 LYS B CA  
4712  C C   . LYS B 136 ? 0.2851 0.3475 0.3283 -0.0118 -0.0178 0.0152  136 LYS B C   
4713  O O   . LYS B 136 ? 0.2522 0.3056 0.2887 -0.0158 -0.0181 0.0164  136 LYS B O   
4714  C CB  . LYS B 136 ? 0.2181 0.2987 0.2905 -0.0150 -0.0221 0.0227  136 LYS B CB  
4715  C CG  . LYS B 136 ? 0.2650 0.3479 0.3441 -0.0206 -0.0197 0.0299  136 LYS B CG  
4716  C CD  . LYS B 136 ? 0.3183 0.3854 0.3907 -0.0291 -0.0276 0.0293  136 LYS B CD  
4717  C CE  . LYS B 136 ? 0.4141 0.4795 0.4905 -0.0335 -0.0250 0.0352  136 LYS B CE  
4718  N NZ  . LYS B 136 ? 0.4559 0.5097 0.5355 -0.0433 -0.0351 0.0362  136 LYS B NZ  
4719  N N   . ALA B 137 ? 0.2597 0.3288 0.3007 -0.0041 -0.0126 0.0123  137 ALA B N   
4720  C CA  . ALA B 137 ? 0.2113 0.2784 0.2417 -0.0003 -0.0078 0.0112  137 ALA B CA  
4721  C C   . ALA B 137 ? 0.2756 0.3295 0.2945 -0.0024 -0.0107 0.0073  137 ALA B C   
4722  O O   . ALA B 137 ? 0.2661 0.3143 0.2787 -0.0035 -0.0090 0.0089  137 ALA B O   
4723  C CB  . ALA B 137 ? 0.2609 0.3364 0.2891 0.0087  -0.0039 0.0071  137 ALA B CB  
4724  N N   . HIS B 138 ? 0.2332 0.2820 0.2503 -0.0032 -0.0150 0.0032  138 HIS B N   
4725  C CA  . HIS B 138 ? 0.2340 0.2727 0.2413 -0.0044 -0.0161 0.0004  138 HIS B CA  
4726  C C   . HIS B 138 ? 0.2575 0.2864 0.2596 -0.0102 -0.0183 0.0021  138 HIS B C   
4727  O O   . HIS B 138 ? 0.2592 0.2805 0.2529 -0.0099 -0.0167 0.0009  138 HIS B O   
4728  C CB  . HIS B 138 ? 0.2255 0.2621 0.2326 -0.0038 -0.0191 -0.0029 138 HIS B CB  
4729  C CG  . HIS B 138 ? 0.2248 0.2560 0.2247 -0.0029 -0.0177 -0.0051 138 HIS B CG  
4730  N ND1 . HIS B 138 ? 0.2549 0.2871 0.2514 0.0005  -0.0144 -0.0060 138 HIS B ND1 
4731  C CD2 . HIS B 138 ? 0.2359 0.2622 0.2326 -0.0045 -0.0187 -0.0056 138 HIS B CD2 
4732  C CE1 . HIS B 138 ? 0.2435 0.2725 0.2371 0.0011  -0.0138 -0.0075 138 HIS B CE1 
4733  N NE2 . HIS B 138 ? 0.2464 0.2722 0.2402 -0.0020 -0.0157 -0.0071 138 HIS B NE2 
4734  N N   . TYR B 139 ? 0.2384 0.2672 0.2459 -0.0149 -0.0224 0.0047  139 TYR B N   
4735  C CA  . TYR B 139 ? 0.2556 0.2740 0.2582 -0.0205 -0.0260 0.0056  139 TYR B CA  
4736  C C   . TYR B 139 ? 0.2706 0.2853 0.2712 -0.0200 -0.0221 0.0073  139 TYR B C   
4737  O O   . TYR B 139 ? 0.2836 0.2864 0.2744 -0.0206 -0.0225 0.0049  139 TYR B O   
4738  C CB  . TYR B 139 ? 0.2443 0.2665 0.2576 -0.0257 -0.0317 0.0091  139 TYR B CB  
4739  C CG  . TYR B 139 ? 0.2723 0.2833 0.2823 -0.0322 -0.0381 0.0093  139 TYR B CG  
4740  C CD1 . TYR B 139 ? 0.3281 0.3357 0.3424 -0.0352 -0.0372 0.0123  139 TYR B CD1 
4741  C CD2 . TYR B 139 ? 0.2932 0.2959 0.2947 -0.0355 -0.0457 0.0066  139 TYR B CD2 
4742  C CE1 . TYR B 139 ? 0.3590 0.3539 0.3707 -0.0416 -0.0447 0.0114  139 TYR B CE1 
4743  C CE2 . TYR B 139 ? 0.3335 0.3239 0.3293 -0.0411 -0.0530 0.0050  139 TYR B CE2 
4744  C CZ  . TYR B 139 ? 0.3594 0.3455 0.3611 -0.0443 -0.0529 0.0069  139 TYR B CZ  
4745  O OH  . TYR B 139 ? 0.3773 0.3492 0.3741 -0.0502 -0.0619 0.0044  139 TYR B OH  
4746  N N   . GLU B 140 ? 0.2484 0.2731 0.2582 -0.0183 -0.0181 0.0119  140 GLU B N   
4747  C CA  . GLU B 140 ? 0.2255 0.2468 0.2344 -0.0183 -0.0147 0.0156  140 GLU B CA  
4748  C C   . GLU B 140 ? 0.2793 0.2966 0.2776 -0.0124 -0.0110 0.0124  140 GLU B C   
4749  O O   . GLU B 140 ? 0.3076 0.3150 0.3010 -0.0126 -0.0105 0.0132  140 GLU B O   
4750  C CB  . GLU B 140 ? 0.2326 0.2674 0.2533 -0.0177 -0.0105 0.0229  140 GLU B CB  
4751  C CG  . GLU B 140 ? 0.2383 0.2788 0.2737 -0.0239 -0.0141 0.0275  140 GLU B CG  
4752  C CD  . GLU B 140 ? 0.3567 0.3844 0.3953 -0.0326 -0.0205 0.0299  140 GLU B CD  
4753  O OE1 . GLU B 140 ? 0.3624 0.3762 0.3914 -0.0330 -0.0210 0.0281  140 GLU B OE1 
4754  O OE2 . GLU B 140 ? 0.3599 0.3915 0.4118 -0.0387 -0.0257 0.0333  140 GLU B OE2 
4755  N N   . GLU B 141 ? 0.2386 0.2625 0.2344 -0.0072 -0.0093 0.0086  141 GLU B N   
4756  C CA  . GLU B 141 ? 0.2621 0.2833 0.2504 -0.0022 -0.0072 0.0057  141 GLU B CA  
4757  C C   . GLU B 141 ? 0.2700 0.2791 0.2512 -0.0038 -0.0087 0.0023  141 GLU B C   
4758  O O   . GLU B 141 ? 0.2949 0.2977 0.2715 -0.0012 -0.0068 0.0021  141 GLU B O   
4759  C CB  . GLU B 141 ? 0.2387 0.2686 0.2280 0.0024  -0.0070 0.0018  141 GLU B CB  
4760  C CG  . GLU B 141 ? 0.2418 0.2827 0.2344 0.0063  -0.0048 0.0035  141 GLU B CG  
4761  C CD  . GLU B 141 ? 0.3292 0.3724 0.3175 0.0101  -0.0013 0.0075  141 GLU B CD  
4762  O OE1 . GLU B 141 ? 0.3350 0.3708 0.3190 0.0101  -0.0009 0.0091  141 GLU B OE1 
4763  O OE2 . GLU B 141 ? 0.3035 0.3564 0.2921 0.0140  0.0015  0.0093  141 GLU B OE2 
4764  N N   . VAL B 142 ? 0.2683 0.2743 0.2480 -0.0071 -0.0118 -0.0002 142 VAL B N   
4765  C CA  . VAL B 142 ? 0.2621 0.2575 0.2322 -0.0075 -0.0122 -0.0036 142 VAL B CA  
4766  C C   . VAL B 142 ? 0.3011 0.2838 0.2664 -0.0098 -0.0137 -0.0035 142 VAL B C   
4767  O O   . VAL B 142 ? 0.3223 0.2963 0.2803 -0.0066 -0.0115 -0.0061 142 VAL B O   
4768  C CB  . VAL B 142 ? 0.2982 0.2934 0.2659 -0.0104 -0.0155 -0.0051 142 VAL B CB  
4769  C CG1 . VAL B 142 ? 0.3132 0.2975 0.2682 -0.0105 -0.0154 -0.0082 142 VAL B CG1 
4770  C CG2 . VAL B 142 ? 0.2534 0.2585 0.2267 -0.0078 -0.0141 -0.0052 142 VAL B CG2 
4771  N N   . GLN B 143 ? 0.2653 0.2467 0.2363 -0.0151 -0.0176 -0.0005 143 GLN B N   
4772  C CA  . GLN B 143 ? 0.2908 0.2587 0.2596 -0.0181 -0.0203 -0.0002 143 GLN B CA  
4773  C C   . GLN B 143 ? 0.3468 0.3127 0.3169 -0.0139 -0.0159 0.0027  143 GLN B C   
4774  O O   . GLN B 143 ? 0.3263 0.2779 0.2906 -0.0129 -0.0165 0.0006  143 GLN B O   
4775  C CB  . GLN B 143 ? 0.3013 0.2704 0.2805 -0.0253 -0.0257 0.0041  143 GLN B CB  
4776  C CG  . GLN B 143 ? 0.3170 0.2718 0.2981 -0.0295 -0.0293 0.0059  143 GLN B CG  
4777  C CD  . GLN B 143 ? 0.3458 0.2809 0.3130 -0.0305 -0.0349 -0.0020 143 GLN B CD  
4778  O OE1 . GLN B 143 ? 0.3683 0.3016 0.3241 -0.0289 -0.0362 -0.0078 143 GLN B OE1 
4779  N NE2 . GLN B 143 ? 0.3463 0.2658 0.3137 -0.0326 -0.0381 -0.0021 143 GLN B NE2 
4780  N N   . ALA B 144 ? 0.2912 0.2704 0.2681 -0.0109 -0.0117 0.0074  144 ALA B N   
4781  C CA  . ALA B 144 ? 0.3006 0.2783 0.2774 -0.0066 -0.0082 0.0112  144 ALA B CA  
4782  C C   . ALA B 144 ? 0.2981 0.2714 0.2674 -0.0002 -0.0060 0.0062  144 ALA B C   
4783  O O   . ALA B 144 ? 0.2998 0.2638 0.2669 0.0029  -0.0051 0.0072  144 ALA B O   
4784  C CB  . ALA B 144 ? 0.3052 0.2986 0.2877 -0.0038 -0.0046 0.0169  144 ALA B CB  
4785  N N   . PHE B 145 ? 0.2724 0.2520 0.2391 0.0019  -0.0051 0.0015  145 PHE B N   
4786  C CA  . PHE B 145 ? 0.2805 0.2578 0.2429 0.0077  -0.0023 -0.0022 145 PHE B CA  
4787  C C   . PHE B 145 ? 0.3201 0.2815 0.2741 0.0077  -0.0027 -0.0064 145 PHE B C   
4788  O O   . PHE B 145 ? 0.3346 0.2897 0.2860 0.0132  -0.0001 -0.0079 145 PHE B O   
4789  C CB  . PHE B 145 ? 0.2665 0.2545 0.2305 0.0086  -0.0014 -0.0048 145 PHE B CB  
4790  C CG  . PHE B 145 ? 0.3060 0.2982 0.2714 0.0145  0.0019  -0.0064 145 PHE B CG  
4791  C CD1 . PHE B 145 ? 0.3273 0.3168 0.2936 0.0200  0.0038  -0.0053 145 PHE B CD1 
4792  C CD2 . PHE B 145 ? 0.2789 0.2784 0.2468 0.0142  0.0029  -0.0081 145 PHE B CD2 
4793  C CE1 . PHE B 145 ? 0.3258 0.3215 0.2966 0.0253  0.0066  -0.0063 145 PHE B CE1 
4794  C CE2 . PHE B 145 ? 0.3435 0.3492 0.3165 0.0187  0.0059  -0.0084 145 PHE B CE2 
4795  C CZ  . PHE B 145 ? 0.3187 0.3233 0.2936 0.0243  0.0077  -0.0077 145 PHE B CZ  
4796  N N   . ARG B 146 ? 0.3171 0.2715 0.2664 0.0022  -0.0065 -0.0088 146 ARG B N   
4797  C CA  . ARG B 146 ? 0.3180 0.2552 0.2563 0.0023  -0.0083 -0.0142 146 ARG B CA  
4798  C C   . ARG B 146 ? 0.3685 0.2925 0.3084 0.0033  -0.0096 -0.0129 146 ARG B C   
4799  O O   . ARG B 146 ? 0.3694 0.2810 0.3020 0.0085  -0.0081 -0.0174 146 ARG B O   
4800  C CB  . ARG B 146 ? 0.3559 0.2886 0.2898 -0.0047 -0.0145 -0.0162 146 ARG B CB  
4801  C CG  . ARG B 146 ? 0.3923 0.3054 0.3115 -0.0046 -0.0182 -0.0234 146 ARG B CG  
4802  C CD  . ARG B 146 ? 0.4714 0.3761 0.3940 -0.0128 -0.0272 -0.0226 146 ARG B CD  
4803  N NE  . ARG B 146 ? 0.4603 0.3477 0.3672 -0.0140 -0.0334 -0.0306 146 ARG B NE  
4804  C CZ  . ARG B 146 ? 0.4650 0.3504 0.3702 -0.0209 -0.0421 -0.0314 146 ARG B CZ  
4805  N NH1 . ARG B 146 ? 0.4478 0.3484 0.3676 -0.0267 -0.0444 -0.0246 146 ARG B NH1 
4806  N NH2 . ARG B 146 ? 0.4873 0.3558 0.3752 -0.0212 -0.0487 -0.0397 146 ARG B NH2 
4807  N N   . VAL B 147 ? 0.3541 0.2808 0.3041 -0.0013 -0.0121 -0.0060 147 VAL B N   
4808  C CA  . VAL B 147 ? 0.3230 0.2367 0.2764 -0.0013 -0.0136 -0.0025 147 VAL B CA  
4809  C C   . VAL B 147 ? 0.3611 0.2763 0.3150 0.0074  -0.0085 -0.0009 147 VAL B C   
4810  O O   . VAL B 147 ? 0.3604 0.2602 0.3116 0.0113  -0.0089 -0.0027 147 VAL B O   
4811  C CB  . VAL B 147 ? 0.3740 0.2937 0.3397 -0.0084 -0.0160 0.0066  147 VAL B CB  
4812  C CG1 . VAL B 147 ? 0.4127 0.3229 0.3842 -0.0079 -0.0161 0.0136  147 VAL B CG1 
4813  C CG2 . VAL B 147 ? 0.3577 0.2722 0.3252 -0.0173 -0.0230 0.0047  147 VAL B CG2 
4814  N N   . PHE B 148 ? 0.3213 0.2545 0.2790 0.0110  -0.0045 0.0020  148 PHE B N   
4815  C CA  . PHE B 148 ? 0.3267 0.2634 0.2857 0.0193  -0.0010 0.0033  148 PHE B CA  
4816  C C   . PHE B 148 ? 0.3248 0.2529 0.2777 0.0256  0.0015  -0.0041 148 PHE B C   
4817  O O   . PHE B 148 ? 0.3496 0.2691 0.3032 0.0319  0.0027  -0.0038 148 PHE B O   
4818  C CB  . PHE B 148 ? 0.2874 0.2442 0.2505 0.0213  0.0010  0.0053  148 PHE B CB  
4819  C CG  . PHE B 148 ? 0.2881 0.2508 0.2540 0.0296  0.0032  0.0057  148 PHE B CG  
4820  C CD1 . PHE B 148 ? 0.3114 0.2782 0.2776 0.0337  0.0059  0.0004  148 PHE B CD1 
4821  C CD2 . PHE B 148 ? 0.2649 0.2314 0.2340 0.0331  0.0025  0.0126  148 PHE B CD2 
4822  C CE1 . PHE B 148 ? 0.3089 0.2832 0.2811 0.0412  0.0075  0.0013  148 PHE B CE1 
4823  C CE2 . PHE B 148 ? 0.3310 0.3040 0.3039 0.0409  0.0030  0.0131  148 PHE B CE2 
4824  C CZ  . PHE B 148 ? 0.3430 0.3204 0.3188 0.0446  0.0053  0.0073  148 PHE B CZ  
4825  N N   . LEU B 149 ? 0.3245 0.2549 0.2712 0.0246  0.0028  -0.0103 149 LEU B N   
4826  C CA  . LEU B 149 ? 0.3312 0.2569 0.2714 0.0314  0.0072  -0.0167 149 LEU B CA  
4827  C C   . LEU B 149 ? 0.3581 0.2609 0.2890 0.0333  0.0053  -0.0222 149 LEU B C   
4828  O O   . LEU B 149 ? 0.3911 0.2869 0.3197 0.0419  0.0091  -0.0256 149 LEU B O   
4829  C CB  . LEU B 149 ? 0.3770 0.3112 0.3119 0.0292  0.0092  -0.0201 149 LEU B CB  
4830  C CG  . LEU B 149 ? 0.3322 0.2873 0.2777 0.0293  0.0114  -0.0159 149 LEU B CG  
4831  C CD1 . LEU B 149 ? 0.3715 0.3319 0.3124 0.0249  0.0116  -0.0177 149 LEU B CD1 
4832  C CD2 . LEU B 149 ? 0.3122 0.2754 0.2643 0.0376  0.0169  -0.0156 149 LEU B CD2 
4833  N N   . GLN B 150 ? 0.3635 0.2542 0.2903 0.0256  -0.0012 -0.0231 150 GLN B N   
4834  C CA  . GLN B 150 ? 0.3964 0.2627 0.3149 0.0262  -0.0054 -0.0291 150 GLN B CA  
4835  C C   . GLN B 150 ? 0.4021 0.2588 0.3284 0.0306  -0.0057 -0.0250 150 GLN B C   
4836  O O   . GLN B 150 ? 0.4368 0.2744 0.3573 0.0365  -0.0062 -0.0309 150 GLN B O   
4837  C CB  . GLN B 150 ? 0.4335 0.2913 0.3518 0.0152  -0.0142 -0.0285 150 GLN B CB  
4838  C CG  . GLN B 150 ? 0.5287 0.3912 0.4394 0.0100  -0.0169 -0.0321 150 GLN B CG  
4839  C CD  . GLN B 150 ? 0.5082 0.3592 0.4204 0.0002  -0.0270 -0.0323 150 GLN B CD  
4840  O OE1 . GLN B 150 ? 0.5520 0.3934 0.4519 -0.0023 -0.0324 -0.0395 150 GLN B OE1 
4841  N NE2 . GLN B 150 ? 0.4737 0.3261 0.4018 -0.0057 -0.0300 -0.0233 150 GLN B NE2 
4842  N N   . THR B 151 ? 0.3664 0.2348 0.3054 0.0277  -0.0058 -0.0145 151 THR B N   
4843  C CA  . THR B 151 ? 0.4042 0.2649 0.3510 0.0314  -0.0064 -0.0081 151 THR B CA  
4844  C C   . THR B 151 ? 0.3894 0.2548 0.3370 0.0433  -0.0006 -0.0097 151 THR B C   
4845  O O   . THR B 151 ? 0.4423 0.2919 0.3898 0.0502  -0.0007 -0.0117 151 THR B O   
4846  C CB  . THR B 151 ? 0.4101 0.2842 0.3673 0.0258  -0.0074 0.0041  151 THR B CB  
4847  O OG1 . THR B 151 ? 0.4128 0.2846 0.3722 0.0149  -0.0121 0.0062  151 THR B OG1 
4848  C CG2 . THR B 151 ? 0.4129 0.2786 0.3768 0.0297  -0.0081 0.0122  151 THR B CG2 
4849  N N   . LEU B 152 ? 0.3746 0.2611 0.3238 0.0458  0.0041  -0.0099 152 LEU B N   
4850  C CA  . LEU B 152 ? 0.3773 0.2729 0.3311 0.0562  0.0094  -0.0105 152 LEU B CA  
4851  C C   . LEU B 152 ? 0.4255 0.3077 0.3720 0.0645  0.0132  -0.0197 152 LEU B C   
4852  O O   . LEU B 152 ? 0.4473 0.3238 0.3985 0.0740  0.0153  -0.0196 152 LEU B O   
4853  C CB  . LEU B 152 ? 0.3565 0.2760 0.3141 0.0550  0.0125  -0.0098 152 LEU B CB  
4854  C CG  . LEU B 152 ? 0.3778 0.3107 0.3444 0.0643  0.0171  -0.0091 152 LEU B CG  
4855  C CD1 . LEU B 152 ? 0.4301 0.3679 0.4063 0.0680  0.0142  -0.0014 152 LEU B CD1 
4856  C CD2 . LEU B 152 ? 0.3961 0.3493 0.3664 0.0610  0.0193  -0.0094 152 LEU B CD2 
4857  N N   . THR B 153 ? 0.4092 0.2864 0.3434 0.0620  0.0144  -0.0278 153 THR B N   
4858  C CA  . THR B 153 ? 0.4274 0.2928 0.3508 0.0709  0.0192  -0.0375 153 THR B CA  
4859  C C   . THR B 153 ? 0.4635 0.2995 0.3778 0.0719  0.0138  -0.0438 153 THR B C   
4860  O O   . THR B 153 ? 0.5026 0.3257 0.4089 0.0820  0.0175  -0.0521 153 THR B O   
4861  C CB  . THR B 153 ? 0.4462 0.3186 0.3574 0.0683  0.0227  -0.0430 153 THR B CB  
4862  O OG1 . THR B 153 ? 0.5072 0.3696 0.4098 0.0576  0.0148  -0.0446 153 THR B OG1 
4863  C CG2 . THR B 153 ? 0.4290 0.3286 0.3507 0.0666  0.0273  -0.0368 153 THR B CG2 
4864  N N   . GLY B 154 ? 0.4953 0.3205 0.4117 0.0619  0.0050  -0.0400 154 GLY B N   
4865  C CA  . GLY B 154 ? 0.5256 0.3217 0.4353 0.0602  -0.0024 -0.0456 154 GLY B CA  
4866  C C   . GLY B 154 ? 0.6226 0.4053 0.5137 0.0574  -0.0058 -0.0574 154 GLY B C   
4867  O O   . GLY B 154 ? 0.5970 0.3532 0.4806 0.0569  -0.0129 -0.0646 154 GLY B O   
4868  N N   . LYS B 155 ? 0.5176 0.3164 0.4005 0.0559  -0.0017 -0.0596 155 LYS B N   
4869  C CA  . LYS B 155 ? 0.5638 0.3519 0.4260 0.0543  -0.0045 -0.0702 155 LYS B CA  
4870  C C   . LYS B 155 ? 0.5552 0.3526 0.4195 0.0407  -0.0114 -0.0655 155 LYS B C   
4871  O O   . LYS B 155 ? 0.5394 0.3603 0.4147 0.0369  -0.0077 -0.0568 155 LYS B O   
4872  C CB  . LYS B 155 ? 0.6253 0.4247 0.4748 0.0644  0.0066  -0.0757 155 LYS B CB  
4873  C CG  . LYS B 155 ? 0.6230 0.4210 0.4744 0.0794  0.0161  -0.0787 155 LYS B CG  
4874  C CD  . LYS B 155 ? 0.7635 0.5300 0.6021 0.0861  0.0115  -0.0903 155 LYS B CD  
4875  C CE  . LYS B 155 ? 0.7966 0.5501 0.6068 0.0890  0.0111  -0.1035 155 LYS B CE  
4876  N NZ  . LYS B 155 ? 0.8982 0.6216 0.6934 0.0993  0.0087  -0.1171 155 LYS B NZ  
4877  N N   . GLU B 156 ? 0.5300 0.3090 0.3850 0.0337  -0.0220 -0.0714 156 GLU B N   
4878  C CA  . GLU B 156 ? 0.5215 0.3108 0.3805 0.0215  -0.0287 -0.0666 156 GLU B CA  
4879  C C   . GLU B 156 ? 0.5196 0.3268 0.3681 0.0231  -0.0227 -0.0674 156 GLU B C   
4880  O O   . GLU B 156 ? 0.5038 0.3054 0.3325 0.0307  -0.0186 -0.0760 156 GLU B O   
4881  C CB  . GLU B 156 ? 0.5729 0.3391 0.4241 0.0139  -0.0425 -0.0735 156 GLU B CB  
4882  C CG  . GLU B 156 ? 0.5642 0.3407 0.4210 0.0016  -0.0505 -0.0688 156 GLU B CG  
4883  C CD  . GLU B 156 ? 0.6830 0.4364 0.5322 -0.0060 -0.0659 -0.0766 156 GLU B CD  
4884  O OE1 . GLU B 156 ? 0.7704 0.4982 0.6071 -0.0011 -0.0704 -0.0871 156 GLU B OE1 
4885  O OE2 . GLU B 156 ? 0.6944 0.4550 0.5490 -0.0161 -0.0742 -0.0732 156 GLU B OE2 
4886  N N   . ILE B 157 ? 0.4619 0.2903 0.3232 0.0164  -0.0220 -0.0582 157 ILE B N   
4887  C CA  . ILE B 157 ? 0.4473 0.2922 0.3018 0.0164  -0.0177 -0.0572 157 ILE B CA  
4888  C C   . ILE B 157 ? 0.4554 0.2964 0.3055 0.0064  -0.0287 -0.0580 157 ILE B C   
4889  O O   . ILE B 157 ? 0.4962 0.3467 0.3628 -0.0020 -0.0335 -0.0505 157 ILE B O   
4890  C CB  . ILE B 157 ? 0.4355 0.3051 0.3074 0.0162  -0.0106 -0.0474 157 ILE B CB  
4891  C CG1 . ILE B 157 ? 0.4169 0.2916 0.2946 0.0260  -0.0010 -0.0464 157 ILE B CG1 
4892  C CG2 . ILE B 157 ? 0.4692 0.3536 0.3361 0.0145  -0.0081 -0.0456 157 ILE B CG2 
4893  C CD1 . ILE B 157 ? 0.4190 0.3153 0.3149 0.0252  0.0031  -0.0374 157 ILE B CD1 
4894  N N   . THR B 158 ? 0.4558 0.2841 0.2836 0.0081  -0.0327 -0.0668 158 THR B N   
4895  C CA  . THR B 158 ? 0.4707 0.2908 0.2923 -0.0008 -0.0458 -0.0692 158 THR B CA  
4896  C C   . THR B 158 ? 0.4881 0.3272 0.3108 -0.0049 -0.0456 -0.0630 158 THR B C   
4897  O O   . THR B 158 ? 0.4743 0.3288 0.2969 -0.0001 -0.0352 -0.0590 158 THR B O   
4898  C CB  . THR B 158 ? 0.5258 0.3227 0.3199 0.0037  -0.0514 -0.0823 158 THR B CB  
4899  O OG1 . THR B 158 ? 0.5194 0.3231 0.2932 0.0124  -0.0417 -0.0850 158 THR B OG1 
4900  C CG2 . THR B 158 ? 0.4974 0.2731 0.2897 0.0095  -0.0514 -0.0896 158 THR B CG2 
4901  N N   . ASP B 159 ? 0.3619 0.2954 0.3454 -0.0229 -0.0111 -0.0521 159 ASP B N   
4902  C CA  . ASP B 159 ? 0.3800 0.3272 0.3621 -0.0225 -0.0162 -0.0513 159 ASP B CA  
4903  C C   . ASP B 159 ? 0.4271 0.3680 0.3898 -0.0199 -0.0178 -0.0573 159 ASP B C   
4904  O O   . ASP B 159 ? 0.3609 0.3106 0.3189 -0.0158 -0.0174 -0.0553 159 ASP B O   
4905  C CB  . ASP B 159 ? 0.4337 0.3880 0.4272 -0.0303 -0.0250 -0.0511 159 ASP B CB  
4906  C CG  . ASP B 159 ? 0.4503 0.4156 0.4644 -0.0319 -0.0220 -0.0435 159 ASP B CG  
4907  O OD1 . ASP B 159 ? 0.4602 0.4264 0.4772 -0.0271 -0.0137 -0.0386 159 ASP B OD1 
4908  O OD2 . ASP B 159 ? 0.5484 0.5218 0.5762 -0.0380 -0.0278 -0.0422 159 ASP B OD2 
4909  N N   . ALA B 160 ? 0.4362 0.3604 0.3866 -0.0226 -0.0187 -0.0649 160 ALA B N   
4910  C CA  . ALA B 160 ? 0.4406 0.3573 0.3706 -0.0200 -0.0184 -0.0708 160 ALA B CA  
4911  C C   . ALA B 160 ? 0.4396 0.3589 0.3662 -0.0112 -0.0089 -0.0680 160 ALA B C   
4912  O O   . ALA B 160 ? 0.4398 0.3630 0.3557 -0.0083 -0.0084 -0.0685 160 ALA B O   
4913  C CB  . ALA B 160 ? 0.4350 0.3312 0.3512 -0.0243 -0.0195 -0.0800 160 ALA B CB  
4914  N N   . MET B 161 ? 0.3802 0.2981 0.3162 -0.0071 -0.0016 -0.0643 161 MET B N   
4915  C CA  . MET B 161 ? 0.3840 0.3063 0.3187 0.0009  0.0062  -0.0612 161 MET B CA  
4916  C C   . MET B 161 ? 0.4077 0.3479 0.3483 0.0024  0.0048  -0.0549 161 MET B C   
4917  O O   . MET B 161 ? 0.3944 0.3398 0.3292 0.0065  0.0080  -0.0541 161 MET B O   
4918  C CB  . MET B 161 ? 0.4278 0.3464 0.3726 0.0053  0.0130  -0.0571 161 MET B CB  
4919  C CG  . MET B 161 ? 0.3961 0.2957 0.3334 0.0075  0.0183  -0.0631 161 MET B CG  
4920  S SD  . MET B 161 ? 0.4370 0.3269 0.3882 0.0079  0.0217  -0.0587 161 MET B SD  
4921  C CE  . MET B 161 ? 0.4244 0.3269 0.3831 0.0182  0.0287  -0.0502 161 MET B CE  
4922  N N   . LEU B 162 ? 0.3461 0.2948 0.2982 -0.0011 0.0007  -0.0507 162 LEU B N   
4923  C CA  . LEU B 162 ? 0.3299 0.2933 0.2872 0.0003  0.0001  -0.0454 162 LEU B CA  
4924  C C   . LEU B 162 ? 0.3692 0.3354 0.3173 -0.0009 -0.0049 -0.0479 162 LEU B C   
4925  O O   . LEU B 162 ? 0.3712 0.3444 0.3163 0.0020  -0.0032 -0.0455 162 LEU B O   
4926  C CB  . LEU B 162 ? 0.3633 0.3338 0.3349 -0.0027 -0.0016 -0.0406 162 LEU B CB  
4927  C CG  . LEU B 162 ? 0.3602 0.3304 0.3404 -0.0009 0.0039  -0.0355 162 LEU B CG  
4928  C CD1 . LEU B 162 ? 0.3640 0.3387 0.3572 -0.0052 0.0026  -0.0318 162 LEU B CD1 
4929  C CD2 . LEU B 162 ? 0.3737 0.3517 0.3523 0.0042  0.0083  -0.0311 162 LEU B CD2 
4930  N N   . SER B 163 ? 0.3628 0.3231 0.3059 -0.0056 -0.0114 -0.0523 163 SER B N   
4931  C CA  . SER B 163 ? 0.3874 0.3498 0.3201 -0.0064 -0.0168 -0.0537 163 SER B CA  
4932  C C   . SER B 163 ? 0.4059 0.3621 0.3219 -0.0029 -0.0122 -0.0567 163 SER B C   
4933  O O   . SER B 163 ? 0.4150 0.3761 0.3249 -0.0012 -0.0126 -0.0547 163 SER B O   
4934  C CB  . SER B 163 ? 0.4160 0.3742 0.3460 -0.0128 -0.0264 -0.0575 163 SER B CB  
4935  O OG  . SER B 163 ? 0.4731 0.4417 0.4221 -0.0158 -0.0305 -0.0530 163 SER B OG  
4936  N N   . ASP B 164 ? 0.4116 0.3564 0.3202 -0.0017 -0.0072 -0.0613 164 ASP B N   
4937  C CA  . ASP B 164 ? 0.4143 0.3540 0.3085 0.0021  -0.0011 -0.0638 164 ASP B CA  
4938  C C   . ASP B 164 ? 0.4442 0.3953 0.3461 0.0069  0.0051  -0.0580 164 ASP B C   
4939  O O   . ASP B 164 ? 0.4141 0.3680 0.3079 0.0084  0.0073  -0.0572 164 ASP B O   
4940  C CB  . ASP B 164 ? 0.4815 0.4069 0.3692 0.0036  0.0048  -0.0696 164 ASP B CB  
4941  C CG  . ASP B 164 ? 0.6049 0.5293 0.4859 0.0095  0.0146  -0.0700 164 ASP B CG  
4942  O OD1 . ASP B 164 ? 0.6856 0.6037 0.5492 0.0092  0.0158  -0.0739 164 ASP B OD1 
4943  O OD2 . ASP B 164 ? 0.6604 0.5920 0.5538 0.0143  0.0208  -0.0655 164 ASP B OD2 
4944  N N   . ALA B 165 ? 0.3898 0.3478 0.3070 0.0085  0.0071  -0.0535 165 ALA B N   
4945  C CA  . ALA B 165 ? 0.3854 0.3541 0.3090 0.0119  0.0115  -0.0484 165 ALA B CA  
4946  C C   . ALA B 165 ? 0.3208 0.2979 0.2444 0.0102  0.0077  -0.0453 165 ALA B C   
4947  O O   . ALA B 165 ? 0.3901 0.3720 0.3107 0.0117  0.0105  -0.0435 165 ALA B O   
4948  C CB  . ALA B 165 ? 0.3544 0.3278 0.2919 0.0136  0.0137  -0.0439 165 ALA B CB  
4949  N N   . LEU B 166 ? 0.3165 0.2953 0.2446 0.0072  0.0017  -0.0446 166 LEU B N   
4950  C CA  . LEU B 166 ? 0.3496 0.3351 0.2782 0.0067  -0.0013 -0.0415 166 LEU B CA  
4951  C C   . LEU B 166 ? 0.3391 0.3202 0.2534 0.0065  -0.0029 -0.0434 166 LEU B C   
4952  O O   . LEU B 166 ? 0.3482 0.3328 0.2599 0.0074  -0.0020 -0.0407 166 LEU B O   
4953  C CB  . LEU B 166 ? 0.3818 0.3708 0.3204 0.0042  -0.0070 -0.0400 166 LEU B CB  
4954  C CG  . LEU B 166 ? 0.3421 0.3375 0.2841 0.0044  -0.0102 -0.0367 166 LEU B CG  
4955  C CD1 . LEU B 166 ? 0.3259 0.3264 0.2709 0.0069  -0.0049 -0.0334 166 LEU B CD1 
4956  C CD2 . LEU B 166 ? 0.3309 0.3307 0.2854 0.0020  -0.0157 -0.0353 166 LEU B CD2 
4957  N N   . ALA B 167 ? 0.3832 0.3552 0.2865 0.0050  -0.0051 -0.0481 167 ALA B N   
4958  C CA  . ALA B 167 ? 0.3586 0.3254 0.2452 0.0045  -0.0066 -0.0495 167 ALA B CA  
4959  C C   . ALA B 167 ? 0.3942 0.3614 0.2751 0.0073  0.0019  -0.0486 167 ALA B C   
4960  O O   . ALA B 167 ? 0.4367 0.4047 0.3103 0.0074  0.0022  -0.0462 167 ALA B O   
4961  C CB  . ALA B 167 ? 0.3641 0.3196 0.2372 0.0018  -0.0103 -0.0555 167 ALA B CB  
4962  N N   . VAL B 168 ? 0.3605 0.3281 0.2467 0.0097  0.0088  -0.0497 168 VAL B N   
4963  C CA  . VAL B 168 ? 0.3937 0.3646 0.2787 0.0121  0.0167  -0.0482 168 VAL B CA  
4964  C C   . VAL B 168 ? 0.3764 0.3574 0.2701 0.0117  0.0166  -0.0429 168 VAL B C   
4965  O O   . VAL B 168 ? 0.4078 0.3903 0.2965 0.0114  0.0198  -0.0411 168 VAL B O   
4966  C CB  . VAL B 168 ? 0.4835 0.4542 0.3757 0.0154  0.0233  -0.0497 168 VAL B CB  
4967  C CG1 . VAL B 168 ? 0.4945 0.4726 0.3909 0.0178  0.0309  -0.0469 168 VAL B CG1 
4968  C CG2 . VAL B 168 ? 0.4921 0.4492 0.3716 0.0159  0.0253  -0.0561 168 VAL B CG2 
4969  N N   . CYS B 169 ? 0.3181 0.3047 0.2239 0.0114  0.0137  -0.0407 169 CYS B N   
4970  C CA  . CYS B 169 ? 0.3211 0.3151 0.2332 0.0107  0.0137  -0.0367 169 CYS B CA  
4971  C C   . CYS B 169 ? 0.3620 0.3533 0.2670 0.0094  0.0103  -0.0354 169 CYS B C   
4972  O O   . CYS B 169 ? 0.3620 0.3545 0.2645 0.0087  0.0126  -0.0333 169 CYS B O   
4973  C CB  . CYS B 169 ? 0.3212 0.3201 0.2450 0.0108  0.0120  -0.0349 169 CYS B CB  
4974  S SG  . CYS B 169 ? 0.3775 0.3804 0.3095 0.0131  0.0165  -0.0341 169 CYS B SG  
4975  N N   . ASP B 170 ? 0.3156 0.3032 0.2182 0.0089  0.0043  -0.0363 170 ASP B N   
4976  C CA  . ASP B 170 ? 0.3420 0.3276 0.2392 0.0085  0.0005  -0.0338 170 ASP B CA  
4977  C C   . ASP B 170 ? 0.3700 0.3496 0.2520 0.0082  0.0029  -0.0338 170 ASP B C   
4978  O O   . ASP B 170 ? 0.3864 0.3644 0.2642 0.0081  0.0030  -0.0305 170 ASP B O   
4979  C CB  . ASP B 170 ? 0.3630 0.3476 0.2620 0.0080  -0.0074 -0.0341 170 ASP B CB  
4980  C CG  . ASP B 170 ? 0.3614 0.3529 0.2766 0.0084  -0.0092 -0.0322 170 ASP B CG  
4981  O OD1 . ASP B 170 ? 0.3344 0.3296 0.2558 0.0095  -0.0047 -0.0304 170 ASP B OD1 
4982  O OD2 . ASP B 170 ? 0.4162 0.4093 0.3375 0.0072  -0.0150 -0.0327 170 ASP B OD2 
4983  N N   . GLU B 171 ? 0.3627 0.3378 0.2356 0.0080  0.0056  -0.0373 171 GLU B N   
4984  C CA  . GLU B 171 ? 0.4116 0.3809 0.2691 0.0077  0.0096  -0.0370 171 GLU B CA  
4985  C C   . GLU B 171 ? 0.4225 0.3968 0.2851 0.0074  0.0168  -0.0343 171 GLU B C   
4986  O O   . GLU B 171 ? 0.4133 0.3847 0.2683 0.0063  0.0187  -0.0312 171 GLU B O   
4987  C CB  . GLU B 171 ? 0.4277 0.3907 0.2748 0.0080  0.0129  -0.0421 171 GLU B CB  
4988  C CG  . GLU B 171 ? 0.4535 0.4124 0.2872 0.0081  0.0210  -0.0417 171 GLU B CG  
4989  C CD  . GLU B 171 ? 0.6279 0.5761 0.4431 0.0083  0.0232  -0.0468 171 GLU B CD  
4990  O OE1 . GLU B 171 ? 0.6776 0.6238 0.4965 0.0096  0.0249  -0.0516 171 GLU B OE1 
4991  O OE2 . GLU B 171 ? 0.7348 0.6757 0.5311 0.0072  0.0242  -0.0459 171 GLU B OE2 
4992  N N   . ASN B 172 ? 0.3948 0.3766 0.2705 0.0080  0.0204  -0.0348 172 ASN B N   
4993  C CA  . ASN B 172 ? 0.3783 0.3665 0.2608 0.0067  0.0254  -0.0321 172 ASN B CA  
4994  C C   . ASN B 172 ? 0.3751 0.3625 0.2586 0.0049  0.0225  -0.0290 172 ASN B C   
4995  O O   . ASN B 172 ? 0.3834 0.3698 0.2636 0.0026  0.0260  -0.0266 172 ASN B O   
4996  C CB  . ASN B 172 ? 0.3727 0.3698 0.2694 0.0077  0.0272  -0.0325 172 ASN B CB  
4997  C CG  . ASN B 172 ? 0.3397 0.3450 0.2435 0.0057  0.0321  -0.0300 172 ASN B CG  
4998  O OD1 . ASN B 172 ? 0.3735 0.3841 0.2848 0.0035  0.0302  -0.0283 172 ASN B OD1 
4999  N ND2 . ASN B 172 ? 0.3897 0.3961 0.2911 0.0061  0.0385  -0.0300 172 ASN B ND2 
5000  N N   . ARG B 173 ? 0.3379 0.3253 0.2266 0.0058  0.0169  -0.0289 173 ARG B N   
5001  C CA  . ARG B 173 ? 0.3655 0.3509 0.2556 0.0051  0.0152  -0.0262 173 ARG B CA  
5002  C C   . ARG B 173 ? 0.3901 0.3672 0.2686 0.0052  0.0140  -0.0235 173 ARG B C   
5003  O O   . ARG B 173 ? 0.3656 0.3388 0.2423 0.0039  0.0159  -0.0209 173 ARG B O   
5004  C CB  . ARG B 173 ? 0.3534 0.3411 0.2522 0.0069  0.0109  -0.0265 173 ARG B CB  
5005  C CG  . ARG B 173 ? 0.3557 0.3505 0.2643 0.0066  0.0127  -0.0280 173 ARG B CG  
5006  C CD  . ARG B 173 ? 0.3583 0.3555 0.2752 0.0083  0.0093  -0.0282 173 ARG B CD  
5007  N NE  . ARG B 173 ? 0.3441 0.3469 0.2685 0.0080  0.0112  -0.0287 173 ARG B NE  
5008  C CZ  . ARG B 173 ? 0.3525 0.3574 0.2833 0.0089  0.0096  -0.0292 173 ARG B CZ  
5009  N NH1 . ARG B 173 ? 0.3405 0.3434 0.2727 0.0095  0.0057  -0.0298 173 ARG B NH1 
5010  N NH2 . ARG B 173 ? 0.3293 0.3385 0.2654 0.0088  0.0116  -0.0285 173 ARG B NH2 
5011  N N   . ARG B 174 ? 0.3939 0.3671 0.2637 0.0064  0.0104  -0.0240 174 ARG B N   
5012  C CA  . ARG B 174 ? 0.3818 0.3471 0.2390 0.0067  0.0080  -0.0205 174 ARG B CA  
5013  C C   . ARG B 174 ? 0.3887 0.3499 0.2355 0.0044  0.0150  -0.0191 174 ARG B C   
5014  O O   . ARG B 174 ? 0.4188 0.3737 0.2593 0.0037  0.0160  -0.0147 174 ARG B O   
5015  C CB  . ARG B 174 ? 0.4331 0.3958 0.2824 0.0078  0.0011  -0.0216 174 ARG B CB  
5016  C CG  . ARG B 174 ? 0.4516 0.4192 0.3134 0.0095  -0.0062 -0.0216 174 ARG B CG  
5017  C CD  . ARG B 174 ? 0.5716 0.5368 0.4261 0.0096  -0.0152 -0.0213 174 ARG B CD  
5018  N NE  . ARG B 174 ? 0.5963 0.5685 0.4667 0.0108  -0.0216 -0.0206 174 ARG B NE  
5019  C CZ  . ARG B 174 ? 0.5623 0.5389 0.4404 0.0094  -0.0249 -0.0243 174 ARG B CZ  
5020  N NH1 . ARG B 174 ? 0.4951 0.4684 0.3655 0.0071  -0.0231 -0.0296 174 ARG B NH1 
5021  N NH2 . ARG B 174 ? 0.5926 0.5765 0.4869 0.0103  -0.0298 -0.0224 174 ARG B NH2 
5022  N N   . LEU B 175 ? 0.3944 0.3590 0.2402 0.0035  0.0204  -0.0222 175 LEU B N   
5023  C CA  . LEU B 175 ? 0.4061 0.3688 0.2446 0.0012  0.0285  -0.0206 175 LEU B CA  
5024  C C   . LEU B 175 ? 0.4037 0.3695 0.2517 -0.0019 0.0322  -0.0180 175 LEU B C   
5025  O O   . LEU B 175 ? 0.3973 0.3575 0.2379 -0.0044 0.0361  -0.0143 175 LEU B O   
5026  C CB  . LEU B 175 ? 0.4229 0.3899 0.2620 0.0018  0.0345  -0.0244 175 LEU B CB  
5027  C CG  . LEU B 175 ? 0.4316 0.3913 0.2558 0.0038  0.0321  -0.0275 175 LEU B CG  
5028  C CD1 . LEU B 175 ? 0.4434 0.4068 0.2715 0.0055  0.0383  -0.0324 175 LEU B CD1 
5029  C CD2 . LEU B 175 ? 0.4589 0.4080 0.2610 0.0028  0.0336  -0.0249 175 LEU B CD2 
5030  N N   . LEU B 176 ? 0.4049 0.3786 0.2678 -0.0023 0.0310  -0.0198 176 LEU B N   
5031  C CA  . LEU B 176 ? 0.3542 0.3295 0.2242 -0.0063 0.0333  -0.0182 176 LEU B CA  
5032  C C   . LEU B 176 ? 0.3959 0.3606 0.2602 -0.0065 0.0310  -0.0151 176 LEU B C   
5033  O O   . LEU B 176 ? 0.4006 0.3605 0.2627 -0.0105 0.0347  -0.0127 176 LEU B O   
5034  C CB  . LEU B 176 ? 0.3646 0.3490 0.2482 -0.0066 0.0314  -0.0208 176 LEU B CB  
5035  C CG  . LEU B 176 ? 0.3440 0.3399 0.2364 -0.0071 0.0349  -0.0222 176 LEU B CG  
5036  C CD1 . LEU B 176 ? 0.3487 0.3525 0.2523 -0.0065 0.0314  -0.0239 176 LEU B CD1 
5037  C CD2 . LEU B 176 ? 0.3681 0.3683 0.2632 -0.0120 0.0408  -0.0200 176 LEU B CD2 
5038  N N   . ARG B 177 ? 0.3899 0.3505 0.2523 -0.0023 0.0251  -0.0148 177 ARG B N   
5039  C CA  . ARG B 177 ? 0.4193 0.3695 0.2771 -0.0010 0.0230  -0.0109 177 ARG B CA  
5040  C C   . ARG B 177 ? 0.4162 0.3574 0.2597 -0.0020 0.0251  -0.0062 177 ARG B C   
5041  O O   . ARG B 177 ? 0.4594 0.3911 0.2991 -0.0034 0.0272  -0.0022 177 ARG B O   
5042  C CB  . ARG B 177 ? 0.4394 0.3901 0.3007 0.0042  0.0160  -0.0106 177 ARG B CB  
5043  C CG  . ARG B 177 ? 0.4608 0.4150 0.3352 0.0059  0.0149  -0.0127 177 ARG B CG  
5044  C CD  . ARG B 177 ? 0.4409 0.3875 0.3166 0.0041  0.0192  -0.0121 177 ARG B CD  
5045  N NE  . ARG B 177 ? 0.4551 0.3917 0.3289 0.0082  0.0176  -0.0077 177 ARG B NE  
5046  C CZ  . ARG B 177 ? 0.4778 0.4155 0.3595 0.0136  0.0144  -0.0067 177 ARG B CZ  
5047  N NH1 . ARG B 177 ? 0.4288 0.3768 0.3202 0.0151  0.0123  -0.0098 177 ARG B NH1 
5048  N NH2 . ARG B 177 ? 0.5337 0.4621 0.4149 0.0177  0.0138  -0.0019 177 ARG B NH2 
5049  N N   . GLU B 178 ? 0.4120 0.3542 0.2457 -0.0013 0.0251  -0.0064 178 GLU B N   
5050  C CA  . GLU B 178 ? 0.4188 0.3521 0.2363 -0.0025 0.0280  -0.0018 178 GLU B CA  
5051  C C   . GLU B 178 ? 0.4144 0.3470 0.2327 -0.0079 0.0371  -0.0003 178 GLU B C   
5052  O O   . GLU B 178 ? 0.4570 0.3796 0.2657 -0.0099 0.0402  0.0052  178 GLU B O   
5053  C CB  . GLU B 178 ? 0.4798 0.4141 0.2851 -0.0013 0.0276  -0.0039 178 GLU B CB  
5054  C CG  . GLU B 178 ? 0.5627 0.4941 0.3606 0.0025  0.0177  -0.0036 178 GLU B CG  
5055  C CD  . GLU B 178 ? 0.6437 0.5732 0.4259 0.0025  0.0176  -0.0068 178 GLU B CD  
5056  O OE1 . GLU B 178 ? 0.6769 0.6021 0.4462 0.0005  0.0253  -0.0060 178 GLU B OE1 
5057  O OE2 . GLU B 178 ? 0.7465 0.6781 0.5287 0.0042  0.0100  -0.0101 178 GLU B OE2 
5058  N N   . LEU B 179 ? 0.4387 0.3824 0.2688 -0.0105 0.0413  -0.0045 179 LEU B N   
5059  C CA  . LEU B 179 ? 0.4300 0.3765 0.2652 -0.0165 0.0490  -0.0032 179 LEU B CA  
5060  C C   . LEU B 179 ? 0.4293 0.3685 0.2684 -0.0200 0.0484  -0.0010 179 LEU B C   
5061  O O   . LEU B 179 ? 0.4606 0.3933 0.2960 -0.0249 0.0537  0.0028  179 LEU B O   
5062  C CB  . LEU B 179 ? 0.4221 0.3837 0.2725 -0.0179 0.0513  -0.0075 179 LEU B CB  
5063  C CG  . LEU B 179 ? 0.4560 0.4244 0.3138 -0.0241 0.0591  -0.0058 179 LEU B CG  
5064  C CD1 . LEU B 179 ? 0.5011 0.4701 0.3505 -0.0235 0.0671  -0.0040 179 LEU B CD1 
5065  C CD2 . LEU B 179 ? 0.4647 0.4484 0.3407 -0.0254 0.0579  -0.0092 179 LEU B CD2 
5066  N N   . TYR B 180 ? 0.3897 0.3289 0.2360 -0.0177 0.0427  -0.0037 180 TYR B N   
5067  C CA  . TYR B 180 ? 0.3861 0.3160 0.2350 -0.0203 0.0426  -0.0029 180 TYR B CA  
5068  C C   . TYR B 180 ? 0.4819 0.3955 0.3191 -0.0187 0.0429  0.0031  180 TYR B C   
5069  O O   . TYR B 180 ? 0.4550 0.3581 0.2914 -0.0228 0.0460  0.0051  180 TYR B O   
5070  C CB  . TYR B 180 ? 0.3977 0.3296 0.2542 -0.0167 0.0375  -0.0068 180 TYR B CB  
5071  C CG  . TYR B 180 ? 0.4214 0.3630 0.2885 -0.0212 0.0381  -0.0117 180 TYR B CG  
5072  C CD1 . TYR B 180 ? 0.3987 0.3542 0.2719 -0.0241 0.0400  -0.0131 180 TYR B CD1 
5073  C CD2 . TYR B 180 ? 0.3888 0.3256 0.2591 -0.0224 0.0370  -0.0146 180 TYR B CD2 
5074  C CE1 . TYR B 180 ? 0.4139 0.3793 0.2971 -0.0281 0.0392  -0.0165 180 TYR B CE1 
5075  C CE2 . TYR B 180 ? 0.3861 0.3315 0.2635 -0.0269 0.0365  -0.0188 180 TYR B CE2 
5076  C CZ  . TYR B 180 ? 0.4038 0.3639 0.2879 -0.0299 0.0369  -0.0193 180 TYR B CZ  
5077  O OH  . TYR B 180 ? 0.4501 0.4190 0.3412 -0.0345 0.0352  -0.0225 180 TYR B OH  
5078  N N   . GLU B 181 ? 0.4739 0.3847 0.3020 -0.0127 0.0389  0.0062  181 GLU B N   
5079  C CA  . GLU B 181 ? 0.4940 0.3899 0.3106 -0.0101 0.0378  0.0133  181 GLU B CA  
5080  C C   . GLU B 181 ? 0.5478 0.4346 0.3557 -0.0161 0.0452  0.0182  181 GLU B C   
5081  O O   . GLU B 181 ? 0.5284 0.4003 0.3307 -0.0160 0.0462  0.0238  181 GLU B O   
5082  C CB  . GLU B 181 ? 0.5491 0.4463 0.3555 -0.0045 0.0318  0.0158  181 GLU B CB  
5083  C CG  . GLU B 181 ? 0.6008 0.4990 0.4130 0.0024  0.0231  0.0161  181 GLU B CG  
5084  C CD  . GLU B 181 ? 0.6016 0.4871 0.4150 0.0057  0.0221  0.0217  181 GLU B CD  
5085  O OE1 . GLU B 181 ? 0.7893 0.6630 0.5902 0.0064  0.0224  0.0293  181 GLU B OE1 
5086  O OE2 . GLU B 181 ? 0.7469 0.6334 0.5729 0.0081  0.0213  0.0190  181 GLU B OE2 
5087  N N   . TYR B 182 ? 0.5054 0.4006 0.3131 -0.0211 0.0511  0.0167  182 TYR B N   
5088  C CA  . TYR B 182 ? 0.5304 0.4187 0.3316 -0.0276 0.0594  0.0216  182 TYR B CA  
5089  C C   . TYR B 182 ? 0.5085 0.3910 0.3191 -0.0345 0.0628  0.0212  182 TYR B C   
5090  O O   . TYR B 182 ? 0.5187 0.3894 0.3230 -0.0394 0.0683  0.0267  182 TYR B O   
5091  C CB  . TYR B 182 ? 0.4878 0.3890 0.2901 -0.0308 0.0657  0.0197  182 TYR B CB  
5092  C CG  . TYR B 182 ? 0.5174 0.4176 0.3033 -0.0263 0.0660  0.0217  182 TYR B CG  
5093  C CD1 . TYR B 182 ? 0.5523 0.4416 0.3209 -0.0281 0.0718  0.0288  182 TYR B CD1 
5094  C CD2 . TYR B 182 ? 0.4893 0.3977 0.2752 -0.0208 0.0605  0.0165  182 TYR B CD2 
5095  C CE1 . TYR B 182 ? 0.5811 0.4682 0.3316 -0.0247 0.0723  0.0301  182 TYR B CE1 
5096  C CE2 . TYR B 182 ? 0.5295 0.4351 0.2978 -0.0177 0.0607  0.0175  182 TYR B CE2 
5097  C CZ  . TYR B 182 ? 0.5717 0.4667 0.3218 -0.0196 0.0664  0.0240  182 TYR B CZ  
5098  O OH  . TYR B 182 ? 0.6112 0.5015 0.3399 -0.0169 0.0666  0.0247  182 TYR B OH  
5099  N N   . ARG B 183 ? 0.4787 0.3678 0.3026 -0.0355 0.0596  0.0147  183 ARG B N   
5100  C CA  . ARG B 183 ? 0.4959 0.3778 0.3265 -0.0426 0.0618  0.0130  183 ARG B CA  
5101  C C   . ARG B 183 ? 0.5235 0.3839 0.3468 -0.0401 0.0611  0.0167  183 ARG B C   
5102  O O   . ARG B 183 ? 0.5305 0.3797 0.3555 -0.0469 0.0645  0.0162  183 ARG B O   
5103  C CB  . ARG B 183 ? 0.4923 0.3869 0.3359 -0.0437 0.0579  0.0049  183 ARG B CB  
5104  C CG  . ARG B 183 ? 0.4597 0.3757 0.3117 -0.0443 0.0581  0.0022  183 ARG B CG  
5105  C CD  . ARG B 183 ? 0.4799 0.4067 0.3424 -0.0436 0.0530  -0.0045 183 ARG B CD  
5106  N NE  . ARG B 183 ? 0.4793 0.4076 0.3493 -0.0528 0.0536  -0.0074 183 ARG B NE  
5107  C CZ  . ARG B 183 ? 0.4826 0.4169 0.3589 -0.0541 0.0493  -0.0129 183 ARG B CZ  
5108  N NH1 . ARG B 183 ? 0.4932 0.4329 0.3706 -0.0466 0.0450  -0.0156 183 ARG B NH1 
5109  N NH2 . ARG B 183 ? 0.4472 0.3825 0.3284 -0.0637 0.0492  -0.0154 183 ARG B NH2 
5110  N N   . LYS B 184 ? 0.5330 0.3869 0.3487 -0.0307 0.0568  0.0207  184 LYS B N   
5111  C CA  . LYS B 184 ? 0.5420 0.3757 0.3523 -0.0269 0.0565  0.0256  184 LYS B CA  
5112  C C   . LYS B 184 ? 0.6034 0.4214 0.4023 -0.0309 0.0621  0.0341  184 LYS B C   
5113  O O   . LYS B 184 ? 0.6001 0.3987 0.3959 -0.0300 0.0637  0.0380  184 LYS B O   
5114  C CB  . LYS B 184 ? 0.5887 0.4220 0.3964 -0.0155 0.0494  0.0288  184 LYS B CB  
5115  C CG  . LYS B 184 ? 0.5122 0.3596 0.3313 -0.0111 0.0443  0.0216  184 LYS B CG  
5116  C CD  . LYS B 184 ? 0.6194 0.4718 0.4374 -0.0017 0.0368  0.0248  184 LYS B CD  
5117  C CE  . LYS B 184 ? 0.6089 0.4604 0.4377 0.0050  0.0338  0.0226  184 LYS B CE  
5118  N NZ  . LYS B 184 ? 0.5927 0.4578 0.4265 0.0115  0.0261  0.0223  184 LYS B NZ  
5119  N N   . ALA B 185 ? 0.5353 0.3602 0.3279 -0.0351 0.0659  0.0373  185 ALA B N   
5120  C CA  . ALA B 185 ? 0.5772 0.3871 0.3572 -0.0387 0.0720  0.0465  185 ALA B CA  
5121  C C   . ALA B 185 ? 0.6012 0.3996 0.3868 -0.0491 0.0787  0.0461  185 ALA B C   
5122  O O   . ALA B 185 ? 0.5445 0.3504 0.3429 -0.0552 0.0790  0.0381  185 ALA B O   
5123  C CB  . ALA B 185 ? 0.5891 0.4099 0.3608 -0.0410 0.0761  0.0492  185 ALA B CB  
5124  N N   . ALA B 186 ? 0.6144 0.3933 0.3892 -0.0514 0.0837  0.0551  186 ALA B N   
5125  C CA  . ALA B 186 ? 0.6277 0.3932 0.4066 -0.0625 0.0906  0.0554  186 ALA B CA  
5126  C C   . ALA B 186 ? 0.6325 0.4151 0.4215 -0.0742 0.0961  0.0515  186 ALA B C   
5127  O O   . ALA B 186 ? 0.6376 0.4199 0.4377 -0.0839 0.0977  0.0460  186 ALA B O   
5128  C CB  . ALA B 186 ? 0.6314 0.3733 0.3961 -0.0630 0.0957  0.0673  186 ALA B CB  
5129  N N   . ASP B 187 ? 0.6138 0.4121 0.3997 -0.0734 0.0987  0.0539  187 ASP B N   
5130  C CA  . ASP B 187 ? 0.5851 0.4022 0.3829 -0.0829 0.1046  0.0512  187 ASP B CA  
5131  C C   . ASP B 187 ? 0.5943 0.4345 0.3970 -0.0763 0.1006  0.0454  187 ASP B C   
5132  O O   . ASP B 187 ? 0.5990 0.4451 0.3920 -0.0720 0.1036  0.0490  187 ASP B O   
5133  C CB  . ASP B 187 ? 0.6561 0.4678 0.4455 -0.0890 0.1152  0.0605  187 ASP B CB  
5134  C CG  . ASP B 187 ? 0.7042 0.4977 0.4959 -0.0998 0.1205  0.0645  187 ASP B CG  
5135  O OD1 . ASP B 187 ? 0.8105 0.5801 0.5898 -0.0961 0.1193  0.0698  187 ASP B OD1 
5136  O OD2 . ASP B 187 ? 0.8281 0.6309 0.6349 -0.1118 0.1251  0.0620  187 ASP B OD2 
5137  N N   . PRO B 188 ? 0.5763 0.4288 0.3927 -0.0757 0.0943  0.0365  188 PRO B N   
5138  C CA  . PRO B 188 ? 0.4936 0.3641 0.3133 -0.0677 0.0891  0.0314  188 PRO B CA  
5139  C C   . PRO B 188 ? 0.5593 0.4481 0.3838 -0.0699 0.0956  0.0319  188 PRO B C   
5140  O O   . PRO B 188 ? 0.5572 0.4556 0.3945 -0.0790 0.1013  0.0319  188 PRO B O   
5141  C CB  . PRO B 188 ? 0.5513 0.4293 0.3853 -0.0693 0.0827  0.0228  188 PRO B CB  
5142  C CG  . PRO B 188 ? 0.5238 0.3828 0.3564 -0.0744 0.0826  0.0230  188 PRO B CG  
5143  C CD  . PRO B 188 ? 0.5301 0.3773 0.3567 -0.0819 0.0911  0.0309  188 PRO B CD  
5144  N N   . LYS B 189 ? 0.5196 0.4131 0.3341 -0.0615 0.0949  0.0322  189 LYS B N   
5145  C CA  . LYS B 189 ? 0.5234 0.4332 0.3415 -0.0616 0.1017  0.0316  189 LYS B CA  
5146  C C   . LYS B 189 ? 0.5003 0.4309 0.3377 -0.0608 0.0982  0.0240  189 LYS B C   
5147  O O   . LYS B 189 ? 0.5526 0.4980 0.3965 -0.0600 0.1039  0.0230  189 LYS B O   
5148  C CB  . LYS B 189 ? 0.5724 0.4768 0.3698 -0.0533 0.1022  0.0338  189 LYS B CB  
5149  C CG  . LYS B 189 ? 0.5591 0.4457 0.3371 -0.0553 0.1079  0.0429  189 LYS B CG  
5150  C CD  . LYS B 189 ? 0.6918 0.5757 0.4483 -0.0498 0.1113  0.0453  189 LYS B CD  
5151  C CE  . LYS B 189 ? 0.6924 0.5566 0.4256 -0.0503 0.1146  0.0550  189 LYS B CE  
5152  N NZ  . LYS B 189 ? 0.7908 0.6516 0.5299 -0.0599 0.1257  0.0610  189 LYS B NZ  
5153  N N   . VAL B 190 ? 0.4918 0.4229 0.3379 -0.0606 0.0896  0.0192  190 VAL B N   
5154  C CA  . VAL B 190 ? 0.4780 0.4269 0.3410 -0.0599 0.0848  0.0127  190 VAL B CA  
5155  C C   . VAL B 190 ? 0.4696 0.4169 0.3432 -0.0679 0.0811  0.0104  190 VAL B C   
5156  O O   . VAL B 190 ? 0.4730 0.4042 0.3386 -0.0674 0.0770  0.0099  190 VAL B O   
5157  C CB  . VAL B 190 ? 0.4519 0.4008 0.3099 -0.0501 0.0768  0.0084  190 VAL B CB  
5158  C CG1 . VAL B 190 ? 0.4770 0.4429 0.3515 -0.0495 0.0723  0.0027  190 VAL B CG1 
5159  C CG2 . VAL B 190 ? 0.5059 0.4528 0.3495 -0.0429 0.0795  0.0101  190 VAL B CG2 
5160  N N   . THR B 191 ? 0.4656 0.4291 0.3567 -0.0754 0.0826  0.0091  191 THR B N   
5161  C CA  . THR B 191 ? 0.3854 0.3477 0.2850 -0.0841 0.0777  0.0059  191 THR B CA  
5162  C C   . THR B 191 ? 0.4263 0.3950 0.3299 -0.0795 0.0685  -0.0005 191 THR B C   
5163  O O   . THR B 191 ? 0.4538 0.4316 0.3581 -0.0708 0.0664  -0.0021 191 THR B O   
5164  C CB  . THR B 191 ? 0.4570 0.4355 0.3749 -0.0950 0.0813  0.0075  191 THR B CB  
5165  O OG1 . THR B 191 ? 0.4273 0.4300 0.3606 -0.0916 0.0802  0.0061  191 THR B OG1 
5166  C CG2 . THR B 191 ? 0.4497 0.4236 0.3658 -0.1007 0.0920  0.0144  191 THR B CG2 
5167  N N   . GLY B 192 ? 0.4257 0.3891 0.3314 -0.0864 0.0636  -0.0044 192 GLY B N   
5168  C CA  . GLY B 192 ? 0.4428 0.4116 0.3509 -0.0833 0.0557  -0.0102 192 GLY B CA  
5169  C C   . GLY B 192 ? 0.4034 0.3972 0.3272 -0.0828 0.0532  -0.0106 192 GLY B C   
5170  O O   . GLY B 192 ? 0.4132 0.4136 0.3377 -0.0756 0.0488  -0.0131 192 GLY B O   
5171  N N   . VAL B 193 ? 0.3957 0.4038 0.3337 -0.0908 0.0562  -0.0077 193 VAL B N   
5172  C CA  . VAL B 193 ? 0.3773 0.4106 0.3332 -0.0896 0.0545  -0.0069 193 VAL B CA  
5173  C C   . VAL B 193 ? 0.3973 0.4363 0.3523 -0.0778 0.0591  -0.0050 193 VAL B C   
5174  O O   . VAL B 193 ? 0.3806 0.4305 0.3412 -0.0711 0.0552  -0.0066 193 VAL B O   
5175  C CB  . VAL B 193 ? 0.4467 0.4951 0.4205 -0.1006 0.0576  -0.0032 193 VAL B CB  
5176  C CG1 . VAL B 193 ? 0.4038 0.4785 0.3976 -0.0964 0.0587  -0.0003 193 VAL B CG1 
5177  C CG2 . VAL B 193 ? 0.4150 0.4623 0.3923 -0.1133 0.0497  -0.0064 193 VAL B CG2 
5178  N N   . GLU B 194 ? 0.4009 0.4309 0.3470 -0.0752 0.0674  -0.0017 194 GLU B N   
5179  C CA  . GLU B 194 ? 0.3919 0.4246 0.3337 -0.0647 0.0718  -0.0010 194 GLU B CA  
5180  C C   . GLU B 194 ? 0.4271 0.4509 0.3574 -0.0557 0.0654  -0.0050 194 GLU B C   
5181  O O   . GLU B 194 ? 0.4075 0.4396 0.3411 -0.0482 0.0648  -0.0064 194 GLU B O   
5182  C CB  . GLU B 194 ? 0.3658 0.3875 0.2955 -0.0644 0.0812  0.0031  194 GLU B CB  
5183  C CG  . GLU B 194 ? 0.4129 0.4464 0.3560 -0.0717 0.0901  0.0078  194 GLU B CG  
5184  C CD  . GLU B 194 ? 0.4946 0.5141 0.4233 -0.0735 0.0997  0.0126  194 GLU B CD  
5185  O OE1 . GLU B 194 ? 0.4741 0.4731 0.3840 -0.0724 0.0975  0.0130  194 GLU B OE1 
5186  O OE2 . GLU B 194 ? 0.4825 0.5122 0.4203 -0.0768 0.1095  0.0167  194 GLU B OE2 
5187  N N   . ALA B 195 ? 0.4276 0.4342 0.3451 -0.0562 0.0612  -0.0065 195 ALA B N   
5188  C CA  . ALA B 195 ? 0.4201 0.4199 0.3295 -0.0485 0.0552  -0.0099 195 ALA B CA  
5189  C C   . ALA B 195 ? 0.4186 0.4315 0.3390 -0.0473 0.0492  -0.0132 195 ALA B C   
5190  O O   . ALA B 195 ? 0.3808 0.3960 0.3002 -0.0397 0.0466  -0.0149 195 ALA B O   
5191  C CB  . ALA B 195 ? 0.4190 0.4003 0.3170 -0.0498 0.0525  -0.0107 195 ALA B CB  
5192  N N   . LEU B 196 ? 0.3744 0.3954 0.3047 -0.0553 0.0466  -0.0137 196 LEU B N   
5193  C CA  . LEU B 196 ? 0.3790 0.4122 0.3183 -0.0552 0.0401  -0.0160 196 LEU B CA  
5194  C C   . LEU B 196 ? 0.3837 0.4353 0.3366 -0.0503 0.0416  -0.0138 196 LEU B C   
5195  O O   . LEU B 196 ? 0.3452 0.4031 0.3016 -0.0454 0.0372  -0.0149 196 LEU B O   
5196  C CB  . LEU B 196 ? 0.4070 0.4434 0.3515 -0.0661 0.0361  -0.0170 196 LEU B CB  
5197  C CG  . LEU B 196 ? 0.4212 0.4680 0.3711 -0.0679 0.0280  -0.0191 196 LEU B CG  
5198  C CD1 . LEU B 196 ? 0.4158 0.4518 0.3536 -0.0614 0.0248  -0.0227 196 LEU B CD1 
5199  C CD2 . LEU B 196 ? 0.4233 0.4695 0.3742 -0.0807 0.0236  -0.0210 196 LEU B CD2 
5200  N N   . TYR B 197 ? 0.3498 0.4098 0.3111 -0.0517 0.0484  -0.0103 197 TYR B N   
5201  C CA  . TYR B 197 ? 0.3765 0.4523 0.3508 -0.0455 0.0515  -0.0084 197 TYR B CA  
5202  C C   . TYR B 197 ? 0.3814 0.4485 0.3451 -0.0353 0.0525  -0.0105 197 TYR B C   
5203  O O   . TYR B 197 ? 0.3575 0.4319 0.3276 -0.0294 0.0498  -0.0112 197 TYR B O   
5204  C CB  . TYR B 197 ? 0.3651 0.4495 0.3488 -0.0481 0.0609  -0.0045 197 TYR B CB  
5205  C CG  . TYR B 197 ? 0.3472 0.4497 0.3512 -0.0570 0.0596  -0.0012 197 TYR B CG  
5206  C CD1 . TYR B 197 ? 0.4096 0.5322 0.4326 -0.0556 0.0549  0.0005  197 TYR B CD1 
5207  C CD2 . TYR B 197 ? 0.3990 0.4992 0.4043 -0.0670 0.0634  0.0009  197 TYR B CD2 
5208  C CE1 . TYR B 197 ? 0.4246 0.5662 0.4681 -0.0641 0.0528  0.0041  197 TYR B CE1 
5209  C CE2 . TYR B 197 ? 0.4201 0.5387 0.4462 -0.0763 0.0619  0.0040  197 TYR B CE2 
5210  C CZ  . TYR B 197 ? 0.4311 0.5709 0.4764 -0.0749 0.0562  0.0056  197 TYR B CZ  
5211  O OH  . TYR B 197 ? 0.5044 0.6642 0.5717 -0.0845 0.0533  0.0092  197 TYR B OH  
5212  N N   . ALA B 198 ? 0.3956 0.4461 0.3424 -0.0335 0.0552  -0.0116 198 ALA B N   
5213  C CA  . ALA B 198 ? 0.3645 0.4056 0.2998 -0.0252 0.0550  -0.0139 198 ALA B CA  
5214  C C   . ALA B 198 ? 0.3978 0.4363 0.3318 -0.0223 0.0469  -0.0167 198 ALA B C   
5215  O O   . ALA B 198 ? 0.3986 0.4400 0.3350 -0.0162 0.0457  -0.0181 198 ALA B O   
5216  C CB  . ALA B 198 ? 0.3773 0.4020 0.2949 -0.0253 0.0577  -0.0134 198 ALA B CB  
5217  N N   . SER B 199 ? 0.3509 0.3826 0.2805 -0.0265 0.0421  -0.0177 199 SER B N   
5218  C CA  . SER B 199 ? 0.3541 0.3819 0.2809 -0.0236 0.0359  -0.0202 199 SER B CA  
5219  C C   . SER B 199 ? 0.3307 0.3717 0.2690 -0.0235 0.0321  -0.0201 199 SER B C   
5220  O O   . SER B 199 ? 0.3462 0.3867 0.2841 -0.0188 0.0290  -0.0213 199 SER B O   
5221  C CB  . SER B 199 ? 0.3914 0.4070 0.3098 -0.0277 0.0336  -0.0214 199 SER B CB  
5222  O OG  . SER B 199 ? 0.4026 0.4227 0.3260 -0.0358 0.0327  -0.0213 199 SER B OG  
5223  N N   . LEU B 200 ? 0.3342 0.3872 0.2831 -0.0289 0.0319  -0.0182 200 LEU B N   
5224  C CA  . LEU B 200 ? 0.3371 0.4038 0.2971 -0.0287 0.0272  -0.0169 200 LEU B CA  
5225  C C   . LEU B 200 ? 0.3311 0.4067 0.3006 -0.0211 0.0298  -0.0150 200 LEU B C   
5226  O O   . LEU B 200 ? 0.3334 0.4127 0.3063 -0.0169 0.0261  -0.0144 200 LEU B O   
5227  C CB  . LEU B 200 ? 0.3949 0.4736 0.3652 -0.0373 0.0251  -0.0149 200 LEU B CB  
5228  C CG  . LEU B 200 ? 0.4304 0.5100 0.3981 -0.0442 0.0175  -0.0163 200 LEU B CG  
5229  C CD1 . LEU B 200 ? 0.4365 0.5345 0.4201 -0.0511 0.0145  -0.0129 200 LEU B CD1 
5230  C CD2 . LEU B 200 ? 0.3633 0.4408 0.3252 -0.0400 0.0123  -0.0174 200 LEU B CD2 
5231  N N   . THR B 201 ? 0.3123 0.3908 0.2860 -0.0192 0.0369  -0.0137 201 THR B N   
5232  C CA  . THR B 201 ? 0.3310 0.4160 0.3131 -0.0114 0.0408  -0.0125 201 THR B CA  
5233  C C   . THR B 201 ? 0.3193 0.3911 0.2900 -0.0048 0.0406  -0.0158 201 THR B C   
5234  O O   . THR B 201 ? 0.3109 0.3855 0.2875 0.0014  0.0414  -0.0154 201 THR B O   
5235  C CB  . THR B 201 ? 0.3483 0.4385 0.3365 -0.0106 0.0501  -0.0109 201 THR B CB  
5236  O OG1 . THR B 201 ? 0.3041 0.3804 0.2765 -0.0123 0.0548  -0.0128 201 THR B OG1 
5237  C CG2 . THR B 201 ? 0.3262 0.4341 0.3318 -0.0170 0.0502  -0.0066 201 THR B CG2 
5238  N N   . ALA B 202 ? 0.3244 0.3821 0.2801 -0.0061 0.0394  -0.0186 202 ALA B N   
5239  C CA  . ALA B 202 ? 0.3181 0.3654 0.2652 -0.0013 0.0373  -0.0213 202 ALA B CA  
5240  C C   . ALA B 202 ? 0.3519 0.4037 0.3059 0.0011  0.0324  -0.0206 202 ALA B C   
5241  O O   . ALA B 202 ? 0.3518 0.3982 0.3037 0.0057  0.0319  -0.0221 202 ALA B O   
5242  C CB  . ALA B 202 ? 0.3736 0.4085 0.3076 -0.0035 0.0346  -0.0231 202 ALA B CB  
5243  N N   . GLN B 203 ? 0.2905 0.3516 0.2516 -0.0026 0.0285  -0.0183 203 GLN B N   
5244  C CA  . GLN B 203 ? 0.3121 0.3762 0.2763 -0.0014 0.0234  -0.0170 203 GLN B CA  
5245  C C   . GLN B 203 ? 0.2850 0.3610 0.2630 0.0026  0.0234  -0.0130 203 GLN B C   
5246  O O   . GLN B 203 ? 0.3095 0.3882 0.2900 0.0042  0.0193  -0.0108 203 GLN B O   
5247  C CB  . GLN B 203 ? 0.2920 0.3571 0.2523 -0.0080 0.0187  -0.0170 203 GLN B CB  
5248  C CG  . GLN B 203 ? 0.2773 0.3294 0.2252 -0.0110 0.0197  -0.0205 203 GLN B CG  
5249  C CD  . GLN B 203 ? 0.3142 0.3637 0.2562 -0.0168 0.0163  -0.0216 203 GLN B CD  
5250  O OE1 . GLN B 203 ? 0.3400 0.3915 0.2809 -0.0170 0.0127  -0.0212 203 GLN B OE1 
5251  N NE2 . GLN B 203 ? 0.3436 0.3858 0.2794 -0.0214 0.0179  -0.0234 203 GLN B NE2 
5252  N N   . PHE B 204 ? 0.2848 0.3674 0.2715 0.0050  0.0287  -0.0118 204 PHE B N   
5253  C CA  . PHE B 204 ? 0.2977 0.3902 0.2987 0.0108  0.0297  -0.0078 204 PHE B CA  
5254  C C   . PHE B 204 ? 0.2813 0.3735 0.2876 0.0164  0.0385  -0.0085 204 PHE B C   
5255  O O   . PHE B 204 ? 0.3086 0.4118 0.3302 0.0211  0.0410  -0.0045 204 PHE B O   
5256  C CB  . PHE B 204 ? 0.3016 0.4120 0.3163 0.0071  0.0247  -0.0023 204 PHE B CB  
5257  C CG  . PHE B 204 ? 0.3244 0.4422 0.3424 0.0000  0.0260  -0.0023 204 PHE B CG  
5258  C CD1 . PHE B 204 ? 0.2858 0.4107 0.3141 0.0018  0.0337  -0.0012 204 PHE B CD1 
5259  C CD2 . PHE B 204 ? 0.3273 0.4443 0.3381 -0.0088 0.0201  -0.0035 204 PHE B CD2 
5260  C CE1 . PHE B 204 ? 0.3397 0.4718 0.3724 -0.0056 0.0354  -0.0004 204 PHE B CE1 
5261  C CE2 . PHE B 204 ? 0.3735 0.4958 0.3874 -0.0164 0.0213  -0.0035 204 PHE B CE2 
5262  C CZ  . PHE B 204 ? 0.3380 0.4684 0.3635 -0.0150 0.0288  -0.0016 204 PHE B CZ  
5263  N N   . ILE B 205 ? 0.2784 0.3582 0.2719 0.0164  0.0435  -0.0132 205 ILE B N   
5264  C CA  . ILE B 205 ? 0.2638 0.3391 0.2567 0.0218  0.0526  -0.0154 205 ILE B CA  
5265  C C   . ILE B 205 ? 0.3208 0.3788 0.2996 0.0249  0.0523  -0.0204 205 ILE B C   
5266  O O   . ILE B 205 ? 0.3524 0.4026 0.3210 0.0216  0.0463  -0.0223 205 ILE B O   
5267  C CB  . ILE B 205 ? 0.2930 0.3688 0.2809 0.0177  0.0584  -0.0162 205 ILE B CB  
5268  C CG1 . ILE B 205 ? 0.3166 0.4107 0.3207 0.0131  0.0579  -0.0110 205 ILE B CG1 
5269  C CG2 . ILE B 205 ? 0.3288 0.3964 0.3097 0.0225  0.0686  -0.0194 205 ILE B CG2 
5270  C CD1 . ILE B 205 ? 0.3242 0.4353 0.3511 0.0184  0.0610  -0.0060 205 ILE B CD1 
5271  N N   . ASP B 206 ? 0.3611 0.4135 0.3409 0.0314  0.0586  -0.0223 206 ASP B N   
5272  C CA  . ASP B 206 ? 0.3839 0.4190 0.3497 0.0331  0.0583  -0.0279 206 ASP B CA  
5273  C C   . ASP B 206 ? 0.4089 0.4340 0.3562 0.0282  0.0565  -0.0319 206 ASP B C   
5274  O O   . ASP B 206 ? 0.4040 0.4284 0.3447 0.0270  0.0620  -0.0327 206 ASP B O   
5275  C CB  . ASP B 206 ? 0.3959 0.4242 0.3623 0.0401  0.0675  -0.0306 206 ASP B CB  
5276  C CG  . ASP B 206 ? 0.5151 0.5252 0.4693 0.0416  0.0660  -0.0364 206 ASP B CG  
5277  O OD1 . ASP B 206 ? 0.5131 0.5127 0.4500 0.0374  0.0636  -0.0410 206 ASP B OD1 
5278  O OD2 . ASP B 206 ? 0.4925 0.4985 0.4542 0.0465  0.0671  -0.0360 206 ASP B OD2 
5279  N N   . LYS B 207 ? 0.5228 0.3557 0.3098 0.0448  0.0422  -0.0468 207 LYS B N   
5280  C CA  . LYS B 207 ? 0.5141 0.3706 0.3213 0.0356  0.0422  -0.0471 207 LYS B CA  
5281  C C   . LYS B 207 ? 0.4923 0.3633 0.3032 0.0392  0.0396  -0.0520 207 LYS B C   
5282  O O   . LYS B 207 ? 0.4774 0.3721 0.3017 0.0379  0.0375  -0.0501 207 LYS B O   
5283  C CB  . LYS B 207 ? 0.6088 0.4525 0.4193 0.0213  0.0470  -0.0508 207 LYS B CB  
5284  C CG  . LYS B 207 ? 0.6740 0.5088 0.4840 0.0158  0.0501  -0.0458 207 LYS B CG  
5285  C CD  . LYS B 207 ? 0.5727 0.4330 0.4032 0.0113  0.0482  -0.0418 207 LYS B CD  
5286  C CE  . LYS B 207 ? 0.6176 0.4683 0.4474 0.0053  0.0516  -0.0378 207 LYS B CE  
5287  N NZ  . LYS B 207 ? 0.6484 0.4716 0.4555 0.0108  0.0536  -0.0352 207 LYS B NZ  
5288  N N   A ARG B 208 ? 0.5034 0.3582 0.3006 0.0438  0.0399  -0.0583 208 ARG B N   
5289  N N   B ARG B 208 ? 0.5036 0.3584 0.3008 0.0438  0.0399  -0.0582 208 ARG B N   
5290  C CA  A ARG B 208 ? 0.5315 0.3995 0.3303 0.0483  0.0372  -0.0633 208 ARG B CA  
5291  C CA  B ARG B 208 ? 0.5316 0.3995 0.3303 0.0484  0.0372  -0.0633 208 ARG B CA  
5292  C C   A ARG B 208 ? 0.5192 0.4111 0.3222 0.0587  0.0345  -0.0586 208 ARG B C   
5293  C C   B ARG B 208 ? 0.5190 0.4111 0.3222 0.0586  0.0345  -0.0585 208 ARG B C   
5294  O O   A ARG B 208 ? 0.5147 0.4270 0.3252 0.0588  0.0330  -0.0586 208 ARG B O   
5295  O O   B ARG B 208 ? 0.5145 0.4271 0.3254 0.0586  0.0331  -0.0584 208 ARG B O   
5296  C CB  A ARG B 208 ? 0.5742 0.4181 0.3561 0.0522  0.0380  -0.0712 208 ARG B CB  
5297  C CB  B ARG B 208 ? 0.5744 0.4180 0.3557 0.0528  0.0380  -0.0708 208 ARG B CB  
5298  C CG  A ARG B 208 ? 0.6132 0.4343 0.3920 0.0393  0.0424  -0.0780 208 ARG B CG  
5299  C CG  B ARG B 208 ? 0.6135 0.4349 0.3915 0.0404  0.0421  -0.0780 208 ARG B CG  
5300  C CD  A ARG B 208 ? 0.6454 0.4372 0.4045 0.0424  0.0443  -0.0855 208 ARG B CD  
5301  C CD  B ARG B 208 ? 0.6427 0.4374 0.4018 0.0445  0.0434  -0.0855 208 ARG B CD  
5302  N NE  A ARG B 208 ? 0.6770 0.4481 0.4344 0.0279  0.0501  -0.0937 208 ARG B NE  
5303  N NE  B ARG B 208 ? 0.6774 0.4399 0.4160 0.0481  0.0463  -0.0821 208 ARG B NE  
5304  C CZ  A ARG B 208 ? 0.6432 0.4267 0.4146 0.0186  0.0499  -0.1029 208 ARG B CZ  
5305  C CZ  B ARG B 208 ? 0.6684 0.4271 0.3954 0.0630  0.0428  -0.0775 208 ARG B CZ  
5306  N NH1 A ARG B 208 ? 0.6751 0.4883 0.4596 0.0234  0.0436  -0.1044 208 ARG B NH1 
5307  N NH1 B ARG B 208 ? 0.6573 0.4450 0.3937 0.0740  0.0377  -0.0755 208 ARG B NH1 
5308  N NH2 A ARG B 208 ? 0.6805 0.4452 0.4516 0.0043  0.0565  -0.1116 208 ARG B NH2 
5309  N NH2 B ARG B 208 ? 0.6910 0.4150 0.3949 0.0674  0.0445  -0.0761 208 ARG B NH2 
5310  N N   . GLU B 209 ? 0.4745 0.3638 0.2719 0.0675  0.0341  -0.0553 209 GLU B N   
5311  C CA  . GLU B 209 ? 0.4893 0.4036 0.2933 0.0761  0.0329  -0.0525 209 GLU B CA  
5312  C C   . GLU B 209 ? 0.4612 0.3970 0.2812 0.0691  0.0339  -0.0456 209 GLU B C   
5313  O O   . GLU B 209 ? 0.4607 0.4181 0.2874 0.0700  0.0347  -0.0440 209 GLU B O   
5314  C CB  . GLU B 209 ? 0.5077 0.4155 0.3037 0.0879  0.0311  -0.0530 209 GLU B CB  
5315  C CG  . GLU B 209 ? 0.5829 0.4742 0.3622 0.0995  0.0292  -0.0604 209 GLU B CG  
5316  C CD  . GLU B 209 ? 0.6745 0.5430 0.4385 0.1100  0.0263  -0.0612 209 GLU B CD  
5317  O OE1 . GLU B 209 ? 0.5984 0.4806 0.3684 0.1173  0.0237  -0.0592 209 GLU B OE1 
5318  O OE2 . GLU B 209 ? 0.7606 0.5976 0.5051 0.1130  0.0260  -0.0653 209 GLU B OE2 
5319  N N   . HIS B 210 ? 0.4183 0.3464 0.2426 0.0618  0.0344  -0.0415 210 HIS B N   
5320  C CA  . HIS B 210 ? 0.3950 0.3406 0.2340 0.0548  0.0351  -0.0351 210 HIS B CA  
5321  C C   . HIS B 210 ? 0.4568 0.4118 0.3016 0.0482  0.0348  -0.0353 210 HIS B C   
5322  O O   . HIS B 210 ? 0.4253 0.3980 0.2770 0.0472  0.0353  -0.0309 210 HIS B O   
5323  C CB  . HIS B 210 ? 0.3942 0.3265 0.2346 0.0486  0.0357  -0.0320 210 HIS B CB  
5324  C CG  . HIS B 210 ? 0.4264 0.3751 0.2804 0.0443  0.0359  -0.0257 210 HIS B CG  
5325  N ND1 . HIS B 210 ? 0.4289 0.3847 0.2930 0.0352  0.0363  -0.0231 210 HIS B ND1 
5326  C CD2 . HIS B 210 ? 0.3948 0.3535 0.2538 0.0481  0.0354  -0.0225 210 HIS B CD2 
5327  C CE1 . HIS B 210 ? 0.4404 0.4079 0.3140 0.0332  0.0366  -0.0177 210 HIS B CE1 
5328  N NE2 . HIS B 210 ? 0.4119 0.3823 0.2835 0.0402  0.0363  -0.0176 210 HIS B NE2 
5329  N N   . ASN B 211 ? 0.4295 0.3718 0.2704 0.0441  0.0340  -0.0411 211 ASN B N   
5330  C CA  . ASN B 211 ? 0.4455 0.3971 0.2912 0.0402  0.0317  -0.0431 211 ASN B CA  
5331  C C   . ASN B 211 ? 0.4826 0.4477 0.3229 0.0474  0.0310  -0.0430 211 ASN B C   
5332  O O   . ASN B 211 ? 0.4425 0.4187 0.2847 0.0462  0.0295  -0.0405 211 ASN B O   
5333  C CB  . ASN B 211 ? 0.4553 0.3929 0.2986 0.0356  0.0308  -0.0524 211 ASN B CB  
5334  C CG  . ASN B 211 ? 0.4723 0.3996 0.3229 0.0255  0.0327  -0.0536 211 ASN B CG  
5335  O OD1 . ASN B 211 ? 0.4504 0.3823 0.3081 0.0224  0.0336  -0.0472 211 ASN B OD1 
5336  N ND2 . ASN B 211 ? 0.4711 0.3829 0.3188 0.0201  0.0345  -0.0624 211 ASN B ND2 
5337  N N   . GLU B 212 ? 0.4754 0.4373 0.3067 0.0553  0.0321  -0.0465 212 GLU B N   
5338  C CA  . GLU B 212 ? 0.4323 0.4071 0.2577 0.0620  0.0326  -0.0473 212 GLU B CA  
5339  C C   . GLU B 212 ? 0.4487 0.4415 0.2799 0.0619  0.0360  -0.0397 212 GLU B C   
5340  O O   . GLU B 212 ? 0.4466 0.4501 0.2742 0.0621  0.0374  -0.0374 212 GLU B O   
5341  C CB  . GLU B 212 ? 0.5210 0.4881 0.3366 0.0708  0.0329  -0.0538 212 GLU B CB  
5342  C CG  . GLU B 212 ? 0.5389 0.5191 0.3483 0.0783  0.0344  -0.0560 212 GLU B CG  
5343  C CD  . GLU B 212 ? 0.6194 0.5970 0.4211 0.0780  0.0315  -0.0614 212 GLU B CD  
5344  O OE1 . GLU B 212 ? 0.6920 0.6573 0.4950 0.0725  0.0281  -0.0654 212 GLU B OE1 
5345  O OE2 . GLU B 212 ? 0.6697 0.6585 0.4646 0.0831  0.0330  -0.0623 212 GLU B OE2 
5346  N N   A MET B 213 ? 0.4645 0.4593 0.3033 0.0612  0.0377  -0.0359 213 MET B N   
5347  N N   B MET B 213 ? 0.4646 0.4595 0.3033 0.0613  0.0378  -0.0360 213 MET B N   
5348  C CA  A MET B 213 ? 0.4730 0.4853 0.3195 0.0595  0.0417  -0.0300 213 MET B CA  
5349  C CA  B MET B 213 ? 0.4731 0.4854 0.3196 0.0594  0.0417  -0.0299 213 MET B CA  
5350  C C   A MET B 213 ? 0.4549 0.4693 0.3065 0.0507  0.0416  -0.0233 213 MET B C   
5351  C C   B MET B 213 ? 0.4552 0.4694 0.3063 0.0507  0.0415  -0.0235 213 MET B C   
5352  O O   A MET B 213 ? 0.4584 0.4843 0.3103 0.0485  0.0455  -0.0187 213 MET B O   
5353  O O   B MET B 213 ? 0.4588 0.4841 0.3096 0.0487  0.0453  -0.0189 213 MET B O   
5354  C CB  A MET B 213 ? 0.4820 0.4969 0.3359 0.0623  0.0422  -0.0298 213 MET B CB  
5355  C CB  B MET B 213 ? 0.4820 0.4971 0.3363 0.0617  0.0422  -0.0294 213 MET B CB  
5356  C CG  A MET B 213 ? 0.4604 0.4962 0.3244 0.0608  0.0468  -0.0265 213 MET B CG  
5357  C CG  B MET B 213 ? 0.4584 0.4936 0.3232 0.0589  0.0469  -0.0253 213 MET B CG  
5358  S SD  A MET B 213 ? 0.5390 0.5930 0.3988 0.0659  0.0527  -0.0304 213 MET B SD  
5359  S SD  B MET B 213 ? 0.5497 0.6051 0.4121 0.0631  0.0533  -0.0282 213 MET B SD  
5360  C CE  A MET B 213 ? 0.4983 0.5664 0.3656 0.0548  0.0597  -0.0225 213 MET B CE  
5361  C CE  B MET B 213 ? 0.4305 0.4781 0.2831 0.0759  0.0497  -0.0377 213 MET B CE  
5362  N N   . LEU B 214 ? 0.4267 0.4293 0.2814 0.0455  0.0377  -0.0233 214 LEU B N   
5363  C CA  . LEU B 214 ? 0.4037 0.4074 0.2622 0.0391  0.0361  -0.0186 214 LEU B CA  
5364  C C   . LEU B 214 ? 0.4205 0.4256 0.2686 0.0414  0.0342  -0.0196 214 LEU B C   
5365  O O   . LEU B 214 ? 0.4039 0.4126 0.2489 0.0394  0.0348  -0.0139 214 LEU B O   
5366  C CB  . LEU B 214 ? 0.4202 0.4131 0.2855 0.0337  0.0326  -0.0207 214 LEU B CB  
5367  C CG  . LEU B 214 ? 0.4260 0.4154 0.2994 0.0304  0.0344  -0.0181 214 LEU B CG  
5368  C CD1 . LEU B 214 ? 0.3908 0.3672 0.2678 0.0249  0.0327  -0.0221 214 LEU B CD1 
5369  C CD2 . LEU B 214 ? 0.4244 0.4236 0.3056 0.0264  0.0361  -0.0106 214 LEU B CD2 
5370  N N   . LYS B 215 ? 0.4486 0.4490 0.2889 0.0462  0.0317  -0.0269 215 LYS B N   
5371  C CA  . LYS B 215 ? 0.4455 0.4469 0.2743 0.0497  0.0288  -0.0289 215 LYS B CA  
5372  C C   . LYS B 215 ? 0.4394 0.4496 0.2580 0.0527  0.0346  -0.0238 215 LYS B C   
5373  O O   . LYS B 215 ? 0.4591 0.4691 0.2673 0.0529  0.0342  -0.0197 215 LYS B O   
5374  C CB  . LYS B 215 ? 0.4283 0.4232 0.2519 0.0537  0.0249  -0.0393 215 LYS B CB  
5375  C CG  . LYS B 215 ? 0.5208 0.5079 0.3536 0.0486  0.0195  -0.0456 215 LYS B CG  
5376  C CD  . LYS B 215 ? 0.5066 0.4881 0.3349 0.0510  0.0156  -0.0572 215 LYS B CD  
5377  C CE  . LYS B 215 ? 0.5795 0.5489 0.4109 0.0483  0.0185  -0.0628 215 LYS B CE  
5378  N NZ  . LYS B 215 ? 0.6824 0.6446 0.5138 0.0465  0.0148  -0.0756 215 LYS B NZ  
5379  N N   . LYS B 216 ? 0.4338 0.4513 0.2545 0.0552  0.0404  -0.0245 216 LYS B N   
5380  C CA  . LYS B 216 ? 0.4409 0.4695 0.2549 0.0564  0.0480  -0.0210 216 LYS B CA  
5381  C C   . LYS B 216 ? 0.4763 0.5079 0.2935 0.0490  0.0522  -0.0120 216 LYS B C   
5382  O O   . LYS B 216 ? 0.4693 0.5011 0.2737 0.0476  0.0565  -0.0074 216 LYS B O   
5383  C CB  . LYS B 216 ? 0.4853 0.5243 0.3061 0.0606  0.0527  -0.0253 216 LYS B CB  
5384  C CG  . LYS B 216 ? 0.5207 0.5760 0.3446 0.0578  0.0624  -0.0218 216 LYS B CG  
5385  C CD  . LYS B 216 ? 0.5568 0.6262 0.3872 0.0642  0.0663  -0.0289 216 LYS B CD  
5386  C CE  . LYS B 216 ? 0.5605 0.6489 0.3985 0.0591  0.0766  -0.0270 216 LYS B CE  
5387  N NZ  . LYS B 216 ? 0.5739 0.6804 0.4162 0.0662  0.0817  -0.0359 216 LYS B NZ  
5388  N N   . THR B 217 ? 0.4391 0.4714 0.2714 0.0441  0.0515  -0.0094 217 THR B N   
5389  C CA  . THR B 217 ? 0.4398 0.4737 0.2772 0.0365  0.0550  -0.0017 217 THR B CA  
5390  C C   . THR B 217 ? 0.4450 0.4673 0.2706 0.0346  0.0513  0.0033  217 THR B C   
5391  O O   . THR B 217 ? 0.4853 0.5060 0.3008 0.0313  0.0567  0.0096  217 THR B O   
5392  C CB  . THR B 217 ? 0.4743 0.5080 0.3286 0.0330  0.0523  -0.0014 217 THR B CB  
5393  O OG1 . THR B 217 ? 0.4613 0.5038 0.3238 0.0368  0.0543  -0.0064 217 THR B OG1 
5394  C CG2 . THR B 217 ? 0.4472 0.4818 0.3072 0.0249  0.0554  0.0061  217 THR B CG2 
5395  N N   . LEU B 218 ? 0.4527 0.4660 0.2779 0.0373  0.0421  -0.0004 218 LEU B N   
5396  C CA  . LEU B 218 ? 0.4319 0.4351 0.2464 0.0380  0.0363  0.0024  218 LEU B CA  
5397  C C   . LEU B 218 ? 0.5276 0.5265 0.3189 0.0434  0.0372  0.0034  218 LEU B C   
5398  O O   . LEU B 218 ? 0.5607 0.5498 0.3373 0.0439  0.0356  0.0089  218 LEU B O   
5399  C CB  . LEU B 218 ? 0.4851 0.4839 0.3077 0.0397  0.0266  -0.0048 218 LEU B CB  
5400  C CG  . LEU B 218 ? 0.4500 0.4498 0.2920 0.0337  0.0262  -0.0049 218 LEU B CG  
5401  C CD1 . LEU B 218 ? 0.4676 0.4639 0.3174 0.0343  0.0188  -0.0144 218 LEU B CD1 
5402  C CD2 . LEU B 218 ? 0.3565 0.3534 0.2015 0.0289  0.0266  0.0028  218 LEU B CD2 
5403  N N   . ALA B 219 ? 0.4899 0.4938 0.2754 0.0483  0.0390  -0.0023 219 ALA B N   
5404  C CA  . ALA B 219 ? 0.5518 0.5524 0.3139 0.0532  0.0415  -0.0015 219 ALA B CA  
5405  C C   . ALA B 219 ? 0.5384 0.5394 0.2899 0.0480  0.0533  0.0073  219 ALA B C   
5406  O O   . ALA B 219 ? 0.5503 0.5414 0.2773 0.0502  0.0555  0.0115  219 ALA B O   
5407  C CB  . ALA B 219 ? 0.4958 0.5033 0.2566 0.0590  0.0421  -0.0102 219 ALA B CB  
5408  N N   . ALA B 220 ? 0.5132 0.5245 0.2817 0.0408  0.0612  0.0098  220 ALA B N   
5409  C CA  . ALA B 220 ? 0.6042 0.6182 0.3662 0.0336  0.0741  0.0162  220 ALA B CA  
5410  C C   . ALA B 220 ? 0.5781 0.5783 0.3347 0.0271  0.0744  0.0254  220 ALA B C   
5411  O O   . ALA B 220 ? 0.5868 0.5792 0.3262 0.0220  0.0840  0.0320  220 ALA B O   
5412  C CB  . ALA B 220 ? 0.5239 0.5578 0.3084 0.0292  0.0820  0.0126  220 ALA B CB  
5413  N N   . LEU B 221 ? 0.5303 0.5265 0.3005 0.0271  0.0648  0.0254  221 LEU B N   
5414  C CA  . LEU B 221 ? 0.5083 0.4940 0.2788 0.0207  0.0652  0.0330  221 LEU B CA  
5415  C C   . LEU B 221 ? 0.6284 0.5926 0.3689 0.0225  0.0650  0.0402  221 LEU B C   
5416  O O   . LEU B 221 ? 0.6384 0.5933 0.3715 0.0147  0.0731  0.0479  221 LEU B O   
5417  C CB  . LEU B 221 ? 0.4922 0.4768 0.2804 0.0221  0.0537  0.0302  221 LEU B CB  
5418  C CG  . LEU B 221 ? 0.5320 0.5325 0.3466 0.0184  0.0555  0.0257  221 LEU B CG  
5419  C CD1 . LEU B 221 ? 0.4152 0.4135 0.2456 0.0190  0.0458  0.0224  221 LEU B CD1 
5420  C CD2 . LEU B 221 ? 0.5137 0.5228 0.3359 0.0096  0.0671  0.0297  221 LEU B CD2 
5421  N N   . PRO B 222 ? 0.6305 0.5843 0.3518 0.0325  0.0560  0.0380  222 PRO B N   
5422  C CA  . PRO B 222 ? 0.6807 0.6104 0.3690 0.0360  0.0547  0.0453  222 PRO B CA  
5423  C C   . PRO B 222 ? 0.7334 0.6548 0.4004 0.0284  0.0711  0.0531  222 PRO B C   
5424  O O   . PRO B 222 ? 0.7670 0.6652 0.4105 0.0262  0.0740  0.0619  222 PRO B O   
5425  C CB  . PRO B 222 ? 0.7011 0.6278 0.3742 0.0487  0.0438  0.0386  222 PRO B CB  
5426  C CG  . PRO B 222 ? 0.6589 0.6030 0.3628 0.0507  0.0346  0.0285  222 PRO B CG  
5427  C CD  . PRO B 222 ? 0.6129 0.5743 0.3406 0.0414  0.0455  0.0282  222 PRO B CD  
5428  N N   . ASN B 223 ? 0.6317 0.5706 0.3062 0.0239  0.0828  0.0496  223 ASN B N   
5429  C CA  . ASN B 223 ? 0.7308 0.6639 0.3852 0.0159  0.1000  0.0551  223 ASN B CA  
5430  C C   . ASN B 223 ? 0.7028 0.6534 0.3812 0.0021  0.1142  0.0548  223 ASN B C   
5431  O O   . ASN B 223 ? 0.6551 0.6071 0.3231 -0.0065 0.1307  0.0566  223 ASN B O   
5432  C CB  . ASN B 223 ? 0.8062 0.7446 0.4447 0.0226  0.1031  0.0501  223 ASN B CB  
5433  C CG  . ASN B 223 ? 0.8122 0.7299 0.4217 0.0355  0.0900  0.0510  223 ASN B CG  
5434  O OD1 . ASN B 223 ? 0.8376 0.7291 0.4213 0.0368  0.0873  0.0591  223 ASN B OD1 
5435  N ND2 . ASN B 223 ? 0.8108 0.7393 0.4255 0.0457  0.0800  0.0418  223 ASN B ND2 
5436  N N   . ARG B 224 ? 0.6705 0.6330 0.3795 -0.0006 0.1083  0.0524  224 ARG B N   
5437  C CA  . ARG B 224 ? 0.6137 0.5959 0.3493 -0.0117 0.1186  0.0500  224 ARG B CA  
5438  C C   . ARG B 224 ? 0.6458 0.6113 0.3707 -0.0239 0.1287  0.0585  224 ARG B C   
5439  O O   . ARG B 224 ? 0.6880 0.6321 0.4032 -0.0226 0.1208  0.0649  224 ARG B O   
5440  C CB  . ARG B 224 ? 0.5828 0.5793 0.3501 -0.0089 0.1072  0.0448  224 ARG B CB  
5441  C CG  . ARG B 224 ? 0.5695 0.5918 0.3648 -0.0150 0.1146  0.0384  224 ARG B CG  
5442  C CD  . ARG B 224 ? 0.5329 0.5626 0.3542 -0.0144 0.1049  0.0359  224 ARG B CD  
5443  N NE  . ARG B 224 ? 0.4982 0.5527 0.3439 -0.0191 0.1117  0.0290  224 ARG B NE  
5444  C CZ  . ARG B 224 ? 0.5368 0.6026 0.4056 -0.0180 0.1055  0.0247  224 ARG B CZ  
5445  N NH1 . ARG B 224 ? 0.4955 0.5492 0.3676 -0.0160 0.0950  0.0278  224 ARG B NH1 
5446  N NH2 . ARG B 224 ? 0.5110 0.6008 0.3999 -0.0193 0.1104  0.0168  224 ARG B NH2 
5447  N N   . LYS B 225 ? 0.7044 0.6794 0.4313 -0.0357 0.1463  0.0577  225 LYS B N   
5448  C CA  . LYS B 225 ? 0.7526 0.7115 0.4707 -0.0495 0.1577  0.0648  225 LYS B CA  
5449  C C   . LYS B 225 ? 0.7304 0.7031 0.4819 -0.0556 0.1542  0.0620  225 LYS B C   
5450  O O   . LYS B 225 ? 0.7976 0.7997 0.5804 -0.0541 0.1515  0.0528  225 LYS B O   
5451  C CB  . LYS B 225 ? 0.8063 0.7717 0.5160 -0.0621 0.1797  0.0633  225 LYS B CB  
5452  C CG  . LYS B 225 ? 0.9123 0.9169 0.6607 -0.0698 0.1884  0.0515  225 LYS B CG  
5453  C CD  . LYS B 225 ? 0.9561 0.9618 0.7060 -0.0895 0.2093  0.0516  225 LYS B CD  
5454  C CE  . LYS B 225 ? 0.9845 0.9910 0.7186 -0.0931 0.2231  0.0505  225 LYS B CE  
5455  N NZ  . LYS B 225 ? 1.0315 1.0319 0.7678 -0.1088 0.2367  0.0523  225 LYS B NZ  
5456  N N   . VAL B 226 ? 0.7135 0.6631 0.4565 -0.0607 0.1524  0.0696  226 VAL B N   
5457  C CA  . VAL B 226 ? 0.6577 0.6179 0.4295 -0.0679 0.1506  0.0672  226 VAL B CA  
5458  C C   . VAL B 226 ? 0.6906 0.6486 0.4618 -0.0859 0.1695  0.0684  226 VAL B C   
5459  O O   . VAL B 226 ? 0.7450 0.6728 0.4845 -0.0922 0.1784  0.0772  226 VAL B O   
5460  C CB  . VAL B 226 ? 0.7030 0.6415 0.4700 -0.0614 0.1354  0.0730  226 VAL B CB  
5461  C CG1 . VAL B 226 ? 0.6476 0.5968 0.4437 -0.0693 0.1341  0.0703  226 VAL B CG1 
5462  C CG2 . VAL B 226 ? 0.6645 0.6074 0.4344 -0.0454 0.1183  0.0698  226 VAL B CG2 
5463  N N   . GLU B 227 ? 0.6473 0.6366 0.4521 -0.0943 0.1761  0.0589  227 GLU B N   
5464  C CA  . GLU B 227 ? 0.7317 0.7226 0.5409 -0.1131 0.1945  0.0576  227 GLU B CA  
5465  C C   . GLU B 227 ? 0.6919 0.6790 0.5183 -0.1205 0.1909  0.0581  227 GLU B C   
5466  O O   . GLU B 227 ? 0.6781 0.6457 0.4933 -0.1347 0.2026  0.0626  227 GLU B O   
5467  C CB  . GLU B 227 ? 0.7787 0.8094 0.6148 -0.1191 0.2062  0.0443  227 GLU B CB  
5468  C CG  . GLU B 227 ? 0.8538 0.8867 0.6713 -0.1190 0.2179  0.0431  227 GLU B CG  
5469  C CD  . GLU B 227 ? 0.9464 0.9573 0.7447 -0.1299 0.2302  0.0490  227 GLU B CD  
5470  O OE1 . GLU B 227 ? 0.9596 0.9622 0.7655 -0.1418 0.2348  0.0501  227 GLU B OE1 
5471  O OE2 . GLU B 227 ? 1.0040 1.0057 0.7787 -0.1266 0.2355  0.0518  227 GLU B OE2 
5472  N N   . ARG B 228 ? 0.6144 0.6181 0.4663 -0.1113 0.1754  0.0534  228 ARG B N   
5473  C CA  . ARG B 228 ? 0.6081 0.6147 0.4811 -0.1170 0.1711  0.0514  228 ARG B CA  
5474  C C   . ARG B 228 ? 0.6463 0.6150 0.4967 -0.1164 0.1648  0.0627  228 ARG B C   
5475  O O   . ARG B 228 ? 0.6522 0.5977 0.4774 -0.1054 0.1559  0.0704  228 ARG B O   
5476  C CB  . ARG B 228 ? 0.5606 0.5936 0.4627 -0.1055 0.1561  0.0433  228 ARG B CB  
5477  C CG  . ARG B 228 ? 0.5530 0.5729 0.4435 -0.0894 0.1397  0.0482  228 ARG B CG  
5478  C CD  . ARG B 228 ? 0.5542 0.5988 0.4693 -0.0790 0.1281  0.0398  228 ARG B CD  
5479  N NE  . ARG B 228 ? 0.4907 0.5426 0.4273 -0.0826 0.1234  0.0363  228 ARG B NE  
5480  C CZ  . ARG B 228 ? 0.5157 0.5497 0.4489 -0.0806 0.1144  0.0414  228 ARG B CZ  
5481  N NH1 . ARG B 228 ? 0.4861 0.4956 0.3977 -0.0741 0.1078  0.0492  228 ARG B NH1 
5482  N NH2 . ARG B 228 ? 0.4805 0.5223 0.4330 -0.0846 0.1113  0.0374  228 ARG B NH2 
5483  N N   . LYS B 229 ? 0.5684 0.5319 0.4292 -0.1277 0.1685  0.0623  229 LYS B N   
5484  C CA  . LYS B 229 ? 0.6521 0.5820 0.4956 -0.1257 0.1606  0.0713  229 LYS B CA  
5485  C C   . LYS B 229 ? 0.6083 0.5484 0.4708 -0.1128 0.1417  0.0685  229 LYS B C   
5486  O O   . LYS B 229 ? 0.5552 0.5258 0.4479 -0.1117 0.1380  0.0592  229 LYS B O   
5487  C CB  . LYS B 229 ? 0.6713 0.5894 0.5169 -0.1433 0.1727  0.0718  229 LYS B CB  
5488  C CG  . LYS B 229 ? 0.7218 0.6272 0.5487 -0.1557 0.1905  0.0741  229 LYS B CG  
5489  C CD  . LYS B 229 ? 0.8305 0.6949 0.6129 -0.1488 0.1896  0.0864  229 LYS B CD  
5490  C CE  . LYS B 229 ? 0.9682 0.8023 0.7342 -0.1591 0.1973  0.0909  229 LYS B CE  
5491  N NZ  . LYS B 229 ? 0.9688 0.7554 0.6948 -0.1504 0.1895  0.1031  229 LYS B NZ  
5492  N N   . THR B 230 ? 0.5849 0.4990 0.4283 -0.1023 0.1296  0.0756  230 THR B N   
5493  C CA  . THR B 230 ? 0.5804 0.5033 0.4401 -0.0906 0.1130  0.0724  230 THR B CA  
5494  C C   . THR B 230 ? 0.5352 0.4652 0.4180 -0.0975 0.1114  0.0683  230 THR B C   
5495  O O   . THR B 230 ? 0.5269 0.4799 0.4344 -0.0935 0.1042  0.0612  230 THR B O   
5496  C CB  . THR B 230 ? 0.5747 0.4699 0.4097 -0.0784 0.1013  0.0791  230 THR B CB  
5497  O OG1 . THR B 230 ? 0.6588 0.5489 0.4723 -0.0716 0.1023  0.0819  230 THR B OG1 
5498  C CG2 . THR B 230 ? 0.5745 0.4796 0.4264 -0.0673 0.0855  0.0745  230 THR B CG2 
5499  N N   . GLY B 231 ? 0.5472 0.4560 0.4204 -0.1083 0.1186  0.0725  231 GLY B N   
5500  C CA  . GLY B 231 ? 0.5324 0.4463 0.4264 -0.1133 0.1153  0.0682  231 GLY B CA  
5501  C C   . GLY B 231 ? 0.5310 0.4375 0.4267 -0.1005 0.0988  0.0689  231 GLY B C   
5502  O O   . GLY B 231 ? 0.5907 0.4818 0.4682 -0.0891 0.0905  0.0736  231 GLY B O   
5503  N N   . ALA B 232 ? 0.5133 0.4326 0.4321 -0.1021 0.0939  0.0630  232 ALA B N   
5504  C CA  . ALA B 232 ? 0.5063 0.4196 0.4281 -0.0916 0.0800  0.0625  232 ALA B CA  
5505  C C   . ALA B 232 ? 0.4645 0.3935 0.3916 -0.0793 0.0713  0.0594  232 ALA B C   
5506  O O   . ALA B 232 ? 0.4852 0.4370 0.4242 -0.0791 0.0739  0.0549  232 ALA B O   
5507  C CB  . ALA B 232 ? 0.4598 0.3829 0.4035 -0.0964 0.0776  0.0565  232 ALA B CB  
5508  N N   . ARG B 233 ? 0.4630 0.3792 0.3815 -0.0689 0.0608  0.0610  233 ARG B N   
5509  C CA  . ARG B 233 ? 0.4541 0.3820 0.3769 -0.0582 0.0526  0.0573  233 ARG B CA  
5510  C C   . ARG B 233 ? 0.4256 0.3678 0.3697 -0.0566 0.0467  0.0504  233 ARG B C   
5511  O O   . ARG B 233 ? 0.4266 0.3599 0.3736 -0.0548 0.0409  0.0492  233 ARG B O   
5512  C CB  . ARG B 233 ? 0.4502 0.3593 0.3541 -0.0481 0.0446  0.0603  233 ARG B CB  
5513  C CG  . ARG B 233 ? 0.4822 0.3739 0.3593 -0.0480 0.0499  0.0676  233 ARG B CG  
5514  C CD  . ARG B 233 ? 0.4818 0.3552 0.3402 -0.0355 0.0392  0.0691  233 ARG B CD  
5515  N NE  . ARG B 233 ? 0.4626 0.3519 0.3288 -0.0262 0.0314  0.0629  233 ARG B NE  
5516  C CZ  . ARG B 233 ? 0.5141 0.4076 0.3700 -0.0226 0.0329  0.0633  233 ARG B CZ  
5517  N NH1 . ARG B 233 ? 0.4913 0.3759 0.3291 -0.0272 0.0423  0.0697  233 ARG B NH1 
5518  N NH2 . ARG B 233 ? 0.4812 0.3886 0.3457 -0.0150 0.0259  0.0565  233 ARG B NH2 
5519  N N   . PHE B 234 ? 0.4156 0.3785 0.3730 -0.0570 0.0485  0.0456  234 PHE B N   
5520  C CA  . PHE B 234 ? 0.3359 0.3107 0.3099 -0.0560 0.0445  0.0396  234 PHE B CA  
5521  C C   . PHE B 234 ? 0.3763 0.3555 0.3506 -0.0479 0.0389  0.0361  234 PHE B C   
5522  O O   . PHE B 234 ? 0.3704 0.3508 0.3365 -0.0436 0.0391  0.0370  234 PHE B O   
5523  C CB  . PHE B 234 ? 0.3777 0.3707 0.3643 -0.0610 0.0497  0.0357  234 PHE B CB  
5524  C CG  . PHE B 234 ? 0.3673 0.3606 0.3612 -0.0705 0.0545  0.0353  234 PHE B CG  
5525  C CD1 . PHE B 234 ? 0.4134 0.3901 0.4042 -0.0738 0.0529  0.0378  234 PHE B CD1 
5526  C CD2 . PHE B 234 ? 0.4264 0.4378 0.4321 -0.0758 0.0600  0.0307  234 PHE B CD2 
5527  C CE1 . PHE B 234 ? 0.4808 0.4563 0.4784 -0.0836 0.0578  0.0367  234 PHE B CE1 
5528  C CE2 . PHE B 234 ? 0.4801 0.4938 0.4952 -0.0857 0.0647  0.0283  234 PHE B CE2 
5529  C CZ  . PHE B 234 ? 0.4459 0.4408 0.4566 -0.0902 0.0638  0.0315  234 PHE B CZ  
5530  N N   . MET B 235 ? 0.3250 0.3061 0.3082 -0.0464 0.0346  0.0316  235 MET B N   
5531  C CA  . MET B 235 ? 0.3254 0.3117 0.3104 -0.0414 0.0319  0.0271  235 MET B CA  
5532  C C   . MET B 235 ? 0.3538 0.3489 0.3471 -0.0428 0.0331  0.0233  235 MET B C   
5533  O O   . MET B 235 ? 0.3678 0.3638 0.3679 -0.0467 0.0333  0.0225  235 MET B O   
5534  C CB  . MET B 235 ? 0.3757 0.3545 0.3611 -0.0380 0.0264  0.0239  235 MET B CB  
5535  C CG  . MET B 235 ? 0.3529 0.3355 0.3431 -0.0362 0.0253  0.0176  235 MET B CG  
5536  S SD  . MET B 235 ? 0.3830 0.3609 0.3772 -0.0333 0.0197  0.0117  235 MET B SD  
5537  C CE  . MET B 235 ? 0.3408 0.3234 0.3350 -0.0318 0.0211  0.0051  235 MET B CE  
5538  N N   . THR B 236 ? 0.3223 0.3226 0.3134 -0.0390 0.0335  0.0207  236 THR B N   
5539  C CA  . THR B 236 ? 0.3178 0.3222 0.3123 -0.0382 0.0333  0.0170  236 THR B CA  
5540  C C   . THR B 236 ? 0.3243 0.3206 0.3151 -0.0363 0.0319  0.0135  236 THR B C   
5541  O O   . THR B 236 ? 0.3242 0.3164 0.3106 -0.0345 0.0317  0.0127  236 THR B O   
5542  C CB  . THR B 236 ? 0.3534 0.3672 0.3460 -0.0346 0.0348  0.0158  236 THR B CB  
5543  O OG1 . THR B 236 ? 0.3406 0.3523 0.3251 -0.0307 0.0354  0.0165  236 THR B OG1 
5544  C CG2 . THR B 236 ? 0.3298 0.3550 0.3294 -0.0385 0.0377  0.0169  236 THR B CG2 
5545  N N   . ILE B 237 ? 0.2929 0.2867 0.2855 -0.0373 0.0313  0.0107  237 ILE B N   
5546  C CA  . ILE B 237 ? 0.2889 0.2736 0.2776 -0.0376 0.0320  0.0069  237 ILE B CA  
5547  C C   . ILE B 237 ? 0.3345 0.3149 0.3154 -0.0353 0.0326  0.0048  237 ILE B C   
5548  O O   . ILE B 237 ? 0.3203 0.3058 0.3038 -0.0345 0.0308  0.0048  237 ILE B O   
5549  C CB  . ILE B 237 ? 0.3130 0.2953 0.3096 -0.0415 0.0310  0.0049  237 ILE B CB  
5550  C CG1 . ILE B 237 ? 0.2983 0.2820 0.2997 -0.0416 0.0287  0.0068  237 ILE B CG1 
5551  C CG2 . ILE B 237 ? 0.3584 0.3335 0.3522 -0.0430 0.0335  -0.0005 237 ILE B CG2 
5552  C CD1 . ILE B 237 ? 0.3305 0.3112 0.3398 -0.0435 0.0262  0.0039  237 ILE B CD1 
5553  N N   . GLY B 238 ? 0.3216 0.2917 0.2912 -0.0337 0.0350  0.0027  238 GLY B N   
5554  C CA  . GLY B 238 ? 0.3501 0.3112 0.3070 -0.0302 0.0352  0.0014  238 GLY B CA  
5555  C C   . GLY B 238 ? 0.3373 0.2829 0.2786 -0.0290 0.0391  -0.0001 238 GLY B C   
5556  O O   . GLY B 238 ? 0.3538 0.2970 0.2973 -0.0329 0.0422  -0.0017 238 GLY B O   
5557  N N   . SER B 239 ? 0.3822 0.3160 0.3067 -0.0236 0.0387  -0.0004 239 SER B N   
5558  C CA  . SER B 239 ? 0.3856 0.2994 0.2911 -0.0228 0.0431  -0.0015 239 SER B CA  
5559  C C   . SER B 239 ? 0.3569 0.2729 0.2586 -0.0166 0.0411  -0.0002 239 SER B C   
5560  O O   . SER B 239 ? 0.4182 0.3379 0.3263 -0.0201 0.0432  -0.0008 239 SER B O   
5561  C CB  . SER B 239 ? 0.3801 0.2745 0.2640 -0.0190 0.0437  -0.0019 239 SER B CB  
5562  O OG  . SER B 239 ? 0.3651 0.2672 0.2471 -0.0091 0.0360  -0.0011 239 SER B OG  
5563  N N   . GLU B 240 ? 0.3876 0.3045 0.2811 -0.0067 0.0360  0.0005  240 GLU B N   
5564  C CA  . GLU B 240 ? 0.4207 0.3399 0.3101 0.0002  0.0341  0.0007  240 GLU B CA  
5565  C C   . GLU B 240 ? 0.4216 0.3680 0.3322 0.0007  0.0310  0.0015  240 GLU B C   
5566  O O   . GLU B 240 ? 0.4128 0.3658 0.3293 -0.0011 0.0325  0.0022  240 GLU B O   
5567  C CB  . GLU B 240 ? 0.4806 0.3863 0.3492 0.0122  0.0300  -0.0004 240 GLU B CB  
5568  C CG  . GLU B 240 ? 0.5059 0.4223 0.3765 0.0209  0.0264  -0.0015 240 GLU B CG  
5569  C CD  . GLU B 240 ? 0.5418 0.4469 0.4050 0.0188  0.0309  -0.0013 240 GLU B CD  
5570  O OE1 . GLU B 240 ? 0.5567 0.4474 0.4155 0.0098  0.0370  -0.0011 240 GLU B OE1 
5571  O OE2 . GLU B 240 ? 0.6077 0.5229 0.4739 0.0251  0.0286  -0.0024 240 GLU B OE2 
5572  N N   . ASN B 241 ? 0.3889 0.3501 0.3097 0.0025  0.0270  0.0009  241 ASN B N   
5573  C CA  . ASN B 241 ? 0.4020 0.3874 0.3418 0.0012  0.0258  0.0010  241 ASN B CA  
5574  C C   . ASN B 241 ? 0.4231 0.4163 0.3613 0.0081  0.0251  -0.0002 241 ASN B C   
5575  O O   . ASN B 241 ? 0.3777 0.3788 0.3227 0.0045  0.0280  0.0016  241 ASN B O   
5576  C CB  . ASN B 241 ? 0.3852 0.3764 0.3383 -0.0090 0.0292  0.0042  241 ASN B CB  
5577  C CG  . ASN B 241 ? 0.3877 0.3779 0.3477 -0.0150 0.0290  0.0043  241 ASN B CG  
5578  O OD1 . ASN B 241 ? 0.3983 0.3846 0.3536 -0.0122 0.0266  0.0021  241 ASN B OD1 
5579  N ND2 . ASN B 241 ? 0.3979 0.3905 0.3675 -0.0222 0.0308  0.0064  241 ASN B ND2 
5580  N N   . ASP B 242 ? 0.3885 0.3788 0.3162 0.0190  0.0208  -0.0039 242 ASP B N   
5581  C CA  . ASP B 242 ? 0.4495 0.4473 0.3757 0.0265  0.0201  -0.0061 242 ASP B CA  
5582  C C   . ASP B 242 ? 0.4746 0.4982 0.4151 0.0322  0.0166  -0.0117 242 ASP B C   
5583  O O   . ASP B 242 ? 0.5067 0.5377 0.4455 0.0407  0.0150  -0.0155 242 ASP B O   
5584  C CB  . ASP B 242 ? 0.4633 0.4379 0.3658 0.0363  0.0179  -0.0074 242 ASP B CB  
5585  C CG  . ASP B 242 ? 0.5161 0.4783 0.4042 0.0454  0.0122  -0.0100 242 ASP B CG  
5586  O OD1 . ASP B 242 ? 0.5695 0.5411 0.4666 0.0434  0.0097  -0.0112 242 ASP B OD1 
5587  O OD2 . ASP B 242 ? 0.6296 0.5703 0.4948 0.0554  0.0096  -0.0112 242 ASP B OD2 
5588  N N   . ASP B 243 ? 0.4323 0.4709 0.3879 0.0275  0.0156  -0.0134 243 ASP B N   
5589  C CA  . ASP B 243 ? 0.4297 0.4957 0.4021 0.0313  0.0132  -0.0208 243 ASP B CA  
5590  C C   . ASP B 243 ? 0.4439 0.5278 0.4323 0.0216  0.0207  -0.0192 243 ASP B C   
5591  O O   . ASP B 243 ? 0.4259 0.5185 0.4277 0.0105  0.0247  -0.0175 243 ASP B O   
5592  C CB  . ASP B 243 ? 0.4431 0.5172 0.4247 0.0300  0.0091  -0.0248 243 ASP B CB  
5593  C CG  . ASP B 243 ? 0.4981 0.6011 0.4964 0.0366  0.0047  -0.0359 243 ASP B CG  
5594  O OD1 . ASP B 243 ? 0.4790 0.5989 0.4859 0.0385  0.0075  -0.0395 243 ASP B OD1 
5595  O OD2 . ASP B 243 ? 0.5338 0.6440 0.5373 0.0400  -0.0014 -0.0420 243 ASP B OD2 
5596  N N   . ILE B 244 ? 0.4189 0.4934 0.5214 -0.0388 0.0521  -0.0470 244 ILE B N   
5597  C CA  . ILE B 244 ? 0.3992 0.4739 0.4948 -0.0475 0.0653  -0.0462 244 ILE B CA  
5598  C C   . ILE B 244 ? 0.4180 0.5005 0.5275 -0.0567 0.0724  -0.0518 244 ILE B C   
5599  O O   . ILE B 244 ? 0.4278 0.5029 0.5259 -0.0656 0.0812  -0.0475 244 ILE B O   
5600  C CB  . ILE B 244 ? 0.4354 0.5189 0.5334 -0.0456 0.0704  -0.0508 244 ILE B CB  
5601  C CG1 . ILE B 244 ? 0.4210 0.4978 0.5085 -0.0360 0.0618  -0.0465 244 ILE B CG1 
5602  C CG2 . ILE B 244 ? 0.4100 0.4897 0.4939 -0.0546 0.0839  -0.0482 244 ILE B CG2 
5603  C CD1 . ILE B 244 ? 0.4318 0.5108 0.5121 -0.0348 0.0676  -0.0473 244 ILE B CD1 
5604  N N   . ALA B 245 ? 0.4160 0.5127 0.5500 -0.0551 0.0684  -0.0615 245 ALA B N   
5605  C CA  . ALA B 245 ? 0.4565 0.5614 0.6058 -0.0641 0.0746  -0.0675 245 ALA B CA  
5606  C C   . ALA B 245 ? 0.4692 0.5594 0.6059 -0.0687 0.0734  -0.0594 245 ALA B C   
5607  O O   . ALA B 245 ? 0.4263 0.5153 0.5625 -0.0792 0.0825  -0.0595 245 ALA B O   
5608  C CB  . ALA B 245 ? 0.4657 0.5871 0.6441 -0.0598 0.0674  -0.0794 245 ALA B CB  
5609  N N   . PHE B 246 ? 0.4730 0.5520 0.5999 -0.0615 0.0622  -0.0531 246 PHE B N   
5610  C CA  . PHE B 246 ? 0.4099 0.4750 0.5249 -0.0651 0.0607  -0.0461 246 PHE B CA  
5611  C C   . PHE B 246 ? 0.4368 0.4877 0.5284 -0.0710 0.0690  -0.0372 246 PHE B C   
5612  O O   . PHE B 246 ? 0.4290 0.4720 0.5148 -0.0793 0.0740  -0.0343 246 PHE B O   
5613  C CB  . PHE B 246 ? 0.4233 0.4795 0.5316 -0.0562 0.0477  -0.0419 246 PHE B CB  
5614  C CG  . PHE B 246 ? 0.4307 0.4723 0.5263 -0.0593 0.0460  -0.0351 246 PHE B CG  
5615  C CD1 . PHE B 246 ? 0.4109 0.4373 0.4842 -0.0597 0.0481  -0.0259 246 PHE B CD1 
5616  C CD2 . PHE B 246 ? 0.4982 0.5418 0.6057 -0.0620 0.0424  -0.0388 246 PHE B CD2 
5617  C CE1 . PHE B 246 ? 0.4403 0.4539 0.5039 -0.0623 0.0462  -0.0210 246 PHE B CE1 
5618  C CE2 . PHE B 246 ? 0.4546 0.4851 0.5515 -0.0649 0.0409  -0.0335 246 PHE B CE2 
5619  C CZ  . PHE B 246 ? 0.5088 0.5244 0.5840 -0.0649 0.0429  -0.0247 246 PHE B CZ  
5620  N N   . MET B 247 ? 0.3885 0.4349 0.4661 -0.0667 0.0699  -0.0330 247 MET B N   
5621  C CA  . MET B 247 ? 0.4355 0.4676 0.4901 -0.0716 0.0766  -0.0249 247 MET B CA  
5622  C C   . MET B 247 ? 0.3874 0.4228 0.4432 -0.0836 0.0897  -0.0277 247 MET B C   
5623  O O   . MET B 247 ? 0.4515 0.4723 0.4899 -0.0908 0.0946  -0.0212 247 MET B O   
5624  C CB  . MET B 247 ? 0.3982 0.4275 0.4405 -0.0650 0.0753  -0.0216 247 MET B CB  
5625  C CG  . MET B 247 ? 0.4772 0.5002 0.5136 -0.0546 0.0636  -0.0174 247 MET B CG  
5626  S SD  . MET B 247 ? 0.4367 0.4458 0.4654 -0.0534 0.0558  -0.0115 247 MET B SD  
5627  C CE  . MET B 247 ? 0.4158 0.4206 0.4356 -0.0424 0.0465  -0.0079 247 MET B CE  
5628  N N   . GLY B 248 ? 0.4135 0.4674 0.4891 -0.0861 0.0955  -0.0377 248 GLY B N   
5629  C CA  . GLY B 248 ? 0.4252 0.4842 0.5037 -0.0986 0.1092  -0.0419 248 GLY B CA  
5630  C C   . GLY B 248 ? 0.4255 0.4811 0.5091 -0.1075 0.1116  -0.0422 248 GLY B C   
5631  O O   . GLY B 248 ? 0.4334 0.4815 0.5062 -0.1192 0.1219  -0.0397 248 GLY B O   
5632  N N   . MET B 249 ? 0.4567 0.5163 0.5554 -0.1026 0.1019  -0.0448 249 MET B N   
5633  C CA  . MET B 249 ? 0.4407 0.4950 0.5427 -0.1104 0.1027  -0.0443 249 MET B CA  
5634  C C   . MET B 249 ? 0.4598 0.4896 0.5341 -0.1133 0.1020  -0.0322 249 MET B C   
5635  O O   . MET B 249 ? 0.5281 0.5489 0.5948 -0.1245 0.1094  -0.0298 249 MET B O   
5636  C CB  . MET B 249 ? 0.4444 0.5065 0.5660 -0.1033 0.0911  -0.0493 249 MET B CB  
5637  C CG  . MET B 249 ? 0.5241 0.5806 0.6503 -0.1096 0.0896  -0.0491 249 MET B CG  
5638  S SD  . MET B 249 ? 0.5188 0.5487 0.6174 -0.1072 0.0825  -0.0359 249 MET B SD  
5639  C CE  . MET B 249 ? 0.5124 0.5453 0.6189 -0.0931 0.0664  -0.0373 249 MET B CE  
5640  N N   . VAL B 250 ? 0.4498 0.4683 0.5085 -0.1035 0.0933  -0.0248 250 VAL B N   
5641  C CA  . VAL B 250 ? 0.5062 0.5019 0.5404 -0.1046 0.0907  -0.0143 250 VAL B CA  
5642  C C   . VAL B 250 ? 0.5043 0.4887 0.5197 -0.1151 0.1017  -0.0099 250 VAL B C   
5643  O O   . VAL B 250 ? 0.5365 0.5055 0.5398 -0.1232 0.1041  -0.0050 250 VAL B O   
5644  C CB  . VAL B 250 ? 0.4684 0.4567 0.4908 -0.0924 0.0808  -0.0088 250 VAL B CB  
5645  C CG1 . VAL B 250 ? 0.5229 0.4882 0.5215 -0.0930 0.0779  0.0009  250 VAL B CG1 
5646  C CG2 . VAL B 250 ? 0.4620 0.4590 0.4996 -0.0831 0.0700  -0.0127 250 VAL B CG2 
5647  N N   . GLU B 251 ? 0.4633 0.4548 0.4758 -0.1157 0.1087  -0.0119 251 GLU B N   
5648  C CA  . GLU B 251 ? 0.4810 0.4612 0.4726 -0.1253 0.1191  -0.0077 251 GLU B CA  
5649  C C   . GLU B 251 ? 0.5467 0.5331 0.5457 -0.1400 0.1321  -0.0131 251 GLU B C   
5650  O O   . GLU B 251 ? 0.6475 0.6230 0.6274 -0.1500 0.1418  -0.0096 251 GLU B O   
5651  C CB  . GLU B 251 ? 0.4648 0.4516 0.4515 -0.1203 0.1217  -0.0090 251 GLU B CB  
5652  C CG  . GLU B 251 ? 0.4306 0.4073 0.4047 -0.1082 0.1105  -0.0023 251 GLU B CG  
5653  C CD  . GLU B 251 ? 0.4740 0.4500 0.4353 -0.1048 0.1131  -0.0009 251 GLU B CD  
5654  O OE1 . GLU B 251 ? 0.4680 0.4610 0.4416 -0.1060 0.1200  -0.0086 251 GLU B OE1 
5655  O OE2 . GLU B 251 ? 0.4597 0.4190 0.4002 -0.1000 0.1071  0.0071  251 GLU B OE2 
5656  N N   . SER B 252 ? 0.4885 0.4924 0.5146 -0.1418 0.1328  -0.0221 252 SER B N   
5657  C CA  . SER B 252 ? 0.5202 0.5306 0.5553 -0.1565 0.1453  -0.0279 252 SER B CA  
5658  C C   . SER B 252 ? 0.5394 0.5342 0.5683 -0.1641 0.1437  -0.0230 252 SER B C   
5659  O O   . SER B 252 ? 0.5766 0.5733 0.6100 -0.1779 0.1543  -0.0267 252 SER B O   
5660  C CB  . SER B 252 ? 0.5170 0.5564 0.5874 -0.1549 0.1473  -0.0420 252 SER B CB  
5661  O OG  . SER B 252 ? 0.5488 0.5921 0.6362 -0.1482 0.1357  -0.0441 252 SER B OG  
5662  N N   . VAL B 253 ? 0.5417 0.5210 0.5605 -0.1559 0.1311  -0.0154 253 VAL B N   
5663  C CA  . VAL B 253 ? 0.5677 0.5318 0.5814 -0.1624 0.1286  -0.0113 253 VAL B CA  
5664  C C   . VAL B 253 ? 0.5658 0.5016 0.5467 -0.1698 0.1313  -0.0003 253 VAL B C   
5665  O O   . VAL B 253 ? 0.6108 0.5315 0.5848 -0.1776 0.1309  0.0033  253 VAL B O   
5666  C CB  . VAL B 253 ? 0.5638 0.5262 0.5857 -0.1506 0.1137  -0.0102 253 VAL B CB  
5667  C CG1 . VAL B 253 ? 0.5840 0.5708 0.6332 -0.1413 0.1088  -0.0196 253 VAL B CG1 
5668  C CG2 . VAL B 253 ? 0.5293 0.4735 0.5283 -0.1410 0.1046  -0.0007 253 VAL B CG2 
5669  N N   . GLY B 254 ? 0.5524 0.4798 0.5125 -0.1683 0.1339  0.0048  254 GLY B N   
5670  C CA  . GLY B 254 ? 0.6000 0.4988 0.5270 -0.1753 0.1355  0.0151  254 GLY B CA  
5671  C C   . GLY B 254 ? 0.5679 0.4526 0.4780 -0.1619 0.1232  0.0228  254 GLY B C   
5672  O O   . GLY B 254 ? 0.5809 0.4421 0.4727 -0.1607 0.1152  0.0308  254 GLY B O   
5673  N N   . ALA B 255 ? 0.5660 0.4657 0.4839 -0.1515 0.1208  0.0196  255 ALA B N   
5674  C CA  . ALA B 255 ? 0.5247 0.4151 0.4310 -0.1383 0.1094  0.0253  255 ALA B CA  
5675  C C   . ALA B 255 ? 0.4979 0.3993 0.4030 -0.1332 0.1125  0.0231  255 ALA B C   
5676  O O   . ALA B 255 ? 0.5030 0.4237 0.4226 -0.1369 0.1216  0.0156  255 ALA B O   
5677  C CB  . ALA B 255 ? 0.5339 0.4327 0.4582 -0.1267 0.0977  0.0228  255 ALA B CB  
5678  N N   . THR B 256 ? 0.4713 0.3622 0.3620 -0.1234 0.1039  0.0286  256 THR B N   
5679  C CA  . THR B 256 ? 0.4681 0.3700 0.3601 -0.1155 0.1038  0.0265  256 THR B CA  
5680  C C   . THR B 256 ? 0.4834 0.3857 0.3799 -0.1013 0.0907  0.0280  256 THR B C   
5681  O O   . THR B 256 ? 0.4836 0.3689 0.3683 -0.0980 0.0824  0.0338  256 THR B O   
5682  C CB  . THR B 256 ? 0.4888 0.3753 0.3537 -0.1200 0.1084  0.0318  256 THR B CB  
5683  O OG1 . THR B 256 ? 0.5560 0.4388 0.4133 -0.1350 0.1212  0.0310  256 THR B OG1 
5684  C CG2 . THR B 256 ? 0.5031 0.4016 0.3701 -0.1118 0.1083  0.0289  256 THR B CG2 
5685  N N   . ILE B 257 ? 0.4246 0.3461 0.3383 -0.0932 0.0888  0.0224  257 ILE B N   
5686  C CA  . ILE B 257 ? 0.4381 0.3603 0.3539 -0.0807 0.0779  0.0237  257 ILE B CA  
5687  C C   . ILE B 257 ? 0.4590 0.3720 0.3562 -0.0769 0.0767  0.0280  257 ILE B C   
5688  O O   . ILE B 257 ? 0.4581 0.3805 0.3562 -0.0770 0.0821  0.0250  257 ILE B O   
5689  C CB  . ILE B 257 ? 0.4633 0.4071 0.4028 -0.0742 0.0757  0.0164  257 ILE B CB  
5690  C CG1 . ILE B 257 ? 0.4430 0.3946 0.4002 -0.0780 0.0759  0.0120  257 ILE B CG1 
5691  C CG2 . ILE B 257 ? 0.4211 0.3641 0.3603 -0.0628 0.0655  0.0181  257 ILE B CG2 
5692  C CD1 . ILE B 257 ? 0.4874 0.4609 0.4685 -0.0746 0.0759  0.0035  257 ILE B CD1 
5693  N N   . VAL B 258 ? 0.4629 0.3571 0.3432 -0.0737 0.0694  0.0344  258 VAL B N   
5694  C CA  . VAL B 258 ? 0.4522 0.3356 0.3134 -0.0709 0.0679  0.0385  258 VAL B CA  
5695  C C   . VAL B 258 ? 0.4577 0.3470 0.3240 -0.0590 0.0595  0.0376  258 VAL B C   
5696  O O   . VAL B 258 ? 0.4501 0.3348 0.3045 -0.0557 0.0583  0.0394  258 VAL B O   
5697  C CB  . VAL B 258 ? 0.4699 0.3270 0.3066 -0.0750 0.0647  0.0459  258 VAL B CB  
5698  C CG1 . VAL B 258 ? 0.5228 0.3723 0.3502 -0.0892 0.0751  0.0472  258 VAL B CG1 
5699  C CG2 . VAL B 258 ? 0.4863 0.3343 0.3256 -0.0698 0.0546  0.0479  258 VAL B CG2 
5700  N N   . ILE B 259 ? 0.4092 0.3083 0.2921 -0.0529 0.0540  0.0346  259 ILE B N   
5701  C CA  . ILE B 259 ? 0.4040 0.3093 0.2924 -0.0427 0.0469  0.0333  259 ILE B CA  
5702  C C   . ILE B 259 ? 0.4256 0.3440 0.3333 -0.0394 0.0440  0.0289  259 ILE B C   
5703  O O   . ILE B 259 ? 0.3725 0.2930 0.2882 -0.0441 0.0460  0.0274  259 ILE B O   
5704  C CB  . ILE B 259 ? 0.4737 0.3618 0.3474 -0.0380 0.0388  0.0379  259 ILE B CB  
5705  C CG1 . ILE B 259 ? 0.3901 0.2841 0.2676 -0.0285 0.0325  0.0363  259 ILE B CG1 
5706  C CG2 . ILE B 259 ? 0.4461 0.3254 0.3214 -0.0385 0.0339  0.0391  259 ILE B CG2 
5707  C CD1 . ILE B 259 ? 0.4218 0.3251 0.2990 -0.0271 0.0364  0.0346  259 ILE B CD1 
5708  N N   . ASP B 260 ? 0.4006 0.3277 0.3153 -0.0319 0.0396  0.0267  260 ASP B N   
5709  C CA  . ASP B 260 ? 0.3937 0.3325 0.3245 -0.0289 0.0368  0.0225  260 ASP B CA  
5710  C C   . ASP B 260 ? 0.3579 0.2972 0.2883 -0.0212 0.0302  0.0224  260 ASP B C   
5711  O O   . ASP B 260 ? 0.3567 0.2917 0.2783 -0.0178 0.0286  0.0243  260 ASP B O   
5712  C CB  . ASP B 260 ? 0.3353 0.2893 0.2786 -0.0302 0.0412  0.0178  260 ASP B CB  
5713  C CG  . ASP B 260 ? 0.4291 0.3877 0.3693 -0.0263 0.0420  0.0171  260 ASP B CG  
5714  O OD1 . ASP B 260 ? 0.4187 0.3813 0.3623 -0.0200 0.0368  0.0161  260 ASP B OD1 
5715  O OD2 . ASP B 260 ? 0.4384 0.3942 0.3700 -0.0296 0.0474  0.0183  260 ASP B OD2 
5716  N N   . ASP B 261 ? 0.3274 0.2718 0.2672 -0.0188 0.0264  0.0198  261 ASP B N   
5717  C CA  . ASP B 261 ? 0.3498 0.2970 0.2912 -0.0127 0.0212  0.0186  261 ASP B CA  
5718  C C   . ASP B 261 ? 0.3300 0.2884 0.2830 -0.0123 0.0206  0.0148  261 ASP B C   
5719  O O   . ASP B 261 ? 0.3018 0.2610 0.2602 -0.0129 0.0181  0.0131  261 ASP B O   
5720  C CB  . ASP B 261 ? 0.3327 0.2722 0.2715 -0.0107 0.0165  0.0190  261 ASP B CB  
5721  C CG  . ASP B 261 ? 0.3289 0.2728 0.2701 -0.0058 0.0126  0.0166  261 ASP B CG  
5722  O OD1 . ASP B 261 ? 0.3758 0.3216 0.3139 -0.0028 0.0124  0.0170  261 ASP B OD1 
5723  O OD2 . ASP B 261 ? 0.3315 0.2770 0.2771 -0.0054 0.0103  0.0143  261 ASP B OD2 
5724  N N   . GLN B 262 ? 0.3113 0.2773 0.2677 -0.0111 0.0221  0.0132  262 GLN B N   
5725  C CA  . GLN B 262 ? 0.3213 0.2965 0.2886 -0.0104 0.0204  0.0094  262 GLN B CA  
5726  C C   . GLN B 262 ? 0.2941 0.2746 0.2619 -0.0072 0.0203  0.0082  262 GLN B C   
5727  O O   . GLN B 262 ? 0.3160 0.2949 0.2775 -0.0070 0.0234  0.0099  262 GLN B O   
5728  C CB  . GLN B 262 ? 0.3357 0.3163 0.3127 -0.0151 0.0238  0.0067  262 GLN B CB  
5729  C CG  . GLN B 262 ? 0.3406 0.3242 0.3172 -0.0183 0.0305  0.0063  262 GLN B CG  
5730  C CD  . GLN B 262 ? 0.3487 0.3324 0.3290 -0.0252 0.0361  0.0055  262 GLN B CD  
5731  O OE1 . GLN B 262 ? 0.3631 0.3409 0.3425 -0.0278 0.0349  0.0069  262 GLN B OE1 
5732  N NE2 . GLN B 262 ? 0.3731 0.3633 0.3573 -0.0288 0.0426  0.0029  262 GLN B NE2 
5733  N N   . CYS B 263 ? 0.2950 0.2806 0.2693 -0.0048 0.0162  0.0055  263 CYS B N   
5734  C CA  . CYS B 263 ? 0.2940 0.2832 0.2686 -0.0014 0.0147  0.0042  263 CYS B CA  
5735  C C   . CYS B 263 ? 0.3340 0.3313 0.3170 -0.0021 0.0182  0.0007  263 CYS B C   
5736  O O   . CYS B 263 ? 0.3168 0.3168 0.2996 0.0007  0.0178  -0.0005 263 CYS B O   
5737  C CB  . CYS B 263 ? 0.2762 0.2648 0.2519 0.0013  0.0080  0.0030  263 CYS B CB  
5738  S SG  . CYS B 263 ? 0.2875 0.2684 0.2507 0.0030  0.0063  0.0065  263 CYS B SG  
5739  N N   . SER B 264 ? 0.2949 0.2967 0.2860 -0.0060 0.0218  -0.0017 264 SER B N   
5740  C CA  . SER B 264 ? 0.3080 0.3180 0.3063 -0.0079 0.0273  -0.0056 264 SER B CA  
5741  C C   . SER B 264 ? 0.3406 0.3461 0.3274 -0.0103 0.0339  -0.0024 264 SER B C   
5742  O O   . SER B 264 ? 0.3310 0.3426 0.3207 -0.0115 0.0390  -0.0055 264 SER B O   
5743  C CB  . SER B 264 ? 0.3384 0.3550 0.3492 -0.0125 0.0304  -0.0098 264 SER B CB  
5744  O OG  . SER B 264 ? 0.3269 0.3363 0.3308 -0.0174 0.0338  -0.0059 264 SER B OG  
5745  N N   . GLY B 265 ? 0.3343 0.3292 0.3081 -0.0107 0.0333  0.0032  265 GLY B N   
5746  C CA  . GLY B 265 ? 0.3623 0.3496 0.3232 -0.0132 0.0380  0.0070  265 GLY B CA  
5747  C C   . GLY B 265 ? 0.3486 0.3271 0.2974 -0.0091 0.0338  0.0112  265 GLY B C   
5748  O O   . GLY B 265 ? 0.3375 0.3185 0.2862 -0.0047 0.0310  0.0103  265 GLY B O   
5749  N N   . SER B 266 ? 0.3533 0.3212 0.2925 -0.0105 0.0331  0.0152  266 SER B N   
5750  C CA  . SER B 266 ? 0.3303 0.2899 0.2584 -0.0068 0.0295  0.0184  266 SER B CA  
5751  C C   . SER B 266 ? 0.3559 0.3189 0.2883 -0.0014 0.0240  0.0171  266 SER B C   
5752  O O   . SER B 266 ? 0.3306 0.2921 0.2579 0.0020  0.0219  0.0176  266 SER B O   
5753  C CB  . SER B 266 ? 0.3476 0.2952 0.2673 -0.0086 0.0280  0.0219  266 SER B CB  
5754  O OG  . SER B 266 ? 0.3558 0.3045 0.2830 -0.0085 0.0251  0.0209  266 SER B OG  
5755  N N   . ARG B 267 ? 0.3240 0.2908 0.2646 -0.0012 0.0214  0.0153  267 ARG B N   
5756  C CA  . ARG B 267 ? 0.3157 0.2836 0.2573 0.0026  0.0167  0.0144  267 ARG B CA  
5757  C C   . ARG B 267 ? 0.3560 0.3295 0.3000 0.0050  0.0160  0.0127  267 ARG B C   
5758  O O   . ARG B 267 ? 0.3578 0.3308 0.2998 0.0076  0.0129  0.0125  267 ARG B O   
5759  C CB  . ARG B 267 ? 0.3180 0.2870 0.2651 0.0017  0.0142  0.0130  267 ARG B CB  
5760  C CG  . ARG B 267 ? 0.3218 0.2888 0.2666 0.0040  0.0105  0.0125  267 ARG B CG  
5761  C CD  . ARG B 267 ? 0.3102 0.2781 0.2587 0.0027  0.0083  0.0108  267 ARG B CD  
5762  N NE  . ARG B 267 ? 0.2801 0.2444 0.2296 0.0005  0.0089  0.0111  267 ARG B NE  
5763  C CZ  . ARG B 267 ? 0.3223 0.2884 0.2773 -0.0021 0.0092  0.0102  267 ARG B CZ  
5764  N NH1 . ARG B 267 ? 0.2807 0.2525 0.2416 -0.0025 0.0086  0.0085  267 ARG B NH1 
5765  N NH2 . ARG B 267 ? 0.2891 0.2510 0.2445 -0.0042 0.0097  0.0106  267 ARG B NH2 
5766  N N   . TYR B 268 ? 0.3009 0.2800 0.2497 0.0040  0.0187  0.0108  268 TYR B N   
5767  C CA  . TYR B 268 ? 0.2967 0.2804 0.2478 0.0069  0.0174  0.0088  268 TYR B CA  
5768  C C   . TYR B 268 ? 0.3312 0.3117 0.2738 0.0088  0.0184  0.0102  268 TYR B C   
5769  O O   . TYR B 268 ? 0.3432 0.3237 0.2844 0.0117  0.0153  0.0099  268 TYR B O   
5770  C CB  . TYR B 268 ? 0.3041 0.2954 0.2643 0.0056  0.0199  0.0051  268 TYR B CB  
5771  C CG  . TYR B 268 ? 0.3248 0.3207 0.2872 0.0085  0.0196  0.0024  268 TYR B CG  
5772  C CD1 . TYR B 268 ? 0.3418 0.3379 0.3064 0.0119  0.0139  0.0012  268 TYR B CD1 
5773  C CD2 . TYR B 268 ? 0.3047 0.3033 0.2655 0.0074  0.0251  0.0009  268 TYR B CD2 
5774  C CE1 . TYR B 268 ? 0.3560 0.3553 0.3228 0.0148  0.0129  -0.0016 268 TYR B CE1 
5775  C CE2 . TYR B 268 ? 0.3489 0.3519 0.3121 0.0103  0.0248  -0.0024 268 TYR B CE2 
5776  C CZ  . TYR B 268 ? 0.3737 0.3770 0.3407 0.0143  0.0183  -0.0036 268 TYR B CZ  
5777  O OH  . TYR B 268 ? 0.3998 0.4065 0.3695 0.0174  0.0171  -0.0071 268 TYR B OH  
5778  N N   . PHE B 269 ? 0.3112 0.2884 0.2474 0.0068  0.0225  0.0118  269 PHE B N   
5779  C CA  . PHE B 269 ? 0.3244 0.2992 0.2527 0.0085  0.0233  0.0124  269 PHE B CA  
5780  C C   . PHE B 269 ? 0.3625 0.3278 0.2799 0.0096  0.0212  0.0157  269 PHE B C   
5781  O O   . PHE B 269 ? 0.3824 0.3448 0.2925 0.0114  0.0208  0.0161  269 PHE B O   
5782  C CB  . PHE B 269 ? 0.3013 0.2786 0.2281 0.0054  0.0296  0.0109  269 PHE B CB  
5783  C CG  . PHE B 269 ? 0.3315 0.3025 0.2515 0.0003  0.0338  0.0136  269 PHE B CG  
5784  C CD1 . PHE B 269 ? 0.3312 0.2913 0.2366 -0.0004 0.0338  0.0173  269 PHE B CD1 
5785  C CD2 . PHE B 269 ? 0.3376 0.3132 0.2657 -0.0039 0.0374  0.0120  269 PHE B CD2 
5786  C CE1 . PHE B 269 ? 0.3589 0.3106 0.2560 -0.0055 0.0371  0.0203  269 PHE B CE1 
5787  C CE2 . PHE B 269 ? 0.3659 0.3349 0.2873 -0.0096 0.0416  0.0145  269 PHE B CE2 
5788  C CZ  . PHE B 269 ? 0.3390 0.2954 0.2442 -0.0105 0.0414  0.0189  269 PHE B CZ  
5789  N N   . TRP B 270 ? 0.3410 0.3011 0.2574 0.0087  0.0194  0.0176  270 TRP B N   
5790  C CA  . TRP B 270 ? 0.3612 0.3107 0.2670 0.0090  0.0177  0.0205  270 TRP B CA  
5791  C C   . TRP B 270 ? 0.3868 0.3329 0.2861 0.0130  0.0143  0.0205  270 TRP B C   
5792  O O   . TRP B 270 ? 0.3889 0.3273 0.2770 0.0126  0.0145  0.0224  270 TRP B O   
5793  C CB  . TRP B 270 ? 0.3061 0.2521 0.2148 0.0094  0.0143  0.0209  270 TRP B CB  
5794  C CG  . TRP B 270 ? 0.3664 0.3001 0.2649 0.0086  0.0126  0.0239  270 TRP B CG  
5795  C CD1 . TRP B 270 ? 0.4087 0.3353 0.3035 0.0123  0.0070  0.0240  270 TRP B CD1 
5796  C CD2 . TRP B 270 ? 0.4123 0.3383 0.3028 0.0038  0.0161  0.0268  270 TRP B CD2 
5797  N NE1 . TRP B 270 ? 0.4652 0.3790 0.3495 0.0107  0.0056  0.0271  270 TRP B NE1 
5798  C CE2 . TRP B 270 ? 0.3879 0.3005 0.2683 0.0050  0.0116  0.0293  270 TRP B CE2 
5799  C CE3 . TRP B 270 ? 0.4207 0.3499 0.3118 -0.0016 0.0227  0.0270  270 TRP B CE3 
5800  C CZ2 . TRP B 270 ? 0.4527 0.3529 0.3215 0.0003  0.0132  0.0330  270 TRP B CZ2 
5801  C CZ3 . TRP B 270 ? 0.4467 0.3657 0.3278 -0.0069 0.0256  0.0301  270 TRP B CZ3 
5802  C CH2 . TRP B 270 ? 0.4552 0.3587 0.3239 -0.0061 0.0208  0.0336  270 TRP B CH2 
5803  N N   . ASN B 271 ? 0.3404 0.2914 0.2459 0.0164  0.0108  0.0183  271 ASN B N   
5804  C CA  . ASN B 271 ? 0.3364 0.2849 0.2379 0.0202  0.0069  0.0175  271 ASN B CA  
5805  C C   . ASN B 271 ? 0.3204 0.2747 0.2233 0.0214  0.0080  0.0157  271 ASN B C   
5806  O O   . ASN B 271 ? 0.3476 0.3090 0.2581 0.0208  0.0093  0.0141  271 ASN B O   
5807  C CB  . ASN B 271 ? 0.3423 0.2921 0.2498 0.0226  0.0027  0.0155  271 ASN B CB  
5808  C CG  . ASN B 271 ? 0.3789 0.3372 0.2958 0.0216  0.0038  0.0133  271 ASN B CG  
5809  O OD1 . ASN B 271 ? 0.3325 0.2938 0.2530 0.0189  0.0064  0.0138  271 ASN B OD1 
5810  N ND2 . ASN B 271 ? 0.3490 0.3105 0.2693 0.0233  0.0016  0.0109  271 ASN B ND2 
5811  N N   . ALA B 272 ? 0.3300 0.2801 0.2247 0.0234  0.0066  0.0160  272 ALA B N   
5812  C CA  . ALA B 272 ? 0.3787 0.3334 0.2750 0.0255  0.0060  0.0137  272 ALA B CA  
5813  C C   . ALA B 272 ? 0.3577 0.3140 0.2590 0.0285  0.0011  0.0116  272 ALA B C   
5814  O O   . ALA B 272 ? 0.3807 0.3336 0.2824 0.0297  -0.0022 0.0115  272 ALA B O   
5815  C CB  . ALA B 272 ? 0.4075 0.3567 0.2922 0.0260  0.0068  0.0143  272 ALA B CB  
5816  N N   . SER B 273 ? 0.3493 0.3106 0.2549 0.0296  0.0004  0.0093  273 SER B N   
5817  C CA  . SER B 273 ? 0.3151 0.2782 0.2255 0.0313  -0.0034 0.0070  273 SER B CA  
5818  C C   . SER B 273 ? 0.3434 0.3014 0.2486 0.0346  -0.0076 0.0062  273 SER B C   
5819  O O   . SER B 273 ? 0.4139 0.3658 0.3093 0.0356  -0.0080 0.0078  273 SER B O   
5820  C CB  . SER B 273 ? 0.3511 0.3185 0.2652 0.0314  -0.0036 0.0050  273 SER B CB  
5821  O OG  . SER B 273 ? 0.3596 0.3250 0.2678 0.0337  -0.0044 0.0044  273 SER B OG  
5822  N N   . LYS B 274 ? 0.3551 0.3153 0.2669 0.0360  -0.0112 0.0032  274 LYS B N   
5823  C CA  . LYS B 274 ? 0.3500 0.3065 0.2599 0.0397  -0.0167 0.0010  274 LYS B CA  
5824  C C   . LYS B 274 ? 0.3678 0.3258 0.2765 0.0412  -0.0183 -0.0009 274 LYS B C   
5825  O O   . LYS B 274 ? 0.3930 0.3564 0.3068 0.0393  -0.0159 -0.0019 274 LYS B O   
5826  C CB  . LYS B 274 ? 0.3872 0.3479 0.3076 0.0403  -0.0192 -0.0031 274 LYS B CB  
5827  C CG  . LYS B 274 ? 0.4134 0.3721 0.3357 0.0399  -0.0191 -0.0026 274 LYS B CG  
5828  C CD  . LYS B 274 ? 0.4695 0.4175 0.3808 0.0420  -0.0220 0.0008  274 LYS B CD  
5829  C CE  . LYS B 274 ? 0.4870 0.4325 0.4015 0.0419  -0.0230 0.0006  274 LYS B CE  
5830  N NZ  . LYS B 274 ? 0.5217 0.4550 0.4238 0.0426  -0.0251 0.0049  274 LYS B NZ  
5831  N N   . PRO B 275 ? 0.4089 0.3613 0.3109 0.0447  -0.0230 -0.0017 275 PRO B N   
5832  C CA  . PRO B 275 ? 0.4004 0.3543 0.3022 0.0464  -0.0252 -0.0042 275 PRO B CA  
5833  C C   . PRO B 275 ? 0.4055 0.3668 0.3204 0.0459  -0.0268 -0.0087 275 PRO B C   
5834  O O   . PRO B 275 ? 0.3753 0.3388 0.2977 0.0463  -0.0287 -0.0113 275 PRO B O   
5835  C CB  . PRO B 275 ? 0.3743 0.3193 0.2657 0.0504  -0.0311 -0.0043 275 PRO B CB  
5836  C CG  . PRO B 275 ? 0.3822 0.3225 0.2737 0.0516  -0.0343 -0.0037 275 PRO B CG  
5837  C CD  . PRO B 275 ? 0.3435 0.2869 0.2382 0.0475  -0.0279 -0.0007 275 PRO B CD  
5838  N N   . GLU B 276 ? 0.3591 0.3245 0.2772 0.0444  -0.0252 -0.0100 276 GLU B N   
5839  C CA  . GLU B 276 ? 0.3694 0.3413 0.2985 0.0415  -0.0245 -0.0134 276 GLU B CA  
5840  C C   . GLU B 276 ? 0.3934 0.3661 0.3221 0.0405  -0.0242 -0.0141 276 GLU B C   
5841  O O   . GLU B 276 ? 0.3957 0.3661 0.3183 0.0405  -0.0222 -0.0114 276 GLU B O   
5842  C CB  . GLU B 276 ? 0.3682 0.3431 0.3013 0.0374  -0.0198 -0.0117 276 GLU B CB  
5843  C CG  . GLU B 276 ? 0.3926 0.3720 0.3324 0.0328  -0.0174 -0.0137 276 GLU B CG  
5844  C CD  . GLU B 276 ? 0.4171 0.4013 0.3662 0.0321  -0.0192 -0.0194 276 GLU B CD  
5845  O OE1 . GLU B 276 ? 0.3982 0.3843 0.3521 0.0344  -0.0213 -0.0223 276 GLU B OE1 
5846  O OE2 . GLU B 276 ? 0.4392 0.4253 0.3913 0.0291  -0.0188 -0.0216 276 GLU B OE2 
5847  N N   . GLY B 277 ? 0.3537 0.3296 0.2895 0.0398  -0.0266 -0.0184 277 GLY B N   
5848  C CA  . GLY B 277 ? 0.3338 0.3091 0.2689 0.0392  -0.0275 -0.0195 277 GLY B CA  
5849  C C   . GLY B 277 ? 0.3777 0.3536 0.3147 0.0341  -0.0241 -0.0182 277 GLY B C   
5850  O O   . GLY B 277 ? 0.3714 0.3446 0.3054 0.0341  -0.0249 -0.0177 277 GLY B O   
5851  N N   . ASP B 278 ? 0.3506 0.3289 0.2916 0.0299  -0.0209 -0.0178 278 ASP B N   
5852  C CA  . ASP B 278 ? 0.3361 0.3128 0.2763 0.0245  -0.0181 -0.0160 278 ASP B CA  
5853  C C   . ASP B 278 ? 0.3596 0.3338 0.2945 0.0254  -0.0163 -0.0116 278 ASP B C   
5854  O O   . ASP B 278 ? 0.3162 0.2920 0.2517 0.0247  -0.0139 -0.0103 278 ASP B O   
5855  C CB  . ASP B 278 ? 0.3515 0.3318 0.2974 0.0189  -0.0152 -0.0184 278 ASP B CB  
5856  C CG  . ASP B 278 ? 0.3752 0.3514 0.3173 0.0125  -0.0128 -0.0163 278 ASP B CG  
5857  O OD1 . ASP B 278 ? 0.3522 0.3232 0.2880 0.0131  -0.0133 -0.0122 278 ASP B OD1 
5858  O OD2 . ASP B 278 ? 0.3971 0.3747 0.3421 0.0065  -0.0104 -0.0189 278 ASP B OD2 
5859  N N   . VAL B 279 ? 0.3231 0.2938 0.2538 0.0269  -0.0174 -0.0099 279 VAL B N   
5860  C CA  . VAL B 279 ? 0.3302 0.3002 0.2579 0.0284  -0.0158 -0.0070 279 VAL B CA  
5861  C C   . VAL B 279 ? 0.3404 0.3095 0.2684 0.0242  -0.0137 -0.0048 279 VAL B C   
5862  O O   . VAL B 279 ? 0.3440 0.3142 0.2715 0.0248  -0.0118 -0.0029 279 VAL B O   
5863  C CB  . VAL B 279 ? 0.3369 0.3048 0.2623 0.0311  -0.0174 -0.0071 279 VAL B CB  
5864  C CG1 . VAL B 279 ? 0.3198 0.2834 0.2455 0.0286  -0.0199 -0.0073 279 VAL B CG1 
5865  C CG2 . VAL B 279 ? 0.3530 0.3223 0.2771 0.0330  -0.0150 -0.0055 279 VAL B CG2 
5866  N N   . ILE B 280 ? 0.2873 0.2537 0.2151 0.0195  -0.0141 -0.0051 280 ILE B N   
5867  C CA  . ILE B 280 ? 0.3064 0.2707 0.2323 0.0151  -0.0123 -0.0032 280 ILE B CA  
5868  C C   . ILE B 280 ? 0.3125 0.2817 0.2414 0.0142  -0.0089 -0.0038 280 ILE B C   
5869  O O   . ILE B 280 ? 0.3326 0.3017 0.2604 0.0135  -0.0074 -0.0019 280 ILE B O   
5870  C CB  . ILE B 280 ? 0.3373 0.2960 0.2597 0.0091  -0.0130 -0.0033 280 ILE B CB  
5871  C CG1 . ILE B 280 ? 0.3354 0.2875 0.2545 0.0106  -0.0176 -0.0024 280 ILE B CG1 
5872  C CG2 . ILE B 280 ? 0.3379 0.2935 0.2561 0.0037  -0.0109 -0.0016 280 ILE B CG2 
5873  C CD1 . ILE B 280 ? 0.3510 0.2997 0.2680 0.0129  -0.0200 -0.0002 280 ILE B CD1 
5874  N N   . LYS B 281 ? 0.3058 0.2792 0.2392 0.0143  -0.0083 -0.0070 281 LYS B N   
5875  C CA  . LYS B 281 ? 0.3335 0.3114 0.2710 0.0147  -0.0063 -0.0086 281 LYS B CA  
5876  C C   . LYS B 281 ? 0.3421 0.3198 0.2781 0.0196  -0.0069 -0.0062 281 LYS B C   
5877  O O   . LYS B 281 ? 0.3469 0.3253 0.2833 0.0191  -0.0051 -0.0053 281 LYS B O   
5878  C CB  . LYS B 281 ? 0.3508 0.3336 0.2953 0.0154  -0.0070 -0.0136 281 LYS B CB  
5879  C CG  . LYS B 281 ? 0.3606 0.3483 0.3113 0.0167  -0.0061 -0.0167 281 LYS B CG  
5880  C CD  . LYS B 281 ? 0.3939 0.3871 0.3537 0.0172  -0.0076 -0.0230 281 LYS B CD  
5881  C CE  . LYS B 281 ? 0.4726 0.4711 0.4407 0.0190  -0.0077 -0.0277 281 LYS B CE  
5882  N NZ  . LYS B 281 ? 0.4952 0.4896 0.4599 0.0259  -0.0121 -0.0251 281 LYS B NZ  
5883  N N   . ALA B 282 ? 0.2926 0.2689 0.2261 0.0239  -0.0090 -0.0054 282 ALA B N   
5884  C CA  . ALA B 282 ? 0.2964 0.2715 0.2265 0.0273  -0.0088 -0.0031 282 ALA B CA  
5885  C C   . ALA B 282 ? 0.3764 0.3507 0.3051 0.0255  -0.0064 -0.0002 282 ALA B C   
5886  O O   . ALA B 282 ? 0.3550 0.3291 0.2832 0.0257  -0.0049 0.0013  282 ALA B O   
5887  C CB  . ALA B 282 ? 0.3216 0.2949 0.2476 0.0309  -0.0105 -0.0030 282 ALA B CB  
5888  N N   . ILE B 283 ? 0.3316 0.3048 0.2598 0.0240  -0.0067 0.0004  283 ILE B N   
5889  C CA  . ILE B 283 ? 0.3300 0.3024 0.2579 0.0226  -0.0058 0.0024  283 ILE B CA  
5890  C C   . ILE B 283 ? 0.3386 0.3108 0.2672 0.0190  -0.0044 0.0029  283 ILE B C   
5891  O O   . ILE B 283 ? 0.3385 0.3114 0.2676 0.0189  -0.0029 0.0041  283 ILE B O   
5892  C CB  . ILE B 283 ? 0.3401 0.3100 0.2675 0.0225  -0.0082 0.0022  283 ILE B CB  
5893  C CG1 . ILE B 283 ? 0.3320 0.3029 0.2594 0.0263  -0.0091 0.0009  283 ILE B CG1 
5894  C CG2 . ILE B 283 ? 0.3246 0.2936 0.2528 0.0214  -0.0086 0.0035  283 ILE B CG2 
5895  C CD1 . ILE B 283 ? 0.3162 0.2838 0.2438 0.0266  -0.0129 -0.0003 283 ILE B CD1 
5896  N N   . ALA B 284 ? 0.3011 0.2723 0.2293 0.0155  -0.0046 0.0016  284 ALA B N   
5897  C CA  . ALA B 284 ? 0.2947 0.2654 0.2222 0.0114  -0.0027 0.0015  284 ALA B CA  
5898  C C   . ALA B 284 ? 0.3299 0.3042 0.2609 0.0128  -0.0007 0.0005  284 ALA B C   
5899  O O   . ALA B 284 ? 0.3402 0.3142 0.2709 0.0114  0.0006  0.0013  284 ALA B O   
5900  C CB  . ALA B 284 ? 0.3393 0.3085 0.2651 0.0065  -0.0020 -0.0004 284 ALA B CB  
5901  N N   . GLU B 285 ? 0.3025 0.2793 0.2365 0.0156  -0.0012 -0.0015 285 GLU B N   
5902  C CA  . GLU B 285 ? 0.3040 0.2826 0.2412 0.0173  -0.0007 -0.0028 285 GLU B CA  
5903  C C   . GLU B 285 ? 0.3394 0.3156 0.2741 0.0199  -0.0009 0.0003  285 GLU B C   
5904  O O   . GLU B 285 ? 0.3228 0.2987 0.2590 0.0201  -0.0005 -0.0001 285 GLU B O   
5905  C CB  . GLU B 285 ? 0.3032 0.2843 0.2447 0.0200  -0.0026 -0.0064 285 GLU B CB  
5906  C CG  . GLU B 285 ? 0.3252 0.3100 0.2708 0.0162  -0.0012 -0.0105 285 GLU B CG  
5907  C CD  . GLU B 285 ? 0.4090 0.3984 0.3623 0.0181  -0.0028 -0.0159 285 GLU B CD  
5908  O OE1 . GLU B 285 ? 0.4350 0.4233 0.3892 0.0233  -0.0065 -0.0163 285 GLU B OE1 
5909  O OE2 . GLU B 285 ? 0.3630 0.3568 0.3213 0.0138  -0.0003 -0.0203 285 GLU B OE2 
5910  N N   . ARG B 286 ? 0.3221 0.2966 0.2535 0.0217  -0.0015 0.0026  286 ARG B N   
5911  C CA  . ARG B 286 ? 0.3248 0.2974 0.2536 0.0227  -0.0004 0.0053  286 ARG B CA  
5912  C C   . ARG B 286 ? 0.3164 0.2892 0.2468 0.0199  0.0013  0.0063  286 ARG B C   
5913  O O   . ARG B 286 ? 0.3248 0.2960 0.2548 0.0199  0.0021  0.0074  286 ARG B O   
5914  C CB  . ARG B 286 ? 0.3228 0.2953 0.2491 0.0240  0.0000  0.0064  286 ARG B CB  
5915  C CG  . ARG B 286 ? 0.3228 0.2938 0.2462 0.0241  0.0023  0.0084  286 ARG B CG  
5916  C CD  . ARG B 286 ? 0.3341 0.3074 0.2612 0.0218  0.0041  0.0089  286 ARG B CD  
5917  N NE  . ARG B 286 ? 0.3179 0.2900 0.2434 0.0206  0.0069  0.0105  286 ARG B NE  
5918  C CZ  . ARG B 286 ? 0.3044 0.2787 0.2339 0.0185  0.0086  0.0106  286 ARG B CZ  
5919  N NH1 . ARG B 286 ? 0.3038 0.2807 0.2385 0.0178  0.0069  0.0094  286 ARG B NH1 
5920  N NH2 . ARG B 286 ? 0.3142 0.2869 0.2419 0.0167  0.0116  0.0119  286 ARG B NH2 
5921  N N   . TYR B 287 ? 0.2928 0.2664 0.2240 0.0174  0.0011  0.0060  287 TYR B N   
5922  C CA  . TYR B 287 ? 0.2973 0.2703 0.2292 0.0149  0.0018  0.0067  287 TYR B CA  
5923  C C   . TYR B 287 ? 0.3284 0.3015 0.2612 0.0131  0.0027  0.0051  287 TYR B C   
5924  O O   . TYR B 287 ? 0.3220 0.2944 0.2556 0.0123  0.0034  0.0057  287 TYR B O   
5925  C CB  . TYR B 287 ? 0.3417 0.3133 0.2723 0.0130  0.0000  0.0070  287 TYR B CB  
5926  C CG  . TYR B 287 ? 0.3225 0.2949 0.2545 0.0154  -0.0010 0.0075  287 TYR B CG  
5927  C CD1 . TYR B 287 ? 0.2916 0.2656 0.2268 0.0158  -0.0005 0.0079  287 TYR B CD1 
5928  C CD2 . TYR B 287 ? 0.3292 0.3016 0.2605 0.0172  -0.0023 0.0068  287 TYR B CD2 
5929  C CE1 . TYR B 287 ? 0.3255 0.3019 0.2638 0.0178  -0.0009 0.0070  287 TYR B CE1 
5930  C CE2 . TYR B 287 ? 0.3484 0.3223 0.2817 0.0196  -0.0030 0.0062  287 TYR B CE2 
5931  C CZ  . TYR B 287 ? 0.3177 0.2941 0.2550 0.0199  -0.0021 0.0060  287 TYR B CZ  
5932  O OH  . TYR B 287 ? 0.3252 0.3046 0.2663 0.0220  -0.0020 0.0041  287 TYR B OH  
5933  N N   . CYS B 288 ? 0.2924 0.2670 0.2260 0.0123  0.0029  0.0024  288 CYS B N   
5934  C CA  . CYS B 288 ? 0.3185 0.2947 0.2547 0.0108  0.0043  -0.0006 288 CYS B CA  
5935  C C   . CYS B 288 ? 0.3332 0.3089 0.2721 0.0142  0.0034  -0.0009 288 CYS B C   
5936  O O   . CYS B 288 ? 0.3202 0.2963 0.2615 0.0136  0.0040  -0.0029 288 CYS B O   
5937  C CB  . CYS B 288 ? 0.3041 0.2834 0.2427 0.0091  0.0052  -0.0047 288 CYS B CB  
5938  S SG  . CYS B 288 ? 0.3563 0.3333 0.2890 0.0033  0.0064  -0.0043 288 CYS B SG  
5939  N N   . ASP B 289 ? 0.3016 0.2758 0.2394 0.0178  0.0017  0.0006  289 ASP B N   
5940  C CA  . ASP B 289 ? 0.3118 0.2829 0.2498 0.0210  -0.0002 0.0006  289 ASP B CA  
5941  C C   . ASP B 289 ? 0.3270 0.2937 0.2612 0.0206  0.0005  0.0045  289 ASP B C   
5942  O O   . ASP B 289 ? 0.3600 0.3218 0.2924 0.0224  -0.0012 0.0052  289 ASP B O   
5943  C CB  . ASP B 289 ? 0.3601 0.3298 0.2965 0.0245  -0.0030 0.0003  289 ASP B CB  
5944  C CG  . ASP B 289 ? 0.3748 0.3491 0.3172 0.0253  -0.0043 -0.0049 289 ASP B CG  
5945  O OD1 . ASP B 289 ? 0.4020 0.3804 0.3501 0.0233  -0.0028 -0.0087 289 ASP B OD1 
5946  O OD2 . ASP B 289 ? 0.3602 0.3343 0.3019 0.0279  -0.0068 -0.0056 289 ASP B OD2 
5947  N N   . ARG B 290 ? 0.3288 0.2967 0.2618 0.0183  0.0025  0.0067  290 ARG B N   
5948  C CA  . ARG B 290 ? 0.3411 0.3064 0.2721 0.0171  0.0040  0.0096  290 ARG B CA  
5949  C C   . ARG B 290 ? 0.3260 0.2892 0.2589 0.0158  0.0040  0.0092  290 ARG B C   
5950  O O   . ARG B 290 ? 0.3206 0.2859 0.2566 0.0149  0.0037  0.0065  290 ARG B O   
5951  C CB  . ARG B 290 ? 0.3231 0.2917 0.2556 0.0153  0.0053  0.0103  290 ARG B CB  
5952  C CG  . ARG B 290 ? 0.3198 0.2881 0.2525 0.0139  0.0075  0.0121  290 ARG B CG  
5953  C CD  . ARG B 290 ? 0.3168 0.2888 0.2539 0.0123  0.0074  0.0113  290 ARG B CD  
5954  N NE  . ARG B 290 ? 0.3049 0.2761 0.2442 0.0102  0.0066  0.0108  290 ARG B NE  
5955  C CZ  . ARG B 290 ? 0.3047 0.2777 0.2474 0.0088  0.0054  0.0100  290 ARG B CZ  
5956  N NH1 . ARG B 290 ? 0.3276 0.3034 0.2730 0.0096  0.0045  0.0093  290 ARG B NH1 
5957  N NH2 . ARG B 290 ? 0.3083 0.2800 0.2519 0.0070  0.0046  0.0095  290 ARG B NH2 
5958  N N   . PRO B 291 ? 0.3563 0.3151 0.2868 0.0151  0.0046  0.0115  291 PRO B N   
5959  C CA  . PRO B 291 ? 0.3101 0.2669 0.2430 0.0134  0.0045  0.0109  291 PRO B CA  
5960  C C   . PRO B 291 ? 0.3335 0.2952 0.2702 0.0110  0.0054  0.0095  291 PRO B C   
5961  O O   . PRO B 291 ? 0.3621 0.3267 0.2996 0.0098  0.0063  0.0103  291 PRO B O   
5962  C CB  . PRO B 291 ? 0.3356 0.2875 0.2652 0.0115  0.0060  0.0141  291 PRO B CB  
5963  C CG  . PRO B 291 ? 0.4063 0.3558 0.3300 0.0126  0.0068  0.0162  291 PRO B CG  
5964  C CD  . PRO B 291 ? 0.3609 0.3159 0.2860 0.0148  0.0060  0.0145  291 PRO B CD  
5965  N N   . ALA B 292 ? 0.3042 0.2661 0.2429 0.0105  0.0047  0.0068  292 ALA B N   
5966  C CA  . ALA B 292 ? 0.3082 0.2731 0.2477 0.0081  0.0050  0.0051  292 ALA B CA  
5967  C C   . ALA B 292 ? 0.3252 0.2893 0.2659 0.0057  0.0049  0.0060  292 ALA B C   
5968  O O   . ALA B 292 ? 0.3347 0.2960 0.2768 0.0053  0.0049  0.0062  292 ALA B O   
5969  C CB  . ALA B 292 ? 0.3080 0.2740 0.2486 0.0078  0.0051  0.0009  292 ALA B CB  
5970  N N   . CYS B 293 ? 0.3185 0.2843 0.2586 0.0041  0.0042  0.0061  293 CYS B N   
5971  C CA  . CYS B 293 ? 0.3051 0.2700 0.2459 0.0019  0.0027  0.0055  293 CYS B CA  
5972  C C   . CYS B 293 ? 0.2998 0.2629 0.2392 0.0006  0.0029  0.0029  293 CYS B C   
5973  O O   . CYS B 293 ? 0.3117 0.2754 0.2491 0.0007  0.0040  0.0008  293 CYS B O   
5974  C CB  . CYS B 293 ? 0.3049 0.2696 0.2425 0.0007  0.0003  0.0053  293 CYS B CB  
5975  S SG  . CYS B 293 ? 0.3652 0.3276 0.3029 -0.0014 -0.0035 0.0044  293 CYS B SG  
5976  N N   . PRO B 294 ? 0.3045 0.2659 0.2458 -0.0008 0.0020  0.0023  294 PRO B N   
5977  C CA  . PRO B 294 ? 0.2824 0.2420 0.2220 -0.0021 0.0021  -0.0010 294 PRO B CA  
5978  C C   . PRO B 294 ? 0.3165 0.2761 0.2497 -0.0042 0.0024  -0.0033 294 PRO B C   
5979  O O   . PRO B 294 ? 0.3447 0.3050 0.2767 -0.0049 0.0044  -0.0069 294 PRO B O   
5980  C CB  . PRO B 294 ? 0.3020 0.2596 0.2437 -0.0037 0.0001  -0.0010 294 PRO B CB  
5981  C CG  . PRO B 294 ? 0.3096 0.2682 0.2565 -0.0029 0.0006  0.0019  294 PRO B CG  
5982  C CD  . PRO B 294 ? 0.2926 0.2541 0.2385 -0.0014 0.0014  0.0038  294 PRO B CD  
5983  N N   . THR B 295 ? 0.2717 0.2301 0.2007 -0.0055 0.0005  -0.0016 295 THR B N   
5984  C CA  . THR B 295 ? 0.2823 0.2383 0.2025 -0.0085 0.0007  -0.0028 295 THR B CA  
5985  C C   . THR B 295 ? 0.3422 0.3012 0.2620 -0.0085 0.0042  -0.0044 295 THR B C   
5986  O O   . THR B 295 ? 0.3113 0.2693 0.2247 -0.0121 0.0064  -0.0071 295 THR B O   
5987  C CB  . THR B 295 ? 0.3215 0.2743 0.2376 -0.0089 -0.0033 -0.0001 295 THR B CB  
5988  O OG1 . THR B 295 ? 0.3929 0.3428 0.3091 -0.0095 -0.0073 -0.0001 295 THR B OG1 
5989  C CG2 . THR B 295 ? 0.3750 0.3228 0.2795 -0.0126 -0.0035 -0.0003 295 THR B CG2 
5990  N N   . LYS B 296 ? 0.2867 0.2490 0.2124 -0.0051 0.0049  -0.0029 296 LYS B N   
5991  C CA  . LYS B 296 ? 0.2868 0.2523 0.2135 -0.0045 0.0073  -0.0046 296 LYS B CA  
5992  C C   . LYS B 296 ? 0.3226 0.2912 0.2560 -0.0020 0.0088  -0.0080 296 LYS B C   
5993  O O   . LYS B 296 ? 0.3004 0.2723 0.2371 -0.0003 0.0099  -0.0099 296 LYS B O   
5994  C CB  . LYS B 296 ? 0.3043 0.2704 0.2318 -0.0023 0.0060  -0.0013 296 LYS B CB  
5995  C CG  . LYS B 296 ? 0.3129 0.2753 0.2344 -0.0042 0.0035  0.0011  296 LYS B CG  
5996  C CD  . LYS B 296 ? 0.2745 0.2380 0.1968 -0.0022 0.0028  0.0028  296 LYS B CD  
5997  C CE  . LYS B 296 ? 0.3030 0.2621 0.2207 -0.0030 -0.0011 0.0050  296 LYS B CE  
5998  N NZ  . LYS B 296 ? 0.3115 0.2647 0.2191 -0.0076 -0.0017 0.0046  296 LYS B NZ  
5999  N N   . ASP B 297 ? 0.3239 0.2912 0.2595 -0.0016 0.0083  -0.0093 297 ASP B N   
6000  C CA  . ASP B 297 ? 0.3096 0.2779 0.2517 0.0017  0.0080  -0.0120 297 ASP B CA  
6001  C C   . ASP B 297 ? 0.3124 0.2826 0.2561 0.0001  0.0099  -0.0184 297 ASP B C   
6002  O O   . ASP B 297 ? 0.3125 0.2802 0.2566 -0.0002 0.0091  -0.0197 297 ASP B O   
6003  C CB  . ASP B 297 ? 0.3009 0.2651 0.2447 0.0037  0.0057  -0.0083 297 ASP B CB  
6004  C CG  . ASP B 297 ? 0.3380 0.3003 0.2859 0.0078  0.0040  -0.0089 297 ASP B CG  
6005  O OD1 . ASP B 297 ? 0.3175 0.2823 0.2672 0.0101  0.0039  -0.0105 297 ASP B OD1 
6006  O OD2 . ASP B 297 ? 0.3214 0.2789 0.2705 0.0087  0.0022  -0.0082 297 ASP B OD2 
6007  N N   . TYR B 298 ? 0.3008 0.2758 0.2453 -0.0014 0.0128  -0.0230 298 TYR B N   
6008  C CA  . TYR B 298 ? 0.2859 0.2647 0.2329 -0.0034 0.0159  -0.0306 298 TYR B CA  
6009  C C   . TYR B 298 ? 0.3058 0.2915 0.2582 -0.0034 0.0186  -0.0357 298 TYR B C   
6010  O O   . TYR B 298 ? 0.2787 0.2648 0.2288 -0.0040 0.0187  -0.0324 298 TYR B O   
6011  C CB  . TYR B 298 ? 0.2776 0.2540 0.2149 -0.0094 0.0184  -0.0312 298 TYR B CB  
6012  C CG  . TYR B 298 ? 0.2741 0.2489 0.2018 -0.0142 0.0202  -0.0285 298 TYR B CG  
6013  C CD1 . TYR B 298 ? 0.3161 0.2951 0.2420 -0.0187 0.0253  -0.0336 298 TYR B CD1 
6014  C CD2 . TYR B 298 ? 0.2933 0.2624 0.2146 -0.0143 0.0167  -0.0213 298 TYR B CD2 
6015  C CE1 . TYR B 298 ? 0.2936 0.2690 0.2089 -0.0238 0.0267  -0.0305 298 TYR B CE1 
6016  C CE2 . TYR B 298 ? 0.2863 0.2519 0.1978 -0.0185 0.0172  -0.0188 298 TYR B CE2 
6017  C CZ  . TYR B 298 ? 0.3293 0.2974 0.2374 -0.0232 0.0220  -0.0230 298 TYR B CZ  
6018  O OH  . TYR B 298 ? 0.3122 0.2751 0.2091 -0.0283 0.0226  -0.0205 298 TYR B OH  
6019  N N   . PRO B 299 ? 0.2872 0.2787 0.2477 -0.0028 0.0207  -0.0443 299 PRO B N   
6020  C CA  . PRO B 299 ? 0.2670 0.2586 0.2317 -0.0016 0.0204  -0.0496 299 PRO B CA  
6021  C C   . PRO B 299 ? 0.3189 0.3052 0.2887 0.0049  0.0142  -0.0469 299 PRO B C   
6022  O O   . PRO B 299 ? 0.3007 0.2836 0.2705 0.0053  0.0129  -0.0481 299 PRO B O   
6023  C CB  . PRO B 299 ? 0.2951 0.2964 0.2701 -0.0019 0.0242  -0.0606 299 PRO B CB  
6024  C CG  . PRO B 299 ? 0.2907 0.2961 0.2711 0.0003  0.0233  -0.0602 299 PRO B CG  
6025  C CD  . PRO B 299 ? 0.3189 0.3187 0.2868 -0.0033 0.0237  -0.0507 299 PRO B CD  
6026  N N   . ALA B 300 ? 0.3134 0.2984 0.2869 0.0095  0.0104  -0.0438 300 ALA B N   
6027  C CA  . ALA B 300 ? 0.3045 0.2821 0.2802 0.0148  0.0044  -0.0408 300 ALA B CA  
6028  C C   . ALA B 300 ? 0.3240 0.2940 0.2909 0.0133  0.0032  -0.0315 300 ALA B C   
6029  O O   . ALA B 300 ? 0.3253 0.2956 0.2863 0.0108  0.0049  -0.0263 300 ALA B O   
6030  C CB  . ALA B 300 ? 0.3216 0.2992 0.3026 0.0201  0.0003  -0.0414 300 ALA B CB  
6031  N N   . HIS B 301 ? 0.3139 0.2770 0.2808 0.0150  -0.0001 -0.0299 301 HIS B N   
6032  C CA  . HIS B 301 ? 0.3109 0.2671 0.2715 0.0137  -0.0013 -0.0218 301 HIS B CA  
6033  C C   . HIS B 301 ? 0.3240 0.2750 0.2831 0.0171  -0.0046 -0.0173 301 HIS B C   
6034  O O   . HIS B 301 ? 0.3177 0.2600 0.2755 0.0190  -0.0083 -0.0151 301 HIS B O   
6035  C CB  . HIS B 301 ? 0.3346 0.2849 0.2954 0.0131  -0.0032 -0.0219 301 HIS B CB  
6036  C CG  . HIS B 301 ? 0.3672 0.3205 0.3268 0.0092  -0.0005 -0.0247 301 HIS B CG  
6037  N ND1 . HIS B 301 ? 0.3508 0.3052 0.3048 0.0051  0.0016  -0.0208 301 HIS B ND1 
6038  C CD2 . HIS B 301 ? 0.3414 0.2954 0.3039 0.0089  -0.0003 -0.0310 301 HIS B CD2 
6039  C CE1 . HIS B 301 ? 0.3881 0.3432 0.3406 0.0024  0.0026  -0.0243 301 HIS B CE1 
6040  N NE2 . HIS B 301 ? 0.3652 0.3204 0.3225 0.0044  0.0020  -0.0306 301 HIS B NE2 
6041  N N   . THR B 302 ? 0.3086 0.2634 0.2663 0.0176  -0.0034 -0.0157 302 THR B N   
6042  C CA  . THR B 302 ? 0.3174 0.2665 0.2718 0.0205  -0.0065 -0.0115 302 THR B CA  
6043  C C   . THR B 302 ? 0.3351 0.2775 0.2826 0.0182  -0.0061 -0.0044 302 THR B C   
6044  O O   . THR B 302 ? 0.3822 0.3166 0.3249 0.0199  -0.0087 -0.0008 302 THR B O   
6045  C CB  . THR B 302 ? 0.3506 0.3053 0.3046 0.0211  -0.0052 -0.0112 302 THR B CB  
6046  O OG1 . THR B 302 ? 0.3612 0.3189 0.3111 0.0172  -0.0015 -0.0072 302 THR B OG1 
6047  C CG2 . THR B 302 ? 0.3571 0.3202 0.3186 0.0220  -0.0043 -0.0187 302 THR B CG2 
6048  N N   . ARG B 303 ? 0.3241 0.2693 0.2709 0.0142  -0.0028 -0.0027 303 ARG B N   
6049  C CA  . ARG B 303 ? 0.3351 0.2761 0.2780 0.0113  -0.0017 0.0026  303 ARG B CA  
6050  C C   . ARG B 303 ? 0.3594 0.2905 0.3005 0.0115  -0.0043 0.0039  303 ARG B C   
6051  O O   . ARG B 303 ? 0.3577 0.2823 0.2934 0.0099  -0.0040 0.0086  303 ARG B O   
6052  C CB  . ARG B 303 ? 0.3539 0.2999 0.2986 0.0077  0.0008  0.0024  303 ARG B CB  
6053  C CG  . ARG B 303 ? 0.3823 0.3260 0.3261 0.0045  0.0022  0.0064  303 ARG B CG  
6054  C CD  . ARG B 303 ? 0.3037 0.2533 0.2501 0.0019  0.0032  0.0054  303 ARG B CD  
6055  N NE  . ARG B 303 ? 0.3594 0.3084 0.3077 -0.0010 0.0044  0.0078  303 ARG B NE  
6056  C CZ  . ARG B 303 ? 0.3547 0.3029 0.3063 -0.0036 0.0038  0.0067  303 ARG B CZ  
6057  N NH1 . ARG B 303 ? 0.3411 0.2893 0.2933 -0.0036 0.0019  0.0035  303 ARG B NH1 
6058  N NH2 . ARG B 303 ? 0.3415 0.2893 0.2958 -0.0065 0.0054  0.0085  303 ARG B NH2 
6059  N N   . PHE B 304 ? 0.3515 0.2806 0.2963 0.0131  -0.0068 -0.0004 304 PHE B N   
6060  C CA  . PHE B 304 ? 0.3358 0.2539 0.2786 0.0132  -0.0102 0.0008  304 PHE B CA  
6061  C C   . PHE B 304 ? 0.3640 0.2719 0.3002 0.0159  -0.0140 0.0040  304 PHE B C   
6062  O O   . PHE B 304 ? 0.4140 0.3107 0.3434 0.0138  -0.0152 0.0084  304 PHE B O   
6063  C CB  . PHE B 304 ? 0.3695 0.2875 0.3185 0.0155  -0.0130 -0.0056 304 PHE B CB  
6064  C CG  . PHE B 304 ? 0.3769 0.3019 0.3297 0.0124  -0.0099 -0.0087 304 PHE B CG  
6065  C CD1 . PHE B 304 ? 0.3488 0.2796 0.3001 0.0084  -0.0060 -0.0058 304 PHE B CD1 
6066  C CD2 . PHE B 304 ? 0.3890 0.3140 0.3467 0.0137  -0.0116 -0.0149 304 PHE B CD2 
6067  C CE1 . PHE B 304 ? 0.4018 0.3374 0.3550 0.0058  -0.0043 -0.0086 304 PHE B CE1 
6068  C CE2 . PHE B 304 ? 0.4164 0.3467 0.3756 0.0105  -0.0090 -0.0178 304 PHE B CE2 
6069  C CZ  . PHE B 304 ? 0.4234 0.3584 0.3797 0.0065  -0.0057 -0.0142 304 PHE B CZ  
6070  N N   . ASP B 305 ? 0.3827 0.2930 0.3203 0.0204  -0.0165 0.0013  305 ASP B N   
6071  C CA  . ASP B 305 ? 0.3929 0.2921 0.3228 0.0233  -0.0213 0.0043  305 ASP B CA  
6072  C C   . ASP B 305 ? 0.4205 0.3178 0.3411 0.0199  -0.0177 0.0108  305 ASP B C   
6073  O O   . ASP B 305 ? 0.4081 0.2925 0.3179 0.0192  -0.0201 0.0155  305 ASP B O   
6074  C CB  . ASP B 305 ? 0.4571 0.3601 0.3923 0.0293  -0.0256 -0.0011 305 ASP B CB  
6075  C CG  . ASP B 305 ? 0.5534 0.4599 0.4995 0.0330  -0.0290 -0.0093 305 ASP B CG  
6076  O OD1 . ASP B 305 ? 0.5240 0.4213 0.4698 0.0338  -0.0328 -0.0100 305 ASP B OD1 
6077  O OD2 . ASP B 305 ? 0.5501 0.4688 0.5053 0.0347  -0.0272 -0.0155 305 ASP B OD2 
6078  N N   . HIS B 306 ? 0.3572 0.2663 0.2810 0.0178  -0.0122 0.0109  306 HIS B N   
6079  C CA  . HIS B 306 ? 0.3721 0.2815 0.2892 0.0147  -0.0082 0.0158  306 HIS B CA  
6080  C C   . HIS B 306 ? 0.4101 0.3134 0.3224 0.0092  -0.0050 0.0199  306 HIS B C   
6081  O O   . HIS B 306 ? 0.4190 0.3138 0.3213 0.0068  -0.0040 0.0243  306 HIS B O   
6082  C CB  . HIS B 306 ? 0.3412 0.2644 0.2644 0.0139  -0.0038 0.0141  306 HIS B CB  
6083  C CG  . HIS B 306 ? 0.3636 0.2890 0.2828 0.0108  0.0006  0.0177  306 HIS B CG  
6084  N ND1 . HIS B 306 ? 0.3840 0.3052 0.2952 0.0118  0.0004  0.0202  306 HIS B ND1 
6085  C CD2 . HIS B 306 ? 0.3547 0.2865 0.2772 0.0070  0.0050  0.0184  306 HIS B CD2 
6086  C CE1 . HIS B 306 ? 0.4302 0.3557 0.3403 0.0086  0.0052  0.0219  306 HIS B CE1 
6087  N NE2 . HIS B 306 ? 0.3670 0.2993 0.2847 0.0059  0.0079  0.0207  306 HIS B NE2 
6088  N N   . VAL B 307 ? 0.3574 0.2642 0.2763 0.0067  -0.0035 0.0183  307 VAL B N   
6089  C CA  . VAL B 307 ? 0.3857 0.2880 0.3023 0.0009  -0.0004 0.0213  307 VAL B CA  
6090  C C   . VAL B 307 ? 0.4100 0.2957 0.3171 -0.0001 -0.0039 0.0244  307 VAL B C   
6091  O O   . VAL B 307 ? 0.4127 0.2907 0.3110 -0.0050 -0.0009 0.0288  307 VAL B O   
6092  C CB  . VAL B 307 ? 0.3655 0.2754 0.2918 -0.0010 0.0010  0.0183  307 VAL B CB  
6093  C CG1 . VAL B 307 ? 0.4064 0.3116 0.3319 -0.0072 0.0038  0.0206  307 VAL B CG1 
6094  C CG2 . VAL B 307 ? 0.3414 0.2646 0.2739 -0.0012 0.0041  0.0165  307 VAL B CG2 
6095  N N   . LEU B 308 ? 0.3657 0.2445 0.2738 0.0042  -0.0102 0.0219  308 LEU B N   
6096  C CA  . LEU B 308 ? 0.4105 0.2708 0.3082 0.0038  -0.0152 0.0249  308 LEU B CA  
6097  C C   . LEU B 308 ? 0.4351 0.2853 0.3194 0.0045  -0.0171 0.0291  308 LEU B C   
6098  O O   . LEU B 308 ? 0.4566 0.2917 0.3276 0.0002  -0.0173 0.0342  308 LEU B O   
6099  C CB  . LEU B 308 ? 0.4094 0.2656 0.3127 0.0094  -0.0226 0.0201  308 LEU B CB  
6100  C CG  . LEU B 308 ? 0.4651 0.3003 0.3578 0.0097  -0.0295 0.0229  308 LEU B CG  
6101  C CD1 . LEU B 308 ? 0.4991 0.3263 0.3863 0.0016  -0.0255 0.0274  308 LEU B CD1 
6102  C CD2 . LEU B 308 ? 0.4691 0.3013 0.3695 0.0165  -0.0376 0.0166  308 LEU B CD2 
6103  N N   . GLY B 309 ? 0.4477 0.3054 0.3340 0.0093  -0.0182 0.0271  309 GLY B N   
6104  C CA  . GLY B 309 ? 0.4607 0.3090 0.3337 0.0103  -0.0203 0.0307  309 GLY B CA  
6105  C C   . GLY B 309 ? 0.4396 0.2866 0.3029 0.0031  -0.0127 0.0358  309 GLY B C   
6106  O O   . GLY B 309 ? 0.4836 0.3150 0.3307 0.0002  -0.0138 0.0406  309 GLY B O   
6107  N N   . MET B 310 ? 0.4346 0.2975 0.3074 0.0001  -0.0051 0.0344  310 MET B N   
6108  C CA  . MET B 310 ? 0.4556 0.3199 0.3230 -0.0071 0.0029  0.0375  310 MET B CA  
6109  C C   . MET B 310 ? 0.4691 0.3210 0.3290 -0.0141 0.0048  0.0410  310 MET B C   
6110  O O   . MET B 310 ? 0.4752 0.3174 0.3213 -0.0199 0.0086  0.0450  310 MET B O   
6111  C CB  . MET B 310 ? 0.4685 0.3521 0.3505 -0.0078 0.0086  0.0340  310 MET B CB  
6112  C CG  . MET B 310 ? 0.4665 0.3589 0.3489 -0.0046 0.0099  0.0329  310 MET B CG  
6113  S SD  . MET B 310 ? 0.4562 0.3681 0.3529 -0.0058 0.0158  0.0293  310 MET B SD  
6114  C CE  . MET B 310 ? 0.3873 0.3047 0.2969 -0.0056 0.0138  0.0263  310 MET B CE  
6115  N N   . ALA B 311 ? 0.4449 0.2962 0.3128 -0.0143 0.0026  0.0392  311 ALA B N   
6116  C CA  . ALA B 311 ? 0.4641 0.3032 0.3256 -0.0212 0.0041  0.0423  311 ALA B CA  
6117  C C   . ALA B 311 ? 0.4956 0.3115 0.3374 -0.0222 -0.0011 0.0473  311 ALA B C   
6118  O O   . ALA B 311 ? 0.5004 0.3045 0.3299 -0.0302 0.0028  0.0516  311 ALA B O   
6119  C CB  . ALA B 311 ? 0.4843 0.3253 0.3573 -0.0198 0.0007  0.0390  311 ALA B CB  
6120  N N   . LYS B 312 ? 0.4981 0.3062 0.3366 -0.0143 -0.0104 0.0464  312 LYS B N   
6121  C CA  . LYS B 312 ? 0.5021 0.2861 0.3210 -0.0142 -0.0175 0.0510  312 LYS B CA  
6122  C C   . LYS B 312 ? 0.5340 0.3116 0.3358 -0.0175 -0.0141 0.0553  312 LYS B C   
6123  O O   . LYS B 312 ? 0.5819 0.3399 0.3637 -0.0238 -0.0139 0.0610  312 LYS B O   
6124  C CB  . LYS B 312 ? 0.5256 0.3052 0.3488 -0.0038 -0.0292 0.0473  312 LYS B CB  
6125  C CG  . LYS B 312 ? 0.5463 0.3265 0.3822 -0.0011 -0.0337 0.0432  312 LYS B CG  
6126  C CD  . LYS B 312 ? 0.5998 0.3612 0.4251 -0.0078 -0.0346 0.0475  312 LYS B CD  
6127  C CE  . LYS B 312 ? 0.5623 0.3244 0.4011 -0.0038 -0.0403 0.0424  312 LYS B CE  
6128  N NZ  . LYS B 312 ? 0.6250 0.3633 0.4520 -0.0069 -0.0463 0.0458  312 LYS B NZ  
6129  N N   . GLU B 313 ? 0.5231 0.3167 0.3319 -0.0140 -0.0110 0.0527  313 GLU B N   
6130  C CA  . GLU B 313 ? 0.5474 0.3367 0.3413 -0.0158 -0.0083 0.0557  313 GLU B CA  
6131  C C   . GLU B 313 ? 0.5214 0.3105 0.3069 -0.0268 0.0031  0.0588  313 GLU B C   
6132  O O   . GLU B 313 ? 0.5778 0.3546 0.3435 -0.0313 0.0054  0.0628  313 GLU B O   
6133  C CB  . GLU B 313 ? 0.5165 0.3251 0.3234 -0.0092 -0.0076 0.0511  313 GLU B CB  
6134  C CG  . GLU B 313 ? 0.5740 0.3795 0.3676 -0.0090 -0.0066 0.0528  313 GLU B CG  
6135  C CD  . GLU B 313 ? 0.6459 0.4727 0.4544 -0.0044 -0.0036 0.0481  313 GLU B CD  
6136  O OE1 . GLU B 313 ? 0.7063 0.5360 0.5078 -0.0062 0.0009  0.0488  313 GLU B OE1 
6137  O OE2 . GLU B 313 ? 0.7194 0.5601 0.5463 0.0005  -0.0055 0.0436  313 GLU B OE2 
6138  N N   . TYR B 314 ? 0.5343 0.3372 0.3346 -0.0314 0.0105  0.0564  314 TYR B N   
6139  C CA  . TYR B 314 ? 0.5446 0.3500 0.3409 -0.0421 0.0218  0.0578  314 TYR B CA  
6140  C C   . TYR B 314 ? 0.5573 0.3484 0.3471 -0.0501 0.0229  0.0609  314 TYR B C   
6141  O O   . TYR B 314 ? 0.5550 0.3503 0.3456 -0.0598 0.0328  0.0609  314 TYR B O   
6142  C CB  . TYR B 314 ? 0.4768 0.3085 0.2952 -0.0420 0.0293  0.0521  314 TYR B CB  
6143  C CG  . TYR B 314 ? 0.4741 0.3179 0.2954 -0.0368 0.0304  0.0496  314 TYR B CG  
6144  C CD1 . TYR B 314 ? 0.4521 0.3012 0.2804 -0.0269 0.0227  0.0475  314 TYR B CD1 
6145  C CD2 . TYR B 314 ? 0.4992 0.3481 0.3152 -0.0421 0.0392  0.0492  314 TYR B CD2 
6146  C CE1 . TYR B 314 ? 0.4840 0.3433 0.3145 -0.0227 0.0237  0.0453  314 TYR B CE1 
6147  C CE2 . TYR B 314 ? 0.4919 0.3501 0.3094 -0.0375 0.0397  0.0469  314 TYR B CE2 
6148  C CZ  . TYR B 314 ? 0.4679 0.3306 0.2921 -0.0279 0.0318  0.0453  314 TYR B CZ  
6149  O OH  . TYR B 314 ? 0.4969 0.3691 0.3231 -0.0239 0.0327  0.0429  314 TYR B OH  
6150  N N   . ASN B 315 ? 0.4992 0.2726 0.2819 -0.0467 0.0129  0.0633  315 ASN B N   
6151  C CA  . ASN B 315 ? 0.5787 0.3346 0.3521 -0.0546 0.0128  0.0670  315 ASN B CA  
6152  C C   . ASN B 315 ? 0.5505 0.3217 0.3426 -0.0601 0.0203  0.0634  315 ASN B C   
6153  O O   . ASN B 315 ? 0.5782 0.3445 0.3648 -0.0710 0.0280  0.0654  315 ASN B O   
6154  C CB  . ASN B 315 ? 0.5993 0.3344 0.3455 -0.0645 0.0171  0.0733  315 ASN B CB  
6155  C CG  . ASN B 315 ? 0.7672 0.4765 0.4908 -0.0597 0.0053  0.0781  315 ASN B CG  
6156  O OD1 . ASN B 315 ? 0.8227 0.5193 0.5463 -0.0540 -0.0059 0.0785  315 ASN B OD1 
6157  N ND2 . ASN B 315 ? 0.8427 0.5442 0.5474 -0.0615 0.0071  0.0811  315 ASN B ND2 
6158  N N   . VAL B 316 ? 0.5163 0.3054 0.3304 -0.0527 0.0175  0.0580  316 VAL B N   
6159  C CA  . VAL B 316 ? 0.4835 0.2875 0.3158 -0.0568 0.0232  0.0541  316 VAL B CA  
6160  C C   . VAL B 316 ? 0.5435 0.3330 0.3736 -0.0607 0.0194  0.0557  316 VAL B C   
6161  O O   . VAL B 316 ? 0.5462 0.3220 0.3713 -0.0548 0.0095  0.0567  316 VAL B O   
6162  C CB  . VAL B 316 ? 0.4835 0.3089 0.3367 -0.0480 0.0209  0.0481  316 VAL B CB  
6163  C CG1 . VAL B 316 ? 0.4991 0.3353 0.3690 -0.0506 0.0231  0.0443  316 VAL B CG1 
6164  C CG2 . VAL B 316 ? 0.4587 0.2993 0.3152 -0.0469 0.0267  0.0464  316 VAL B CG2 
6165  N N   . GLU B 317 ? 0.4940 0.2869 0.3291 -0.0704 0.0272  0.0551  317 GLU B N   
6166  C CA  . GLU B 317 ? 0.5090 0.2893 0.3439 -0.0748 0.0241  0.0561  317 GLU B CA  
6167  C C   . GLU B 317 ? 0.5760 0.3729 0.4339 -0.0716 0.0230  0.0500  317 GLU B C   
6168  O O   . GLU B 317 ? 0.5556 0.3430 0.4153 -0.0701 0.0164  0.0496  317 GLU B O   
6169  C CB  . GLU B 317 ? 0.5639 0.3334 0.3871 -0.0889 0.0329  0.0597  317 GLU B CB  
6170  C CG  . GLU B 317 ? 0.6331 0.3803 0.4281 -0.0924 0.0325  0.0666  317 GLU B CG  
6171  C CD  . GLU B 317 ? 0.6885 0.4271 0.4692 -0.1075 0.0438  0.0700  317 GLU B CD  
6172  O OE1 . GLU B 317 ? 0.6250 0.3802 0.4199 -0.1154 0.0545  0.0659  317 GLU B OE1 
6173  O OE2 . GLU B 317 ? 0.8050 0.5182 0.5589 -0.1119 0.0417  0.0767  317 GLU B OE2 
6174  N N   . GLY B 318 ? 0.5042 0.3245 0.3790 -0.0705 0.0285  0.0451  318 GLY B N   
6175  C CA  . GLY B 318 ? 0.4676 0.3032 0.3626 -0.0675 0.0270  0.0393  318 GLY B CA  
6176  C C   . GLY B 318 ? 0.4178 0.2747 0.3257 -0.0614 0.0285  0.0350  318 GLY B C   
6177  O O   . GLY B 318 ? 0.4756 0.3408 0.3829 -0.0637 0.0349  0.0350  318 GLY B O   
6178  N N   . ALA B 319 ? 0.4027 0.2682 0.3217 -0.0539 0.0229  0.0310  319 ALA B N   
6179  C CA  . ALA B 319 ? 0.3814 0.2645 0.3106 -0.0478 0.0230  0.0273  319 ALA B CA  
6180  C C   . ALA B 319 ? 0.3982 0.2953 0.3441 -0.0489 0.0237  0.0221  319 ALA B C   
6181  O O   . ALA B 319 ? 0.4235 0.3172 0.3738 -0.0488 0.0197  0.0203  319 ALA B O   
6182  C CB  . ALA B 319 ? 0.4037 0.2849 0.3303 -0.0384 0.0157  0.0267  319 ALA B CB  
6183  N N   . ILE B 320 ? 0.3690 0.2813 0.3244 -0.0495 0.0280  0.0192  320 ILE B N   
6184  C CA  . ILE B 320 ? 0.3690 0.2948 0.3406 -0.0503 0.0279  0.0138  320 ILE B CA  
6185  C C   . ILE B 320 ? 0.3752 0.3111 0.3519 -0.0423 0.0235  0.0111  320 ILE B C   
6186  O O   . ILE B 320 ? 0.3685 0.3116 0.3452 -0.0400 0.0257  0.0110  320 ILE B O   
6187  C CB  . ILE B 320 ? 0.4232 0.3585 0.4034 -0.0573 0.0355  0.0114  320 ILE B CB  
6188  C CG1 . ILE B 320 ? 0.4462 0.3705 0.4197 -0.0669 0.0411  0.0143  320 ILE B CG1 
6189  C CG2 . ILE B 320 ? 0.3879 0.3374 0.3867 -0.0572 0.0338  0.0049  320 ILE B CG2 
6190  C CD1 . ILE B 320 ? 0.4562 0.3907 0.4380 -0.0751 0.0504  0.0111  320 ILE B CD1 
6191  N N   . PHE B 321 ? 0.3481 0.2846 0.3290 -0.0388 0.0177  0.0085  321 PHE B N   
6192  C CA  . PHE B 321 ? 0.3410 0.2859 0.3257 -0.0329 0.0137  0.0058  321 PHE B CA  
6193  C C   . PHE B 321 ? 0.3733 0.3300 0.3713 -0.0347 0.0138  0.0013  321 PHE B C   
6194  O O   . PHE B 321 ? 0.3440 0.3016 0.3499 -0.0379 0.0126  -0.0015 321 PHE B O   
6195  C CB  . PHE B 321 ? 0.3701 0.3103 0.3523 -0.0293 0.0078  0.0043  321 PHE B CB  
6196  C CG  . PHE B 321 ? 0.3571 0.2881 0.3288 -0.0259 0.0064  0.0069  321 PHE B CG  
6197  C CD1 . PHE B 321 ? 0.3928 0.3121 0.3595 -0.0279 0.0060  0.0089  321 PHE B CD1 
6198  C CD2 . PHE B 321 ? 0.3357 0.2693 0.3031 -0.0208 0.0052  0.0069  321 PHE B CD2 
6199  C CE1 . PHE B 321 ? 0.3960 0.3066 0.3543 -0.0240 0.0034  0.0104  321 PHE B CE1 
6200  C CE2 . PHE B 321 ? 0.3423 0.2686 0.3022 -0.0174 0.0036  0.0082  321 PHE B CE2 
6201  C CZ  . PHE B 321 ? 0.4378 0.3527 0.3938 -0.0187 0.0022  0.0097  321 PHE B CZ  
6202  N N   . LEU B 322 ? 0.3514 0.3169 0.3528 -0.0322 0.0147  0.0002  322 LEU B N   
6203  C CA  . LEU B 322 ? 0.3273 0.3037 0.3419 -0.0321 0.0128  -0.0049 322 LEU B CA  
6204  C C   . LEU B 322 ? 0.3902 0.3672 0.4021 -0.0262 0.0059  -0.0059 322 LEU B C   
6205  O O   . LEU B 322 ? 0.3739 0.3501 0.3783 -0.0225 0.0057  -0.0038 322 LEU B O   
6206  C CB  . LEU B 322 ? 0.3491 0.3344 0.3695 -0.0332 0.0179  -0.0063 322 LEU B CB  
6207  C CG  . LEU B 322 ? 0.3618 0.3443 0.3796 -0.0399 0.0263  -0.0041 322 LEU B CG  
6208  C CD1 . LEU B 322 ? 0.4896 0.4815 0.5126 -0.0411 0.0319  -0.0063 322 LEU B CD1 
6209  C CD2 . LEU B 322 ? 0.3920 0.3755 0.4197 -0.0460 0.0273  -0.0071 322 LEU B CD2 
6210  N N   A GLN B 323 ? 0.3618 0.3390 0.3781 -0.0257 0.0003  -0.0091 323 GLN B N   
6211  N N   B GLN B 323 ? 0.3616 0.3388 0.3780 -0.0258 0.0003  -0.0091 323 GLN B N   
6212  C CA  A GLN B 323 ? 0.3729 0.3480 0.3829 -0.0212 -0.0060 -0.0096 323 GLN B CA  
6213  C CA  B GLN B 323 ? 0.3729 0.3480 0.3831 -0.0212 -0.0060 -0.0097 323 GLN B CA  
6214  C C   A GLN B 323 ? 0.3520 0.3330 0.3708 -0.0196 -0.0120 -0.0141 323 GLN B C   
6215  C C   B GLN B 323 ? 0.3513 0.3327 0.3706 -0.0196 -0.0119 -0.0141 323 GLN B C   
6216  O O   A GLN B 323 ? 0.3610 0.3455 0.3906 -0.0218 -0.0143 -0.0180 323 GLN B O   
6217  O O   B GLN B 323 ? 0.3601 0.3454 0.3905 -0.0218 -0.0140 -0.0181 323 GLN B O   
6218  C CB  A GLN B 323 ? 0.3809 0.3478 0.3833 -0.0212 -0.0087 -0.0093 323 GLN B CB  
6219  C CB  B GLN B 323 ? 0.3802 0.3474 0.3835 -0.0214 -0.0089 -0.0096 323 GLN B CB  
6220  C CG  A GLN B 323 ? 0.4215 0.3850 0.4132 -0.0174 -0.0125 -0.0089 323 GLN B CG  
6221  C CG  B GLN B 323 ? 0.4226 0.3860 0.4146 -0.0176 -0.0120 -0.0087 323 GLN B CG  
6222  C CD  A GLN B 323 ? 0.4088 0.3665 0.3906 -0.0164 -0.0097 -0.0064 323 GLN B CD  
6223  C CD  B GLN B 323 ? 0.3751 0.3330 0.3621 -0.0178 -0.0163 -0.0109 323 GLN B CD  
6224  O OE1 A GLN B 323 ? 0.4369 0.3950 0.4156 -0.0152 -0.0061 -0.0036 323 GLN B OE1 
6225  O OE1 B GLN B 323 ? 0.4038 0.3565 0.3861 -0.0182 -0.0146 -0.0104 323 GLN B OE1 
6226  N NE2 A GLN B 323 ? 0.3665 0.3190 0.3437 -0.0166 -0.0117 -0.0080 323 GLN B NE2 
6227  N NE2 B GLN B 323 ? 0.4150 0.3733 0.4027 -0.0172 -0.0224 -0.0138 323 GLN B NE2 
6228  N N   . GLN B 324 ? 0.3372 0.3187 0.3514 -0.0157 -0.0153 -0.0137 324 GLN B N   
6229  C CA  . GLN B 324 ? 0.3440 0.3277 0.3632 -0.0133 -0.0234 -0.0176 324 GLN B CA  
6230  C C   . GLN B 324 ? 0.3590 0.3351 0.3709 -0.0134 -0.0295 -0.0184 324 GLN B C   
6231  O O   . GLN B 324 ? 0.3458 0.3149 0.3448 -0.0135 -0.0281 -0.0156 324 GLN B O   
6232  C CB  . GLN B 324 ? 0.2962 0.2791 0.3092 -0.0094 -0.0260 -0.0163 324 GLN B CB  
6233  C CG  . GLN B 324 ? 0.3822 0.3729 0.4026 -0.0086 -0.0209 -0.0165 324 GLN B CG  
6234  C CD  . GLN B 324 ? 0.4246 0.4251 0.4631 -0.0086 -0.0231 -0.0225 324 GLN B CD  
6235  O OE1 . GLN B 324 ? 0.4490 0.4498 0.4919 -0.0055 -0.0317 -0.0262 324 GLN B OE1 
6236  N NE2 . GLN B 324 ? 0.4384 0.4465 0.4875 -0.0123 -0.0156 -0.0242 324 GLN B NE2 
6237  N N   . LYS B 325 ? 0.3144 0.2925 0.3353 -0.0135 -0.0361 -0.0231 325 LYS B N   
6238  C CA  . LYS B 325 ? 0.3590 0.3291 0.3714 -0.0131 -0.0434 -0.0243 325 LYS B CA  
6239  C C   . LYS B 325 ? 0.3715 0.3333 0.3663 -0.0108 -0.0466 -0.0214 325 LYS B C   
6240  O O   . LYS B 325 ? 0.3255 0.2883 0.3193 -0.0083 -0.0482 -0.0205 325 LYS B O   
6241  C CB  . LYS B 325 ? 0.3952 0.3684 0.4195 -0.0121 -0.0522 -0.0300 325 LYS B CB  
6242  C CG  . LYS B 325 ? 0.4832 0.4602 0.5199 -0.0155 -0.0515 -0.0336 325 LYS B CG  
6243  C CD  . LYS B 325 ? 0.5338 0.5159 0.5854 -0.0139 -0.0608 -0.0403 325 LYS B CD  
6244  C CE  . LYS B 325 ? 0.5925 0.5635 0.6309 -0.0114 -0.0722 -0.0412 325 LYS B CE  
6245  N NZ  . LYS B 325 ? 0.5763 0.5431 0.6141 -0.0140 -0.0751 -0.0436 325 LYS B NZ  
6246  N N   . PHE B 326 ? 0.3594 0.3129 0.3406 -0.0121 -0.0470 -0.0204 326 PHE B N   
6247  C CA  . PHE B 326 ? 0.3384 0.2830 0.3013 -0.0116 -0.0493 -0.0183 326 PHE B CA  
6248  C C   . PHE B 326 ? 0.3837 0.3288 0.3395 -0.0112 -0.0425 -0.0144 326 PHE B C   
6249  O O   . PHE B 326 ? 0.3999 0.3383 0.3414 -0.0113 -0.0442 -0.0129 326 PHE B O   
6250  C CB  . PHE B 326 ? 0.3473 0.2870 0.3062 -0.0095 -0.0595 -0.0196 326 PHE B CB  
6251  C CG  . PHE B 326 ? 0.3791 0.3177 0.3448 -0.0094 -0.0680 -0.0241 326 PHE B CG  
6252  C CD1 . PHE B 326 ? 0.3798 0.3125 0.3380 -0.0117 -0.0694 -0.0256 326 PHE B CD1 
6253  C CD2 . PHE B 326 ? 0.4141 0.3577 0.3941 -0.0067 -0.0749 -0.0276 326 PHE B CD2 
6254  C CE1 . PHE B 326 ? 0.4516 0.3828 0.4157 -0.0116 -0.0778 -0.0301 326 PHE B CE1 
6255  C CE2 . PHE B 326 ? 0.4311 0.3738 0.4181 -0.0062 -0.0837 -0.0325 326 PHE B CE2 
6256  C CZ  . PHE B 326 ? 0.4810 0.4173 0.4600 -0.0088 -0.0853 -0.0335 326 PHE B CZ  
6257  N N   . CYS B 327 ? 0.3136 0.2657 0.2781 -0.0111 -0.0352 -0.0128 327 CYS B N   
6258  C CA  . CYS B 327 ? 0.3302 0.2834 0.2898 -0.0101 -0.0298 -0.0096 327 CYS B CA  
6259  C C   . CYS B 327 ? 0.3040 0.2527 0.2525 -0.0114 -0.0257 -0.0087 327 CYS B C   
6260  O O   . CYS B 327 ? 0.3560 0.3061 0.3078 -0.0120 -0.0209 -0.0086 327 CYS B O   
6261  C CB  . CYS B 327 ? 0.3113 0.2721 0.2826 -0.0097 -0.0242 -0.0085 327 CYS B CB  
6262  S SG  . CYS B 327 ? 0.3151 0.2770 0.2810 -0.0082 -0.0182 -0.0048 327 CYS B SG  
6263  N N   . ASP B 328 ? 0.3340 0.2765 0.2689 -0.0122 -0.0278 -0.0087 328 ASP B N   
6264  C CA  . ASP B 328 ? 0.3451 0.2847 0.2707 -0.0139 -0.0235 -0.0094 328 ASP B CA  
6265  C C   . ASP B 328 ? 0.3291 0.2732 0.2577 -0.0128 -0.0168 -0.0081 328 ASP B C   
6266  O O   . ASP B 328 ? 0.3141 0.2584 0.2436 -0.0131 -0.0135 -0.0100 328 ASP B O   
6267  C CB  . ASP B 328 ? 0.3819 0.3139 0.2913 -0.0163 -0.0259 -0.0097 328 ASP B CB  
6268  C CG  . ASP B 328 ? 0.3827 0.3080 0.2864 -0.0175 -0.0334 -0.0114 328 ASP B CG  
6269  O OD1 . ASP B 328 ? 0.3970 0.3209 0.3008 -0.0187 -0.0340 -0.0142 328 ASP B OD1 
6270  O OD2 . ASP B 328 ? 0.4430 0.3646 0.3442 -0.0166 -0.0398 -0.0102 328 ASP B OD2 
6271  N N   . PRO B 329 ? 0.3235 0.2704 0.2535 -0.0112 -0.0151 -0.0055 329 PRO B N   
6272  C CA  . PRO B 329 ? 0.3138 0.2639 0.2456 -0.0100 -0.0096 -0.0049 329 PRO B CA  
6273  C C   . PRO B 329 ? 0.3495 0.3018 0.2902 -0.0089 -0.0074 -0.0048 329 PRO B C   
6274  O O   . PRO B 329 ? 0.3403 0.2921 0.2809 -0.0083 -0.0047 -0.0061 329 PRO B O   
6275  C CB  . PRO B 329 ? 0.3218 0.2743 0.2540 -0.0084 -0.0094 -0.0021 329 PRO B CB  
6276  C CG  . PRO B 329 ? 0.3282 0.2768 0.2546 -0.0094 -0.0144 -0.0020 329 PRO B CG  
6277  C CD  . PRO B 329 ? 0.3283 0.2752 0.2578 -0.0101 -0.0186 -0.0037 329 PRO B CD  
6278  N N   . HIS B 330 ? 0.2866 0.2406 0.2350 -0.0089 -0.0089 -0.0037 330 HIS B N   
6279  C CA  . HIS B 330 ? 0.3433 0.2976 0.2981 -0.0090 -0.0064 -0.0030 330 HIS B CA  
6280  C C   . HIS B 330 ? 0.3037 0.2543 0.2591 -0.0105 -0.0077 -0.0056 330 HIS B C   
6281  O O   . HIS B 330 ? 0.3452 0.2934 0.3027 -0.0103 -0.0060 -0.0054 330 HIS B O   
6282  C CB  . HIS B 330 ? 0.3355 0.2935 0.2981 -0.0095 -0.0060 -0.0015 330 HIS B CB  
6283  C CG  . HIS B 330 ? 0.3103 0.2715 0.2724 -0.0078 -0.0038 0.0008  330 HIS B CG  
6284  N ND1 . HIS B 330 ? 0.3184 0.2797 0.2812 -0.0074 0.0001  0.0031  330 HIS B ND1 
6285  C CD2 . HIS B 330 ? 0.2820 0.2450 0.2413 -0.0063 -0.0053 0.0010  330 HIS B CD2 
6286  C CE1 . HIS B 330 ? 0.2837 0.2479 0.2451 -0.0057 0.0011  0.0043  330 HIS B CE1 
6287  N NE2 . HIS B 330 ? 0.3059 0.2713 0.2658 -0.0049 -0.0022 0.0031  330 HIS B NE2 
6288  N N   . GLU B 331 ? 0.3162 0.2656 0.2699 -0.0118 -0.0115 -0.0079 331 GLU B N   
6289  C CA  . GLU B 331 ? 0.3269 0.2726 0.2797 -0.0132 -0.0132 -0.0111 331 GLU B CA  
6290  C C   . GLU B 331 ? 0.3595 0.3029 0.3063 -0.0124 -0.0107 -0.0133 331 GLU B C   
6291  O O   . GLU B 331 ? 0.3360 0.2768 0.2849 -0.0124 -0.0105 -0.0157 331 GLU B O   
6292  C CB  . GLU B 331 ? 0.3216 0.2653 0.2706 -0.0145 -0.0183 -0.0132 331 GLU B CB  
6293  C CG  . GLU B 331 ? 0.3114 0.2575 0.2698 -0.0152 -0.0220 -0.0134 331 GLU B CG  
6294  C CD  . GLU B 331 ? 0.3315 0.2747 0.2856 -0.0157 -0.0288 -0.0156 331 GLU B CD  
6295  O OE1 . GLU B 331 ? 0.3765 0.3154 0.3186 -0.0157 -0.0308 -0.0155 331 GLU B OE1 
6296  O OE2 . GLU B 331 ? 0.3717 0.3164 0.3345 -0.0164 -0.0327 -0.0175 331 GLU B OE2 
6297  N N   . GLY B 332 ? 0.3188 0.2635 0.2591 -0.0119 -0.0090 -0.0133 332 GLY B N   
6298  C CA  . GLY B 332 ? 0.3490 0.2936 0.2856 -0.0114 -0.0060 -0.0167 332 GLY B CA  
6299  C C   . GLY B 332 ? 0.3571 0.3024 0.3002 -0.0086 -0.0040 -0.0165 332 GLY B C   
6300  O O   . GLY B 332 ? 0.3658 0.3101 0.3101 -0.0076 -0.0033 -0.0207 332 GLY B O   
6301  N N   . ASP B 333 ? 0.3342 0.2805 0.2811 -0.0072 -0.0035 -0.0121 333 ASP B N   
6302  C CA  . ASP B 333 ? 0.3145 0.2590 0.2651 -0.0047 -0.0027 -0.0110 333 ASP B CA  
6303  C C   . ASP B 333 ? 0.3608 0.2999 0.3153 -0.0054 -0.0043 -0.0101 333 ASP B C   
6304  O O   . ASP B 333 ? 0.3502 0.2846 0.3059 -0.0034 -0.0050 -0.0103 333 ASP B O   
6305  C CB  . ASP B 333 ? 0.3322 0.2786 0.2828 -0.0036 -0.0013 -0.0064 333 ASP B CB  
6306  C CG  . ASP B 333 ? 0.3656 0.3157 0.3134 -0.0019 0.0003  -0.0074 333 ASP B CG  
6307  O OD1 . ASP B 333 ? 0.3763 0.3283 0.3219 -0.0023 0.0010  -0.0116 333 ASP B OD1 
6308  O OD2 . ASP B 333 ? 0.3883 0.3398 0.3361 -0.0006 0.0011  -0.0041 333 ASP B OD2 
6309  N N   . TYR B 334 ? 0.3349 0.2738 0.2914 -0.0082 -0.0055 -0.0092 334 TYR B N   
6310  C CA  . TYR B 334 ? 0.3235 0.2581 0.2842 -0.0101 -0.0060 -0.0071 334 TYR B CA  
6311  C C   . TYR B 334 ? 0.3242 0.2517 0.2855 -0.0094 -0.0077 -0.0095 334 TYR B C   
6312  O O   . TYR B 334 ? 0.3447 0.2658 0.3062 -0.0096 -0.0078 -0.0067 334 TYR B O   
6313  C CB  . TYR B 334 ? 0.3611 0.2985 0.3260 -0.0133 -0.0071 -0.0072 334 TYR B CB  
6314  C CG  . TYR B 334 ? 0.3600 0.2931 0.3299 -0.0163 -0.0074 -0.0066 334 TYR B CG  
6315  C CD1 . TYR B 334 ? 0.3629 0.2941 0.3344 -0.0183 -0.0045 -0.0026 334 TYR B CD1 
6316  C CD2 . TYR B 334 ? 0.3219 0.2516 0.2938 -0.0177 -0.0103 -0.0100 334 TYR B CD2 
6317  C CE1 . TYR B 334 ? 0.3971 0.3232 0.3720 -0.0222 -0.0042 -0.0019 334 TYR B CE1 
6318  C CE2 . TYR B 334 ? 0.3791 0.3041 0.3557 -0.0211 -0.0105 -0.0093 334 TYR B CE2 
6319  C CZ  . TYR B 334 ? 0.4010 0.3240 0.3789 -0.0236 -0.0072 -0.0051 334 TYR B CZ  
6320  O OH  . TYR B 334 ? 0.4216 0.3389 0.4030 -0.0280 -0.0069 -0.0045 334 TYR B OH  
6321  N N   . PRO B 335 ? 0.3201 0.2471 0.2810 -0.0089 -0.0095 -0.0145 335 PRO B N   
6322  C CA  . PRO B 335 ? 0.3706 0.2905 0.3334 -0.0082 -0.0118 -0.0172 335 PRO B CA  
6323  C C   . PRO B 335 ? 0.3628 0.2782 0.3250 -0.0045 -0.0124 -0.0170 335 PRO B C   
6324  O O   . PRO B 335 ? 0.3739 0.2803 0.3365 -0.0045 -0.0146 -0.0151 335 PRO B O   
6325  C CB  . PRO B 335 ? 0.3551 0.2771 0.3168 -0.0080 -0.0128 -0.0235 335 PRO B CB  
6326  C CG  . PRO B 335 ? 0.3391 0.2666 0.2981 -0.0106 -0.0123 -0.0225 335 PRO B CG  
6327  C CD  . PRO B 335 ? 0.3318 0.2635 0.2897 -0.0098 -0.0098 -0.0180 335 PRO B CD  
6328  N N   . ASP B 336 ? 0.3339 0.2544 0.2947 -0.0015 -0.0110 -0.0187 336 ASP B N   
6329  C CA  . ASP B 336 ? 0.3653 0.2813 0.3267 0.0027  -0.0128 -0.0193 336 ASP B CA  
6330  C C   . ASP B 336 ? 0.3780 0.2902 0.3363 0.0026  -0.0125 -0.0126 336 ASP B C   
6331  O O   . ASP B 336 ? 0.3601 0.2638 0.3170 0.0052  -0.0157 -0.0115 336 ASP B O   
6332  C CB  . ASP B 336 ? 0.3533 0.2766 0.3165 0.0058  -0.0116 -0.0253 336 ASP B CB  
6333  C CG  . ASP B 336 ? 0.4190 0.3433 0.3853 0.0066  -0.0124 -0.0334 336 ASP B CG  
6334  O OD1 . ASP B 336 ? 0.4223 0.3423 0.3886 0.0044  -0.0140 -0.0337 336 ASP B OD1 
6335  O OD2 . ASP B 336 ? 0.4514 0.3806 0.4211 0.0093  -0.0117 -0.0400 336 ASP B OD2 
6336  N N   . LEU B 337 ? 0.3264 0.2439 0.2827 0.0000  -0.0093 -0.0083 337 LEU B N   
6337  C CA  . LEU B 337 ? 0.3059 0.2188 0.2584 -0.0006 -0.0085 -0.0023 337 LEU B CA  
6338  C C   . LEU B 337 ? 0.3746 0.2774 0.3254 -0.0041 -0.0095 0.0011  337 LEU B C   
6339  O O   . LEU B 337 ? 0.3835 0.2766 0.3289 -0.0039 -0.0109 0.0046  337 LEU B O   
6340  C CB  . LEU B 337 ? 0.3543 0.2754 0.3063 -0.0027 -0.0047 0.0007  337 LEU B CB  
6341  C CG  . LEU B 337 ? 0.3324 0.2502 0.2802 -0.0038 -0.0029 0.0060  337 LEU B CG  
6342  C CD1 . LEU B 337 ? 0.3257 0.2375 0.2686 0.0004  -0.0054 0.0067  337 LEU B CD1 
6343  C CD2 . LEU B 337 ? 0.3476 0.2758 0.2970 -0.0049 0.0004  0.0069  337 LEU B CD2 
6344  N N   . LYS B 338 ? 0.3630 0.2672 0.3176 -0.0079 -0.0088 0.0001  338 LYS B N   
6345  C CA  . LYS B 338 ? 0.3883 0.2824 0.3421 -0.0118 -0.0098 0.0023  338 LYS B CA  
6346  C C   . LYS B 338 ? 0.3933 0.2750 0.3439 -0.0086 -0.0148 0.0012  338 LYS B C   
6347  O O   . LYS B 338 ? 0.4381 0.3076 0.3823 -0.0103 -0.0161 0.0055  338 LYS B O   
6348  C CB  . LYS B 338 ? 0.4158 0.3140 0.3759 -0.0152 -0.0097 -0.0006 338 LYS B CB  
6349  C CG  . LYS B 338 ? 0.4293 0.3175 0.3903 -0.0196 -0.0111 0.0004  338 LYS B CG  
6350  C CD  . LYS B 338 ? 0.4627 0.3565 0.4307 -0.0219 -0.0118 -0.0037 338 LYS B CD  
6351  C CE  . LYS B 338 ? 0.5270 0.4128 0.4973 -0.0273 -0.0125 -0.0029 338 LYS B CE  
6352  N NZ  . LYS B 338 ? 0.5429 0.4159 0.5096 -0.0252 -0.0169 -0.0040 338 LYS B NZ  
6353  N N   . ARG B 339 ? 0.4055 0.2892 0.3598 -0.0043 -0.0179 -0.0049 339 ARG B N   
6354  C CA  . ARG B 339 ? 0.4334 0.3058 0.3868 -0.0005 -0.0236 -0.0074 339 ARG B CA  
6355  C C   . ARG B 339 ? 0.4295 0.2946 0.3770 0.0030  -0.0261 -0.0043 339 ARG B C   
6356  O O   . ARG B 339 ? 0.4361 0.2861 0.3782 0.0034  -0.0309 -0.0019 339 ARG B O   
6357  C CB  . ARG B 339 ? 0.4511 0.3297 0.4109 0.0040  -0.0255 -0.0159 339 ARG B CB  
6358  C CG  . ARG B 339 ? 0.4839 0.3641 0.4475 0.0011  -0.0253 -0.0195 339 ARG B CG  
6359  C CD  . ARG B 339 ? 0.5149 0.4019 0.4833 0.0048  -0.0260 -0.0283 339 ARG B CD  
6360  N NE  . ARG B 339 ? 0.4647 0.3436 0.4360 0.0098  -0.0315 -0.0332 339 ARG B NE  
6361  C CZ  . ARG B 339 ? 0.4928 0.3774 0.4697 0.0140  -0.0322 -0.0422 339 ARG B CZ  
6362  N NH1 . ARG B 339 ? 0.4940 0.3916 0.4721 0.0132  -0.0273 -0.0467 339 ARG B NH1 
6363  N NH2 . ARG B 339 ? 0.5058 0.3821 0.4868 0.0187  -0.0383 -0.0474 339 ARG B NH2 
6364  N N   . HIS B 340 ? 0.3900 0.2648 0.3376 0.0052  -0.0235 -0.0042 340 HIS B N   
6365  C CA  . HIS B 340 ? 0.4195 0.2885 0.3617 0.0089  -0.0263 -0.0018 340 HIS B CA  
6366  C C   . HIS B 340 ? 0.4425 0.2982 0.3740 0.0048  -0.0263 0.0061  340 HIS B C   
6367  O O   . HIS B 340 ? 0.4675 0.3088 0.3917 0.0071  -0.0320 0.0082  340 HIS B O   
6368  C CB  . HIS B 340 ? 0.3864 0.2690 0.3307 0.0106  -0.0224 -0.0027 340 HIS B CB  
6369  C CG  . HIS B 340 ? 0.4338 0.3128 0.3750 0.0156  -0.0260 -0.0024 340 HIS B CG  
6370  N ND1 . HIS B 340 ? 0.4403 0.3143 0.3849 0.0216  -0.0326 -0.0077 340 HIS B ND1 
6371  C CD2 . HIS B 340 ? 0.4345 0.3146 0.3702 0.0156  -0.0244 0.0017  340 HIS B CD2 
6372  C CE1 . HIS B 340 ? 0.4666 0.3383 0.4080 0.0252  -0.0354 -0.0065 340 HIS B CE1 
6373  N NE2 . HIS B 340 ? 0.4821 0.3574 0.4174 0.0216  -0.0303 -0.0007 340 HIS B NE2 
6374  N N   . LEU B 341 ? 0.4151 0.2752 0.3453 -0.0016 -0.0202 0.0102  341 LEU B N   
6375  C CA  . LEU B 341 ? 0.4059 0.2547 0.3258 -0.0071 -0.0184 0.0171  341 LEU B CA  
6376  C C   . LEU B 341 ? 0.4712 0.3034 0.3866 -0.0099 -0.0224 0.0185  341 LEU B C   
6377  O O   . LEU B 341 ? 0.4893 0.3045 0.3927 -0.0110 -0.0258 0.0230  341 LEU B O   
6378  C CB  . LEU B 341 ? 0.4216 0.2814 0.3445 -0.0133 -0.0106 0.0190  341 LEU B CB  
6379  C CG  . LEU B 341 ? 0.4614 0.3350 0.3869 -0.0108 -0.0072 0.0185  341 LEU B CG  
6380  C CD1 . LEU B 341 ? 0.4491 0.3321 0.3785 -0.0167 -0.0005 0.0198  341 LEU B CD1 
6381  C CD2 . LEU B 341 ? 0.4894 0.3556 0.4049 -0.0085 -0.0087 0.0219  341 LEU B CD2 
6382  N N   . GLU B 342 ? 0.4468 0.2823 0.3705 -0.0113 -0.0226 0.0147  342 GLU B N   
6383  C CA  . GLU B 342 ? 0.4608 0.2807 0.3809 -0.0148 -0.0261 0.0160  342 GLU B CA  
6384  C C   . GLU B 342 ? 0.4834 0.2879 0.3987 -0.0086 -0.0353 0.0145  342 GLU B C   
6385  O O   . GLU B 342 ? 0.4968 0.2819 0.4022 -0.0113 -0.0395 0.0185  342 GLU B O   
6386  C CB  . GLU B 342 ? 0.4557 0.2840 0.3868 -0.0167 -0.0249 0.0113  342 GLU B CB  
6387  C CG  . GLU B 342 ? 0.5080 0.3494 0.4439 -0.0229 -0.0172 0.0127  342 GLU B CG  
6388  C CD  . GLU B 342 ? 0.5799 0.4255 0.5243 -0.0272 -0.0161 0.0097  342 GLU B CD  
6389  O OE1 . GLU B 342 ? 0.6006 0.4509 0.5476 -0.0340 -0.0108 0.0118  342 GLU B OE1 
6390  O OE2 . GLU B 342 ? 0.6125 0.4569 0.5616 -0.0241 -0.0205 0.0048  342 GLU B OE2 
6391  N N   . GLU B 343 ? 0.4542 0.2666 0.3767 -0.0005 -0.0390 0.0083  343 GLU B N   
6392  C CA  . GLU B 343 ? 0.4970 0.2965 0.4174 0.0065  -0.0485 0.0054  343 GLU B CA  
6393  C C   . GLU B 343 ? 0.5058 0.2912 0.4126 0.0074  -0.0522 0.0115  343 GLU B C   
6394  O O   . GLU B 343 ? 0.5560 0.3241 0.4571 0.0115  -0.0615 0.0112  343 GLU B O   
6395  C CB  . GLU B 343 ? 0.5131 0.3269 0.4460 0.0144  -0.0503 -0.0037 343 GLU B CB  
6396  C CG  . GLU B 343 ? 0.4808 0.3040 0.4244 0.0139  -0.0484 -0.0103 343 GLU B CG  
6397  C CD  . GLU B 343 ? 0.5255 0.3657 0.4806 0.0193  -0.0471 -0.0196 343 GLU B CD  
6398  O OE1 . GLU B 343 ? 0.5852 0.4322 0.5420 0.0235  -0.0471 -0.0214 343 GLU B OE1 
6399  O OE2 . GLU B 343 ? 0.6017 0.4480 0.5636 0.0186  -0.0457 -0.0252 343 GLU B OE2 
6400  N N   . ASN B 344 ? 0.4605 0.2519 0.3615 0.0038  -0.0458 0.0166  344 ASN B N   
6401  C CA  . ASN B 344 ? 0.5249 0.3038 0.4115 0.0040  -0.0484 0.0224  344 ASN B CA  
6402  C C   . ASN B 344 ? 0.6059 0.3716 0.4779 -0.0058 -0.0440 0.0308  344 ASN B C   
6403  O O   . ASN B 344 ? 0.6437 0.4034 0.5029 -0.0083 -0.0420 0.0362  344 ASN B O   
6404  C CB  . ASN B 344 ? 0.5421 0.3370 0.4320 0.0071  -0.0444 0.0214  344 ASN B CB  
6405  C CG  . ASN B 344 ? 0.5608 0.3633 0.4615 0.0168  -0.0504 0.0135  344 ASN B CG  
6406  O OD1 . ASN B 344 ? 0.5700 0.3609 0.4656 0.0223  -0.0588 0.0130  344 ASN B OD1 
6407  N ND2 . ASN B 344 ? 0.5058 0.3272 0.4210 0.0185  -0.0463 0.0071  344 ASN B ND2 
6408  N N   . GLY B 345 ? 0.5597 0.3836 0.3952 0.0949  0.0249  0.0305  345 GLY B N   
6409  C CA  . GLY B 345 ? 0.5875 0.3914 0.4164 0.0813  0.0236  0.0433  345 GLY B CA  
6410  C C   . GLY B 345 ? 0.5532 0.3684 0.3901 0.0592  0.0280  0.0406  345 GLY B C   
6411  O O   . GLY B 345 ? 0.6118 0.4191 0.4445 0.0458  0.0284  0.0513  345 GLY B O   
6412  N N   . ILE B 346 ? 0.5158 0.3501 0.3651 0.0550  0.0314  0.0276  346 ILE B N   
6413  C CA  . ILE B 346 ? 0.5089 0.3585 0.3706 0.0369  0.0358  0.0249  346 ILE B CA  
6414  C C   . ILE B 346 ? 0.5266 0.3575 0.3915 0.0308  0.0329  0.0175  346 ILE B C   
6415  O O   . ILE B 346 ? 0.5108 0.3506 0.3813 0.0367  0.0328  0.0079  346 ILE B O   
6416  C CB  . ILE B 346 ? 0.4951 0.3843 0.3717 0.0366  0.0422  0.0174  346 ILE B CB  
6417  C CG1 . ILE B 346 ? 0.5164 0.4274 0.3880 0.0418  0.0443  0.0229  346 ILE B CG1 
6418  C CG2 . ILE B 346 ? 0.4641 0.3679 0.3571 0.0198  0.0475  0.0145  346 ILE B CG2 
6419  C CD1 . ILE B 346 ? 0.5234 0.4662 0.4050 0.0471  0.0488  0.0135  346 ILE B CD1 
6420  N N   . PRO B 347 ? 0.5474 0.3565 0.4091 0.0174  0.0306  0.0219  347 PRO B N   
6421  C CA  . PRO B 347 ? 0.5714 0.3701 0.4376 0.0085  0.0274  0.0144  347 PRO B CA  
6422  C C   . PRO B 347 ? 0.4899 0.3210 0.3764 0.0013  0.0307  0.0094  347 PRO B C   
6423  O O   . PRO B 347 ? 0.4551 0.3123 0.3542 -0.0025 0.0369  0.0117  347 PRO B O   
6424  C CB  . PRO B 347 ? 0.5871 0.3595 0.4466 -0.0067 0.0252  0.0215  347 PRO B CB  
6425  C CG  . PRO B 347 ? 0.6085 0.3816 0.4619 -0.0078 0.0283  0.0345  347 PRO B CG  
6426  C CD  . PRO B 347 ? 0.6039 0.4036 0.4591 0.0068  0.0316  0.0347  347 PRO B CD  
6427  N N   . THR B 348 ? 0.5111 0.3408 0.4011 -0.0001 0.0266  0.0022  348 THR B N   
6428  C CA  . THR B 348 ? 0.4151 0.2735 0.3255 -0.0041 0.0284  -0.0006 348 THR B CA  
6429  C C   . THR B 348 ? 0.4473 0.3048 0.3650 -0.0174 0.0228  -0.0016 348 THR B C   
6430  O O   . THR B 348 ? 0.4472 0.2810 0.3514 -0.0234 0.0169  -0.0040 348 THR B O   
6431  C CB  . THR B 348 ? 0.4716 0.3415 0.3818 0.0091  0.0289  -0.0060 348 THR B CB  
6432  O OG1 . THR B 348 ? 0.5318 0.3846 0.4275 0.0124  0.0226  -0.0118 348 THR B OG1 
6433  C CG2 . THR B 348 ? 0.4436 0.3188 0.3476 0.0215  0.0338  -0.0057 348 THR B CG2 
6434  N N   . LEU B 349 ? 0.3996 0.2844 0.3405 -0.0223 0.0249  -0.0002 349 LEU B N   
6435  C CA  . LEU B 349 ? 0.4353 0.3303 0.3896 -0.0336 0.0193  0.0004  349 LEU B CA  
6436  C C   . LEU B 349 ? 0.3894 0.3079 0.3605 -0.0270 0.0186  0.0009  349 LEU B C   
6437  O O   . LEU B 349 ? 0.3878 0.3200 0.3708 -0.0192 0.0257  0.0015  349 LEU B O   
6438  C CB  . LEU B 349 ? 0.3635 0.2712 0.3352 -0.0466 0.0233  0.0044  349 LEU B CB  
6439  C CG  . LEU B 349 ? 0.4015 0.3277 0.3930 -0.0580 0.0179  0.0058  349 LEU B CG  
6440  C CD1 . LEU B 349 ? 0.4478 0.3546 0.4218 -0.0681 0.0079  0.0029  349 LEU B CD1 
6441  C CD2 . LEU B 349 ? 0.4124 0.3583 0.4258 -0.0689 0.0245  0.0087  349 LEU B CD2 
6442  N N   . PHE B 350 ? 0.4009 0.3239 0.3719 -0.0308 0.0099  0.0008  350 PHE B N   
6443  C CA  . PHE B 350 ? 0.3824 0.3266 0.3675 -0.0251 0.0076  0.0047  350 PHE B CA  
6444  C C   . PHE B 350 ? 0.3890 0.3559 0.3994 -0.0339 0.0025  0.0109  350 PHE B C   
6445  O O   . PHE B 350 ? 0.3956 0.3616 0.4008 -0.0453 -0.0056 0.0099  350 PHE B O   
6446  C CB  . PHE B 350 ? 0.3584 0.2947 0.3207 -0.0211 0.0011  0.0011  350 PHE B CB  
6447  C CG  . PHE B 350 ? 0.3969 0.3550 0.3706 -0.0172 -0.0023 0.0080  350 PHE B CG  
6448  C CD1 . PHE B 350 ? 0.3955 0.3599 0.3754 -0.0066 0.0046  0.0107  350 PHE B CD1 
6449  C CD2 . PHE B 350 ? 0.3900 0.3632 0.3683 -0.0252 -0.0128 0.0129  350 PHE B CD2 
6450  C CE1 . PHE B 350 ? 0.4109 0.3921 0.4008 -0.0039 0.0018  0.0193  350 PHE B CE1 
6451  C CE2 . PHE B 350 ? 0.4393 0.4331 0.4279 -0.0214 -0.0168 0.0229  350 PHE B CE2 
6452  C CZ  . PHE B 350 ? 0.4317 0.4274 0.4259 -0.0106 -0.0092 0.0268  350 PHE B CZ  
6453  N N   . LEU B 351 ? 0.3502 0.3379 0.3895 -0.0288 0.0074  0.0167  351 LEU B N   
6454  C CA  . LEU B 351 ? 0.3146 0.3272 0.3829 -0.0338 0.0024  0.0239  351 LEU B CA  
6455  C C   . LEU B 351 ? 0.3163 0.3441 0.4022 -0.0236 0.0008  0.0328  351 LEU B C   
6456  O O   . LEU B 351 ? 0.3272 0.3501 0.4164 -0.0141 0.0093  0.0323  351 LEU B O   
6457  C CB  . LEU B 351 ? 0.2982 0.3223 0.3916 -0.0376 0.0114  0.0225  351 LEU B CB  
6458  C CG  . LEU B 351 ? 0.3286 0.3390 0.4068 -0.0490 0.0148  0.0165  351 LEU B CG  
6459  C CD1 . LEU B 351 ? 0.3609 0.3889 0.4661 -0.0514 0.0266  0.0149  351 LEU B CD1 
6460  C CD2 . LEU B 351 ? 0.4070 0.4168 0.4772 -0.0633 0.0042  0.0168  351 LEU B CD2 
6461  N N   . GLU B 352 ? 0.2906 0.3375 0.3883 -0.0265 -0.0102 0.0419  352 GLU B N   
6462  C CA  . GLU B 352 ? 0.3018 0.3616 0.4129 -0.0176 -0.0141 0.0542  352 GLU B CA  
6463  C C   . GLU B 352 ? 0.3113 0.3977 0.4646 -0.0152 -0.0165 0.0650  352 GLU B C   
6464  O O   . GLU B 352 ? 0.3193 0.4224 0.4829 -0.0240 -0.0235 0.0656  352 GLU B O   
6465  C CB  . GLU B 352 ? 0.3589 0.4205 0.4424 -0.0217 -0.0269 0.0579  352 GLU B CB  
6466  C CG  . GLU B 352 ? 0.3794 0.4548 0.4737 -0.0138 -0.0313 0.0736  352 GLU B CG  
6467  C CD  . GLU B 352 ? 0.4795 0.5548 0.5394 -0.0174 -0.0402 0.0750  352 GLU B CD  
6468  O OE1 . GLU B 352 ? 0.4710 0.5360 0.5171 -0.0110 -0.0343 0.0754  352 GLU B OE1 
6469  O OE2 . GLU B 352 ? 0.5392 0.6267 0.5862 -0.0276 -0.0522 0.0746  352 GLU B OE2 
6470  N N   . PHE B 353 ? 0.2660 0.3567 0.4453 -0.0031 -0.0111 0.0739  353 PHE B N   
6471  C CA  . PHE B 353 ? 0.3272 0.4387 0.5523 0.0033  -0.0093 0.0820  353 PHE B CA  
6472  C C   . PHE B 353 ? 0.3054 0.4296 0.5491 0.0124  -0.0180 0.1020  353 PHE B C   
6473  O O   . PHE B 353 ? 0.2952 0.4063 0.5245 0.0171  -0.0175 0.1082  353 PHE B O   
6474  C CB  . PHE B 353 ? 0.2941 0.3957 0.5397 0.0099  0.0088  0.0718  353 PHE B CB  
6475  C CG  . PHE B 353 ? 0.3033 0.3987 0.5355 0.0006  0.0169  0.0555  353 PHE B CG  
6476  C CD1 . PHE B 353 ? 0.2877 0.3604 0.4826 -0.0033 0.0208  0.0458  353 PHE B CD1 
6477  C CD2 . PHE B 353 ? 0.3718 0.4862 0.6280 -0.0047 0.0196  0.0516  353 PHE B CD2 
6478  C CE1 . PHE B 353 ? 0.3276 0.3938 0.5090 -0.0117 0.0269  0.0343  353 PHE B CE1 
6479  C CE2 . PHE B 353 ? 0.3392 0.4482 0.5805 -0.0152 0.0265  0.0392  353 PHE B CE2 
6480  C CZ  . PHE B 353 ? 0.3517 0.4352 0.5548 -0.0185 0.0298  0.0315  353 PHE B CZ  
6481  N N   . ASP B 354 ? 0.3367 0.4884 0.6146 0.0147  -0.0258 0.1131  354 ASP B N   
6482  C CA  . ASP B 354 ? 0.3279 0.4947 0.6370 0.0266  -0.0327 0.1345  354 ASP B CA  
6483  C C   . ASP B 354 ? 0.3508 0.5159 0.7071 0.0398  -0.0181 0.1326  354 ASP B C   
6484  O O   . ASP B 354 ? 0.3396 0.4914 0.6975 0.0384  -0.0024 0.1138  354 ASP B O   
6485  C CB  . ASP B 354 ? 0.3668 0.5683 0.6836 0.0210  -0.0514 0.1472  354 ASP B CB  
6486  C CG  . ASP B 354 ? 0.4983 0.7116 0.8139 0.0263  -0.0657 0.1715  354 ASP B CG  
6487  O OD1 . ASP B 354 ? 0.4312 0.6384 0.7740 0.0408  -0.0615 0.1860  354 ASP B OD1 
6488  O OD2 . ASP B 354 ? 0.5749 0.8027 0.8612 0.0152  -0.0807 0.1760  354 ASP B OD2 
6489  N N   . ILE B 355 ? 0.3111 0.4893 0.7058 0.0530  -0.0229 0.1522  355 ILE B N   
6490  C CA  . ILE B 355 ? 0.3465 0.5242 0.7915 0.0671  -0.0094 0.1500  355 ILE B CA  
6491  C C   . ILE B 355 ? 0.3700 0.5701 0.8383 0.0633  -0.0035 0.1345  355 ILE B C   
6492  O O   . ILE B 355 ? 0.3230 0.5164 0.8130 0.0672  0.0142  0.1180  355 ILE B O   
6493  C CB  . ILE B 355 ? 0.3338 0.5233 0.8172 0.0829  -0.0186 0.1770  355 ILE B CB  
6494  C CG1 . ILE B 355 ? 0.3323 0.4982 0.7949 0.0860  -0.0223 0.1941  355 ILE B CG1 
6495  C CG2 . ILE B 355 ? 0.3201 0.5102 0.8608 0.0990  -0.0045 0.1731  355 ILE B CG2 
6496  C CD1 . ILE B 355 ? 0.3242 0.4917 0.8317 0.1041  -0.0260 0.2205  355 ILE B CD1 
6497  N N   . THR B 356 ? 0.3640 0.5935 0.8283 0.0543  -0.0179 0.1392  356 THR B N   
6498  C CA  . THR B 356 ? 0.3444 0.5968 0.8232 0.0459  -0.0135 0.1247  356 THR B CA  
6499  C C   . THR B 356 ? 0.3267 0.5842 0.7623 0.0257  -0.0252 0.1200  356 THR B C   
6500  O O   . THR B 356 ? 0.3676 0.6251 0.7759 0.0211  -0.0406 0.1317  356 THR B O   
6501  C CB  . THR B 356 ? 0.3422 0.6337 0.8776 0.0570  -0.0183 0.1359  356 THR B CB  
6502  O OG1 . THR B 356 ? 0.3690 0.6894 0.9001 0.0523  -0.0408 0.1544  356 THR B OG1 
6503  C CG2 . THR B 356 ? 0.2943 0.5772 0.8728 0.0795  -0.0108 0.1461  356 THR B CG2 
6504  N N   . ASN B 357 ? 0.4075 0.6673 0.8349 0.0127  -0.0171 0.1022  357 ASN B N   
6505  C CA  . ASN B 357 ? 0.3843 0.6481 0.7763 -0.0072 -0.0278 0.0976  357 ASN B CA  
6506  C C   . ASN B 357 ? 0.3882 0.6739 0.7984 -0.0187 -0.0210 0.0857  357 ASN B C   
6507  O O   . ASN B 357 ? 0.3600 0.6414 0.7867 -0.0151 -0.0036 0.0740  357 ASN B O   
6508  C CB  . ASN B 357 ? 0.3969 0.6212 0.7342 -0.0161 -0.0247 0.0871  357 ASN B CB  
6509  C CG  . ASN B 357 ? 0.4276 0.6278 0.7458 -0.0051 -0.0261 0.0951  357 ASN B CG  
6510  O OD1 . ASN B 357 ? 0.3665 0.5518 0.6981 0.0071  -0.0140 0.0941  357 ASN B OD1 
6511  N ND2 . ASN B 357 ? 0.4279 0.6262 0.7151 -0.0110 -0.0405 0.1023  357 ASN B ND2 
6512  N N   . PRO B 358 ? 0.4302 0.7395 0.8351 -0.0346 -0.0335 0.0870  358 PRO B N   
6513  C CA  . PRO B 358 ? 0.4387 0.7661 0.8556 -0.0492 -0.0259 0.0751  358 PRO B CA  
6514  C C   . PRO B 358 ? 0.4457 0.7357 0.8228 -0.0608 -0.0137 0.0599  358 PRO B C   
6515  O O   . PRO B 358 ? 0.4155 0.6735 0.7483 -0.0668 -0.0189 0.0581  358 PRO B O   
6516  C CB  . PRO B 358 ? 0.4426 0.7998 0.8567 -0.0658 -0.0442 0.0806  358 PRO B CB  
6517  C CG  . PRO B 358 ? 0.4873 0.8279 0.8667 -0.0651 -0.0598 0.0896  358 PRO B CG  
6518  C CD  . PRO B 358 ? 0.4854 0.7933 0.8559 -0.0457 -0.0520 0.0934  358 PRO B CD  
6519  N N   . ILE B 359 ? 0.4351 0.7306 0.8289 -0.0630 0.0031  0.0492  359 ILE B N   
6520  C CA  . ILE B 359 ? 0.4101 0.6713 0.7695 -0.0699 0.0160  0.0374  359 ILE B CA  
6521  C C   . ILE B 359 ? 0.4132 0.6626 0.7383 -0.0934 0.0120  0.0327  359 ILE B C   
6522  O O   . ILE B 359 ? 0.3886 0.6021 0.6757 -0.0981 0.0170  0.0272  359 ILE B O   
6523  C CB  . ILE B 359 ? 0.4296 0.7021 0.8169 -0.0639 0.0361  0.0275  359 ILE B CB  
6524  C CG1 . ILE B 359 ? 0.4795 0.7150 0.8348 -0.0605 0.0477  0.0192  359 ILE B CG1 
6525  C CG2 . ILE B 359 ? 0.4299 0.7324 0.8339 -0.0805 0.0424  0.0212  359 ILE B CG2 
6526  C CD1 . ILE B 359 ? 0.4718 0.7164 0.8539 -0.0511 0.0669  0.0087  359 ILE B CD1 
6527  N N   . GLY B 360 ? 0.3833 0.6611 0.7211 -0.1081 0.0025  0.0353  360 GLY B N   
6528  C CA  . GLY B 360 ? 0.3836 0.6507 0.6935 -0.1328 -0.0007 0.0306  360 GLY B CA  
6529  C C   . GLY B 360 ? 0.4121 0.6346 0.6714 -0.1390 -0.0090 0.0292  360 GLY B C   
6530  O O   . GLY B 360 ? 0.4200 0.6122 0.6494 -0.1511 -0.0030 0.0236  360 GLY B O   
6531  N N   . PRO B 361 ? 0.4204 0.6387 0.6693 -0.1314 -0.0228 0.0345  361 PRO B N   
6532  C CA  . PRO B 361 ? 0.4467 0.6227 0.6483 -0.1351 -0.0286 0.0307  361 PRO B CA  
6533  C C   . PRO B 361 ? 0.4425 0.5806 0.6209 -0.1233 -0.0166 0.0268  361 PRO B C   
6534  O O   . PRO B 361 ? 0.4315 0.5330 0.5736 -0.1302 -0.0160 0.0213  361 PRO B O   
6535  C CB  . PRO B 361 ? 0.4458 0.6345 0.6473 -0.1262 -0.0434 0.0380  361 PRO B CB  
6536  C CG  . PRO B 361 ? 0.4250 0.6638 0.6694 -0.1267 -0.0501 0.0461  361 PRO B CG  
6537  C CD  . PRO B 361 ? 0.4382 0.6911 0.7166 -0.1200 -0.0343 0.0449  361 PRO B CD  
6538  N N   . PHE B 362 ? 0.3960 0.5423 0.5958 -0.1059 -0.0068 0.0292  362 PHE B N   
6539  C CA  . PHE B 362 ? 0.3829 0.4988 0.5624 -0.0965 0.0047  0.0247  362 PHE B CA  
6540  C C   . PHE B 362 ? 0.4014 0.5076 0.5715 -0.1091 0.0158  0.0192  362 PHE B C   
6541  O O   . PHE B 362 ? 0.4427 0.5164 0.5810 -0.1093 0.0197  0.0163  362 PHE B O   
6542  C CB  . PHE B 362 ? 0.3673 0.4957 0.5738 -0.0773 0.0129  0.0269  362 PHE B CB  
6543  C CG  . PHE B 362 ? 0.4037 0.5336 0.6129 -0.0641 0.0031  0.0349  362 PHE B CG  
6544  C CD1 . PHE B 362 ? 0.3921 0.4940 0.5713 -0.0562 0.0022  0.0343  362 PHE B CD1 
6545  C CD2 . PHE B 362 ? 0.4368 0.5984 0.6782 -0.0603 -0.0056 0.0443  362 PHE B CD2 
6546  C CE1 . PHE B 362 ? 0.3748 0.4794 0.5543 -0.0461 -0.0062 0.0427  362 PHE B CE1 
6547  C CE2 . PHE B 362 ? 0.4177 0.5811 0.6593 -0.0492 -0.0152 0.0546  362 PHE B CE2 
6548  C CZ  . PHE B 362 ? 0.3956 0.5301 0.6050 -0.0432 -0.0152 0.0537  362 PHE B CZ  
6549  N N   . ARG B 363 ? 0.3744 0.5103 0.5718 -0.1196 0.0208  0.0185  363 ARG B N   
6550  C CA  . ARG B 363 ? 0.3779 0.5074 0.5652 -0.1334 0.0318  0.0149  363 ARG B CA  
6551  C C   . ARG B 363 ? 0.4316 0.5285 0.5822 -0.1504 0.0248  0.0155  363 ARG B C   
6552  O O   . ARG B 363 ? 0.4417 0.5094 0.5648 -0.1541 0.0308  0.0152  363 ARG B O   
6553  C CB  . ARG B 363 ? 0.4429 0.6153 0.6683 -0.1430 0.0387  0.0137  363 ARG B CB  
6554  C CG  . ARG B 363 ? 0.3984 0.5707 0.6149 -0.1598 0.0511  0.0110  363 ARG B CG  
6555  C CD  . ARG B 363 ? 0.4536 0.6740 0.7099 -0.1708 0.0571  0.0089  363 ARG B CD  
6556  N NE  . ARG B 363 ? 0.5900 0.8414 0.8848 -0.1533 0.0673  0.0040  363 ARG B NE  
6557  C CZ  . ARG B 363 ? 0.5458 0.8336 0.8833 -0.1444 0.0636  0.0048  363 ARG B CZ  
6558  N NH1 . ARG B 363 ? 0.4864 0.7912 0.8344 -0.1528 0.0492  0.0105  363 ARG B NH1 
6559  N NH2 . ARG B 363 ? 0.5013 0.8093 0.8727 -0.1266 0.0744  -0.0005 363 ARG B NH2 
6560  N N   . ILE B 364 ? 0.4184 0.5199 0.5686 -0.1610 0.0118  0.0162  364 ILE B N   
6561  C CA  . ILE B 364 ? 0.4675 0.5348 0.5841 -0.1779 0.0054  0.0144  364 ILE B CA  
6562  C C   . ILE B 364 ? 0.4724 0.4936 0.5522 -0.1658 0.0049  0.0128  364 ILE B C   
6563  O O   . ILE B 364 ? 0.4904 0.4763 0.5431 -0.1739 0.0077  0.0126  364 ILE B O   
6564  C CB  . ILE B 364 ? 0.4688 0.5517 0.5911 -0.1900 -0.0093 0.0128  364 ILE B CB  
6565  C CG1 . ILE B 364 ? 0.4235 0.5550 0.5839 -0.2032 -0.0085 0.0147  364 ILE B CG1 
6566  C CG2 . ILE B 364 ? 0.5093 0.5527 0.5968 -0.2082 -0.0151 0.0079  364 ILE B CG2 
6567  C CD1 . ILE B 364 ? 0.4453 0.6062 0.6198 -0.2110 -0.0238 0.0148  364 ILE B CD1 
6568  N N   . ARG B 365 ? 0.4479 0.4695 0.5273 -0.1463 0.0011  0.0126  365 ARG B N   
6569  C CA  . ARG B 365 ? 0.4944 0.4785 0.5422 -0.1335 0.0011  0.0103  365 ARG B CA  
6570  C C   . ARG B 365 ? 0.4557 0.4251 0.4947 -0.1262 0.0133  0.0120  365 ARG B C   
6571  O O   . ARG B 365 ? 0.4825 0.4167 0.4925 -0.1226 0.0138  0.0112  365 ARG B O   
6572  C CB  . ARG B 365 ? 0.5119 0.5071 0.5652 -0.1159 -0.0042 0.0109  365 ARG B CB  
6573  C CG  . ARG B 365 ? 0.5317 0.5423 0.5883 -0.1228 -0.0179 0.0105  365 ARG B CG  
6574  C CD  . ARG B 365 ? 0.6158 0.6061 0.6459 -0.1134 -0.0241 0.0069  365 ARG B CD  
6575  N NE  . ARG B 365 ? 0.6281 0.5771 0.6275 -0.1093 -0.0187 0.0011  365 ARG B NE  
6576  C CZ  . ARG B 365 ? 0.7142 0.6456 0.6931 -0.0958 -0.0192 -0.0024 365 ARG B CZ  
6577  N NH1 . ARG B 365 ? 0.6827 0.6330 0.6670 -0.0858 -0.0236 0.0001  365 ARG B NH1 
6578  N NH2 . ARG B 365 ? 0.7053 0.6003 0.6585 -0.0921 -0.0152 -0.0077 365 ARG B NH2 
6579  N N   . ILE B 366 ? 0.4435 0.4411 0.5077 -0.1222 0.0231  0.0136  366 ILE B N   
6580  C CA  . ILE B 366 ? 0.4330 0.4225 0.4881 -0.1176 0.0347  0.0143  366 ILE B CA  
6581  C C   . ILE B 366 ? 0.4751 0.4482 0.5134 -0.1353 0.0379  0.0181  366 ILE B C   
6582  O O   . ILE B 366 ? 0.4933 0.4401 0.5063 -0.1326 0.0409  0.0213  366 ILE B O   
6583  C CB  . ILE B 366 ? 0.4447 0.4700 0.5318 -0.1107 0.0453  0.0121  366 ILE B CB  
6584  C CG1 . ILE B 366 ? 0.4167 0.4513 0.5190 -0.0933 0.0415  0.0108  366 ILE B CG1 
6585  C CG2 . ILE B 366 ? 0.4450 0.4673 0.5218 -0.1088 0.0573  0.0112  366 ILE B CG2 
6586  C CD1 . ILE B 366 ? 0.4423 0.4987 0.5699 -0.0821 0.0530  0.0070  366 ILE B CD1 
6587  N N   . GLU B 367 ? 0.4588 0.4478 0.5110 -0.1540 0.0367  0.0190  367 GLU B N   
6588  C CA  . GLU B 367 ? 0.5194 0.4907 0.5550 -0.1738 0.0395  0.0240  367 GLU B CA  
6589  C C   . GLU B 367 ? 0.5137 0.4347 0.5146 -0.1752 0.0316  0.0257  367 GLU B C   
6590  O O   . GLU B 367 ? 0.5412 0.4343 0.5198 -0.1801 0.0354  0.0324  367 GLU B O   
6591  C CB  . GLU B 367 ? 0.5298 0.5297 0.5884 -0.1950 0.0391  0.0236  367 GLU B CB  
6592  C CG  . GLU B 367 ? 0.5265 0.5752 0.6200 -0.1942 0.0499  0.0217  367 GLU B CG  
6593  C CD  . GLU B 367 ? 0.5920 0.6796 0.7179 -0.2091 0.0473  0.0197  367 GLU B CD  
6594  O OE1 . GLU B 367 ? 0.5276 0.6120 0.6538 -0.2155 0.0348  0.0187  367 GLU B OE1 
6595  O OE2 . GLU B 367 ? 0.6011 0.7248 0.7515 -0.2160 0.0584  0.0185  367 GLU B OE2 
6596  N N   . ALA B 368 ? 0.5543 0.4634 0.5501 -0.1699 0.0210  0.0197  368 ALA B N   
6597  C CA  . ALA B 368 ? 0.5587 0.4199 0.5235 -0.1696 0.0145  0.0177  368 ALA B CA  
6598  C C   . ALA B 368 ? 0.5920 0.4290 0.5370 -0.1486 0.0178  0.0201  368 ALA B C   
6599  O O   . ALA B 368 ? 0.5905 0.3878 0.5115 -0.1490 0.0178  0.0239  368 ALA B O   
6600  C CB  . ALA B 368 ? 0.5716 0.4333 0.5362 -0.1696 0.0031  0.0084  368 ALA B CB  
6601  N N   . PHE B 369 ? 0.5456 0.4062 0.5020 -0.1302 0.0205  0.0182  369 PHE B N   
6602  C CA  . PHE B 369 ? 0.5213 0.3681 0.4629 -0.1114 0.0243  0.0201  369 PHE B CA  
6603  C C   . PHE B 369 ? 0.5583 0.3979 0.4905 -0.1167 0.0319  0.0297  369 PHE B C   
6604  O O   . PHE B 369 ? 0.5817 0.3936 0.4923 -0.1075 0.0317  0.0345  369 PHE B O   
6605  C CB  . PHE B 369 ? 0.5224 0.4018 0.4828 -0.0961 0.0277  0.0166  369 PHE B CB  
6606  C CG  . PHE B 369 ? 0.4838 0.3547 0.4312 -0.0769 0.0307  0.0163  369 PHE B CG  
6607  C CD1 . PHE B 369 ? 0.5062 0.3462 0.4304 -0.0664 0.0255  0.0144  369 PHE B CD1 
6608  C CD2 . PHE B 369 ? 0.4656 0.3621 0.4256 -0.0700 0.0394  0.0165  369 PHE B CD2 
6609  C CE1 . PHE B 369 ? 0.5116 0.3501 0.4271 -0.0490 0.0283  0.0142  369 PHE B CE1 
6610  C CE2 . PHE B 369 ? 0.4898 0.3834 0.4394 -0.0546 0.0420  0.0156  369 PHE B CE2 
6611  C CZ  . PHE B 369 ? 0.4819 0.3484 0.4100 -0.0440 0.0362  0.0152  369 PHE B CZ  
6612  N N   . LEU B 370 ? 0.5479 0.4164 0.4974 -0.1302 0.0389  0.0329  370 LEU B N   
6613  C CA  . LEU B 370 ? 0.6044 0.4718 0.5438 -0.1375 0.0467  0.0427  370 LEU B CA  
6614  C C   . LEU B 370 ? 0.6550 0.4781 0.5688 -0.1474 0.0424  0.0520  370 LEU B C   
6615  O O   . LEU B 370 ? 0.6965 0.5016 0.5911 -0.1438 0.0447  0.0626  370 LEU B O   
6616  C CB  . LEU B 370 ? 0.6196 0.5266 0.5824 -0.1537 0.0554  0.0426  370 LEU B CB  
6617  C CG  . LEU B 370 ? 0.6550 0.5838 0.6162 -0.1582 0.0670  0.0480  370 LEU B CG  
6618  C CD1 . LEU B 370 ? 0.6116 0.5592 0.5777 -0.1391 0.0718  0.0417  370 LEU B CD1 
6619  C CD2 . LEU B 370 ? 0.6700 0.6354 0.6552 -0.1766 0.0751  0.0458  370 LEU B CD2 
6620  N N   . GLU B 371 ? 0.6877 0.4922 0.6013 -0.1597 0.0357  0.0481  371 GLU B N   
6621  C CA  . GLU B 371 ? 0.7657 0.5223 0.6567 -0.1705 0.0319  0.0549  371 GLU B CA  
6622  C C   . GLU B 371 ? 0.8559 0.5724 0.7248 -0.1497 0.0273  0.0554  371 GLU B C   
6623  O O   . GLU B 371 ? 0.8905 0.5709 0.7400 -0.1500 0.0275  0.0670  371 GLU B O   
6624  C CB  . GLU B 371 ? 0.7713 0.5199 0.6684 -0.1885 0.0257  0.0464  371 GLU B CB  
6625  C CG  . GLU B 371 ? 0.8316 0.6090 0.7463 -0.2148 0.0299  0.0493  371 GLU B CG  
6626  C CD  . GLU B 371 ? 0.9979 0.7511 0.8977 -0.2337 0.0351  0.0638  371 GLU B CD  
6627  O OE1 . GLU B 371 ? 1.0191 0.7197 0.8961 -0.2366 0.0312  0.0685  371 GLU B OE1 
6628  O OE2 . GLU B 371 ? 1.0125 0.7994 0.9239 -0.2461 0.0436  0.0707  371 GLU B OE2 
6629  N N   . THR B 372 ? 0.7792 0.5018 0.6514 -0.1314 0.0232  0.0437  372 THR B N   
6630  C CA  . THR B 372 ? 0.8525 0.5433 0.7067 -0.1103 0.0198  0.0421  372 THR B CA  
6631  C C   . THR B 372 ? 0.8592 0.5522 0.7050 -0.0973 0.0244  0.0548  372 THR B C   
6632  O O   . THR B 372 ? 0.9102 0.5678 0.7384 -0.0868 0.0222  0.0619  372 THR B O   
6633  C CB  . THR B 372 ? 0.8712 0.5795 0.7325 -0.0944 0.0165  0.0282  372 THR B CB  
6634  O OG1 . THR B 372 ? 0.8730 0.5807 0.7394 -0.1068 0.0109  0.0173  372 THR B OG1 
6635  C CG2 . THR B 372 ? 0.9354 0.6154 0.7796 -0.0720 0.0142  0.0252  372 THR B CG2 
6636  N N   . LEU B 373 ? 0.7977 0.5337 0.6568 -0.0975 0.0306  0.0572  373 LEU B N   
6637  C CA  . LEU B 373 ? 0.8065 0.5532 0.6578 -0.0874 0.0349  0.0677  373 LEU B CA  
6638  C C   . LEU B 373 ? 0.8683 0.5896 0.7026 -0.0986 0.0356  0.0858  373 LEU B C   
6639  O O   . LEU B 373 ? 0.8741 0.5797 0.6928 -0.0860 0.0340  0.0973  373 LEU B O   
6640  C CB  . LEU B 373 ? 0.7020 0.5001 0.5722 -0.0903 0.0429  0.0636  373 LEU B CB  
6641  C CG  . LEU B 373 ? 0.6869 0.5118 0.5735 -0.0763 0.0436  0.0497  373 LEU B CG  
6642  C CD1 . LEU B 373 ? 0.6095 0.4777 0.5105 -0.0768 0.0531  0.0473  373 LEU B CD1 
6643  C CD2 . LEU B 373 ? 0.6488 0.4538 0.5221 -0.0552 0.0384  0.0476  373 LEU B CD2 
6644  N N   . SER B 374 ? 0.9021 0.6198 0.7398 -0.1227 0.0377  0.0897  374 SER B N   
6645  C CA  . SER B 374 ? 0.9699 0.6663 0.7924 -0.1382 0.0396  0.1086  374 SER B CA  
6646  C C   . SER B 374 ? 1.0339 0.6692 0.8371 -0.1339 0.0328  0.1169  374 SER B C   
6647  O O   . SER B 374 ? 1.0546 0.6661 0.8432 -0.1438 0.0336  0.1361  374 SER B O   
6648  C CB  . SER B 374 ? 0.8886 0.6039 0.7233 -0.1670 0.0448  0.1085  374 SER B CB  
6649  O OG  . SER B 374 ? 0.9913 0.6695 0.8231 -0.1817 0.0400  0.1063  374 SER B OG  
6650  N N   . GLU B 375 ? 1.1255 0.7346 0.9282 -0.1201 0.0268  0.1033  375 GLU B N   
6651  C CA  . GLU B 375 ? 1.2591 0.8099 1.0452 -0.1105 0.0215  0.1083  375 GLU B CA  
6652  C C   . GLU B 375 ? 1.3375 0.8869 1.1182 -0.0791 0.0187  0.1083  375 GLU B C   
6653  O O   . GLU B 375 ? 1.2378 0.8275 1.0284 -0.0662 0.0200  0.0986  375 GLU B O   
6654  C CB  . GLU B 375 ? 1.2537 0.7737 1.0415 -0.1183 0.0175  0.0907  375 GLU B CB  
6655  C CG  . GLU B 375 ? 1.2034 0.7626 1.0090 -0.1339 0.0183  0.0753  375 GLU B CG  
6656  C CD  . GLU B 375 ? 1.2775 0.8211 1.0843 -0.1320 0.0130  0.0544  375 GLU B CD  
6657  O OE1 . GLU B 375 ? 1.2404 0.7899 1.0467 -0.1095 0.0108  0.0440  375 GLU B OE1 
6658  O OE2 . GLU B 375 ? 1.2965 0.8247 1.1042 -0.1541 0.0111  0.0479  375 GLU B OE2 
6659  N N   . GLU B 376 ? 1.4486 0.9506 1.2152 -0.0671 0.0151  0.1196  376 GLU B N   
6660  C CA  . GLU B 376 ? 1.4620 0.9610 1.2243 -0.0365 0.0121  0.1224  376 GLU B CA  
6661  C C   . GLU B 376 ? 1.4275 0.9786 1.1923 -0.0285 0.0143  0.1320  376 GLU B C   
6662  O O   . GLU B 376 ? 1.3529 0.9342 1.1249 -0.0106 0.0143  0.1208  376 GLU B O   
6663  C CB  . GLU B 376 ? 1.4779 0.9760 1.2469 -0.0198 0.0102  0.0978  376 GLU B CB  
6664  C CG  . GLU B 376 ? 1.4373 0.8936 1.2042 -0.0301 0.0086  0.0822  376 GLU B CG  
6665  C CD  . GLU B 376 ? 1.4179 0.8477 1.1820 -0.0060 0.0063  0.0672  376 GLU B CD  
6666  O OE1 . GLU B 376 ? 1.4305 0.8943 1.2006 0.0122  0.0066  0.0577  376 GLU B OE1 
6667  O OE2 . GLU B 376 ? 1.4761 0.8517 1.2327 -0.0058 0.0050  0.0640  376 GLU B OE2 
6668  N N   . ASN C 6   ? 0.8576 1.0415 0.9299 0.0035  0.3167  0.1279  6   ASN C N   
6669  C CA  . ASN C 6   ? 0.9154 1.1398 1.0131 -0.0071 0.2929  0.1418  6   ASN C CA  
6670  C C   . ASN C 6   ? 0.8829 1.1078 0.9468 -0.0279 0.2776  0.1352  6   ASN C C   
6671  O O   . ASN C 6   ? 0.9334 1.1353 0.9676 -0.0320 0.2861  0.1252  6   ASN C O   
6672  C CB  . ASN C 6   ? 0.8654 1.0812 0.9564 0.0019  0.2848  0.1387  6   ASN C CB  
6673  C CG  . ASN C 6   ? 0.7967 1.0579 0.9498 0.0048  0.2751  0.1620  6   ASN C CG  
6674  O OD1 . ASN C 6   ? 0.7772 1.0829 0.9601 -0.0115 0.2564  0.1789  6   ASN C OD1 
6675  N ND2 . ASN C 6   ? 0.7804 1.0287 0.9507 0.0232  0.2860  0.1628  6   ASN C ND2 
6676  N N   . LYS C 7   ? 0.8153 1.0636 0.8824 -0.0421 0.2558  0.1402  7   LYS C N   
6677  C CA  . LYS C 7   ? 0.7248 0.9690 0.7625 -0.0637 0.2452  0.1323  7   LYS C CA  
6678  C C   . LYS C 7   ? 0.7088 0.9062 0.6927 -0.0600 0.2403  0.1121  7   LYS C C   
6679  O O   . LYS C 7   ? 0.7381 0.9075 0.6896 -0.0631 0.2481  0.1032  7   LYS C O   
6680  C CB  . LYS C 7   ? 0.6995 0.9846 0.7613 -0.0872 0.2227  0.1425  7   LYS C CB  
6681  C CG  . LYS C 7   ? 0.6669 0.9379 0.6948 -0.1119 0.2105  0.1287  7   LYS C CG  
6682  C CD  . LYS C 7   ? 0.7547 0.9884 0.7490 -0.1146 0.2245  0.1156  7   LYS C CD  
6683  C CE  . LYS C 7   ? 0.8148 1.0560 0.8265 -0.1127 0.2412  0.1228  7   LYS C CE  
6684  N NZ  . LYS C 7   ? 0.8276 1.0292 0.8058 -0.1088 0.2570  0.1132  7   LYS C NZ  
6685  N N   . TYR C 8   ? 0.6309 0.8194 0.6077 -0.0533 0.2263  0.1063  8   TYR C N   
6686  C CA  . TYR C 8   ? 0.6106 0.7578 0.5429 -0.0501 0.2191  0.0896  8   TYR C CA  
6687  C C   . TYR C 8   ? 0.6210 0.7407 0.5369 -0.0299 0.2253  0.0829  8   TYR C C   
6688  O O   . TYR C 8   ? 0.5767 0.7101 0.5195 -0.0192 0.2300  0.0890  8   TYR C O   
6689  C CB  . TYR C 8   ? 0.5698 0.7222 0.4998 -0.0617 0.1982  0.0850  8   TYR C CB  
6690  C CG  . TYR C 8   ? 0.5916 0.7679 0.5315 -0.0878 0.1927  0.0882  8   TYR C CG  
6691  C CD1 . TYR C 8   ? 0.5977 0.7539 0.5156 -0.1004 0.1996  0.0807  8   TYR C CD1 
6692  C CD2 . TYR C 8   ? 0.5348 0.7538 0.5053 -0.1023 0.1813  0.0999  8   TYR C CD2 
6693  C CE1 . TYR C 8   ? 0.5830 0.7528 0.5073 -0.1249 0.1960  0.0802  8   TYR C CE1 
6694  C CE2 . TYR C 8   ? 0.5220 0.7599 0.4947 -0.1315 0.1754  0.1009  8   TYR C CE2 
6695  C CZ  . TYR C 8   ? 0.6043 0.8113 0.5532 -0.1405 0.1825  0.0882  8   TYR C CZ  
6696  O OH  . TYR C 8   ? 0.6058 0.8185 0.5553 -0.1653 0.1755  0.0843  8   TYR C OH  
6697  N N   . PRO C 9   ? 0.6363 0.7176 0.5090 -0.0264 0.2249  0.0717  9   PRO C N   
6698  C CA  . PRO C 9   ? 0.6020 0.6563 0.4514 -0.0135 0.2262  0.0634  9   PRO C CA  
6699  C C   . PRO C 9   ? 0.5915 0.6537 0.4539 -0.0101 0.2090  0.0613  9   PRO C C   
6700  O O   . PRO C 9   ? 0.5388 0.6157 0.4122 -0.0193 0.1927  0.0627  9   PRO C O   
6701  C CB  . PRO C 9   ? 0.6148 0.6352 0.4176 -0.0170 0.2216  0.0570  9   PRO C CB  
6702  C CG  . PRO C 9   ? 0.6515 0.6812 0.4622 -0.0291 0.2120  0.0607  9   PRO C CG  
6703  C CD  . PRO C 9   ? 0.5973 0.6597 0.4429 -0.0360 0.2220  0.0684  9   PRO C CD  
6704  N N   . THR C 10  ? 0.5815 0.6300 0.4394 0.0016  0.2148  0.0565  10  THR C N   
6705  C CA  . THR C 10  ? 0.5786 0.6323 0.4485 0.0059  0.1999  0.0546  10  THR C CA  
6706  C C   . THR C 10  ? 0.6070 0.6248 0.4410 0.0127  0.2020  0.0420  10  THR C C   
6707  O O   . THR C 10  ? 0.6553 0.6482 0.4606 0.0139  0.2191  0.0361  10  THR C O   
6708  C CB  . THR C 10  ? 0.5522 0.6398 0.4738 0.0117  0.2058  0.0676  10  THR C CB  
6709  O OG1 . THR C 10  ? 0.6089 0.7117 0.5465 0.0102  0.1862  0.0698  10  THR C OG1 
6710  C CG2 . THR C 10  ? 0.6073 0.6779 0.5345 0.0262  0.2314  0.0657  10  THR C CG2 
6711  N N   . GLU C 11  ? 0.5893 0.6044 0.4225 0.0145  0.1849  0.0378  11  GLU C N   
6712  C CA  . GLU C 11  ? 0.6138 0.5976 0.4130 0.0175  0.1834  0.0261  11  GLU C CA  
6713  C C   . GLU C 11  ? 0.5620 0.5530 0.3777 0.0212  0.1673  0.0246  11  GLU C C   
6714  O O   . GLU C 11  ? 0.5331 0.5458 0.3701 0.0171  0.1513  0.0301  11  GLU C O   
6715  C CB  . GLU C 11  ? 0.7164 0.6772 0.4708 0.0087  0.1731  0.0221  11  GLU C CB  
6716  C CG  . GLU C 11  ? 0.7250 0.6668 0.4524 0.0063  0.1560  0.0155  11  GLU C CG  
6717  C CD  . GLU C 11  ? 0.8375 0.7653 0.5313 -0.0031 0.1435  0.0195  11  GLU C CD  
6718  O OE1 . GLU C 11  ? 0.7761 0.7027 0.4600 -0.0075 0.1521  0.0252  11  GLU C OE1 
6719  O OE2 . GLU C 11  ? 0.7883 0.7093 0.4711 -0.0059 0.1247  0.0196  11  GLU C OE2 
6720  N N   . GLN C 12  ? 0.5454 0.5162 0.3493 0.0268  0.1740  0.0161  12  GLN C N   
6721  C CA  . GLN C 12  ? 0.5589 0.5324 0.3738 0.0299  0.1589  0.0137  12  GLN C CA  
6722  C C   . GLN C 12  ? 0.5867 0.5479 0.3727 0.0222  0.1358  0.0085  12  GLN C C   
6723  O O   . GLN C 12  ? 0.6256 0.5688 0.3762 0.0152  0.1334  0.0057  12  GLN C O   
6724  C CB  . GLN C 12  ? 0.5398 0.4918 0.3505 0.0371  0.1758  0.0053  12  GLN C CB  
6725  C CG  . GLN C 12  ? 0.6047 0.5633 0.4469 0.0462  0.2042  0.0117  12  GLN C CG  
6726  C CD  . GLN C 12  ? 0.5813 0.5664 0.4778 0.0565  0.2042  0.0245  12  GLN C CD  
6727  O OE1 . GLN C 12  ? 0.6630 0.6720 0.5767 0.0538  0.1804  0.0317  12  GLN C OE1 
6728  N NE2 . GLN C 12  ? 0.6881 0.6660 0.6117 0.0676  0.2331  0.0277  12  GLN C NE2 
6729  N N   . LEU C 13  ? 0.5428 0.5165 0.3478 0.0226  0.1190  0.0099  13  LEU C N   
6730  C CA  . LEU C 13  ? 0.5663 0.5304 0.3547 0.0172  0.0990  0.0069  13  LEU C CA  
6731  C C   . LEU C 13  ? 0.6179 0.5556 0.3737 0.0163  0.0971  -0.0023 13  LEU C C   
6732  O O   . LEU C 13  ? 0.6006 0.5316 0.3607 0.0213  0.1037  -0.0085 13  LEU C O   
6733  C CB  . LEU C 13  ? 0.5234 0.5055 0.3407 0.0171  0.0861  0.0092  13  LEU C CB  
6734  C CG  . LEU C 13  ? 0.5535 0.5333 0.3696 0.0109  0.0700  0.0092  13  LEU C CG  
6735  C CD1 . LEU C 13  ? 0.5814 0.5621 0.3951 0.0042  0.0718  0.0145  13  LEU C CD1 
6736  C CD2 . LEU C 13  ? 0.5380 0.5357 0.3814 0.0088  0.0631  0.0098  13  LEU C CD2 
6737  N N   . LYS C 14  ? 0.6135 0.5369 0.3375 0.0081  0.0879  -0.0014 14  LYS C N   
6738  C CA  . LYS C 14  ? 0.6480 0.5489 0.3352 0.0009  0.0824  -0.0084 14  LYS C CA  
6739  C C   . LYS C 14  ? 0.6215 0.5243 0.3217 0.0027  0.0666  -0.0113 14  LYS C C   
6740  O O   . LYS C 14  ? 0.6392 0.5258 0.3209 -0.0001 0.0688  -0.0212 14  LYS C O   
6741  C CB  . LYS C 14  ? 0.6730 0.5662 0.3283 -0.0109 0.0709  -0.0002 14  LYS C CB  
6742  C CG  . LYS C 14  ? 0.7462 0.6304 0.3750 -0.0163 0.0874  0.0007  14  LYS C CG  
6743  C CD  . LYS C 14  ? 0.7470 0.6337 0.3609 -0.0253 0.0737  0.0163  14  LYS C CD  
6744  C CE  . LYS C 14  ? 0.7432 0.6449 0.3865 -0.0184 0.0815  0.0249  14  LYS C CE  
6745  N NZ  . LYS C 14  ? 0.9091 0.8018 0.5246 -0.0246 0.0973  0.0268  14  LYS C NZ  
6746  N N   . LEU C 15  ? 0.5571 0.4775 0.2884 0.0060  0.0532  -0.0042 15  LEU C N   
6747  C CA  . LEU C 15  ? 0.5485 0.4701 0.2917 0.0066  0.0383  -0.0061 15  LEU C CA  
6748  C C   . LEU C 15  ? 0.5212 0.4498 0.2883 0.0145  0.0450  -0.0123 15  LEU C C   
6749  O O   . LEU C 15  ? 0.5191 0.4501 0.2991 0.0153  0.0339  -0.0139 15  LEU C O   
6750  C CB  . LEU C 15  ? 0.4989 0.4318 0.2651 0.0053  0.0255  0.0037  15  LEU C CB  
6751  C CG  . LEU C 15  ? 0.5507 0.4778 0.3006 -0.0015 0.0158  0.0152  15  LEU C CG  
6752  C CD1 . LEU C 15  ? 0.5204 0.4566 0.3020 -0.0004 0.0137  0.0264  15  LEU C CD1 
6753  C CD2 . LEU C 15  ? 0.5469 0.4658 0.2783 -0.0083 -0.0007 0.0168  15  LEU C CD2 
6754  N N   . TRP C 16  ? 0.5216 0.4553 0.2986 0.0202  0.0629  -0.0130 16  TRP C N   
6755  C CA  . TRP C 16  ? 0.5134 0.4578 0.3193 0.0281  0.0696  -0.0129 16  TRP C CA  
6756  C C   . TRP C 16  ? 0.5457 0.4727 0.3423 0.0292  0.0669  -0.0217 16  TRP C C   
6757  O O   . TRP C 16  ? 0.4879 0.4237 0.3049 0.0315  0.0574  -0.0206 16  TRP C O   
6758  C CB  . TRP C 16  ? 0.5757 0.5237 0.3928 0.0345  0.0924  -0.0098 16  TRP C CB  
6759  C CG  . TRP C 16  ? 0.5975 0.5667 0.4575 0.0431  0.0989  -0.0008 16  TRP C CG  
6760  C CD1 . TRP C 16  ? 0.6291 0.5899 0.5049 0.0526  0.1170  -0.0010 16  TRP C CD1 
6761  C CD2 . TRP C 16  ? 0.5837 0.5859 0.4762 0.0407  0.0878  0.0116  16  TRP C CD2 
6762  N NE1 . TRP C 16  ? 0.6269 0.6184 0.5489 0.0582  0.1152  0.0149  16  TRP C NE1 
6763  C CE2 . TRP C 16  ? 0.5695 0.5873 0.4983 0.0489  0.0958  0.0223  16  TRP C CE2 
6764  C CE3 . TRP C 16  ? 0.5780 0.5964 0.4714 0.0302  0.0735  0.0150  16  TRP C CE3 
6765  C CZ2 . TRP C 16  ? 0.5550 0.6087 0.5177 0.0447  0.0857  0.0383  16  TRP C CZ2 
6766  C CZ3 . TRP C 16  ? 0.4749 0.5229 0.3960 0.0244  0.0669  0.0259  16  TRP C CZ3 
6767  C CH2 . TRP C 16  ? 0.4608 0.5289 0.4152 0.0304  0.0706  0.0386  16  TRP C CH2 
6768  N N   . GLY C 17  ? 0.5216 0.4222 0.2836 0.0248  0.0760  -0.0314 17  GLY C N   
6769  C CA  . GLY C 17  ? 0.5867 0.4665 0.3347 0.0227  0.0773  -0.0422 17  GLY C CA  
6770  C C   . GLY C 17  ? 0.6079 0.4917 0.3556 0.0175  0.0522  -0.0417 17  GLY C C   
6771  O O   . GLY C 17  ? 0.5193 0.4009 0.2801 0.0206  0.0494  -0.0455 17  GLY C O   
6772  N N   . LYS C 18  ? 0.5346 0.4248 0.2717 0.0101  0.0350  -0.0352 18  LYS C N   
6773  C CA  . LYS C 18  ? 0.5100 0.4060 0.2554 0.0064  0.0134  -0.0317 18  LYS C CA  
6774  C C   . LYS C 18  ? 0.4777 0.3922 0.2633 0.0146  0.0102  -0.0280 18  LYS C C   
6775  O O   . LYS C 18  ? 0.4979 0.4119 0.2937 0.0144  0.0008  -0.0303 18  LYS C O   
6776  C CB  . LYS C 18  ? 0.4892 0.3897 0.2243 -0.0016 -0.0011 -0.0208 18  LYS C CB  
6777  C CG  . LYS C 18  ? 0.5439 0.4493 0.2910 -0.0058 -0.0215 -0.0146 18  LYS C CG  
6778  C CD  . LYS C 18  ? 0.5882 0.4980 0.3270 -0.0146 -0.0360 0.0008  18  LYS C CD  
6779  C CE  . LYS C 18  ? 0.5913 0.5073 0.3451 -0.0195 -0.0560 0.0100  18  LYS C CE  
6780  N NZ  . LYS C 18  ? 0.6527 0.5761 0.3997 -0.0289 -0.0699 0.0304  18  LYS C NZ  
6781  N N   . ALA C 19  ? 0.4164 0.3474 0.2231 0.0193  0.0182  -0.0222 19  ALA C N   
6782  C CA  . ALA C 19  ? 0.4554 0.4043 0.2933 0.0212  0.0149  -0.0187 19  ALA C CA  
6783  C C   . ALA C 19  ? 0.4326 0.3810 0.2820 0.0267  0.0187  -0.0219 19  ALA C C   
6784  O O   . ALA C 19  ? 0.4001 0.3530 0.2633 0.0256  0.0102  -0.0222 19  ALA C O   
6785  C CB  . ALA C 19  ? 0.4256 0.3939 0.2794 0.0203  0.0229  -0.0116 19  ALA C CB  
6786  N N   . LYS C 20  ? 0.4510 0.3904 0.2946 0.0325  0.0338  -0.0242 20  LYS C N   
6787  C CA  . LYS C 20  ? 0.4596 0.3957 0.3189 0.0393  0.0417  -0.0252 20  LYS C CA  
6788  C C   . LYS C 20  ? 0.4390 0.3543 0.2814 0.0358  0.0337  -0.0359 20  LYS C C   
6789  O O   . LYS C 20  ? 0.4697 0.3884 0.3303 0.0386  0.0300  -0.0350 20  LYS C O   
6790  C CB  . LYS C 20  ? 0.4922 0.4184 0.3524 0.0466  0.0658  -0.0254 20  LYS C CB  
6791  C CG  . LYS C 20  ? 0.5222 0.4729 0.4071 0.0509  0.0750  -0.0119 20  LYS C CG  
6792  C CD  . LYS C 20  ? 0.5862 0.5702 0.5103 0.0522  0.0665  0.0038  20  LYS C CD  
6793  C CE  . LYS C 20  ? 0.6274 0.6353 0.5852 0.0585  0.0809  0.0208  20  LYS C CE  
6794  N NZ  . LYS C 20  ? 0.5711 0.6188 0.5616 0.0527  0.0680  0.0396  20  LYS C NZ  
6795  N N   . GLU C 21  ? 0.4917 0.3873 0.2992 0.0276  0.0301  -0.0444 21  GLU C N   
6796  C CA  . GLU C 21  ? 0.5252 0.4024 0.3140 0.0205  0.0217  -0.0537 21  GLU C CA  
6797  C C   . GLU C 21  ? 0.4483 0.3390 0.2543 0.0182  0.0008  -0.0490 21  GLU C C   
6798  O O   . GLU C 21  ? 0.4915 0.3764 0.3036 0.0178  -0.0036 -0.0534 21  GLU C O   
6799  C CB  . GLU C 21  ? 0.5487 0.4062 0.2933 0.0070  0.0199  -0.0607 21  GLU C CB  
6800  C CG  . GLU C 21  ? 0.7163 0.5659 0.4431 -0.0058 0.0008  -0.0643 21  GLU C CG  
6801  C CD  . GLU C 21  ? 0.9271 0.7607 0.6051 -0.0249 -0.0037 -0.0682 21  GLU C CD  
6802  O OE1 . GLU C 21  ? 0.9674 0.8142 0.6401 -0.0328 -0.0232 -0.0561 21  GLU C OE1 
6803  O OE2 . GLU C 21  ? 1.0155 0.8224 0.6608 -0.0337 0.0137  -0.0826 21  GLU C OE2 
6804  N N   . LEU C 22  ? 0.4216 0.3287 0.2384 0.0169  -0.0091 -0.0402 22  LEU C N   
6805  C CA  . LEU C 22  ? 0.4300 0.3467 0.2671 0.0148  -0.0229 -0.0363 22  LEU C CA  
6806  C C   . LEU C 22  ? 0.3800 0.3060 0.2422 0.0194  -0.0197 -0.0366 22  LEU C C   
6807  O O   . LEU C 22  ? 0.4101 0.3348 0.2824 0.0175  -0.0275 -0.0385 22  LEU C O   
6808  C CB  . LEU C 22  ? 0.3765 0.3047 0.2241 0.0126  -0.0265 -0.0273 22  LEU C CB  
6809  C CG  . LEU C 22  ? 0.4090 0.3319 0.2390 0.0068  -0.0350 -0.0212 22  LEU C CG  
6810  C CD1 . LEU C 22  ? 0.4405 0.3733 0.2852 0.0076  -0.0305 -0.0123 22  LEU C CD1 
6811  C CD2 . LEU C 22  ? 0.4186 0.3397 0.2523 0.0006  -0.0519 -0.0161 22  LEU C CD2 
6812  N N   . ARG C 23  ? 0.3406 0.2780 0.2140 0.0242  -0.0088 -0.0325 23  ARG C N   
6813  C CA  . ARG C 23  ? 0.3842 0.3352 0.2810 0.0260  -0.0074 -0.0280 23  ARG C CA  
6814  C C   . ARG C 23  ? 0.3473 0.2849 0.2452 0.0313  -0.0040 -0.0324 23  ARG C C   
6815  O O   . ARG C 23  ? 0.3647 0.3057 0.2760 0.0302  -0.0094 -0.0316 23  ARG C O   
6816  C CB  . ARG C 23  ? 0.3841 0.3552 0.2951 0.0282  0.0019  -0.0176 23  ARG C CB  
6817  C CG  . ARG C 23  ? 0.3413 0.3318 0.2775 0.0280  0.0016  -0.0072 23  ARG C CG  
6818  C CD  . ARG C 23  ? 0.3452 0.3635 0.2995 0.0264  0.0068  0.0080  23  ARG C CD  
6819  N NE  . ARG C 23  ? 0.3643 0.4048 0.3460 0.0260  0.0050  0.0237  23  ARG C NE  
6820  C CZ  . ARG C 23  ? 0.4213 0.4619 0.4248 0.0388  0.0151  0.0332  23  ARG C CZ  
6821  N NH1 . ARG C 23  ? 0.4174 0.4344 0.4147 0.0511  0.0305  0.0254  23  ARG C NH1 
6822  N NH2 . ARG C 23  ? 0.3932 0.4582 0.4262 0.0377  0.0117  0.0525  23  ARG C NH2 
6823  N N   . GLU C 24  ? 0.3874 0.3075 0.2705 0.0356  0.0076  -0.0378 24  GLU C N   
6824  C CA  . GLU C 24  ? 0.3975 0.2996 0.2812 0.0391  0.0152  -0.0439 24  GLU C CA  
6825  C C   . GLU C 24  ? 0.4384 0.3274 0.3079 0.0311  0.0013  -0.0532 24  GLU C C   
6826  O O   . GLU C 24  ? 0.4204 0.3038 0.3008 0.0326  0.0013  -0.0552 24  GLU C O   
6827  C CB  . GLU C 24  ? 0.4948 0.3735 0.3610 0.0420  0.0360  -0.0514 24  GLU C CB  
6828  C CG  . GLU C 24  ? 0.5579 0.4484 0.4467 0.0522  0.0543  -0.0404 24  GLU C CG  
6829  C CD  . GLU C 24  ? 0.7181 0.6164 0.6472 0.0636  0.0672  -0.0284 24  GLU C CD  
6830  O OE1 . GLU C 24  ? 0.7891 0.7114 0.7496 0.0710  0.0745  -0.0111 24  GLU C OE1 
6831  O OE2 . GLU C 24  ? 0.7692 0.6525 0.7021 0.0647  0.0693  -0.0332 24  GLU C OE2 
6832  N N   . GLN C 25  ? 0.4110 0.2954 0.2580 0.0223  -0.0102 -0.0570 25  GLN C N   
6833  C CA  . GLN C 25  ? 0.4409 0.3189 0.2805 0.0136  -0.0257 -0.0613 25  GLN C CA  
6834  C C   . GLN C 25  ? 0.4142 0.3072 0.2830 0.0153  -0.0350 -0.0559 25  GLN C C   
6835  O O   . GLN C 25  ? 0.4352 0.3221 0.3080 0.0120  -0.0417 -0.0598 25  GLN C O   
6836  C CB  . GLN C 25  ? 0.4361 0.3150 0.2566 0.0039  -0.0387 -0.0584 25  GLN C CB  
6837  C CG  . GLN C 25  ? 0.5518 0.4198 0.3545 -0.0086 -0.0514 -0.0628 25  GLN C CG  
6838  C CD  . GLN C 25  ? 0.7026 0.5438 0.4689 -0.0170 -0.0393 -0.0770 25  GLN C CD  
6839  O OE1 . GLN C 25  ? 0.7314 0.5582 0.5006 -0.0150 -0.0294 -0.0862 25  GLN C OE1 
6840  N NE2 . GLN C 25  ? 0.7979 0.6300 0.5289 -0.0279 -0.0377 -0.0790 25  GLN C NE2 
6841  N N   . TYR C 26  ? 0.3750 0.2863 0.2615 0.0178  -0.0344 -0.0480 26  TYR C N   
6842  C CA  . TYR C 26  ? 0.3447 0.2669 0.2534 0.0155  -0.0392 -0.0449 26  TYR C CA  
6843  C C   . TYR C 26  ? 0.3694 0.2906 0.2889 0.0184  -0.0358 -0.0457 26  TYR C C   
6844  O O   . TYR C 26  ? 0.3606 0.2782 0.2878 0.0151  -0.0418 -0.0485 26  TYR C O   
6845  C CB  . TYR C 26  ? 0.3399 0.2786 0.2586 0.0131  -0.0350 -0.0385 26  TYR C CB  
6846  C CG  . TYR C 26  ? 0.3477 0.2961 0.2827 0.0063  -0.0350 -0.0369 26  TYR C CG  
6847  C CD1 . TYR C 26  ? 0.3383 0.2830 0.2826 -0.0004 -0.0369 -0.0393 26  TYR C CD1 
6848  C CD2 . TYR C 26  ? 0.2812 0.2428 0.2236 0.0049  -0.0315 -0.0312 26  TYR C CD2 
6849  C CE1 . TYR C 26  ? 0.3202 0.2695 0.2743 -0.0102 -0.0327 -0.0403 26  TYR C CE1 
6850  C CE2 . TYR C 26  ? 0.2870 0.2583 0.2375 -0.0067 -0.0317 -0.0293 26  TYR C CE2 
6851  C CZ  . TYR C 26  ? 0.3284 0.2909 0.2813 -0.0152 -0.0310 -0.0362 26  TYR C CZ  
6852  O OH  . TYR C 26  ? 0.3117 0.2791 0.2672 -0.0299 -0.0272 -0.0371 26  TYR C OH  
6853  N N   . TYR C 27  ? 0.3879 0.3129 0.3119 0.0250  -0.0252 -0.0411 27  TYR C N   
6854  C CA  . TYR C 27  ? 0.3705 0.2962 0.3107 0.0291  -0.0208 -0.0370 27  TYR C CA  
6855  C C   . TYR C 27  ? 0.4133 0.3138 0.3433 0.0306  -0.0184 -0.0478 27  TYR C C   
6856  O O   . TYR C 27  ? 0.3894 0.2867 0.3306 0.0303  -0.0200 -0.0477 27  TYR C O   
6857  C CB  . TYR C 27  ? 0.3363 0.2757 0.2925 0.0367  -0.0090 -0.0241 27  TYR C CB  
6858  C CG  . TYR C 27  ? 0.3313 0.2999 0.2989 0.0300  -0.0142 -0.0117 27  TYR C CG  
6859  C CD1 . TYR C 27  ? 0.3109 0.2952 0.2888 0.0201  -0.0225 -0.0052 27  TYR C CD1 
6860  C CD2 . TYR C 27  ? 0.3266 0.3061 0.2913 0.0303  -0.0099 -0.0072 27  TYR C CD2 
6861  C CE1 . TYR C 27  ? 0.2949 0.3039 0.2756 0.0076  -0.0263 0.0041  27  TYR C CE1 
6862  C CE2 . TYR C 27  ? 0.3317 0.3375 0.3032 0.0198  -0.0145 0.0030  27  TYR C CE2 
6863  C CZ  . TYR C 27  ? 0.3082 0.3278 0.2858 0.0072  -0.0225 0.0079  27  TYR C CZ  
6864  O OH  . TYR C 27  ? 0.2870 0.3305 0.2648 -0.0089 -0.0260 0.0163  27  TYR C OH  
6865  N N   A MET C 28  ? 0.4071 0.2885 0.3128 0.0292  -0.0142 -0.0575 28  MET C N   
6866  N N   B MET C 28  ? 0.4075 0.2890 0.3132 0.0292  -0.0141 -0.0575 28  MET C N   
6867  C CA  A MET C 28  ? 0.4555 0.3115 0.3457 0.0248  -0.0117 -0.0696 28  MET C CA  
6868  C CA  B MET C 28  ? 0.4558 0.3118 0.3449 0.0246  -0.0120 -0.0697 28  MET C CA  
6869  C C   A MET C 28  ? 0.4493 0.3069 0.3381 0.0154  -0.0302 -0.0730 28  MET C C   
6870  C C   B MET C 28  ? 0.4488 0.3070 0.3384 0.0157  -0.0301 -0.0727 28  MET C C   
6871  O O   A MET C 28  ? 0.4566 0.3033 0.3488 0.0130  -0.0309 -0.0781 28  MET C O   
6872  O O   B MET C 28  ? 0.4545 0.3028 0.3492 0.0139  -0.0305 -0.0771 28  MET C O   
6873  C CB  A MET C 28  ? 0.4901 0.3240 0.3475 0.0199  -0.0015 -0.0800 28  MET C CB  
6874  C CB  B MET C 28  ? 0.4902 0.3259 0.3452 0.0184  -0.0045 -0.0800 28  MET C CB  
6875  C CG  A MET C 28  ? 0.5058 0.3263 0.3675 0.0293  0.0251  -0.0804 28  MET C CG  
6876  C CG  B MET C 28  ? 0.5417 0.3556 0.3684 0.0039  -0.0109 -0.0930 28  MET C CG  
6877  S SD  A MET C 28  ? 0.6290 0.4518 0.5337 0.0441  0.0415  -0.0694 28  MET C SD  
6878  S SD  B MET C 28  ? 0.6319 0.4142 0.4111 -0.0085 0.0056  -0.1079 28  MET C SD  
6879  C CE  A MET C 28  ? 0.6247 0.4177 0.5142 0.0347  0.0414  -0.0852 28  MET C CE  
6880  C CE  B MET C 28  ? 0.6618 0.4355 0.4074 -0.0335 -0.0163 -0.1160 28  MET C CE  
6881  N N   . ASN C 29  ? 0.4453 0.3168 0.3345 0.0108  -0.0434 -0.0686 29  ASN C N   
6882  C CA  . ASN C 29  ? 0.4283 0.3035 0.3255 0.0033  -0.0586 -0.0682 29  ASN C CA  
6883  C C   . ASN C 29  ? 0.4133 0.2952 0.3360 0.0058  -0.0583 -0.0660 29  ASN C C   
6884  O O   . ASN C 29  ? 0.4226 0.2996 0.3518 0.0009  -0.0651 -0.0690 29  ASN C O   
6885  C CB  . ASN C 29  ? 0.4280 0.3174 0.3308 0.0007  -0.0675 -0.0599 29  ASN C CB  
6886  C CG  . ASN C 29  ? 0.4560 0.3403 0.3331 -0.0059 -0.0733 -0.0595 29  ASN C CG  
6887  O OD1 . ASN C 29  ? 0.5528 0.4215 0.4034 -0.0135 -0.0734 -0.0674 29  ASN C OD1 
6888  N ND2 . ASN C 29  ? 0.5358 0.4319 0.4179 -0.0054 -0.0767 -0.0502 29  ASN C ND2 
6889  N N   . TYR C 30  ? 0.3801 0.2742 0.3159 0.0109  -0.0509 -0.0598 30  TYR C N   
6890  C CA  . TYR C 30  ? 0.3700 0.2704 0.3243 0.0094  -0.0506 -0.0570 30  TYR C CA  
6891  C C   . TYR C 30  ? 0.3983 0.2853 0.3537 0.0123  -0.0467 -0.0603 30  TYR C C   
6892  O O   . TYR C 30  ? 0.4089 0.2916 0.3727 0.0083  -0.0509 -0.0631 30  TYR C O   
6893  C CB  . TYR C 30  ? 0.3528 0.2715 0.3156 0.0093  -0.0451 -0.0476 30  TYR C CB  
6894  C CG  . TYR C 30  ? 0.3098 0.2363 0.2854 0.0028  -0.0454 -0.0435 30  TYR C CG  
6895  C CD1 . TYR C 30  ? 0.3334 0.2618 0.3134 -0.0074 -0.0469 -0.0468 30  TYR C CD1 
6896  C CD2 . TYR C 30  ? 0.3275 0.2598 0.3122 0.0058  -0.0421 -0.0343 30  TYR C CD2 
6897  C CE1 . TYR C 30  ? 0.3553 0.2891 0.3412 -0.0172 -0.0450 -0.0443 30  TYR C CE1 
6898  C CE2 . TYR C 30  ? 0.3592 0.3017 0.3521 -0.0038 -0.0437 -0.0281 30  TYR C CE2 
6899  C CZ  . TYR C 30  ? 0.3664 0.3081 0.3560 -0.0164 -0.0452 -0.0350 30  TYR C CZ  
6900  O OH  . TYR C 30  ? 0.4342 0.3823 0.4258 -0.0294 -0.0446 -0.0313 30  TYR C OH  
6901  N N   . ALA C 31  ? 0.3922 0.2702 0.3412 0.0193  -0.0359 -0.0603 31  ALA C N   
6902  C CA  . ALA C 31  ? 0.4007 0.2610 0.3528 0.0228  -0.0267 -0.0637 31  ALA C CA  
6903  C C   . ALA C 31  ? 0.4285 0.2678 0.3638 0.0140  -0.0323 -0.0777 31  ALA C C   
6904  O O   . ALA C 31  ? 0.4429 0.2714 0.3853 0.0126  -0.0302 -0.0809 31  ALA C O   
6905  C CB  . ALA C 31  ? 0.4104 0.2609 0.3620 0.0321  -0.0083 -0.0613 31  ALA C CB  
6906  N N   . ARG C 32  ? 0.3614 0.2818 0.3002 0.0130  -0.0562 -0.0497 32  ARG C N   
6907  C CA  . ARG C 32  ? 0.3730 0.2889 0.3088 0.0118  -0.0661 -0.0549 32  ARG C CA  
6908  C C   . ARG C 32  ? 0.4001 0.3246 0.3486 0.0084  -0.0723 -0.0532 32  ARG C C   
6909  O O   . ARG C 32  ? 0.4222 0.3446 0.3703 0.0071  -0.0816 -0.0574 32  ARG C O   
6910  C CB  . ARG C 32  ? 0.4425 0.3498 0.3566 0.0170  -0.0686 -0.0582 32  ARG C CB  
6911  C CG  . ARG C 32  ? 0.4911 0.3902 0.3918 0.0213  -0.0612 -0.0594 32  ARG C CG  
6912  C CD  . ARG C 32  ? 0.5459 0.4343 0.4241 0.0264  -0.0643 -0.0637 32  ARG C CD  
6913  N NE  . ARG C 32  ? 0.6630 0.5421 0.5362 0.0251  -0.0736 -0.0712 32  ARG C NE  
6914  C CZ  . ARG C 32  ? 0.7108 0.5809 0.5659 0.0282  -0.0804 -0.0759 32  ARG C CZ  
6915  N NH1 . ARG C 32  ? 0.7466 0.6157 0.5863 0.0333  -0.0788 -0.0735 32  ARG C NH1 
6916  N NH2 . ARG C 32  ? 0.7309 0.5920 0.5824 0.0264  -0.0891 -0.0833 32  ARG C NH2 
6917  N N   . ALA C 33  ? 0.3861 0.3201 0.3469 0.0068  -0.0675 -0.0474 33  ALA C N   
6918  C CA  . ALA C 33  ? 0.3869 0.3294 0.3593 0.0047  -0.0717 -0.0449 33  ALA C CA  
6919  C C   . ALA C 33  ? 0.3846 0.3287 0.3700 0.0003  -0.0798 -0.0482 33  ALA C C   
6920  O O   . ALA C 33  ? 0.4028 0.3518 0.3931 -0.0002 -0.0866 -0.0483 33  ALA C O   
6921  C CB  . ALA C 33  ? 0.4169 0.3674 0.4007 0.0035  -0.0643 -0.0388 33  ALA C CB  
6922  N N   . LYS C 34  ? 0.3868 0.3267 0.3783 -0.0028 -0.0792 -0.0509 34  LYS C N   
6923  C CA  . LYS C 34  ? 0.4320 0.3740 0.4389 -0.0079 -0.0858 -0.0533 34  LYS C CA  
6924  C C   . LYS C 34  ? 0.4500 0.3848 0.4499 -0.0085 -0.0962 -0.0604 34  LYS C C   
6925  O O   . LYS C 34  ? 0.4788 0.4169 0.4926 -0.0130 -0.1035 -0.0626 34  LYS C O   
6926  C CB  . LYS C 34  ? 0.4188 0.3590 0.4367 -0.0114 -0.0801 -0.0525 34  LYS C CB  
6927  C CG  . LYS C 34  ? 0.3943 0.3421 0.4222 -0.0118 -0.0719 -0.0459 34  LYS C CG  
6928  C CD  . LYS C 34  ? 0.4354 0.3938 0.4776 -0.0138 -0.0746 -0.0427 34  LYS C CD  
6929  C CE  . LYS C 34  ? 0.3785 0.3430 0.4275 -0.0134 -0.0661 -0.0364 34  LYS C CE  
6930  N NZ  . LYS C 34  ? 0.3289 0.3033 0.3915 -0.0145 -0.0678 -0.0331 34  LYS C NZ  
6931  N N   . GLU C 35  ? 0.4367 0.3619 0.4155 -0.0042 -0.0972 -0.0641 35  GLU C N   
6932  C CA  . GLU C 35  ? 0.4677 0.3845 0.4368 -0.0042 -0.1076 -0.0714 35  GLU C CA  
6933  C C   . GLU C 35  ? 0.4790 0.4029 0.4552 -0.0056 -0.1184 -0.0722 35  GLU C C   
6934  O O   . GLU C 35  ? 0.4800 0.4012 0.4609 -0.0091 -0.1284 -0.0778 35  GLU C O   
6935  C CB  . GLU C 35  ? 0.4914 0.3974 0.4344 0.0022  -0.1058 -0.0740 35  GLU C CB  
6936  C CG  . GLU C 35  ? 0.5615 0.4604 0.4990 0.0037  -0.0961 -0.0739 35  GLU C CG  
6937  C CD  . GLU C 35  ? 0.5932 0.4814 0.5060 0.0102  -0.0930 -0.0763 35  GLU C CD  
6938  O OE1 . GLU C 35  ? 0.6630 0.5482 0.5611 0.0137  -0.0986 -0.0783 35  GLU C OE1 
6939  O OE2 . GLU C 35  ? 0.6005 0.4836 0.5089 0.0123  -0.0847 -0.0759 35  GLU C OE2 
6940  N N   . LYS C 36  ? 0.4523 0.3851 0.4293 -0.0028 -0.1168 -0.0668 36  LYS C N   
6941  C CA  . LYS C 36  ? 0.4354 0.3760 0.4197 -0.0032 -0.1266 -0.0667 36  LYS C CA  
6942  C C   . LYS C 36  ? 0.4442 0.3986 0.4509 -0.0058 -0.1228 -0.0603 36  LYS C C   
6943  O O   . LYS C 36  ? 0.4372 0.3997 0.4486 -0.0041 -0.1270 -0.0575 36  LYS C O   
6944  C CB  . LYS C 36  ? 0.4839 0.4213 0.4472 0.0034  -0.1295 -0.0663 36  LYS C CB  
6945  C CG  . LYS C 36  ? 0.5690 0.4922 0.5083 0.0067  -0.1345 -0.0730 36  LYS C CG  
6946  C CD  . LYS C 36  ? 0.6775 0.5957 0.6211 0.0023  -0.1465 -0.0810 36  LYS C CD  
6947  C CE  . LYS C 36  ? 0.6395 0.5682 0.5999 -0.0009 -0.1591 -0.0817 36  LYS C CE  
6948  N NZ  . LYS C 36  ? 0.6201 0.5408 0.5754 -0.0032 -0.1729 -0.0906 36  LYS C NZ  
6949  N N   . GLY C 37  ? 0.4050 0.3617 0.4249 -0.0094 -0.1146 -0.0577 37  GLY C N   
6950  C CA  . GLY C 37  ? 0.4010 0.3695 0.4424 -0.0121 -0.1111 -0.0523 37  GLY C CA  
6951  C C   . GLY C 37  ? 0.3666 0.3403 0.4046 -0.0080 -0.1033 -0.0458 37  GLY C C   
6952  O O   . GLY C 37  ? 0.3582 0.3417 0.4108 -0.0087 -0.1021 -0.0414 37  GLY C O   
6953  N N   . GLY C 38  ? 0.3526 0.3197 0.3726 -0.0041 -0.0971 -0.0449 38  GLY C N   
6954  C CA  . GLY C 38  ? 0.3293 0.3003 0.3465 -0.0011 -0.0893 -0.0390 38  GLY C CA  
6955  C C   . GLY C 38  ? 0.3664 0.3414 0.3959 -0.0036 -0.0801 -0.0348 38  GLY C C   
6956  O O   . GLY C 38  ? 0.3463 0.3208 0.3862 -0.0074 -0.0787 -0.0359 38  GLY C O   
6957  N N   . ILE C 39  ? 0.3595 0.3374 0.3864 -0.0011 -0.0737 -0.0299 39  ILE C N   
6958  C CA  . ILE C 39  ? 0.3285 0.3093 0.3635 -0.0025 -0.0650 -0.0258 39  ILE C CA  
6959  C C   . ILE C 39  ? 0.3383 0.3137 0.3604 -0.0006 -0.0582 -0.0250 39  ILE C C   
6960  O O   . ILE C 39  ? 0.3810 0.3531 0.3894 0.0026  -0.0580 -0.0250 39  ILE C O   
6961  C CB  . ILE C 39  ? 0.3579 0.3459 0.4006 -0.0012 -0.0632 -0.0211 39  ILE C CB  
6962  C CG1 . ILE C 39  ? 0.3566 0.3517 0.4164 -0.0035 -0.0688 -0.0213 39  ILE C CG1 
6963  C CG2 . ILE C 39  ? 0.3601 0.3492 0.4057 -0.0016 -0.0541 -0.0170 39  ILE C CG2 
6964  C CD1 . ILE C 39  ? 0.3743 0.3763 0.4408 -0.0012 -0.0681 -0.0171 39  ILE C CD1 
6965  N N   . ARG C 40  ? 0.2921 0.2664 0.3187 -0.0026 -0.0527 -0.0241 40  ARG C N   
6966  C CA  . ARG C 40  ? 0.3151 0.2865 0.3339 -0.0013 -0.0458 -0.0225 40  ARG C CA  
6967  C C   . ARG C 40  ? 0.3274 0.3030 0.3532 -0.0020 -0.0400 -0.0180 40  ARG C C   
6968  O O   . ARG C 40  ? 0.3038 0.2820 0.3412 -0.0043 -0.0391 -0.0169 40  ARG C O   
6969  C CB  . ARG C 40  ? 0.3494 0.3157 0.3675 -0.0024 -0.0443 -0.0251 40  ARG C CB  
6970  C CG  . ARG C 40  ? 0.4204 0.3802 0.4277 -0.0009 -0.0480 -0.0296 40  ARG C CG  
6971  C CD  . ARG C 40  ? 0.4337 0.3882 0.4371 -0.0003 -0.0439 -0.0309 40  ARG C CD  
6972  N NE  . ARG C 40  ? 0.4553 0.4070 0.4674 -0.0034 -0.0454 -0.0328 40  ARG C NE  
6973  C CZ  . ARG C 40  ? 0.4219 0.3669 0.4311 -0.0040 -0.0497 -0.0377 40  ARG C CZ  
6974  N NH1 . ARG C 40  ? 0.4917 0.4315 0.4880 -0.0014 -0.0533 -0.0415 40  ARG C NH1 
6975  N NH2 . ARG C 40  ? 0.4300 0.3723 0.4487 -0.0073 -0.0503 -0.0388 40  ARG C NH2 
6976  N N   . TRP C 41  ? 0.2987 0.2741 0.3175 -0.0002 -0.0356 -0.0156 41  TRP C N   
6977  C CA  . TRP C 41  ? 0.2732 0.2507 0.2966 -0.0010 -0.0302 -0.0121 41  TRP C CA  
6978  C C   . TRP C 41  ? 0.2749 0.2504 0.2904 0.0000  -0.0259 -0.0113 41  TRP C C   
6979  O O   . TRP C 41  ? 0.2764 0.2498 0.2833 0.0017  -0.0262 -0.0125 41  TRP C O   
6980  C CB  . TRP C 41  ? 0.2845 0.2656 0.3117 -0.0003 -0.0297 -0.0093 41  TRP C CB  
6981  C CG  . TRP C 41  ? 0.2844 0.2647 0.3030 0.0020  -0.0303 -0.0085 41  TRP C CG  
6982  C CD1 . TRP C 41  ? 0.2956 0.2758 0.3103 0.0037  -0.0353 -0.0097 41  TRP C CD1 
6983  C CD2 . TRP C 41  ? 0.2971 0.2760 0.3094 0.0029  -0.0260 -0.0062 41  TRP C CD2 
6984  N NE1 . TRP C 41  ? 0.2870 0.2653 0.2928 0.0060  -0.0335 -0.0078 41  TRP C NE1 
6985  C CE2 . TRP C 41  ? 0.3147 0.2922 0.3196 0.0051  -0.0278 -0.0058 41  TRP C CE2 
6986  C CE3 . TRP C 41  ? 0.3183 0.2964 0.3302 0.0019  -0.0213 -0.0047 41  TRP C CE3 
6987  C CZ2 . TRP C 41  ? 0.3060 0.2812 0.3042 0.0060  -0.0241 -0.0035 41  TRP C CZ2 
6988  C CZ3 . TRP C 41  ? 0.3093 0.2856 0.3148 0.0025  -0.0185 -0.0029 41  TRP C CZ3 
6989  C CH2 . TRP C 41  ? 0.3030 0.2778 0.3021 0.0043  -0.0196 -0.0023 41  TRP C CH2 
6990  N N   . SER C 42  ? 0.2430 0.2192 0.2615 -0.0008 -0.0220 -0.0092 42  SER C N   
6991  C CA  . SER C 42  ? 0.2773 0.2527 0.2903 -0.0002 -0.0188 -0.0085 42  SER C CA  
6992  C C   . SER C 42  ? 0.3083 0.2849 0.3218 -0.0006 -0.0159 -0.0057 42  SER C C   
6993  O O   . SER C 42  ? 0.3026 0.2798 0.3208 -0.0012 -0.0151 -0.0043 42  SER C O   
6994  C CB  . SER C 42  ? 0.4045 0.3785 0.4187 -0.0003 -0.0174 -0.0092 42  SER C CB  
6995  O OG  . SER C 42  ? 0.4737 0.4474 0.4948 -0.0016 -0.0172 -0.0085 42  SER C OG  
6996  N N   . GLY C 43  ? 0.3064 0.2830 0.3150 -0.0003 -0.0141 -0.0050 43  GLY C N   
6997  C CA  . GLY C 43  ? 0.2777 0.2543 0.2855 -0.0010 -0.0119 -0.0030 43  GLY C CA  
6998  C C   . GLY C 43  ? 0.2931 0.2700 0.2967 -0.0012 -0.0105 -0.0026 43  GLY C C   
6999  O O   . GLY C 43  ? 0.2759 0.2531 0.2771 -0.0002 -0.0105 -0.0036 43  GLY C O   
7000  N N   . SER C 44  ? 0.2762 0.2526 0.2791 -0.0024 -0.0090 -0.0013 44  SER C N   
7001  C CA  . SER C 44  ? 0.2379 0.2148 0.2387 -0.0033 -0.0074 -0.0006 44  SER C CA  
7002  C C   . SER C 44  ? 0.2743 0.2498 0.2709 -0.0023 -0.0067 0.0000  44  SER C C   
7003  O O   . SER C 44  ? 0.2657 0.2391 0.2602 -0.0011 -0.0079 0.0003  44  SER C O   
7004  C CB  . SER C 44  ? 0.2660 0.2412 0.2666 -0.0052 -0.0067 0.0003  44  SER C CB  
7005  O OG  . SER C 44  ? 0.2912 0.2668 0.2914 -0.0070 -0.0053 0.0011  44  SER C OG  
7006  N N   . ALA C 45  ? 0.2733 0.2497 0.2688 -0.0028 -0.0045 0.0008  45  ALA C N   
7007  C CA  . ALA C 45  ? 0.2729 0.2468 0.2634 -0.0022 -0.0025 0.0023  45  ALA C CA  
7008  C C   . ALA C 45  ? 0.2982 0.2684 0.2873 -0.0032 -0.0023 0.0038  45  ALA C C   
7009  O O   . ALA C 45  ? 0.2923 0.2591 0.2764 -0.0019 -0.0015 0.0053  45  ALA C O   
7010  C CB  . ALA C 45  ? 0.2948 0.2708 0.2862 -0.0032 0.0010  0.0035  45  ALA C CB  
7011  N N   . TRP C 46  ? 0.2624 0.2323 0.2547 -0.0051 -0.0030 0.0035  46  TRP C N   
7012  C CA  . TRP C 46  ? 0.2875 0.2527 0.2778 -0.0058 -0.0025 0.0045  46  TRP C CA  
7013  C C   . TRP C 46  ? 0.3122 0.2762 0.3026 -0.0036 -0.0041 0.0042  46  TRP C C   
7014  O O   . TRP C 46  ? 0.2835 0.2433 0.2722 -0.0033 -0.0034 0.0051  46  TRP C O   
7015  C CB  . TRP C 46  ? 0.2570 0.2215 0.2496 -0.0089 -0.0023 0.0039  46  TRP C CB  
7016  C CG  . TRP C 46  ? 0.2985 0.2634 0.2924 -0.0116 -0.0006 0.0047  46  TRP C CG  
7017  C CD1 . TRP C 46  ? 0.2989 0.2630 0.2912 -0.0116 0.0021  0.0066  46  TRP C CD1 
7018  C CD2 . TRP C 46  ? 0.2974 0.2638 0.2952 -0.0150 -0.0014 0.0039  46  TRP C CD2 
7019  N NE1 . TRP C 46  ? 0.3007 0.2659 0.2970 -0.0152 0.0037  0.0072  46  TRP C NE1 
7020  C CE2 . TRP C 46  ? 0.3097 0.2767 0.3099 -0.0175 0.0010  0.0053  46  TRP C CE2 
7021  C CE3 . TRP C 46  ? 0.2950 0.2618 0.2941 -0.0162 -0.0041 0.0022  46  TRP C CE3 
7022  C CZ2 . TRP C 46  ? 0.3025 0.2716 0.3084 -0.0215 0.0003  0.0049  46  TRP C CZ2 
7023  C CZ3 . TRP C 46  ? 0.3252 0.2936 0.3281 -0.0197 -0.0055 0.0015  46  TRP C CZ3 
7024  C CH2 . TRP C 46  ? 0.3227 0.2927 0.3299 -0.0226 -0.0035 0.0028  46  TRP C CH2 
7025  N N   . ALA C 47  ? 0.2666 0.2339 0.2594 -0.0020 -0.0061 0.0031  47  ALA C N   
7026  C CA  . ALA C 47  ? 0.2520 0.2193 0.2467 0.0000  -0.0076 0.0033  47  ALA C CA  
7027  C C   . ALA C 47  ? 0.2736 0.2384 0.2647 0.0021  -0.0079 0.0049  47  ALA C C   
7028  O O   . ALA C 47  ? 0.3244 0.2880 0.3107 0.0027  -0.0076 0.0055  47  ALA C O   
7029  C CB  . ALA C 47  ? 0.2705 0.2416 0.2690 0.0007  -0.0101 0.0017  47  ALA C CB  
7030  N N   . LEU C 48  ? 0.3002 0.2642 0.2936 0.0037  -0.0081 0.0058  48  LEU C N   
7031  C CA  . LEU C 48  ? 0.2970 0.2588 0.2878 0.0065  -0.0087 0.0077  48  LEU C CA  
7032  C C   . LEU C 48  ? 0.2923 0.2583 0.2854 0.0086  -0.0130 0.0070  48  LEU C C   
7033  O O   . LEU C 48  ? 0.2840 0.2532 0.2833 0.0102  -0.0151 0.0072  48  LEU C O   
7034  C CB  . LEU C 48  ? 0.2687 0.2274 0.2610 0.0079  -0.0067 0.0092  48  LEU C CB  
7035  C CG  . LEU C 48  ? 0.3137 0.2651 0.2994 0.0070  -0.0035 0.0104  48  LEU C CG  
7036  C CD1 . LEU C 48  ? 0.3387 0.2893 0.3234 0.0028  -0.0021 0.0087  48  LEU C CD1 
7037  C CD2 . LEU C 48  ? 0.3170 0.2638 0.3026 0.0090  -0.0013 0.0116  48  LEU C CD2 
7038  N N   . ASP C 49  ? 0.2859 0.2519 0.2739 0.0086  -0.0143 0.0061  49  ASP C N   
7039  C CA  . ASP C 49  ? 0.3057 0.2748 0.2944 0.0100  -0.0190 0.0043  49  ASP C CA  
7040  C C   . ASP C 49  ? 0.2878 0.2572 0.2757 0.0134  -0.0229 0.0054  49  ASP C C   
7041  O O   . ASP C 49  ? 0.2911 0.2637 0.2816 0.0142  -0.0280 0.0035  49  ASP C O   
7042  C CB  . ASP C 49  ? 0.3108 0.2784 0.2923 0.0098  -0.0190 0.0028  49  ASP C CB  
7043  C CG  . ASP C 49  ? 0.3388 0.3019 0.3118 0.0105  -0.0154 0.0050  49  ASP C CG  
7044  O OD1 . ASP C 49  ? 0.3493 0.3113 0.3237 0.0082  -0.0113 0.0062  49  ASP C OD1 
7045  O OD2 . ASP C 49  ? 0.3438 0.3042 0.3085 0.0133  -0.0167 0.0056  49  ASP C OD2 
7046  N N   . ALA C 50  ? 0.2530 0.2193 0.2379 0.0155  -0.0213 0.0083  50  ALA C N   
7047  C CA  . ALA C 50  ? 0.2906 0.2582 0.2762 0.0193  -0.0256 0.0096  50  ALA C CA  
7048  C C   . ALA C 50  ? 0.2831 0.2570 0.2816 0.0194  -0.0280 0.0092  50  ALA C C   
7049  O O   . ALA C 50  ? 0.3115 0.2891 0.3136 0.0220  -0.0333 0.0093  50  ALA C O   
7050  C CB  . ALA C 50  ? 0.2794 0.2414 0.2593 0.0220  -0.0226 0.0132  50  ALA C CB  
7051  N N   . ILE C 51  ? 0.2749 0.2503 0.2807 0.0169  -0.0243 0.0088  51  ILE C N   
7052  C CA  . ILE C 51  ? 0.2831 0.2646 0.3018 0.0170  -0.0254 0.0089  51  ILE C CA  
7053  C C   . ILE C 51  ? 0.2500 0.2368 0.2747 0.0154  -0.0309 0.0060  51  ILE C C   
7054  O O   . ILE C 51  ? 0.2813 0.2733 0.3137 0.0170  -0.0357 0.0062  51  ILE C O   
7055  C CB  . ILE C 51  ? 0.3005 0.2809 0.3231 0.0150  -0.0195 0.0094  51  ILE C CB  
7056  C CG1 . ILE C 51  ? 0.3219 0.2964 0.3392 0.0170  -0.0148 0.0118  51  ILE C CG1 
7057  C CG2 . ILE C 51  ? 0.2867 0.2734 0.3227 0.0147  -0.0198 0.0095  51  ILE C CG2 
7058  C CD1 . ILE C 51  ? 0.3243 0.3005 0.3471 0.0209  -0.0148 0.0143  51  ILE C CD1 
7059  N N   . PRO C 52  ? 0.2907 0.2766 0.3133 0.0123  -0.0307 0.0034  52  PRO C N   
7060  C CA  . PRO C 52  ? 0.2948 0.2840 0.3220 0.0109  -0.0363 0.0004  52  PRO C CA  
7061  C C   . PRO C 52  ? 0.2943 0.2831 0.3151 0.0135  -0.0429 -0.0007 52  PRO C C   
7062  O O   . PRO C 52  ? 0.2879 0.2804 0.3148 0.0131  -0.0491 -0.0029 52  PRO C O   
7063  C CB  . PRO C 52  ? 0.2868 0.2728 0.3091 0.0082  -0.0340 -0.0019 52  PRO C CB  
7064  C CG  . PRO C 52  ? 0.3134 0.2970 0.3337 0.0074  -0.0276 0.0000  52  PRO C CG  
7065  C CD  . PRO C 52  ? 0.2725 0.2544 0.2896 0.0099  -0.0257 0.0029  52  PRO C CD  
7066  N N   . ALA C 53  ? 0.2821 0.2659 0.2904 0.0163  -0.0418 0.0009  53  ALA C N   
7067  C CA  . ALA C 53  ? 0.3325 0.3149 0.3326 0.0196  -0.0479 0.0003  53  ALA C CA  
7068  C C   . ALA C 53  ? 0.3023 0.2903 0.3113 0.0221  -0.0535 0.0016  53  ALA C C   
7069  O O   . ALA C 53  ? 0.3025 0.2911 0.3077 0.0244  -0.0610 0.0002  53  ALA C O   
7070  C CB  . ALA C 53  ? 0.3022 0.2777 0.2876 0.0222  -0.0443 0.0028  53  ALA C CB  
7071  N N   . GLY C 54  ? 0.2869 0.2790 0.3073 0.0223  -0.0503 0.0043  54  GLY C N   
7072  C CA  . GLY C 54  ? 0.2569 0.2558 0.2883 0.0249  -0.0554 0.0057  54  GLY C CA  
7073  C C   . GLY C 54  ? 0.2574 0.2637 0.3018 0.0224  -0.0622 0.0026  54  GLY C C   
7074  O O   . GLY C 54  ? 0.2832 0.2964 0.3382 0.0243  -0.0679 0.0034  54  GLY C O   
7075  N N   . LEU C 55  ? 0.2710 0.2758 0.3154 0.0181  -0.0618 -0.0008 55  LEU C N   
7076  C CA  . LEU C 55  ? 0.2618 0.2721 0.3185 0.0149  -0.0678 -0.0040 55  LEU C CA  
7077  C C   . LEU C 55  ? 0.3452 0.3527 0.3926 0.0153  -0.0768 -0.0082 55  LEU C C   
7078  O O   . LEU C 55  ? 0.2942 0.3048 0.3503 0.0123  -0.0827 -0.0117 55  LEU C O   
7079  C CB  . LEU C 55  ? 0.2616 0.2707 0.3234 0.0102  -0.0621 -0.0053 55  LEU C CB  
7080  C CG  . LEU C 55  ? 0.2893 0.2998 0.3589 0.0093  -0.0531 -0.0019 55  LEU C CG  
7081  C CD1 . LEU C 55  ? 0.2942 0.3024 0.3661 0.0050  -0.0493 -0.0037 55  LEU C CD1 
7082  C CD2 . LEU C 55  ? 0.2978 0.3169 0.3844 0.0101  -0.0541 0.0006  55  LEU C CD2 
7083  N N   . GLY C 56  ? 0.3062 0.3073 0.3358 0.0190  -0.0780 -0.0080 56  GLY C N   
7084  C CA  . GLY C 56  ? 0.3223 0.3193 0.3401 0.0204  -0.0863 -0.0119 56  GLY C CA  
7085  C C   . GLY C 56  ? 0.3692 0.3562 0.3662 0.0220  -0.0819 -0.0125 56  GLY C C   
7086  O O   . GLY C 56  ? 0.3300 0.3140 0.3238 0.0210  -0.0730 -0.0106 56  GLY C O   
7087  N N   . GLU C 57  ? 0.3532 0.3351 0.3361 0.0247  -0.0887 -0.0154 57  GLU C N   
7088  C CA  . GLU C 57  ? 0.3780 0.3502 0.3404 0.0269  -0.0849 -0.0161 57  GLU C CA  
7089  C C   . GLU C 57  ? 0.4181 0.3862 0.3778 0.0236  -0.0838 -0.0209 57  GLU C C   
7090  O O   . GLU C 57  ? 0.4659 0.4263 0.4098 0.0255  -0.0799 -0.0216 57  GLU C O   
7091  C CB  . GLU C 57  ? 0.4025 0.3697 0.3486 0.0322  -0.0921 -0.0166 57  GLU C CB  
7092  C CG  . GLU C 57  ? 0.4931 0.4640 0.4418 0.0361  -0.0931 -0.0115 57  GLU C CG  
7093  C CD  . GLU C 57  ? 0.6368 0.6006 0.5654 0.0424  -0.0972 -0.0102 57  GLU C CD  
7094  O OE1 . GLU C 57  ? 0.7518 0.7101 0.6696 0.0454  -0.0898 -0.0056 57  GLU C OE1 
7095  O OE2 . GLU C 57  ? 0.7261 0.6894 0.6497 0.0443  -0.1078 -0.0137 57  GLU C OE2 
7096  N N   . ASP C 58  ? 0.3622 0.3350 0.3372 0.0191  -0.0867 -0.0238 58  ASP C N   
7097  C CA  . ASP C 58  ? 0.3847 0.3535 0.3593 0.0158  -0.0857 -0.0282 58  ASP C CA  
7098  C C   . ASP C 58  ? 0.3772 0.3499 0.3654 0.0120  -0.0776 -0.0260 58  ASP C C   
7099  O O   . ASP C 58  ? 0.3540 0.3282 0.3530 0.0080  -0.0785 -0.0284 58  ASP C O   
7100  C CB  . ASP C 58  ? 0.3839 0.3534 0.3644 0.0136  -0.0962 -0.0336 58  ASP C CB  
7101  C CG  . ASP C 58  ? 0.4132 0.3932 0.4167 0.0102  -0.0996 -0.0322 58  ASP C CG  
7102  O OD1 . ASP C 58  ? 0.3553 0.3416 0.3664 0.0115  -0.0961 -0.0272 58  ASP C OD1 
7103  O OD2 . ASP C 58  ? 0.3590 0.3410 0.3738 0.0063  -0.1052 -0.0359 58  ASP C OD2 
7104  N N   . VAL C 59  ? 0.3178 0.2916 0.3049 0.0132  -0.0699 -0.0213 59  VAL C N   
7105  C CA  . VAL C 59  ? 0.3416 0.3182 0.3385 0.0103  -0.0621 -0.0189 59  VAL C CA  
7106  C C   . VAL C 59  ? 0.3651 0.3361 0.3501 0.0113  -0.0550 -0.0182 59  VAL C C   
7107  O O   . VAL C 59  ? 0.3473 0.3159 0.3222 0.0141  -0.0520 -0.0156 59  VAL C O   
7108  C CB  . VAL C 59  ? 0.3757 0.3581 0.3824 0.0107  -0.0596 -0.0143 59  VAL C CB  
7109  C CG1 . VAL C 59  ? 0.3974 0.3816 0.4124 0.0080  -0.0519 -0.0121 59  VAL C CG1 
7110  C CG2 . VAL C 59  ? 0.3322 0.3213 0.3521 0.0102  -0.0667 -0.0147 59  VAL C CG2 
7111  N N   . TYR C 60  ? 0.3270 0.2961 0.3136 0.0091  -0.0522 -0.0202 60  TYR C N   
7112  C CA  . TYR C 60  ? 0.3412 0.3056 0.3176 0.0103  -0.0465 -0.0202 60  TYR C CA  
7113  C C   . TYR C 60  ? 0.3566 0.3237 0.3407 0.0080  -0.0400 -0.0179 60  TYR C C   
7114  O O   . TYR C 60  ? 0.3337 0.3025 0.3277 0.0053  -0.0402 -0.0189 60  TYR C O   
7115  C CB  . TYR C 60  ? 0.3357 0.2944 0.3050 0.0107  -0.0492 -0.0250 60  TYR C CB  
7116  C CG  . TYR C 60  ? 0.3872 0.3424 0.3472 0.0131  -0.0568 -0.0280 60  TYR C CG  
7117  C CD1 . TYR C 60  ? 0.4204 0.3710 0.3645 0.0173  -0.0560 -0.0271 60  TYR C CD1 
7118  C CD2 . TYR C 60  ? 0.4085 0.3650 0.3758 0.0111  -0.0648 -0.0312 60  TYR C CD2 
7119  C CE1 . TYR C 60  ? 0.4704 0.4171 0.4042 0.0201  -0.0635 -0.0297 60  TYR C CE1 
7120  C CE2 . TYR C 60  ? 0.4381 0.3915 0.3968 0.0133  -0.0729 -0.0343 60  TYR C CE2 
7121  C CZ  . TYR C 60  ? 0.4590 0.4073 0.4004 0.0180  -0.0725 -0.0335 60  TYR C CZ  
7122  O OH  . TYR C 60  ? 0.5398 0.4846 0.4717 0.0204  -0.0814 -0.0366 60  TYR C OH  
7123  N N   . SER C 61  ? 0.3103 0.2771 0.2897 0.0090  -0.0344 -0.0148 61  SER C N   
7124  C CA  . SER C 61  ? 0.3022 0.2711 0.2874 0.0070  -0.0290 -0.0130 61  SER C CA  
7125  C C   . SER C 61  ? 0.2853 0.2518 0.2661 0.0076  -0.0258 -0.0144 61  SER C C   
7126  O O   . SER C 61  ? 0.2960 0.2586 0.2673 0.0100  -0.0260 -0.0162 61  SER C O   
7127  C CB  . SER C 61  ? 0.2888 0.2591 0.2735 0.0071  -0.0250 -0.0092 61  SER C CB  
7128  O OG  . SER C 61  ? 0.3225 0.2900 0.2972 0.0091  -0.0221 -0.0082 61  SER C OG  
7129  N N   . LEU C 62  ? 0.2714 0.2401 0.2589 0.0059  -0.0227 -0.0135 62  LEU C N   
7130  C CA  . LEU C 62  ? 0.2789 0.2473 0.2643 0.0066  -0.0183 -0.0132 62  LEU C CA  
7131  C C   . LEU C 62  ? 0.2988 0.2709 0.2889 0.0050  -0.0148 -0.0100 62  LEU C C   
7132  O O   . LEU C 62  ? 0.2992 0.2730 0.2960 0.0032  -0.0149 -0.0092 62  LEU C O   
7133  C CB  . LEU C 62  ? 0.2887 0.2554 0.2773 0.0064  -0.0188 -0.0156 62  LEU C CB  
7134  C CG  . LEU C 62  ? 0.3070 0.2738 0.2940 0.0080  -0.0146 -0.0153 62  LEU C CG  
7135  C CD1 . LEU C 62  ? 0.3064 0.2699 0.2836 0.0112  -0.0131 -0.0168 62  LEU C CD1 
7136  C CD2 . LEU C 62  ? 0.3026 0.2678 0.2944 0.0078  -0.0149 -0.0167 62  LEU C CD2 
7137  N N   . THR C 63  ? 0.2919 0.2647 0.2782 0.0055  -0.0115 -0.0080 63  THR C N   
7138  C CA  . THR C 63  ? 0.2930 0.2686 0.2836 0.0035  -0.0090 -0.0055 63  THR C CA  
7139  C C   . THR C 63  ? 0.2892 0.2676 0.2839 0.0032  -0.0069 -0.0054 63  THR C C   
7140  O O   . THR C 63  ? 0.2825 0.2608 0.2749 0.0051  -0.0051 -0.0062 63  THR C O   
7141  C CB  . THR C 63  ? 0.3012 0.2760 0.2875 0.0035  -0.0066 -0.0032 63  THR C CB  
7142  O OG1 . THR C 63  ? 0.2978 0.2714 0.2782 0.0057  -0.0042 -0.0034 63  THR C OG1 
7143  C CG2 . THR C 63  ? 0.3394 0.3117 0.3228 0.0041  -0.0092 -0.0027 63  THR C CG2 
7144  N N   . GLY C 64  ? 0.2681 0.2483 0.2683 0.0015  -0.0073 -0.0046 64  GLY C N   
7145  C CA  . GLY C 64  ? 0.2854 0.2681 0.2898 0.0017  -0.0066 -0.0047 64  GLY C CA  
7146  C C   . GLY C 64  ? 0.2806 0.2672 0.2869 0.0018  -0.0040 -0.0035 64  GLY C C   
7147  O O   . GLY C 64  ? 0.2979 0.2862 0.3059 0.0038  -0.0027 -0.0039 64  GLY C O   
7148  N N   . GLU C 65  ? 0.2667 0.2547 0.2734 -0.0002 -0.0027 -0.0018 65  GLU C N   
7149  C CA  . GLU C 65  ? 0.2497 0.2425 0.2610 -0.0008 -0.0002 -0.0004 65  GLU C CA  
7150  C C   . GLU C 65  ? 0.2643 0.2573 0.2728 0.0017  0.0035  -0.0002 65  GLU C C   
7151  O O   . GLU C 65  ? 0.2711 0.2686 0.2843 0.0030  0.0059  0.0004  65  GLU C O   
7152  C CB  . GLU C 65  ? 0.2858 0.2792 0.2989 -0.0042 0.0001  0.0012  65  GLU C CB  
7153  C CG  . GLU C 65  ? 0.2831 0.2748 0.2968 -0.0063 -0.0033 0.0007  65  GLU C CG  
7154  C CD  . GLU C 65  ? 0.2614 0.2475 0.2695 -0.0061 -0.0042 0.0004  65  GLU C CD  
7155  O OE1 . GLU C 65  ? 0.2909 0.2750 0.2951 -0.0045 -0.0032 0.0003  65  GLU C OE1 
7156  O OE2 . GLU C 65  ? 0.2983 0.2821 0.3058 -0.0072 -0.0059 0.0002  65  GLU C OE2 
7157  N N   . PRO C 66  ? 0.2695 0.2581 0.2704 0.0027  0.0045  -0.0003 66  PRO C N   
7158  C CA  . PRO C 66  ? 0.2601 0.2476 0.2561 0.0057  0.0085  -0.0001 66  PRO C CA  
7159  C C   . PRO C 66  ? 0.2664 0.2527 0.2604 0.0091  0.0082  -0.0025 66  PRO C C   
7160  O O   . PRO C 66  ? 0.2971 0.2850 0.2913 0.0117  0.0123  -0.0021 66  PRO C O   
7161  C CB  . PRO C 66  ? 0.3449 0.3266 0.3314 0.0064  0.0081  0.0001  66  PRO C CB  
7162  C CG  . PRO C 66  ? 0.2719 0.2534 0.2614 0.0028  0.0059  0.0014  66  PRO C CG  
7163  C CD  . PRO C 66  ? 0.2668 0.2511 0.2631 0.0015  0.0025  -0.0001 66  PRO C CD  
7164  N N   . TYR C 67  ? 0.2729 0.2562 0.2659 0.0091  0.0038  -0.0048 67  TYR C N   
7165  C CA  . TYR C 67  ? 0.2748 0.2559 0.2667 0.0119  0.0033  -0.0073 67  TYR C CA  
7166  C C   . TYR C 67  ? 0.2907 0.2771 0.2907 0.0126  0.0053  -0.0061 67  TYR C C   
7167  O O   . TYR C 67  ? 0.2865 0.2729 0.2858 0.0159  0.0083  -0.0067 67  TYR C O   
7168  C CB  . TYR C 67  ? 0.2613 0.2385 0.2527 0.0109  -0.0015 -0.0095 67  TYR C CB  
7169  C CG  . TYR C 67  ? 0.2757 0.2495 0.2664 0.0133  -0.0020 -0.0121 67  TYR C CG  
7170  C CD1 . TYR C 67  ? 0.3274 0.2957 0.3097 0.0163  -0.0014 -0.0147 67  TYR C CD1 
7171  C CD2 . TYR C 67  ? 0.2966 0.2719 0.2939 0.0129  -0.0027 -0.0117 67  TYR C CD2 
7172  C CE1 . TYR C 67  ? 0.2874 0.2510 0.2683 0.0187  -0.0016 -0.0173 67  TYR C CE1 
7173  C CE2 . TYR C 67  ? 0.2761 0.2470 0.2725 0.0153  -0.0027 -0.0138 67  TYR C CE2 
7174  C CZ  . TYR C 67  ? 0.3126 0.2776 0.3010 0.0181  -0.0021 -0.0167 67  TYR C CZ  
7175  O OH  . TYR C 67  ? 0.3310 0.2907 0.3182 0.0205  -0.0019 -0.0190 67  TYR C OH  
7176  N N   . ALA C 68  ? 0.2680 0.2589 0.2756 0.0098  0.0035  -0.0046 68  ALA C N   
7177  C CA  . ALA C 68  ? 0.3071 0.3036 0.3226 0.0108  0.0044  -0.0033 68  ALA C CA  
7178  C C   . ALA C 68  ? 0.2794 0.2816 0.2990 0.0119  0.0090  -0.0015 68  ALA C C   
7179  O O   . ALA C 68  ? 0.2929 0.2993 0.3181 0.0145  0.0108  -0.0008 68  ALA C O   
7180  C CB  . ALA C 68  ? 0.2809 0.2808 0.3023 0.0078  0.0010  -0.0021 68  ALA C CB  
7181  N N   . ALA C 69  ? 0.2567 0.2598 0.2752 0.0099  0.0113  0.0000  69  ALA C N   
7182  C CA  . ALA C 69  ? 0.2388 0.2471 0.2618 0.0109  0.0168  0.0023  69  ALA C CA  
7183  C C   . ALA C 69  ? 0.2755 0.2802 0.2917 0.0159  0.0214  0.0014  69  ALA C C   
7184  O O   . ALA C 69  ? 0.3194 0.3291 0.3412 0.0185  0.0260  0.0028  69  ALA C O   
7185  C CB  . ALA C 69  ? 0.2766 0.2848 0.2988 0.0074  0.0186  0.0043  69  ALA C CB  
7186  N N   . ALA C 70  ? 0.2785 0.2746 0.2829 0.0176  0.0199  -0.0012 70  ALA C N   
7187  C CA  . ALA C 70  ? 0.2986 0.2894 0.2944 0.0226  0.0231  -0.0031 70  ALA C CA  
7188  C C   . ALA C 70  ? 0.3175 0.3096 0.3181 0.0257  0.0231  -0.0043 70  ALA C C   
7189  O O   . ALA C 70  ? 0.3582 0.3503 0.3579 0.0302  0.0283  -0.0042 70  ALA C O   
7190  C CB  . ALA C 70  ? 0.3022 0.2834 0.2850 0.0231  0.0194  -0.0063 70  ALA C CB  
7191  N N   . VAL C 71  ? 0.3174 0.3101 0.3230 0.0238  0.0180  -0.0052 71  VAL C N   
7192  C CA  . VAL C 71  ? 0.2851 0.2787 0.2956 0.0269  0.0179  -0.0057 71  VAL C CA  
7193  C C   . VAL C 71  ? 0.3297 0.3337 0.3521 0.0280  0.0214  -0.0024 71  VAL C C   
7194  O O   . VAL C 71  ? 0.3281 0.3336 0.3531 0.0326  0.0251  -0.0021 71  VAL C O   
7195  C CB  . VAL C 71  ? 0.2692 0.2607 0.2818 0.0245  0.0121  -0.0067 71  VAL C CB  
7196  C CG1 . VAL C 71  ? 0.2849 0.2785 0.3039 0.0277  0.0122  -0.0060 71  VAL C CG1 
7197  C CG2 . VAL C 71  ? 0.3014 0.2830 0.3042 0.0238  0.0090  -0.0101 71  VAL C CG2 
7198  N N   . ALA C 72  ? 0.2937 0.3053 0.3242 0.0237  0.0202  0.0001  72  ALA C N   
7199  C CA  . ALA C 72  ? 0.2614 0.2841 0.3054 0.0238  0.0222  0.0032  72  ALA C CA  
7200  C C   . ALA C 72  ? 0.3282 0.3539 0.3740 0.0275  0.0300  0.0047  72  ALA C C   
7201  O O   . ALA C 72  ? 0.3662 0.4007 0.4236 0.0297  0.0326  0.0069  72  ALA C O   
7202  C CB  . ALA C 72  ? 0.2933 0.3214 0.3437 0.0178  0.0193  0.0049  72  ALA C CB  
7203  N N   . HIS C 73  ? 0.3234 0.3422 0.3578 0.0285  0.0339  0.0039  73  HIS C N   
7204  C CA  . HIS C 73  ? 0.3879 0.4077 0.4212 0.0328  0.0424  0.0054  73  HIS C CA  
7205  C C   . HIS C 73  ? 0.3689 0.3864 0.4007 0.0395  0.0452  0.0040  73  HIS C C   
7206  O O   . HIS C 73  ? 0.4027 0.4246 0.4391 0.0438  0.0525  0.0060  73  HIS C O   
7207  C CB  . HIS C 73  ? 0.4253 0.4357 0.4431 0.0330  0.0448  0.0043  73  HIS C CB  
7208  C CG  . HIS C 73  ? 0.5014 0.5106 0.5145 0.0379  0.0540  0.0059  73  HIS C CG  
7209  N ND1 . HIS C 73  ? 0.5494 0.5646 0.5685 0.0364  0.0604  0.0102  73  HIS C ND1 
7210  C CD2 . HIS C 73  ? 0.4581 0.4601 0.4606 0.0444  0.0584  0.0039  73  HIS C CD2 
7211  C CE1 . HIS C 73  ? 0.5223 0.5342 0.5345 0.0421  0.0689  0.0111  73  HIS C CE1 
7212  N NE2 . HIS C 73  ? 0.5467 0.5506 0.5483 0.0472  0.0678  0.0071  73  HIS C NE2 
7213  N N   . ASP C 74  ? 0.3569 0.3671 0.3826 0.0406  0.0401  0.0006  74  ASP C N   
7214  C CA  . ASP C 74  ? 0.3542 0.3606 0.3783 0.0467  0.0417  -0.0011 74  ASP C CA  
7215  C C   . ASP C 74  ? 0.3224 0.3372 0.3607 0.0463  0.0380  0.0008  74  ASP C C   
7216  O O   . ASP C 74  ? 0.3338 0.3448 0.3706 0.0443  0.0317  -0.0007 74  ASP C O   
7217  C CB  . ASP C 74  ? 0.3886 0.3808 0.3973 0.0474  0.0381  -0.0058 74  ASP C CB  
7218  C CG  . ASP C 74  ? 0.4087 0.3940 0.4140 0.0533  0.0394  -0.0082 74  ASP C CG  
7219  O OD1 . ASP C 74  ? 0.3909 0.3825 0.4065 0.0569  0.0418  -0.0060 74  ASP C OD1 
7220  O OD2 . ASP C 74  ? 0.4915 0.4645 0.4838 0.0542  0.0374  -0.0124 74  ASP C OD2 
7221  N N   . ARG C 75  ? 0.3229 0.3496 0.3752 0.0484  0.0419  0.0044  75  ARG C N   
7222  C CA  . ARG C 75  ? 0.3166 0.3532 0.3834 0.0477  0.0374  0.0067  75  ARG C CA  
7223  C C   . ARG C 75  ? 0.3133 0.3430 0.3762 0.0513  0.0338  0.0049  75  ARG C C   
7224  O O   . ARG C 75  ? 0.2912 0.3218 0.3569 0.0487  0.0272  0.0052  75  ARG C O   
7225  C CB  . ARG C 75  ? 0.4191 0.4690 0.5016 0.0507  0.0429  0.0105  75  ARG C CB  
7226  C CG  . ARG C 75  ? 0.4620 0.5210 0.5531 0.0456  0.0453  0.0132  75  ARG C CG  
7227  C CD  . ARG C 75  ? 0.6199 0.6955 0.7325 0.0469  0.0475  0.0173  75  ARG C CD  
7228  N NE  . ARG C 75  ? 0.6779 0.7604 0.7978 0.0455  0.0552  0.0203  75  ARG C NE  
7229  C CZ  . ARG C 75  ? 0.7471 0.8287 0.8651 0.0511  0.0653  0.0216  75  ARG C CZ  
7230  N NH1 . ARG C 75  ? 0.7620 0.8359 0.8708 0.0587  0.0688  0.0197  75  ARG C NH1 
7231  N NH2 . ARG C 75  ? 0.7110 0.7987 0.8358 0.0491  0.0725  0.0248  75  ARG C NH2 
7232  N N   . LYS C 76  ? 0.3005 0.3219 0.3557 0.0572  0.0382  0.0029  76  LYS C N   
7233  C CA  . LYS C 76  ? 0.2903 0.3037 0.3417 0.0607  0.0354  0.0013  76  LYS C CA  
7234  C C   . LYS C 76  ? 0.3085 0.3118 0.3500 0.0560  0.0290  -0.0015 76  LYS C C   
7235  O O   . LYS C 76  ? 0.3286 0.3305 0.3724 0.0555  0.0244  -0.0009 76  LYS C O   
7236  C CB  . LYS C 76  ? 0.2902 0.2950 0.3340 0.0680  0.0418  -0.0007 76  LYS C CB  
7237  C CG  . LYS C 76  ? 0.3697 0.3631 0.4074 0.0713  0.0394  -0.0029 76  LYS C CG  
7238  C CD  . LYS C 76  ? 0.4975 0.4803 0.5253 0.0783  0.0460  -0.0057 76  LYS C CD  
7239  C CE  . LYS C 76  ? 0.5494 0.5171 0.5683 0.0809  0.0438  -0.0091 76  LYS C CE  
7240  N NZ  . LYS C 76  ? 0.5405 0.5118 0.5687 0.0815  0.0397  -0.0062 76  LYS C NZ  
7241  N N   . PHE C 77  ? 0.3078 0.3035 0.3381 0.0527  0.0289  -0.0044 77  PHE C N   
7242  C CA  . PHE C 77  ? 0.2960 0.2834 0.3192 0.0482  0.0231  -0.0068 77  PHE C CA  
7243  C C   . PHE C 77  ? 0.2822 0.2773 0.3128 0.0427  0.0181  -0.0044 77  PHE C C   
7244  O O   . PHE C 77  ? 0.2796 0.2709 0.3092 0.0404  0.0135  -0.0046 77  PHE C O   
7245  C CB  . PHE C 77  ? 0.3339 0.3130 0.3449 0.0463  0.0234  -0.0102 77  PHE C CB  
7246  C CG  . PHE C 77  ? 0.3327 0.3034 0.3375 0.0421  0.0177  -0.0129 77  PHE C CG  
7247  C CD1 . PHE C 77  ? 0.3309 0.2949 0.3358 0.0427  0.0149  -0.0140 77  PHE C CD1 
7248  C CD2 . PHE C 77  ? 0.3088 0.2782 0.3084 0.0377  0.0153  -0.0141 77  PHE C CD2 
7249  C CE1 . PHE C 77  ? 0.3279 0.2850 0.3290 0.0383  0.0102  -0.0161 77  PHE C CE1 
7250  C CE2 . PHE C 77  ? 0.3223 0.2853 0.3181 0.0338  0.0101  -0.0164 77  PHE C CE2 
7251  C CZ  . PHE C 77  ? 0.3455 0.3027 0.3427 0.0339  0.0077  -0.0173 77  PHE C CZ  
7252  N N   . ALA C 78  ? 0.2786 0.2839 0.3161 0.0403  0.0191  -0.0020 78  ALA C N   
7253  C CA  . ALA C 78  ? 0.2478 0.2596 0.2917 0.0354  0.0142  0.0000  78  ALA C CA  
7254  C C   . ALA C 78  ? 0.2549 0.2703 0.3058 0.0373  0.0109  0.0019  78  ALA C C   
7255  O O   . ALA C 78  ? 0.2684 0.2817 0.3179 0.0345  0.0060  0.0022  78  ALA C O   
7256  C CB  . ALA C 78  ? 0.2688 0.2904 0.3199 0.0326  0.0162  0.0022  78  ALA C CB  
7257  N N   . LYS C 79  ? 0.2764 0.2972 0.3347 0.0426  0.0137  0.0036  79  LYS C N   
7258  C CA  . LYS C 79  ? 0.2769 0.3010 0.3414 0.0455  0.0103  0.0058  79  LYS C CA  
7259  C C   . LYS C 79  ? 0.2834 0.2953 0.3388 0.0466  0.0082  0.0043  79  LYS C C   
7260  O O   . LYS C 79  ? 0.2765 0.2879 0.3320 0.0454  0.0035  0.0057  79  LYS C O   
7261  C CB  . LYS C 79  ? 0.2933 0.3249 0.3674 0.0519  0.0143  0.0078  79  LYS C CB  
7262  C CG  . LYS C 79  ? 0.3894 0.4263 0.4714 0.0555  0.0105  0.0107  79  LYS C CG  
7263  C CD  . LYS C 79  ? 0.4800 0.5150 0.5640 0.0636  0.0151  0.0113  79  LYS C CD  
7264  C CE  . LYS C 79  ? 0.5117 0.5497 0.6016 0.0683  0.0110  0.0143  79  LYS C CE  
7265  N NZ  . LYS C 79  ? 0.5455 0.5695 0.6259 0.0733  0.0130  0.0132  79  LYS C NZ  
7266  N N   . GLU C 80  ? 0.3024 0.3040 0.3496 0.0490  0.0116  0.0016  80  GLU C N   
7267  C CA  . GLU C 80  ? 0.3008 0.2900 0.3402 0.0492  0.0099  0.0000  80  GLU C CA  
7268  C C   . GLU C 80  ? 0.2966 0.2829 0.3322 0.0430  0.0055  -0.0004 80  GLU C C   
7269  O O   . GLU C 80  ? 0.2617 0.2438 0.2963 0.0427  0.0028  0.0009  80  GLU C O   
7270  C CB  . GLU C 80  ? 0.2985 0.2768 0.3292 0.0514  0.0137  -0.0039 80  GLU C CB  
7271  C CG  . GLU C 80  ? 0.3443 0.3229 0.3772 0.0586  0.0186  -0.0035 80  GLU C CG  
7272  C CD  . GLU C 80  ? 0.3878 0.3560 0.4105 0.0610  0.0227  -0.0078 80  GLU C CD  
7273  O OE1 . GLU C 80  ? 0.3879 0.3535 0.4039 0.0570  0.0223  -0.0104 80  GLU C OE1 
7274  O OE2 . GLU C 80  ? 0.4058 0.3680 0.4266 0.0672  0.0263  -0.0085 80  GLU C OE2 
7275  N N   . CYS C 81  ? 0.2847 0.2732 0.3182 0.0383  0.0053  -0.0018 81  CYS C N   
7276  C CA  . CYS C 81  ? 0.3003 0.2864 0.3308 0.0330  0.0017  -0.0021 81  CYS C CA  
7277  C C   . CYS C 81  ? 0.3097 0.3019 0.3449 0.0318  -0.0017 0.0010  81  CYS C C   
7278  O O   . CYS C 81  ? 0.2841 0.2713 0.3162 0.0303  -0.0040 0.0017  81  CYS C O   
7279  C CB  . CYS C 81  ? 0.3000 0.2880 0.3279 0.0290  0.0021  -0.0036 81  CYS C CB  
7280  S SG  . CYS C 81  ? 0.3098 0.2881 0.3286 0.0295  0.0042  -0.0078 81  CYS C SG  
7281  N N   . MET C 82  ? 0.2741 0.2768 0.3167 0.0324  -0.0022 0.0029  82  MET C N   
7282  C CA  . MET C 82  ? 0.2799 0.2879 0.3261 0.0314  -0.0066 0.0053  82  MET C CA  
7283  C C   . MET C 82  ? 0.2690 0.2737 0.3148 0.0358  -0.0081 0.0073  82  MET C C   
7284  O O   . MET C 82  ? 0.2945 0.2976 0.3375 0.0350  -0.0117 0.0088  82  MET C O   
7285  C CB  . MET C 82  ? 0.2827 0.3030 0.3383 0.0304  -0.0078 0.0067  82  MET C CB  
7286  C CG  . MET C 82  ? 0.3020 0.3245 0.3574 0.0257  -0.0058 0.0053  82  MET C CG  
7287  S SD  . MET C 82  ? 0.3096 0.3455 0.3773 0.0238  -0.0064 0.0070  82  MET C SD  
7288  C CE  . MET C 82  ? 0.3641 0.4019 0.4350 0.0282  0.0011  0.0070  82  MET C CE  
7289  N N   . ASP C 83  ? 0.2798 0.2825 0.3271 0.0410  -0.0051 0.0074  83  ASP C N   
7290  C CA  . ASP C 83  ? 0.2824 0.2805 0.3287 0.0457  -0.0063 0.0096  83  ASP C CA  
7291  C C   . ASP C 83  ? 0.2802 0.2659 0.3176 0.0439  -0.0063 0.0091  83  ASP C C   
7292  O O   . ASP C 83  ? 0.2913 0.2733 0.3261 0.0456  -0.0084 0.0117  83  ASP C O   
7293  C CB  . ASP C 83  ? 0.2955 0.2927 0.3449 0.0520  -0.0026 0.0098  83  ASP C CB  
7294  C CG  . ASP C 83  ? 0.3423 0.3532 0.4029 0.0548  -0.0025 0.0116  83  ASP C CG  
7295  O OD1 . ASP C 83  ? 0.3524 0.3731 0.4187 0.0521  -0.0065 0.0130  83  ASP C OD1 
7296  O OD2 . ASP C 83  ? 0.3230 0.3346 0.3868 0.0596  0.0018  0.0114  83  ASP C OD2 
7297  N N   . ALA C 84  ? 0.2776 0.2568 0.3107 0.0407  -0.0040 0.0060  84  ALA C N   
7298  C CA  . ALA C 84  ? 0.2946 0.2633 0.3217 0.0382  -0.0041 0.0057  84  ALA C CA  
7299  C C   . ALA C 84  ? 0.2970 0.2676 0.3221 0.0345  -0.0069 0.0073  84  ALA C C   
7300  O O   . ALA C 84  ? 0.2929 0.2569 0.3144 0.0349  -0.0071 0.0094  84  ALA C O   
7301  C CB  . ALA C 84  ? 0.2879 0.2505 0.3120 0.0353  -0.0022 0.0019  84  ALA C CB  
7302  N N   . ALA C 85  ? 0.2723 0.2506 0.2992 0.0311  -0.0085 0.0065  85  ALA C N   
7303  C CA  . ALA C 85  ? 0.3011 0.2806 0.3253 0.0279  -0.0110 0.0077  85  ALA C CA  
7304  C C   . ALA C 85  ? 0.2632 0.2441 0.2864 0.0309  -0.0140 0.0108  85  ALA C C   
7305  O O   . ALA C 85  ? 0.2734 0.2500 0.2909 0.0301  -0.0152 0.0124  85  ALA C O   
7306  C CB  . ALA C 85  ? 0.2704 0.2574 0.2970 0.0241  -0.0121 0.0061  85  ALA C CB  
7307  N N   . GLU C 86  ? 0.2774 0.2649 0.3060 0.0347  -0.0154 0.0119  86  GLU C N   
7308  C CA  . GLU C 86  ? 0.3059 0.2957 0.3338 0.0381  -0.0193 0.0149  86  GLU C CA  
7309  C C   . GLU C 86  ? 0.3070 0.2867 0.3291 0.0421  -0.0178 0.0174  86  GLU C C   
7310  O O   . GLU C 86  ? 0.3074 0.2833 0.3230 0.0432  -0.0201 0.0198  86  GLU C O   
7311  C CB  . GLU C 86  ? 0.3055 0.3061 0.3430 0.0413  -0.0210 0.0155  86  GLU C CB  
7312  C CG  . GLU C 86  ? 0.3445 0.3488 0.3827 0.0454  -0.0261 0.0186  86  GLU C CG  
7313  C CD  . GLU C 86  ? 0.3926 0.4109 0.4422 0.0458  -0.0295 0.0187  86  GLU C CD  
7314  O OE1 . GLU C 86  ? 0.3759 0.4006 0.4309 0.0412  -0.0287 0.0165  86  GLU C OE1 
7315  O OE2 . GLU C 86  ? 0.3998 0.4228 0.4536 0.0508  -0.0327 0.0212  86  GLU C OE2 
7316  N N   . ALA C 87  ? 0.2926 0.2663 0.3156 0.0439  -0.0137 0.0167  87  ALA C N   
7317  C CA  . ALA C 87  ? 0.3234 0.2860 0.3415 0.0471  -0.0115 0.0190  87  ALA C CA  
7318  C C   . ALA C 87  ? 0.3317 0.2862 0.3427 0.0436  -0.0104 0.0198  87  ALA C C   
7319  O O   . ALA C 87  ? 0.3341 0.2811 0.3394 0.0462  -0.0098 0.0232  87  ALA C O   
7320  C CB  . ALA C 87  ? 0.2878 0.2447 0.3081 0.0483  -0.0074 0.0168  87  ALA C CB  
7321  N N   . TYR C 88  ? 0.2950 0.2507 0.3064 0.0380  -0.0096 0.0170  88  TYR C N   
7322  C CA  . TYR C 88  ? 0.3207 0.2704 0.3268 0.0348  -0.0082 0.0180  88  TYR C CA  
7323  C C   . TYR C 88  ? 0.3593 0.3102 0.3592 0.0361  -0.0111 0.0207  88  TYR C C   
7324  O O   . TYR C 88  ? 0.3200 0.2631 0.3132 0.0367  -0.0092 0.0235  88  TYR C O   
7325  C CB  . TYR C 88  ? 0.2680 0.2202 0.2765 0.0292  -0.0074 0.0146  88  TYR C CB  
7326  C CG  . TYR C 88  ? 0.2664 0.2124 0.2713 0.0264  -0.0051 0.0159  88  TYR C CG  
7327  C CD1 . TYR C 88  ? 0.3138 0.2613 0.3137 0.0253  -0.0063 0.0171  88  TYR C CD1 
7328  C CD2 . TYR C 88  ? 0.3001 0.2386 0.3070 0.0248  -0.0015 0.0158  88  TYR C CD2 
7329  C CE1 . TYR C 88  ? 0.3012 0.2432 0.2981 0.0232  -0.0031 0.0184  88  TYR C CE1 
7330  C CE2 . TYR C 88  ? 0.3471 0.2812 0.3529 0.0221  0.0013  0.0173  88  TYR C CE2 
7331  C CZ  . TYR C 88  ? 0.3564 0.2923 0.3569 0.0217  0.0009  0.0189  88  TYR C CZ  
7332  O OH  . TYR C 88  ? 0.3792 0.3111 0.3788 0.0197  0.0044  0.0206  88  TYR C OH  
7333  N N   . GLY C 89  ? 0.3063 0.2664 0.3080 0.0367  -0.0157 0.0201  89  GLY C N   
7334  C CA  . GLY C 89  ? 0.3022 0.2635 0.2976 0.0386  -0.0200 0.0222  89  GLY C CA  
7335  C C   . GLY C 89  ? 0.3104 0.2787 0.3062 0.0347  -0.0235 0.0198  89  GLY C C   
7336  O O   . GLY C 89  ? 0.3200 0.2885 0.3094 0.0357  -0.0277 0.0207  89  GLY C O   
7337  N N   . PHE C 90  ? 0.2995 0.2730 0.3021 0.0307  -0.0223 0.0166  90  PHE C N   
7338  C CA  . PHE C 90  ? 0.2839 0.2633 0.2873 0.0266  -0.0252 0.0144  90  PHE C CA  
7339  C C   . PHE C 90  ? 0.3084 0.2978 0.3181 0.0276  -0.0304 0.0142  90  PHE C C   
7340  O O   . PHE C 90  ? 0.3178 0.3126 0.3353 0.0304  -0.0303 0.0147  90  PHE C O   
7341  C CB  . PHE C 90  ? 0.3073 0.2886 0.3156 0.0224  -0.0219 0.0116  90  PHE C CB  
7342  C CG  . PHE C 90  ? 0.2967 0.2704 0.2999 0.0201  -0.0184 0.0114  90  PHE C CG  
7343  C CD1 . PHE C 90  ? 0.2907 0.2613 0.2870 0.0184  -0.0192 0.0115  90  PHE C CD1 
7344  C CD2 . PHE C 90  ? 0.3112 0.2804 0.3164 0.0200  -0.0144 0.0111  90  PHE C CD2 
7345  C CE1 . PHE C 90  ? 0.3431 0.3073 0.3358 0.0168  -0.0154 0.0118  90  PHE C CE1 
7346  C CE2 . PHE C 90  ? 0.2633 0.2268 0.2659 0.0177  -0.0114 0.0112  90  PHE C CE2 
7347  C CZ  . PHE C 90  ? 0.3157 0.2773 0.3127 0.0164  -0.0116 0.0117  90  PHE C CZ  
7348  N N   . ALA C 91  ? 0.2511 0.2430 0.2581 0.0253  -0.0349 0.0132  91  ALA C N   
7349  C CA  . ALA C 91  ? 0.2676 0.2695 0.2818 0.0252  -0.0408 0.0128  91  ALA C CA  
7350  C C   . ALA C 91  ? 0.3143 0.3255 0.3412 0.0227  -0.0387 0.0112  91  ALA C C   
7351  O O   . ALA C 91  ? 0.3168 0.3265 0.3441 0.0188  -0.0350 0.0094  91  ALA C O   
7352  C CB  . ALA C 91  ? 0.2669 0.2682 0.2753 0.0217  -0.0458 0.0110  91  ALA C CB  
7353  N N   . ARG C 92  ? 0.2987 0.3198 0.3360 0.0249  -0.0416 0.0122  92  ARG C N   
7354  C CA  . ARG C 92  ? 0.3059 0.3359 0.3555 0.0233  -0.0387 0.0113  92  ARG C CA  
7355  C C   . ARG C 92  ? 0.2512 0.2861 0.3050 0.0171  -0.0404 0.0093  92  ARG C C   
7356  O O   . ARG C 92  ? 0.2981 0.3381 0.3599 0.0150  -0.0364 0.0087  92  ARG C O   
7357  C CB  . ARG C 92  ? 0.3328 0.3727 0.3938 0.0278  -0.0405 0.0134  92  ARG C CB  
7358  C CG  . ARG C 92  ? 0.3417 0.3881 0.4134 0.0281  -0.0347 0.0131  92  ARG C CG  
7359  C CD  . ARG C 92  ? 0.3706 0.4285 0.4555 0.0327  -0.0362 0.0154  92  ARG C CD  
7360  N NE  . ARG C 92  ? 0.3166 0.3693 0.3974 0.0396  -0.0355 0.0174  92  ARG C NE  
7361  C CZ  . ARG C 92  ? 0.3613 0.4217 0.4518 0.0453  -0.0362 0.0197  92  ARG C CZ  
7362  N NH1 . ARG C 92  ? 0.3454 0.4201 0.4512 0.0449  -0.0382 0.0206  92  ARG C NH1 
7363  N NH2 . ARG C 92  ? 0.3668 0.4203 0.4522 0.0516  -0.0347 0.0216  92  ARG C NH2 
7364  N N   . ASP C 93  ? 0.2926 0.3255 0.3409 0.0145  -0.0460 0.0083  93  ASP C N   
7365  C CA  . ASP C 93  ? 0.2677 0.3040 0.3202 0.0083  -0.0473 0.0063  93  ASP C CA  
7366  C C   . ASP C 93  ? 0.2931 0.3198 0.3360 0.0049  -0.0434 0.0046  93  ASP C C   
7367  O O   . ASP C 93  ? 0.2788 0.3061 0.3232 -0.0001 -0.0442 0.0029  93  ASP C O   
7368  C CB  . ASP C 93  ? 0.3025 0.3415 0.3548 0.0065  -0.0558 0.0054  93  ASP C CB  
7369  C CG  . ASP C 93  ? 0.3459 0.3751 0.3830 0.0095  -0.0594 0.0055  93  ASP C CG  
7370  O OD1 . ASP C 93  ? 0.4021 0.4313 0.4370 0.0150  -0.0613 0.0078  93  ASP C OD1 
7371  O OD2 . ASP C 93  ? 0.3965 0.4168 0.4230 0.0066  -0.0587 0.0038  93  ASP C OD2 
7372  N N   . LEU C 94  ? 0.2497 0.2679 0.2839 0.0072  -0.0390 0.0050  94  LEU C N   
7373  C CA  . LEU C 94  ? 0.2760 0.2875 0.3045 0.0043  -0.0347 0.0037  94  LEU C CA  
7374  C C   . LEU C 94  ? 0.2608 0.2775 0.2978 0.0023  -0.0304 0.0033  94  LEU C C   
7375  O O   . LEU C 94  ? 0.2756 0.2997 0.3216 0.0041  -0.0291 0.0043  94  LEU C O   
7376  C CB  . LEU C 94  ? 0.2643 0.2671 0.2844 0.0072  -0.0311 0.0046  94  LEU C CB  
7377  C CG  . LEU C 94  ? 0.2567 0.2519 0.2659 0.0089  -0.0334 0.0053  94  LEU C CG  
7378  C CD1 . LEU C 94  ? 0.2712 0.2602 0.2765 0.0121  -0.0294 0.0069  94  LEU C CD1 
7379  C CD2 . LEU C 94  ? 0.2973 0.2867 0.2994 0.0053  -0.0331 0.0036  94  LEU C CD2 
7380  N N   . CYS C 95  ? 0.2725 0.2850 0.3058 -0.0010 -0.0278 0.0021  95  CYS C N   
7381  C CA  . CYS C 95  ? 0.2361 0.2507 0.2738 -0.0028 -0.0234 0.0019  95  CYS C CA  
7382  C C   . CYS C 95  ? 0.2540 0.2715 0.2956 0.0008  -0.0197 0.0027  95  CYS C C   
7383  O O   . CYS C 95  ? 0.2373 0.2497 0.2741 0.0037  -0.0184 0.0027  95  CYS C O   
7384  C CB  . CYS C 95  ? 0.2747 0.2811 0.3041 -0.0044 -0.0209 0.0010  95  CYS C CB  
7385  S SG  . CYS C 95  ? 0.2498 0.2568 0.2812 -0.0054 -0.0156 0.0009  95  CYS C SG  
7386  N N   . SER C 96  ? 0.2470 0.2723 0.2978 0.0007  -0.0178 0.0034  96  SER C N   
7387  C CA  . SER C 96  ? 0.2583 0.2854 0.3117 0.0050  -0.0141 0.0040  96  SER C CA  
7388  C C   . SER C 96  ? 0.2442 0.2642 0.2903 0.0057  -0.0099 0.0028  96  SER C C   
7389  O O   . SER C 96  ? 0.2382 0.2552 0.2820 0.0094  -0.0080 0.0024  96  SER C O   
7390  C CB  . SER C 96  ? 0.2452 0.2827 0.3106 0.0054  -0.0124 0.0053  96  SER C CB  
7391  O OG  . SER C 96  ? 0.2912 0.3304 0.3590 0.0015  -0.0097 0.0054  96  SER C OG  
7392  N N   . TYR C 97  ? 0.2677 0.2844 0.3097 0.0024  -0.0087 0.0021  97  TYR C N   
7393  C CA  . TYR C 97  ? 0.2552 0.2653 0.2899 0.0033  -0.0060 0.0009  97  TYR C CA  
7394  C C   . TYR C 97  ? 0.2746 0.2782 0.3037 0.0043  -0.0080 0.0000  97  TYR C C   
7395  O O   . TYR C 97  ? 0.2570 0.2566 0.2833 0.0067  -0.0067 -0.0010 97  TYR C O   
7396  C CB  . TYR C 97  ? 0.2725 0.2802 0.3039 0.0000  -0.0049 0.0008  97  TYR C CB  
7397  C CG  . TYR C 97  ? 0.2854 0.2977 0.3210 -0.0008 -0.0013 0.0020  97  TYR C CG  
7398  C CD1 . TYR C 97  ? 0.2898 0.3069 0.3302 0.0022  0.0019  0.0027  97  TYR C CD1 
7399  C CD2 . TYR C 97  ? 0.2910 0.3017 0.3250 -0.0041 -0.0002 0.0026  97  TYR C CD2 
7400  C CE1 . TYR C 97  ? 0.3205 0.3419 0.3651 0.0016  0.0065  0.0043  97  TYR C CE1 
7401  C CE2 . TYR C 97  ? 0.2991 0.3132 0.3368 -0.0048 0.0040  0.0042  97  TYR C CE2 
7402  C CZ  . TYR C 97  ? 0.3420 0.3616 0.3851 -0.0021 0.0075  0.0052  97  TYR C CZ  
7403  O OH  . TYR C 97  ? 0.3954 0.4184 0.4426 -0.0028 0.0129  0.0074  97  TYR C OH  
7404  N N   . MET C 98  ? 0.2184 0.2202 0.2458 0.0026  -0.0109 0.0004  98  MET C N   
7405  C CA  . MET C 98  ? 0.2342 0.2301 0.2571 0.0036  -0.0120 0.0003  98  MET C CA  
7406  C C   . MET C 98  ? 0.2525 0.2481 0.2769 0.0072  -0.0118 0.0008  98  MET C C   
7407  O O   . MET C 98  ? 0.2579 0.2482 0.2797 0.0084  -0.0107 0.0002  98  MET C O   
7408  C CB  . MET C 98  ? 0.2439 0.2383 0.2640 0.0019  -0.0146 0.0009  98  MET C CB  
7409  C CG  . MET C 98  ? 0.2464 0.2340 0.2612 0.0026  -0.0143 0.0012  98  MET C CG  
7410  S SD  . MET C 98  ? 0.2657 0.2495 0.2743 0.0012  -0.0162 0.0017  98  MET C SD  
7411  C CE  . MET C 98  ? 0.2634 0.2515 0.2734 0.0020  -0.0204 0.0023  98  MET C CE  
7412  N N   . ARG C 99  ? 0.2214 0.2226 0.2507 0.0090  -0.0130 0.0018  99  ARG C N   
7413  C CA  . ARG C 99  ? 0.2098 0.2103 0.2404 0.0131  -0.0129 0.0027  99  ARG C CA  
7414  C C   . ARG C 99  ? 0.2356 0.2343 0.2667 0.0153  -0.0094 0.0014  99  ARG C C   
7415  O O   . ARG C 99  ? 0.2498 0.2425 0.2782 0.0174  -0.0085 0.0010  99  ARG C O   
7416  C CB  . ARG C 99  ? 0.2616 0.2696 0.2983 0.0149  -0.0154 0.0043  99  ARG C CB  
7417  C CG  . ARG C 99  ? 0.2889 0.2967 0.3229 0.0136  -0.0200 0.0053  99  ARG C CG  
7418  C CD  . ARG C 99  ? 0.2581 0.2736 0.2985 0.0159  -0.0237 0.0068  99  ARG C CD  
7419  N NE  . ARG C 99  ? 0.2554 0.2803 0.3054 0.0138  -0.0236 0.0065  99  ARG C NE  
7420  C CZ  . ARG C 99  ? 0.2650 0.2974 0.3242 0.0164  -0.0218 0.0074  99  ARG C CZ  
7421  N NH1 . ARG C 99  ? 0.2859 0.3164 0.3451 0.0215  -0.0196 0.0083  99  ARG C NH1 
7422  N NH2 . ARG C 99  ? 0.2569 0.2989 0.3261 0.0141  -0.0224 0.0077  99  ARG C NH2 
7423  N N   . ILE C 100 ? 0.2385 0.2411 0.2717 0.0146  -0.0072 0.0006  100 ILE C N   
7424  C CA  . ILE C 100 ? 0.2293 0.2289 0.2604 0.0169  -0.0038 -0.0010 100 ILE C CA  
7425  C C   . ILE C 100 ? 0.2397 0.2308 0.2641 0.0156  -0.0041 -0.0030 100 ILE C C   
7426  O O   . ILE C 100 ? 0.2632 0.2485 0.2851 0.0178  -0.0034 -0.0044 100 ILE C O   
7427  C CB  . ILE C 100 ? 0.2390 0.2434 0.2719 0.0161  -0.0009 -0.0010 100 ILE C CB  
7428  C CG1 . ILE C 100 ? 0.2530 0.2663 0.2948 0.0181  0.0004  0.0009  100 ILE C CG1 
7429  C CG2 . ILE C 100 ? 0.2509 0.2497 0.2777 0.0182  0.0022  -0.0032 100 ILE C CG2 
7430  C CD1 . ILE C 100 ? 0.3083 0.3277 0.3542 0.0164  0.0035  0.0019  100 ILE C CD1 
7431  N N   . TYR C 101 ? 0.2226 0.2128 0.2448 0.0121  -0.0055 -0.0031 101 TYR C N   
7432  C CA  . TYR C 101 ? 0.2483 0.2322 0.2662 0.0107  -0.0062 -0.0048 101 TYR C CA  
7433  C C   . TYR C 101 ? 0.2812 0.2598 0.2991 0.0114  -0.0070 -0.0047 101 TYR C C   
7434  O O   . TYR C 101 ? 0.2677 0.2408 0.2840 0.0120  -0.0069 -0.0065 101 TYR C O   
7435  C CB  . TYR C 101 ? 0.2468 0.2314 0.2633 0.0073  -0.0072 -0.0044 101 TYR C CB  
7436  C CG  . TYR C 101 ? 0.2388 0.2188 0.2523 0.0060  -0.0080 -0.0060 101 TYR C CG  
7437  C CD1 . TYR C 101 ? 0.2664 0.2424 0.2809 0.0053  -0.0091 -0.0061 101 TYR C CD1 
7438  C CD2 . TYR C 101 ? 0.2678 0.2477 0.2780 0.0058  -0.0077 -0.0072 101 TYR C CD2 
7439  C CE1 . TYR C 101 ? 0.2414 0.2145 0.2553 0.0039  -0.0104 -0.0076 101 TYR C CE1 
7440  C CE2 . TYR C 101 ? 0.2956 0.2719 0.3034 0.0050  -0.0094 -0.0088 101 TYR C CE2 
7441  C CZ  . TYR C 101 ? 0.3166 0.2903 0.3271 0.0039  -0.0110 -0.0091 101 TYR C CZ  
7442  O OH  . TYR C 101 ? 0.3257 0.2973 0.3356 0.0029  -0.0132 -0.0106 101 TYR C OH  
7443  N N   . TRP C 102 ? 0.2495 0.2292 0.2689 0.0114  -0.0080 -0.0024 102 TRP C N   
7444  C CA  . TRP C 102 ? 0.2528 0.2270 0.2718 0.0125  -0.0080 -0.0014 102 TRP C CA  
7445  C C   . TRP C 102 ? 0.2782 0.2490 0.2977 0.0159  -0.0068 -0.0022 102 TRP C C   
7446  O O   . TRP C 102 ? 0.2672 0.2311 0.2860 0.0159  -0.0062 -0.0030 102 TRP C O   
7447  C CB  . TRP C 102 ? 0.2618 0.2376 0.2804 0.0130  -0.0092 0.0013  102 TRP C CB  
7448  C CG  . TRP C 102 ? 0.2506 0.2263 0.2669 0.0101  -0.0099 0.0019  102 TRP C CG  
7449  C CD1 . TRP C 102 ? 0.2397 0.2134 0.2553 0.0075  -0.0092 0.0010  102 TRP C CD1 
7450  C CD2 . TRP C 102 ? 0.2633 0.2405 0.2772 0.0101  -0.0116 0.0036  102 TRP C CD2 
7451  N NE1 . TRP C 102 ? 0.2772 0.2508 0.2901 0.0061  -0.0096 0.0022  102 TRP C NE1 
7452  C CE2 . TRP C 102 ? 0.2608 0.2361 0.2719 0.0075  -0.0112 0.0035  102 TRP C CE2 
7453  C CE3 . TRP C 102 ? 0.2961 0.2764 0.3100 0.0122  -0.0139 0.0050  102 TRP C CE3 
7454  C CZ2 . TRP C 102 ? 0.2501 0.2246 0.2568 0.0071  -0.0126 0.0046  102 TRP C CZ2 
7455  C CZ3 . TRP C 102 ? 0.2673 0.2477 0.2772 0.0113  -0.0163 0.0058  102 TRP C CZ3 
7456  C CH2 . TRP C 102 ? 0.2576 0.2345 0.2633 0.0089  -0.0154 0.0055  102 TRP C CH2 
7457  N N   . GLY C 103 ? 0.2682 0.2436 0.2898 0.0189  -0.0063 -0.0016 103 GLY C N   
7458  C CA  . GLY C 103 ? 0.2677 0.2396 0.2897 0.0229  -0.0046 -0.0021 103 GLY C CA  
7459  C C   . GLY C 103 ? 0.3049 0.2707 0.3237 0.0228  -0.0033 -0.0056 103 GLY C C   
7460  O O   . GLY C 103 ? 0.2816 0.2397 0.2989 0.0245  -0.0026 -0.0068 103 GLY C O   
7461  N N   . GLY C 104 ? 0.3154 0.2839 0.3323 0.0212  -0.0031 -0.0075 104 GLY C N   
7462  C CA  . GLY C 104 ? 0.3180 0.2802 0.3300 0.0214  -0.0027 -0.0111 104 GLY C CA  
7463  C C   . GLY C 104 ? 0.3126 0.2680 0.3237 0.0182  -0.0050 -0.0127 104 GLY C C   
7464  O O   . GLY C 104 ? 0.3222 0.2700 0.3304 0.0186  -0.0055 -0.0158 104 GLY C O   
7465  N N   . MET C 105 ? 0.2970 0.2547 0.3110 0.0151  -0.0064 -0.0107 105 MET C N   
7466  C CA  . MET C 105 ? 0.2925 0.2449 0.3081 0.0121  -0.0078 -0.0114 105 MET C CA  
7467  C C   . MET C 105 ? 0.2702 0.2157 0.2873 0.0135  -0.0067 -0.0106 105 MET C C   
7468  O O   . MET C 105 ? 0.3176 0.2561 0.3353 0.0121  -0.0075 -0.0129 105 MET C O   
7469  C CB  . MET C 105 ? 0.2827 0.2394 0.3009 0.0092  -0.0084 -0.0088 105 MET C CB  
7470  C CG  . MET C 105 ? 0.3084 0.2615 0.3301 0.0059  -0.0094 -0.0091 105 MET C CG  
7471  S SD  . MET C 105 ? 0.3418 0.2984 0.3661 0.0040  -0.0083 -0.0052 105 MET C SD  
7472  C CE  . MET C 105 ? 0.3117 0.2691 0.3333 0.0070  -0.0066 -0.0020 105 MET C CE  
7473  N N   . HIS C 106 ? 0.2500 0.1972 0.2681 0.0160  -0.0053 -0.0073 106 HIS C N   
7474  C CA  . HIS C 106 ? 0.2776 0.2175 0.2963 0.0180  -0.0038 -0.0059 106 HIS C CA  
7475  C C   . HIS C 106 ? 0.3133 0.2470 0.3298 0.0210  -0.0030 -0.0089 106 HIS C C   
7476  O O   . HIS C 106 ? 0.3090 0.2334 0.3257 0.0207  -0.0024 -0.0098 106 HIS C O   
7477  C CB  . HIS C 106 ? 0.3051 0.2488 0.3239 0.0210  -0.0031 -0.0017 106 HIS C CB  
7478  C CG  . HIS C 106 ? 0.2737 0.2188 0.2927 0.0186  -0.0034 0.0013  106 HIS C CG  
7479  N ND1 . HIS C 106 ? 0.3092 0.2475 0.3287 0.0178  -0.0017 0.0035  106 HIS C ND1 
7480  C CD2 . HIS C 106 ? 0.2847 0.2364 0.3032 0.0169  -0.0045 0.0023  106 HIS C CD2 
7481  C CE1 . HIS C 106 ? 0.3337 0.2745 0.3522 0.0162  -0.0016 0.0059  106 HIS C CE1 
7482  N NE2 . HIS C 106 ? 0.2930 0.2416 0.3106 0.0158  -0.0035 0.0050  106 HIS C NE2 
7483  N N   . LEU C 107 ? 0.2978 0.2357 0.3120 0.0239  -0.0024 -0.0103 107 LEU C N   
7484  C CA  . LEU C 107 ? 0.2933 0.2246 0.3039 0.0273  -0.0010 -0.0135 107 LEU C CA  
7485  C C   . LEU C 107 ? 0.3003 0.2249 0.3072 0.0242  -0.0030 -0.0183 107 LEU C C   
7486  O O   . LEU C 107 ? 0.3301 0.2457 0.3330 0.0262  -0.0025 -0.0217 107 LEU C O   
7487  C CB  . LEU C 107 ? 0.2907 0.2290 0.3003 0.0314  0.0010  -0.0134 107 LEU C CB  
7488  C CG  . LEU C 107 ? 0.3268 0.2720 0.3412 0.0348  0.0022  -0.0090 107 LEU C CG  
7489  C CD1 . LEU C 107 ? 0.3509 0.3048 0.3670 0.0378  0.0042  -0.0086 107 LEU C CD1 
7490  C CD2 . LEU C 107 ? 0.3283 0.2656 0.3428 0.0389  0.0036  -0.0078 107 LEU C CD2 
7491  N N   . ASN C 108 ? 0.2996 0.2282 0.3076 0.0198  -0.0055 -0.0189 108 ASN C N   
7492  C CA  . ASN C 108 ? 0.3157 0.2394 0.3209 0.0167  -0.0086 -0.0233 108 ASN C CA  
7493  C C   . ASN C 108 ? 0.3145 0.2359 0.3114 0.0198  -0.0084 -0.0272 108 ASN C C   
7494  O O   . ASN C 108 ? 0.3086 0.2209 0.3004 0.0200  -0.0100 -0.0316 108 ASN C O   
7495  C CB  . ASN C 108 ? 0.3337 0.2476 0.3416 0.0144  -0.0099 -0.0250 108 ASN C CB  
7496  C CG  . ASN C 108 ? 0.3773 0.2884 0.3856 0.0100  -0.0144 -0.0290 108 ASN C CG  
7497  O OD1 . ASN C 108 ? 0.3810 0.2987 0.3892 0.0082  -0.0166 -0.0292 108 ASN C OD1 
7498  N ND2 . ASN C 108 ? 0.3863 0.2871 0.3949 0.0085  -0.0161 -0.0324 108 ASN C ND2 
7499  N N   . LYS C 109 ? 0.3418 0.2711 0.3369 0.0220  -0.0063 -0.0254 109 LYS C N   
7500  C CA  . LYS C 109 ? 0.3312 0.2587 0.3179 0.0256  -0.0046 -0.0281 109 LYS C CA  
7501  C C   . LYS C 109 ? 0.3116 0.2470 0.2969 0.0241  -0.0050 -0.0270 109 LYS C C   
7502  O O   . LYS C 109 ? 0.3315 0.2755 0.3227 0.0228  -0.0041 -0.0231 109 LYS C O   
7503  C CB  . LYS C 109 ? 0.2943 0.2233 0.2811 0.0312  0.0004  -0.0264 109 LYS C CB  
7504  C CG  . LYS C 109 ? 0.3172 0.2372 0.3044 0.0337  0.0013  -0.0274 109 LYS C CG  
7505  C CD  . LYS C 109 ? 0.3642 0.2871 0.3533 0.0399  0.0063  -0.0250 109 LYS C CD  
7506  C CE  . LYS C 109 ? 0.3499 0.2726 0.3320 0.0442  0.0099  -0.0269 109 LYS C CE  
7507  N NZ  . LYS C 109 ? 0.3954 0.3203 0.3807 0.0509  0.0152  -0.0247 109 LYS C NZ  
7508  N N   . TYR C 110 ? 0.3414 0.2725 0.3180 0.0243  -0.0068 -0.0305 110 TYR C N   
7509  C CA  . TYR C 110 ? 0.3138 0.2505 0.2869 0.0237  -0.0067 -0.0293 110 TYR C CA  
7510  C C   . TYR C 110 ? 0.3289 0.2667 0.2961 0.0285  -0.0012 -0.0287 110 TYR C C   
7511  O O   . TYR C 110 ? 0.3864 0.3167 0.3462 0.0325  0.0007  -0.0317 110 TYR C O   
7512  C CB  . TYR C 110 ? 0.3063 0.2375 0.2727 0.0217  -0.0120 -0.0331 110 TYR C CB  
7513  C CG  . TYR C 110 ? 0.3404 0.2765 0.3041 0.0202  -0.0135 -0.0318 110 TYR C CG  
7514  C CD1 . TYR C 110 ? 0.3490 0.2935 0.3206 0.0176  -0.0130 -0.0277 110 TYR C CD1 
7515  C CD2 . TYR C 110 ? 0.3672 0.2979 0.3192 0.0218  -0.0160 -0.0349 110 TYR C CD2 
7516  C CE1 . TYR C 110 ? 0.3060 0.2537 0.2747 0.0166  -0.0142 -0.0264 110 TYR C CE1 
7517  C CE2 . TYR C 110 ? 0.3782 0.3124 0.3269 0.0210  -0.0177 -0.0334 110 TYR C CE2 
7518  C CZ  . TYR C 110 ? 0.3370 0.2797 0.2947 0.0183  -0.0166 -0.0290 110 TYR C CZ  
7519  O OH  . TYR C 110 ? 0.3392 0.2847 0.2939 0.0177  -0.0178 -0.0272 110 TYR C OH  
7520  N N   . ALA C 111 ? 0.3273 0.2739 0.2976 0.0282  0.0016  -0.0249 111 ALA C N   
7521  C CA  . ALA C 111 ? 0.3656 0.3146 0.3327 0.0324  0.0077  -0.0235 111 ALA C CA  
7522  C C   . ALA C 111 ? 0.3918 0.3323 0.3444 0.0357  0.0087  -0.0269 111 ALA C C   
7523  O O   . ALA C 111 ? 0.4327 0.3716 0.3805 0.0406  0.0145  -0.0269 111 ALA C O   
7524  C CB  . ALA C 111 ? 0.3489 0.3079 0.3221 0.0303  0.0100  -0.0191 111 ALA C CB  
7525  N N   . PHE C 112 ? 0.3819 0.3168 0.3271 0.0335  0.0032  -0.0299 112 PHE C N   
7526  C CA  . PHE C 112 ? 0.4241 0.3503 0.3535 0.0368  0.0030  -0.0333 112 PHE C CA  
7527  C C   . PHE C 112 ? 0.4874 0.4020 0.4095 0.0378  -0.0012 -0.0392 112 PHE C C   
7528  O O   . PHE C 112 ? 0.5355 0.4416 0.4441 0.0393  -0.0044 -0.0432 112 PHE C O   
7529  C CB  . PHE C 112 ? 0.4490 0.3769 0.3742 0.0343  -0.0006 -0.0325 112 PHE C CB  
7530  C CG  . PHE C 112 ? 0.4444 0.3819 0.3758 0.0333  0.0040  -0.0269 112 PHE C CG  
7531  C CD1 . PHE C 112 ? 0.3857 0.3316 0.3306 0.0288  0.0026  -0.0237 112 PHE C CD1 
7532  C CD2 . PHE C 112 ? 0.5317 0.4690 0.4553 0.0368  0.0102  -0.0248 112 PHE C CD2 
7533  C CE1 . PHE C 112 ? 0.3947 0.3482 0.3453 0.0276  0.0063  -0.0193 112 PHE C CE1 
7534  C CE2 . PHE C 112 ? 0.5093 0.4549 0.4398 0.0353  0.0145  -0.0197 112 PHE C CE2 
7535  C CZ  . PHE C 112 ? 0.4611 0.4147 0.4053 0.0304  0.0121  -0.0172 112 PHE C CZ  
7536  N N   . GLY C 113 ? 0.4283 0.3418 0.3586 0.0371  -0.0015 -0.0399 113 GLY C N   
7537  C CA  . GLY C 113 ? 0.4570 0.3586 0.3811 0.0378  -0.0052 -0.0455 113 GLY C CA  
7538  C C   . GLY C 113 ? 0.4729 0.3736 0.4052 0.0319  -0.0124 -0.0471 113 GLY C C   
7539  O O   . GLY C 113 ? 0.4344 0.3397 0.3698 0.0279  -0.0170 -0.0463 113 GLY C O   
7540  N N   . GLY C 114 ? 0.4213 0.3154 0.3574 0.0315  -0.0131 -0.0492 114 GLY C N   
7541  C CA  . GLY C 114 ? 0.4158 0.3073 0.3590 0.0259  -0.0196 -0.0511 114 GLY C CA  
7542  C C   . GLY C 114 ? 0.3807 0.2811 0.3393 0.0225  -0.0183 -0.0459 114 GLY C C   
7543  O O   . GLY C 114 ? 0.3462 0.2536 0.3093 0.0247  -0.0130 -0.0414 114 GLY C O   
7544  N N   . GLU C 115 ? 0.3509 0.2505 0.3176 0.0173  -0.0231 -0.0466 115 GLU C N   
7545  C CA  . GLU C 115 ? 0.3727 0.2790 0.3526 0.0142  -0.0217 -0.0418 115 GLU C CA  
7546  C C   . GLU C 115 ? 0.3722 0.2902 0.3557 0.0131  -0.0209 -0.0375 115 GLU C C   
7547  O O   . GLU C 115 ? 0.3587 0.2791 0.3361 0.0137  -0.0225 -0.0385 115 GLU C O   
7548  C CB  . GLU C 115 ? 0.4136 0.3163 0.4018 0.0088  -0.0263 -0.0433 115 GLU C CB  
7549  C CG  . GLU C 115 ? 0.4518 0.3577 0.4409 0.0053  -0.0324 -0.0453 115 GLU C CG  
7550  C CD  . GLU C 115 ? 0.5330 0.4360 0.5318 -0.0003 -0.0374 -0.0472 115 GLU C CD  
7551  O OE1 . GLU C 115 ? 0.5443 0.4400 0.5474 -0.0018 -0.0367 -0.0483 115 GLU C OE1 
7552  O OE2 . GLU C 115 ? 0.6056 0.5145 0.6090 -0.0033 -0.0418 -0.0473 115 GLU C OE2 
7553  N N   . PHE C 116 ? 0.3161 0.2405 0.3086 0.0119  -0.0184 -0.0328 116 PHE C N   
7554  C CA  . PHE C 116 ? 0.2993 0.2336 0.2952 0.0104  -0.0180 -0.0291 116 PHE C CA  
7555  C C   . PHE C 116 ? 0.3688 0.3044 0.3693 0.0061  -0.0227 -0.0299 116 PHE C C   
7556  O O   . PHE C 116 ? 0.3497 0.2835 0.3580 0.0031  -0.0238 -0.0295 116 PHE C O   
7557  C CB  . PHE C 116 ? 0.2957 0.2356 0.2981 0.0106  -0.0145 -0.0242 116 PHE C CB  
7558  C CG  . PHE C 116 ? 0.3155 0.2640 0.3192 0.0096  -0.0139 -0.0212 116 PHE C CG  
7559  C CD1 . PHE C 116 ? 0.3342 0.2858 0.3324 0.0118  -0.0124 -0.0212 116 PHE C CD1 
7560  C CD2 . PHE C 116 ? 0.3405 0.2926 0.3503 0.0065  -0.0148 -0.0187 116 PHE C CD2 
7561  C CE1 . PHE C 116 ? 0.3557 0.3141 0.3548 0.0106  -0.0118 -0.0186 116 PHE C CE1 
7562  C CE2 . PHE C 116 ? 0.3690 0.3277 0.3789 0.0058  -0.0143 -0.0164 116 PHE C CE2 
7563  C CZ  . PHE C 116 ? 0.3477 0.3091 0.3523 0.0077  -0.0130 -0.0164 116 PHE C CZ  
7564  N N   . PRO C 117 ? 0.3338 0.2722 0.3301 0.0058  -0.0254 -0.0309 117 PRO C N   
7565  C CA  . PRO C 117 ? 0.3509 0.2899 0.3522 0.0022  -0.0308 -0.0324 117 PRO C CA  
7566  C C   . PRO C 117 ? 0.3770 0.3227 0.3893 -0.0006 -0.0295 -0.0281 117 PRO C C   
7567  O O   . PRO C 117 ? 0.4026 0.3538 0.4150 0.0003  -0.0263 -0.0245 117 PRO C O   
7568  C CB  . PRO C 117 ? 0.3679 0.3080 0.3603 0.0039  -0.0337 -0.0339 117 PRO C CB  
7569  C CG  . PRO C 117 ? 0.3709 0.3074 0.3521 0.0083  -0.0299 -0.0348 117 PRO C CG  
7570  C CD  . PRO C 117 ? 0.3333 0.2729 0.3198 0.0090  -0.0241 -0.0312 117 PRO C CD  
7571  N N   . LYS C 118 ? 0.3685 0.3133 0.3901 -0.0041 -0.0319 -0.0286 118 LYS C N   
7572  C CA  . LYS C 118 ? 0.3680 0.3184 0.3998 -0.0063 -0.0298 -0.0243 118 LYS C CA  
7573  C C   . LYS C 118 ? 0.3362 0.2932 0.3695 -0.0068 -0.0320 -0.0232 118 LYS C C   
7574  O O   . LYS C 118 ? 0.3397 0.2969 0.3734 -0.0077 -0.0374 -0.0260 118 LYS C O   
7575  C CB  . LYS C 118 ? 0.3973 0.3449 0.4398 -0.0099 -0.0307 -0.0247 118 LYS C CB  
7576  C CG  . LYS C 118 ? 0.4374 0.3905 0.4904 -0.0119 -0.0276 -0.0200 118 LYS C CG  
7577  C CD  . LYS C 118 ? 0.4868 0.4368 0.5510 -0.0154 -0.0271 -0.0195 118 LYS C CD  
7578  C CE  . LYS C 118 ? 0.5392 0.4958 0.6162 -0.0182 -0.0267 -0.0167 118 LYS C CE  
7579  N NZ  . LYS C 118 ? 0.5093 0.4720 0.5878 -0.0184 -0.0322 -0.0186 118 LYS C NZ  
7580  N N   . PRO C 119 ? 0.3627 0.3246 0.3965 -0.0059 -0.0284 -0.0192 119 PRO C N   
7581  C CA  . PRO C 119 ? 0.3296 0.2971 0.3657 -0.0061 -0.0299 -0.0177 119 PRO C CA  
7582  C C   . PRO C 119 ? 0.3619 0.3325 0.4107 -0.0089 -0.0310 -0.0166 119 PRO C C   
7583  O O   . PRO C 119 ? 0.3326 0.3016 0.3885 -0.0107 -0.0286 -0.0154 119 PRO C O   
7584  C CB  . PRO C 119 ? 0.3190 0.2890 0.3513 -0.0045 -0.0251 -0.0141 119 PRO C CB  
7585  C CG  . PRO C 119 ? 0.3594 0.3266 0.3914 -0.0042 -0.0213 -0.0130 119 PRO C CG  
7586  C CD  . PRO C 119 ? 0.3629 0.3249 0.3946 -0.0045 -0.0231 -0.0162 119 PRO C CD  
7587  N N   . ASP C 120 ? 0.2821 0.2571 0.3341 -0.0090 -0.0345 -0.0166 120 ASP C N   
7588  C CA  . ASP C 120 ? 0.2889 0.2687 0.3549 -0.0112 -0.0348 -0.0147 120 ASP C CA  
7589  C C   . ASP C 120 ? 0.3136 0.2963 0.3823 -0.0102 -0.0284 -0.0099 120 ASP C C   
7590  O O   . ASP C 120 ? 0.2890 0.2736 0.3683 -0.0118 -0.0255 -0.0075 120 ASP C O   
7591  C CB  . ASP C 120 ? 0.2617 0.2460 0.3313 -0.0110 -0.0411 -0.0161 120 ASP C CB  
7592  C CG  . ASP C 120 ? 0.3389 0.3197 0.4060 -0.0122 -0.0484 -0.0212 120 ASP C CG  
7593  O OD1 . ASP C 120 ? 0.3694 0.3462 0.4407 -0.0148 -0.0488 -0.0233 120 ASP C OD1 
7594  O OD2 . ASP C 120 ? 0.3303 0.3116 0.3906 -0.0103 -0.0537 -0.0232 120 ASP C OD2 
7595  N N   . PHE C 121 ? 0.2689 0.2511 0.3276 -0.0077 -0.0260 -0.0086 121 PHE C N   
7596  C CA  . PHE C 121 ? 0.2780 0.2613 0.3366 -0.0066 -0.0204 -0.0048 121 PHE C CA  
7597  C C   . PHE C 121 ? 0.2688 0.2497 0.3153 -0.0047 -0.0187 -0.0046 121 PHE C C   
7598  O O   . PHE C 121 ? 0.2634 0.2432 0.3027 -0.0039 -0.0213 -0.0067 121 PHE C O   
7599  C CB  . PHE C 121 ? 0.2559 0.2442 0.3217 -0.0059 -0.0204 -0.0026 121 PHE C CB  
7600  C CG  . PHE C 121 ? 0.2491 0.2396 0.3113 -0.0043 -0.0251 -0.0039 121 PHE C CG  
7601  C CD1 . PHE C 121 ? 0.2701 0.2592 0.3226 -0.0019 -0.0235 -0.0027 121 PHE C CD1 
7602  C CD2 . PHE C 121 ? 0.2654 0.2587 0.3334 -0.0051 -0.0313 -0.0061 121 PHE C CD2 
7603  C CE1 . PHE C 121 ? 0.2694 0.2596 0.3179 -0.0001 -0.0275 -0.0033 121 PHE C CE1 
7604  C CE2 . PHE C 121 ? 0.2982 0.2930 0.3618 -0.0030 -0.0360 -0.0070 121 PHE C CE2 
7605  C CZ  . PHE C 121 ? 0.2874 0.2805 0.3410 -0.0003 -0.0338 -0.0054 121 PHE C CZ  
7606  N N   . VAL C 122 ? 0.2977 0.2780 0.3424 -0.0040 -0.0142 -0.0019 122 VAL C N   
7607  C CA  . VAL C 122 ? 0.2729 0.2514 0.3081 -0.0028 -0.0125 -0.0014 122 VAL C CA  
7608  C C   . VAL C 122 ? 0.2903 0.2700 0.3247 -0.0016 -0.0117 0.0002  122 VAL C C   
7609  O O   . VAL C 122 ? 0.2898 0.2707 0.3299 -0.0012 -0.0097 0.0021  122 VAL C O   
7610  C CB  . VAL C 122 ? 0.2741 0.2500 0.3069 -0.0027 -0.0089 0.0002  122 VAL C CB  
7611  C CG1 . VAL C 122 ? 0.3113 0.2858 0.3362 -0.0019 -0.0073 0.0010  122 VAL C CG1 
7612  C CG2 . VAL C 122 ? 0.3019 0.2762 0.3346 -0.0031 -0.0097 -0.0012 122 VAL C CG2 
7613  N N   . PHE C 123 ? 0.2465 0.2256 0.2741 -0.0008 -0.0128 -0.0003 123 PHE C N   
7614  C CA  . PHE C 123 ? 0.2593 0.2378 0.2842 0.0004  -0.0116 0.0012  123 PHE C CA  
7615  C C   . PHE C 123 ? 0.3063 0.2820 0.3229 0.0001  -0.0102 0.0011  123 PHE C C   
7616  O O   . PHE C 123 ? 0.2899 0.2655 0.3024 0.0000  -0.0117 0.0001  123 PHE C O   
7617  C CB  . PHE C 123 ? 0.2787 0.2592 0.3048 0.0017  -0.0150 0.0009  123 PHE C CB  
7618  C CG  . PHE C 123 ? 0.2925 0.2724 0.3179 0.0036  -0.0136 0.0030  123 PHE C CG  
7619  C CD1 . PHE C 123 ? 0.3084 0.2908 0.3419 0.0047  -0.0124 0.0047  123 PHE C CD1 
7620  C CD2 . PHE C 123 ? 0.3089 0.2858 0.3263 0.0045  -0.0133 0.0035  123 PHE C CD2 
7621  C CE1 . PHE C 123 ? 0.3215 0.3030 0.3545 0.0072  -0.0109 0.0068  123 PHE C CE1 
7622  C CE2 . PHE C 123 ? 0.3120 0.2868 0.3280 0.0066  -0.0117 0.0056  123 PHE C CE2 
7623  C CZ  . PHE C 123 ? 0.2967 0.2738 0.3203 0.0082  -0.0107 0.0071  123 PHE C CZ  
7624  N N   . GLN C 124 ? 0.2859 0.2589 0.2999 0.0000  -0.0073 0.0023  124 GLN C N   
7625  C CA  . GLN C 124 ? 0.2598 0.2306 0.2680 -0.0011 -0.0066 0.0019  124 GLN C CA  
7626  C C   . GLN C 124 ? 0.2853 0.2521 0.2889 -0.0009 -0.0049 0.0028  124 GLN C C   
7627  O O   . GLN C 124 ? 0.3050 0.2700 0.3095 0.0005  -0.0032 0.0039  124 GLN C O   
7628  C CB  . GLN C 124 ? 0.2667 0.2372 0.2754 -0.0017 -0.0059 0.0017  124 GLN C CB  
7629  C CG  . GLN C 124 ? 0.2533 0.2224 0.2571 -0.0028 -0.0060 0.0013  124 GLN C CG  
7630  C CD  . GLN C 124 ? 0.2621 0.2338 0.2656 -0.0038 -0.0074 0.0004  124 GLN C CD  
7631  O OE1 . GLN C 124 ? 0.2687 0.2412 0.2720 -0.0037 -0.0076 0.0003  124 GLN C OE1 
7632  N NE2 . GLN C 124 ? 0.2342 0.2073 0.2375 -0.0045 -0.0081 0.0000  124 GLN C NE2 
7633  N N   . THR C 125 ? 0.2572 0.2225 0.2566 -0.0025 -0.0051 0.0023  125 THR C N   
7634  C CA  . THR C 125 ? 0.2637 0.2238 0.2581 -0.0032 -0.0038 0.0026  125 THR C CA  
7635  C C   . THR C 125 ? 0.3116 0.2706 0.3038 -0.0047 -0.0043 0.0016  125 THR C C   
7636  O O   . THR C 125 ? 0.3064 0.2692 0.3006 -0.0058 -0.0058 0.0009  125 THR C O   
7637  C CB  . THR C 125 ? 0.2775 0.2365 0.2697 -0.0042 -0.0038 0.0029  125 THR C CB  
7638  O OG1 . THR C 125 ? 0.2963 0.2551 0.2889 -0.0020 -0.0036 0.0041  125 THR C OG1 
7639  C CG2 . THR C 125 ? 0.2844 0.2373 0.2719 -0.0061 -0.0028 0.0027  125 THR C CG2 
7640  N N   . GLN C 126 ? 0.2673 0.2207 0.2547 -0.0044 -0.0032 0.0014  126 GLN C N   
7641  C CA  . GLN C 126 ? 0.3068 0.2582 0.2904 -0.0055 -0.0045 0.0003  126 GLN C CA  
7642  C C   . GLN C 126 ? 0.3135 0.2595 0.2919 -0.0077 -0.0053 -0.0009 126 GLN C C   
7643  O O   . GLN C 126 ? 0.3061 0.2453 0.2795 -0.0067 -0.0035 -0.0010 126 GLN C O   
7644  C CB  . GLN C 126 ? 0.2813 0.2296 0.2617 -0.0031 -0.0028 0.0009  126 GLN C CB  
7645  C CG  . GLN C 126 ? 0.2786 0.2258 0.2548 -0.0035 -0.0048 0.0001  126 GLN C CG  
7646  C CD  . GLN C 126 ? 0.3044 0.2447 0.2720 -0.0046 -0.0064 -0.0017 126 GLN C CD  
7647  O OE1 . GLN C 126 ? 0.3079 0.2410 0.2689 -0.0030 -0.0040 -0.0018 126 GLN C OE1 
7648  N NE2 . GLN C 126 ? 0.2954 0.2379 0.2635 -0.0074 -0.0106 -0.0032 126 GLN C NE2 
7649  N N   . ILE C 127 ? 0.2938 0.2425 0.2741 -0.0107 -0.0080 -0.0019 127 ILE C N   
7650  C CA  . ILE C 127 ? 0.2688 0.2126 0.2455 -0.0137 -0.0096 -0.0034 127 ILE C CA  
7651  C C   . ILE C 127 ? 0.3078 0.2555 0.2864 -0.0158 -0.0137 -0.0047 127 ILE C C   
7652  O O   . ILE C 127 ? 0.3181 0.2609 0.2912 -0.0170 -0.0164 -0.0066 127 ILE C O   
7653  C CB  . ILE C 127 ? 0.2672 0.2101 0.2463 -0.0159 -0.0083 -0.0028 127 ILE C CB  
7654  C CG1 . ILE C 127 ? 0.3137 0.2496 0.2889 -0.0194 -0.0099 -0.0046 127 ILE C CG1 
7655  C CG2 . ILE C 127 ? 0.2883 0.2396 0.2750 -0.0169 -0.0081 -0.0015 127 ILE C CG2 
7656  C CD1 . ILE C 127 ? 0.3331 0.2649 0.3091 -0.0215 -0.0076 -0.0036 127 ILE C CD1 
7657  N N   . CYS C 128 ? 0.2940 0.2505 0.2800 -0.0158 -0.0144 -0.0038 128 CYS C N   
7658  C CA  . CYS C 128 ? 0.2811 0.2425 0.2698 -0.0163 -0.0181 -0.0045 128 CYS C CA  
7659  C C   . CYS C 128 ? 0.2968 0.2563 0.2804 -0.0128 -0.0184 -0.0041 128 CYS C C   
7660  O O   . CYS C 128 ? 0.2973 0.2563 0.2808 -0.0102 -0.0152 -0.0029 128 CYS C O   
7661  C CB  . CYS C 128 ? 0.2672 0.2379 0.2653 -0.0166 -0.0177 -0.0033 128 CYS C CB  
7662  S SG  . CYS C 128 ? 0.2886 0.2665 0.2917 -0.0163 -0.0220 -0.0036 128 CYS C SG  
7663  N N   . CYS C 129 ? 0.2957 0.2538 0.2752 -0.0127 -0.0222 -0.0052 129 CYS C N   
7664  C CA  . CYS C 129 ? 0.2927 0.2479 0.2663 -0.0089 -0.0216 -0.0042 129 CYS C CA  
7665  C C   . CYS C 129 ? 0.2958 0.2570 0.2760 -0.0068 -0.0196 -0.0023 129 CYS C C   
7666  O O   . CYS C 129 ? 0.3323 0.2905 0.3097 -0.0040 -0.0167 -0.0009 129 CYS C O   
7667  C CB  . CYS C 129 ? 0.2793 0.2327 0.2471 -0.0084 -0.0266 -0.0052 129 CYS C CB  
7668  S SG  . CYS C 129 ? 0.3400 0.2841 0.2979 -0.0109 -0.0295 -0.0083 129 CYS C SG  
7669  N N   . SER C 130 ? 0.3110 0.2800 0.3000 -0.0080 -0.0207 -0.0021 130 SER C N   
7670  C CA  . SER C 130 ? 0.2630 0.2363 0.2569 -0.0056 -0.0191 -0.0007 130 SER C CA  
7671  C C   . SER C 130 ? 0.2717 0.2442 0.2676 -0.0051 -0.0152 -0.0002 130 SER C C   
7672  O O   . SER C 130 ? 0.2764 0.2506 0.2753 -0.0034 -0.0138 0.0005  130 SER C O   
7673  C CB  . SER C 130 ? 0.2685 0.2499 0.2705 -0.0063 -0.0212 -0.0008 130 SER C CB  
7674  O OG  . SER C 130 ? 0.3022 0.2851 0.3034 -0.0063 -0.0257 -0.0010 130 SER C OG  
7675  N N   . HIS C 131 ? 0.2613 0.2311 0.2557 -0.0066 -0.0136 -0.0007 131 HIS C N   
7676  C CA  . HIS C 131 ? 0.2608 0.2303 0.2572 -0.0059 -0.0109 -0.0002 131 HIS C CA  
7677  C C   . HIS C 131 ? 0.2718 0.2387 0.2672 -0.0037 -0.0089 0.0008  131 HIS C C   
7678  O O   . HIS C 131 ? 0.2824 0.2511 0.2821 -0.0029 -0.0078 0.0011  131 HIS C O   
7679  C CB  . HIS C 131 ? 0.2918 0.2580 0.2858 -0.0072 -0.0097 -0.0004 131 HIS C CB  
7680  C CG  . HIS C 131 ? 0.2941 0.2630 0.2906 -0.0094 -0.0102 -0.0007 131 HIS C CG  
7681  N ND1 . HIS C 131 ? 0.2747 0.2398 0.2686 -0.0115 -0.0100 -0.0011 131 HIS C ND1 
7682  C CD2 . HIS C 131 ? 0.2887 0.2631 0.2901 -0.0097 -0.0102 -0.0006 131 HIS C CD2 
7683  C CE1 . HIS C 131 ? 0.2878 0.2564 0.2856 -0.0133 -0.0097 -0.0008 131 HIS C CE1 
7684  N NE2 . HIS C 131 ? 0.2598 0.2341 0.2618 -0.0120 -0.0096 -0.0004 131 HIS C NE2 
7685  N N   . SER C 132 ? 0.2849 0.2468 0.2745 -0.0026 -0.0084 0.0013  132 SER C N   
7686  C CA  . SER C 132 ? 0.2991 0.2583 0.2883 -0.0005 -0.0056 0.0029  132 SER C CA  
7687  C C   . SER C 132 ? 0.2673 0.2284 0.2588 0.0006  -0.0062 0.0037  132 SER C C   
7688  O O   . SER C 132 ? 0.3098 0.2718 0.3063 0.0012  -0.0045 0.0046  132 SER C O   
7689  C CB  . SER C 132 ? 0.2587 0.2111 0.2394 0.0010  -0.0038 0.0036  132 SER C CB  
7690  O OG  . SER C 132 ? 0.3097 0.2600 0.2839 0.0011  -0.0068 0.0029  132 SER C OG  
7691  N N   . LYS C 133 ? 0.2907 0.2524 0.2793 0.0009  -0.0091 0.0034  133 LYS C N   
7692  C CA  . LYS C 133 ? 0.2718 0.2342 0.2615 0.0028  -0.0095 0.0046  133 LYS C CA  
7693  C C   . LYS C 133 ? 0.2854 0.2522 0.2829 0.0025  -0.0094 0.0041  133 LYS C C   
7694  O O   . LYS C 133 ? 0.2826 0.2481 0.2823 0.0039  -0.0079 0.0052  133 LYS C O   
7695  C CB  . LYS C 133 ? 0.2976 0.2605 0.2831 0.0036  -0.0134 0.0045  133 LYS C CB  
7696  C CG  . LYS C 133 ? 0.3039 0.2606 0.2790 0.0041  -0.0143 0.0044  133 LYS C CG  
7697  C CD  . LYS C 133 ? 0.3282 0.2780 0.2971 0.0068  -0.0102 0.0066  133 LYS C CD  
7698  C CE  . LYS C 133 ? 0.3297 0.2720 0.2870 0.0076  -0.0098 0.0062  133 LYS C CE  
7699  N NZ  . LYS C 133 ? 0.3654 0.3017 0.3193 0.0100  -0.0034 0.0087  133 LYS C NZ  
7700  N N   . TRP C 134 ? 0.2557 0.2270 0.2569 0.0008  -0.0106 0.0026  134 TRP C N   
7701  C CA  . TRP C 134 ? 0.2261 0.2006 0.2327 0.0009  -0.0103 0.0017  134 TRP C CA  
7702  C C   . TRP C 134 ? 0.2711 0.2430 0.2800 0.0011  -0.0083 0.0019  134 TRP C C   
7703  O O   . TRP C 134 ? 0.2945 0.2657 0.3061 0.0022  -0.0080 0.0018  134 TRP C O   
7704  C CB  . TRP C 134 ? 0.2387 0.2167 0.2467 -0.0008 -0.0109 0.0004  134 TRP C CB  
7705  C CG  . TRP C 134 ? 0.2417 0.2226 0.2531 -0.0004 -0.0104 -0.0006 134 TRP C CG  
7706  C CD1 . TRP C 134 ? 0.2691 0.2485 0.2821 0.0008  -0.0098 -0.0013 134 TRP C CD1 
7707  C CD2 . TRP C 134 ? 0.2450 0.2298 0.2579 -0.0010 -0.0103 -0.0011 134 TRP C CD2 
7708  N NE1 . TRP C 134 ? 0.2799 0.2614 0.2935 0.0013  -0.0095 -0.0026 134 TRP C NE1 
7709  C CE2 . TRP C 134 ? 0.2916 0.2767 0.3054 0.0004  -0.0093 -0.0021 134 TRP C CE2 
7710  C CE3 . TRP C 134 ? 0.2479 0.2356 0.2616 -0.0028 -0.0107 -0.0008 134 TRP C CE3 
7711  C CZ2 . TRP C 134 ? 0.2673 0.2552 0.2814 0.0006  -0.0080 -0.0025 134 TRP C CZ2 
7712  C CZ3 . TRP C 134 ? 0.2646 0.2558 0.2805 -0.0031 -0.0093 -0.0009 134 TRP C CZ3 
7713  C CH2 . TRP C 134 ? 0.2714 0.2627 0.2871 -0.0010 -0.0075 -0.0016 134 TRP C CH2 
7714  N N   . TYR C 135 ? 0.2598 0.2305 0.2687 0.0001  -0.0072 0.0019  135 TYR C N   
7715  C CA  . TYR C 135 ? 0.2653 0.2352 0.2788 -0.0002 -0.0061 0.0019  135 TYR C CA  
7716  C C   . TYR C 135 ? 0.2706 0.2369 0.2851 0.0004  -0.0035 0.0040  135 TYR C C   
7717  O O   . TYR C 135 ? 0.3011 0.2670 0.3213 -0.0001 -0.0026 0.0041  135 TYR C O   
7718  C CB  . TYR C 135 ? 0.2883 0.2597 0.3031 -0.0012 -0.0065 0.0011  135 TYR C CB  
7719  C CG  . TYR C 135 ? 0.2768 0.2509 0.2911 -0.0015 -0.0085 -0.0007 135 TYR C CG  
7720  C CD1 . TYR C 135 ? 0.2898 0.2643 0.3065 -0.0012 -0.0097 -0.0023 135 TYR C CD1 
7721  C CD2 . TYR C 135 ? 0.2917 0.2670 0.3026 -0.0020 -0.0088 -0.0009 135 TYR C CD2 
7722  C CE1 . TYR C 135 ? 0.3309 0.3069 0.3453 -0.0008 -0.0108 -0.0038 135 TYR C CE1 
7723  C CE2 . TYR C 135 ? 0.2862 0.2636 0.2963 -0.0020 -0.0095 -0.0019 135 TYR C CE2 
7724  C CZ  . TYR C 135 ? 0.3233 0.3010 0.3346 -0.0011 -0.0102 -0.0033 135 TYR C CZ  
7725  O OH  . TYR C 135 ? 0.3343 0.3131 0.3432 -0.0005 -0.0102 -0.0043 135 TYR C OH  
7726  N N   . GLN C 136 ? 0.2821 0.2455 0.2910 0.0016  -0.0021 0.0057  136 GLN C N   
7727  C CA  . GLN C 136 ? 0.2561 0.2152 0.2645 0.0029  0.0012  0.0082  136 GLN C CA  
7728  C C   . GLN C 136 ? 0.2737 0.2318 0.2850 0.0034  0.0009  0.0086  136 GLN C C   
7729  O O   . GLN C 136 ? 0.2946 0.2502 0.3104 0.0032  0.0036  0.0100  136 GLN C O   
7730  C CB  . GLN C 136 ? 0.2737 0.2286 0.2727 0.0047  0.0021  0.0097  136 GLN C CB  
7731  C CG  . GLN C 136 ? 0.3161 0.2698 0.3122 0.0045  0.0039  0.0096  136 GLN C CG  
7732  C CD  . GLN C 136 ? 0.3009 0.2486 0.2859 0.0065  0.0050  0.0106  136 GLN C CD  
7733  O OE1 . GLN C 136 ? 0.3267 0.2740 0.3058 0.0067  0.0014  0.0095  136 GLN C OE1 
7734  N NE2 . GLN C 136 ? 0.3103 0.2534 0.2928 0.0083  0.0100  0.0130  136 GLN C NE2 
7735  N N   . HIS C 137 ? 0.2533 0.2129 0.2624 0.0043  -0.0019 0.0075  137 HIS C N   
7736  C CA  . HIS C 137 ? 0.2738 0.2317 0.2853 0.0054  -0.0019 0.0078  137 HIS C CA  
7737  C C   . HIS C 137 ? 0.2810 0.2397 0.2994 0.0036  -0.0022 0.0057  137 HIS C C   
7738  O O   . HIS C 137 ? 0.2866 0.2416 0.3088 0.0034  -0.0007 0.0064  137 HIS C O   
7739  C CB  . HIS C 137 ? 0.2509 0.2111 0.2594 0.0073  -0.0047 0.0073  137 HIS C CB  
7740  C CG  . HIS C 137 ? 0.2563 0.2142 0.2664 0.0094  -0.0044 0.0079  137 HIS C CG  
7741  N ND1 . HIS C 137 ? 0.3030 0.2550 0.3108 0.0113  -0.0023 0.0108  137 HIS C ND1 
7742  C CD2 . HIS C 137 ? 0.2807 0.2401 0.2941 0.0100  -0.0054 0.0060  137 HIS C CD2 
7743  C CE1 . HIS C 137 ? 0.3019 0.2519 0.3119 0.0130  -0.0023 0.0106  137 HIS C CE1 
7744  N NE2 . HIS C 137 ? 0.2793 0.2337 0.2927 0.0123  -0.0041 0.0076  137 HIS C NE2 
7745  N N   . VAL C 138 ? 0.2581 0.2210 0.2779 0.0023  -0.0044 0.0031  138 VAL C N   
7746  C CA  . VAL C 138 ? 0.2808 0.2441 0.3053 0.0009  -0.0057 0.0007  138 VAL C CA  
7747  C C   . VAL C 138 ? 0.2783 0.2400 0.3089 -0.0010 -0.0044 0.0014  138 VAL C C   
7748  O O   . VAL C 138 ? 0.2624 0.2218 0.2980 -0.0021 -0.0048 0.0004  138 VAL C O   
7749  C CB  . VAL C 138 ? 0.2746 0.2419 0.2975 0.0004  -0.0079 -0.0015 138 VAL C CB  
7750  C CG1 . VAL C 138 ? 0.3064 0.2734 0.3327 -0.0009 -0.0099 -0.0041 138 VAL C CG1 
7751  C CG2 . VAL C 138 ? 0.2726 0.2420 0.2919 0.0020  -0.0087 -0.0023 138 VAL C CG2 
7752  N N   . ALA C 139 ? 0.2596 0.2228 0.2908 -0.0014 -0.0028 0.0032  139 ALA C N   
7753  C CA  . ALA C 139 ? 0.2867 0.2501 0.3259 -0.0031 -0.0012 0.0041  139 ALA C CA  
7754  C C   . ALA C 139 ? 0.3023 0.2612 0.3451 -0.0033 0.0021  0.0065  139 ALA C C   
7755  O O   . ALA C 139 ? 0.2933 0.2519 0.3452 -0.0055 0.0025  0.0065  139 ALA C O   
7756  C CB  . ALA C 139 ? 0.3166 0.2822 0.3553 -0.0027 0.0007  0.0059  139 ALA C CB  
7757  N N   . LYS C 140 ? 0.3016 0.2567 0.3375 -0.0011 0.0043  0.0087  140 LYS C N   
7758  C CA  . LYS C 140 ? 0.3012 0.2508 0.3389 -0.0007 0.0080  0.0116  140 LYS C CA  
7759  C C   . LYS C 140 ? 0.2966 0.2432 0.3376 -0.0014 0.0061  0.0097  140 LYS C C   
7760  O O   . LYS C 140 ? 0.3196 0.2624 0.3673 -0.0031 0.0084  0.0109  140 LYS C O   
7761  C CB  . LYS C 140 ? 0.3155 0.2615 0.3431 0.0026  0.0102  0.0145  140 LYS C CB  
7762  C CG  . LYS C 140 ? 0.3925 0.3316 0.4194 0.0039  0.0147  0.0183  140 LYS C CG  
7763  C CD  . LYS C 140 ? 0.3921 0.3281 0.4156 0.0057  0.0127  0.0179  140 LYS C CD  
7764  C CE  . LYS C 140 ? 0.4171 0.3553 0.4317 0.0084  0.0093  0.0170  140 LYS C CE  
7765  N NZ  . LYS C 140 ? 0.4456 0.3796 0.4567 0.0114  0.0088  0.0183  140 LYS C NZ  
7766  N N   . GLU C 141 ? 0.3091 0.2567 0.3455 -0.0002 0.0026  0.0069  141 GLU C N   
7767  C CA  . GLU C 141 ? 0.3394 0.2831 0.3776 -0.0002 0.0011  0.0047  141 GLU C CA  
7768  C C   . GLU C 141 ? 0.3203 0.2646 0.3658 -0.0035 -0.0015 0.0013  141 GLU C C   
7769  O O   . GLU C 141 ? 0.3458 0.2847 0.3949 -0.0047 -0.0019 -0.0001 141 GLU C O   
7770  C CB  . GLU C 141 ? 0.3390 0.2843 0.3707 0.0025  -0.0013 0.0029  141 GLU C CB  
7771  C CG  . GLU C 141 ? 0.3579 0.3022 0.3836 0.0059  0.0002  0.0060  141 GLU C CG  
7772  C CD  . GLU C 141 ? 0.3748 0.3114 0.4006 0.0075  0.0028  0.0085  141 GLU C CD  
7773  O OE1 . GLU C 141 ? 0.3666 0.2993 0.3955 0.0070  0.0023  0.0064  141 GLU C OE1 
7774  O OE2 . GLU C 141 ? 0.3925 0.3265 0.4145 0.0093  0.0053  0.0124  141 GLU C OE2 
7775  N N   . GLU C 142 ? 0.3093 0.2594 0.3567 -0.0050 -0.0038 -0.0003 142 GLU C N   
7776  C CA  . GLU C 142 ? 0.2906 0.2418 0.3444 -0.0079 -0.0075 -0.0037 142 GLU C CA  
7777  C C   . GLU C 142 ? 0.2973 0.2503 0.3622 -0.0109 -0.0060 -0.0018 142 GLU C C   
7778  O O   . GLU C 142 ? 0.3427 0.2965 0.4152 -0.0138 -0.0094 -0.0044 142 GLU C O   
7779  C CB  . GLU C 142 ? 0.2932 0.2496 0.3426 -0.0073 -0.0112 -0.0063 142 GLU C CB  
7780  C CG  . GLU C 142 ? 0.3544 0.3104 0.3944 -0.0044 -0.0122 -0.0080 142 GLU C CG  
7781  C CD  . GLU C 142 ? 0.4114 0.3626 0.4492 -0.0042 -0.0148 -0.0121 142 GLU C CD  
7782  O OE1 . GLU C 142 ? 0.3907 0.3372 0.4341 -0.0062 -0.0155 -0.0132 142 GLU C OE1 
7783  O OE2 . GLU C 142 ? 0.3392 0.2909 0.3699 -0.0019 -0.0158 -0.0140 142 GLU C OE2 
7784  N N   . LYS C 143 ? 0.2975 0.2513 0.3636 -0.0102 -0.0011 0.0027  143 LYS C N   
7785  C CA  . LYS C 143 ? 0.2795 0.2359 0.3566 -0.0124 0.0017  0.0052  143 LYS C CA  
7786  C C   . LYS C 143 ? 0.2917 0.2553 0.3748 -0.0138 -0.0024 0.0031  143 LYS C C   
7787  O O   . LYS C 143 ? 0.3038 0.2698 0.3986 -0.0170 -0.0049 0.0019  143 LYS C O   
7788  C CB  . LYS C 143 ? 0.3361 0.2882 0.4236 -0.0155 0.0034  0.0061  143 LYS C CB  
7789  C CG  . LYS C 143 ? 0.4757 0.4194 0.5586 -0.0141 0.0082  0.0091  143 LYS C CG  
7790  C CD  . LYS C 143 ? 0.5171 0.4553 0.6084 -0.0176 0.0068  0.0072  143 LYS C CD  
7791  C CE  . LYS C 143 ? 0.5332 0.4622 0.6222 -0.0165 0.0121  0.0107  143 LYS C CE  
7792  N NZ  . LYS C 143 ? 0.6546 0.5830 0.7402 -0.0140 0.0192  0.0169  143 LYS C NZ  
7793  N N   . ILE C 144 ? 0.2780 0.2451 0.3535 -0.0115 -0.0031 0.0030  144 ILE C N   
7794  C CA  . ILE C 144 ? 0.2731 0.2463 0.3519 -0.0118 -0.0069 0.0014  144 ILE C CA  
7795  C C   . ILE C 144 ? 0.2797 0.2556 0.3559 -0.0096 -0.0031 0.0045  144 ILE C C   
7796  O O   . ILE C 144 ? 0.3054 0.2780 0.3731 -0.0075 0.0008  0.0066  144 ILE C O   
7797  C CB  . ILE C 144 ? 0.2575 0.2308 0.3279 -0.0109 -0.0125 -0.0027 144 ILE C CB  
7798  C CG1 . ILE C 144 ? 0.3176 0.2884 0.3754 -0.0083 -0.0107 -0.0023 144 ILE C CG1 
7799  C CG2 . ILE C 144 ? 0.2907 0.2604 0.3635 -0.0130 -0.0165 -0.0063 144 ILE C CG2 
7800  C CD1 . ILE C 144 ? 0.3115 0.2831 0.3614 -0.0071 -0.0147 -0.0054 144 ILE C CD1 
7801  N N   . PRO C 145 ? 0.2596 0.2411 0.3425 -0.0096 -0.0046 0.0048  145 PRO C N   
7802  C CA  . PRO C 145 ? 0.2490 0.2320 0.3285 -0.0071 -0.0010 0.0073  145 PRO C CA  
7803  C C   . PRO C 145 ? 0.2596 0.2406 0.3257 -0.0051 -0.0026 0.0059  145 PRO C C   
7804  O O   . PRO C 145 ? 0.2783 0.2591 0.3395 -0.0055 -0.0071 0.0029  145 PRO C O   
7805  C CB  . PRO C 145 ? 0.2863 0.2762 0.3777 -0.0074 -0.0029 0.0077  145 PRO C CB  
7806  C CG  . PRO C 145 ? 0.3373 0.3294 0.4368 -0.0104 -0.0091 0.0046  145 PRO C CG  
7807  C CD  . PRO C 145 ? 0.3114 0.2977 0.4068 -0.0120 -0.0091 0.0031  145 PRO C CD  
7808  N N   . GLU C 146 ? 0.2423 0.2216 0.3024 -0.0029 0.0015  0.0081  146 GLU C N   
7809  C CA  . GLU C 146 ? 0.2427 0.2195 0.2908 -0.0016 0.0006  0.0070  146 GLU C CA  
7810  C C   . GLU C 146 ? 0.2643 0.2405 0.3093 0.0004  0.0033  0.0087  146 GLU C C   
7811  O O   . GLU C 146 ? 0.2783 0.2534 0.3256 0.0017  0.0082  0.0113  146 GLU C O   
7812  C CB  . GLU C 146 ? 0.2744 0.2464 0.3143 -0.0014 0.0022  0.0073  146 GLU C CB  
7813  C CG  . GLU C 146 ? 0.2989 0.2672 0.3378 -0.0001 0.0080  0.0105  146 GLU C CG  
7814  C CD  . GLU C 146 ? 0.3622 0.3258 0.3934 0.0005  0.0088  0.0110  146 GLU C CD  
7815  O OE1 . GLU C 146 ? 0.3374 0.3000 0.3607 0.0009  0.0061  0.0095  146 GLU C OE1 
7816  O OE2 . GLU C 146 ? 0.4217 0.3827 0.4557 0.0007  0.0121  0.0132  146 GLU C OE2 
7817  N N   . PHE C 147 ? 0.2561 0.2324 0.2954 0.0010  0.0007  0.0073  147 PHE C N   
7818  C CA  . PHE C 147 ? 0.2803 0.2548 0.3155 0.0030  0.0028  0.0084  147 PHE C CA  
7819  C C   . PHE C 147 ? 0.2623 0.2328 0.2863 0.0027  0.0016  0.0070  147 PHE C C   
7820  O O   . PHE C 147 ? 0.2812 0.2530 0.3031 0.0014  -0.0018 0.0052  147 PHE C O   
7821  C CB  . PHE C 147 ? 0.2334 0.2122 0.2750 0.0039  0.0005  0.0086  147 PHE C CB  
7822  C CG  . PHE C 147 ? 0.2540 0.2303 0.2917 0.0064  0.0030  0.0100  147 PHE C CG  
7823  C CD1 . PHE C 147 ? 0.3055 0.2815 0.3475 0.0087  0.0077  0.0124  147 PHE C CD1 
7824  C CD2 . PHE C 147 ? 0.2820 0.2553 0.3113 0.0066  0.0010  0.0089  147 PHE C CD2 
7825  C CE1 . PHE C 147 ? 0.3600 0.3324 0.3974 0.0115  0.0103  0.0135  147 PHE C CE1 
7826  C CE2 . PHE C 147 ? 0.3400 0.3096 0.3652 0.0090  0.0034  0.0101  147 PHE C CE2 
7827  C CZ  . PHE C 147 ? 0.3153 0.2843 0.3443 0.0115  0.0079  0.0122  147 PHE C CZ  
7828  N N   . TYR C 148 ? 0.2527 0.2181 0.2696 0.0039  0.0046  0.0078  148 TYR C N   
7829  C CA  . TYR C 148 ? 0.2480 0.2095 0.2556 0.0031  0.0034  0.0064  148 TYR C CA  
7830  C C   . TYR C 148 ? 0.2860 0.2435 0.2896 0.0046  0.0052  0.0069  148 TYR C C   
7831  O O   . TYR C 148 ? 0.2851 0.2396 0.2882 0.0069  0.0090  0.0083  148 TYR C O   
7832  C CB  . TYR C 148 ? 0.2723 0.2294 0.2729 0.0028  0.0045  0.0061  148 TYR C CB  
7833  C CG  . TYR C 148 ? 0.2727 0.2330 0.2770 0.0019  0.0032  0.0060  148 TYR C CG  
7834  C CD1 . TYR C 148 ? 0.2832 0.2445 0.2933 0.0027  0.0057  0.0077  148 TYR C CD1 
7835  C CD2 . TYR C 148 ? 0.2779 0.2399 0.2805 0.0003  -0.0001 0.0044  148 TYR C CD2 
7836  C CE1 . TYR C 148 ? 0.2904 0.2533 0.3036 0.0018  0.0047  0.0076  148 TYR C CE1 
7837  C CE2 . TYR C 148 ? 0.2788 0.2430 0.2846 0.0000  -0.0011 0.0044  148 TYR C CE2 
7838  C CZ  . TYR C 148 ? 0.2959 0.2598 0.3061 0.0007  0.0012  0.0058  148 TYR C CZ  
7839  O OH  . TYR C 148 ? 0.3118 0.2766 0.3248 0.0004  0.0003  0.0057  148 TYR C OH  
7840  N N   . LEU C 149 ? 0.2757 0.2325 0.2762 0.0037  0.0029  0.0060  149 LEU C N   
7841  C CA  . LEU C 149 ? 0.3013 0.2526 0.2966 0.0048  0.0044  0.0063  149 LEU C CA  
7842  C C   . LEU C 149 ? 0.2822 0.2271 0.2686 0.0029  0.0044  0.0048  149 LEU C C   
7843  O O   . LEU C 149 ? 0.3121 0.2582 0.2973 0.0002  0.0018  0.0036  149 LEU C O   
7844  C CB  . LEU C 149 ? 0.2795 0.2331 0.2765 0.0047  0.0021  0.0066  149 LEU C CB  
7845  C CG  . LEU C 149 ? 0.2689 0.2160 0.2605 0.0059  0.0038  0.0073  149 LEU C CG  
7846  C CD1 . LEU C 149 ? 0.3157 0.2616 0.3101 0.0099  0.0068  0.0092  149 LEU C CD1 
7847  C CD2 . LEU C 149 ? 0.2984 0.2463 0.2891 0.0054  0.0017  0.0078  149 LEU C CD2 
7848  N N   . ASP C 150 ? 0.2961 0.2341 0.2764 0.0045  0.0072  0.0047  150 ASP C N   
7849  C CA  . ASP C 150 ? 0.2974 0.2282 0.2684 0.0027  0.0063  0.0027  150 ASP C CA  
7850  C C   . ASP C 150 ? 0.3071 0.2325 0.2746 0.0019  0.0063  0.0022  150 ASP C C   
7851  O O   . ASP C 150 ? 0.3194 0.2395 0.2844 0.0047  0.0093  0.0031  150 ASP C O   
7852  C CB  . ASP C 150 ? 0.2959 0.2203 0.2601 0.0054  0.0096  0.0028  150 ASP C CB  
7853  C CG  . ASP C 150 ? 0.3430 0.2578 0.2954 0.0043  0.0085  0.0003  150 ASP C CG  
7854  O OD1 . ASP C 150 ? 0.3206 0.2355 0.2723 0.0006  0.0045  -0.0015 150 ASP C OD1 
7855  O OD2 . ASP C 150 ? 0.3266 0.2339 0.2708 0.0071  0.0116  0.0001  150 ASP C OD2 
7856  N N   . VAL C 151 ? 0.2604 0.1873 0.2285 -0.0017 0.0033  0.0012  151 VAL C N   
7857  C CA  . VAL C 151 ? 0.3164 0.2376 0.2816 -0.0030 0.0037  0.0012  151 VAL C CA  
7858  C C   . VAL C 151 ? 0.3095 0.2223 0.2673 -0.0059 0.0024  -0.0014 151 VAL C C   
7859  O O   . VAL C 151 ? 0.3241 0.2319 0.2802 -0.0082 0.0024  -0.0017 151 VAL C O   
7860  C CB  . VAL C 151 ? 0.3031 0.2300 0.2736 -0.0051 0.0022  0.0022  151 VAL C CB  
7861  C CG1 . VAL C 151 ? 0.3161 0.2498 0.2923 -0.0021 0.0026  0.0042  151 VAL C CG1 
7862  C CG2 . VAL C 151 ? 0.3156 0.2472 0.2885 -0.0089 -0.0007 0.0008  151 VAL C CG2 
7863  N N   . GLY C 152 ? 0.3228 0.2326 0.2752 -0.0056 0.0016  -0.0031 152 GLY C N   
7864  C CA  . GLY C 152 ? 0.3209 0.2235 0.2661 -0.0086 -0.0011 -0.0061 152 GLY C CA  
7865  C C   . GLY C 152 ? 0.3473 0.2367 0.2828 -0.0070 0.0013  -0.0074 152 GLY C C   
7866  O O   . GLY C 152 ? 0.3919 0.2741 0.3181 -0.0047 0.0021  -0.0090 152 GLY C O   
7867  N N   . VAL C 153 ? 0.3543 0.2396 0.2909 -0.0078 0.0029  -0.0066 153 VAL C N   
7868  C CA  . VAL C 153 ? 0.3912 0.2631 0.3187 -0.0059 0.0056  -0.0077 153 VAL C CA  
7869  C C   . VAL C 153 ? 0.3814 0.2449 0.3053 -0.0112 0.0030  -0.0103 153 VAL C C   
7870  O O   . VAL C 153 ? 0.3945 0.2458 0.3113 -0.0103 0.0051  -0.0112 153 VAL C O   
7871  C CB  . VAL C 153 ? 0.3773 0.2490 0.3078 -0.0014 0.0103  -0.0043 153 VAL C CB  
7872  C CG1 . VAL C 153 ? 0.3773 0.2561 0.3116 0.0037  0.0131  -0.0021 153 VAL C CG1 
7873  C CG2 . VAL C 153 ? 0.3878 0.2657 0.3265 -0.0038 0.0095  -0.0019 153 VAL C CG2 
7874  N N   . GLY C 154 ? 0.3717 0.2411 0.3007 -0.0166 -0.0017 -0.0116 154 GLY C N   
7875  C CA  . GLY C 154 ? 0.3593 0.2216 0.2868 -0.0224 -0.0048 -0.0143 154 GLY C CA  
7876  C C   . GLY C 154 ? 0.3439 0.2077 0.2790 -0.0250 -0.0026 -0.0116 154 GLY C C   
7877  O O   . GLY C 154 ? 0.3666 0.2371 0.3068 -0.0219 0.0006  -0.0078 154 GLY C O   
7878  N N   . PRO C 155 ? 0.3578 0.2150 0.2934 -0.0308 -0.0046 -0.0134 155 PRO C N   
7879  C CA  . PRO C 155 ? 0.4107 0.2693 0.3539 -0.0340 -0.0022 -0.0104 155 PRO C CA  
7880  C C   . PRO C 155 ? 0.3872 0.2398 0.3269 -0.0292 0.0035  -0.0070 155 PRO C C   
7881  O O   . PRO C 155 ? 0.3679 0.2086 0.2983 -0.0259 0.0055  -0.0080 155 PRO C O   
7882  C CB  . PRO C 155 ? 0.3950 0.2437 0.3372 -0.0409 -0.0050 -0.0137 155 PRO C CB  
7883  C CG  . PRO C 155 ? 0.4212 0.2700 0.3594 -0.0425 -0.0112 -0.0185 155 PRO C CG  
7884  C CD  . PRO C 155 ? 0.4067 0.2557 0.3364 -0.0350 -0.0095 -0.0183 155 PRO C CD  
7885  N N   . TYR C 156 ? 0.3874 0.2476 0.3341 -0.0287 0.0060  -0.0028 156 TYR C N   
7886  C CA  . TYR C 156 ? 0.3765 0.2312 0.3200 -0.0242 0.0107  0.0010  156 TYR C CA  
7887  C C   . TYR C 156 ? 0.3699 0.2077 0.3066 -0.0255 0.0129  0.0003  156 TYR C C   
7888  O O   . TYR C 156 ? 0.3985 0.2279 0.3288 -0.0202 0.0162  0.0018  156 TYR C O   
7889  C CB  . TYR C 156 ? 0.3775 0.2404 0.3279 -0.0248 0.0126  0.0052  156 TYR C CB  
7890  C CG  . TYR C 156 ? 0.3729 0.2316 0.3195 -0.0191 0.0165  0.0093  156 TYR C CG  
7891  C CD1 . TYR C 156 ? 0.3714 0.2343 0.3164 -0.0125 0.0166  0.0103  156 TYR C CD1 
7892  C CD2 . TYR C 156 ? 0.3924 0.2430 0.3375 -0.0204 0.0200  0.0125  156 TYR C CD2 
7893  C CE1 . TYR C 156 ? 0.3531 0.2131 0.2953 -0.0070 0.0192  0.0140  156 TYR C CE1 
7894  C CE2 . TYR C 156 ? 0.4238 0.2705 0.3646 -0.0145 0.0231  0.0166  156 TYR C CE2 
7895  C CZ  . TYR C 156 ? 0.3760 0.2279 0.3156 -0.0078 0.0222  0.0172  156 TYR C CZ  
7896  O OH  . TYR C 156 ? 0.4205 0.2687 0.3563 -0.0019 0.0245  0.0213  156 TYR C OH  
7897  N N   . ARG C 157 ? 0.3551 0.1878 0.2937 -0.0326 0.0112  -0.0018 157 ARG C N   
7898  C CA  . ARG C 157 ? 0.4063 0.2221 0.3389 -0.0346 0.0133  -0.0024 157 ARG C CA  
7899  C C   . ARG C 157 ? 0.4125 0.2151 0.3337 -0.0322 0.0124  -0.0068 157 ARG C C   
7900  O O   . ARG C 157 ? 0.4452 0.2319 0.3595 -0.0322 0.0150  -0.0072 157 ARG C O   
7901  C CB  . ARG C 157 ? 0.4670 0.2812 0.4066 -0.0437 0.0116  -0.0036 157 ARG C CB  
7902  C CG  . ARG C 157 ? 0.4803 0.2946 0.4205 -0.0491 0.0051  -0.0095 157 ARG C CG  
7903  C CD  . ARG C 157 ? 0.5383 0.3545 0.4895 -0.0585 0.0032  -0.0098 157 ARG C CD  
7904  N NE  . ARG C 157 ? 0.5189 0.3390 0.4736 -0.0640 -0.0042 -0.0151 157 ARG C NE  
7905  C CZ  . ARG C 157 ? 0.6039 0.4305 0.5711 -0.0720 -0.0073 -0.0158 157 ARG C CZ  
7906  N NH1 . ARG C 157 ? 0.5672 0.3977 0.5452 -0.0755 -0.0028 -0.0112 157 ARG C NH1 
7907  N NH2 . ARG C 157 ? 0.6205 0.4501 0.5898 -0.0762 -0.0151 -0.0208 157 ARG C NH2 
7908  N N   . ASP C 158 ? 0.4015 0.2093 0.3199 -0.0301 0.0092  -0.0099 158 ASP C N   
7909  C CA  . ASP C 158 ? 0.4428 0.2390 0.3489 -0.0263 0.0092  -0.0136 158 ASP C CA  
7910  C C   . ASP C 158 ? 0.4243 0.2236 0.3274 -0.0173 0.0134  -0.0109 158 ASP C C   
7911  O O   . ASP C 158 ? 0.4542 0.2467 0.3482 -0.0131 0.0142  -0.0133 158 ASP C O   
7912  C CB  . ASP C 158 ? 0.4608 0.2599 0.3646 -0.0295 0.0032  -0.0186 158 ASP C CB  
7913  C CG  . ASP C 158 ? 0.4856 0.2814 0.3927 -0.0384 -0.0020 -0.0221 158 ASP C CG  
7914  O OD1 . ASP C 158 ? 0.5443 0.3293 0.4513 -0.0422 -0.0005 -0.0220 158 ASP C OD1 
7915  O OD2 . ASP C 158 ? 0.5385 0.3426 0.4487 -0.0417 -0.0077 -0.0247 158 ASP C OD2 
7916  N N   . MET C 159 ? 0.3891 0.1985 0.2998 -0.0141 0.0160  -0.0058 159 MET C N   
7917  C CA  . MET C 159 ? 0.4113 0.2273 0.3224 -0.0064 0.0186  -0.0034 159 MET C CA  
7918  C C   . MET C 159 ? 0.4429 0.2454 0.3449 -0.0001 0.0231  -0.0033 159 MET C C   
7919  O O   . MET C 159 ? 0.4392 0.2281 0.3359 -0.0001 0.0255  -0.0032 159 MET C O   
7920  C CB  . MET C 159 ? 0.4535 0.2819 0.3740 -0.0045 0.0195  0.0016  159 MET C CB  
7921  C CG  . MET C 159 ? 0.4902 0.3266 0.4134 0.0025  0.0212  0.0040  159 MET C CG  
7922  S SD  . MET C 159 ? 0.5115 0.3634 0.4411 0.0011  0.0177  0.0025  159 MET C SD  
7923  C CE  . MET C 159 ? 0.4568 0.3121 0.3894 -0.0074 0.0133  0.0002  159 MET C CE  
7924  N N   . THR C 160 ? 0.4180 0.2240 0.3183 0.0056  0.0248  -0.0035 160 THR C N   
7925  C CA  . THR C 160 ? 0.4012 0.1972 0.2947 0.0128  0.0300  -0.0028 160 THR C CA  
7926  C C   . THR C 160 ? 0.4315 0.2400 0.3340 0.0194  0.0326  0.0020  160 THR C C   
7927  O O   . THR C 160 ? 0.3882 0.2121 0.3002 0.0180  0.0299  0.0035  160 THR C O   
7928  C CB  . THR C 160 ? 0.4389 0.2272 0.3219 0.0142  0.0305  -0.0071 160 THR C CB  
7929  O OG1 . THR C 160 ? 0.4084 0.2104 0.2967 0.0156  0.0297  -0.0064 160 THR C OG1 
7930  C CG2 . THR C 160 ? 0.5119 0.2905 0.3872 0.0066  0.0257  -0.0125 160 THR C CG2 
7931  N N   . ASP C 161 ? 0.3400 0.3052 0.3401 0.0316  0.0182  -0.0158 161 ASP C N   
7932  C CA  . ASP C 161 ? 0.3164 0.2850 0.3225 0.0371  0.0149  -0.0127 161 ASP C CA  
7933  C C   . ASP C 161 ? 0.3370 0.3197 0.3485 0.0381  0.0162  -0.0141 161 ASP C C   
7934  O O   . ASP C 161 ? 0.3037 0.2918 0.3168 0.0388  0.0139  -0.0112 161 ASP C O   
7935  C CB  . ASP C 161 ? 0.3836 0.3459 0.3962 0.0433  0.0134  -0.0141 161 ASP C CB  
7936  C CG  . ASP C 161 ? 0.4477 0.3911 0.4531 0.0432  0.0097  -0.0116 161 ASP C CG  
7937  O OD1 . ASP C 161 ? 0.4673 0.4024 0.4626 0.0392  0.0063  -0.0065 161 ASP C OD1 
7938  O OD2 . ASP C 161 ? 0.5270 0.4625 0.5359 0.0470  0.0097  -0.0149 161 ASP C OD2 
7939  N N   . ALA C 162 ? 0.2944 0.2812 0.3070 0.0377  0.0196  -0.0185 162 ALA C N   
7940  C CA  . ALA C 162 ? 0.3135 0.3095 0.3270 0.0372  0.0204  -0.0194 162 ALA C CA  
7941  C C   . ALA C 162 ? 0.3008 0.3007 0.3106 0.0346  0.0177  -0.0175 162 ALA C C   
7942  O O   . ALA C 162 ? 0.2985 0.3033 0.3087 0.0350  0.0162  -0.0159 162 ALA C O   
7943  C CB  . ALA C 162 ? 0.3443 0.3405 0.3550 0.0354  0.0240  -0.0243 162 ALA C CB  
7944  N N   . ARG C 163 ? 0.2829 0.2813 0.2899 0.0317  0.0171  -0.0189 163 ARG C N   
7945  C CA  . ARG C 163 ? 0.2648 0.2687 0.2720 0.0302  0.0145  -0.0191 163 ARG C CA  
7946  C C   . ARG C 163 ? 0.3112 0.3161 0.3195 0.0308  0.0133  -0.0154 163 ARG C C   
7947  O O   . ARG C 163 ? 0.2518 0.2614 0.2611 0.0314  0.0111  -0.0147 163 ARG C O   
7948  C CB  . ARG C 163 ? 0.3069 0.3116 0.3144 0.0265  0.0151  -0.0233 163 ARG C CB  
7949  C CG  . ARG C 163 ? 0.3071 0.3119 0.3133 0.0258  0.0144  -0.0273 163 ARG C CG  
7950  C CD  . ARG C 163 ? 0.2874 0.2941 0.2957 0.0214  0.0154  -0.0327 163 ARG C CD  
7951  N NE  . ARG C 163 ? 0.3117 0.3186 0.3183 0.0211  0.0131  -0.0363 163 ARG C NE  
7952  C CZ  . ARG C 163 ? 0.3349 0.3444 0.3437 0.0175  0.0129  -0.0419 163 ARG C CZ  
7953  N NH1 . ARG C 163 ? 0.3006 0.3133 0.3138 0.0132  0.0160  -0.0451 163 ARG C NH1 
7954  N NH2 . ARG C 163 ? 0.3047 0.3134 0.3104 0.0172  0.0096  -0.0447 163 ARG C NH2 
7955  N N   . LEU C 164 ? 0.2867 0.2855 0.2931 0.0301  0.0141  -0.0129 164 LEU C N   
7956  C CA  . LEU C 164 ? 0.3092 0.3071 0.3140 0.0298  0.0121  -0.0091 164 LEU C CA  
7957  C C   . LEU C 164 ? 0.2979 0.2998 0.3071 0.0340  0.0099  -0.0065 164 LEU C C   
7958  O O   . LEU C 164 ? 0.2782 0.2839 0.2874 0.0335  0.0081  -0.0048 164 LEU C O   
7959  C CB  . LEU C 164 ? 0.3175 0.3038 0.3156 0.0274  0.0118  -0.0065 164 LEU C CB  
7960  C CG  . LEU C 164 ? 0.3250 0.3068 0.3173 0.0255  0.0088  -0.0021 164 LEU C CG  
7961  C CD1 . LEU C 164 ? 0.3286 0.3177 0.3194 0.0212  0.0104  -0.0039 164 LEU C CD1 
7962  C CD2 . LEU C 164 ? 0.3263 0.2921 0.3068 0.0210  0.0079  0.0006  164 LEU C CD2 
7963  N N   . ASP C 165 ? 0.2933 0.2954 0.3070 0.0373  0.0108  -0.0074 165 ASP C N   
7964  C CA  . ASP C 165 ? 0.2747 0.2832 0.2942 0.0398  0.0103  -0.0070 165 ASP C CA  
7965  C C   . ASP C 165 ? 0.2826 0.2963 0.2993 0.0375  0.0104  -0.0073 165 ASP C C   
7966  O O   . ASP C 165 ? 0.2907 0.3083 0.3089 0.0374  0.0089  -0.0055 165 ASP C O   
7967  C CB  . ASP C 165 ? 0.2951 0.3052 0.3202 0.0420  0.0135  -0.0107 165 ASP C CB  
7968  C CG  . ASP C 165 ? 0.3624 0.3672 0.3935 0.0463  0.0121  -0.0112 165 ASP C CG  
7969  O OD1 . ASP C 165 ? 0.3364 0.3354 0.3666 0.0478  0.0072  -0.0073 165 ASP C OD1 
7970  O OD2 . ASP C 165 ? 0.3198 0.3249 0.3555 0.0479  0.0156  -0.0159 165 ASP C OD2 
7971  N N   . TYR C 166 ? 0.2442 0.2568 0.2565 0.0357  0.0111  -0.0097 166 TYR C N   
7972  C CA  . TYR C 166 ? 0.2313 0.2452 0.2394 0.0342  0.0090  -0.0098 166 TYR C CA  
7973  C C   . TYR C 166 ? 0.2583 0.2738 0.2669 0.0341  0.0061  -0.0082 166 TYR C C   
7974  O O   . TYR C 166 ? 0.2814 0.2978 0.2884 0.0336  0.0044  -0.0068 166 TYR C O   
7975  C CB  . TYR C 166 ? 0.2341 0.2455 0.2381 0.0331  0.0077  -0.0128 166 TYR C CB  
7976  C CG  . TYR C 166 ? 0.2420 0.2512 0.2405 0.0324  0.0030  -0.0127 166 TYR C CG  
7977  C CD1 . TYR C 166 ? 0.2556 0.2622 0.2480 0.0305  0.0029  -0.0106 166 TYR C CD1 
7978  C CD2 . TYR C 166 ? 0.2560 0.2648 0.2554 0.0334  -0.0018 -0.0156 166 TYR C CD2 
7979  C CE1 . TYR C 166 ? 0.2626 0.2625 0.2463 0.0293  -0.0029 -0.0099 166 TYR C CE1 
7980  C CE2 . TYR C 166 ? 0.2701 0.2742 0.2644 0.0340  -0.0087 -0.0157 166 TYR C CE2 
7981  C CZ  . TYR C 166 ? 0.2836 0.2814 0.2684 0.0318  -0.0095 -0.0122 166 TYR C CZ  
7982  O OH  . TYR C 166 ? 0.2926 0.2819 0.2700 0.0323  -0.0176 -0.0118 166 TYR C OH  
7983  N N   . VAL C 167 ? 0.2492 0.2648 0.2592 0.0335  0.0061  -0.0091 167 VAL C N   
7984  C CA  . VAL C 167 ? 0.2624 0.2799 0.2725 0.0325  0.0045  -0.0090 167 VAL C CA  
7985  C C   . VAL C 167 ? 0.2941 0.3116 0.3037 0.0324  0.0040  -0.0049 167 VAL C C   
7986  O O   . VAL C 167 ? 0.2627 0.2818 0.2716 0.0318  0.0022  -0.0041 167 VAL C O   
7987  C CB  . VAL C 167 ? 0.2943 0.3127 0.3053 0.0299  0.0064  -0.0127 167 VAL C CB  
7988  C CG1 . VAL C 167 ? 0.2778 0.2989 0.2889 0.0278  0.0063  -0.0145 167 VAL C CG1 
7989  C CG2 . VAL C 167 ? 0.2748 0.2955 0.2890 0.0307  0.0054  -0.0178 167 VAL C CG2 
7990  N N   . ALA C 168 ? 0.2461 0.2609 0.2561 0.0330  0.0045  -0.0025 168 ALA C N   
7991  C CA  . ALA C 168 ? 0.2895 0.3042 0.3001 0.0336  0.0018  0.0011  168 ALA C CA  
7992  C C   . ALA C 168 ? 0.3016 0.3222 0.3169 0.0349  0.0012  0.0014  168 ALA C C   
7993  O O   . ALA C 168 ? 0.2731 0.2960 0.2880 0.0337  -0.0011 0.0031  168 ALA C O   
7994  C CB  . ALA C 168 ? 0.2914 0.3002 0.3025 0.0355  0.0003  0.0031  168 ALA C CB  
7995  N N   . ASN C 169 ? 0.2531 0.2759 0.2714 0.0358  0.0037  -0.0007 169 ASN C N   
7996  C CA  . ASN C 169 ? 0.2618 0.2899 0.2829 0.0348  0.0047  -0.0014 169 ASN C CA  
7997  C C   . ASN C 169 ? 0.2428 0.2692 0.2571 0.0318  0.0035  -0.0008 169 ASN C C   
7998  O O   . ASN C 169 ? 0.2928 0.3221 0.3076 0.0297  0.0028  0.0000  169 ASN C O   
7999  C CB  . ASN C 169 ? 0.2721 0.3018 0.2952 0.0345  0.0090  -0.0047 169 ASN C CB  
8000  C CG  . ASN C 169 ? 0.2947 0.3264 0.3275 0.0385  0.0099  -0.0066 169 ASN C CG  
8001  O OD1 . ASN C 169 ? 0.3364 0.3679 0.3741 0.0415  0.0059  -0.0045 169 ASN C OD1 
8002  N ND2 . ASN C 169 ? 0.3404 0.3726 0.3750 0.0386  0.0143  -0.0106 169 ASN C ND2 
8003  N N   . GLN C 170 ? 0.2293 0.2509 0.2382 0.0317  0.0025  -0.0018 170 GLN C N   
8004  C CA  . GLN C 170 ? 0.2151 0.2334 0.2188 0.0302  -0.0005 -0.0018 170 GLN C CA  
8005  C C   . GLN C 170 ? 0.3013 0.3214 0.3063 0.0298  -0.0021 -0.0007 170 GLN C C   
8006  O O   . GLN C 170 ? 0.2642 0.2829 0.2663 0.0279  -0.0039 -0.0001 170 GLN C O   
8007  C CB  . GLN C 170 ? 0.2463 0.2605 0.2478 0.0318  -0.0029 -0.0045 170 GLN C CB  
8008  C CG  . GLN C 170 ? 0.2730 0.2824 0.2692 0.0314  -0.0038 -0.0055 170 GLN C CG  
8009  C CD  . GLN C 170 ? 0.3305 0.3377 0.3278 0.0339  -0.0081 -0.0089 170 GLN C CD  
8010  O OE1 . GLN C 170 ? 0.2968 0.3001 0.2928 0.0352  -0.0133 -0.0102 170 GLN C OE1 
8011  N NE2 . GLN C 170 ? 0.2920 0.3024 0.2935 0.0347  -0.0062 -0.0114 170 GLN C NE2 
8012  N N   . LEU C 171 ? 0.2511 0.2727 0.2584 0.0303  -0.0016 -0.0005 171 LEU C N   
8013  C CA  . LEU C 171 ? 0.2782 0.3002 0.2837 0.0284  -0.0030 0.0004  171 LEU C CA  
8014  C C   . LEU C 171 ? 0.3038 0.3289 0.3110 0.0275  -0.0046 0.0033  171 LEU C C   
8015  O O   . LEU C 171 ? 0.2919 0.3171 0.2967 0.0252  -0.0063 0.0037  171 LEU C O   
8016  C CB  . LEU C 171 ? 0.2630 0.2833 0.2664 0.0272  -0.0021 0.0008  171 LEU C CB  
8017  C CG  . LEU C 171 ? 0.2667 0.2865 0.2693 0.0259  0.0004  -0.0040 171 LEU C CG  
8018  C CD1 . LEU C 171 ? 0.3214 0.3375 0.3194 0.0228  0.0024  -0.0033 171 LEU C CD1 
8019  C CD2 . LEU C 171 ? 0.2886 0.3097 0.2902 0.0238  0.0003  -0.0077 171 LEU C CD2 
8020  N N   . HIS C 172 ? 0.2896 0.3183 0.3025 0.0291  -0.0039 0.0041  172 HIS C N   
8021  C CA  . HIS C 172 ? 0.2883 0.3229 0.3063 0.0281  -0.0054 0.0050  172 HIS C CA  
8022  C C   . HIS C 172 ? 0.2986 0.3335 0.3133 0.0244  -0.0040 0.0039  172 HIS C C   
8023  O O   . HIS C 172 ? 0.3132 0.3506 0.3280 0.0216  -0.0057 0.0045  172 HIS C O   
8024  C CB  . HIS C 172 ? 0.2996 0.3401 0.3280 0.0311  -0.0046 0.0038  172 HIS C CB  
8025  C CG  . HIS C 172 ? 0.3128 0.3508 0.3441 0.0347  -0.0089 0.0057  172 HIS C CG  
8026  N ND1 . HIS C 172 ? 0.3152 0.3539 0.3481 0.0351  -0.0150 0.0081  172 HIS C ND1 
8027  C CD2 . HIS C 172 ? 0.3276 0.3597 0.3579 0.0375  -0.0087 0.0060  172 HIS C CD2 
8028  C CE1 . HIS C 172 ? 0.3456 0.3772 0.3769 0.0381  -0.0192 0.0103  172 HIS C CE1 
8029  N NE2 . HIS C 172 ? 0.3193 0.3467 0.3493 0.0395  -0.0150 0.0090  172 HIS C NE2 
8030  N N   . ASP C 173 ? 0.3070 0.3374 0.3168 0.0236  -0.0017 0.0026  173 ASP C N   
8031  C CA  . ASP C 173 ? 0.2912 0.3159 0.2926 0.0193  -0.0020 0.0025  173 ASP C CA  
8032  C C   . ASP C 173 ? 0.3157 0.3353 0.3126 0.0191  -0.0056 0.0030  173 ASP C C   
8033  O O   . ASP C 173 ? 0.2963 0.3126 0.2882 0.0151  -0.0067 0.0033  173 ASP C O   
8034  C CB  . ASP C 173 ? 0.3073 0.3237 0.3007 0.0190  -0.0016 0.0017  173 ASP C CB  
8035  C CG  . ASP C 173 ? 0.3873 0.4070 0.3819 0.0171  0.0032  0.0002  173 ASP C CG  
8036  O OD1 . ASP C 173 ? 0.3807 0.4105 0.3849 0.0167  0.0066  -0.0012 173 ASP C OD1 
8037  O OD2 . ASP C 173 ? 0.4146 0.4263 0.3999 0.0156  0.0032  -0.0001 173 ASP C OD2 
8038  N N   . GLY C 174 ? 0.2947 0.3131 0.2927 0.0225  -0.0068 0.0020  174 GLY C N   
8039  C CA  . GLY C 174 ? 0.3032 0.3181 0.2984 0.0222  -0.0090 0.0003  174 GLY C CA  
8040  C C   . GLY C 174 ? 0.2943 0.3126 0.2895 0.0192  -0.0096 0.0016  174 GLY C C   
8041  O O   . GLY C 174 ? 0.3024 0.3167 0.2935 0.0171  -0.0112 0.0003  174 GLY C O   
8042  N N   . ILE C 175 ? 0.2816 0.3062 0.2810 0.0191  -0.0094 0.0038  175 ILE C N   
8043  C CA  . ILE C 175 ? 0.2721 0.3001 0.2716 0.0162  -0.0119 0.0053  175 ILE C CA  
8044  C C   . ILE C 175 ? 0.3420 0.3717 0.3418 0.0126  -0.0120 0.0052  175 ILE C C   
8045  O O   . ILE C 175 ? 0.3248 0.3522 0.3201 0.0090  -0.0135 0.0047  175 ILE C O   
8046  C CB  . ILE C 175 ? 0.3057 0.3385 0.3105 0.0181  -0.0140 0.0077  175 ILE C CB  
8047  C CG1 . ILE C 175 ? 0.2934 0.3208 0.2927 0.0189  -0.0139 0.0081  175 ILE C CG1 
8048  C CG2 . ILE C 175 ? 0.3189 0.3563 0.3257 0.0157  -0.0185 0.0091  175 ILE C CG2 
8049  C CD1 . ILE C 175 ? 0.2966 0.3238 0.2986 0.0214  -0.0173 0.0111  175 ILE C CD1 
8050  N N   . ALA C 176 ? 0.2464 0.2792 0.2500 0.0123  -0.0095 0.0049  176 ALA C N   
8051  C CA  . ALA C 176 ? 0.2995 0.3334 0.3016 0.0065  -0.0082 0.0041  176 ALA C CA  
8052  C C   . ALA C 176 ? 0.3108 0.3319 0.3007 0.0037  -0.0093 0.0040  176 ALA C C   
8053  O O   . ALA C 176 ? 0.3184 0.3372 0.3040 -0.0018 -0.0099 0.0037  176 ALA C O   
8054  C CB  . ALA C 176 ? 0.3147 0.3535 0.3209 0.0049  -0.0038 0.0025  176 ALA C CB  
8055  N N   . PHE C 177 ? 0.2731 0.2851 0.2580 0.0075  -0.0102 0.0036  177 PHE C N   
8056  C CA  . PHE C 177 ? 0.2766 0.2747 0.2514 0.0067  -0.0133 0.0028  177 PHE C CA  
8057  C C   . PHE C 177 ? 0.3242 0.3209 0.2986 0.0064  -0.0154 0.0011  177 PHE C C   
8058  O O   . PHE C 177 ? 0.3064 0.2942 0.2734 0.0027  -0.0174 0.0007  177 PHE C O   
8059  C CB  . PHE C 177 ? 0.3154 0.3070 0.2892 0.0124  -0.0153 0.0015  177 PHE C CB  
8060  C CG  . PHE C 177 ? 0.3016 0.2802 0.2698 0.0147  -0.0206 -0.0010 177 PHE C CG  
8061  C CD1 . PHE C 177 ? 0.3108 0.2920 0.2851 0.0183  -0.0214 -0.0053 177 PHE C CD1 
8062  C CD2 . PHE C 177 ? 0.3157 0.2784 0.2720 0.0129  -0.0251 0.0003  177 PHE C CD2 
8063  C CE1 . PHE C 177 ? 0.3203 0.2906 0.2928 0.0214  -0.0265 -0.0095 177 PHE C CE1 
8064  C CE2 . PHE C 177 ? 0.3268 0.2753 0.2790 0.0165  -0.0321 -0.0024 177 PHE C CE2 
8065  C CZ  . PHE C 177 ? 0.2997 0.2533 0.2621 0.0216  -0.0328 -0.0081 177 PHE C CZ  
8066  N N   . VAL C 178 ? 0.2911 0.2951 0.2713 0.0092  -0.0148 -0.0001 178 VAL C N   
8067  C CA  . VAL C 178 ? 0.2648 0.2660 0.2423 0.0077  -0.0160 -0.0029 178 VAL C CA  
8068  C C   . VAL C 178 ? 0.3069 0.3114 0.2823 0.0018  -0.0166 -0.0011 178 VAL C C   
8069  O O   . VAL C 178 ? 0.3262 0.3252 0.2965 -0.0012 -0.0178 -0.0033 178 VAL C O   
8070  C CB  . VAL C 178 ? 0.3051 0.3109 0.2857 0.0099  -0.0142 -0.0056 178 VAL C CB  
8071  C CG1 . VAL C 178 ? 0.2875 0.2916 0.2721 0.0152  -0.0134 -0.0091 178 VAL C CG1 
8072  C CG2 . VAL C 178 ? 0.3178 0.3318 0.3003 0.0085  -0.0137 -0.0018 178 VAL C CG2 
8073  N N   . GLU C 179 ? 0.2755 0.2896 0.2563 0.0001  -0.0160 0.0018  179 GLU C N   
8074  C CA  . GLU C 179 ? 0.3195 0.3390 0.3012 -0.0056 -0.0172 0.0024  179 GLU C CA  
8075  C C   . GLU C 179 ? 0.3186 0.3299 0.2933 -0.0111 -0.0165 0.0017  179 GLU C C   
8076  O O   . GLU C 179 ? 0.3500 0.3581 0.3198 -0.0162 -0.0179 0.0007  179 GLU C O   
8077  C CB  . GLU C 179 ? 0.3571 0.3898 0.3497 -0.0051 -0.0171 0.0039  179 GLU C CB  
8078  C CG  . GLU C 179 ? 0.3442 0.3823 0.3412 -0.0012 -0.0202 0.0054  179 GLU C CG  
8079  C CD  . GLU C 179 ? 0.3600 0.4106 0.3701 0.0003  -0.0223 0.0058  179 GLU C CD  
8080  O OE1 . GLU C 179 ? 0.3762 0.4314 0.3938 0.0027  -0.0189 0.0048  179 GLU C OE1 
8081  O OE2 . GLU C 179 ? 0.3432 0.3989 0.3563 -0.0004 -0.0280 0.0067  179 GLU C OE2 
8082  N N   . LYS C 180 ? 0.3125 0.3194 0.2849 -0.0113 -0.0144 0.0024  180 LYS C N   
8083  C CA  . LYS C 180 ? 0.3763 0.3711 0.3374 -0.0180 -0.0141 0.0025  180 LYS C CA  
8084  C C   . LYS C 180 ? 0.3703 0.3482 0.3212 -0.0168 -0.0182 0.0013  180 LYS C C   
8085  O O   . LYS C 180 ? 0.4017 0.3704 0.3440 -0.0231 -0.0194 0.0008  180 LYS C O   
8086  C CB  . LYS C 180 ? 0.3418 0.3316 0.2985 -0.0184 -0.0118 0.0037  180 LYS C CB  
8087  C CG  . LYS C 180 ? 0.4433 0.4162 0.3832 -0.0272 -0.0118 0.0046  180 LYS C CG  
8088  C CD  . LYS C 180 ? 0.4560 0.4259 0.3902 -0.0296 -0.0085 0.0056  180 LYS C CD  
8089  C CE  . LYS C 180 ? 0.6566 0.6048 0.5684 -0.0398 -0.0092 0.0073  180 LYS C CE  
8090  N NZ  . LYS C 180 ? 0.6508 0.5892 0.5513 -0.0411 -0.0085 0.0089  180 LYS C NZ  
8091  N N   . ALA C 181 ? 0.3494 0.3229 0.3020 -0.0088 -0.0203 -0.0002 181 ALA C N   
8092  C CA  . ALA C 181 ? 0.3623 0.3199 0.3083 -0.0061 -0.0247 -0.0031 181 ALA C CA  
8093  C C   . ALA C 181 ? 0.3730 0.3318 0.3194 -0.0081 -0.0248 -0.0064 181 ALA C C   
8094  O O   . ALA C 181 ? 0.3856 0.3300 0.3247 -0.0091 -0.0281 -0.0090 181 ALA C O   
8095  C CB  . ALA C 181 ? 0.3335 0.2898 0.2852 0.0031  -0.0266 -0.0058 181 ALA C CB  
8096  N N   . SER C 182 ? 0.3298 0.3037 0.2833 -0.0089 -0.0221 -0.0066 182 SER C N   
8097  C CA  . SER C 182 ? 0.3216 0.2969 0.2735 -0.0118 -0.0221 -0.0098 182 SER C CA  
8098  C C   . SER C 182 ? 0.3590 0.3380 0.3077 -0.0202 -0.0225 -0.0077 182 SER C C   
8099  O O   . SER C 182 ? 0.4215 0.3976 0.3657 -0.0241 -0.0233 -0.0105 182 SER C O   
8100  C CB  . SER C 182 ? 0.3542 0.3411 0.3118 -0.0094 -0.0200 -0.0107 182 SER C CB  
8101  O OG  . SER C 182 ? 0.3545 0.3531 0.3164 -0.0114 -0.0201 -0.0058 182 SER C OG  
8102  N N   . GLY C 183 ? 0.3367 0.3238 0.2891 -0.0233 -0.0215 -0.0040 183 GLY C N   
8103  C CA  . GLY C 183 ? 0.3612 0.3577 0.3158 -0.0309 -0.0217 -0.0033 183 GLY C CA  
8104  C C   . GLY C 183 ? 0.4004 0.4104 0.3617 -0.0303 -0.0239 -0.0030 183 GLY C C   
8105  O O   . GLY C 183 ? 0.4041 0.4217 0.3676 -0.0362 -0.0259 -0.0033 183 GLY C O   
8106  N N   . ARG C 184 ? 0.3477 0.3598 0.3112 -0.0241 -0.0241 -0.0024 184 ARG C N   
8107  C CA  . ARG C 184 ? 0.3105 0.3312 0.2763 -0.0240 -0.0273 -0.0010 184 ARG C CA  
8108  C C   . ARG C 184 ? 0.3339 0.3652 0.3107 -0.0193 -0.0285 0.0021  184 ARG C C   
8109  O O   . ARG C 184 ? 0.3385 0.3700 0.3200 -0.0153 -0.0252 0.0026  184 ARG C O   
8110  C CB  . ARG C 184 ? 0.3317 0.3455 0.2891 -0.0227 -0.0265 -0.0029 184 ARG C CB  
8111  C CG  . ARG C 184 ? 0.3829 0.3868 0.3310 -0.0270 -0.0252 -0.0078 184 ARG C CG  
8112  C CD  . ARG C 184 ? 0.3613 0.3621 0.3017 -0.0280 -0.0235 -0.0111 184 ARG C CD  
8113  N NE  . ARG C 184 ? 0.3764 0.3683 0.3098 -0.0311 -0.0210 -0.0179 184 ARG C NE  
8114  C CZ  . ARG C 184 ? 0.4069 0.3963 0.3335 -0.0335 -0.0176 -0.0232 184 ARG C CZ  
8115  N NH1 . ARG C 184 ? 0.3729 0.3660 0.2958 -0.0345 -0.0167 -0.0212 184 ARG C NH1 
8116  N NH2 . ARG C 184 ? 0.3664 0.3485 0.2889 -0.0357 -0.0148 -0.0311 184 ARG C NH2 
8117  N N   . LYS C 185 ? 0.3588 0.3979 0.3393 -0.0198 -0.0340 0.0039  185 LYS C N   
8118  C CA  . LYS C 185 ? 0.3529 0.4000 0.3438 -0.0142 -0.0370 0.0064  185 LYS C CA  
8119  C C   . LYS C 185 ? 0.3793 0.4183 0.3619 -0.0108 -0.0374 0.0086  185 LYS C C   
8120  O O   . LYS C 185 ? 0.3871 0.4193 0.3574 -0.0145 -0.0397 0.0090  185 LYS C O   
8121  C CB  . LYS C 185 ? 0.3993 0.4573 0.3991 -0.0156 -0.0451 0.0069  185 LYS C CB  
8122  C CG  . LYS C 185 ? 0.4208 0.4865 0.4340 -0.0083 -0.0494 0.0084  185 LYS C CG  
8123  C CD  . LYS C 185 ? 0.4997 0.5781 0.5265 -0.0080 -0.0589 0.0074  185 LYS C CD  
8124  C CE  . LYS C 185 ? 0.5567 0.6410 0.5983 0.0008  -0.0636 0.0079  185 LYS C CE  
8125  N NZ  . LYS C 185 ? 0.6045 0.6972 0.6597 0.0038  -0.0547 0.0042  185 LYS C NZ  
8126  N N   . PHE C 186 ? 0.3818 0.4215 0.3701 -0.0051 -0.0347 0.0095  186 PHE C N   
8127  C CA  . PHE C 186 ? 0.3380 0.3705 0.3194 -0.0025 -0.0343 0.0113  186 PHE C CA  
8128  C C   . PHE C 186 ? 0.3799 0.4110 0.3583 -0.0023 -0.0427 0.0151  186 PHE C C   
8129  O O   . PHE C 186 ? 0.3817 0.4210 0.3718 0.0005  -0.0490 0.0162  186 PHE C O   
8130  C CB  . PHE C 186 ? 0.2909 0.3256 0.2810 0.0033  -0.0299 0.0110  186 PHE C CB  
8131  C CG  . PHE C 186 ? 0.2919 0.3199 0.2764 0.0056  -0.0279 0.0118  186 PHE C CG  
8132  C CD1 . PHE C 186 ? 0.3000 0.3229 0.2791 0.0048  -0.0220 0.0087  186 PHE C CD1 
8133  C CD2 . PHE C 186 ? 0.3243 0.3513 0.3109 0.0088  -0.0323 0.0151  186 PHE C CD2 
8134  C CE1 . PHE C 186 ? 0.3361 0.3548 0.3120 0.0062  -0.0191 0.0083  186 PHE C CE1 
8135  C CE2 . PHE C 186 ? 0.3050 0.3249 0.2859 0.0100  -0.0296 0.0158  186 PHE C CE2 
8136  C CZ  . PHE C 186 ? 0.3031 0.3198 0.2786 0.0080  -0.0225 0.0122  186 PHE C CZ  
8137  N N   . ASP C 187 ? 0.3068 0.3273 0.2695 -0.0059 -0.0434 0.0165  187 ASP C N   
8138  C CA  . ASP C 187 ? 0.3230 0.3367 0.2764 -0.0074 -0.0529 0.0211  187 ASP C CA  
8139  C C   . ASP C 187 ? 0.3427 0.3471 0.2897 -0.0052 -0.0525 0.0239  187 ASP C C   
8140  O O   . ASP C 187 ? 0.3228 0.3197 0.2578 -0.0095 -0.0452 0.0221  187 ASP C O   
8141  C CB  . ASP C 187 ? 0.3712 0.3767 0.3056 -0.0165 -0.0545 0.0208  187 ASP C CB  
8142  C CG  . ASP C 187 ? 0.3995 0.3958 0.3215 -0.0190 -0.0662 0.0263  187 ASP C CG  
8143  O OD1 . ASP C 187 ? 0.4460 0.4482 0.3759 -0.0171 -0.0764 0.0280  187 ASP C OD1 
8144  O OD2 . ASP C 187 ? 0.4200 0.4024 0.3240 -0.0230 -0.0660 0.0287  187 ASP C OD2 
8145  N N   . ASP C 188 ? 0.4120 0.3170 0.3401 0.0307  -0.0543 -0.0058 188 ASP C N   
8146  C CA  . ASP C 188 ? 0.4131 0.3084 0.3347 0.0339  -0.0478 -0.0001 188 ASP C CA  
8147  C C   . ASP C 188 ? 0.4177 0.3126 0.3257 0.0374  -0.0508 0.0035  188 ASP C C   
8148  O O   . ASP C 188 ? 0.4324 0.3170 0.3305 0.0372  -0.0454 0.0054  188 ASP C O   
8149  C CB  . ASP C 188 ? 0.3982 0.2951 0.3325 0.0389  -0.0441 0.0053  188 ASP C CB  
8150  C CG  . ASP C 188 ? 0.4521 0.3455 0.3973 0.0349  -0.0374 0.0018  188 ASP C CG  
8151  O OD1 . ASP C 188 ? 0.4923 0.3801 0.4319 0.0284  -0.0347 -0.0029 188 ASP C OD1 
8152  O OD2 . ASP C 188 ? 0.5264 0.4237 0.4861 0.0383  -0.0346 0.0043  188 ASP C OD2 
8153  N N   . GLU C 189 ? 0.3836 0.2903 0.2904 0.0401  -0.0590 0.0046  189 GLU C N   
8154  C CA  . GLU C 189 ? 0.4055 0.3131 0.2979 0.0432  -0.0616 0.0088  189 GLU C CA  
8155  C C   . GLU C 189 ? 0.4562 0.3562 0.3353 0.0385  -0.0599 0.0029  189 GLU C C   
8156  O O   . GLU C 189 ? 0.4239 0.3159 0.2923 0.0398  -0.0557 0.0063  189 GLU C O   
8157  C CB  . GLU C 189 ? 0.4445 0.3694 0.3366 0.0455  -0.0717 0.0106  189 GLU C CB  
8158  C CG  . GLU C 189 ? 0.5024 0.4295 0.3766 0.0477  -0.0745 0.0146  189 GLU C CG  
8159  C CD  . GLU C 189 ? 0.6722 0.6195 0.5448 0.0502  -0.0850 0.0188  189 GLU C CD  
8160  O OE1 . GLU C 189 ? 0.5998 0.5593 0.4761 0.0452  -0.0917 0.0108  189 GLU C OE1 
8161  O OE2 . GLU C 189 ? 0.7492 0.7009 0.6157 0.0563  -0.0865 0.0299  189 GLU C OE2 
8162  N N   . LEU C 190 ? 0.4237 0.3258 0.3050 0.0330  -0.0621 -0.0057 190 LEU C N   
8163  C CA  . LEU C 190 ? 0.4122 0.3067 0.2847 0.0292  -0.0590 -0.0105 190 LEU C CA  
8164  C C   . LEU C 190 ? 0.3784 0.2614 0.2504 0.0282  -0.0513 -0.0078 190 LEU C C   
8165  O O   . LEU C 190 ? 0.4093 0.2864 0.2723 0.0274  -0.0480 -0.0076 190 LEU C O   
8166  C CB  . LEU C 190 ? 0.3597 0.2565 0.2387 0.0239  -0.0607 -0.0193 190 LEU C CB  
8167  C CG  . LEU C 190 ? 0.4247 0.3330 0.3022 0.0221  -0.0678 -0.0254 190 LEU C CG  
8168  C CD1 . LEU C 190 ? 0.4143 0.3211 0.2999 0.0162  -0.0667 -0.0347 190 LEU C CD1 
8169  C CD2 . LEU C 190 ? 0.4473 0.3577 0.3083 0.0229  -0.0696 -0.0262 190 LEU C CD2 
8170  N N   . PHE C 191 ? 0.3980 0.2789 0.2801 0.0270  -0.0482 -0.0067 191 PHE C N   
8171  C CA  . PHE C 191 ? 0.4122 0.2844 0.2928 0.0244  -0.0411 -0.0049 191 PHE C CA  
8172  C C   . PHE C 191 ? 0.4054 0.2715 0.2776 0.0275  -0.0369 0.0002  191 PHE C C   
8173  O O   . PHE C 191 ? 0.4122 0.2725 0.2776 0.0250  -0.0326 0.0006  191 PHE C O   
8174  C CB  . PHE C 191 ? 0.3694 0.2412 0.2606 0.0222  -0.0379 -0.0052 191 PHE C CB  
8175  C CG  . PHE C 191 ? 0.3854 0.2500 0.2736 0.0183  -0.0304 -0.0040 191 PHE C CG  
8176  C CD1 . PHE C 191 ? 0.3977 0.2606 0.2806 0.0137  -0.0290 -0.0049 191 PHE C CD1 
8177  C CD2 . PHE C 191 ? 0.4009 0.2613 0.2928 0.0188  -0.0245 -0.0024 191 PHE C CD2 
8178  C CE1 . PHE C 191 ? 0.3908 0.2499 0.2704 0.0085  -0.0228 -0.0043 191 PHE C CE1 
8179  C CE2 . PHE C 191 ? 0.3852 0.2393 0.2735 0.0133  -0.0166 -0.0033 191 PHE C CE2 
8180  C CZ  . PHE C 191 ? 0.3820 0.2365 0.2631 0.0076  -0.0165 -0.0043 191 PHE C CZ  
8181  N N   . ILE C 192 ? 0.4397 0.3073 0.3145 0.0326  -0.0373 0.0049  192 ILE C N   
8182  C CA  . ILE C 192 ? 0.4254 0.2856 0.2941 0.0358  -0.0318 0.0108  192 ILE C CA  
8183  C C   . ILE C 192 ? 0.4171 0.2769 0.2723 0.0367  -0.0336 0.0119  192 ILE C C   
8184  O O   . ILE C 192 ? 0.4627 0.3146 0.3110 0.0356  -0.0278 0.0138  192 ILE C O   
8185  C CB  . ILE C 192 ? 0.4331 0.2957 0.3098 0.0425  -0.0318 0.0175  192 ILE C CB  
8186  C CG1 . ILE C 192 ? 0.4203 0.2806 0.3105 0.0407  -0.0268 0.0155  192 ILE C CG1 
8187  C CG2 . ILE C 192 ? 0.4366 0.2917 0.3069 0.0470  -0.0266 0.0254  192 ILE C CG2 
8188  C CD1 . ILE C 192 ? 0.4862 0.3506 0.3891 0.0478  -0.0265 0.0220  192 ILE C CD1 
8189  N N   . LYS C 193 ? 0.4129 0.2816 0.2642 0.0378  -0.0411 0.0099  193 LYS C N   
8190  C CA  . LYS C 193 ? 0.4138 0.2822 0.2516 0.0377  -0.0418 0.0095  193 LYS C CA  
8191  C C   . LYS C 193 ? 0.4236 0.2852 0.2588 0.0328  -0.0368 0.0053  193 LYS C C   
8192  O O   . LYS C 193 ? 0.4179 0.2749 0.2439 0.0328  -0.0329 0.0071  193 LYS C O   
8193  C CB  . LYS C 193 ? 0.4595 0.3389 0.2935 0.0376  -0.0498 0.0051  193 LYS C CB  
8194  C CG  . LYS C 193 ? 0.5825 0.4725 0.4175 0.0423  -0.0561 0.0107  193 LYS C CG  
8195  C CD  . LYS C 193 ? 0.6628 0.5641 0.4861 0.0412  -0.0631 0.0074  193 LYS C CD  
8196  C CE  . LYS C 193 ? 0.7342 0.6521 0.5635 0.0430  -0.0722 0.0093  193 LYS C CE  
8197  N NZ  . LYS C 193 ? 0.7713 0.7012 0.5866 0.0453  -0.0782 0.0147  193 LYS C NZ  
8198  N N   . ALA C 194 ? 0.4239 0.2864 0.2678 0.0287  -0.0371 0.0002  194 ALA C N   
8199  C CA  . ALA C 194 ? 0.4250 0.2841 0.2689 0.0245  -0.0334 -0.0023 194 ALA C CA  
8200  C C   . ALA C 194 ? 0.4100 0.2631 0.2529 0.0222  -0.0271 0.0011  194 ALA C C   
8201  O O   . ALA C 194 ? 0.4311 0.2821 0.2699 0.0201  -0.0236 0.0015  194 ALA C O   
8202  C CB  . ALA C 194 ? 0.3937 0.2559 0.2481 0.0211  -0.0354 -0.0064 194 ALA C CB  
8203  N N   . VAL C 195 ? 0.3911 0.2418 0.2387 0.0220  -0.0248 0.0030  195 VAL C N   
8204  C CA  . VAL C 195 ? 0.4309 0.2751 0.2769 0.0189  -0.0175 0.0048  195 VAL C CA  
8205  C C   . VAL C 195 ? 0.4272 0.2660 0.2643 0.0215  -0.0139 0.0085  195 VAL C C   
8206  O O   . VAL C 195 ? 0.4135 0.2493 0.2468 0.0176  -0.0092 0.0084  195 VAL C O   
8207  C CB  . VAL C 195 ? 0.4088 0.2498 0.2617 0.0189  -0.0141 0.0053  195 VAL C CB  
8208  C CG1 . VAL C 195 ? 0.4061 0.2384 0.2564 0.0154  -0.0049 0.0061  195 VAL C CG1 
8209  C CG2 . VAL C 195 ? 0.4095 0.2556 0.2701 0.0145  -0.0161 0.0015  195 VAL C CG2 
8210  N N   . LYS C 196 ? 0.4414 0.2805 0.2755 0.0278  -0.0164 0.0124  196 LYS C N   
8211  C CA  . LYS C 196 ? 0.4512 0.2850 0.2766 0.0309  -0.0125 0.0178  196 LYS C CA  
8212  C C   . LYS C 196 ? 0.4522 0.2879 0.2688 0.0292  -0.0130 0.0157  196 LYS C C   
8213  O O   . LYS C 196 ? 0.4329 0.2634 0.2445 0.0274  -0.0070 0.0175  196 LYS C O   
8214  C CB  . LYS C 196 ? 0.4600 0.2967 0.2837 0.0384  -0.0163 0.0242  196 LYS C CB  
8215  C CG  . LYS C 196 ? 0.4923 0.3276 0.3279 0.0416  -0.0148 0.0276  196 LYS C CG  
8216  C CD  . LYS C 196 ? 0.5200 0.3561 0.3545 0.0496  -0.0154 0.0377  196 LYS C CD  
8217  C CE  . LYS C 196 ? 0.6482 0.4970 0.4743 0.0528  -0.0254 0.0394  196 LYS C CE  
8218  N NZ  . LYS C 196 ? 0.6676 0.5256 0.4981 0.0606  -0.0307 0.0491  196 LYS C NZ  
8219  N N   . ASN C 197 ? 0.4170 0.2599 0.2336 0.0290  -0.0190 0.0112  197 ASN C N   
8220  C CA  . ASN C 197 ? 0.4094 0.2535 0.2200 0.0273  -0.0179 0.0084  197 ASN C CA  
8221  C C   . ASN C 197 ? 0.4204 0.2629 0.2361 0.0220  -0.0131 0.0069  197 ASN C C   
8222  O O   . ASN C 197 ? 0.4170 0.2582 0.2284 0.0208  -0.0089 0.0074  197 ASN C O   
8223  C CB  . ASN C 197 ? 0.4578 0.3086 0.2692 0.0277  -0.0239 0.0027  197 ASN C CB  
8224  C CG  . ASN C 197 ? 0.4800 0.3351 0.2813 0.0316  -0.0282 0.0038  197 ASN C CG  
8225  O OD1 . ASN C 197 ? 0.4926 0.3454 0.2840 0.0341  -0.0258 0.0094  197 ASN C OD1 
8226  N ND2 . ASN C 197 ? 0.5207 0.3827 0.3240 0.0313  -0.0343 -0.0014 197 ASN C ND2 
8227  N N   . GLU C 198 ? 0.3971 0.2414 0.2222 0.0184  -0.0138 0.0054  198 GLU C N   
8228  C CA  . GLU C 198 ? 0.4144 0.2605 0.2439 0.0127  -0.0103 0.0050  198 GLU C CA  
8229  C C   . GLU C 198 ? 0.4210 0.2615 0.2463 0.0098  -0.0035 0.0073  198 GLU C C   
8230  O O   . GLU C 198 ? 0.4170 0.2593 0.2419 0.0061  0.0002  0.0076  198 GLU C O   
8231  C CB  . GLU C 198 ? 0.3908 0.2415 0.2293 0.0087  -0.0126 0.0037  198 GLU C CB  
8232  C CG  . GLU C 198 ? 0.3801 0.2358 0.2221 0.0019  -0.0098 0.0044  198 GLU C CG  
8233  C CD  . GLU C 198 ? 0.4332 0.2958 0.2828 -0.0021 -0.0128 0.0043  198 GLU C CD  
8234  O OE1 . GLU C 198 ? 0.4236 0.2869 0.2776 0.0014  -0.0170 0.0035  198 GLU C OE1 
8235  O OE2 . GLU C 198 ? 0.4435 0.3110 0.2941 -0.0090 -0.0109 0.0050  198 GLU C OE2 
8236  N N   . MET C 199 ? 0.3940 0.2278 0.2177 0.0112  -0.0010 0.0090  199 MET C N   
8237  C CA  . MET C 199 ? 0.4003 0.2262 0.2207 0.0088  0.0071  0.0110  199 MET C CA  
8238  C C   . MET C 199 ? 0.4146 0.2379 0.2269 0.0116  0.0098  0.0141  199 MET C C   
8239  O O   . MET C 199 ? 0.4226 0.2442 0.2337 0.0070  0.0157  0.0140  199 MET C O   
8240  C CB  . MET C 199 ? 0.4745 0.2926 0.2964 0.0125  0.0097  0.0135  199 MET C CB  
8241  C CG  . MET C 199 ? 0.4763 0.2948 0.3058 0.0069  0.0113  0.0092  199 MET C CG  
8242  S SD  . MET C 199 ? 0.4767 0.2866 0.3115 0.0126  0.0151  0.0123  199 MET C SD  
8243  C CE  . MET C 199 ? 0.4714 0.2817 0.3129 0.0033  0.0194  0.0050  199 MET C CE  
8244  N N   . ARG C 200 ? 0.4017 0.2261 0.2081 0.0183  0.0055  0.0164  200 ARG C N   
8245  C CA  . ARG C 200 ? 0.4692 0.2923 0.2663 0.0206  0.0082  0.0190  200 ARG C CA  
8246  C C   . ARG C 200 ? 0.4728 0.3010 0.2716 0.0164  0.0096  0.0153  200 ARG C C   
8247  O O   . ARG C 200 ? 0.4605 0.2861 0.2565 0.0141  0.0160  0.0168  200 ARG C O   
8248  C CB  . ARG C 200 ? 0.4303 0.2570 0.2198 0.0268  0.0022  0.0205  200 ARG C CB  
8249  C CG  . ARG C 200 ? 0.4648 0.2888 0.2512 0.0326  0.0008  0.0273  200 ARG C CG  
8250  C CD  . ARG C 200 ? 0.5498 0.3825 0.3280 0.0369  -0.0072 0.0274  200 ARG C CD  
8251  N NE  . ARG C 200 ? 0.5302 0.3645 0.2960 0.0365  -0.0054 0.0266  200 ARG C NE  
8252  C CZ  . ARG C 200 ? 0.5697 0.4117 0.3284 0.0366  -0.0105 0.0216  200 ARG C CZ  
8253  N NH1 . ARG C 200 ? 0.5611 0.4103 0.3248 0.0367  -0.0181 0.0168  200 ARG C NH1 
8254  N NH2 . ARG C 200 ? 0.5467 0.3894 0.2928 0.0361  -0.0071 0.0212  200 ARG C NH2 
8255  N N   . SER C 201 ? 0.4337 0.2695 0.2391 0.0156  0.0045  0.0111  201 SER C N   
8256  C CA  . SER C 201 ? 0.4041 0.2452 0.2129 0.0137  0.0063  0.0090  201 SER C CA  
8257  C C   . SER C 201 ? 0.4151 0.2594 0.2313 0.0071  0.0104  0.0098  201 SER C C   
8258  O O   . SER C 201 ? 0.4368 0.2833 0.2537 0.0054  0.0152  0.0104  201 SER C O   
8259  C CB  . SER C 201 ? 0.3851 0.2323 0.2010 0.0151  0.0010  0.0052  201 SER C CB  
8260  O OG  . SER C 201 ? 0.4258 0.2770 0.2516 0.0120  -0.0020 0.0052  201 SER C OG  
8261  N N   . THR C 202 ? 0.3972 0.2430 0.2189 0.0029  0.0089  0.0094  202 THR C N   
8262  C CA  . THR C 202 ? 0.3742 0.2257 0.2018 -0.0050 0.0120  0.0093  202 THR C CA  
8263  C C   . THR C 202 ? 0.4070 0.2510 0.2290 -0.0084 0.0200  0.0101  202 THR C C   
8264  O O   . THR C 202 ? 0.4132 0.2627 0.2388 -0.0142 0.0240  0.0100  202 THR C O   
8265  C CB  . THR C 202 ? 0.3934 0.2490 0.2260 -0.0098 0.0088  0.0078  202 THR C CB  
8266  O OG1 . THR C 202 ? 0.4203 0.2654 0.2478 -0.0080 0.0102  0.0070  202 THR C OG1 
8267  C CG2 . THR C 202 ? 0.3941 0.2572 0.2336 -0.0067 0.0018  0.0082  202 THR C CG2 
8268  N N   . SER C 203 ? 0.3856 0.2178 0.2006 -0.0050 0.0229  0.0115  203 SER C N   
8269  C CA  . SER C 203 ? 0.4110 0.2342 0.2216 -0.0072 0.0318  0.0133  203 SER C CA  
8270  C C   . SER C 203 ? 0.4596 0.2830 0.2652 -0.0044 0.0348  0.0158  203 SER C C   
8271  O O   . SER C 203 ? 0.4322 0.2551 0.2388 -0.0096 0.0417  0.0158  203 SER C O   
8272  C CB  . SER C 203 ? 0.4545 0.2652 0.2606 -0.0024 0.0345  0.0164  203 SER C CB  
8273  O OG  . SER C 203 ? 0.4657 0.2658 0.2690 -0.0047 0.0445  0.0189  203 SER C OG  
8274  N N   . ARG C 204 ? 0.4150 0.2396 0.2152 0.0029  0.0303  0.0171  204 ARG C N   
8275  C CA  . ARG C 204 ? 0.4643 0.2887 0.2580 0.0054  0.0339  0.0187  204 ARG C CA  
8276  C C   . ARG C 204 ? 0.4700 0.3043 0.2727 0.0010  0.0357  0.0160  204 ARG C C   
8277  O O   . ARG C 204 ? 0.4615 0.2951 0.2627 -0.0010 0.0428  0.0173  204 ARG C O   
8278  C CB  . ARG C 204 ? 0.4902 0.3150 0.2752 0.0127  0.0287  0.0189  204 ARG C CB  
8279  C CG  . ARG C 204 ? 0.4989 0.3204 0.2713 0.0159  0.0332  0.0218  204 ARG C CG  
8280  C CD  . ARG C 204 ? 0.5085 0.3200 0.2754 0.0155  0.0404  0.0285  204 ARG C CD  
8281  N NE  . ARG C 204 ? 0.6136 0.4213 0.3659 0.0210  0.0412  0.0344  204 ARG C NE  
8282  C CZ  . ARG C 204 ? 0.7216 0.5202 0.4685 0.0224  0.0477  0.0423  204 ARG C CZ  
8283  N NH1 . ARG C 204 ? 0.6431 0.4338 0.3984 0.0185  0.0542  0.0437  204 ARG C NH1 
8284  N NH2 . ARG C 204 ? 0.6720 0.4694 0.4043 0.0273  0.0484  0.0490  204 ARG C NH2 
8285  N N   . TRP C 205 ? 0.4270 0.2711 0.2402 -0.0004 0.0299  0.0134  205 TRP C N   
8286  C CA  . TRP C 205 ? 0.4152 0.2706 0.2398 -0.0042 0.0315  0.0130  205 TRP C CA  
8287  C C   . TRP C 205 ? 0.4231 0.2810 0.2516 -0.0126 0.0370  0.0136  205 TRP C C   
8288  O O   . TRP C 205 ? 0.4236 0.2864 0.2563 -0.0150 0.0424  0.0143  205 TRP C O   
8289  C CB  . TRP C 205 ? 0.3965 0.2623 0.2328 -0.0042 0.0245  0.0123  205 TRP C CB  
8290  C CG  . TRP C 205 ? 0.4331 0.3124 0.2833 -0.0077 0.0262  0.0141  205 TRP C CG  
8291  C CD1 . TRP C 205 ? 0.3937 0.2858 0.2544 -0.0145 0.0238  0.0159  205 TRP C CD1 
8292  C CD2 . TRP C 205 ? 0.3806 0.2632 0.2358 -0.0048 0.0312  0.0145  205 TRP C CD2 
8293  N NE1 . TRP C 205 ? 0.3634 0.2681 0.2369 -0.0156 0.0261  0.0186  205 TRP C NE1 
8294  C CE2 . TRP C 205 ? 0.3716 0.2698 0.2427 -0.0094 0.0314  0.0176  205 TRP C CE2 
8295  C CE3 . TRP C 205 ? 0.4032 0.2782 0.2509 0.0009  0.0358  0.0124  205 TRP C CE3 
8296  C CZ2 . TRP C 205 ? 0.3876 0.2935 0.2701 -0.0074 0.0364  0.0193  205 TRP C CZ2 
8297  C CZ3 . TRP C 205 ? 0.4551 0.3362 0.3122 0.0022  0.0417  0.0127  205 TRP C CZ3 
8298  C CH2 . TRP C 205 ? 0.4182 0.3144 0.2939 -0.0015 0.0422  0.0164  205 TRP C CH2 
8299  N N   . ALA C 206 ? 0.3837 0.2380 0.2109 -0.0176 0.0369  0.0126  206 ALA C N   
8300  C CA  . ALA C 206 ? 0.4144 0.2691 0.2437 -0.0268 0.0438  0.0115  206 ALA C CA  
8301  C C   . ALA C 206 ? 0.4232 0.2669 0.2453 -0.0253 0.0529  0.0135  206 ALA C C   
8302  O O   . ALA C 206 ? 0.4301 0.2785 0.2569 -0.0311 0.0589  0.0133  206 ALA C O   
8303  C CB  . ALA C 206 ? 0.4052 0.2551 0.2333 -0.0329 0.0443  0.0086  206 ALA C CB  
8304  N N   . ASP C 207 ? 0.4536 0.2840 0.2645 -0.0178 0.0541  0.0163  207 ASP C N   
8305  C CA  . ASP C 207 ? 0.4677 0.2881 0.2705 -0.0160 0.0629  0.0200  207 ASP C CA  
8306  C C   . ASP C 207 ? 0.4683 0.2967 0.2731 -0.0155 0.0656  0.0202  207 ASP C C   
8307  O O   . ASP C 207 ? 0.4783 0.3045 0.2833 -0.0194 0.0744  0.0214  207 ASP C O   
8308  C CB  . ASP C 207 ? 0.5255 0.3347 0.3155 -0.0067 0.0617  0.0248  207 ASP C CB  
8309  C CG  . ASP C 207 ? 0.5379 0.3368 0.3270 -0.0059 0.0620  0.0266  207 ASP C CG  
8310  O OD1 . ASP C 207 ? 0.5255 0.3204 0.3209 -0.0133 0.0674  0.0240  207 ASP C OD1 
8311  O OD2 . ASP C 207 ? 0.5382 0.3335 0.3204 0.0020  0.0573  0.0303  207 ASP C OD2 
8312  N N   . ILE C 208 ? 0.4243 0.2613 0.2317 -0.0108 0.0593  0.0187  208 ILE C N   
8313  C CA  . ILE C 208 ? 0.4445 0.2886 0.2556 -0.0097 0.0630  0.0183  208 ILE C CA  
8314  C C   . ILE C 208 ? 0.4171 0.2734 0.2437 -0.0177 0.0662  0.0174  208 ILE C C   
8315  O O   . ILE C 208 ? 0.4385 0.2969 0.2675 -0.0197 0.0739  0.0182  208 ILE C O   
8316  C CB  . ILE C 208 ? 0.4370 0.2866 0.2502 -0.0035 0.0565  0.0159  208 ILE C CB  
8317  C CG1 . ILE C 208 ? 0.4797 0.3193 0.2761 0.0032  0.0542  0.0162  208 ILE C CG1 
8318  C CG2 . ILE C 208 ? 0.4077 0.2660 0.2304 -0.0031 0.0610  0.0148  208 ILE C CG2 
8319  C CD1 . ILE C 208 ? 0.5023 0.3457 0.3008 0.0077  0.0465  0.0125  208 ILE C CD1 
8320  N N   . CYS C 209 ? 0.4277 0.2937 0.2647 -0.0227 0.0601  0.0161  209 CYS C N   
8321  C CA  . CYS C 209 ? 0.3856 0.2674 0.2376 -0.0313 0.0611  0.0158  209 CYS C CA  
8322  C C   . CYS C 209 ? 0.4077 0.2843 0.2574 -0.0394 0.0702  0.0149  209 CYS C C   
8323  O O   . CYS C 209 ? 0.4100 0.2972 0.2698 -0.0449 0.0750  0.0151  209 CYS C O   
8324  C CB  . CYS C 209 ? 0.3912 0.2840 0.2508 -0.0361 0.0524  0.0149  209 CYS C CB  
8325  S SG  . CYS C 209 ? 0.4140 0.3164 0.2823 -0.0277 0.0432  0.0172  209 CYS C SG  
8326  N N   . ALA C 210 ? 0.4462 0.3061 0.2840 -0.0399 0.0734  0.0143  210 ALA C N   
8327  C CA  . ALA C 210 ? 0.4675 0.3190 0.3035 -0.0478 0.0836  0.0134  210 ALA C CA  
8328  C C   . ALA C 210 ? 0.4651 0.3099 0.2965 -0.0448 0.0930  0.0167  210 ALA C C   
8329  O O   . ALA C 210 ? 0.4988 0.3419 0.3338 -0.0525 0.1023  0.0160  210 ALA C O   
8330  C CB  . ALA C 210 ? 0.4687 0.3028 0.2956 -0.0480 0.0858  0.0127  210 ALA C CB  
8331  N N   . LEU C 211 ? 0.4777 0.3196 0.3016 -0.0347 0.0915  0.0198  211 LEU C N   
8332  C CA  . LEU C 211 ? 0.4702 0.3087 0.2897 -0.0326 0.1007  0.0225  211 LEU C CA  
8333  C C   . LEU C 211 ? 0.4769 0.3324 0.3127 -0.0379 0.1037  0.0206  211 LEU C C   
8334  O O   . LEU C 211 ? 0.4763 0.3300 0.3117 -0.0393 0.1134  0.0221  211 LEU C O   
8335  C CB  . LEU C 211 ? 0.4638 0.2972 0.2703 -0.0220 0.0984  0.0246  211 LEU C CB  
8336  C CG  . LEU C 211 ? 0.5165 0.3351 0.3064 -0.0158 0.0957  0.0282  211 LEU C CG  
8337  C CD1 . LEU C 211 ? 0.5232 0.3420 0.3012 -0.0073 0.0921  0.0286  211 LEU C CD1 
8338  C CD2 . LEU C 211 ? 0.5373 0.3415 0.3181 -0.0175 0.1065  0.0339  211 LEU C CD2 
8339  N N   . ASN C 212 ? 0.4581 0.3311 0.3090 -0.0405 0.0956  0.0184  212 ASN C N   
8340  C CA  . ASN C 212 ? 0.4183 0.3107 0.2879 -0.0449 0.0974  0.0184  212 ASN C CA  
8341  C C   . ASN C 212 ? 0.4558 0.3552 0.3343 -0.0574 0.1029  0.0167  212 ASN C C   
8342  O O   . ASN C 212 ? 0.4353 0.3533 0.3309 -0.0623 0.1044  0.0170  212 ASN C O   
8343  C CB  . ASN C 212 ? 0.3952 0.3051 0.2789 -0.0427 0.0867  0.0188  212 ASN C CB  
8344  C CG  . ASN C 212 ? 0.4458 0.3668 0.3426 -0.0370 0.0893  0.0208  212 ASN C CG  
8345  O OD1 . ASN C 212 ? 0.4409 0.3524 0.3304 -0.0325 0.0980  0.0205  212 ASN C OD1 
8346  N ND2 . ASN C 212 ? 0.3757 0.3171 0.2924 -0.0375 0.0829  0.0232  212 ASN C ND2 
8347  N N   . LYS C 213 ? 0.4774 0.3626 0.3460 -0.0631 0.1067  0.0148  213 LYS C N   
8348  C CA  . LYS C 213 ? 0.4668 0.3561 0.3430 -0.0764 0.1138  0.0116  213 LYS C CA  
8349  C C   . LYS C 213 ? 0.5142 0.4016 0.3935 -0.0785 0.1261  0.0132  213 LYS C C   
8350  O O   . LYS C 213 ? 0.5128 0.4117 0.4046 -0.0901 0.1309  0.0103  213 LYS C O   
8351  C CB  . LYS C 213 ? 0.4417 0.3125 0.3069 -0.0809 0.1170  0.0088  213 LYS C CB  
8352  C CG  . LYS C 213 ? 0.4781 0.3515 0.3414 -0.0814 0.1066  0.0059  213 LYS C CG  
8353  C CD  . LYS C 213 ? 0.4787 0.3325 0.3335 -0.0870 0.1131  0.0023  213 LYS C CD  
8354  C CE  . LYS C 213 ? 0.4529 0.3066 0.3037 -0.0850 0.1033  0.0000  213 LYS C CE  
8355  N NZ  . LYS C 213 ? 0.4897 0.3263 0.3356 -0.0913 0.1107  -0.0045 213 LYS C NZ  
8356  N N   . VAL C 214 ? 0.4799 0.3547 0.3482 -0.0685 0.1315  0.0174  214 VAL C N   
8357  C CA  . VAL C 214 ? 0.5668 0.4368 0.4351 -0.0707 0.1448  0.0193  214 VAL C CA  
8358  C C   . VAL C 214 ? 0.5173 0.4097 0.4045 -0.0722 0.1457  0.0189  214 VAL C C   
8359  O O   . VAL C 214 ? 0.4983 0.4059 0.3953 -0.0672 0.1366  0.0191  214 VAL C O   
8360  C CB  . VAL C 214 ? 0.5914 0.4418 0.4393 -0.0600 0.1500  0.0243  214 VAL C CB  
8361  C CG1 . VAL C 214 ? 0.6369 0.4672 0.4693 -0.0578 0.1493  0.0265  214 VAL C CG1 
8362  C CG2 . VAL C 214 ? 0.5257 0.3830 0.3712 -0.0492 0.1426  0.0247  214 VAL C CG2 
8363  N N   . LYS C 215 ? 0.5198 0.4136 0.4134 -0.0786 0.1578  0.0191  215 LYS C N   
8364  C CA  . LYS C 215 ? 0.5173 0.4288 0.4274 -0.0777 0.1618  0.0200  215 LYS C CA  
8365  C C   . LYS C 215 ? 0.5388 0.4359 0.4348 -0.0690 0.1719  0.0230  215 LYS C C   
8366  O O   . LYS C 215 ? 0.5463 0.4250 0.4275 -0.0705 0.1819  0.0251  215 LYS C O   
8367  C CB  . LYS C 215 ? 0.5409 0.4672 0.4696 -0.0912 0.1689  0.0179  215 LYS C CB  
8368  C CG  . LYS C 215 ? 0.5068 0.4506 0.4488 -0.1027 0.1596  0.0139  215 LYS C CG  
8369  C CD  . LYS C 215 ? 0.5211 0.4826 0.4826 -0.1170 0.1671  0.0113  215 LYS C CD  
8370  C CE  . LYS C 215 ? 0.5457 0.5351 0.5244 -0.1279 0.1555  0.0082  215 LYS C CE  
8371  N NZ  . LYS C 215 ? 0.5875 0.5950 0.5831 -0.1455 0.1608  0.0035  215 LYS C NZ  
8372  N N   . PRO C 216 ? 0.5213 0.4257 0.4213 -0.0603 0.1711  0.0235  216 PRO C N   
8373  C CA  . PRO C 216 ? 0.5001 0.4242 0.4185 -0.0563 0.1614  0.0228  216 PRO C CA  
8374  C C   . PRO C 216 ? 0.5001 0.4167 0.4065 -0.0500 0.1486  0.0223  216 PRO C C   
8375  O O   . PRO C 216 ? 0.4988 0.3952 0.3819 -0.0460 0.1486  0.0226  216 PRO C O   
8376  C CB  . PRO C 216 ? 0.5128 0.4389 0.4349 -0.0489 0.1703  0.0229  216 PRO C CB  
8377  C CG  . PRO C 216 ? 0.5465 0.4479 0.4386 -0.0444 0.1773  0.0233  216 PRO C CG  
8378  C CD  . PRO C 216 ? 0.5480 0.4385 0.4312 -0.0530 0.1809  0.0251  216 PRO C CD  
8379  N N   . ALA C 217 ? 0.4604 0.3936 0.3827 -0.0488 0.1377  0.0225  217 ALA C N   
8380  C CA  . ALA C 217 ? 0.4598 0.3863 0.3719 -0.0431 0.1262  0.0220  217 ALA C CA  
8381  C C   . ALA C 217 ? 0.4670 0.3817 0.3668 -0.0319 0.1283  0.0211  217 ALA C C   
8382  O O   . ALA C 217 ? 0.4692 0.3919 0.3812 -0.0275 0.1333  0.0208  217 ALA C O   
8383  C CB  . ALA C 217 ? 0.4443 0.3925 0.3772 -0.0443 0.1149  0.0236  217 ALA C CB  
8384  N N   . PRO C 218 ? 0.4483 0.3453 0.3255 -0.0274 0.1246  0.0202  218 PRO C N   
8385  C CA  . PRO C 218 ? 0.4867 0.3750 0.3518 -0.0184 0.1261  0.0180  218 PRO C CA  
8386  C C   . PRO C 218 ? 0.4299 0.3269 0.3076 -0.0129 0.1179  0.0165  218 PRO C C   
8387  O O   . PRO C 218 ? 0.4678 0.3611 0.3422 -0.0066 0.1211  0.0132  218 PRO C O   
8388  C CB  . PRO C 218 ? 0.5239 0.3938 0.3625 -0.0163 0.1231  0.0187  218 PRO C CB  
8389  C CG  . PRO C 218 ? 0.4781 0.3484 0.3203 -0.0226 0.1166  0.0205  218 PRO C CG  
8390  C CD  . PRO C 218 ? 0.4611 0.3442 0.3218 -0.0309 0.1220  0.0210  218 PRO C CD  
8391  N N   . LEU C 219 ? 0.4129 0.3206 0.3038 -0.0155 0.1079  0.0184  219 LEU C N   
8392  C CA  . LEU C 219 ? 0.4501 0.3669 0.3553 -0.0105 0.1003  0.0187  219 LEU C CA  
8393  C C   . LEU C 219 ? 0.4441 0.3836 0.3766 -0.0146 0.0975  0.0233  219 LEU C C   
8394  O O   . LEU C 219 ? 0.4777 0.4253 0.4137 -0.0233 0.0959  0.0250  219 LEU C O   
8395  C CB  . LEU C 219 ? 0.4523 0.3618 0.3461 -0.0091 0.0893  0.0180  219 LEU C CB  
8396  C CG  . LEU C 219 ? 0.5162 0.4068 0.3852 -0.0043 0.0896  0.0143  219 LEU C CG  
8397  C CD1 . LEU C 219 ? 0.5167 0.4019 0.3770 -0.0040 0.0787  0.0144  219 LEU C CD1 
8398  C CD2 . LEU C 219 ? 0.4928 0.3817 0.3638 0.0025  0.0945  0.0104  219 LEU C CD2 
8399  N N   . ASP C 220 ? 0.4437 0.3940 0.3962 -0.0089 0.0974  0.0254  220 ASP C N   
8400  C CA  . ASP C 220 ? 0.4269 0.4012 0.4069 -0.0107 0.0920  0.0321  220 ASP C CA  
8401  C C   . ASP C 220 ? 0.4497 0.4266 0.4323 -0.0078 0.0802  0.0348  220 ASP C C   
8402  O O   . ASP C 220 ? 0.4269 0.3880 0.3962 -0.0022 0.0784  0.0310  220 ASP C O   
8403  C CB  . ASP C 220 ? 0.4383 0.4233 0.4423 -0.0052 0.1008  0.0346  220 ASP C CB  
8404  C CG  . ASP C 220 ? 0.4728 0.4455 0.4761 0.0049  0.1043  0.0314  220 ASP C CG  
8405  O OD1 . ASP C 220 ? 0.6128 0.5666 0.5957 0.0071  0.1116  0.0240  220 ASP C OD1 
8406  O OD2 . ASP C 220 ? 0.5486 0.5287 0.5681 0.0097  0.0988  0.0358  220 ASP C OD2 
8407  N N   . GLU C 221 ? 0.3812 0.3798 0.3816 -0.0120 0.0722  0.0418  221 GLU C N   
8408  C CA  . GLU C 221 ? 0.4186 0.4184 0.4172 -0.0108 0.0611  0.0444  221 GLU C CA  
8409  C C   . GLU C 221 ? 0.4102 0.4076 0.4219 0.0000  0.0618  0.0470  221 GLU C C   
8410  O O   . GLU C 221 ? 0.4154 0.4023 0.4178 0.0033  0.0563  0.0455  221 GLU C O   
8411  C CB  . GLU C 221 ? 0.3900 0.4142 0.4008 -0.0193 0.0518  0.0511  221 GLU C CB  
8412  C CG  . GLU C 221 ? 0.4121 0.4378 0.4194 -0.0187 0.0407  0.0542  221 GLU C CG  
8413  C CD  . GLU C 221 ? 0.4168 0.4642 0.4275 -0.0299 0.0317  0.0583  221 GLU C CD  
8414  O OE1 . GLU C 221 ? 0.4096 0.4799 0.4377 -0.0351 0.0323  0.0633  221 GLU C OE1 
8415  O OE2 . GLU C 221 ? 0.4013 0.4442 0.3985 -0.0335 0.0244  0.0567  221 GLU C OE2 
8416  N N   . LYS C 222 ? 0.3863 0.3916 0.4198 0.0058  0.0698  0.0503  222 LYS C N   
8417  C CA  . LYS C 222 ? 0.4181 0.4190 0.4651 0.0157  0.0716  0.0524  222 LYS C CA  
8418  C C   . LYS C 222 ? 0.4191 0.3929 0.4435 0.0199  0.0769  0.0411  222 LYS C C   
8419  O O   . LYS C 222 ? 0.4416 0.4069 0.4648 0.0245  0.0736  0.0400  222 LYS C O   
8420  C CB  . LYS C 222 ? 0.4536 0.4694 0.5321 0.0212  0.0801  0.0589  222 LYS C CB  
8421  C CG  . LYS C 222 ? 0.5383 0.5468 0.6136 0.0214  0.0931  0.0522  222 LYS C CG  
8422  C CD  . LYS C 222 ? 0.6265 0.6541 0.7359 0.0255  0.1010  0.0598  222 LYS C CD  
8423  C CE  . LYS C 222 ? 0.6428 0.6871 0.7549 0.0165  0.1010  0.0621  222 LYS C CE  
8424  N NZ  . LYS C 222 ? 0.6662 0.6919 0.7486 0.0107  0.1075  0.0510  222 LYS C NZ  
8425  N N   . THR C 223 ? 0.4348 0.3960 0.4387 0.0171  0.0837  0.0331  223 THR C N   
8426  C CA  . THR C 223 ? 0.4457 0.3840 0.4234 0.0191  0.0864  0.0231  223 THR C CA  
8427  C C   . THR C 223 ? 0.4225 0.3531 0.3810 0.0163  0.0749  0.0219  223 THR C C   
8428  O O   . THR C 223 ? 0.4360 0.3548 0.3852 0.0199  0.0725  0.0172  223 THR C O   
8429  C CB  . THR C 223 ? 0.4935 0.4227 0.4535 0.0162  0.0957  0.0174  223 THR C CB  
8430  O OG1 . THR C 223 ? 0.4535 0.3886 0.4311 0.0191  0.1079  0.0173  223 THR C OG1 
8431  C CG2 . THR C 223 ? 0.4420 0.3509 0.3740 0.0180  0.0975  0.0084  223 THR C CG2 
8432  N N   . MET C 224 ? 0.3887 0.3260 0.3416 0.0094  0.0682  0.0254  224 MET C N   
8433  C CA  . MET C 224 ? 0.4115 0.3424 0.3497 0.0071  0.0584  0.0245  224 MET C CA  
8434  C C   . MET C 224 ? 0.3988 0.3360 0.3498 0.0101  0.0505  0.0287  224 MET C C   
8435  O O   . MET C 224 ? 0.3995 0.3281 0.3374 0.0098  0.0439  0.0262  224 MET C O   
8436  C CB  . MET C 224 ? 0.4434 0.3786 0.3732 -0.0017 0.0548  0.0260  224 MET C CB  
8437  C CG  . MET C 224 ? 0.4599 0.3972 0.3888 -0.0062 0.0633  0.0255  224 MET C CG  
8438  S SD  . MET C 224 ? 0.5490 0.4943 0.4747 -0.0183 0.0603  0.0269  224 MET C SD  
8439  C CE  . MET C 224 ? 0.5592 0.4847 0.4599 -0.0187 0.0553  0.0226  224 MET C CE  
8440  N N   . TYR C 225 ? 0.3802 0.3312 0.3567 0.0137  0.0515  0.0353  225 TYR C N   
8441  C CA  . TYR C 225 ? 0.4250 0.3792 0.4125 0.0174  0.0451  0.0399  225 TYR C CA  
8442  C C   . TYR C 225 ? 0.4171 0.3517 0.3942 0.0229  0.0476  0.0318  225 TYR C C   
8443  O O   . TYR C 225 ? 0.4191 0.3504 0.3943 0.0237  0.0410  0.0324  225 TYR C O   
8444  C CB  . TYR C 225 ? 0.4297 0.4026 0.4489 0.0214  0.0467  0.0506  225 TYR C CB  
8445  C CG  . TYR C 225 ? 0.3754 0.3728 0.4053 0.0145  0.0399  0.0602  225 TYR C CG  
8446  C CD1 . TYR C 225 ? 0.4174 0.4187 0.4323 0.0062  0.0305  0.0602  225 TYR C CD1 
8447  C CD2 . TYR C 225 ? 0.4402 0.4577 0.4955 0.0157  0.0435  0.0686  225 TYR C CD2 
8448  C CE1 . TYR C 225 ? 0.4355 0.4599 0.4579 -0.0021 0.0246  0.0670  225 TYR C CE1 
8449  C CE2 . TYR C 225 ? 0.4431 0.4858 0.5075 0.0080  0.0366  0.0768  225 TYR C CE2 
8450  C CZ  . TYR C 225 ? 0.4791 0.5252 0.5258 -0.0016 0.0270  0.0754  225 TYR C CZ  
8451  O OH  . TYR C 225 ? 0.4746 0.5464 0.5282 -0.0112 0.0201  0.0818  225 TYR C OH  
8452  N N   . SER C 226 ? 0.3921 0.3143 0.3616 0.0258  0.0571  0.0235  226 SER C N   
8453  C CA  . SER C 226 ? 0.3953 0.3009 0.3533 0.0292  0.0589  0.0146  226 SER C CA  
8454  C C   . SER C 226 ? 0.4409 0.3353 0.3702 0.0256  0.0533  0.0084  226 SER C C   
8455  O O   . SER C 226 ? 0.4272 0.3102 0.3452 0.0272  0.0529  0.0010  226 SER C O   
8456  C CB  . SER C 226 ? 0.4573 0.3558 0.4197 0.0331  0.0719  0.0078  226 SER C CB  
8457  O OG  . SER C 226 ? 0.4525 0.3604 0.4457 0.0379  0.0771  0.0144  226 SER C OG  
8458  N N   . LEU C 227 ? 0.4057 0.3036 0.3242 0.0206  0.0496  0.0113  227 LEU C N   
8459  C CA  . LEU C 227 ? 0.4115 0.2992 0.3056 0.0180  0.0455  0.0073  227 LEU C CA  
8460  C C   . LEU C 227 ? 0.4119 0.3032 0.3043 0.0145  0.0358  0.0113  227 LEU C C   
8461  O O   . LEU C 227 ? 0.3892 0.2725 0.2701 0.0152  0.0306  0.0081  227 LEU C O   
8462  C CB  . LEU C 227 ? 0.3876 0.2731 0.2698 0.0151  0.0514  0.0069  227 LEU C CB  
8463  C CG  . LEU C 227 ? 0.4371 0.3203 0.3198 0.0173  0.0627  0.0033  227 LEU C CG  
8464  C CD1 . LEU C 227 ? 0.4666 0.3491 0.3397 0.0136  0.0689  0.0047  227 LEU C CD1 
8465  C CD2 . LEU C 227 ? 0.4523 0.3241 0.3219 0.0208  0.0651  -0.0052 227 LEU C CD2 
8466  N N   . TYR C 228 ? 0.3815 0.2862 0.2865 0.0105  0.0332  0.0179  228 TYR C N   
8467  C CA  . TYR C 228 ? 0.4127 0.3214 0.3155 0.0060  0.0249  0.0207  228 TYR C CA  
8468  C C   . TYR C 228 ? 0.3878 0.2968 0.2983 0.0095  0.0195  0.0218  228 TYR C C   
8469  O O   . TYR C 228 ? 0.3904 0.2975 0.2944 0.0072  0.0133  0.0217  228 TYR C O   
8470  C CB  . TYR C 228 ? 0.3550 0.2807 0.2691 -0.0005 0.0230  0.0269  228 TYR C CB  
8471  C CG  . TYR C 228 ? 0.3623 0.3039 0.2971 0.0006  0.0187  0.0346  228 TYR C CG  
8472  C CD1 . TYR C 228 ? 0.4037 0.3495 0.3564 0.0073  0.0228  0.0379  228 TYR C CD1 
8473  C CD2 . TYR C 228 ? 0.3886 0.3411 0.3250 -0.0052 0.0112  0.0389  228 TYR C CD2 
8474  C CE1 . TYR C 228 ? 0.3463 0.3074 0.3202 0.0091  0.0190  0.0474  228 TYR C CE1 
8475  C CE2 . TYR C 228 ? 0.4117 0.3809 0.3665 -0.0044 0.0066  0.0480  228 TYR C CE2 
8476  C CZ  . TYR C 228 ? 0.4043 0.3778 0.3787 0.0034  0.0105  0.0531  228 TYR C CZ  
8477  O OH  . TYR C 228 ? 0.3835 0.3735 0.3787 0.0056  0.0067  0.0645  228 TYR C OH  
8478  N N   . VAL C 229 ? 0.3357 0.2445 0.2593 0.0152  0.0232  0.0219  229 VAL C N   
8479  C CA  . VAL C 229 ? 0.3530 0.2625 0.2868 0.0181  0.0191  0.0242  229 VAL C CA  
8480  C C   . VAL C 229 ? 0.3632 0.2586 0.2811 0.0190  0.0162  0.0165  229 VAL C C   
8481  O O   . VAL C 229 ? 0.3583 0.2534 0.2798 0.0192  0.0112  0.0178  229 VAL C O   
8482  C CB  . VAL C 229 ? 0.3560 0.2683 0.3111 0.0240  0.0256  0.0267  229 VAL C CB  
8483  C CG1 . VAL C 229 ? 0.3921 0.2908 0.3397 0.0274  0.0342  0.0168  229 VAL C CG1 
8484  C CG2 . VAL C 229 ? 0.3491 0.2628 0.3179 0.0267  0.0222  0.0313  229 VAL C CG2 
8485  N N   . LEU C 230 ? 0.3596 0.2444 0.2603 0.0195  0.0191  0.0091  230 LEU C N   
8486  C CA  . LEU C 230 ? 0.3858 0.2604 0.2736 0.0205  0.0157  0.0025  230 LEU C CA  
8487  C C   . LEU C 230 ? 0.3888 0.2642 0.2706 0.0175  0.0078  0.0048  230 LEU C C   
8488  O O   . LEU C 230 ? 0.3957 0.2680 0.2778 0.0183  0.0036  0.0026  230 LEU C O   
8489  C CB  . LEU C 230 ? 0.3926 0.2589 0.2622 0.0212  0.0196  -0.0040 230 LEU C CB  
8490  C CG  . LEU C 230 ? 0.3853 0.2496 0.2600 0.0238  0.0287  -0.0084 230 LEU C CG  
8491  C CD1 . LEU C 230 ? 0.4796 0.3378 0.3355 0.0236  0.0335  -0.0142 230 LEU C CD1 
8492  C CD2 . LEU C 230 ? 0.4104 0.2716 0.2979 0.0264  0.0304  -0.0131 230 LEU C CD2 
8493  N N   . CYS C 231 ? 0.3615 0.2406 0.2382 0.0135  0.0066  0.0085  231 CYS C N   
8494  C CA  . CYS C 231 ? 0.3894 0.2691 0.2619 0.0101  0.0010  0.0100  231 CYS C CA  
8495  C C   . CYS C 231 ? 0.3811 0.2697 0.2674 0.0086  -0.0031 0.0146  231 CYS C C   
8496  O O   . CYS C 231 ? 0.4035 0.2917 0.2869 0.0063  -0.0075 0.0147  231 CYS C O   
8497  C CB  . CYS C 231 ? 0.4232 0.3045 0.2888 0.0048  0.0023  0.0119  231 CYS C CB  
8498  S SG  . CYS C 231 ? 0.4508 0.3196 0.2981 0.0066  0.0062  0.0084  231 CYS C SG  
8499  N N   . THR C 232 ? 0.3555 0.2529 0.2573 0.0098  -0.0014 0.0196  232 THR C N   
8500  C CA  . THR C 232 ? 0.3456 0.2523 0.2611 0.0090  -0.0052 0.0262  232 THR C CA  
8501  C C   . THR C 232 ? 0.3423 0.2418 0.2644 0.0138  -0.0052 0.0241  232 THR C C   
8502  O O   . THR C 232 ? 0.3559 0.2608 0.2881 0.0135  -0.0082 0.0297  232 THR C O   
8503  C CB  . THR C 232 ? 0.3401 0.2613 0.2725 0.0090  -0.0035 0.0348  232 THR C CB  
8504  O OG1 . THR C 232 ? 0.3523 0.2691 0.2967 0.0158  0.0023  0.0340  232 THR C OG1 
8505  C CG2 . THR C 232 ? 0.3787 0.3070 0.3061 0.0041  -0.0020 0.0354  232 THR C CG2 
8506  N N   . LEU C 233 ? 0.3523 0.2404 0.2685 0.0175  -0.0016 0.0160  233 LEU C N   
8507  C CA  . LEU C 233 ? 0.3679 0.2484 0.2893 0.0206  -0.0008 0.0114  233 LEU C CA  
8508  C C   . LEU C 233 ? 0.3899 0.2642 0.2983 0.0188  -0.0060 0.0058  233 LEU C C   
8509  O O   . LEU C 233 ? 0.3701 0.2451 0.2844 0.0181  -0.0093 0.0074  233 LEU C O   
8510  C CB  . LEU C 233 ? 0.3492 0.2222 0.2716 0.0242  0.0064  0.0043  233 LEU C CB  
8511  C CG  . LEU C 233 ? 0.3729 0.2516 0.3088 0.0266  0.0131  0.0092  233 LEU C CG  
8512  C CD1 . LEU C 233 ? 0.3660 0.2354 0.3023 0.0296  0.0217  0.0002  233 LEU C CD1 
8513  C CD2 . LEU C 233 ? 0.3349 0.2222 0.2949 0.0287  0.0133  0.0198  233 LEU C CD2 
8514  N N   . SER C 234 ? 0.3982 0.2678 0.2897 0.0182  -0.0068 0.0007  234 SER C N   
8515  C CA  . SER C 234 ? 0.3889 0.2548 0.2704 0.0173  -0.0118 -0.0030 234 SER C CA  
8516  C C   . SER C 234 ? 0.3897 0.2538 0.2559 0.0164  -0.0123 -0.0030 234 SER C C   
8517  O O   . SER C 234 ? 0.4124 0.2720 0.2674 0.0182  -0.0122 -0.0073 234 SER C O   
8518  C CB  . SER C 234 ? 0.4161 0.2764 0.2961 0.0190  -0.0120 -0.0111 234 SER C CB  
8519  O OG  . SER C 234 ? 0.4214 0.2811 0.2960 0.0181  -0.0176 -0.0132 234 SER C OG  
8520  N N   . LYS C 235 ? 0.3739 0.2415 0.2394 0.0131  -0.0127 0.0019  235 LYS C N   
8521  C CA  . LYS C 235 ? 0.3932 0.2572 0.2462 0.0122  -0.0112 0.0021  235 LYS C CA  
8522  C C   . LYS C 235 ? 0.4101 0.2687 0.2546 0.0142  -0.0144 -0.0002 235 LYS C C   
8523  O O   . LYS C 235 ? 0.4182 0.2724 0.2521 0.0158  -0.0129 0.0001  235 LYS C O   
8524  C CB  . LYS C 235 ? 0.3703 0.2390 0.2254 0.0069  -0.0100 0.0063  235 LYS C CB  
8525  C CG  . LYS C 235 ? 0.3715 0.2450 0.2331 0.0033  -0.0136 0.0080  235 LYS C CG  
8526  C CD  . LYS C 235 ? 0.3808 0.2613 0.2430 -0.0039 -0.0121 0.0109  235 LYS C CD  
8527  C CE  . LYS C 235 ? 0.4634 0.3538 0.3327 -0.0088 -0.0152 0.0142  235 LYS C CE  
8528  N NZ  . LYS C 235 ? 0.4450 0.3299 0.3127 -0.0077 -0.0174 0.0116  235 LYS C NZ  
8529  N N   . SER C 236 ? 0.3835 0.2433 0.2335 0.0144  -0.0186 -0.0018 236 SER C N   
8530  C CA  . SER C 236 ? 0.4134 0.2705 0.2579 0.0165  -0.0220 -0.0034 236 SER C CA  
8531  C C   . SER C 236 ? 0.4246 0.2815 0.2637 0.0198  -0.0245 -0.0078 236 SER C C   
8532  O O   . SER C 236 ? 0.4278 0.2856 0.2637 0.0217  -0.0284 -0.0086 236 SER C O   
8533  C CB  . SER C 236 ? 0.3843 0.2436 0.2371 0.0147  -0.0250 -0.0034 236 SER C CB  
8534  O OG  . SER C 236 ? 0.4330 0.2950 0.2950 0.0145  -0.0270 -0.0059 236 SER C OG  
8535  N N   . SER C 237 ? 0.4154 0.2722 0.2539 0.0202  -0.0221 -0.0112 237 SER C N   
8536  C CA  . SER C 237 ? 0.4270 0.2844 0.2587 0.0216  -0.0240 -0.0171 237 SER C CA  
8537  C C   . SER C 237 ? 0.4566 0.3132 0.2726 0.0235  -0.0231 -0.0157 237 SER C C   
8538  O O   . SER C 237 ? 0.4387 0.2925 0.2501 0.0238  -0.0186 -0.0114 237 SER C O   
8539  C CB  . SER C 237 ? 0.4741 0.3306 0.3121 0.0207  -0.0203 -0.0229 237 SER C CB  
8540  O OG  . SER C 237 ? 0.4961 0.3508 0.3318 0.0212  -0.0143 -0.0206 237 SER C OG  
8541  N N   . GLN C 238 ? 0.5076 0.3458 0.2840 0.0198  0.0284  -0.0296 238 GLN C N   
8542  C CA  . GLN C 238 ? 0.4963 0.3398 0.2692 0.0249  0.0263  -0.0247 238 GLN C CA  
8543  C C   . GLN C 238 ? 0.4929 0.3334 0.2588 0.0256  0.0286  -0.0216 238 GLN C C   
8544  O O   . GLN C 238 ? 0.4901 0.3307 0.2536 0.0285  0.0287  -0.0148 238 GLN C O   
8545  C CB  . GLN C 238 ? 0.5094 0.3643 0.2808 0.0261  0.0226  -0.0289 238 GLN C CB  
8546  C CG  . GLN C 238 ? 0.5732 0.4362 0.3404 0.0310  0.0193  -0.0227 238 GLN C CG  
8547  C CD  . GLN C 238 ? 0.6472 0.5111 0.4220 0.0348  0.0164  -0.0171 238 GLN C CD  
8548  O OE1 . GLN C 238 ? 0.6418 0.5061 0.4254 0.0339  0.0156  -0.0214 238 GLN C OE1 
8549  N NE2 . GLN C 238 ? 0.6563 0.5209 0.4285 0.0389  0.0148  -0.0076 238 GLN C NE2 
8550  N N   . TRP C 239 ? 0.4950 0.3328 0.2584 0.0228  0.0307  -0.0268 239 TRP C N   
8551  C CA  . TRP C 239 ? 0.5146 0.3512 0.2730 0.0236  0.0330  -0.0256 239 TRP C CA  
8552  C C   . TRP C 239 ? 0.4892 0.3185 0.2490 0.0244  0.0354  -0.0192 239 TRP C C   
8553  O O   . TRP C 239 ? 0.5095 0.3402 0.2654 0.0262  0.0370  -0.0157 239 TRP C O   
8554  C CB  . TRP C 239 ? 0.5083 0.3426 0.2670 0.0208  0.0348  -0.0334 239 TRP C CB  
8555  C CG  . TRP C 239 ? 0.4794 0.3033 0.2433 0.0176  0.0363  -0.0343 239 TRP C CG  
8556  C CD1 . TRP C 239 ? 0.5315 0.3528 0.2991 0.0136  0.0358  -0.0386 239 TRP C CD1 
8557  C CD2 . TRP C 239 ? 0.5147 0.3306 0.2806 0.0176  0.0384  -0.0304 239 TRP C CD2 
8558  N NE1 . TRP C 239 ? 0.5297 0.3414 0.3005 0.0112  0.0372  -0.0364 239 TRP C NE1 
8559  C CE2 . TRP C 239 ? 0.5746 0.3833 0.3447 0.0139  0.0385  -0.0314 239 TRP C CE2 
8560  C CE3 . TRP C 239 ? 0.5396 0.3545 0.3042 0.0202  0.0402  -0.0259 239 TRP C CE3 
8561  C CZ2 . TRP C 239 ? 0.5276 0.3287 0.3004 0.0131  0.0395  -0.0274 239 TRP C CZ2 
8562  C CZ3 . TRP C 239 ? 0.5196 0.3271 0.2880 0.0195  0.0415  -0.0231 239 TRP C CZ3 
8563  C CH2 . TRP C 239 ? 0.5122 0.3133 0.2845 0.0163  0.0409  -0.0237 239 TRP C CH2 
8564  N N   . CYS C 240 ? 0.4935 0.3160 0.2586 0.0224  0.0360  -0.0182 240 CYS C N   
8565  C CA  . CYS C 240 ? 0.4850 0.3019 0.2520 0.0225  0.0382  -0.0131 240 CYS C CA  
8566  C C   . CYS C 240 ? 0.4973 0.3159 0.2649 0.0251  0.0379  -0.0070 240 CYS C C   
8567  O O   . CYS C 240 ? 0.4940 0.3117 0.2597 0.0265  0.0399  -0.0025 240 CYS C O   
8568  C CB  . CYS C 240 ? 0.5092 0.3210 0.2812 0.0189  0.0386  -0.0139 240 CYS C CB  
8569  S SG  . CYS C 240 ? 0.5215 0.3282 0.2955 0.0184  0.0411  -0.0090 240 CYS C SG  
8570  N N   . ALA C 241 ? 0.4668 0.2881 0.2383 0.0259  0.0355  -0.0069 241 ALA C N   
8571  C CA  . ALA C 241 ? 0.4579 0.2799 0.2322 0.0289  0.0347  -0.0008 241 ALA C CA  
8572  C C   . ALA C 241 ? 0.4857 0.3125 0.2527 0.0319  0.0338  0.0043  241 ALA C C   
8573  O O   . ALA C 241 ? 0.5130 0.3377 0.2795 0.0332  0.0352  0.0112  241 ALA C O   
8574  C CB  . ALA C 241 ? 0.4716 0.2966 0.2530 0.0299  0.0317  -0.0029 241 ALA C CB  
8575  N N   . ASP C 242 ? 0.4648 0.2991 0.2259 0.0324  0.0317  0.0009  242 ASP C N   
8576  C CA  . ASP C 242 ? 0.5070 0.3484 0.2599 0.0343  0.0309  0.0054  242 ASP C CA  
8577  C C   . ASP C 242 ? 0.5381 0.3774 0.2860 0.0329  0.0353  0.0065  242 ASP C C   
8578  O O   . ASP C 242 ? 0.5441 0.3861 0.2871 0.0337  0.0363  0.0132  242 ASP C O   
8579  C CB  . ASP C 242 ? 0.5190 0.3707 0.2669 0.0341  0.0281  -0.0006 242 ASP C CB  
8580  C CG  . ASP C 242 ? 0.5960 0.4534 0.3482 0.0363  0.0230  -0.0001 242 ASP C CG  
8581  O OD1 . ASP C 242 ? 0.5624 0.4159 0.3217 0.0387  0.0215  0.0056  242 ASP C OD1 
8582  O OD2 . ASP C 242 ? 0.5537 0.4199 0.3035 0.0357  0.0206  -0.0064 242 ASP C OD2 
8583  N N   . PHE C 243 ? 0.4980 0.3330 0.2477 0.0307  0.0380  0.0003  243 PHE C N   
8584  C CA  . PHE C 243 ? 0.4987 0.3325 0.2459 0.0299  0.0420  0.0007  243 PHE C CA  
8585  C C   . PHE C 243 ? 0.4949 0.3228 0.2455 0.0300  0.0442  0.0078  243 PHE C C   
8586  O O   . PHE C 243 ? 0.4869 0.3173 0.2336 0.0299  0.0468  0.0119  243 PHE C O   
8587  C CB  . PHE C 243 ? 0.5016 0.3313 0.2521 0.0282  0.0436  -0.0068 243 PHE C CB  
8588  C CG  . PHE C 243 ? 0.4981 0.3283 0.2479 0.0280  0.0474  -0.0078 243 PHE C CG  
8589  C CD1 . PHE C 243 ? 0.5106 0.3497 0.2542 0.0281  0.0490  -0.0107 243 PHE C CD1 
8590  C CD2 . PHE C 243 ? 0.5645 0.3883 0.3198 0.0275  0.0494  -0.0060 243 PHE C CD2 
8591  C CE1 . PHE C 243 ? 0.5693 0.4104 0.3132 0.0278  0.0530  -0.0126 243 PHE C CE1 
8592  C CE2 . PHE C 243 ? 0.5253 0.3508 0.2814 0.0277  0.0529  -0.0075 243 PHE C CE2 
8593  C CZ  . PHE C 243 ? 0.5122 0.3463 0.2629 0.0278  0.0549  -0.0111 243 PHE C CZ  
8594  N N   . MET C 244 ? 0.4811 0.3023 0.2392 0.0295  0.0436  0.0089  244 MET C N   
8595  C CA  . MET C 244 ? 0.5021 0.3184 0.2646 0.0291  0.0459  0.0145  244 MET C CA  
8596  C C   . MET C 244 ? 0.4963 0.3148 0.2560 0.0309  0.0455  0.0227  244 MET C C   
8597  O O   . MET C 244 ? 0.4905 0.3079 0.2490 0.0301  0.0487  0.0276  244 MET C O   
8598  C CB  . MET C 244 ? 0.4678 0.2789 0.2391 0.0280  0.0451  0.0129  244 MET C CB  
8599  C CG  . MET C 244 ? 0.4478 0.2569 0.2209 0.0253  0.0456  0.0068  244 MET C CG  
8600  S SD  . MET C 244 ? 0.5340 0.3413 0.3074 0.0241  0.0492  0.0076  244 MET C SD  
8601  C CE  . MET C 244 ? 0.5457 0.3550 0.3150 0.0246  0.0488  0.0024  244 MET C CE  
8602  N N   . ASP C 245 ? 0.4894 0.3118 0.2476 0.0332  0.0415  0.0250  245 ASP C N   
8603  C CA  . ASP C 245 ? 0.5091 0.3339 0.2640 0.0349  0.0404  0.0346  245 ASP C CA  
8604  C C   . ASP C 245 ? 0.5179 0.3495 0.2617 0.0336  0.0429  0.0370  245 ASP C C   
8605  O O   . ASP C 245 ? 0.5396 0.3701 0.2815 0.0328  0.0452  0.0449  245 ASP C O   
8606  C CB  . ASP C 245 ? 0.5263 0.3563 0.2814 0.0380  0.0347  0.0365  245 ASP C CB  
8607  C CG  . ASP C 245 ? 0.5560 0.3798 0.3237 0.0398  0.0327  0.0368  245 ASP C CG  
8608  O OD1 . ASP C 245 ? 0.5838 0.3992 0.3596 0.0386  0.0359  0.0376  245 ASP C OD1 
8609  O OD2 . ASP C 245 ? 0.5523 0.3809 0.3227 0.0424  0.0280  0.0355  245 ASP C OD2 
8610  N N   . GLU C 246 ? 0.4844 0.3234 0.2217 0.0327  0.0429  0.0295  246 GLU C N   
8611  C CA  . GLU C 246 ? 0.5182 0.3659 0.2458 0.0309  0.0458  0.0293  246 GLU C CA  
8612  C C   . GLU C 246 ? 0.4967 0.3401 0.2265 0.0288  0.0513  0.0300  246 GLU C C   
8613  O O   . GLU C 246 ? 0.5107 0.3587 0.2344 0.0270  0.0543  0.0350  246 GLU C O   
8614  C CB  . GLU C 246 ? 0.5710 0.4256 0.2953 0.0301  0.0457  0.0182  246 GLU C CB  
8615  C CG  . GLU C 246 ? 0.6110 0.4763 0.3288 0.0307  0.0418  0.0159  246 GLU C CG  
8616  C CD  . GLU C 246 ? 0.7181 0.5908 0.4328 0.0288  0.0440  0.0041  246 GLU C CD  
8617  O OE1 . GLU C 246 ? 0.7926 0.6752 0.4996 0.0268  0.0469  0.0030  246 GLU C OE1 
8618  O OE2 . GLU C 246 ? 0.6793 0.5474 0.4003 0.0287  0.0436  -0.0043 246 GLU C OE2 
8619  N N   . LEU C 247 ? 0.5252 0.3609 0.2635 0.0285  0.0528  0.0246  247 LEU C N   
8620  C CA  . LEU C 247 ? 0.5326 0.3653 0.2747 0.0268  0.0574  0.0235  247 LEU C CA  
8621  C C   . LEU C 247 ? 0.5542 0.3822 0.2991 0.0257  0.0594  0.0324  247 LEU C C   
8622  O O   . LEU C 247 ? 0.5325 0.3628 0.2757 0.0236  0.0637  0.0346  247 LEU C O   
8623  C CB  . LEU C 247 ? 0.5047 0.3311 0.2552 0.0268  0.0571  0.0169  247 LEU C CB  
8624  C CG  . LEU C 247 ? 0.5293 0.3537 0.2854 0.0255  0.0608  0.0151  247 LEU C CG  
8625  C CD1 . LEU C 247 ? 0.5330 0.3649 0.2856 0.0250  0.0643  0.0112  247 LEU C CD1 
8626  C CD2 . LEU C 247 ? 0.5032 0.3219 0.2668 0.0255  0.0590  0.0104  247 LEU C CD2 
8627  N N   . TYR C 248 ? 0.5073 0.3288 0.2576 0.0270  0.0567  0.0368  248 TYR C N   
8628  C CA  . TYR C 248 ? 0.5196 0.3355 0.2743 0.0261  0.0584  0.0453  248 TYR C CA  
8629  C C   . TYR C 248 ? 0.5415 0.3628 0.2871 0.0251  0.0597  0.0539  248 TYR C C   
8630  O O   . TYR C 248 ? 0.5665 0.3859 0.3129 0.0225  0.0640  0.0589  248 TYR C O   
8631  C CB  . TYR C 248 ? 0.5157 0.3252 0.2785 0.0284  0.0547  0.0478  248 TYR C CB  
8632  C CG  . TYR C 248 ? 0.5310 0.3331 0.3011 0.0280  0.0561  0.0561  248 TYR C CG  
8633  C CD1 . TYR C 248 ? 0.5394 0.3353 0.3189 0.0254  0.0601  0.0542  248 TYR C CD1 
8634  C CD2 . TYR C 248 ? 0.5742 0.3760 0.3425 0.0301  0.0534  0.0662  248 TYR C CD2 
8635  C CE1 . TYR C 248 ? 0.5033 0.2916 0.2918 0.0246  0.0620  0.0610  248 TYR C CE1 
8636  C CE2 . TYR C 248 ? 0.6532 0.4465 0.4303 0.0298  0.0548  0.0745  248 TYR C CE2 
8637  C CZ  . TYR C 248 ? 0.6359 0.4220 0.4235 0.0269  0.0594  0.0710  248 TYR C CZ  
8638  O OH  . TYR C 248 ? 0.6438 0.4208 0.4416 0.0262  0.0613  0.0781  248 TYR C OH  
8639  N N   . GLU C 249 ? 0.5171 0.3460 0.2536 0.0267  0.0562  0.0557  249 GLU C N   
8640  C CA  . GLU C 249 ? 0.5351 0.3714 0.2612 0.0249  0.0573  0.0646  249 GLU C CA  
8641  C C   . GLU C 249 ? 0.5324 0.3753 0.2529 0.0209  0.0634  0.0609  249 GLU C C   
8642  O O   . GLU C 249 ? 0.5616 0.4057 0.2782 0.0177  0.0670  0.0687  249 GLU C O   
8643  C CB  . GLU C 249 ? 0.5694 0.4160 0.2858 0.0266  0.0523  0.0658  249 GLU C CB  
8644  C CG  . GLU C 249 ? 0.6297 0.4721 0.3516 0.0307  0.0458  0.0708  249 GLU C CG  
8645  C CD  . GLU C 249 ? 0.6761 0.5095 0.4040 0.0316  0.0452  0.0842  249 GLU C CD  
8646  O OE1 . GLU C 249 ? 0.6793 0.5150 0.4002 0.0290  0.0472  0.0944  249 GLU C OE1 
8647  O OE2 . GLU C 249 ? 0.6551 0.4793 0.3955 0.0346  0.0427  0.0841  249 GLU C OE2 
8648  N N   . GLU C 250 ? 0.5547 0.4014 0.2760 0.0210  0.0648  0.0490  250 GLU C N   
8649  C CA  . GLU C 250 ? 0.5618 0.4157 0.2803 0.0178  0.0705  0.0441  250 GLU C CA  
8650  C C   . GLU C 250 ? 0.5619 0.4087 0.2887 0.0158  0.0750  0.0462  250 GLU C C   
8651  O O   . GLU C 250 ? 0.5772 0.4289 0.3007 0.0121  0.0800  0.0492  250 GLU C O   
8652  C CB  . GLU C 250 ? 0.5645 0.4231 0.2848 0.0189  0.0708  0.0308  250 GLU C CB  
8653  C CG  . GLU C 250 ? 0.5824 0.4489 0.3022 0.0161  0.0770  0.0254  250 GLU C CG  
8654  C CD  . GLU C 250 ? 0.6501 0.5235 0.3717 0.0169  0.0780  0.0123  250 GLU C CD  
8655  O OE1 . GLU C 250 ? 0.6196 0.4914 0.3419 0.0194  0.0740  0.0071  250 GLU C OE1 
8656  O OE2 . GLU C 250 ? 0.6324 0.5128 0.3559 0.0150  0.0832  0.0067  250 GLU C OE2 
8657  N N   . VAL C 251 ? 0.5767 0.4130 0.3144 0.0175  0.0734  0.0447  251 VAL C N   
8658  C CA  . VAL C 251 ? 0.5169 0.3481 0.2632 0.0152  0.0775  0.0451  251 VAL C CA  
8659  C C   . VAL C 251 ? 0.5602 0.3870 0.3065 0.0127  0.0796  0.0562  251 VAL C C   
8660  O O   . VAL C 251 ? 0.5537 0.3812 0.3024 0.0089  0.0849  0.0577  251 VAL C O   
8661  C CB  . VAL C 251 ? 0.4846 0.3079 0.2417 0.0169  0.0752  0.0400  251 VAL C CB  
8662  C CG1 . VAL C 251 ? 0.5110 0.3316 0.2767 0.0140  0.0795  0.0398  251 VAL C CG1 
8663  C CG2 . VAL C 251 ? 0.5072 0.3344 0.2645 0.0191  0.0732  0.0300  251 VAL C CG2 
8664  N N   . LYS C 252 ? 0.5188 0.3407 0.2636 0.0146  0.0756  0.0643  252 LYS C N   
8665  C CA  . LYS C 252 ? 0.6123 0.4295 0.3569 0.0125  0.0771  0.0766  252 LYS C CA  
8666  C C   . LYS C 252 ? 0.5964 0.4232 0.3296 0.0081  0.0815  0.0813  252 LYS C C   
8667  O O   . LYS C 252 ? 0.6287 0.4528 0.3634 0.0039  0.0862  0.0881  252 LYS C O   
8668  C CB  . LYS C 252 ? 0.6525 0.4661 0.3960 0.0162  0.0708  0.0847  252 LYS C CB  
8669  C CG  . LYS C 252 ? 0.6952 0.4966 0.4529 0.0189  0.0684  0.0851  252 LYS C CG  
8670  C CD  . LYS C 252 ? 0.7722 0.5644 0.5359 0.0180  0.0691  0.0979  252 LYS C CD  
8671  C CE  . LYS C 252 ? 0.7755 0.5560 0.5571 0.0184  0.0702  0.0940  252 LYS C CE  
8672  N NZ  . LYS C 252 ? 0.8395 0.6092 0.6317 0.0202  0.0683  0.1040  252 LYS C NZ  
8673  N N   . ASP C 253 ? 0.6036 0.4426 0.3254 0.0085  0.0803  0.0773  253 ASP C N   
8674  C CA  . ASP C 253 ? 0.6020 0.4530 0.3120 0.0037  0.0847  0.0807  253 ASP C CA  
8675  C C   . ASP C 253 ? 0.6207 0.4755 0.3347 -0.0003 0.0920  0.0736  253 ASP C C   
8676  O O   . ASP C 253 ? 0.6011 0.4598 0.3110 -0.0057 0.0974  0.0796  253 ASP C O   
8677  C CB  . ASP C 253 ? 0.6133 0.4779 0.3116 0.0047  0.0820  0.0756  253 ASP C CB  
8678  C CG  . ASP C 253 ? 0.7481 0.6281 0.4330 -0.0010 0.0868  0.0776  253 ASP C CG  
8679  O OD1 . ASP C 253 ? 0.6705 0.5520 0.3474 -0.0046 0.0876  0.0911  253 ASP C OD1 
8680  O OD2 . ASP C 253 ? 0.7580 0.6490 0.4409 -0.0020 0.0898  0.0653  253 ASP C OD2 
8681  N N   . ARG C 254 ? 0.5747 0.4290 0.2974 0.0021  0.0922  0.0612  254 ARG C N   
8682  C CA  . ARG C 254 ? 0.5694 0.4264 0.2993 -0.0007 0.0981  0.0544  254 ARG C CA  
8683  C C   . ARG C 254 ? 0.5718 0.4204 0.3087 -0.0042 0.1016  0.0621  254 ARG C C   
8684  O O   . ARG C 254 ? 0.5997 0.4538 0.3361 -0.0094 0.1079  0.0631  254 ARG C O   
8685  C CB  . ARG C 254 ? 0.5289 0.3838 0.2687 0.0034  0.0958  0.0426  254 ARG C CB  
8686  C CG  . ARG C 254 ? 0.5564 0.4204 0.2916 0.0059  0.0943  0.0334  254 ARG C CG  
8687  C CD  . ARG C 254 ? 0.5649 0.4238 0.3101 0.0102  0.0908  0.0244  254 ARG C CD  
8688  N NE  . ARG C 254 ? 0.5491 0.4104 0.3045 0.0097  0.0943  0.0179  254 ARG C NE  
8689  C CZ  . ARG C 254 ? 0.5677 0.4390 0.3251 0.0098  0.0973  0.0090  254 ARG C CZ  
8690  N NH1 . ARG C 254 ? 0.5937 0.4737 0.3432 0.0097  0.0980  0.0048  254 ARG C NH1 
8691  N NH2 . ARG C 254 ? 0.5562 0.4300 0.3245 0.0099  0.0998  0.0036  254 ARG C NH2 
8692  N N   . VAL C 255 ? 0.5602 0.3958 0.3045 -0.0020 0.0981  0.0668  255 VAL C N   
8693  C CA  . VAL C 255 ? 0.5833 0.4104 0.3360 -0.0058 0.1018  0.0730  255 VAL C CA  
8694  C C   . VAL C 255 ? 0.6002 0.4281 0.3444 -0.0103 0.1048  0.0859  255 VAL C C   
8695  O O   . VAL C 255 ? 0.6429 0.4714 0.3893 -0.0161 0.1112  0.0889  255 VAL C O   
8696  C CB  . VAL C 255 ? 0.5213 0.3352 0.2850 -0.0026 0.0978  0.0741  255 VAL C CB  
8697  C CG1 . VAL C 255 ? 0.5756 0.3802 0.3485 -0.0069 0.1019  0.0810  255 VAL C CG1 
8698  C CG2 . VAL C 255 ? 0.5076 0.3221 0.2795 0.0003  0.0957  0.0616  255 VAL C CG2 
8699  N N   . ALA C 256 ? 0.5918 0.4206 0.3257 -0.0083 0.1003  0.0942  256 ALA C N   
8700  C CA  . ALA C 256 ? 0.6164 0.4473 0.3403 -0.0128 0.1024  0.1082  256 ALA C CA  
8701  C C   . ALA C 256 ? 0.6085 0.4534 0.3237 -0.0194 0.1096  0.1058  256 ALA C C   
8702  O O   . ALA C 256 ? 0.6585 0.5035 0.3695 -0.0256 0.1141  0.1163  256 ALA C O   
8703  C CB  . ALA C 256 ? 0.6806 0.5153 0.3929 -0.0095 0.0957  0.1160  256 ALA C CB  
8704  N N   . ARG C 257 ? 0.6128 0.4698 0.3258 -0.0185 0.1109  0.0923  257 ARG C N   
8705  C CA  . ARG C 257 ? 0.6401 0.5128 0.3451 -0.0243 0.1176  0.0881  257 ARG C CA  
8706  C C   . ARG C 257 ? 0.6980 0.5722 0.4148 -0.0273 0.1241  0.0789  257 ARG C C   
8707  O O   . ARG C 257 ? 0.6704 0.5586 0.3833 -0.0322 0.1304  0.0736  257 ARG C O   
8708  C CB  . ARG C 257 ? 0.6617 0.5483 0.3579 -0.0216 0.1152  0.0783  257 ARG C CB  
8709  C CG  . ARG C 257 ? 0.7585 0.6518 0.4387 -0.0225 0.1116  0.0880  257 ARG C CG  
8710  C CD  . ARG C 257 ? 0.7841 0.6940 0.4560 -0.0216 0.1111  0.0760  257 ARG C CD  
8711  N NE  . ARG C 257 ? 0.7172 0.6212 0.3976 -0.0143 0.1057  0.0657  257 ARG C NE  
8712  C CZ  . ARG C 257 ? 0.7875 0.7001 0.4711 -0.0124 0.1068  0.0503  257 ARG C CZ  
8713  N NH1 . ARG C 257 ? 0.8067 0.7337 0.4882 -0.0168 0.1135  0.0419  257 ARG C NH1 
8714  N NH2 . ARG C 257 ? 0.7495 0.6553 0.4402 -0.0062 0.1015  0.0430  257 ARG C NH2 
8715  N N   . GLY C 258 ? 0.6375 0.4994 0.3689 -0.0246 0.1227  0.0761  258 GLY C N   
8716  C CA  . GLY C 258 ? 0.6056 0.4694 0.3494 -0.0270 0.1279  0.0676  258 GLY C CA  
8717  C C   . GLY C 258 ? 0.6297 0.5042 0.3774 -0.0235 0.1276  0.0526  258 GLY C C   
8718  O O   . GLY C 258 ? 0.5943 0.4774 0.3489 -0.0263 0.1329  0.0449  258 GLY C O   
8719  N N   . ILE C 259 ? 0.5884 0.4626 0.3330 -0.0174 0.1215  0.0482  259 ILE C N   
8720  C CA  . ILE C 259 ? 0.6094 0.4932 0.3575 -0.0138 0.1208  0.0348  259 ILE C CA  
8721  C C   . ILE C 259 ? 0.5737 0.4513 0.3367 -0.0099 0.1182  0.0279  259 ILE C C   
8722  O O   . ILE C 259 ? 0.5591 0.4247 0.3259 -0.0071 0.1133  0.0314  259 ILE C O   
8723  C CB  . ILE C 259 ? 0.6482 0.5333 0.3875 -0.0094 0.1154  0.0331  259 ILE C CB  
8724  C CG1 . ILE C 259 ? 0.6531 0.5500 0.3771 -0.0134 0.1181  0.0369  259 ILE C CG1 
8725  C CG2 . ILE C 259 ? 0.6352 0.5245 0.3826 -0.0045 0.1135  0.0195  259 ILE C CG2 
8726  C CD1 . ILE C 259 ? 0.6965 0.6070 0.4190 -0.0194 0.1261  0.0332  259 ILE C CD1 
8727  N N   . ALA C 260 ? 0.5972 0.4840 0.3687 -0.0096 0.1211  0.0178  260 ALA C N   
8728  C CA  . ALA C 260 ? 0.5734 0.4570 0.3588 -0.0062 0.1182  0.0116  260 ALA C CA  
8729  C C   . ALA C 260 ? 0.5405 0.4272 0.3294 0.0000  0.1140  0.0025  260 ALA C C   
8730  O O   . ALA C 260 ? 0.5361 0.4331 0.3228 0.0004  0.1165  -0.0041 260 ALA C O   
8731  C CB  . ALA C 260 ? 0.5732 0.4652 0.3686 -0.0099 0.1239  0.0072  260 ALA C CB  
8732  N N   . ALA C 261 ? 0.5089 0.3869 0.3037 0.0042  0.1079  0.0020  261 ALA C N   
8733  C CA  . ALA C 261 ? 0.5338 0.4132 0.3354 0.0097  0.1037  -0.0059 261 ALA C CA  
8734  C C   . ALA C 261 ? 0.5221 0.4126 0.3355 0.0103  0.1069  -0.0142 261 ALA C C   
8735  O O   . ALA C 261 ? 0.5677 0.4642 0.3855 0.0137  0.1067  -0.0221 261 ALA C O   
8736  C CB  . ALA C 261 ? 0.5481 0.4170 0.3541 0.0126  0.0972  -0.0035 261 ALA C CB  
8737  N N   . VAL C 262 ? 0.5453 0.4394 0.3653 0.0068  0.1101  -0.0131 262 VAL C N   
8738  C CA  . VAL C 262 ? 0.5832 0.4890 0.4161 0.0075  0.1127  -0.0211 262 VAL C CA  
8739  C C   . VAL C 262 ? 0.5785 0.4939 0.4096 0.0008  0.1211  -0.0212 262 VAL C C   
8740  O O   . VAL C 262 ? 0.5334 0.4461 0.3644 -0.0040 0.1235  -0.0157 262 VAL C O   
8741  C CB  . VAL C 262 ? 0.5737 0.4777 0.4184 0.0093  0.1082  -0.0213 262 VAL C CB  
8742  C CG1 . VAL C 262 ? 0.6230 0.5405 0.4816 0.0094  0.1111  -0.0285 262 VAL C CG1 
8743  C CG2 . VAL C 262 ? 0.6413 0.5373 0.4878 0.0153  0.1002  -0.0211 262 VAL C CG2 
8744  N N   . PRO C 263 ? 0.6211 0.5483 0.4513 -0.0002 0.1262  -0.0277 263 PRO C N   
8745  C CA  . PRO C 263 ? 0.6201 0.5561 0.4442 -0.0079 0.1346  -0.0260 263 PRO C CA  
8746  C C   . PRO C 263 ? 0.6544 0.5965 0.4892 -0.0121 0.1388  -0.0272 263 PRO C C   
8747  O O   . PRO C 263 ? 0.6860 0.6295 0.5150 -0.0196 0.1449  -0.0217 263 PRO C O   
8748  C CB  . PRO C 263 ? 0.6664 0.6163 0.4898 -0.0075 0.1388  -0.0358 263 PRO C CB  
8749  C CG  . PRO C 263 ? 0.6362 0.5856 0.4720 0.0010  0.1330  -0.0446 263 PRO C CG  
8750  C CD  . PRO C 263 ? 0.6151 0.5482 0.4503 0.0053  0.1246  -0.0373 263 PRO C CD  
8751  N N   . ASN C 264 ? 0.6501 0.5960 0.5006 -0.0079 0.1356  -0.0336 264 ASN C N   
8752  C CA  . ASN C 264 ? 0.6557 0.6094 0.5175 -0.0120 0.1392  -0.0358 264 ASN C CA  
8753  C C   . ASN C 264 ? 0.6355 0.5793 0.5012 -0.0119 0.1343  -0.0304 264 ASN C C   
8754  O O   . ASN C 264 ? 0.6158 0.5670 0.4945 -0.0125 0.1340  -0.0345 264 ASN C O   
8755  C CB  . ASN C 264 ? 0.6799 0.6491 0.5585 -0.0080 0.1396  -0.0478 264 ASN C CB  
8756  C CG  . ASN C 264 ? 0.6769 0.6420 0.5653 0.0012  0.1304  -0.0505 264 ASN C CG  
8757  O OD1 . ASN C 264 ? 0.7068 0.6590 0.5874 0.0050  0.1245  -0.0456 264 ASN C OD1 
8758  N ND2 . ASN C 264 ? 0.6651 0.6414 0.5711 0.0046  0.1288  -0.0578 264 ASN C ND2 
8759  N N   . GLU C 265 ? 0.6075 0.5362 0.4628 -0.0114 0.1304  -0.0219 265 GLU C N   
8760  C CA  . GLU C 265 ? 0.5714 0.4913 0.4303 -0.0117 0.1260  -0.0180 265 GLU C CA  
8761  C C   . GLU C 265 ? 0.5531 0.4784 0.4201 -0.0186 0.1312  -0.0187 265 GLU C C   
8762  O O   . GLU C 265 ? 0.5743 0.4987 0.4364 -0.0254 0.1383  -0.0148 265 GLU C O   
8763  C CB  . GLU C 265 ? 0.5748 0.4789 0.4213 -0.0120 0.1235  -0.0089 265 GLU C CB  
8764  C CG  . GLU C 265 ? 0.5227 0.4182 0.3731 -0.0137 0.1205  -0.0056 265 GLU C CG  
8765  C CD  . GLU C 265 ? 0.5546 0.4353 0.3949 -0.0139 0.1187  0.0026  265 GLU C CD  
8766  O OE1 . GLU C 265 ? 0.5412 0.4174 0.3723 -0.0099 0.1157  0.0049  265 GLU C OE1 
8767  O OE2 . GLU C 265 ? 0.5405 0.4145 0.3832 -0.0182 0.1205  0.0063  265 GLU C OE2 
8768  N N   . ALA C 266 ? 0.5596 0.4904 0.4387 -0.0173 0.1276  -0.0231 266 ALA C N   
8769  C CA  . ALA C 266 ? 0.5937 0.5308 0.4823 -0.0238 0.1318  -0.0253 266 ALA C CA  
8770  C C   . ALA C 266 ? 0.5786 0.5112 0.4718 -0.0234 0.1259  -0.0248 266 ALA C C   
8771  O O   . ALA C 266 ? 0.5846 0.5172 0.4828 -0.0297 0.1291  -0.0250 266 ALA C O   
8772  C CB  . ALA C 266 ? 0.6000 0.5557 0.5015 -0.0237 0.1343  -0.0344 266 ALA C CB  
8773  N N   . ILE C 267 ? 0.5234 0.4534 0.4156 -0.0166 0.1176  -0.0246 267 ILE C N   
8774  C CA  . ILE C 267 ? 0.5052 0.4331 0.4004 -0.0163 0.1116  -0.0242 267 ILE C CA  
8775  C C   . ILE C 267 ? 0.4819 0.3958 0.3664 -0.0120 0.1061  -0.0187 267 ILE C C   
8776  O O   . ILE C 267 ? 0.5649 0.4756 0.4439 -0.0065 0.1037  -0.0175 267 ILE C O   
8777  C CB  . ILE C 267 ? 0.5769 0.5195 0.4839 -0.0128 0.1060  -0.0296 267 ILE C CB  
8778  C CG1 . ILE C 267 ? 0.6401 0.5982 0.5584 -0.0158 0.1115  -0.0360 267 ILE C CG1 
8779  C CG2 . ILE C 267 ? 0.5973 0.5407 0.5067 -0.0145 0.1004  -0.0294 267 ILE C CG2 
8780  C CD1 . ILE C 267 ? 0.6789 0.6432 0.6044 -0.0238 0.1150  -0.0389 267 ILE C CD1 
8781  N N   . ARG C 268 ? 0.4896 0.3959 0.3720 -0.0149 0.1047  -0.0163 268 ARG C N   
8782  C CA  . ARG C 268 ? 0.5072 0.4013 0.3805 -0.0118 0.0999  -0.0118 268 ARG C CA  
8783  C C   . ARG C 268 ? 0.4428 0.3410 0.3198 -0.0112 0.0933  -0.0137 268 ARG C C   
8784  O O   . ARG C 268 ? 0.4735 0.3771 0.3568 -0.0163 0.0943  -0.0167 268 ARG C O   
8785  C CB  . ARG C 268 ? 0.5082 0.3897 0.3760 -0.0157 0.1041  -0.0073 268 ARG C CB  
8786  C CG  . ARG C 268 ? 0.5102 0.3874 0.3717 -0.0167 0.1100  -0.0032 268 ARG C CG  
8787  C CD  . ARG C 268 ? 0.4889 0.3558 0.3496 -0.0220 0.1149  0.0016  268 ARG C CD  
8788  N NE  . ARG C 268 ? 0.5088 0.3635 0.3643 -0.0198 0.1110  0.0057  268 ARG C NE  
8789  C CZ  . ARG C 268 ? 0.5067 0.3531 0.3521 -0.0164 0.1095  0.0117  268 ARG C CZ  
8790  N NH1 . ARG C 268 ? 0.5085 0.3577 0.3465 -0.0151 0.1116  0.0142  268 ARG C NH1 
8791  N NH2 . ARG C 268 ? 0.5139 0.3507 0.3567 -0.0145 0.1059  0.0143  268 ARG C NH2 
8792  N N   . LEU C 269 ? 0.4538 0.3498 0.3267 -0.0056 0.0867  -0.0119 269 LEU C N   
8793  C CA  . LEU C 269 ? 0.4666 0.3672 0.3414 -0.0050 0.0799  -0.0122 269 LEU C CA  
8794  C C   . LEU C 269 ? 0.4587 0.3478 0.3246 -0.0047 0.0769  -0.0087 269 LEU C C   
8795  O O   . LEU C 269 ? 0.4980 0.3762 0.3565 -0.0026 0.0784  -0.0058 269 LEU C O   
8796  C CB  . LEU C 269 ? 0.4645 0.3722 0.3437 0.0010  0.0741  -0.0122 269 LEU C CB  
8797  C CG  . LEU C 269 ? 0.4686 0.3896 0.3589 0.0015  0.0767  -0.0166 269 LEU C CG  
8798  C CD1 . LEU C 269 ? 0.4939 0.4200 0.3902 0.0088  0.0705  -0.0164 269 LEU C CD1 
8799  C CD2 . LEU C 269 ? 0.5101 0.4433 0.4081 -0.0044 0.0774  -0.0202 269 LEU C CD2 
8800  N N   . MET C 270 ? 0.4641 0.3575 0.3309 -0.0076 0.0731  -0.0096 270 MET C N   
8801  C CA  . MET C 270 ? 0.4499 0.3358 0.3094 -0.0075 0.0694  -0.0073 270 MET C CA  
8802  C C   . MET C 270 ? 0.4787 0.3719 0.3383 -0.0056 0.0618  -0.0055 270 MET C C   
8803  O O   . MET C 270 ? 0.4713 0.3775 0.3373 -0.0075 0.0596  -0.0073 270 MET C O   
8804  C CB  . MET C 270 ? 0.4945 0.3804 0.3553 -0.0140 0.0720  -0.0105 270 MET C CB  
8805  C CG  . MET C 270 ? 0.4957 0.3722 0.3495 -0.0142 0.0703  -0.0090 270 MET C CG  
8806  S SD  . MET C 270 ? 0.5126 0.3938 0.3715 -0.0223 0.0729  -0.0155 270 MET C SD  
8807  C CE  . MET C 270 ? 0.4597 0.3592 0.3208 -0.0261 0.0678  -0.0181 270 MET C CE  
8808  N N   . THR C 271 ? 0.4480 0.3331 0.3007 -0.0022 0.0577  -0.0016 271 THR C N   
8809  C CA  . THR C 271 ? 0.4112 0.3010 0.2628 -0.0014 0.0505  0.0016  271 THR C CA  
8810  C C   . THR C 271 ? 0.4522 0.3399 0.2970 -0.0063 0.0490  0.0019  271 THR C C   
8811  O O   . THR C 271 ? 0.4877 0.3727 0.3315 -0.0104 0.0537  -0.0018 271 THR C O   
8812  C CB  . THR C 271 ? 0.4606 0.3432 0.3113 0.0056  0.0469  0.0056  271 THR C CB  
8813  O OG1 . THR C 271 ? 0.5067 0.3763 0.3494 0.0067  0.0486  0.0064  271 THR C OG1 
8814  C CG2 . THR C 271 ? 0.4899 0.3754 0.3482 0.0101  0.0497  0.0033  271 THR C CG2 
8815  N N   . ASP C 272 ? 0.4843 0.3736 0.3254 -0.0060 0.0427  0.0063  272 ASP C N   
8816  C CA  . ASP C 272 ? 0.5241 0.4129 0.3584 -0.0112 0.0417  0.0061  272 ASP C CA  
8817  C C   . ASP C 272 ? 0.5486 0.4279 0.3767 -0.0079 0.0374  0.0117  272 ASP C C   
8818  O O   . ASP C 272 ? 0.5867 0.4543 0.4133 -0.0031 0.0392  0.0121  272 ASP C O   
8819  C CB  . ASP C 272 ? 0.5024 0.4072 0.3380 -0.0175 0.0388  0.0050  272 ASP C CB  
8820  C CG  . ASP C 272 ? 0.5353 0.4425 0.3652 -0.0244 0.0397  0.0020  272 ASP C CG  
8821  O OD1 . ASP C 272 ? 0.5406 0.4397 0.3701 -0.0254 0.0449  -0.0025 272 ASP C OD1 
8822  O OD2 . ASP C 272 ? 0.5635 0.4818 0.3898 -0.0292 0.0352  0.0040  272 ASP C OD2 
8823  N N   . THR C 273 ? 0.5181 0.4028 0.3429 -0.0104 0.0317  0.0163  273 THR C N   
8824  C CA  . THR C 273 ? 0.5661 0.4408 0.3848 -0.0089 0.0286  0.0211  273 THR C CA  
8825  C C   . THR C 273 ? 0.6241 0.4896 0.4470 -0.0008 0.0265  0.0248  273 THR C C   
8826  O O   . THR C 273 ? 0.6405 0.5090 0.4713 0.0037  0.0268  0.0241  273 THR C O   
8827  C CB  . THR C 273 ? 0.5793 0.4618 0.3930 -0.0142 0.0229  0.0266  273 THR C CB  
8828  O OG1 . THR C 273 ? 0.6293 0.5195 0.4485 -0.0115 0.0173  0.0321  273 THR C OG1 
8829  C CG2 . THR C 273 ? 0.5665 0.4606 0.3764 -0.0231 0.0251  0.0214  273 THR C CG2 
8830  N N   . GLN C 274 ? 0.6222 0.4774 0.4408 0.0004  0.0248  0.0279  274 GLN C N   
8831  C CA  . GLN C 274 ? 0.6661 0.5114 0.4885 0.0070  0.0227  0.0308  274 GLN C CA  
8832  C C   . GLN C 274 ? 0.5406 0.3904 0.3728 0.0119  0.0180  0.0350  274 GLN C C   
8833  O O   . GLN C 274 ? 0.6057 0.4616 0.4386 0.0099  0.0121  0.0416  274 GLN C O   
8834  C CB  . GLN C 274 ? 0.6606 0.4974 0.4759 0.0043  0.0206  0.0342  274 GLN C CB  
8835  C CG  . GLN C 274 ? 0.6329 0.4727 0.4457 0.0006  0.0143  0.0425  274 GLN C CG  
8836  C CD  . GLN C 274 ? 0.6867 0.5351 0.4902 -0.0088 0.0145  0.0425  274 GLN C CD  
8837  O OE1 . GLN C 274 ? 0.6322 0.4934 0.4354 -0.0127 0.0153  0.0399  274 GLN C OE1 
8838  N NE2 . GLN C 274 ? 0.5451 0.3875 0.3417 -0.0128 0.0137  0.0450  274 GLN C NE2 
8839  N N   . PRO C 275 ? 0.5582 0.4061 0.3987 0.0181  0.0203  0.0314  275 PRO C N   
8840  C CA  . PRO C 275 ? 0.5595 0.4128 0.4117 0.0233  0.0160  0.0342  275 PRO C CA  
8841  C C   . PRO C 275 ? 0.5714 0.4145 0.4290 0.0281  0.0113  0.0394  275 PRO C C   
8842  O O   . PRO C 275 ? 0.5680 0.3992 0.4205 0.0279  0.0128  0.0388  275 PRO C O   
8843  C CB  . PRO C 275 ? 0.6236 0.4793 0.4823 0.0272  0.0219  0.0265  275 PRO C CB  
8844  C CG  . PRO C 275 ? 0.6205 0.4660 0.4712 0.0265  0.0275  0.0221  275 PRO C CG  
8845  C CD  . PRO C 275 ? 0.6315 0.4723 0.4712 0.0209  0.0265  0.0249  275 PRO C CD  
8846  N N   . PRO C 276 ? 0.5658 0.4127 0.4346 0.0326  0.0054  0.0444  276 PRO C N   
8847  C CA  . PRO C 276 ? 0.5244 0.3598 0.4023 0.0385  0.0017  0.0480  276 PRO C CA  
8848  C C   . PRO C 276 ? 0.5983 0.4285 0.4842 0.0444  0.0075  0.0384  276 PRO C C   
8849  O O   . PRO C 276 ? 0.6491 0.4875 0.5376 0.0454  0.0122  0.0314  276 PRO C O   
8850  C CB  . PRO C 276 ? 0.5824 0.4260 0.4724 0.0423  -0.0061 0.0556  276 PRO C CB  
8851  C CG  . PRO C 276 ? 0.5843 0.4434 0.4660 0.0357  -0.0078 0.0583  276 PRO C CG  
8852  C CD  . PRO C 276 ? 0.5734 0.4356 0.4479 0.0322  0.0010  0.0478  276 PRO C CD  
8853  N N   . TRP C 277 ? 0.5733 0.4467 0.6127 0.1368  0.0198  0.0217  277 TRP C N   
8854  C CA  . TRP C 277 ? 0.5568 0.4181 0.5930 0.1391  0.0332  0.0092  277 TRP C CA  
8855  C C   . TRP C 277 ? 0.5592 0.4414 0.6219 0.1526  0.0412  0.0029  277 TRP C C   
8856  O O   . TRP C 277 ? 0.6185 0.5083 0.6820 0.1500  0.0538  -0.0077 277 TRP C O   
8857  C CB  . TRP C 277 ? 0.5305 0.3534 0.5511 0.1424  0.0334  0.0087  277 TRP C CB  
8858  C CG  . TRP C 277 ? 0.6141 0.4183 0.6092 0.1263  0.0318  0.0084  277 TRP C CG  
8859  C CD1 . TRP C 277 ? 0.5997 0.3851 0.5822 0.1203  0.0233  0.0173  277 TRP C CD1 
8860  C CD2 . TRP C 277 ? 0.6891 0.4916 0.6689 0.1141  0.0384  -0.0005 277 TRP C CD2 
8861  N NE1 . TRP C 277 ? 0.6022 0.3778 0.5664 0.1053  0.0241  0.0139  277 TRP C NE1 
8862  C CE2 . TRP C 277 ? 0.6932 0.4784 0.6548 0.1017  0.0322  0.0034  277 TRP C CE2 
8863  C CE3 . TRP C 277 ? 0.7228 0.5365 0.7021 0.1123  0.0488  -0.0109 277 TRP C CE3 
8864  C CZ2 . TRP C 277 ? 0.7109 0.4910 0.6558 0.0888  0.0344  -0.0026 277 TRP C CZ2 
8865  C CZ3 . TRP C 277 ? 0.7862 0.5921 0.7448 0.0989  0.0510  -0.0161 277 TRP C CZ3 
8866  C CH2 . TRP C 277 ? 0.7531 0.5429 0.6957 0.0879  0.0430  -0.0119 277 TRP C CH2 
8867  N N   . SER C 278 ? 0.5141 0.4070 0.5991 0.1667  0.0341  0.0097  278 SER C N   
8868  C CA  . SER C 278 ? 0.5409 0.4589 0.6580 0.1810  0.0395  0.0055  278 SER C CA  
8869  C C   . SER C 278 ? 0.5885 0.5446 0.7215 0.1734  0.0431  0.0019  278 SER C C   
8870  O O   . SER C 278 ? 0.6242 0.6038 0.7849 0.1827  0.0511  -0.0039 278 SER C O   
8871  C CB  . SER C 278 ? 0.5981 0.5211 0.7350 0.1965  0.0262  0.0167  278 SER C CB  
8872  O OG  . SER C 278 ? 0.6967 0.5865 0.8289 0.2092  0.0281  0.0166  278 SER C OG  
8873  N N   . PHE C 279 ? 0.5311 0.4944 0.6492 0.1570  0.0378  0.0053  279 PHE C N   
8874  C CA  . PHE C 279 ? 0.5694 0.5632 0.6985 0.1477  0.0430  0.0007  279 PHE C CA  
8875  C C   . PHE C 279 ? 0.6361 0.6224 0.7534 0.1411  0.0605  -0.0110 279 PHE C C   
8876  O O   . PHE C 279 ? 0.6425 0.6530 0.7726 0.1361  0.0690  -0.0163 279 PHE C O   
8877  C CB  . PHE C 279 ? 0.5451 0.5453 0.6604 0.1330  0.0320  0.0078  279 PHE C CB  
8878  C CG  . PHE C 279 ? 0.5504 0.5840 0.6816 0.1247  0.0328  0.0057  279 PHE C CG  
8879  C CD1 . PHE C 279 ? 0.5032 0.5653 0.6599 0.1299  0.0224  0.0106  279 PHE C CD1 
8880  C CD2 . PHE C 279 ? 0.5671 0.6024 0.6864 0.1109  0.0428  -0.0007 279 PHE C CD2 
8881  C CE1 . PHE C 279 ? 0.4949 0.5877 0.6669 0.1204  0.0226  0.0080  279 PHE C CE1 
8882  C CE2 . PHE C 279 ? 0.5576 0.6211 0.6910 0.1021  0.0439  -0.0026 279 PHE C CE2 
8883  C CZ  . PHE C 279 ? 0.5097 0.6023 0.6701 0.1064  0.0340  0.0013  279 PHE C CZ  
8884  N N   . LEU C 280 ? 0.6571 0.6098 0.7489 0.1399  0.0656  -0.0150 280 LEU C N   
8885  C CA  . LEU C 280 ? 0.6616 0.6051 0.7356 0.1315  0.0800  -0.0253 280 LEU C CA  
8886  C C   . LEU C 280 ? 0.6741 0.6334 0.7684 0.1403  0.0959  -0.0347 280 LEU C C   
8887  O O   . LEU C 280 ? 0.6920 0.6617 0.7826 0.1319  0.1078  -0.0411 280 LEU C O   
8888  C CB  . LEU C 280 ? 0.6826 0.5872 0.7261 0.1290  0.0806  -0.0283 280 LEU C CB  
8889  C CG  . LEU C 280 ? 0.6962 0.5856 0.7128 0.1138  0.0721  -0.0238 280 LEU C CG  
8890  C CD1 . LEU C 280 ? 0.6436 0.5346 0.6621 0.1114  0.0564  -0.0117 280 LEU C CD1 
8891  C CD2 . LEU C 280 ? 0.7444 0.6001 0.7353 0.1114  0.0759  -0.0302 280 LEU C CD2 
8892  N N   . LYS C 281 ? 0.6636 0.6256 0.7810 0.1576  0.0966  -0.0353 281 LYS C N   
8893  C CA  . LYS C 281 ? 0.6797 0.6620 0.8239 0.1681  0.1119  -0.0439 281 LYS C CA  
8894  C C   . LYS C 281 ? 0.6636 0.6890 0.8369 0.1635  0.1116  -0.0417 281 LYS C C   
8895  O O   . LYS C 281 ? 0.6370 0.6810 0.8240 0.1626  0.1278  -0.0499 281 LYS C O   
8896  C CB  . LYS C 281 ? 0.7153 0.6897 0.8796 0.1892  0.1103  -0.0436 281 LYS C CB  
8897  C CG  . LYS C 281 ? 0.6919 0.6995 0.8968 0.2011  0.0993  -0.0354 281 LYS C CG  
8898  C CD  . LYS C 281 ? 0.7051 0.6923 0.9144 0.2171  0.0865  -0.0275 281 LYS C CD  
8899  C CE  . LYS C 281 ? 0.7199 0.6880 0.9368 0.2346  0.1002  -0.0369 281 LYS C CE  
8900  N NZ  . LYS C 281 ? 0.8031 0.8061 1.0628 0.2484  0.1115  -0.0432 281 LYS C NZ  
8901  N N   . ILE C 282 ? 0.6453 0.6863 0.8268 0.1592  0.0941  -0.0310 282 ILE C N   
8902  C CA  . ILE C 282 ? 0.6066 0.6869 0.8133 0.1522  0.0924  -0.0296 282 ILE C CA  
8903  C C   . ILE C 282 ? 0.5824 0.6632 0.7693 0.1335  0.1029  -0.0344 282 ILE C C   
8904  O O   . ILE C 282 ? 0.6025 0.7107 0.8093 0.1286  0.1132  -0.0390 282 ILE C O   
8905  C CB  . ILE C 282 ? 0.5740 0.6667 0.7881 0.1509  0.0704  -0.0177 282 ILE C CB  
8906  C CG1 . ILE C 282 ? 0.5819 0.6910 0.8298 0.1699  0.0614  -0.0131 282 ILE C CG1 
8907  C CG2 . ILE C 282 ? 0.5680 0.6884 0.7893 0.1355  0.0673  -0.0167 282 ILE C CG2 
8908  C CD1 . ILE C 282 ? 0.5368 0.6433 0.7797 0.1712  0.0386  -0.0002 282 ILE C CD1 
8909  N N   . PHE C 283 ? 0.5405 0.5909 0.6891 0.1231  0.1008  -0.0332 283 PHE C N   
8910  C CA  . PHE C 283 ? 0.5926 0.6374 0.7186 0.1070  0.1107  -0.0374 283 PHE C CA  
8911  C C   . PHE C 283 ? 0.6110 0.6569 0.7389 0.1094  0.1324  -0.0481 283 PHE C C   
8912  O O   . PHE C 283 ? 0.6014 0.6662 0.7369 0.1006  0.1435  -0.0514 283 PHE C O   
8913  C CB  . PHE C 283 ? 0.5697 0.5797 0.6562 0.0989  0.1049  -0.0351 283 PHE C CB  
8914  C CG  . PHE C 283 ? 0.5585 0.5682 0.6367 0.0903  0.0883  -0.0258 283 PHE C CG  
8915  C CD1 . PHE C 283 ? 0.5775 0.6084 0.6631 0.0793  0.0855  -0.0232 283 PHE C CD1 
8916  C CD2 . PHE C 283 ? 0.5466 0.5326 0.6076 0.0920  0.0771  -0.0206 283 PHE C CD2 
8917  C CE1 . PHE C 283 ? 0.5274 0.5560 0.6035 0.0717  0.0716  -0.0159 283 PHE C CE1 
8918  C CE2 . PHE C 283 ? 0.5839 0.5692 0.6366 0.0841  0.0640  -0.0128 283 PHE C CE2 
8919  C CZ  . PHE C 283 ? 0.5039 0.5105 0.5637 0.0744  0.0615  -0.0108 283 PHE C CZ  
8920  N N   . ARG C 284 ? 0.5988 0.6222 0.7175 0.1206  0.1395  -0.0539 284 ARG C N   
8921  C CA  . ARG C 284 ? 0.5768 0.5994 0.6957 0.1242  0.1614  -0.0651 284 ARG C CA  
8922  C C   . ARG C 284 ? 0.6174 0.6802 0.7801 0.1304  0.1709  -0.0678 284 ARG C C   
8923  O O   . ARG C 284 ? 0.6445 0.7199 0.8105 0.1242  0.1890  -0.0745 284 ARG C O   
8924  C CB  . ARG C 284 ? 0.6599 0.6524 0.7665 0.1376  0.1658  -0.0714 284 ARG C CB  
8925  C CG  . ARG C 284 ? 0.7537 0.7043 0.8144 0.1297  0.1599  -0.0717 284 ARG C CG  
8926  C CD  . ARG C 284 ? 0.7724 0.7123 0.7987 0.1121  0.1667  -0.0743 284 ARG C CD  
8927  N NE  . ARG C 284 ? 0.7974 0.6992 0.7841 0.1070  0.1618  -0.0765 284 ARG C NE  
8928  C CZ  . ARG C 284 ? 0.7946 0.6829 0.7510 0.0924  0.1560  -0.0734 284 ARG C CZ  
8929  N NH1 . ARG C 284 ? 0.8144 0.7193 0.7698 0.0809  0.1580  -0.0696 284 ARG C NH1 
8930  N NH2 . ARG C 284 ? 0.7742 0.6311 0.7014 0.0891  0.1479  -0.0745 284 ARG C NH2 
8931  N N   . TYR C 285 ? 0.5931 0.6772 0.7901 0.1417  0.1583  -0.0621 285 TYR C N   
8932  C CA  . TYR C 285 ? 0.6135 0.7401 0.8564 0.1470  0.1646  -0.0640 285 TYR C CA  
8933  C C   . TYR C 285 ? 0.5684 0.7200 0.8167 0.1285  0.1650  -0.0617 285 TYR C C   
8934  O O   . TYR C 285 ? 0.6316 0.8097 0.9027 0.1250  0.1807  -0.0674 285 TYR C O   
8935  C CB  . TYR C 285 ? 0.6439 0.7862 0.9197 0.1630  0.1474  -0.0570 285 TYR C CB  
8936  C CG  . TYR C 285 ? 0.6326 0.8224 0.9593 0.1682  0.1490  -0.0575 285 TYR C CG  
8937  C CD1 . TYR C 285 ? 0.6987 0.9057 1.0577 0.1825  0.1662  -0.0661 285 TYR C CD1 
8938  C CD2 . TYR C 285 ? 0.6450 0.8629 0.9891 0.1593  0.1328  -0.0498 285 TYR C CD2 
8939  C CE1 . TYR C 285 ? 0.7273 0.9813 1.1376 0.1873  0.1674  -0.0667 285 TYR C CE1 
8940  C CE2 . TYR C 285 ? 0.6989 0.9620 1.0914 0.1631  0.1325  -0.0505 285 TYR C CE2 
8941  C CZ  . TYR C 285 ? 0.7316 1.0140 1.1587 0.1771  0.1496  -0.0587 285 TYR C CZ  
8942  O OH  . TYR C 285 ? 0.8100 1.1409 1.2898 0.1808  0.1490  -0.0595 285 TYR C OH  
8943  N N   . LEU C 286 ? 0.5905 0.7328 0.8174 0.1161  0.1491  -0.0538 286 LEU C N   
8944  C CA  . LEU C 286 ? 0.5780 0.7403 0.8085 0.0985  0.1489  -0.0518 286 LEU C CA  
8945  C C   . LEU C 286 ? 0.5725 0.7263 0.7831 0.0865  0.1702  -0.0586 286 LEU C C   
8946  O O   . LEU C 286 ? 0.5405 0.7194 0.7691 0.0765  0.1801  -0.0608 286 LEU C O   
8947  C CB  . LEU C 286 ? 0.5588 0.7060 0.7651 0.0888  0.1294  -0.0431 286 LEU C CB  
8948  C CG  . LEU C 286 ? 0.5443 0.7178 0.7803 0.0935  0.1108  -0.0365 286 LEU C CG  
8949  C CD1 . LEU C 286 ? 0.4761 0.6366 0.6894 0.0843  0.0929  -0.0287 286 LEU C CD1 
8950  C CD2 . LEU C 286 ? 0.5251 0.7396 0.7987 0.0882  0.1163  -0.0396 286 LEU C CD2 
8951  N N   . GLU C 287 ? 0.6014 0.7194 0.7745 0.0871  0.1775  -0.0620 287 GLU C N   
8952  C CA  . GLU C 287 ? 0.6556 0.7611 0.8042 0.0770  0.1977  -0.0683 287 GLU C CA  
8953  C C   . GLU C 287 ? 0.6666 0.7992 0.8450 0.0805  0.2201  -0.0765 287 GLU C C   
8954  O O   . GLU C 287 ? 0.6941 0.8276 0.8605 0.0680  0.2369  -0.0797 287 GLU C O   
8955  C CB  . GLU C 287 ? 0.7316 0.7956 0.8387 0.0807  0.2001  -0.0717 287 GLU C CB  
8956  C CG  . GLU C 287 ? 0.8271 0.8756 0.9078 0.0753  0.2227  -0.0801 287 GLU C CG  
8957  C CD  . GLU C 287 ? 0.9465 0.9529 0.9767 0.0701  0.2180  -0.0802 287 GLU C CD  
8958  O OE1 . GLU C 287 ? 0.8818 0.8739 0.9025 0.0713  0.1981  -0.0738 287 GLU C OE1 
8959  O OE2 . GLU C 287 ? 0.9894 0.9782 0.9899 0.0645  0.2339  -0.0863 287 GLU C OE2 
8960  N N   . THR C 288 ? 0.6948 0.8505 0.9132 0.0970  0.2212  -0.0795 288 THR C N   
8961  C CA  . THR C 288 ? 0.6759 0.8616 0.9275 0.1000  0.2436  -0.0876 288 THR C CA  
8962  C C   . THR C 288 ? 0.6599 0.8847 0.9437 0.0869  0.2434  -0.0845 288 THR C C   
8963  O O   . THR C 288 ? 0.6889 0.9363 0.9926 0.0821  0.2645  -0.0906 288 THR C O   
8964  C CB  . THR C 288 ? 0.7268 0.9277 1.0161 0.1230  0.2462  -0.0924 288 THR C CB  
8965  O OG1 . THR C 288 ? 0.7804 1.0197 1.1172 0.1285  0.2302  -0.0864 288 THR C OG1 
8966  C CG2 . THR C 288 ? 0.7403 0.9024 1.0026 0.1367  0.2376  -0.0927 288 THR C CG2 
8967  N N   . TYR C 289 ? 0.6688 0.9015 0.9575 0.0803  0.2208  -0.0756 289 TYR C N   
8968  C CA  . TYR C 289 ? 0.6789 0.9421 0.9903 0.0648  0.2171  -0.0724 289 TYR C CA  
8969  C C   . TYR C 289 ? 0.6191 0.8610 0.8920 0.0435  0.2236  -0.0705 289 TYR C C   
8970  O O   . TYR C 289 ? 0.5709 0.8317 0.8566 0.0285  0.2207  -0.0679 289 TYR C O   
8971  C CB  . TYR C 289 ? 0.7082 0.9826 1.0339 0.0671  0.1887  -0.0641 289 TYR C CB  
8972  C CG  . TYR C 289 ? 0.7488 1.0562 1.1226 0.0843  0.1779  -0.0633 289 TYR C CG  
8973  C CD1 . TYR C 289 ? 0.8058 1.1597 1.2286 0.0814  0.1778  -0.0647 289 TYR C CD1 
8974  C CD2 . TYR C 289 ? 0.7412 1.0320 1.1113 0.1034  0.1670  -0.0608 289 TYR C CD2 
8975  C CE1 . TYR C 289 ? 0.8140 1.1986 1.2816 0.0984  0.1654  -0.0631 289 TYR C CE1 
8976  C CE2 . TYR C 289 ? 0.7760 1.0938 1.1880 0.1204  0.1559  -0.0588 289 TYR C CE2 
8977  C CZ  . TYR C 289 ? 0.8001 1.1653 1.2610 0.1185  0.1544  -0.0597 289 TYR C CZ  
8978  O OH  . TYR C 289 ? 0.7757 1.1680 1.2788 0.1366  0.1413  -0.0568 289 TYR C OH  
8979  N N   . GLY C 290 ? 0.5365 0.7384 0.7619 0.0416  0.2304  -0.0714 290 GLY C N   
8980  C CA  . GLY C 290 ? 0.4926 0.6700 0.6786 0.0236  0.2311  -0.0674 290 GLY C CA  
8981  C C   . GLY C 290 ? 0.4763 0.6389 0.6452 0.0188  0.2069  -0.0591 290 GLY C C   
8982  O O   . GLY C 290 ? 0.4103 0.5581 0.5546 0.0039  0.2053  -0.0550 290 GLY C O   
8983  N N   . ALA C 291 ? 0.3791 0.5432 0.5587 0.0316  0.1889  -0.0562 291 ALA C N   
8984  C CA  . ALA C 291 ? 0.4340 0.5884 0.6020 0.0280  0.1667  -0.0487 291 ALA C CA  
8985  C C   . ALA C 291 ? 0.4298 0.5449 0.5574 0.0320  0.1602  -0.0463 291 ALA C C   
8986  O O   . ALA C 291 ? 0.4535 0.5575 0.5786 0.0457  0.1599  -0.0486 291 ALA C O   
8987  C CB  . ALA C 291 ? 0.3696 0.5501 0.5728 0.0385  0.1504  -0.0460 291 ALA C CB  
8988  N N   . VAL C 292 ? 0.3724 0.4664 0.4698 0.0201  0.1549  -0.0421 292 VAL C N   
8989  C CA  . VAL C 292 ? 0.3481 0.4084 0.4109 0.0223  0.1459  -0.0391 292 VAL C CA  
8990  C C   . VAL C 292 ? 0.3964 0.4553 0.4580 0.0195  0.1264  -0.0322 292 VAL C C   
8991  O O   . VAL C 292 ? 0.3760 0.4462 0.4440 0.0089  0.1228  -0.0297 292 VAL C O   
8992  C CB  . VAL C 292 ? 0.4046 0.4387 0.4306 0.0122  0.1553  -0.0395 292 VAL C CB  
8993  C CG1 . VAL C 292 ? 0.4162 0.4551 0.4398 -0.0029 0.1557  -0.0358 292 VAL C CG1 
8994  C CG2 . VAL C 292 ? 0.4495 0.4519 0.4438 0.0149  0.1441  -0.0366 292 VAL C CG2 
8995  N N   . SER C 293 ? 0.3884 0.4317 0.4401 0.0280  0.1147  -0.0294 293 SER C N   
8996  C CA  . SER C 293 ? 0.3806 0.4162 0.4228 0.0240  0.0989  -0.0231 293 SER C CA  
8997  C C   . SER C 293 ? 0.3801 0.3885 0.3894 0.0159  0.0988  -0.0213 293 SER C C   
8998  O O   . SER C 293 ? 0.4262 0.4135 0.4158 0.0195  0.1016  -0.0230 293 SER C O   
8999  C CB  . SER C 293 ? 0.3627 0.3937 0.4089 0.0352  0.0865  -0.0198 293 SER C CB  
9000  O OG  . SER C 293 ? 0.4064 0.4299 0.4415 0.0297  0.0739  -0.0141 293 SER C OG  
9001  N N   . ILE C 294 ? 0.3338 0.3421 0.3373 0.0052  0.0950  -0.0182 294 ILE C N   
9002  C CA  . ILE C 294 ? 0.3703 0.3540 0.3452 -0.0016 0.0942  -0.0158 294 ILE C CA  
9003  C C   . ILE C 294 ? 0.4052 0.3753 0.3698 0.0010  0.0808  -0.0115 294 ILE C C   
9004  O O   . ILE C 294 ? 0.4191 0.3704 0.3632 -0.0032 0.0782  -0.0092 294 ILE C O   
9005  C CB  . ILE C 294 ? 0.3958 0.3812 0.3672 -0.0141 0.0979  -0.0144 294 ILE C CB  
9006  C CG1 . ILE C 294 ? 0.3431 0.3475 0.3345 -0.0180 0.0903  -0.0132 294 ILE C CG1 
9007  C CG2 . ILE C 294 ? 0.4727 0.4636 0.4454 -0.0186 0.1139  -0.0180 294 ILE C CG2 
9008  C CD1 . ILE C 294 ? 0.3846 0.3808 0.3696 -0.0166 0.0764  -0.0093 294 ILE C CD1 
9009  N N   . GLY C 295 ? 0.3715 0.3508 0.3501 0.0077  0.0722  -0.0099 295 GLY C N   
9010  C CA  . GLY C 295 ? 0.3697 0.3373 0.3394 0.0090  0.0612  -0.0057 295 GLY C CA  
9011  C C   . GLY C 295 ? 0.3700 0.3530 0.3541 0.0093  0.0526  -0.0028 295 GLY C C   
9012  O O   . GLY C 295 ? 0.3502 0.3536 0.3534 0.0111  0.0528  -0.0040 295 GLY C O   
9013  N N   . SER C 296 ? 0.3172 0.2902 0.2917 0.0077  0.0449  0.0009  296 SER C N   
9014  C CA  . SER C 296 ? 0.3467 0.3288 0.3278 0.0080  0.0363  0.0041  296 SER C CA  
9015  C C   . SER C 296 ? 0.3131 0.2814 0.2805 0.0041  0.0324  0.0068  296 SER C C   
9016  O O   . SER C 296 ? 0.3589 0.3117 0.3150 0.0036  0.0340  0.0070  296 SER C O   
9017  C CB  . SER C 296 ? 0.3426 0.3287 0.3323 0.0177  0.0312  0.0067  296 SER C CB  
9018  O OG  . SER C 296 ? 0.3674 0.3349 0.3465 0.0221  0.0308  0.0081  296 SER C OG  
9019  N N   . LEU C 297 ? 0.3278 0.3023 0.2964 0.0016  0.0269  0.0087  297 LEU C N   
9020  C CA  . LEU C 297 ? 0.3211 0.2840 0.2788 -0.0013 0.0246  0.0108  297 LEU C CA  
9021  C C   . LEU C 297 ? 0.3370 0.2885 0.2901 0.0039  0.0221  0.0144  297 LEU C C   
9022  O O   . LEU C 297 ? 0.3612 0.3011 0.3072 0.0021  0.0222  0.0154  297 LEU C O   
9023  C CB  . LEU C 297 ? 0.3229 0.2939 0.2804 -0.0049 0.0204  0.0114  297 LEU C CB  
9024  C CG  . LEU C 297 ? 0.3363 0.2971 0.2842 -0.0082 0.0205  0.0124  297 LEU C CG  
9025  C CD1 . LEU C 297 ? 0.3358 0.2892 0.2803 -0.0130 0.0253  0.0094  297 LEU C CD1 
9026  C CD2 . LEU C 297 ? 0.3902 0.3578 0.3345 -0.0107 0.0165  0.0128  297 LEU C CD2 
9027  N N   . TYR C 298 ? 0.3523 0.3066 0.3109 0.0106  0.0196  0.0163  298 TYR C N   
9028  C CA  . TYR C 298 ? 0.3640 0.3049 0.3182 0.0150  0.0176  0.0194  298 TYR C CA  
9029  C C   . TYR C 298 ? 0.3728 0.3006 0.3208 0.0146  0.0212  0.0165  298 TYR C C   
9030  O O   . TYR C 298 ? 0.3628 0.2791 0.3041 0.0120  0.0197  0.0178  298 TYR C O   
9031  C CB  . TYR C 298 ? 0.3605 0.3060 0.3225 0.0230  0.0145  0.0218  298 TYR C CB  
9032  C CG  . TYR C 298 ? 0.3841 0.3133 0.3420 0.0279  0.0133  0.0243  298 TYR C CG  
9033  C CD1 . TYR C 298 ? 0.4362 0.3570 0.3883 0.0273  0.0090  0.0304  298 TYR C CD1 
9034  C CD2 . TYR C 298 ? 0.4299 0.3503 0.3879 0.0321  0.0174  0.0202  298 TYR C CD2 
9035  C CE1 . TYR C 298 ? 0.4224 0.3259 0.3707 0.0304  0.0081  0.0328  298 TYR C CE1 
9036  C CE2 . TYR C 298 ? 0.4186 0.3212 0.3717 0.0357  0.0161  0.0216  298 TYR C CE2 
9037  C CZ  . TYR C 298 ? 0.4578 0.3520 0.4068 0.0344  0.0113  0.0280  298 TYR C CZ  
9038  O OH  . TYR C 298 ? 0.4914 0.3664 0.4359 0.0368  0.0103  0.0293  298 TYR C OH  
9039  N N   . THR C 299 ? 0.3323 0.2622 0.2825 0.0168  0.0261  0.0122  299 THR C N   
9040  C CA  . THR C 299 ? 0.3403 0.2568 0.2805 0.0158  0.0296  0.0090  299 THR C CA  
9041  C C   . THR C 299 ? 0.3729 0.2839 0.3043 0.0088  0.0289  0.0094  299 THR C C   
9042  O O   . THR C 299 ? 0.3527 0.2507 0.2752 0.0073  0.0265  0.0095  299 THR C O   
9043  C CB  . THR C 299 ? 0.3805 0.3027 0.3240 0.0185  0.0371  0.0042  299 THR C CB  
9044  O OG1 . THR C 299 ? 0.3970 0.3221 0.3502 0.0271  0.0369  0.0039  299 THR C OG1 
9045  C CG2 . THR C 299 ? 0.4441 0.3519 0.3726 0.0163  0.0416  0.0004  299 THR C CG2 
9046  N N   . PHE C 300 ? 0.3716 0.2920 0.3063 0.0045  0.0303  0.0096  300 PHE C N   
9047  C CA  . PHE C 300 ? 0.3726 0.2861 0.2996 -0.0008 0.0303  0.0100  300 PHE C CA  
9048  C C   . PHE C 300 ? 0.3561 0.2655 0.2834 -0.0018 0.0251  0.0131  300 PHE C C   
9049  O O   . PHE C 300 ? 0.3651 0.2657 0.2871 -0.0036 0.0230  0.0140  300 PHE C O   
9050  C CB  . PHE C 300 ? 0.3504 0.2728 0.2809 -0.0054 0.0340  0.0088  300 PHE C CB  
9051  C CG  . PHE C 300 ? 0.3857 0.3133 0.3172 -0.0067 0.0409  0.0058  300 PHE C CG  
9052  C CD1 . PHE C 300 ? 0.3749 0.2984 0.3023 -0.0033 0.0449  0.0037  300 PHE C CD1 
9053  C CD2 . PHE C 300 ? 0.4006 0.3374 0.3375 -0.0123 0.0444  0.0043  300 PHE C CD2 
9054  C CE1 . PHE C 300 ? 0.3845 0.3147 0.3142 -0.0052 0.0536  0.0005  300 PHE C CE1 
9055  C CE2 . PHE C 300 ? 0.3324 0.2756 0.2724 -0.0152 0.0519  0.0017  300 PHE C CE2 
9056  C CZ  . PHE C 300 ? 0.3805 0.3213 0.3175 -0.0114 0.0571  -0.0001 300 PHE C CZ  
9057  N N   . ALA C 301 ? 0.3422 0.2583 0.2760 -0.0006 0.0230  0.0152  301 ALA C N   
9058  C CA  . ALA C 301 ? 0.3615 0.2763 0.2964 -0.0028 0.0210  0.0175  301 ALA C CA  
9059  C C   . ALA C 301 ? 0.3491 0.2626 0.2862 -0.0011 0.0183  0.0209  301 ALA C C   
9060  O O   . ALA C 301 ? 0.3422 0.2571 0.2810 -0.0033 0.0184  0.0228  301 ALA C O   
9061  C CB  . ALA C 301 ? 0.3748 0.2975 0.3114 -0.0059 0.0232  0.0162  301 ALA C CB  
9062  N N   . LEU C 302 ? 0.3209 0.2305 0.2575 0.0025  0.0169  0.0216  302 LEU C N   
9063  C CA  . LEU C 302 ? 0.3318 0.2355 0.2689 0.0030  0.0145  0.0255  302 LEU C CA  
9064  C C   . LEU C 302 ? 0.3716 0.2689 0.3097 -0.0009 0.0132  0.0259  302 LEU C C   
9065  O O   . LEU C 302 ? 0.3522 0.2495 0.2934 -0.0036 0.0132  0.0292  302 LEU C O   
9066  C CB  . LEU C 302 ? 0.3400 0.2360 0.2760 0.0079  0.0132  0.0256  302 LEU C CB  
9067  C CG  . LEU C 302 ? 0.3833 0.2709 0.3190 0.0086  0.0109  0.0305  302 LEU C CG  
9068  C CD1 . LEU C 302 ? 0.3698 0.2652 0.3057 0.0099  0.0103  0.0353  302 LEU C CD1 
9069  C CD2 . LEU C 302 ? 0.4239 0.2990 0.3579 0.0139  0.0100  0.0292  302 LEU C CD2 
9070  N N   . GLU C 303 ? 0.3164 0.2086 0.2517 -0.0015 0.0119  0.0228  303 GLU C N   
9071  C CA  . GLU C 303 ? 0.3059 0.1948 0.2438 -0.0050 0.0087  0.0229  303 GLU C CA  
9072  C C   . GLU C 303 ? 0.3346 0.2251 0.2707 -0.0056 0.0087  0.0213  303 GLU C C   
9073  O O   . GLU C 303 ? 0.3702 0.2619 0.3124 -0.0073 0.0062  0.0224  303 GLU C O   
9074  C CB  . GLU C 303 ? 0.3440 0.2212 0.2778 -0.0059 0.0041  0.0216  303 GLU C CB  
9075  C CG  . GLU C 303 ? 0.3747 0.2447 0.3088 -0.0053 0.0039  0.0231  303 GLU C CG  
9076  C CD  . GLU C 303 ? 0.3918 0.2640 0.3345 -0.0092 0.0038  0.0275  303 GLU C CD  
9077  O OE1 . GLU C 303 ? 0.3937 0.2758 0.3440 -0.0116 0.0053  0.0289  303 GLU C OE1 
9078  O OE2 . GLU C 303 ? 0.3567 0.2197 0.2988 -0.0102 0.0031  0.0293  303 GLU C OE2 
9079  N N   . GLY C 304 ? 0.3242 0.2147 0.2533 -0.0043 0.0115  0.0191  304 GLY C N   
9080  C CA  . GLY C 304 ? 0.3204 0.2092 0.2458 -0.0054 0.0118  0.0186  304 GLY C CA  
9081  C C   . GLY C 304 ? 0.3273 0.2226 0.2610 -0.0063 0.0136  0.0198  304 GLY C C   
9082  O O   . GLY C 304 ? 0.3444 0.2471 0.2822 -0.0065 0.0171  0.0196  304 GLY C O   
9083  N N   . ILE C 305 ? 0.3399 0.2316 0.2754 -0.0064 0.0110  0.0209  305 ILE C N   
9084  C CA  . ILE C 305 ? 0.3096 0.2056 0.2541 -0.0060 0.0134  0.0212  305 ILE C CA  
9085  C C   . ILE C 305 ? 0.3480 0.2374 0.2864 -0.0060 0.0148  0.0209  305 ILE C C   
9086  O O   . ILE C 305 ? 0.3529 0.2336 0.2842 -0.0054 0.0104  0.0228  305 ILE C O   
9087  C CB  . ILE C 305 ? 0.3121 0.2109 0.2693 -0.0051 0.0093  0.0232  305 ILE C CB  
9088  C CG1 . ILE C 305 ? 0.3532 0.2577 0.3164 -0.0068 0.0098  0.0239  305 ILE C CG1 
9089  C CG2 . ILE C 305 ? 0.3472 0.2500 0.3150 -0.0034 0.0132  0.0228  305 ILE C CG2 
9090  C CD1 . ILE C 305 ? 0.3295 0.2409 0.2950 -0.0076 0.0172  0.0232  305 ILE C CD1 
9091  N N   . TRP C 306 ? 0.3356 0.2273 0.2752 -0.0071 0.0206  0.0188  306 TRP C N   
9092  C CA  . TRP C 306 ? 0.3723 0.2568 0.3039 -0.0091 0.0237  0.0178  306 TRP C CA  
9093  C C   . TRP C 306 ? 0.3659 0.2460 0.3025 -0.0081 0.0264  0.0168  306 TRP C C   
9094  O O   . TRP C 306 ? 0.3643 0.2502 0.3105 -0.0063 0.0282  0.0154  306 TRP C O   
9095  C CB  . TRP C 306 ? 0.3705 0.2615 0.2984 -0.0128 0.0284  0.0146  306 TRP C CB  
9096  C CG  . TRP C 306 ? 0.3728 0.2674 0.2968 -0.0126 0.0273  0.0148  306 TRP C CG  
9097  C CD1 . TRP C 306 ? 0.3699 0.2702 0.2972 -0.0104 0.0249  0.0154  306 TRP C CD1 
9098  C CD2 . TRP C 306 ? 0.3740 0.2646 0.2896 -0.0146 0.0297  0.0144  306 TRP C CD2 
9099  N NE1 . TRP C 306 ? 0.3489 0.2489 0.2713 -0.0098 0.0255  0.0146  306 TRP C NE1 
9100  C CE2 . TRP C 306 ? 0.3900 0.2854 0.3055 -0.0124 0.0291  0.0138  306 TRP C CE2 
9101  C CE3 . TRP C 306 ? 0.4089 0.2917 0.3168 -0.0182 0.0335  0.0146  306 TRP C CE3 
9102  C CZ2 . TRP C 306 ? 0.3814 0.2750 0.2900 -0.0132 0.0328  0.0125  306 TRP C CZ2 
9103  C CZ3 . TRP C 306 ? 0.3927 0.2743 0.2929 -0.0202 0.0374  0.0140  306 TRP C CZ3 
9104  C CH2 . TRP C 306 ? 0.3774 0.2652 0.2785 -0.0173 0.0374  0.0125  306 TRP C CH2 
9105  N N   . GLU C 307 ? 0.3428 0.2116 0.2722 -0.0096 0.0281  0.0172  307 GLU C N   
9106  C CA  . GLU C 307 ? 0.3708 0.2318 0.3034 -0.0086 0.0316  0.0155  307 GLU C CA  
9107  C C   . GLU C 307 ? 0.3770 0.2275 0.2989 -0.0141 0.0357  0.0144  307 GLU C C   
9108  O O   . GLU C 307 ? 0.4055 0.2542 0.3182 -0.0176 0.0356  0.0163  307 GLU C O   
9109  C CB  . GLU C 307 ? 0.3485 0.2019 0.2877 -0.0020 0.0265  0.0198  307 GLU C CB  
9110  C CG  . GLU C 307 ? 0.4261 0.2642 0.3534 -0.0017 0.0219  0.0253  307 GLU C CG  
9111  C CD  . GLU C 307 ? 0.4191 0.2498 0.3531 0.0057  0.0142  0.0307  307 GLU C CD  
9112  O OE1 . GLU C 307 ? 0.4285 0.2696 0.3805 0.0108  0.0125  0.0297  307 GLU C OE1 
9113  O OE2 . GLU C 307 ? 0.4676 0.2830 0.3890 0.0063  0.0095  0.0363  307 GLU C OE2 
9114  N N   . ASP C 308 ? 0.3678 0.2103 0.2909 -0.0152 0.0403  0.0111  308 ASP C N   
9115  C CA  . ASP C 308 ? 0.4091 0.2382 0.3227 -0.0211 0.0444  0.0104  308 ASP C CA  
9116  C C   . ASP C 308 ? 0.4809 0.2914 0.3882 -0.0175 0.0411  0.0173  308 ASP C C   
9117  O O   . ASP C 308 ? 0.4289 0.2327 0.3429 -0.0099 0.0379  0.0197  308 ASP C O   
9118  C CB  . ASP C 308 ? 0.4314 0.2554 0.3469 -0.0242 0.0503  0.0034  308 ASP C CB  
9119  C CG  . ASP C 308 ? 0.4774 0.3183 0.3955 -0.0285 0.0523  -0.0031 308 ASP C CG  
9120  O OD1 . ASP C 308 ? 0.4919 0.3469 0.4099 -0.0311 0.0502  -0.0023 308 ASP C OD1 
9121  O OD2 . ASP C 308 ? 0.5174 0.3566 0.4368 -0.0289 0.0560  -0.0092 308 ASP C OD2 
9122  N N   . LYS C 309 ? 0.3879 0.2581 0.3498 -0.0050 0.0444  0.0241  309 LYS C N   
9123  C CA  . LYS C 309 ? 0.4000 0.2575 0.3596 -0.0021 0.0431  0.0338  309 LYS C CA  
9124  C C   . LYS C 309 ? 0.4092 0.2546 0.3781 -0.0040 0.0505  0.0333  309 LYS C C   
9125  O O   . LYS C 309 ? 0.4328 0.2793 0.4072 -0.0092 0.0573  0.0241  309 LYS C O   
9126  C CB  . LYS C 309 ? 0.4270 0.2839 0.3721 -0.0043 0.0418  0.0386  309 LYS C CB  
9127  C CG  . LYS C 309 ? 0.4032 0.2689 0.3395 -0.0028 0.0370  0.0390  309 LYS C CG  
9128  C CD  . LYS C 309 ? 0.4604 0.3246 0.3960 0.0012  0.0301  0.0454  309 LYS C CD  
9129  C CE  . LYS C 309 ? 0.4866 0.3574 0.4110 0.0009  0.0264  0.0456  309 LYS C CE  
9130  N NZ  . LYS C 309 ? 0.4679 0.3390 0.3916 0.0034  0.0186  0.0528  309 LYS C NZ  
9131  N N   . PRO C 310 ? 0.4549 0.2886 0.4259 -0.0008 0.0499  0.0438  310 PRO C N   
9132  C CA  . PRO C 310 ? 0.4192 0.2395 0.4028 -0.0014 0.0586  0.0442  310 PRO C CA  
9133  C C   . PRO C 310 ? 0.4620 0.2778 0.4404 -0.0089 0.0666  0.0381  310 PRO C C   
9134  O O   . PRO C 310 ? 0.4513 0.2568 0.4398 -0.0118 0.0765  0.0340  310 PRO C O   
9135  C CB  . PRO C 310 ? 0.4497 0.2615 0.4356 0.0038  0.0540  0.0605  310 PRO C CB  
9136  C CG  . PRO C 310 ? 0.4818 0.3047 0.4630 0.0078  0.0429  0.0660  310 PRO C CG  
9137  C CD  . PRO C 310 ? 0.4901 0.3237 0.4556 0.0035  0.0410  0.0562  310 PRO C CD  
9138  N N   . ASP C 311 ? 0.4135 0.2361 0.3778 -0.0126 0.0638  0.0376  311 ASP C N   
9139  C CA  . ASP C 311 ? 0.4197 0.2416 0.3804 -0.0201 0.0708  0.0317  311 ASP C CA  
9140  C C   . ASP C 311 ? 0.4300 0.2675 0.3922 -0.0260 0.0720  0.0207  311 ASP C C   
9141  O O   . ASP C 311 ? 0.4770 0.3193 0.4368 -0.0330 0.0761  0.0166  311 ASP C O   
9142  C CB  . ASP C 311 ? 0.4398 0.2596 0.3869 -0.0215 0.0689  0.0382  311 ASP C CB  
9143  C CG  . ASP C 311 ? 0.4589 0.2920 0.3976 -0.0209 0.0634  0.0375  311 ASP C CG  
9144  O OD1 . ASP C 311 ? 0.4479 0.2904 0.3900 -0.0175 0.0588  0.0352  311 ASP C OD1 
9145  O OD2 . ASP C 311 ? 0.4952 0.3286 0.4249 -0.0238 0.0651  0.0393  311 ASP C OD2 
9146  N N   . GLY C 312 ? 0.4148 0.2617 0.3811 -0.0238 0.0683  0.0167  312 GLY C N   
9147  C CA  . GLY C 312 ? 0.3962 0.2596 0.3636 -0.0302 0.0683  0.0081  312 GLY C CA  
9148  C C   . GLY C 312 ? 0.4129 0.2917 0.3748 -0.0287 0.0620  0.0113  312 GLY C C   
9149  O O   . GLY C 312 ? 0.4298 0.3251 0.3941 -0.0335 0.0608  0.0070  312 GLY C O   
9150  N N   . SER C 313 ? 0.3737 0.2475 0.3286 -0.0233 0.0590  0.0191  313 SER C N   
9151  C CA  . SER C 313 ? 0.3927 0.2783 0.3439 -0.0221 0.0563  0.0217  313 SER C CA  
9152  C C   . SER C 313 ? 0.3790 0.2717 0.3303 -0.0168 0.0507  0.0219  313 SER C C   
9153  O O   . SER C 313 ? 0.3660 0.2528 0.3182 -0.0131 0.0477  0.0217  313 SER C O   
9154  C CB  . SER C 313 ? 0.3947 0.2701 0.3365 -0.0210 0.0582  0.0281  313 SER C CB  
9155  O OG  . SER C 313 ? 0.4176 0.2816 0.3520 -0.0165 0.0543  0.0332  313 SER C OG  
9156  N N   . TRP C 314 ? 0.3664 0.2706 0.3177 -0.0159 0.0500  0.0236  314 TRP C N   
9157  C CA  . TRP C 314 ? 0.3701 0.2810 0.3213 -0.0113 0.0457  0.0238  314 TRP C CA  
9158  C C   . TRP C 314 ? 0.3463 0.2468 0.2868 -0.0076 0.0453  0.0283  314 TRP C C   
9159  O O   . TRP C 314 ? 0.3619 0.2571 0.2968 -0.0094 0.0499  0.0313  314 TRP C O   
9160  C CB  . TRP C 314 ? 0.3776 0.3062 0.3363 -0.0122 0.0464  0.0246  314 TRP C CB  
9161  C CG  . TRP C 314 ? 0.3517 0.2911 0.3145 -0.0108 0.0418  0.0218  314 TRP C CG  
9162  C CD1 . TRP C 314 ? 0.3397 0.2760 0.3020 -0.0108 0.0387  0.0166  314 TRP C CD1 
9163  C CD2 . TRP C 314 ? 0.3661 0.3205 0.3349 -0.0090 0.0409  0.0247  314 TRP C CD2 
9164  N NE1 . TRP C 314 ? 0.3446 0.2937 0.3106 -0.0104 0.0355  0.0150  314 TRP C NE1 
9165  C CE2 . TRP C 314 ? 0.3524 0.3126 0.3220 -0.0089 0.0364  0.0206  314 TRP C CE2 
9166  C CE3 . TRP C 314 ? 0.3884 0.3509 0.3638 -0.0073 0.0448  0.0309  314 TRP C CE3 
9167  C CZ2 . TRP C 314 ? 0.3960 0.3705 0.3710 -0.0077 0.0344  0.0229  314 TRP C CZ2 
9168  C CZ3 . TRP C 314 ? 0.3537 0.3304 0.3370 -0.0050 0.0434  0.0341  314 TRP C CZ3 
9169  C CH2 . TRP C 314 ? 0.3642 0.3468 0.3463 -0.0053 0.0377  0.0303  314 TRP C CH2 
9170  N N   . GLY C 315 ? 0.3603 0.2574 0.2972 -0.0039 0.0402  0.0287  315 GLY C N   
9171  C CA  . GLY C 315 ? 0.4157 0.3050 0.3402 -0.0030 0.0390  0.0329  315 GLY C CA  
9172  C C   . GLY C 315 ? 0.3833 0.2769 0.3070 0.0005  0.0337  0.0321  315 GLY C C   
9173  O O   . GLY C 315 ? 0.3545 0.2563 0.2876 0.0030  0.0315  0.0281  315 GLY C O   
9174  N N   . GLY C 316 ? 0.3909 0.2796 0.3022 -0.0006 0.0324  0.0352  316 GLY C N   
9175  C CA  . GLY C 316 ? 0.3982 0.2917 0.3083 0.0018  0.0276  0.0341  316 GLY C CA  
9176  C C   . GLY C 316 ? 0.4414 0.3360 0.3606 0.0055  0.0206  0.0355  316 GLY C C   
9177  O O   . GLY C 316 ? 0.3796 0.2677 0.3012 0.0055  0.0185  0.0405  316 GLY C O   
9178  N N   . ARG C 317 ? 0.3618 0.2642 0.2879 0.0089  0.0181  0.0314  317 ARG C N   
9179  C CA  . ARG C 317 ? 0.3657 0.2692 0.3037 0.0126  0.0137  0.0313  317 ARG C CA  
9180  C C   . ARG C 317 ? 0.3628 0.2631 0.2977 0.0129  0.0073  0.0399  317 ARG C C   
9181  O O   . ARG C 317 ? 0.4144 0.3160 0.3360 0.0097  0.0048  0.0426  317 ARG C O   
9182  C CB  . ARG C 317 ? 0.3325 0.2450 0.2769 0.0152  0.0129  0.0248  317 ARG C CB  
9183  C CG  . ARG C 317 ? 0.3277 0.2398 0.2861 0.0183  0.0111  0.0236  317 ARG C CG  
9184  C CD  . ARG C 317 ? 0.3557 0.2762 0.3195 0.0193  0.0119  0.0155  317 ARG C CD  
9185  N NE  . ARG C 317 ? 0.3608 0.2795 0.3386 0.0221  0.0115  0.0140  317 ARG C NE  
9186  C CZ  . ARG C 317 ? 0.3704 0.2932 0.3552 0.0218  0.0140  0.0062  317 ARG C CZ  
9187  N NH1 . ARG C 317 ? 0.3606 0.2915 0.3392 0.0187  0.0153  0.0002  317 ARG C NH1 
9188  N NH2 . ARG C 317 ? 0.3666 0.2862 0.3657 0.0245  0.0151  0.0054  317 ARG C NH2 
9189  N N   . THR C 318 ? 0.3720 0.2682 0.3194 0.0157  0.0055  0.0451  318 THR C N   
9190  C CA  . THR C 318 ? 0.3829 0.2787 0.3316 0.0162  -0.0018 0.0569  318 THR C CA  
9191  C C   . THR C 318 ? 0.3567 0.2619 0.3081 0.0180  -0.0077 0.0573  318 THR C C   
9192  O O   . THR C 318 ? 0.3604 0.2694 0.3235 0.0220  -0.0058 0.0501  318 THR C O   
9193  C CB  . THR C 318 ? 0.4157 0.3053 0.3834 0.0203  -0.0006 0.0635  318 THR C CB  
9194  O OG1 . THR C 318 ? 0.3970 0.2774 0.3600 0.0176  0.0044  0.0644  318 THR C OG1 
9195  C CG2 . THR C 318 ? 0.4184 0.3110 0.3911 0.0213  -0.0093 0.0793  318 THR C CG2 
9196  N N   . LEU C 319 ? 0.3855 0.2948 0.3242 0.0134  -0.0145 0.0652  319 LEU C N   
9197  C CA  . LEU C 319 ? 0.4132 0.3326 0.3531 0.0135  -0.0205 0.0659  319 LEU C CA  
9198  C C   . LEU C 319 ? 0.4436 0.3672 0.4085 0.0202  -0.0250 0.0737  319 LEU C C   
9199  O O   . LEU C 319 ? 0.3947 0.3145 0.3710 0.0222  -0.0263 0.0846  319 LEU C O   
9200  C CB  . LEU C 319 ? 0.4332 0.3563 0.3513 0.0039  -0.0264 0.0727  319 LEU C CB  
9201  C CG  . LEU C 319 ? 0.3770 0.2925 0.2721 -0.0033 -0.0189 0.0655  319 LEU C CG  
9202  C CD1 . LEU C 319 ? 0.4491 0.3655 0.3208 -0.0155 -0.0228 0.0721  319 LEU C CD1 
9203  C CD2 . LEU C 319 ? 0.4534 0.3708 0.3459 -0.0019 -0.0126 0.0527  319 LEU C CD2 
9204  N N   . PRO C 320 ? 0.4048 0.3354 0.3814 0.0241  -0.0258 0.0689  320 PRO C N   
9205  C CA  . PRO C 320 ? 0.4323 0.3650 0.4377 0.0314  -0.0265 0.0750  320 PRO C CA  
9206  C C   . PRO C 320 ? 0.4456 0.3847 0.4607 0.0314  -0.0358 0.0944  320 PRO C C   
9207  O O   . PRO C 320 ? 0.4668 0.4019 0.5052 0.0371  -0.0338 0.1035  320 PRO C O   
9208  C CB  . PRO C 320 ? 0.4926 0.4330 0.5035 0.0335  -0.0265 0.0663  320 PRO C CB  
9209  C CG  . PRO C 320 ? 0.4465 0.3846 0.4359 0.0295  -0.0217 0.0522  320 PRO C CG  
9210  C CD  . PRO C 320 ? 0.3826 0.3177 0.3496 0.0228  -0.0235 0.0566  320 PRO C CD  
9211  N N   . TRP C 321 ? 0.4245 0.3734 0.4217 0.0237  -0.0453 0.1017  321 TRP C N   
9212  C CA  . TRP C 321 ? 0.4675 0.4264 0.4715 0.0212  -0.0562 0.1224  321 TRP C CA  
9213  C C   . TRP C 321 ? 0.4647 0.4152 0.4658 0.0196  -0.0561 0.1332  321 TRP C C   
9214  O O   . TRP C 321 ? 0.5038 0.4617 0.5174 0.0196  -0.0642 0.1530  321 TRP C O   
9215  C CB  . TRP C 321 ? 0.4885 0.4606 0.4690 0.0097  -0.0660 0.1260  321 TRP C CB  
9216  C CG  . TRP C 321 ? 0.4437 0.4090 0.3885 -0.0010 -0.0622 0.1152  321 TRP C CG  
9217  C CD1 . TRP C 321 ? 0.4967 0.4588 0.4183 -0.0116 -0.0645 0.1216  321 TRP C CD1 
9218  C CD2 . TRP C 321 ? 0.3905 0.3508 0.3206 -0.0024 -0.0540 0.0965  321 TRP C CD2 
9219  N NE1 . TRP C 321 ? 0.4537 0.4082 0.3477 -0.0195 -0.0568 0.1070  321 TRP C NE1 
9220  C CE2 . TRP C 321 ? 0.3935 0.3473 0.2938 -0.0134 -0.0506 0.0925  321 TRP C CE2 
9221  C CE3 . TRP C 321 ? 0.3922 0.3528 0.3323 0.0043  -0.0487 0.0835  321 TRP C CE3 
9222  C CZ2 . TRP C 321 ? 0.4289 0.3764 0.3127 -0.0166 -0.0412 0.0771  321 TRP C CZ2 
9223  C CZ3 . TRP C 321 ? 0.4203 0.3758 0.3422 0.0008  -0.0410 0.0690  321 TRP C CZ3 
9224  C CH2 . TRP C 321 ? 0.4102 0.3591 0.3060 -0.0089 -0.0369 0.0663  321 TRP C CH2 
9225  N N   . ASP C 322 ? 0.4691 0.4056 0.4553 0.0181  -0.0473 0.1220  322 ASP C N   
9226  C CA  . ASP C 322 ? 0.5144 0.4408 0.5007 0.0178  -0.0448 0.1302  322 ASP C CA  
9227  C C   . ASP C 322 ? 0.4771 0.3935 0.4928 0.0282  -0.0360 0.1301  322 ASP C C   
9228  O O   . ASP C 322 ? 0.5193 0.4269 0.5387 0.0286  -0.0333 0.1381  322 ASP C O   
9229  C CB  . ASP C 322 ? 0.5089 0.4256 0.4662 0.0104  -0.0389 0.1189  322 ASP C CB  
9230  C CG  . ASP C 322 ? 0.5178 0.4406 0.4461 -0.0023 -0.0461 0.1238  322 ASP C CG  
9231  O OD1 . ASP C 322 ? 0.6119 0.5454 0.5417 -0.0065 -0.0569 0.1404  322 ASP C OD1 
9232  O OD2 . ASP C 322 ? 0.5278 0.4455 0.4331 -0.0089 -0.0405 0.1120  322 ASP C OD2 
9233  N N   . LYS C 323 ? 0.4692 0.3864 0.5056 0.0354  -0.0307 0.1215  323 LYS C N   
9234  C CA  . LYS C 323 ? 0.5019 0.4089 0.5671 0.0436  -0.0199 0.1194  323 LYS C CA  
9235  C C   . LYS C 323 ? 0.4673 0.3824 0.5642 0.0508  -0.0219 0.1295  323 LYS C C   
9236  O O   . LYS C 323 ? 0.5234 0.4311 0.6434 0.0568  -0.0107 0.1217  323 LYS C O   
9237  C CB  . LYS C 323 ? 0.5948 0.4941 0.6569 0.0438  -0.0084 0.0972  323 LYS C CB  
9238  C CG  . LYS C 323 ? 0.5934 0.4882 0.6288 0.0375  -0.0057 0.0853  323 LYS C CG  
9239  C CD  . LYS C 323 ? 0.5886 0.4846 0.6195 0.0366  0.0002  0.0672  323 LYS C CD  
9240  C CE  . LYS C 323 ? 0.6583 0.5453 0.7061 0.0384  0.0122  0.0574  323 LYS C CE  
9241  N NZ  . LYS C 323 ? 0.6464 0.5385 0.6818 0.0347  0.0146  0.0417  323 LYS C NZ  
9242  N N   . GLY C 324 ? 0.4728 0.4039 0.5702 0.0491  -0.0353 0.1451  324 GLY C N   
9243  C CA  . GLY C 324 ? 0.4681 0.4097 0.5988 0.0562  -0.0381 0.1574  324 GLY C CA  
9244  C C   . GLY C 324 ? 0.4865 0.4321 0.6256 0.0592  -0.0340 0.1428  324 GLY C C   
9245  O O   . GLY C 324 ? 0.4443 0.3936 0.6173 0.0667  -0.0308 0.1494  324 GLY C O   
9246  N N   . ILE C 325 ? 0.4459 0.3913 0.5568 0.0535  -0.0337 0.1245  325 ILE C N   
9247  C CA  . ILE C 325 ? 0.4573 0.4066 0.5724 0.0552  -0.0301 0.1102  325 ILE C CA  
9248  C C   . ILE C 325 ? 0.4788 0.4457 0.5799 0.0498  -0.0433 0.1156  325 ILE C C   
9249  O O   . ILE C 325 ? 0.4924 0.4615 0.5621 0.0413  -0.0490 0.1134  325 ILE C O   
9250  C CB  . ILE C 325 ? 0.4784 0.4168 0.5734 0.0522  -0.0204 0.0877  325 ILE C CB  
9251  C CG1 . ILE C 325 ? 0.5120 0.4342 0.6199 0.0550  -0.0069 0.0813  325 ILE C CG1 
9252  C CG2 . ILE C 325 ? 0.4182 0.3620 0.5135 0.0525  -0.0182 0.0740  325 ILE C CG2 
9253  C CD1 . ILE C 325 ? 0.4975 0.4119 0.5820 0.0495  0.0001  0.0628  325 ILE C CD1 
9254  N N   . GLU C 326 ? 0.4697 0.4487 0.5944 0.0538  -0.0470 0.1225  326 GLU C N   
9255  C CA  . GLU C 326 ? 0.5561 0.5529 0.6686 0.0475  -0.0591 0.1271  326 GLU C CA  
9256  C C   . GLU C 326 ? 0.4989 0.4938 0.5929 0.0448  -0.0544 0.1060  326 GLU C C   
9257  O O   . GLU C 326 ? 0.4498 0.4340 0.5513 0.0496  -0.0430 0.0909  326 GLU C O   
9258  C CB  . GLU C 326 ? 0.5956 0.6090 0.7427 0.0525  -0.0657 0.1441  326 GLU C CB  
9259  C CG  . GLU C 326 ? 0.6955 0.7196 0.8582 0.0524  -0.0760 0.1711  326 GLU C CG  
9260  C CD  . GLU C 326 ? 0.7749 0.8045 0.9873 0.0639  -0.0729 0.1861  326 GLU C CD  
9261  O OE1 . GLU C 326 ? 0.7745 0.7941 1.0067 0.0715  -0.0595 0.1721  326 GLU C OE1 
9262  O OE2 . GLU C 326 ? 0.7870 0.8304 1.0193 0.0647  -0.0828 0.2121  326 GLU C OE2 
9263  N N   . ILE C 327 ? 0.4721 0.4769 0.5400 0.0355  -0.0626 0.1049  327 ILE C N   
9264  C CA  . ILE C 327 ? 0.4395 0.4441 0.4909 0.0325  -0.0588 0.0875  327 ILE C CA  
9265  C C   . ILE C 327 ? 0.4755 0.4989 0.5273 0.0269  -0.0694 0.0954  327 ILE C C   
9266  O O   . ILE C 327 ? 0.4865 0.5168 0.5124 0.0157  -0.0763 0.0983  327 ILE C O   
9267  C CB  . ILE C 327 ? 0.4364 0.4311 0.4534 0.0256  -0.0545 0.0756  327 ILE C CB  
9268  C CG1 . ILE C 327 ? 0.4997 0.4795 0.5168 0.0293  -0.0470 0.0728  327 ILE C CG1 
9269  C CG2 . ILE C 327 ? 0.4129 0.4052 0.4197 0.0253  -0.0478 0.0580  327 ILE C CG2 
9270  C CD1 . ILE C 327 ? 0.5008 0.4707 0.4899 0.0243  -0.0407 0.0606  327 ILE C CD1 
9271  N N   . ASN C 328 ? 0.4314 0.4635 0.5131 0.0335  -0.0701 0.0995  328 ASN C N   
9272  C CA  . ASN C 328 ? 0.4653 0.5185 0.5524 0.0281  -0.0816 0.1107  328 ASN C CA  
9273  C C   . ASN C 328 ? 0.4305 0.4888 0.5232 0.0292  -0.0784 0.0989  328 ASN C C   
9274  O O   . ASN C 328 ? 0.4404 0.5178 0.5421 0.0252  -0.0878 0.1087  328 ASN C O   
9275  C CB  . ASN C 328 ? 0.4927 0.5594 0.6159 0.0335  -0.0893 0.1343  328 ASN C CB  
9276  C CG  . ASN C 328 ? 0.6143 0.6824 0.7303 0.0293  -0.0968 0.1513  328 ASN C CG  
9277  O OD1 . ASN C 328 ? 0.6783 0.7387 0.8170 0.0379  -0.0928 0.1605  328 ASN C OD1 
9278  N ND2 . ASN C 328 ? 0.6341 0.7112 0.7170 0.0149  -0.1066 0.1552  328 ASN C ND2 
9279  N N   . ASP C 329 ? 0.3808 0.4244 0.4706 0.0342  -0.0661 0.0797  329 ASP C N   
9280  C CA  . ASP C 329 ? 0.3756 0.4239 0.4681 0.0342  -0.0631 0.0684  329 ASP C CA  
9281  C C   . ASP C 329 ? 0.3538 0.3860 0.4249 0.0341  -0.0520 0.0479  329 ASP C C   
9282  O O   . ASP C 329 ? 0.3164 0.3352 0.3772 0.0354  -0.0464 0.0435  329 ASP C O   
9283  C CB  . ASP C 329 ? 0.3993 0.4526 0.5319 0.0434  -0.0598 0.0721  329 ASP C CB  
9284  C CG  . ASP C 329 ? 0.4223 0.4593 0.5756 0.0527  -0.0479 0.0684  329 ASP C CG  
9285  O OD1 . ASP C 329 ? 0.4070 0.4284 0.5438 0.0526  -0.0382 0.0521  329 ASP C OD1 
9286  O OD2 . ASP C 329 ? 0.5335 0.5739 0.7223 0.0598  -0.0468 0.0809  329 ASP C OD2 
9287  N N   . ARG C 330 ? 0.2913 0.3263 0.3560 0.0319  -0.0492 0.0366  330 ARG C N   
9288  C CA  . ARG C 330 ? 0.3410 0.3636 0.3851 0.0310  -0.0398 0.0196  330 ARG C CA  
9289  C C   . ARG C 330 ? 0.3062 0.3156 0.3611 0.0378  -0.0299 0.0116  330 ARG C C   
9290  O O   . ARG C 330 ? 0.2903 0.2896 0.3284 0.0366  -0.0248 0.0049  330 ARG C O   
9291  C CB  . ARG C 330 ? 0.2876 0.3163 0.3284 0.0283  -0.0384 0.0107  330 ARG C CB  
9292  C CG  . ARG C 330 ? 0.3133 0.3309 0.3367 0.0279  -0.0289 -0.0046 330 ARG C CG  
9293  C CD  . ARG C 330 ? 0.3660 0.3883 0.3909 0.0266  -0.0262 -0.0131 330 ARG C CD  
9294  N NE  . ARG C 330 ? 0.3327 0.3656 0.3459 0.0188  -0.0325 -0.0097 330 ARG C NE  
9295  C CZ  . ARG C 330 ? 0.3726 0.4089 0.3797 0.0151  -0.0299 -0.0177 330 ARG C CZ  
9296  N NH1 . ARG C 330 ? 0.3303 0.3600 0.3407 0.0190  -0.0215 -0.0289 330 ARG C NH1 
9297  N NH2 . ARG C 330 ? 0.3635 0.4107 0.3607 0.0062  -0.0357 -0.0142 330 ARG C NH2 
9298  N N   . ASP C 331 ? 0.3257 0.3355 0.4092 0.0437  -0.0261 0.0121  331 ASP C N   
9299  C CA  . ASP C 331 ? 0.2813 0.2781 0.3726 0.0471  -0.0147 0.0019  331 ASP C CA  
9300  C C   . ASP C 331 ? 0.3243 0.3119 0.4121 0.0478  -0.0131 0.0061  331 ASP C C   
9301  O O   . ASP C 331 ? 0.3225 0.3008 0.3968 0.0458  -0.0068 -0.0032 331 ASP C O   
9302  C CB  . ASP C 331 ? 0.3492 0.3468 0.4736 0.0522  -0.0087 0.0017  331 ASP C CB  
9303  C CG  . ASP C 331 ? 0.3936 0.3950 0.5181 0.0507  -0.0053 -0.0092 331 ASP C CG  
9304  O OD1 . ASP C 331 ? 0.3738 0.3809 0.4764 0.0463  -0.0104 -0.0122 331 ASP C OD1 
9305  O OD2 . ASP C 331 ? 0.4979 0.4970 0.6464 0.0537  0.0029  -0.0135 331 ASP C OD2 
9306  N N   . THR C 332 ? 0.3022 0.2938 0.4013 0.0499  -0.0197 0.0214  332 THR C N   
9307  C CA  . THR C 332 ? 0.3075 0.2903 0.4026 0.0503  -0.0185 0.0262  332 THR C CA  
9308  C C   . THR C 332 ? 0.3057 0.2853 0.3681 0.0446  -0.0207 0.0221  332 THR C C   
9309  O O   . THR C 332 ? 0.3416 0.3114 0.3957 0.0439  -0.0149 0.0167  332 THR C O   
9310  C CB  . THR C 332 ? 0.3483 0.3380 0.4608 0.0530  -0.0264 0.0455  332 THR C CB  
9311  O OG1 . THR C 332 ? 0.3515 0.3452 0.4997 0.0594  -0.0233 0.0513  332 THR C OG1 
9312  C CG2 . THR C 332 ? 0.3872 0.3659 0.4973 0.0538  -0.0235 0.0498  332 THR C CG2 
9313  N N   . ALA C 333 ? 0.2852 0.2732 0.3296 0.0396  -0.0281 0.0247  333 ALA C N   
9314  C CA  . ALA C 333 ? 0.3621 0.3460 0.3779 0.0340  -0.0278 0.0208  333 ALA C CA  
9315  C C   . ALA C 333 ? 0.3095 0.2867 0.3160 0.0342  -0.0191 0.0068  333 ALA C C   
9316  O O   . ALA C 333 ? 0.2921 0.2628 0.2861 0.0327  -0.0154 0.0042  333 ALA C O   
9317  C CB  . ALA C 333 ? 0.3051 0.2981 0.3044 0.0270  -0.0345 0.0241  333 ALA C CB  
9318  N N   . VAL C 334 ? 0.3037 0.2837 0.3172 0.0355  -0.0158 -0.0014 334 VAL C N   
9319  C CA  . VAL C 334 ? 0.3147 0.2905 0.3189 0.0346  -0.0087 -0.0128 334 VAL C CA  
9320  C C   . VAL C 334 ? 0.3110 0.2797 0.3208 0.0354  -0.0031 -0.0159 334 VAL C C   
9321  O O   . VAL C 334 ? 0.3002 0.2662 0.2975 0.0331  -0.0002 -0.0187 334 VAL C O   
9322  C CB  . VAL C 334 ? 0.3128 0.2928 0.3237 0.0351  -0.0063 -0.0204 334 VAL C CB  
9323  C CG1 . VAL C 334 ? 0.3095 0.2859 0.3154 0.0336  0.0009  -0.0304 334 VAL C CG1 
9324  C CG2 . VAL C 334 ? 0.2922 0.2788 0.2909 0.0320  -0.0106 -0.0192 334 VAL C CG2 
9325  N N   . ARG C 335 ? 0.3251 0.2909 0.3550 0.0382  -0.0007 -0.0148 335 ARG C N   
9326  C CA  . ARG C 335 ? 0.3476 0.3055 0.3821 0.0369  0.0064  -0.0194 335 ARG C CA  
9327  C C   . ARG C 335 ? 0.3257 0.2798 0.3505 0.0360  0.0044  -0.0132 335 ARG C C   
9328  O O   . ARG C 335 ? 0.3053 0.2566 0.3214 0.0324  0.0085  -0.0180 335 ARG C O   
9329  C CB  . ARG C 335 ? 0.3417 0.2949 0.4017 0.0398  0.0121  -0.0198 335 ARG C CB  
9330  C CG  . ARG C 335 ? 0.3390 0.2835 0.4020 0.0354  0.0230  -0.0300 335 ARG C CG  
9331  C CD  . ARG C 335 ? 0.3466 0.2832 0.4360 0.0372  0.0330  -0.0326 335 ARG C CD  
9332  N NE  . ARG C 335 ? 0.3425 0.2704 0.4298 0.0294  0.0449  -0.0451 335 ARG C NE  
9333  C CZ  . ARG C 335 ? 0.3430 0.2718 0.4216 0.0221  0.0505  -0.0577 335 ARG C CZ  
9334  N NH1 . ARG C 335 ? 0.3506 0.2876 0.4231 0.0230  0.0458  -0.0596 335 ARG C NH1 
9335  N NH2 . ARG C 335 ? 0.3453 0.2668 0.4202 0.0124  0.0614  -0.0686 335 ARG C NH2 
9336  N N   . LEU C 336 ? 0.2988 0.2540 0.3244 0.0381  -0.0022 -0.0019 336 LEU C N   
9337  C CA  . LEU C 336 ? 0.3287 0.2795 0.3442 0.0366  -0.0036 0.0039  336 LEU C CA  
9338  C C   . LEU C 336 ? 0.3176 0.2698 0.3113 0.0329  -0.0034 0.0006  336 LEU C C   
9339  O O   . LEU C 336 ? 0.3490 0.2973 0.3359 0.0309  -0.0006 0.0004  336 LEU C O   
9340  C CB  . LEU C 336 ? 0.3229 0.2757 0.3415 0.0379  -0.0111 0.0175  336 LEU C CB  
9341  C CG  . LEU C 336 ? 0.3575 0.3081 0.4010 0.0425  -0.0107 0.0256  336 LEU C CG  
9342  C CD1 . LEU C 336 ? 0.4259 0.3830 0.4694 0.0421  -0.0210 0.0418  336 LEU C CD1 
9343  C CD2 . LEU C 336 ? 0.4012 0.3407 0.4497 0.0427  -0.0032 0.0235  336 LEU C CD2 
9344  N N   . TYR C 337 ? 0.2923 0.2499 0.2769 0.0318  -0.0054 -0.0015 337 TYR C N   
9345  C CA  . TYR C 337 ? 0.3125 0.2707 0.2800 0.0289  -0.0030 -0.0041 337 TYR C CA  
9346  C C   . TYR C 337 ? 0.2786 0.2375 0.2465 0.0283  0.0026  -0.0107 337 TYR C C   
9347  O O   . TYR C 337 ? 0.2982 0.2565 0.2588 0.0267  0.0053  -0.0094 337 TYR C O   
9348  C CB  . TYR C 337 ? 0.3193 0.2821 0.2797 0.0276  -0.0047 -0.0055 337 TYR C CB  
9349  C CG  . TYR C 337 ? 0.3102 0.2714 0.2544 0.0245  -0.0004 -0.0069 337 TYR C CG  
9350  C CD1 . TYR C 337 ? 0.3179 0.2740 0.2521 0.0219  0.0019  -0.0030 337 TYR C CD1 
9351  C CD2 . TYR C 337 ? 0.3078 0.2718 0.2483 0.0240  0.0028  -0.0122 337 TYR C CD2 
9352  C CE1 . TYR C 337 ? 0.3442 0.2973 0.2661 0.0190  0.0088  -0.0046 337 TYR C CE1 
9353  C CE2 . TYR C 337 ? 0.3195 0.2805 0.2482 0.0216  0.0092  -0.0132 337 TYR C CE2 
9354  C CZ  . TYR C 337 ? 0.3210 0.2765 0.2418 0.0193  0.0128  -0.0095 337 TYR C CZ  
9355  O OH  . TYR C 337 ? 0.3437 0.2949 0.2558 0.0170  0.0220  -0.0109 337 TYR C OH  
9356  N N   . ALA C 338 ? 0.2948 0.2562 0.2716 0.0287  0.0044  -0.0171 338 ALA C N   
9357  C CA  . ALA C 338 ? 0.3071 0.2710 0.2839 0.0255  0.0088  -0.0228 338 ALA C CA  
9358  C C   . ALA C 338 ? 0.3249 0.2856 0.3036 0.0230  0.0108  -0.0216 338 ALA C C   
9359  O O   . ALA C 338 ? 0.3308 0.2954 0.3034 0.0198  0.0122  -0.0208 338 ALA C O   
9360  C CB  . ALA C 338 ? 0.3076 0.2725 0.2934 0.0243  0.0114  -0.0306 338 ALA C CB  
9361  N N   . ASP C 339 ? 0.3158 0.2698 0.3044 0.0244  0.0111  -0.0204 339 ASP C N   
9362  C CA  . ASP C 339 ? 0.3160 0.2654 0.3065 0.0215  0.0142  -0.0198 339 ASP C CA  
9363  C C   . ASP C 339 ? 0.3192 0.2687 0.2994 0.0215  0.0120  -0.0131 339 ASP C C   
9364  O O   . ASP C 339 ? 0.3251 0.2761 0.3024 0.0174  0.0145  -0.0138 339 ASP C O   
9365  C CB  . ASP C 339 ? 0.2931 0.2338 0.2984 0.0242  0.0162  -0.0181 339 ASP C CB  
9366  C CG  . ASP C 339 ? 0.3721 0.3062 0.3789 0.0216  0.0198  -0.0167 339 ASP C CG  
9367  O OD1 . ASP C 339 ? 0.3640 0.2961 0.3734 0.0157  0.0267  -0.0245 339 ASP C OD1 
9368  O OD2 . ASP C 339 ? 0.3898 0.3210 0.3929 0.0240  0.0163  -0.0083 339 ASP C OD2 
9369  N N   . TRP C 340 ? 0.2990 0.2471 0.2736 0.0248  0.0079  -0.0066 340 TRP C N   
9370  C CA  . TRP C 340 ? 0.2937 0.2401 0.2581 0.0238  0.0078  -0.0011 340 TRP C CA  
9371  C C   . TRP C 340 ? 0.3146 0.2673 0.2733 0.0218  0.0110  -0.0028 340 TRP C C   
9372  O O   . TRP C 340 ? 0.2992 0.2529 0.2570 0.0196  0.0134  -0.0008 340 TRP C O   
9373  C CB  . TRP C 340 ? 0.3435 0.2880 0.3002 0.0248  0.0040  0.0042  340 TRP C CB  
9374  C CG  . TRP C 340 ? 0.3358 0.2756 0.2816 0.0224  0.0049  0.0094  340 TRP C CG  
9375  C CD1 . TRP C 340 ? 0.3164 0.2560 0.2515 0.0203  0.0093  0.0094  340 TRP C CD1 
9376  C CD2 . TRP C 340 ? 0.3442 0.2779 0.2888 0.0215  0.0025  0.0160  340 TRP C CD2 
9377  N NE1 . TRP C 340 ? 0.3114 0.2445 0.2377 0.0173  0.0102  0.0142  340 TRP C NE1 
9378  C CE2 . TRP C 340 ? 0.3296 0.2595 0.2607 0.0178  0.0053  0.0186  340 TRP C CE2 
9379  C CE3 . TRP C 340 ? 0.3410 0.2716 0.2966 0.0234  -0.0007 0.0205  340 TRP C CE3 
9380  C CZ2 . TRP C 340 ? 0.3509 0.2744 0.2757 0.0149  0.0040  0.0251  340 TRP C CZ2 
9381  C CZ3 . TRP C 340 ? 0.3598 0.2845 0.3111 0.0216  -0.0024 0.0285  340 TRP C CZ3 
9382  C CH2 . TRP C 340 ? 0.3564 0.2778 0.2907 0.0168  -0.0005 0.0305  340 TRP C CH2 
9383  N N   . ASN C 341 ? 0.3058 0.2641 0.2631 0.0226  0.0113  -0.0056 341 ASN C N   
9384  C CA  . ASN C 341 ? 0.3011 0.2666 0.2565 0.0215  0.0146  -0.0045 341 ASN C CA  
9385  C C   . ASN C 341 ? 0.3268 0.3003 0.2875 0.0174  0.0151  -0.0062 341 ASN C C   
9386  O O   . ASN C 341 ? 0.3017 0.2820 0.2633 0.0156  0.0169  -0.0016 341 ASN C O   
9387  C CB  . ASN C 341 ? 0.3305 0.2992 0.2835 0.0233  0.0154  -0.0064 341 ASN C CB  
9388  C CG  . ASN C 341 ? 0.3275 0.2901 0.2722 0.0245  0.0179  -0.0037 341 ASN C CG  
9389  O OD1 . ASN C 341 ? 0.3397 0.3021 0.2826 0.0244  0.0235  -0.0001 341 ASN C OD1 
9390  N ND2 . ASN C 341 ? 0.3432 0.3012 0.2837 0.0244  0.0145  -0.0050 341 ASN C ND2 
9391  N N   . LEU C 342 ? 0.2762 0.2492 0.2410 0.0146  0.0144  -0.0124 342 LEU C N   
9392  C CA  . LEU C 342 ? 0.3226 0.3037 0.2893 0.0072  0.0156  -0.0153 342 LEU C CA  
9393  C C   . LEU C 342 ? 0.3254 0.3059 0.2928 0.0036  0.0168  -0.0126 342 LEU C C   
9394  O O   . LEU C 342 ? 0.3015 0.2921 0.2689 -0.0039 0.0173  -0.0127 342 LEU C O   
9395  C CB  . LEU C 342 ? 0.2814 0.2593 0.2515 0.0034  0.0174  -0.0246 342 LEU C CB  
9396  C CG  . LEU C 342 ? 0.3079 0.2908 0.2767 0.0041  0.0168  -0.0279 342 LEU C CG  
9397  C CD1 . LEU C 342 ? 0.3271 0.3041 0.3012 0.0016  0.0201  -0.0374 342 LEU C CD1 
9398  C CD2 . LEU C 342 ? 0.2993 0.2970 0.2637 -0.0019 0.0159  -0.0249 342 LEU C CD2 
9399  N N   . SER C 343 ? 0.3064 0.2763 0.2737 0.0078  0.0170  -0.0098 343 SER C N   
9400  C CA  . SER C 343 ? 0.3062 0.2743 0.2738 0.0046  0.0186  -0.0071 343 SER C CA  
9401  C C   . SER C 343 ? 0.2857 0.2609 0.2517 0.0053  0.0190  0.0005  343 SER C C   
9402  O O   . SER C 343 ? 0.3275 0.3018 0.2942 0.0029  0.0206  0.0032  343 SER C O   
9403  C CB  . SER C 343 ? 0.3510 0.3049 0.3198 0.0082  0.0190  -0.0060 343 SER C CB  
9404  O OG  . SER C 343 ? 0.3240 0.2732 0.2875 0.0133  0.0171  0.0000  343 SER C OG  
9405  N N   . LYS C 344 ? 0.2967 0.2564 0.2855 -0.0105 -0.0054 0.0003  344 LYS C N   
9406  C CA  . LYS C 344 ? 0.3389 0.2981 0.3231 -0.0127 -0.0048 -0.0007 344 LYS C CA  
9407  C C   . LYS C 344 ? 0.2979 0.2560 0.2835 -0.0141 -0.0019 -0.0030 344 LYS C C   
9408  O O   . LYS C 344 ? 0.3159 0.2768 0.3048 -0.0144 -0.0013 -0.0056 344 LYS C O   
9409  C CB  . LYS C 344 ? 0.3417 0.3046 0.3250 -0.0135 -0.0063 -0.0022 344 LYS C CB  
9410  C CG  . LYS C 344 ? 0.3751 0.3394 0.3557 -0.0136 -0.0092 -0.0004 344 LYS C CG  
9411  C CD  . LYS C 344 ? 0.3922 0.3592 0.3721 -0.0152 -0.0106 -0.0019 344 LYS C CD  
9412  C CE  . LYS C 344 ? 0.3683 0.3323 0.3443 -0.0165 -0.0088 -0.0037 344 LYS C CE  
9413  N NZ  . LYS C 344 ? 0.3581 0.3200 0.3276 -0.0181 -0.0096 -0.0036 344 LYS C NZ  
9414  N N   . PRO C 345 ? 0.2894 0.2445 0.2724 -0.0152 -0.0001 -0.0022 345 PRO C N   
9415  C CA  . PRO C 345 ? 0.3283 0.2843 0.3136 -0.0172 0.0025  -0.0045 345 PRO C CA  
9416  C C   . PRO C 345 ? 0.3124 0.2742 0.2990 -0.0177 0.0022  -0.0067 345 PRO C C   
9417  O O   . PRO C 345 ? 0.2907 0.2559 0.2805 -0.0190 0.0030  -0.0089 345 PRO C O   
9418  C CB  . PRO C 345 ? 0.3112 0.2639 0.2933 -0.0185 0.0045  -0.0027 345 PRO C CB  
9419  C CG  . PRO C 345 ? 0.3347 0.2831 0.3133 -0.0170 0.0033  0.0010  345 PRO C CG  
9420  C CD  . PRO C 345 ? 0.3271 0.2787 0.3053 -0.0152 -0.0002 0.0010  345 PRO C CD  
9421  N N   . GLN C 346 ? 0.2984 0.2613 0.2823 -0.0167 0.0010  -0.0060 346 GLN C N   
9422  C CA  . GLN C 346 ? 0.3289 0.2963 0.3143 -0.0164 0.0012  -0.0070 346 GLN C CA  
9423  C C   . GLN C 346 ? 0.3366 0.3072 0.3244 -0.0159 -0.0004 -0.0077 346 GLN C C   
9424  O O   . GLN C 346 ? 0.3118 0.2859 0.3005 -0.0153 -0.0004 -0.0076 346 GLN C O   
9425  C CB  . GLN C 346 ? 0.3253 0.2907 0.3069 -0.0156 0.0017  -0.0063 346 GLN C CB  
9426  C CG  . GLN C 346 ? 0.3357 0.3013 0.3165 -0.0160 0.0045  -0.0062 346 GLN C CG  
9427  C CD  . GLN C 346 ? 0.3927 0.3644 0.3784 -0.0155 0.0058  -0.0066 346 GLN C CD  
9428  O OE1 . GLN C 346 ? 0.4293 0.4056 0.4185 -0.0153 0.0044  -0.0069 346 GLN C OE1 
9429  N NE2 . GLN C 346 ? 0.3997 0.3730 0.3858 -0.0153 0.0084  -0.0065 346 GLN C NE2 
9430  N N   . TRP C 347 ? 0.3033 0.2733 0.2924 -0.0158 -0.0013 -0.0081 347 TRP C N   
9431  C CA  . TRP C 347 ? 0.2895 0.2637 0.2811 -0.0157 -0.0020 -0.0092 347 TRP C CA  
9432  C C   . TRP C 347 ? 0.2661 0.2430 0.2601 -0.0171 -0.0007 -0.0117 347 TRP C C   
9433  O O   . TRP C 347 ? 0.3084 0.2899 0.3035 -0.0176 -0.0010 -0.0130 347 TRP C O   
9434  C CB  . TRP C 347 ? 0.2915 0.2647 0.2838 -0.0148 -0.0033 -0.0086 347 TRP C CB  
9435  C CG  . TRP C 347 ? 0.2776 0.2502 0.2677 -0.0146 -0.0049 -0.0071 347 TRP C CG  
9436  C CD1 . TRP C 347 ? 0.3131 0.2842 0.3003 -0.0150 -0.0047 -0.0066 347 TRP C CD1 
9437  C CD2 . TRP C 347 ? 0.2674 0.2408 0.2582 -0.0143 -0.0067 -0.0062 347 TRP C CD2 
9438  N NE1 . TRP C 347 ? 0.3121 0.2820 0.2976 -0.0156 -0.0061 -0.0060 347 TRP C NE1 
9439  C CE2 . TRP C 347 ? 0.2924 0.2646 0.2801 -0.0155 -0.0077 -0.0056 347 TRP C CE2 
9440  C CE3 . TRP C 347 ? 0.2851 0.2607 0.2795 -0.0132 -0.0073 -0.0059 347 TRP C CE3 
9441  C CZ2 . TRP C 347 ? 0.2897 0.2634 0.2774 -0.0165 -0.0097 -0.0050 347 TRP C CZ2 
9442  C CZ3 . TRP C 347 ? 0.2707 0.2491 0.2661 -0.0134 -0.0095 -0.0046 347 TRP C CZ3 
9443  C CH2 . TRP C 347 ? 0.2930 0.2707 0.2847 -0.0156 -0.0109 -0.0043 347 TRP C CH2 
9444  N N   . GLN C 348 ? 0.3000 0.2740 0.2943 -0.0184 0.0008  -0.0127 348 GLN C N   
9445  C CA  . GLN C 348 ? 0.2684 0.2434 0.2648 -0.0204 0.0023  -0.0160 348 GLN C CA  
9446  C C   . GLN C 348 ? 0.2774 0.2603 0.2744 -0.0227 0.0021  -0.0178 348 GLN C C   
9447  O O   . GLN C 348 ? 0.3135 0.2999 0.3111 -0.0246 0.0026  -0.0210 348 GLN C O   
9448  C CB  . GLN C 348 ? 0.2549 0.2231 0.2515 -0.0216 0.0044  -0.0163 348 GLN C CB  
9449  C CG  . GLN C 348 ? 0.2703 0.2318 0.2661 -0.0187 0.0040  -0.0132 348 GLN C CG  
9450  C CD  . GLN C 348 ? 0.3297 0.2915 0.3276 -0.0163 0.0034  -0.0135 348 GLN C CD  
9451  O OE1 . GLN C 348 ? 0.3388 0.3001 0.3391 -0.0168 0.0052  -0.0167 348 GLN C OE1 
9452  N NE2 . GLN C 348 ? 0.3351 0.2977 0.3322 -0.0140 0.0011  -0.0104 348 GLN C NE2 
9453  N N   . HIS C 349 ? 0.2788 0.2653 0.2757 -0.0226 0.0016  -0.0158 349 HIS C N   
9454  C CA  . HIS C 349 ? 0.3011 0.2968 0.2996 -0.0245 0.0011  -0.0168 349 HIS C CA  
9455  C C   . HIS C 349 ? 0.2773 0.2791 0.2752 -0.0233 -0.0006 -0.0157 349 HIS C C   
9456  O O   . HIS C 349 ? 0.3096 0.3205 0.3083 -0.0248 -0.0015 -0.0162 349 HIS C O   
9457  C CB  . HIS C 349 ? 0.2934 0.2918 0.2932 -0.0238 0.0014  -0.0144 349 HIS C CB  
9458  C CG  . HIS C 349 ? 0.2933 0.2908 0.2921 -0.0201 0.0006  -0.0110 349 HIS C CG  
9459  N ND1 . HIS C 349 ? 0.3029 0.2922 0.2989 -0.0182 0.0009  -0.0098 349 HIS C ND1 
9460  C CD2 . HIS C 349 ? 0.3160 0.3192 0.3159 -0.0179 -0.0003 -0.0085 349 HIS C CD2 
9461  C CE1 . HIS C 349 ? 0.3463 0.3355 0.3417 -0.0158 0.0005  -0.0076 349 HIS C CE1 
9462  N NE2 . HIS C 349 ? 0.3252 0.3220 0.3231 -0.0152 0.0000  -0.0065 349 HIS C NE2 
9463  N N   . PHE C 350 ? 0.2851 0.2828 0.2816 -0.0209 -0.0012 -0.0141 350 PHE C N   
9464  C CA  . PHE C 350 ? 0.2799 0.2830 0.2757 -0.0204 -0.0023 -0.0131 350 PHE C CA  
9465  C C   . PHE C 350 ? 0.2866 0.2939 0.2818 -0.0230 -0.0018 -0.0168 350 PHE C C   
9466  O O   . PHE C 350 ? 0.3164 0.3306 0.3103 -0.0235 -0.0026 -0.0162 350 PHE C O   
9467  C CB  . PHE C 350 ? 0.2853 0.2836 0.2802 -0.0183 -0.0026 -0.0111 350 PHE C CB  
9468  C CG  . PHE C 350 ? 0.3077 0.3026 0.3020 -0.0162 -0.0029 -0.0079 350 PHE C CG  
9469  C CD1 . PHE C 350 ? 0.2681 0.2660 0.2624 -0.0149 -0.0034 -0.0047 350 PHE C CD1 
9470  C CD2 . PHE C 350 ? 0.2936 0.2818 0.2871 -0.0156 -0.0025 -0.0079 350 PHE C CD2 
9471  C CE1 . PHE C 350 ? 0.2906 0.2835 0.2844 -0.0129 -0.0028 -0.0023 350 PHE C CE1 
9472  C CE2 . PHE C 350 ? 0.2711 0.2556 0.2633 -0.0142 -0.0023 -0.0059 350 PHE C CE2 
9473  C CZ  . PHE C 350 ? 0.2864 0.2725 0.2789 -0.0128 -0.0022 -0.0034 350 PHE C CZ  
9474  N N   . TYR C 351 ? 0.2951 0.2980 0.2908 -0.0247 -0.0001 -0.0207 351 TYR C N   
9475  C CA  . TYR C 351 ? 0.3406 0.3458 0.3356 -0.0274 0.0013  -0.0255 351 TYR C CA  
9476  C C   . TYR C 351 ? 0.3454 0.3535 0.3405 -0.0317 0.0020  -0.0293 351 TYR C C   
9477  O O   . TYR C 351 ? 0.3291 0.3437 0.3224 -0.0350 0.0022  -0.0330 351 TYR C O   
9478  C CB  . TYR C 351 ? 0.3453 0.3421 0.3414 -0.0261 0.0035  -0.0276 351 TYR C CB  
9479  C CG  . TYR C 351 ? 0.3164 0.3106 0.3133 -0.0225 0.0026  -0.0239 351 TYR C CG  
9480  C CD1 . TYR C 351 ? 0.3164 0.3159 0.3125 -0.0218 0.0020  -0.0228 351 TYR C CD1 
9481  C CD2 . TYR C 351 ? 0.3122 0.2995 0.3103 -0.0202 0.0022  -0.0213 351 TYR C CD2 
9482  C CE1 . TYR C 351 ? 0.3252 0.3230 0.3224 -0.0194 0.0011  -0.0196 351 TYR C CE1 
9483  C CE2 . TYR C 351 ? 0.3191 0.3053 0.3179 -0.0177 0.0010  -0.0183 351 TYR C CE2 
9484  C CZ  . TYR C 351 ? 0.3382 0.3297 0.3369 -0.0175 0.0004  -0.0176 351 TYR C CZ  
9485  O OH  . TYR C 351 ? 0.3470 0.3380 0.3467 -0.0160 -0.0007 -0.0150 351 TYR C OH  
9486  N N   . ASP C 352 ? 0.3283 0.3319 0.3252 -0.0322 0.0027  -0.0289 352 ASP C N   
9487  C CA  . ASP C 352 ? 0.3229 0.3280 0.3206 -0.0371 0.0039  -0.0329 352 ASP C CA  
9488  C C   . ASP C 352 ? 0.3277 0.3338 0.3277 -0.0372 0.0034  -0.0298 352 ASP C C   
9489  O O   . ASP C 352 ? 0.3305 0.3277 0.3310 -0.0355 0.0048  -0.0280 352 ASP C O   
9490  C CB  . ASP C 352 ? 0.3523 0.3465 0.3502 -0.0385 0.0073  -0.0371 352 ASP C CB  
9491  C CG  . ASP C 352 ? 0.4013 0.3952 0.3998 -0.0444 0.0093  -0.0420 352 ASP C CG  
9492  O OD1 . ASP C 352 ? 0.3638 0.3670 0.3631 -0.0478 0.0077  -0.0421 352 ASP C OD1 
9493  O OD2 . ASP C 352 ? 0.4147 0.3989 0.4132 -0.0458 0.0127  -0.0460 352 ASP C OD2 
9494  N N   . PRO C 353 ? 0.3511 0.3687 0.3526 -0.0391 0.0017  -0.0291 353 PRO C N   
9495  C CA  . PRO C 353 ? 0.3742 0.3938 0.3788 -0.0386 0.0018  -0.0260 353 PRO C CA  
9496  C C   . PRO C 353 ? 0.3448 0.3579 0.3507 -0.0424 0.0046  -0.0287 353 PRO C C   
9497  O O   . PRO C 353 ? 0.3269 0.3369 0.3341 -0.0411 0.0057  -0.0258 353 PRO C O   
9498  C CB  . PRO C 353 ? 0.3511 0.3865 0.3581 -0.0404 -0.0006 -0.0252 353 PRO C CB  
9499  C CG  . PRO C 353 ? 0.4275 0.4679 0.4319 -0.0453 -0.0012 -0.0307 353 PRO C CG  
9500  C CD  . PRO C 353 ? 0.3848 0.4148 0.3855 -0.0426 -0.0001 -0.0316 353 PRO C CD  
9501  N N   . THR C 354 ? 0.3085 0.3190 0.3136 -0.0473 0.0062  -0.0341 354 THR C N   
9502  C CA  . THR C 354 ? 0.3439 0.3467 0.3504 -0.0515 0.0094  -0.0364 354 THR C CA  
9503  C C   . THR C 354 ? 0.3801 0.3686 0.3853 -0.0476 0.0115  -0.0333 354 THR C C   
9504  O O   . THR C 354 ? 0.3317 0.3144 0.3380 -0.0495 0.0139  -0.0324 354 THR C O   
9505  C CB  . THR C 354 ? 0.3905 0.3911 0.3962 -0.0577 0.0114  -0.0435 354 THR C CB  
9506  O OG1 . THR C 354 ? 0.3807 0.3710 0.3838 -0.0551 0.0130  -0.0454 354 THR C OG1 
9507  C CG2 . THR C 354 ? 0.3782 0.3943 0.3839 -0.0620 0.0088  -0.0468 354 THR C CG2 
9508  N N   . ILE C 355 ? 0.3480 0.3313 0.3511 -0.0425 0.0106  -0.0315 355 ILE C N   
9509  C CA  . ILE C 355 ? 0.3515 0.3237 0.3535 -0.0388 0.0118  -0.0277 355 ILE C CA  
9510  C C   . ILE C 355 ? 0.3172 0.2917 0.3190 -0.0373 0.0112  -0.0232 355 ILE C C   
9511  O O   . ILE C 355 ? 0.3381 0.3055 0.3391 -0.0374 0.0132  -0.0209 355 ILE C O   
9512  C CB  . ILE C 355 ? 0.3459 0.3148 0.3464 -0.0339 0.0105  -0.0264 355 ILE C CB  
9513  C CG1 . ILE C 355 ? 0.3689 0.3353 0.3699 -0.0353 0.0122  -0.0313 355 ILE C CG1 
9514  C CG2 . ILE C 355 ? 0.3434 0.3034 0.3429 -0.0303 0.0109  -0.0220 355 ILE C CG2 
9515  C CD1 . ILE C 355 ? 0.3473 0.3123 0.3479 -0.0305 0.0112  -0.0301 355 ILE C CD1 
9516  N N   . LYS C 356 ? 0.3177 0.3016 0.3200 -0.0356 0.0090  -0.0217 356 LYS C N   
9517  C CA  . LYS C 356 ? 0.3169 0.3031 0.3194 -0.0339 0.0092  -0.0182 356 LYS C CA  
9518  C C   . LYS C 356 ? 0.3614 0.3521 0.3670 -0.0383 0.0113  -0.0191 356 LYS C C   
9519  O O   . LYS C 356 ? 0.3660 0.3543 0.3712 -0.0380 0.0132  -0.0167 356 LYS C O   
9520  C CB  . LYS C 356 ? 0.3076 0.3017 0.3105 -0.0304 0.0068  -0.0163 356 LYS C CB  
9521  C CG  . LYS C 356 ? 0.3064 0.3019 0.3097 -0.0284 0.0079  -0.0134 356 LYS C CG  
9522  C CD  . LYS C 356 ? 0.3504 0.3501 0.3538 -0.0242 0.0062  -0.0112 356 LYS C CD  
9523  C CE  . LYS C 356 ? 0.4037 0.4051 0.4081 -0.0218 0.0080  -0.0090 356 LYS C CE  
9524  N NZ  . LYS C 356 ? 0.3826 0.3942 0.3916 -0.0195 0.0074  -0.0073 356 LYS C NZ  
9525  N N   . SER C 357 ? 0.3351 0.3336 0.3438 -0.0427 0.0110  -0.0227 357 SER C N   
9526  C CA  . SER C 357 ? 0.3299 0.3334 0.3423 -0.0479 0.0130  -0.0239 357 SER C CA  
9527  C C   . SER C 357 ? 0.3676 0.3585 0.3783 -0.0503 0.0166  -0.0237 357 SER C C   
9528  O O   . SER C 357 ? 0.3136 0.3045 0.3255 -0.0516 0.0189  -0.0216 357 SER C O   
9529  C CB  . SER C 357 ? 0.3122 0.3250 0.3273 -0.0537 0.0120  -0.0287 357 SER C CB  
9530  O OG  . SER C 357 ? 0.3539 0.3807 0.3709 -0.0520 0.0085  -0.0279 357 SER C OG  
9531  N N   . ASP C 358 ? 0.3447 0.3246 0.3529 -0.0505 0.0173  -0.0256 358 ASP C N   
9532  C CA  . ASP C 358 ? 0.3662 0.3328 0.3730 -0.0521 0.0209  -0.0245 358 ASP C CA  
9533  C C   . ASP C 358 ? 0.3890 0.3504 0.3925 -0.0475 0.0212  -0.0186 358 ASP C C   
9534  O O   . ASP C 358 ? 0.3294 0.2859 0.3321 -0.0494 0.0242  -0.0161 358 ASP C O   
9535  C CB  . ASP C 358 ? 0.3662 0.3223 0.3716 -0.0516 0.0218  -0.0271 358 ASP C CB  
9536  C CG  . ASP C 358 ? 0.4266 0.3850 0.4341 -0.0577 0.0229  -0.0339 358 ASP C CG  
9537  O OD1 . ASP C 358 ? 0.4202 0.3869 0.4304 -0.0637 0.0234  -0.0366 358 ASP C OD1 
9538  O OD2 . ASP C 358 ? 0.4469 0.3986 0.4533 -0.0566 0.0236  -0.0369 358 ASP C OD2 
9539  N N   . MET C 359 ? 0.3384 0.3009 0.3393 -0.0418 0.0183  -0.0164 359 MET C N   
9540  C CA  . MET C 359 ? 0.3365 0.2951 0.3334 -0.0382 0.0184  -0.0117 359 MET C CA  
9541  C C   . MET C 359 ? 0.3312 0.2963 0.3287 -0.0396 0.0201  -0.0103 359 MET C C   
9542  O O   . MET C 359 ? 0.3329 0.2932 0.3272 -0.0395 0.0223  -0.0071 359 MET C O   
9543  C CB  . MET C 359 ? 0.3489 0.3086 0.3431 -0.0329 0.0151  -0.0102 359 MET C CB  
9544  C CG  . MET C 359 ? 0.3799 0.3320 0.3722 -0.0301 0.0138  -0.0091 359 MET C CG  
9545  S SD  . MET C 359 ? 0.3661 0.3236 0.3583 -0.0262 0.0100  -0.0100 359 MET C SD  
9546  C CE  . MET C 359 ? 0.3791 0.3292 0.3712 -0.0237 0.0093  -0.0092 359 MET C CE  
9547  N N   . MET C 360 ? 0.3511 0.3278 0.3529 -0.0402 0.0192  -0.0122 360 MET C N   
9548  C CA  . MET C 360 ? 0.3413 0.3257 0.3454 -0.0410 0.0213  -0.0110 360 MET C CA  
9549  C C   . MET C 360 ? 0.3379 0.3213 0.3441 -0.0467 0.0250  -0.0112 360 MET C C   
9550  O O   . MET C 360 ? 0.3442 0.3263 0.3485 -0.0468 0.0280  -0.0086 360 MET C O   
9551  C CB  . MET C 360 ? 0.3137 0.3117 0.3231 -0.0397 0.0194  -0.0122 360 MET C CB  
9552  C CG  . MET C 360 ? 0.3522 0.3496 0.3593 -0.0345 0.0163  -0.0115 360 MET C CG  
9553  S SD  . MET C 360 ? 0.3729 0.3852 0.3860 -0.0324 0.0140  -0.0115 360 MET C SD  
9554  C CE  . MET C 360 ? 0.3952 0.4134 0.4113 -0.0290 0.0169  -0.0088 360 MET C CE  
9555  N N   . LEU C 361 ? 0.3128 0.2954 0.3219 -0.0518 0.0254  -0.0144 361 LEU C N   
9556  C CA  . LEU C 361 ? 0.3460 0.3266 0.3575 -0.0583 0.0293  -0.0151 361 LEU C CA  
9557  C C   . LEU C 361 ? 0.3803 0.3463 0.3861 -0.0577 0.0322  -0.0111 361 LEU C C   
9558  O O   . LEU C 361 ? 0.3542 0.3190 0.3601 -0.0612 0.0360  -0.0090 361 LEU C O   
9559  C CB  . LEU C 361 ? 0.3564 0.3371 0.3712 -0.0643 0.0291  -0.0203 361 LEU C CB  
9560  C CG  . LEU C 361 ? 0.3769 0.3741 0.3972 -0.0665 0.0262  -0.0241 361 LEU C CG  
9561  C CD1 . LEU C 361 ? 0.3731 0.3694 0.3943 -0.0720 0.0255  -0.0301 361 LEU C CD1 
9562  C CD2 . LEU C 361 ? 0.3995 0.4096 0.4258 -0.0704 0.0279  -0.0236 361 LEU C CD2 
9563  N N   . ARG C 362 ? 0.3219 0.2778 0.3230 -0.0533 0.0303  -0.0096 362 ARG C N   
9564  C CA  . ARG C 362 ? 0.3577 0.3014 0.3533 -0.0516 0.0322  -0.0047 362 ARG C CA  
9565  C C   . ARG C 362 ? 0.3648 0.3114 0.3558 -0.0488 0.0327  -0.0006 362 ARG C C   
9566  O O   . ARG C 362 ? 0.3655 0.3070 0.3530 -0.0505 0.0358  0.0032  362 ARG C O   
9567  C CB  . ARG C 362 ? 0.3820 0.3173 0.3750 -0.0470 0.0295  -0.0040 362 ARG C CB  
9568  C CG  . ARG C 362 ? 0.3649 0.2878 0.3534 -0.0453 0.0311  0.0016  362 ARG C CG  
9569  C CD  . ARG C 362 ? 0.3549 0.2732 0.3417 -0.0396 0.0280  0.0030  362 ARG C CD  
9570  N NE  . ARG C 362 ? 0.3539 0.2609 0.3376 -0.0374 0.0292  0.0089  362 ARG C NE  
9571  C CZ  . ARG C 362 ? 0.3727 0.2745 0.3566 -0.0326 0.0272  0.0108  362 ARG C CZ  
9572  N NH1 . ARG C 362 ? 0.3650 0.2713 0.3518 -0.0301 0.0244  0.0068  362 ARG C NH1 
9573  N NH2 . ARG C 362 ? 0.3936 0.2858 0.3753 -0.0302 0.0284  0.0172  362 ARG C NH2 
9574  N N   . ILE C 363 ? 0.3339 0.2886 0.3245 -0.0450 0.0301  -0.0016 363 ILE C N   
9575  C CA  . ILE C 363 ? 0.3197 0.2765 0.3055 -0.0428 0.0314  0.0012  363 ILE C CA  
9576  C C   . ILE C 363 ? 0.3498 0.3128 0.3387 -0.0470 0.0359  0.0013  363 ILE C C   
9577  O O   . ILE C 363 ? 0.3595 0.3198 0.3436 -0.0477 0.0391  0.0046  363 ILE C O   
9578  C CB  . ILE C 363 ? 0.3182 0.2811 0.3035 -0.0381 0.0284  -0.0003 363 ILE C CB  
9579  C CG1 . ILE C 363 ? 0.2978 0.2543 0.2788 -0.0343 0.0244  0.0004  363 ILE C CG1 
9580  C CG2 . ILE C 363 ? 0.3657 0.3314 0.3469 -0.0367 0.0310  0.0011  363 ILE C CG2 
9581  C CD1 . ILE C 363 ? 0.3434 0.3057 0.3256 -0.0305 0.0213  -0.0018 363 ILE C CD1 
9582  N N   . ILE C 364 ? 0.3698 0.3426 0.3669 -0.0501 0.0362  -0.0021 364 ILE C N   
9583  C CA  . ILE C 364 ? 0.3722 0.3530 0.3740 -0.0545 0.0404  -0.0021 364 ILE C CA  
9584  C C   . ILE C 364 ? 0.3826 0.3540 0.3815 -0.0595 0.0445  0.0007  364 ILE C C   
9585  O O   . ILE C 364 ? 0.3711 0.3444 0.3686 -0.0613 0.0488  0.0032  364 ILE C O   
9586  C CB  . ILE C 364 ? 0.3415 0.3347 0.3529 -0.0578 0.0392  -0.0061 364 ILE C CB  
9587  C CG1 . ILE C 364 ? 0.3519 0.3554 0.3661 -0.0520 0.0360  -0.0071 364 ILE C CG1 
9588  C CG2 . ILE C 364 ? 0.3978 0.3991 0.4152 -0.0640 0.0437  -0.0062 364 ILE C CG2 
9589  C CD1 . ILE C 364 ? 0.3403 0.3551 0.3622 -0.0541 0.0330  -0.0104 364 ILE C CD1 
9590  N N   . LYS C 365 ? 0.3715 0.3323 0.3694 -0.0614 0.0437  0.0005  365 LYS C N   
9591  C CA  . LYS C 365 ? 0.3721 0.3220 0.3678 -0.0661 0.0478  0.0036  365 LYS C CA  
9592  C C   . LYS C 365 ? 0.3876 0.3292 0.3739 -0.0626 0.0489  0.0098  365 LYS C C   
9593  O O   . LYS C 365 ? 0.4153 0.3565 0.3990 -0.0655 0.0533  0.0132  365 LYS C O   
9594  C CB  . LYS C 365 ? 0.3740 0.3134 0.3712 -0.0678 0.0468  0.0015  365 LYS C CB  
9595  C CG  . LYS C 365 ? 0.4494 0.3768 0.4462 -0.0735 0.0517  0.0040  365 LYS C CG  
9596  C CD  . LYS C 365 ? 0.5211 0.4367 0.5195 -0.0744 0.0514  0.0015  365 LYS C CD  
9597  C CE  . LYS C 365 ? 0.6040 0.5060 0.5963 -0.0681 0.0504  0.0070  365 LYS C CE  
9598  N NZ  . LYS C 365 ? 0.6647 0.5510 0.6565 -0.0718 0.0555  0.0105  365 LYS C NZ  
9599  N N   . GLU C 366 ? 0.3553 0.2913 0.3363 -0.0567 0.0450  0.0114  366 GLU C N   
9600  C CA  . GLU C 366 ? 0.3750 0.3031 0.3468 -0.0539 0.0454  0.0177  366 GLU C CA  
9601  C C   . GLU C 366 ? 0.4033 0.3387 0.3697 -0.0526 0.0467  0.0188  366 GLU C C   
9602  O O   . GLU C 366 ? 0.3973 0.3286 0.3560 -0.0531 0.0491  0.0240  366 GLU C O   
9603  C CB  . GLU C 366 ? 0.3643 0.2864 0.3331 -0.0483 0.0404  0.0187  366 GLU C CB  
9604  C CG  . GLU C 366 ? 0.3795 0.2927 0.3535 -0.0491 0.0401  0.0176  366 GLU C CG  
9605  C CD  . GLU C 366 ? 0.3787 0.2855 0.3501 -0.0433 0.0361  0.0202  366 GLU C CD  
9606  O OE1 . GLU C 366 ? 0.4022 0.3107 0.3673 -0.0391 0.0333  0.0237  366 GLU C OE1 
9607  O OE2 . GLU C 366 ? 0.4049 0.3059 0.3811 -0.0429 0.0358  0.0180  366 GLU C OE2 
9608  N N   . TRP C 367 ? 0.3356 0.2815 0.3053 -0.0504 0.0452  0.0143  367 TRP C N   
9609  C CA  . TRP C 367 ? 0.3609 0.3132 0.3260 -0.0488 0.0472  0.0144  367 TRP C CA  
9610  C C   . TRP C 367 ? 0.3660 0.3268 0.3362 -0.0530 0.0528  0.0135  367 TRP C C   
9611  O O   . TRP C 367 ? 0.3548 0.3215 0.3223 -0.0516 0.0556  0.0130  367 TRP C O   
9612  C CB  . TRP C 367 ? 0.3613 0.3191 0.3271 -0.0438 0.0436  0.0106  367 TRP C CB  
9613  C CG  . TRP C 367 ? 0.3373 0.2884 0.2946 -0.0401 0.0396  0.0124  367 TRP C CG  
9614  C CD1 . TRP C 367 ? 0.3661 0.3166 0.3140 -0.0381 0.0399  0.0133  367 TRP C CD1 
9615  C CD2 . TRP C 367 ? 0.3264 0.2716 0.2840 -0.0381 0.0349  0.0130  367 TRP C CD2 
9616  N NE1 . TRP C 367 ? 0.3422 0.2878 0.2849 -0.0355 0.0349  0.0147  367 TRP C NE1 
9617  C CE2 . TRP C 367 ? 0.3694 0.3119 0.3185 -0.0351 0.0320  0.0148  367 TRP C CE2 
9618  C CE3 . TRP C 367 ? 0.3319 0.2746 0.2965 -0.0388 0.0329  0.0118  367 TRP C CE3 
9619  C CZ2 . TRP C 367 ? 0.3744 0.3125 0.3226 -0.0324 0.0271  0.0161  367 TRP C CZ2 
9620  C CZ3 . TRP C 367 ? 0.3530 0.2906 0.3164 -0.0357 0.0287  0.0127  367 TRP C CZ3 
9621  C CH2 . TRP C 367 ? 0.3214 0.2571 0.2772 -0.0325 0.0258  0.0152  367 TRP C CH2 
9622  N N   . GLN C 368 ? 0.3637 0.3249 0.3410 -0.0583 0.0549  0.0131  368 GLN C N   
9623  C CA  . GLN C 368 ? 0.3953 0.3648 0.3780 -0.0635 0.0604  0.0129  368 GLN C CA  
9624  C C   . GLN C 368 ? 0.3971 0.3816 0.3868 -0.0610 0.0608  0.0090  368 GLN C C   
9625  O O   . GLN C 368 ? 0.3933 0.3844 0.3821 -0.0608 0.0653  0.0096  368 GLN C O   
9626  C CB  . GLN C 368 ? 0.4451 0.4099 0.4193 -0.0655 0.0655  0.0180  368 GLN C CB  
9627  C CG  . GLN C 368 ? 0.4755 0.4254 0.4416 -0.0661 0.0648  0.0234  368 GLN C CG  
9628  C CD  . GLN C 368 ? 0.5167 0.4631 0.4752 -0.0696 0.0706  0.0293  368 GLN C CD  
9629  O OE1 . GLN C 368 ? 0.5350 0.4839 0.4981 -0.0756 0.0758  0.0301  368 GLN C OE1 
9630  N NE2 . GLN C 368 ? 0.5601 0.5020 0.5067 -0.0660 0.0697  0.0333  368 GLN C NE2 
9631  N N   . VAL C 369 ? 0.3546 0.3444 0.3511 -0.0590 0.0564  0.0053  369 VAL C N   
9632  C CA  . VAL C 369 ? 0.3696 0.3726 0.3729 -0.0553 0.0557  0.0025  369 VAL C CA  
9633  C C   . VAL C 369 ? 0.3802 0.3973 0.3953 -0.0602 0.0581  0.0009  369 VAL C C   
9634  O O   . VAL C 369 ? 0.3546 0.3718 0.3744 -0.0658 0.0569  -0.0004 369 VAL C O   
9635  C CB  . VAL C 369 ? 0.3681 0.3704 0.3724 -0.0507 0.0495  0.0002  369 VAL C CB  
9636  C CG1 . VAL C 369 ? 0.3494 0.3660 0.3623 -0.0470 0.0490  -0.0018 369 VAL C CG1 
9637  C CG2 . VAL C 369 ? 0.3995 0.3900 0.3929 -0.0459 0.0471  0.0016  369 VAL C CG2 
9638  N N   . ASP C 370 ? 0.3554 0.3848 0.3757 -0.0580 0.0615  0.0007  370 ASP C N   
9639  C CA  . ASP C 370 ? 0.4095 0.4559 0.4424 -0.0617 0.0639  -0.0004 370 ASP C CA  
9640  C C   . ASP C 370 ? 0.3957 0.4555 0.4384 -0.0580 0.0595  -0.0025 370 ASP C C   
9641  O O   . ASP C 370 ? 0.3612 0.4353 0.4147 -0.0623 0.0591  -0.0037 370 ASP C O   
9642  C CB  . ASP C 370 ? 0.3854 0.4388 0.4192 -0.0607 0.0708  0.0011  370 ASP C CB  
9643  C CG  . ASP C 370 ? 0.4539 0.4951 0.4770 -0.0645 0.0755  0.0040  370 ASP C CG  
9644  O OD1 . ASP C 370 ? 0.4988 0.5338 0.5212 -0.0715 0.0757  0.0051  370 ASP C OD1 
9645  O OD2 . ASP C 370 ? 0.4196 0.4564 0.4343 -0.0605 0.0787  0.0051  370 ASP C OD2 
9646  N N   . GLY C 371 ? 0.3560 0.4124 0.3953 -0.0504 0.0563  -0.0028 371 GLY C N   
9647  C CA  . GLY C 371 ? 0.3610 0.4296 0.4091 -0.0464 0.0523  -0.0036 371 GLY C CA  
9648  C C   . GLY C 371 ? 0.3445 0.4037 0.3860 -0.0396 0.0483  -0.0037 371 GLY C C   
9649  O O   . GLY C 371 ? 0.3301 0.3760 0.3615 -0.0369 0.0495  -0.0033 371 GLY C O   
9650  N N   . VAL C 372 ? 0.3288 0.3951 0.3757 -0.0375 0.0433  -0.0042 372 VAL C N   
9651  C CA  . VAL C 372 ? 0.3397 0.3973 0.3809 -0.0321 0.0393  -0.0042 372 VAL C CA  
9652  C C   . VAL C 372 ? 0.3507 0.4193 0.3995 -0.0253 0.0386  -0.0027 372 VAL C C   
9653  O O   . VAL C 372 ? 0.3497 0.4348 0.4090 -0.0260 0.0376  -0.0019 372 VAL C O   
9654  C CB  . VAL C 372 ? 0.3812 0.4346 0.4200 -0.0361 0.0341  -0.0059 372 VAL C CB  
9655  C CG1 . VAL C 372 ? 0.3839 0.4293 0.4173 -0.0308 0.0301  -0.0057 372 VAL C CG1 
9656  C CG2 . VAL C 372 ? 0.3709 0.4128 0.4035 -0.0423 0.0354  -0.0069 372 VAL C CG2 
9657  N N   . MET C 373 ? 0.3388 0.3984 0.3824 -0.0188 0.0390  -0.0021 373 MET C N   
9658  C CA  . MET C 373 ? 0.3736 0.4397 0.4233 -0.0114 0.0386  -0.0001 373 MET C CA  
9659  C C   . MET C 373 ? 0.3650 0.4220 0.4088 -0.0096 0.0335  -0.0001 373 MET C C   
9660  O O   . MET C 373 ? 0.3908 0.4330 0.4248 -0.0093 0.0336  -0.0014 373 MET C O   
9661  C CB  . MET C 373 ? 0.3416 0.4022 0.3893 -0.0059 0.0446  -0.0002 373 MET C CB  
9662  C CG  . MET C 373 ? 0.3959 0.4621 0.4461 -0.0083 0.0506  -0.0007 373 MET C CG  
9663  S SD  . MET C 373 ? 0.4611 0.5260 0.5128 -0.0003 0.0584  -0.0009 373 MET C SD  
9664  C CE  . MET C 373 ? 0.5158 0.5582 0.5499 -0.0011 0.0584  -0.0038 373 MET C CE  
9665  N N   . LEU C 374 ? 0.3274 0.3941 0.3769 -0.0090 0.0289  0.0015  374 LEU C N   
9666  C CA  . LEU C 374 ? 0.3515 0.4114 0.3960 -0.0080 0.0243  0.0017  374 LEU C CA  
9667  C C   . LEU C 374 ? 0.3387 0.4002 0.3866 -0.0003 0.0243  0.0050  374 LEU C C   
9668  O O   . LEU C 374 ? 0.3225 0.3984 0.3800 0.0028  0.0239  0.0081  374 LEU C O   
9669  C CB  . LEU C 374 ? 0.3482 0.4176 0.3954 -0.0130 0.0194  0.0011  374 LEU C CB  
9670  C CG  . LEU C 374 ? 0.4187 0.4843 0.4622 -0.0210 0.0192  -0.0025 374 LEU C CG  
9671  C CD1 . LEU C 374 ? 0.3868 0.4620 0.4329 -0.0256 0.0145  -0.0038 374 LEU C CD1 
9672  C CD2 . LEU C 374 ? 0.3966 0.4441 0.4298 -0.0217 0.0197  -0.0042 374 LEU C CD2 
9673  N N   . HIS C 375 ? 0.3342 0.3814 0.3748 0.0026  0.0247  0.0046  375 HIS C N   
9674  C CA  . HIS C 375 ? 0.3540 0.3992 0.3967 0.0094  0.0248  0.0078  375 HIS C CA  
9675  C C   . HIS C 375 ? 0.3351 0.3845 0.3779 0.0086  0.0192  0.0098  375 HIS C C   
9676  O O   . HIS C 375 ? 0.3619 0.4033 0.3974 0.0047  0.0165  0.0076  375 HIS C O   
9677  C CB  . HIS C 375 ? 0.3488 0.3765 0.3828 0.0112  0.0277  0.0056  375 HIS C CB  
9678  C CG  . HIS C 375 ? 0.3557 0.3777 0.3908 0.0173  0.0287  0.0082  375 HIS C CG  
9679  N ND1 . HIS C 375 ? 0.3680 0.3747 0.3948 0.0173  0.0291  0.0063  375 HIS C ND1 
9680  C CD2 . HIS C 375 ? 0.3436 0.3731 0.3872 0.0235  0.0294  0.0128  375 HIS C CD2 
9681  C CE1 . HIS C 375 ? 0.3824 0.3859 0.4123 0.0230  0.0305  0.0094  375 HIS C CE1 
9682  N NE2 . HIS C 375 ? 0.3544 0.3713 0.3946 0.0273  0.0308  0.0138  375 HIS C NE2 
9683  N N   . LEU C 376 ? 0.2995 0.3623 0.3505 0.0122  0.0174  0.0144  376 LEU C N   
9684  C CA  . LEU C 376 ? 0.2943 0.3616 0.3449 0.0122  0.0125  0.0172  376 LEU C CA  
9685  C C   . LEU C 376 ? 0.3467 0.4022 0.3948 0.0183  0.0141  0.0201  376 LEU C C   
9686  O O   . LEU C 376 ? 0.3314 0.3904 0.3861 0.0250  0.0163  0.0246  376 LEU C O   
9687  C CB  . LEU C 376 ? 0.3060 0.3942 0.3659 0.0131  0.0094  0.0213  376 LEU C CB  
9688  C CG  . LEU C 376 ? 0.3363 0.4367 0.4002 0.0068  0.0090  0.0180  376 LEU C CG  
9689  C CD1 . LEU C 376 ? 0.3496 0.4732 0.4237 0.0071  0.0058  0.0219  376 LEU C CD1 
9690  C CD2 . LEU C 376 ? 0.3351 0.4289 0.3909 -0.0017 0.0069  0.0123  376 LEU C CD2 
9691  N N   . ASN C 377 ? 0.2877 0.3287 0.3267 0.0158  0.0136  0.0173  377 ASN C N   
9692  C CA  . ASN C 377 ? 0.2980 0.3241 0.3333 0.0198  0.0165  0.0180  377 ASN C CA  
9693  C C   . ASN C 377 ? 0.2926 0.3190 0.3277 0.0219  0.0136  0.0227  377 ASN C C   
9694  O O   . ASN C 377 ? 0.2913 0.3145 0.3206 0.0178  0.0104  0.0214  377 ASN C O   
9695  C CB  . ASN C 377 ? 0.3484 0.3600 0.3744 0.0156  0.0176  0.0125  377 ASN C CB  
9696  C CG  . ASN C 377 ? 0.3197 0.3161 0.3411 0.0181  0.0203  0.0121  377 ASN C CG  
9697  O OD1 . ASN C 377 ? 0.3206 0.3148 0.3459 0.0237  0.0227  0.0158  377 ASN C OD1 
9698  N ND2 . ASN C 377 ? 0.3506 0.3363 0.3637 0.0139  0.0202  0.0077  377 ASN C ND2 
9699  N N   . ARG C 378 ? 0.3068 0.3376 0.3486 0.0285  0.0150  0.0286  378 ARG C N   
9700  C CA  . ARG C 378 ? 0.2961 0.3278 0.3381 0.0311  0.0126  0.0344  378 ARG C CA  
9701  C C   . ARG C 378 ? 0.3112 0.3244 0.3461 0.0307  0.0145  0.0333  378 ARG C C   
9702  O O   . ARG C 378 ? 0.3247 0.3369 0.3583 0.0315  0.0128  0.0377  378 ARG C O   
9703  C CB  . ARG C 378 ? 0.3355 0.3753 0.3870 0.0393  0.0141  0.0421  378 ARG C CB  
9704  C CG  . ARG C 378 ? 0.3593 0.4199 0.4195 0.0401  0.0120  0.0442  378 ARG C CG  
9705  C CD  . ARG C 378 ? 0.4116 0.4802 0.4820 0.0493  0.0136  0.0528  378 ARG C CD  
9706  N NE  . ARG C 378 ? 0.4066 0.4991 0.4856 0.0493  0.0099  0.0559  378 ARG C NE  
9707  C CZ  . ARG C 378 ? 0.4462 0.5541 0.5257 0.0473  0.0039  0.0602  378 ARG C CZ  
9708  N NH1 . ARG C 378 ? 0.4276 0.5300 0.4996 0.0455  0.0011  0.0622  378 ARG C NH1 
9709  N NH2 . ARG C 378 ? 0.4171 0.5475 0.5048 0.0467  0.0007  0.0623  378 ARG C NH2 
9710  N N   . GLY C 379 ? 0.3347 0.3342 0.3650 0.0292  0.0181  0.0277  379 GLY C N   
9711  C CA  . GLY C 379 ? 0.3063 0.2896 0.3304 0.0281  0.0198  0.0263  379 GLY C CA  
9712  C C   . GLY C 379 ? 0.3272 0.3065 0.3437 0.0212  0.0166  0.0221  379 GLY C C   
9713  O O   . GLY C 379 ? 0.3345 0.3016 0.3461 0.0196  0.0177  0.0207  379 GLY C O   
9714  N N   . CYS C 380 ? 0.3095 0.2992 0.3253 0.0171  0.0128  0.0201  380 CYS C N   
9715  C CA  . CYS C 380 ? 0.2943 0.2802 0.3037 0.0111  0.0103  0.0157  380 CYS C CA  
9716  C C   . CYS C 380 ? 0.2993 0.2978 0.3096 0.0082  0.0061  0.0162  380 CYS C C   
9717  O O   . CYS C 380 ? 0.3038 0.3090 0.3154 0.0061  0.0053  0.0136  380 CYS C O   
9718  C CB  . CYS C 380 ? 0.3629 0.3433 0.3689 0.0087  0.0120  0.0103  380 CYS C CB  
9719  S SG  . CYS C 380 ? 0.3287 0.3058 0.3282 0.0023  0.0090  0.0057  380 CYS C SG  
9720  N N   . GLU C 381 ? 0.3049 0.3056 0.3138 0.0073  0.0039  0.0188  381 GLU C N   
9721  C CA  . GLU C 381 ? 0.3174 0.3295 0.3260 0.0039  0.0004  0.0181  381 GLU C CA  
9722  C C   . GLU C 381 ? 0.3227 0.3315 0.3276 -0.0009 -0.0003 0.0120  381 GLU C C   
9723  O O   . GLU C 381 ? 0.2833 0.2998 0.2890 -0.0037 -0.0018 0.0096  381 GLU C O   
9724  C CB  . GLU C 381 ? 0.3186 0.3332 0.3253 0.0038  -0.0013 0.0220  381 GLU C CB  
9725  C CG  . GLU C 381 ? 0.3404 0.3433 0.3427 0.0020  -0.0003 0.0209  381 GLU C CG  
9726  C CD  . GLU C 381 ? 0.3389 0.3462 0.3384 -0.0004 -0.0020 0.0227  381 GLU C CD  
9727  O OE1 . GLU C 381 ? 0.3259 0.3449 0.3252 -0.0019 -0.0043 0.0228  381 GLU C OE1 
9728  O OE2 . GLU C 381 ? 0.3469 0.3460 0.3444 -0.0009 -0.0007 0.0241  381 GLU C OE2 
9729  N N   . GLY C 382 ? 0.3169 0.3146 0.3182 -0.0021 0.0008  0.0096  382 GLY C N   
9730  C CA  . GLY C 382 ? 0.3018 0.2974 0.3002 -0.0059 -0.0003 0.0052  382 GLY C CA  
9731  C C   . GLY C 382 ? 0.3005 0.2971 0.2996 -0.0072 0.0003  0.0022  382 GLY C C   
9732  O O   . GLY C 382 ? 0.3188 0.3182 0.3175 -0.0100 -0.0008 -0.0005 382 GLY C O   
9733  N N   . LEU C 383 ? 0.3167 0.3104 0.3167 -0.0051 0.0025  0.0025  383 LEU C N   
9734  C CA  . LEU C 383 ? 0.3116 0.3062 0.3121 -0.0066 0.0035  0.0001  383 LEU C CA  
9735  C C   . LEU C 383 ? 0.3201 0.3258 0.3258 -0.0064 0.0035  0.0012  383 LEU C C   
9736  O O   . LEU C 383 ? 0.3223 0.3303 0.3290 -0.0088 0.0042  -0.0009 383 LEU C O   
9737  C CB  . LEU C 383 ? 0.3113 0.2977 0.3093 -0.0053 0.0064  -0.0007 383 LEU C CB  
9738  C CG  . LEU C 383 ? 0.3254 0.3021 0.3175 -0.0068 0.0059  -0.0024 383 LEU C CG  
9739  C CD1 . LEU C 383 ? 0.3473 0.3172 0.3356 -0.0065 0.0086  -0.0040 383 LEU C CD1 
9740  C CD2 . LEU C 383 ? 0.3276 0.3049 0.3182 -0.0099 0.0035  -0.0039 383 LEU C CD2 
9741  N N   . SER C 384 ? 0.2818 0.2951 0.2911 -0.0040 0.0025  0.0046  384 SER C N   
9742  C CA  . SER C 384 ? 0.3082 0.3349 0.3233 -0.0039 0.0018  0.0061  384 SER C CA  
9743  C C   . SER C 384 ? 0.3115 0.3476 0.3264 -0.0079 -0.0014 0.0048  384 SER C C   
9744  O O   . SER C 384 ? 0.3133 0.3612 0.3325 -0.0094 -0.0023 0.0049  384 SER C O   
9745  C CB  . SER C 384 ? 0.3269 0.3586 0.3467 0.0016  0.0024  0.0115  384 SER C CB  
9746  O OG  . SER C 384 ? 0.3208 0.3454 0.3418 0.0052  0.0063  0.0117  384 SER C OG  
9747  N N   . VAL C 385 ? 0.3105 0.3427 0.3209 -0.0098 -0.0028 0.0034  385 VAL C N   
9748  C CA  . VAL C 385 ? 0.2898 0.3307 0.2993 -0.0139 -0.0051 0.0013  385 VAL C CA  
9749  C C   . VAL C 385 ? 0.3110 0.3529 0.3214 -0.0184 -0.0044 -0.0035 385 VAL C C   
9750  O O   . VAL C 385 ? 0.3271 0.3590 0.3360 -0.0191 -0.0024 -0.0058 385 VAL C O   
9751  C CB  . VAL C 385 ? 0.3221 0.3581 0.3267 -0.0153 -0.0059 -0.0001 385 VAL C CB  
9752  C CG1 . VAL C 385 ? 0.3448 0.3835 0.3488 -0.0121 -0.0069 0.0051  385 VAL C CG1 
9753  C CG2 . VAL C 385 ? 0.3324 0.3553 0.3343 -0.0151 -0.0042 -0.0023 385 VAL C CG2 
9754  N N   . GLY C 386 ? 0.3238 0.3778 0.3364 -0.0219 -0.0060 -0.0049 386 GLY C N   
9755  C CA  . GLY C 386 ? 0.3172 0.3716 0.3307 -0.0271 -0.0049 -0.0097 386 GLY C CA  
9756  C C   . GLY C 386 ? 0.3612 0.4200 0.3802 -0.0269 -0.0035 -0.0086 386 GLY C C   
9757  O O   . GLY C 386 ? 0.3444 0.4052 0.3650 -0.0319 -0.0025 -0.0121 386 GLY C O   
9758  N N   . ILE C 387 ? 0.3047 0.3650 0.3269 -0.0215 -0.0028 -0.0038 387 ILE C N   
9759  C CA  . ILE C 387 ? 0.3283 0.3900 0.3551 -0.0207 -0.0002 -0.0032 387 ILE C CA  
9760  C C   . ILE C 387 ? 0.3083 0.3855 0.3412 -0.0252 -0.0011 -0.0043 387 ILE C C   
9761  O O   . ILE C 387 ? 0.3898 0.4664 0.4249 -0.0284 0.0013  -0.0065 387 ILE C O   
9762  C CB  . ILE C 387 ? 0.3225 0.3827 0.3517 -0.0135 0.0013  0.0018  387 ILE C CB  
9763  C CG1 . ILE C 387 ? 0.3637 0.4225 0.3963 -0.0125 0.0051  0.0017  387 ILE C CG1 
9764  C CG2 . ILE C 387 ? 0.2840 0.3580 0.3184 -0.0100 -0.0012 0.0067  387 ILE C CG2 
9765  C CD1 . ILE C 387 ? 0.4078 0.4537 0.4349 -0.0156 0.0076  -0.0019 387 ILE C CD1 
9766  N N   . MET C 388 ? 0.3089 0.4006 0.3443 -0.0260 -0.0046 -0.0029 388 MET C N   
9767  C CA  . MET C 388 ? 0.3269 0.4355 0.3684 -0.0310 -0.0060 -0.0041 388 MET C CA  
9768  C C   . MET C 388 ? 0.3216 0.4273 0.3600 -0.0398 -0.0056 -0.0111 388 MET C C   
9769  O O   . MET C 388 ? 0.3567 0.4700 0.4000 -0.0449 -0.0046 -0.0134 388 MET C O   
9770  C CB  . MET C 388 ? 0.3699 0.4965 0.4145 -0.0296 -0.0104 -0.0002 388 MET C CB  
9771  C CG  . MET C 388 ? 0.3938 0.5268 0.4440 -0.0206 -0.0108 0.0079  388 MET C CG  
9772  S SD  . MET C 388 ? 0.4189 0.5535 0.4784 -0.0164 -0.0063 0.0102  388 MET C SD  
9773  C CE  . MET C 388 ? 0.3898 0.5451 0.4564 -0.0249 -0.0082 0.0070  388 MET C CE  
9774  N N   . GLU C 389 ? 0.3528 0.4470 0.3839 -0.0415 -0.0057 -0.0146 389 GLU C N   
9775  C CA  . GLU C 389 ? 0.3792 0.4672 0.4075 -0.0489 -0.0041 -0.0212 389 GLU C CA  
9776  C C   . GLU C 389 ? 0.3234 0.3985 0.3523 -0.0492 0.0001  -0.0219 389 GLU C C   
9777  O O   . GLU C 389 ? 0.3358 0.4098 0.3659 -0.0556 0.0020  -0.0258 389 GLU C O   
9778  C CB  . GLU C 389 ? 0.3265 0.4055 0.3476 -0.0498 -0.0046 -0.0245 389 GLU C CB  
9779  C CG  . GLU C 389 ? 0.3621 0.4545 0.3811 -0.0512 -0.0085 -0.0248 389 GLU C CG  
9780  C CD  . GLU C 389 ? 0.3566 0.4629 0.3771 -0.0598 -0.0100 -0.0298 389 GLU C CD  
9781  O OE1 . GLU C 389 ? 0.3253 0.4282 0.3476 -0.0658 -0.0076 -0.0346 389 GLU C OE1 
9782  O OE2 . GLU C 389 ? 0.3356 0.4567 0.3551 -0.0611 -0.0137 -0.0290 389 GLU C OE2 
9783  N N   . ASN C 390 ? 0.3574 0.4225 0.3847 -0.0428 0.0016  -0.0180 390 ASN C N   
9784  C CA  . ASN C 390 ? 0.3145 0.3695 0.3417 -0.0430 0.0055  -0.0179 390 ASN C CA  
9785  C C   . ASN C 390 ? 0.3176 0.3839 0.3518 -0.0451 0.0070  -0.0169 390 ASN C C   
9786  O O   . ASN C 390 ? 0.3240 0.3866 0.3591 -0.0499 0.0099  -0.0190 390 ASN C O   
9787  C CB  . ASN C 390 ? 0.3193 0.3638 0.3431 -0.0362 0.0065  -0.0143 390 ASN C CB  
9788  C CG  . ASN C 390 ? 0.3487 0.3830 0.3664 -0.0338 0.0050  -0.0148 390 ASN C CG  
9789  O OD1 . ASN C 390 ? 0.3307 0.3617 0.3466 -0.0286 0.0044  -0.0119 390 ASN C OD1 
9790  N ND2 . ASN C 390 ? 0.3474 0.3764 0.3623 -0.0378 0.0049  -0.0187 390 ASN C ND2 
9791  N N   . ARG C 391 ? 0.3171 0.3977 0.3571 -0.0413 0.0053  -0.0133 391 ARG C N   
9792  C CA  . ARG C 391 ? 0.3602 0.4548 0.4087 -0.0430 0.0066  -0.0120 391 ARG C CA  
9793  C C   . ARG C 391 ? 0.3482 0.4515 0.3995 -0.0523 0.0060  -0.0166 391 ARG C C   
9794  O O   . ARG C 391 ? 0.3335 0.4378 0.3883 -0.0569 0.0092  -0.0179 391 ARG C O   
9795  C CB  . ARG C 391 ? 0.3477 0.4576 0.4026 -0.0370 0.0043  -0.0071 391 ARG C CB  
9796  C CG  . ARG C 391 ? 0.3257 0.4494 0.3904 -0.0363 0.0065  -0.0047 391 ARG C CG  
9797  C CD  . ARG C 391 ? 0.3678 0.5134 0.4410 -0.0344 0.0028  -0.0011 391 ARG C CD  
9798  N NE  . ARG C 391 ? 0.4215 0.5798 0.4959 -0.0429 -0.0009 -0.0047 391 ARG C NE  
9799  C CZ  . ARG C 391 ? 0.4095 0.5798 0.4902 -0.0504 -0.0003 -0.0075 391 ARG C CZ  
9800  N NH1 . ARG C 391 ? 0.3835 0.5554 0.4703 -0.0502 0.0041  -0.0066 391 ARG C NH1 
9801  N NH2 . ARG C 391 ? 0.4141 0.5955 0.4947 -0.0586 -0.0040 -0.0114 391 ARG C NH2 
9802  N N   . LEU C 392 ? 0.3330 0.4426 0.3825 -0.0560 0.0022  -0.0193 392 LEU C N   
9803  C CA  . LEU C 392 ? 0.3437 0.4613 0.3949 -0.0659 0.0015  -0.0248 392 LEU C CA  
9804  C C   . LEU C 392 ? 0.3735 0.4744 0.4211 -0.0718 0.0058  -0.0294 392 LEU C C   
9805  O O   . LEU C 392 ? 0.3861 0.4920 0.4379 -0.0794 0.0077  -0.0324 392 LEU C O   
9806  C CB  . LEU C 392 ? 0.3482 0.4720 0.3953 -0.0682 -0.0028 -0.0275 392 LEU C CB  
9807  C CG  . LEU C 392 ? 0.4317 0.5717 0.4809 -0.0774 -0.0057 -0.0323 392 LEU C CG  
9808  C CD1 . LEU C 392 ? 0.4390 0.6024 0.4987 -0.0791 -0.0076 -0.0294 392 LEU C CD1 
9809  C CD2 . LEU C 392 ? 0.3996 0.5448 0.4429 -0.0763 -0.0100 -0.0328 392 LEU C CD2 
9810  N N   . ALA C 393 ? 0.3105 0.3919 0.3506 -0.0685 0.0075  -0.0298 393 ALA C N   
9811  C CA  . ALA C 393 ? 0.3451 0.4096 0.3817 -0.0728 0.0116  -0.0330 393 ALA C CA  
9812  C C   . ALA C 393 ? 0.3687 0.4302 0.4084 -0.0729 0.0156  -0.0300 393 ALA C C   
9813  O O   . ALA C 393 ? 0.3819 0.4381 0.4225 -0.0797 0.0190  -0.0325 393 ALA C O   
9814  C CB  . ALA C 393 ? 0.3513 0.3980 0.3803 -0.0678 0.0120  -0.0326 393 ALA C CB  
9815  N N   . ILE C 394 ? 0.3077 0.3719 0.3487 -0.0657 0.0158  -0.0248 394 ILE C N   
9816  C CA  . ILE C 394 ? 0.3355 0.3985 0.3792 -0.0659 0.0200  -0.0222 394 ILE C CA  
9817  C C   . ILE C 394 ? 0.3430 0.4237 0.3959 -0.0720 0.0208  -0.0232 394 ILE C C   
9818  O O   . ILE C 394 ? 0.3582 0.4365 0.4130 -0.0774 0.0249  -0.0238 394 ILE C O   
9819  C CB  . ILE C 394 ? 0.3155 0.3768 0.3578 -0.0568 0.0205  -0.0173 394 ILE C CB  
9820  C CG1 . ILE C 394 ? 0.3023 0.3462 0.3356 -0.0521 0.0199  -0.0166 394 ILE C CG1 
9821  C CG2 . ILE C 394 ? 0.3353 0.3966 0.3798 -0.0571 0.0253  -0.0151 394 ILE C CG2 
9822  C CD1 . ILE C 394 ? 0.3487 0.3919 0.3804 -0.0439 0.0196  -0.0129 394 ILE C CD1 
9823  N N   . ALA C 395 ? 0.3507 0.4503 0.4097 -0.0711 0.0169  -0.0227 395 ALA C N   
9824  C CA  . ALA C 395 ? 0.3732 0.4924 0.4421 -0.0771 0.0170  -0.0235 395 ALA C CA  
9825  C C   . ALA C 395 ? 0.3907 0.5075 0.4593 -0.0887 0.0182  -0.0295 395 ALA C C   
9826  O O   . ALA C 395 ? 0.4149 0.5362 0.4888 -0.0950 0.0216  -0.0303 395 ALA C O   
9827  C CB  . ALA C 395 ? 0.3305 0.4707 0.4054 -0.0743 0.0118  -0.0217 395 ALA C CB  
9828  N N   . LYS C 396 ? 0.3802 0.4888 0.4423 -0.0919 0.0160  -0.0341 396 LYS C N   
9829  C CA  . LYS C 396 ? 0.4069 0.5106 0.4679 -0.1029 0.0176  -0.0408 396 LYS C CA  
9830  C C   . LYS C 396 ? 0.4058 0.4916 0.4647 -0.1061 0.0238  -0.0407 396 LYS C C   
9831  O O   . LYS C 396 ? 0.3774 0.4632 0.4391 -0.1160 0.0266  -0.0447 396 LYS C O   
9832  C CB  . LYS C 396 ? 0.4301 0.5250 0.4834 -0.1035 0.0151  -0.0454 396 LYS C CB  
9833  C CG  . LYS C 396 ? 0.5333 0.6274 0.5854 -0.1152 0.0157  -0.0538 396 LYS C CG  
9834  C CD  . LYS C 396 ? 0.5549 0.6458 0.6000 -0.1143 0.0126  -0.0580 396 LYS C CD  
9835  C CE  . LYS C 396 ? 0.6101 0.7223 0.6571 -0.1100 0.0064  -0.0550 396 LYS C CE  
9836  N NZ  . LYS C 396 ? 0.6789 0.7923 0.7192 -0.1118 0.0034  -0.0600 396 LYS C NZ  
9837  N N   . SER C 397 ? 0.3989 0.5124 0.5528 -0.1985 -0.0132 -0.0363 397 SER C N   
9838  C CA  . SER C 397 ? 0.3711 0.4834 0.5343 -0.2037 -0.0033 -0.0294 397 SER C CA  
9839  C C   . SER C 397 ? 0.4114 0.5482 0.6012 -0.2068 0.0039  -0.0224 397 SER C C   
9840  O O   . SER C 397 ? 0.3999 0.5350 0.5990 -0.2096 0.0105  -0.0153 397 SER C O   
9841  C CB  . SER C 397 ? 0.4035 0.5001 0.5445 -0.1994 0.0051  -0.0261 397 SER C CB  
9842  O OG  . SER C 397 ? 0.3795 0.4856 0.5148 -0.1907 0.0122  -0.0223 397 SER C OG  
9843  N N   . GLY C 398 ? 0.3812 0.5364 0.5833 -0.2001 0.0026  -0.0226 398 GLY C N   
9844  C CA  . GLY C 398 ? 0.3665 0.5448 0.5976 -0.2010 0.0124  -0.0162 398 GLY C CA  
9845  C C   . GLY C 398 ? 0.3393 0.5199 0.5594 -0.1927 0.0293  -0.0118 398 GLY C C   
9846  O O   . GLY C 398 ? 0.3825 0.5820 0.6262 -0.1918 0.0406  -0.0076 398 GLY C O   
9847  N N   . THR C 399 ? 0.3146 0.4759 0.5011 -0.1871 0.0320  -0.0130 399 THR C N   
9848  C CA  . THR C 399 ? 0.3604 0.5203 0.5314 -0.1789 0.0459  -0.0107 399 THR C CA  
9849  C C   . THR C 399 ? 0.3572 0.5301 0.5381 -0.1672 0.0447  -0.0149 399 THR C C   
9850  O O   . THR C 399 ? 0.3255 0.4938 0.5005 -0.1623 0.0308  -0.0199 399 THR C O   
9851  C CB  . THR C 399 ? 0.3785 0.5122 0.5124 -0.1768 0.0453  -0.0105 399 THR C CB  
9852  O OG1 . THR C 399 ? 0.3975 0.5209 0.5270 -0.1878 0.0483  -0.0041 399 THR C OG1 
9853  C CG2 . THR C 399 ? 0.3695 0.4985 0.4831 -0.1676 0.0560  -0.0104 399 THR C CG2 
9854  N N   . PRO C 400 ? 0.3671 0.5551 0.5638 -0.1628 0.0596  -0.0129 400 PRO C N   
9855  C CA  . PRO C 400 ? 0.3309 0.5313 0.5424 -0.1511 0.0588  -0.0165 400 PRO C CA  
9856  C C   . PRO C 400 ? 0.3395 0.5212 0.5175 -0.1413 0.0540  -0.0208 400 PRO C C   
9857  O O   . PRO C 400 ? 0.3361 0.4982 0.4811 -0.1412 0.0607  -0.0204 400 PRO C O   
9858  C CB  . PRO C 400 ? 0.3254 0.5395 0.5545 -0.1489 0.0816  -0.0138 400 PRO C CB  
9859  C CG  . PRO C 400 ? 0.3162 0.5340 0.5548 -0.1628 0.0903  -0.0072 400 PRO C CG  
9860  C CD  . PRO C 400 ? 0.3361 0.5304 0.5407 -0.1693 0.0786  -0.0068 400 PRO C CD  
9861  N N   . VAL C 401 ? 0.3164 0.5029 0.5032 -0.1339 0.0407  -0.0241 401 VAL C N   
9862  C CA  . VAL C 401 ? 0.2902 0.4591 0.4478 -0.1251 0.0348  -0.0276 401 VAL C CA  
9863  C C   . VAL C 401 ? 0.3531 0.5349 0.5314 -0.1146 0.0287  -0.0291 401 VAL C C   
9864  O O   . VAL C 401 ? 0.3198 0.5176 0.5272 -0.1165 0.0169  -0.0278 401 VAL C O   
9865  C CB  . VAL C 401 ? 0.3051 0.4551 0.4386 -0.1301 0.0205  -0.0291 401 VAL C CB  
9866  C CG1 . VAL C 401 ? 0.3135 0.4722 0.4643 -0.1360 0.0047  -0.0301 401 VAL C CG1 
9867  C CG2 . VAL C 401 ? 0.3142 0.4462 0.4205 -0.1210 0.0158  -0.0318 401 VAL C CG2 
9868  N N   . MET C 402 ? 0.3216 0.4962 0.4873 -0.1040 0.0368  -0.0313 402 MET C N   
9869  C CA  . MET C 402 ? 0.3717 0.5532 0.5524 -0.0925 0.0314  -0.0327 402 MET C CA  
9870  C C   . MET C 402 ? 0.3426 0.5026 0.4905 -0.0862 0.0229  -0.0348 402 MET C C   
9871  O O   . MET C 402 ? 0.3556 0.4955 0.4708 -0.0884 0.0268  -0.0358 402 MET C O   
9872  C CB  . MET C 402 ? 0.3740 0.5665 0.5748 -0.0848 0.0511  -0.0341 402 MET C CB  
9873  C CG  . MET C 402 ? 0.4195 0.5918 0.5856 -0.0799 0.0651  -0.0380 402 MET C CG  
9874  S SD  . MET C 402 ? 0.5404 0.7209 0.7275 -0.0675 0.0862  -0.0427 402 MET C SD  
9875  C CE  . MET C 402 ? 0.4107 0.5861 0.6001 -0.0554 0.0669  -0.0438 402 MET C CE  
9876  N N   . THR C 403 ? 0.2915 0.4555 0.4507 -0.0788 0.0102  -0.0343 403 THR C N   
9877  C CA  . THR C 403 ? 0.3158 0.4617 0.4500 -0.0714 0.0035  -0.0354 403 THR C CA  
9878  C C   . THR C 403 ? 0.3041 0.4565 0.4566 -0.0586 0.0080  -0.0364 403 THR C C   
9879  O O   . THR C 403 ? 0.2933 0.4664 0.4837 -0.0553 0.0103  -0.0352 403 THR C O   
9880  C CB  . THR C 403 ? 0.3252 0.4647 0.4496 -0.0747 -0.0170 -0.0331 403 THR C CB  
9881  O OG1 . THR C 403 ? 0.3363 0.4938 0.4922 -0.0732 -0.0296 -0.0298 403 THR C OG1 
9882  C CG2 . THR C 403 ? 0.3429 0.4742 0.4505 -0.0871 -0.0206 -0.0336 403 THR C CG2 
9883  N N   . PHE C 404 ? 0.3246 0.4588 0.4533 -0.0515 0.0090  -0.0384 404 PHE C N   
9884  C CA  . PHE C 404 ? 0.3260 0.4617 0.4689 -0.0390 0.0091  -0.0393 404 PHE C CA  
9885  C C   . PHE C 404 ? 0.3645 0.4795 0.4802 -0.0351 -0.0019 -0.0382 404 PHE C C   
9886  O O   . PHE C 404 ? 0.3510 0.4474 0.4351 -0.0394 -0.0003 -0.0392 404 PHE C O   
9887  C CB  . PHE C 404 ? 0.3581 0.4925 0.5036 -0.0328 0.0305  -0.0451 404 PHE C CB  
9888  C CG  . PHE C 404 ? 0.4026 0.5125 0.5065 -0.0352 0.0387  -0.0488 404 PHE C CG  
9889  C CD1 . PHE C 404 ? 0.4004 0.5055 0.4857 -0.0459 0.0461  -0.0485 404 PHE C CD1 
9890  C CD2 . PHE C 404 ? 0.3974 0.4883 0.4823 -0.0273 0.0371  -0.0514 404 PHE C CD2 
9891  C CE1 . PHE C 404 ? 0.4513 0.5326 0.4996 -0.0490 0.0503  -0.0502 404 PHE C CE1 
9892  C CE2 . PHE C 404 ? 0.4171 0.4842 0.4653 -0.0303 0.0416  -0.0540 404 PHE C CE2 
9893  C CZ  . PHE C 404 ? 0.4147 0.4768 0.4445 -0.0412 0.0477  -0.0531 404 PHE C CZ  
9894  N N   . GLU C 405 ? 0.3009 0.4188 0.4315 -0.0271 -0.0131 -0.0352 405 GLU C N   
9895  C CA  . GLU C 405 ? 0.3029 0.4016 0.4103 -0.0231 -0.0224 -0.0331 405 GLU C CA  
9896  C C   . GLU C 405 ? 0.3567 0.4431 0.4579 -0.0134 -0.0117 -0.0378 405 GLU C C   
9897  O O   . GLU C 405 ? 0.3200 0.4156 0.4430 -0.0065 -0.0007 -0.0418 405 GLU C O   
9898  C CB  . GLU C 405 ? 0.3388 0.4437 0.4618 -0.0202 -0.0411 -0.0262 405 GLU C CB  
9899  C CG  . GLU C 405 ? 0.3703 0.4833 0.4941 -0.0310 -0.0544 -0.0220 405 GLU C CG  
9900  C CD  . GLU C 405 ? 0.4298 0.5410 0.5556 -0.0302 -0.0757 -0.0142 405 GLU C CD  
9901  O OE1 . GLU C 405 ? 0.4570 0.5588 0.5802 -0.0216 -0.0794 -0.0113 405 GLU C OE1 
9902  O OE2 . GLU C 405 ? 0.4203 0.5383 0.5498 -0.0386 -0.0897 -0.0105 405 GLU C OE2 
9903  N N   . GLY C 406 ? 0.3320 0.3963 0.4037 -0.0134 -0.0137 -0.0378 406 GLY C N   
9904  C CA  . GLY C 406 ? 0.3182 0.3682 0.3826 -0.0049 -0.0072 -0.0419 406 GLY C CA  
9905  C C   . GLY C 406 ? 0.3323 0.3604 0.3729 -0.0047 -0.0154 -0.0388 406 GLY C C   
9906  O O   . GLY C 406 ? 0.3518 0.3770 0.3848 -0.0093 -0.0257 -0.0329 406 GLY C O   
9907  N N   . ASN C 407 ? 0.3275 0.3388 0.3566 0.0004  -0.0102 -0.0430 407 ASN C N   
9908  C CA  . ASN C 407 ? 0.3286 0.3182 0.3385 0.0003  -0.0170 -0.0398 407 ASN C CA  
9909  C C   . ASN C 407 ? 0.3600 0.3317 0.3526 0.0006  -0.0098 -0.0459 407 ASN C C   
9910  O O   . ASN C 407 ? 0.3620 0.3322 0.3597 0.0077  -0.0029 -0.0523 407 ASN C O   
9911  C CB  . ASN C 407 ? 0.3255 0.3129 0.3480 0.0093  -0.0269 -0.0350 407 ASN C CB  
9912  C CG  . ASN C 407 ? 0.3264 0.2924 0.3331 0.0091  -0.0331 -0.0305 407 ASN C CG  
9913  O OD1 . ASN C 407 ? 0.3481 0.2980 0.3409 0.0075  -0.0298 -0.0335 407 ASN C OD1 
9914  N ND2 . ASN C 407 ? 0.3287 0.2935 0.3384 0.0106  -0.0426 -0.0226 407 ASN C ND2 
9915  N N   . MET C 408 ? 0.3596 0.3172 0.3320 -0.0078 -0.0108 -0.0444 408 MET C N   
9916  C CA  . MET C 408 ? 0.4187 0.3587 0.3718 -0.0097 -0.0060 -0.0496 408 MET C CA  
9917  C C   . MET C 408 ? 0.3859 0.3078 0.3355 -0.0014 -0.0097 -0.0524 408 MET C C   
9918  O O   . MET C 408 ? 0.4132 0.3223 0.3487 -0.0002 -0.0041 -0.0597 408 MET C O   
9919  C CB  . MET C 408 ? 0.4068 0.3337 0.3433 -0.0204 -0.0097 -0.0455 408 MET C CB  
9920  C CG  . MET C 408 ? 0.4189 0.3293 0.3550 -0.0197 -0.0201 -0.0397 408 MET C CG  
9921  S SD  . MET C 408 ? 0.3959 0.3158 0.3476 -0.0181 -0.0252 -0.0322 408 MET C SD  
9922  C CE  . MET C 408 ? 0.4007 0.2968 0.3495 -0.0215 -0.0319 -0.0256 408 MET C CE  
9923  N N   . GLY C 409 ? 0.3718 0.2913 0.3328 0.0041  -0.0184 -0.0472 409 GLY C N   
9924  C CA  . GLY C 409 ? 0.3880 0.2880 0.3463 0.0108  -0.0233 -0.0491 409 GLY C CA  
9925  C C   . GLY C 409 ? 0.3861 0.2926 0.3641 0.0224  -0.0233 -0.0511 409 GLY C C   
9926  O O   . GLY C 409 ? 0.4171 0.3080 0.3940 0.0290  -0.0244 -0.0558 409 GLY C O   
9927  N N   . ASP C 410 ? 0.3850 0.3137 0.3824 0.0247  -0.0229 -0.0476 410 ASP C N   
9928  C CA  . ASP C 410 ? 0.3580 0.2949 0.3802 0.0354  -0.0263 -0.0462 410 ASP C CA  
9929  C C   . ASP C 410 ? 0.3579 0.3176 0.4013 0.0384  -0.0179 -0.0504 410 ASP C C   
9930  O O   . ASP C 410 ? 0.3495 0.3281 0.4055 0.0352  -0.0220 -0.0444 410 ASP C O   
9931  C CB  . ASP C 410 ? 0.3575 0.2960 0.3852 0.0346  -0.0388 -0.0342 410 ASP C CB  
9932  C CG  . ASP C 410 ? 0.3772 0.3188 0.4282 0.0450  -0.0461 -0.0299 410 ASP C CG  
9933  O OD1 . ASP C 410 ? 0.3842 0.3301 0.4538 0.0536  -0.0408 -0.0368 410 ASP C OD1 
9934  O OD2 . ASP C 410 ? 0.3902 0.3283 0.4404 0.0439  -0.0564 -0.0193 410 ASP C OD2 
9935  N N   . GLU C 411 ? 0.3767 0.3327 0.4251 0.0448  -0.0063 -0.0608 411 GLU C N   
9936  C CA  . GLU C 411 ? 0.4331 0.4089 0.5059 0.0487  0.0061  -0.0663 411 GLU C CA  
9937  C C   . GLU C 411 ? 0.4133 0.4107 0.5248 0.0546  -0.0027 -0.0585 411 GLU C C   
9938  O O   . GLU C 411 ? 0.3866 0.4051 0.5242 0.0557  0.0045  -0.0598 411 GLU C O   
9939  C CB  . GLU C 411 ? 0.4692 0.4321 0.5423 0.0567  0.0208  -0.0793 411 GLU C CB  
9940  C CG  . GLU C 411 ? 0.5433 0.4964 0.6359 0.0687  0.0137  -0.0793 411 GLU C CG  
9941  C CD  . GLU C 411 ? 0.6795 0.6185 0.7757 0.0776  0.0296  -0.0939 411 GLU C CD  
9942  O OE1 . GLU C 411 ? 0.6146 0.5670 0.7320 0.0816  0.0465  -0.1012 411 GLU C OE1 
9943  O OE2 . GLU C 411 ? 0.6627 0.5763 0.7423 0.0807  0.0254  -0.0983 411 GLU C OE2 
9944  N N   . ARG C 412 ? 0.3626 0.3544 0.4804 0.0586  -0.0184 -0.0497 412 ARG C N   
9945  C CA  . ARG C 412 ? 0.3711 0.3806 0.5230 0.0632  -0.0301 -0.0405 412 ARG C CA  
9946  C C   . ARG C 412 ? 0.3599 0.3885 0.5142 0.0540  -0.0364 -0.0337 412 ARG C C   
9947  O O   . ARG C 412 ? 0.3457 0.3929 0.5322 0.0564  -0.0440 -0.0279 412 ARG C O   
9948  C CB  . ARG C 412 ? 0.3613 0.3581 0.5117 0.0668  -0.0463 -0.0306 412 ARG C CB  
9949  C CG  . ARG C 412 ? 0.3873 0.3677 0.5471 0.0778  -0.0430 -0.0363 412 ARG C CG  
9950  C CD  . ARG C 412 ? 0.3972 0.3631 0.5527 0.0799  -0.0587 -0.0253 412 ARG C CD  
9951  N NE  . ARG C 412 ? 0.3775 0.3266 0.4967 0.0713  -0.0609 -0.0226 412 ARG C NE  
9952  C CZ  . ARG C 412 ? 0.3879 0.3201 0.4989 0.0721  -0.0699 -0.0150 412 ARG C CZ  
9953  N NH1 . ARG C 412 ? 0.3800 0.3092 0.5133 0.0806  -0.0791 -0.0083 412 ARG C NH1 
9954  N NH2 . ARG C 412 ? 0.4069 0.3249 0.4901 0.0642  -0.0693 -0.0133 412 ARG C NH2 
9955  N N   . GLU C 413 ? 0.3954 0.4187 0.5182 0.0431  -0.0345 -0.0339 413 GLU C N   
9956  C CA  . GLU C 413 ? 0.3719 0.4107 0.4943 0.0335  -0.0397 -0.0290 413 GLU C CA  
9957  C C   . GLU C 413 ? 0.3978 0.4482 0.5219 0.0283  -0.0246 -0.0367 413 GLU C C   
9958  O O   . GLU C 413 ? 0.3366 0.3944 0.4516 0.0183  -0.0267 -0.0344 413 GLU C O   
9959  C CB  . GLU C 413 ? 0.3927 0.4180 0.4823 0.0243  -0.0484 -0.0230 413 GLU C CB  
9960  C CG  . GLU C 413 ? 0.4554 0.4720 0.5439 0.0273  -0.0634 -0.0131 413 GLU C CG  
9961  C CD  . GLU C 413 ? 0.4159 0.4188 0.4729 0.0180  -0.0690 -0.0073 413 GLU C CD  
9962  O OE1 . GLU C 413 ? 0.4330 0.4264 0.4692 0.0121  -0.0603 -0.0115 413 GLU C OE1 
9963  O OE2 . GLU C 413 ? 0.4913 0.4917 0.5449 0.0166  -0.0820 0.0022  413 GLU C OE2 
9964  N N   . PHE C 414 ? 0.3836 0.4343 0.5180 0.0345  -0.0087 -0.0459 414 PHE C N   
9965  C CA  . PHE C 414 ? 0.3776 0.4391 0.5149 0.0299  0.0080  -0.0526 414 PHE C CA  
9966  C C   . PHE C 414 ? 0.4057 0.4841 0.5856 0.0391  0.0188  -0.0566 414 PHE C C   
9967  O O   . PHE C 414 ? 0.3991 0.4684 0.5880 0.0493  0.0259  -0.0625 414 PHE C O   
9968  C CB  . PHE C 414 ? 0.3806 0.4205 0.4804 0.0263  0.0207  -0.0606 414 PHE C CB  
9969  C CG  . PHE C 414 ? 0.4239 0.4708 0.5194 0.0202  0.0385  -0.0665 414 PHE C CG  
9970  C CD1 . PHE C 414 ? 0.4087 0.4709 0.5071 0.0101  0.0370  -0.0619 414 PHE C CD1 
9971  C CD2 . PHE C 414 ? 0.4219 0.4588 0.5100 0.0243  0.0576  -0.0769 414 PHE C CD2 
9972  C CE1 . PHE C 414 ? 0.4262 0.4944 0.5211 0.0040  0.0541  -0.0662 414 PHE C CE1 
9973  C CE2 . PHE C 414 ? 0.4974 0.5385 0.5778 0.0180  0.0757  -0.0817 414 PHE C CE2 
9974  C CZ  . PHE C 414 ? 0.4603 0.5181 0.5457 0.0078  0.0738  -0.0755 414 PHE C CZ  
9975  N N   . ASP C 415 ? 0.3524 0.4549 0.5618 0.0355  0.0201  -0.0536 415 ASP C N   
9976  C CA  . ASP C 415 ? 0.4530 0.5750 0.7109 0.0432  0.0319  -0.0565 415 ASP C CA  
9977  C C   . ASP C 415 ? 0.4734 0.5980 0.7230 0.0383  0.0569  -0.0651 415 ASP C C   
9978  O O   . ASP C 415 ? 0.4079 0.5467 0.6614 0.0288  0.0577  -0.0617 415 ASP C O   
9979  C CB  . ASP C 415 ? 0.3938 0.5405 0.6935 0.0416  0.0145  -0.0457 415 ASP C CB  
9980  C CG  . ASP C 415 ? 0.4935 0.6614 0.8537 0.0506  0.0241  -0.0468 415 ASP C CG  
9981  O OD1 . ASP C 415 ? 0.4484 0.6163 0.8182 0.0554  0.0506  -0.0572 415 ASP C OD1 
9982  O OD2 . ASP C 415 ? 0.5208 0.7050 0.9200 0.0522  0.0049  -0.0367 415 ASP C OD2 
9983  N N   . GLU C 416 ? 0.4922 0.6006 0.7269 0.0437  0.0773  -0.0762 416 GLU C N   
9984  C CA  . GLU C 416 ? 0.5256 0.6312 0.7416 0.0373  0.1015  -0.0839 416 GLU C CA  
9985  C C   . GLU C 416 ? 0.5030 0.6352 0.7687 0.0392  0.1184  -0.0846 416 GLU C C   
9986  O O   . GLU C 416 ? 0.4982 0.6378 0.7573 0.0300  0.1307  -0.0847 416 GLU C O   
9987  C CB  . GLU C 416 ? 0.6245 0.7008 0.8022 0.0407  0.1180  -0.0960 416 GLU C CB  
9988  C CG  . GLU C 416 ? 0.6991 0.7681 0.8989 0.0549  0.1235  -0.1030 416 GLU C CG  
9989  C CD  . GLU C 416 ? 0.7879 0.8222 0.9398 0.0562  0.1324  -0.1143 416 GLU C CD  
9990  O OE1 . GLU C 416 ? 0.7271 0.7473 0.8440 0.0495  0.1518  -0.1224 416 GLU C OE1 
9991  O OE2 . GLU C 416 ? 0.7865 0.8064 0.9338 0.0627  0.1181  -0.1141 416 GLU C OE2 
9992  N N   . VAL C 417 ? 0.5151 0.6627 0.8347 0.0505  0.1188  -0.0840 417 VAL C N   
9993  C CA  . VAL C 417 ? 0.5027 0.6768 0.8761 0.0518  0.1353  -0.0837 417 VAL C CA  
9994  C C   . VAL C 417 ? 0.4632 0.6605 0.8554 0.0413  0.1178  -0.0718 417 VAL C C   
9995  O O   . VAL C 417 ? 0.4233 0.6347 0.8291 0.0345  0.1329  -0.0718 417 VAL C O   
9996  C CB  . VAL C 417 ? 0.5380 0.7237 0.9723 0.0666  0.1400  -0.0853 417 VAL C CB  
9997  C CG1 . VAL C 417 ? 0.5731 0.7317 0.9835 0.0766  0.1514  -0.0969 417 VAL C CG1 
9998  C CG2 . VAL C 417 ? 0.5603 0.7625 1.0336 0.0693  0.1069  -0.0715 417 VAL C CG2 
9999  N N   . ARG C 418 ? 0.4373 0.6363 0.8264 0.0388  0.0865  -0.0618 418 ARG C N   
10000 C CA  . ARG C 418 ? 0.3886 0.6053 0.7891 0.0278  0.0692  -0.0519 418 ARG C CA  
10001 C C   . ARG C 418 ? 0.4171 0.6238 0.7694 0.0148  0.0761  -0.0541 418 ARG C C   
10002 O O   . ARG C 418 ? 0.4105 0.6334 0.7780 0.0056  0.0769  -0.0502 418 ARG C O   
10003 C CB  . ARG C 418 ? 0.4467 0.6618 0.8455 0.0273  0.0353  -0.0418 418 ARG C CB  
10004 C CG  . ARG C 418 ? 0.4700 0.6955 0.8662 0.0146  0.0155  -0.0333 418 ARG C CG  
10005 C CD  . ARG C 418 ? 0.5798 0.7886 0.9380 0.0110  -0.0105 -0.0274 418 ARG C CD  
10006 N NE  . ARG C 418 ? 0.6881 0.9081 1.0587 0.0022  -0.0357 -0.0177 418 ARG C NE  
10007 C CZ  . ARG C 418 ? 0.7330 0.9622 1.1024 -0.0097 -0.0376 -0.0166 418 ARG C CZ  
10008 N NH1 . ARG C 418 ? 0.6832 0.9119 1.0377 -0.0148 -0.0160 -0.0233 418 ARG C NH1 
10009 N NH2 . ARG C 418 ? 0.7571 0.9943 1.1385 -0.0174 -0.0628 -0.0082 418 ARG C NH2 
10010 N N   . THR C 419 ? 0.4000 0.5798 0.6968 0.0134  0.0795  -0.0594 419 THR C N   
10011 C CA  . THR C 419 ? 0.3971 0.5656 0.6498 0.0012  0.0845  -0.0604 419 THR C CA  
10012 C C   . THR C 419 ? 0.4658 0.6393 0.7227 -0.0022 0.1131  -0.0659 419 THR C C   
10013 O O   . THR C 419 ? 0.4525 0.6352 0.7087 -0.0130 0.1160  -0.0623 419 THR C O   
10014 C CB  . THR C 419 ? 0.3705 0.5086 0.5690 0.0011  0.0801  -0.0639 419 THR C CB  
10015 O OG1 . THR C 419 ? 0.4282 0.5622 0.6248 0.0038  0.0556  -0.0579 419 THR C OG1 
10016 C CG2 . THR C 419 ? 0.3925 0.5176 0.5480 -0.0119 0.0823  -0.0633 419 THR C CG2 
10017 N N   . GLN C 420 ? 0.4677 0.6345 0.7298 0.0067  0.1356  -0.0748 420 GLN C N   
10018 C CA  . GLN C 420 ? 0.4767 0.6457 0.7398 0.0035  0.1666  -0.0806 420 GLN C CA  
10019 C C   . GLN C 420 ? 0.5229 0.7245 0.8441 0.0010  0.1720  -0.0747 420 GLN C C   
10020 O O   . GLN C 420 ? 0.5228 0.7297 0.8417 -0.0074 0.1906  -0.0747 420 GLN C O   
10021 C CB  . GLN C 420 ? 0.5789 0.7335 0.8396 0.0145  0.1908  -0.0926 420 GLN C CB  
10022 C CG  . GLN C 420 ? 0.6185 0.7648 0.8605 0.0099  0.2262  -0.1006 420 GLN C CG  
10023 C CD  . GLN C 420 ? 0.7437 0.9106 1.0441 0.0177  0.2537  -0.1050 420 GLN C CD  
10024 O OE1 . GLN C 420 ? 0.7527 0.9506 1.1107 0.0172  0.2500  -0.0970 420 GLN C OE1 
10025 N NE2 . GLN C 420 ? 0.7361 0.8845 1.0214 0.0240  0.2826  -0.1179 420 GLN C NE2 
10026 N N   . ALA C 421 ? 0.4635 0.6864 0.8380 0.0076  0.1549  -0.0688 421 ALA C N   
10027 C CA  . ALA C 421 ? 0.4473 0.7014 0.8806 0.0041  0.1544  -0.0615 421 ALA C CA  
10028 C C   . ALA C 421 ? 0.4514 0.7102 0.8670 -0.0106 0.1377  -0.0538 421 ALA C C   
10029 O O   . ALA C 421 ? 0.4609 0.7350 0.8976 -0.0185 0.1497  -0.0511 421 ALA C O   
10030 C CB  . ALA C 421 ? 0.4427 0.7154 0.9349 0.0137  0.1350  -0.0556 421 ALA C CB  
10031 N N   . ARG C 422 ? 0.4440 0.6890 0.8225 -0.0145 0.1113  -0.0505 422 ARG C N   
10032 C CA  . ARG C 422 ? 0.4710 0.7172 0.8306 -0.0281 0.0957  -0.0446 422 ARG C CA  
10033 C C   . ARG C 422 ? 0.4952 0.7296 0.8171 -0.0378 0.1155  -0.0476 422 ARG C C   
10034 O O   . ARG C 422 ? 0.4658 0.7105 0.7952 -0.0489 0.1140  -0.0429 422 ARG C O   
10035 C CB  . ARG C 422 ? 0.4427 0.6726 0.7674 -0.0292 0.0679  -0.0418 422 ARG C CB  
10036 C CG  . ARG C 422 ? 0.5382 0.7683 0.8468 -0.0428 0.0510  -0.0367 422 ARG C CG  
10037 C CD  . ARG C 422 ? 0.5196 0.7749 0.8767 -0.0478 0.0369  -0.0300 422 ARG C CD  
10038 N NE  . ARG C 422 ? 0.5490 0.8013 0.8872 -0.0613 0.0225  -0.0270 422 ARG C NE  
10039 C CZ  . ARG C 422 ? 0.5262 0.7807 0.8587 -0.0713 0.0345  -0.0273 422 ARG C CZ  
10040 N NH1 . ARG C 422 ? 0.4629 0.7242 0.8080 -0.0703 0.0609  -0.0294 422 ARG C NH1 
10041 N NH2 . ARG C 422 ? 0.5115 0.7601 0.8254 -0.0828 0.0204  -0.0254 422 ARG C NH2 
10042 N N   . VAL C 423 ? 0.4989 0.7108 0.7806 -0.0344 0.1328  -0.0549 423 VAL C N   
10043 C CA  . VAL C 423 ? 0.5095 0.7080 0.7544 -0.0436 0.1523  -0.0570 423 VAL C CA  
10044 C C   . VAL C 423 ? 0.5100 0.7273 0.7903 -0.0463 0.1783  -0.0568 423 VAL C C   
10045 O O   . VAL C 423 ? 0.5329 0.7511 0.8018 -0.0579 0.1863  -0.0531 423 VAL C O   
10046 C CB  . VAL C 423 ? 0.5889 0.7567 0.7826 -0.0393 0.1627  -0.0649 423 VAL C CB  
10047 C CG1 . VAL C 423 ? 0.5903 0.7436 0.7477 -0.0488 0.1854  -0.0669 423 VAL C CG1 
10048 C CG2 . VAL C 423 ? 0.5496 0.6982 0.7067 -0.0403 0.1378  -0.0631 423 VAL C CG2 
10049 N N   . ASP C 424 ? 0.5411 0.7732 0.8668 -0.0356 0.1932  -0.0604 424 ASP C N   
10050 C CA  . ASP C 424 ? 0.5556 0.8086 0.9248 -0.0379 0.2193  -0.0594 424 ASP C CA  
10051 C C   . ASP C 424 ? 0.5122 0.7903 0.9205 -0.0475 0.2041  -0.0491 424 ASP C C   
10052 O O   . ASP C 424 ? 0.5454 0.8302 0.9577 -0.0574 0.2199  -0.0459 424 ASP C O   
10053 C CB  . ASP C 424 ? 0.5636 0.8321 0.9889 -0.0242 0.2358  -0.0640 424 ASP C CB  
10054 C CG  . ASP C 424 ? 0.6781 0.9224 1.0725 -0.0134 0.2502  -0.0753 424 ASP C CG  
10055 O OD1 . ASP C 424 ? 0.7324 0.9524 1.0737 -0.0177 0.2720  -0.0821 424 ASP C OD1 
10056 O OD2 . ASP C 424 ? 0.6720 0.9210 1.0965 -0.0010 0.2399  -0.0772 424 ASP C OD2 
10057 N N   . ALA C 425 ? 0.4964 0.7882 0.9354 -0.0449 0.1738  -0.0438 425 ALA C N   
10058 C CA  . ALA C 425 ? 0.4653 0.7775 0.9372 -0.0548 0.1548  -0.0348 425 ALA C CA  
10059 C C   . ALA C 425 ? 0.4930 0.7922 0.9194 -0.0691 0.1519  -0.0325 425 ALA C C   
10060 O O   . ALA C 425 ? 0.4805 0.7937 0.9293 -0.0792 0.1574  -0.0273 425 ALA C O   
10061 C CB  . ALA C 425 ? 0.3980 0.7158 0.8864 -0.0515 0.1189  -0.0304 425 ALA C CB  
10062 N N   . PHE C 426 ? 0.4665 0.7388 0.8323 -0.0702 0.1428  -0.0357 426 PHE C N   
10063 C CA  . PHE C 426 ? 0.5157 0.7733 0.8394 -0.0830 0.1390  -0.0333 426 PHE C CA  
10064 C C   . PHE C 426 ? 0.5083 0.7630 0.8212 -0.0900 0.1682  -0.0329 426 PHE C C   
10065 O O   . PHE C 426 ? 0.5392 0.7987 0.8544 -0.1021 0.1681  -0.0272 426 PHE C O   
10066 C CB  . PHE C 426 ? 0.4590 0.6877 0.7256 -0.0810 0.1270  -0.0368 426 PHE C CB  
10067 C CG  . PHE C 426 ? 0.4644 0.6783 0.6948 -0.0932 0.1169  -0.0335 426 PHE C CG  
10068 C CD1 . PHE C 426 ? 0.4419 0.6671 0.6910 -0.1024 0.1007  -0.0285 426 PHE C CD1 
10069 C CD2 . PHE C 426 ? 0.4610 0.6478 0.6394 -0.0955 0.1224  -0.0355 426 PHE C CD2 
10070 C CE1 . PHE C 426 ? 0.4040 0.6143 0.6227 -0.1130 0.0924  -0.0262 426 PHE C CE1 
10071 C CE2 . PHE C 426 ? 0.4772 0.6499 0.6274 -0.1061 0.1124  -0.0317 426 PHE C CE2 
10072 C CZ  . PHE C 426 ? 0.4162 0.6007 0.5871 -0.1144 0.0985  -0.0274 426 PHE C CZ  
10073 N N   . MET C 427 ? 0.5072 0.7524 0.8067 -0.0831 0.1937  -0.0391 427 MET C N   
10074 C CA  . MET C 427 ? 0.5672 0.8039 0.8454 -0.0905 0.2230  -0.0390 427 MET C CA  
10075 C C   . MET C 427 ? 0.5996 0.8645 0.9328 -0.0963 0.2367  -0.0330 427 MET C C   
10076 O O   . MET C 427 ? 0.6398 0.9032 0.9620 -0.1087 0.2452  -0.0272 427 MET C O   
10077 C CB  . MET C 427 ? 0.5902 0.8109 0.8462 -0.0815 0.2490  -0.0483 427 MET C CB  
10078 C CG  . MET C 427 ? 0.6531 0.8375 0.8375 -0.0820 0.2448  -0.0532 427 MET C CG  
10079 S SD  . MET C 427 ? 0.7773 0.9372 0.9020 -0.0982 0.2312  -0.0460 427 MET C SD  
10080 C CE  . MET C 427 ? 0.5034 0.6699 0.6404 -0.0974 0.1919  -0.0418 427 MET C CE  
10081 N N   . GLU C 428 ? 0.5917 0.8825 0.9881 -0.0876 0.2376  -0.0332 428 GLU C N   
10082 C CA  . GLU C 428 ? 0.5934 0.9135 1.0520 -0.0930 0.2470  -0.0264 428 GLU C CA  
10083 C C   . GLU C 428 ? 0.5462 0.8744 1.0115 -0.1058 0.2214  -0.0179 428 GLU C C   
10084 O O   . GLU C 428 ? 0.5661 0.9059 1.0527 -0.1161 0.2329  -0.0116 428 GLU C O   
10085 C CB  . GLU C 428 ? 0.6039 0.9499 1.1337 -0.0810 0.2460  -0.0270 428 GLU C CB  
10086 C CG  . GLU C 428 ? 0.6991 1.0405 1.2355 -0.0687 0.2791  -0.0358 428 GLU C CG  
10087 C CD  . GLU C 428 ? 0.7270 1.0761 1.2984 -0.0535 0.2651  -0.0394 428 GLU C CD  
10088 O OE1 . GLU C 428 ? 0.7260 1.0665 1.2965 -0.0423 0.2886  -0.0482 428 GLU C OE1 
10089 O OE2 . GLU C 428 ? 0.6649 1.0263 1.2618 -0.0532 0.2301  -0.0334 428 GLU C OE2 
10090 N N   . GLN C 429 ? 0.5544 0.8743 0.9994 -0.1058 0.1882  -0.0180 429 GLN C N   
10091 C CA  . GLN C 429 ? 0.5559 0.8794 1.0027 -0.1181 0.1648  -0.0119 429 GLN C CA  
10092 C C   . GLN C 429 ? 0.5884 0.8933 0.9890 -0.1302 0.1745  -0.0094 429 GLN C C   
10093 O O   . GLN C 429 ? 0.5972 0.9094 1.0118 -0.1420 0.1668  -0.0033 429 GLN C O   
10094 C CB  . GLN C 429 ? 0.5408 0.8553 0.9698 -0.1154 0.1304  -0.0138 429 GLN C CB  
10095 C CG  . GLN C 429 ? 0.5313 0.8360 0.9364 -0.1280 0.1095  -0.0109 429 GLN C CG  
10096 C CD  . GLN C 429 ? 0.6059 0.8939 0.9784 -0.1251 0.0826  -0.0144 429 GLN C CD  
10097 O OE1 . GLN C 429 ? 0.6458 0.9311 1.0158 -0.1140 0.0765  -0.0177 429 GLN C OE1 
10098 N NE2 . GLN C 429 ? 0.5163 0.7927 0.8659 -0.1354 0.0674  -0.0136 429 GLN C NE2 
10099 N N   . LEU C 430 ? 0.5593 0.8396 0.9066 -0.1281 0.1903  -0.0134 430 LEU C N   
10100 C CA  . LEU C 430 ? 0.5937 0.8542 0.8960 -0.1398 0.1992  -0.0096 430 LEU C CA  
10101 C C   . LEU C 430 ? 0.6384 0.9059 0.9533 -0.1463 0.2316  -0.0052 430 LEU C C   
10102 O O   . LEU C 430 ? 0.7027 0.9505 0.9747 -0.1556 0.2430  -0.0016 430 LEU C O   
10103 C CB  . LEU C 430 ? 0.5087 0.7369 0.7465 -0.1360 0.1986  -0.0146 430 LEU C CB  
10104 C CG  . LEU C 430 ? 0.4589 0.6758 0.6776 -0.1319 0.1687  -0.0175 430 LEU C CG  
10105 C CD1 . LEU C 430 ? 0.5008 0.6856 0.6594 -0.1302 0.1682  -0.0207 430 LEU C CD1 
10106 C CD2 . LEU C 430 ? 0.4656 0.6868 0.6942 -0.1424 0.1472  -0.0121 430 LEU C CD2 
10107 N N   . GLY C 431 ? 0.6659 0.9601 1.0390 -0.1423 0.2467  -0.0046 431 GLY C N   
10108 C CA  . GLY C 431 ? 0.7171 1.0186 1.1055 -0.1488 0.2800  0.0000  431 GLY C CA  
10109 C C   . GLY C 431 ? 0.8511 1.1298 1.1932 -0.1439 0.3101  -0.0054 431 GLY C C   
10110 O O   . GLY C 431 ? 0.9263 1.1909 1.2372 -0.1509 0.3268  0.0001  431 GLY C O   
10111 N N   . VAL C 432 ? 0.8558 1.1280 1.1897 -0.1314 0.3149  -0.0159 432 VAL C N   
10112 C CA  . VAL C 432 ? 0.9410 1.1875 1.2261 -0.1269 0.3422  -0.0235 432 VAL C CA  
10113 C C   . VAL C 432 ? 0.9585 1.2155 1.2798 -0.1100 0.3534  -0.0329 432 VAL C C   
10114 O O   . VAL C 432 ? 0.8985 1.1754 1.2654 -0.1019 0.3338  -0.0345 432 VAL C O   
10115 C CB  . VAL C 432 ? 0.9187 1.1291 1.1257 -0.1303 0.3274  -0.0264 432 VAL C CB  
10116 C CG1 . VAL C 432 ? 0.8378 1.0510 1.0466 -0.1321 0.2873  -0.0222 432 VAL C CG1 
10117 C CG2 . VAL C 432 ? 0.9383 1.1284 1.1139 -0.1178 0.3356  -0.0387 432 VAL C CG2 
10118 N N   . ARG C 433 ? 0.9868 1.2278 1.2859 -0.1044 0.3818  -0.0384 433 ARG C N   
10119 C CA  . ARG C 433 ? 1.0343 1.2799 1.3629 -0.0884 0.3960  -0.0481 433 ARG C CA  
10120 C C   . ARG C 433 ? 1.1285 1.3367 1.3886 -0.0847 0.4140  -0.0596 433 ARG C C   
10121 O O   . ARG C 433 ? 1.1562 1.3364 1.3512 -0.0949 0.4220  -0.0582 433 ARG C O   
10122 C CB  . ARG C 433 ? 0.9535 1.2185 1.3360 -0.0847 0.4153  -0.0444 433 ARG C CB  
10123 C CG  . ARG C 433 ? 0.9688 1.2081 1.3071 -0.0854 0.4484  -0.0493 433 ARG C CG  
10124 C CD  . ARG C 433 ? 0.9454 1.2006 1.3244 -0.0877 0.4678  -0.0426 433 ARG C CD  
10125 N NE  . ARG C 433 ? 1.0177 1.2463 1.3537 -0.0873 0.5009  -0.0495 433 ARG C NE  
10126 C CZ  . ARG C 433 ? 1.0776 1.2887 1.3674 -0.0990 0.5157  -0.0443 433 ARG C CZ  
10127 N NH1 . ARG C 433 ? 1.1039 1.3211 1.3849 -0.1121 0.5009  -0.0317 433 ARG C NH1 
10128 N NH2 . ARG C 433 ? 1.0786 1.2643 1.3301 -0.0980 0.5455  -0.0518 433 ARG C NH2 
10129 N N   . ARG C 434 ? 1.2004 1.4067 1.4753 -0.0704 0.4182  -0.0704 434 ARG C N   
10130 C CA  . ARG C 434 ? 1.1875 1.3568 1.3992 -0.0662 0.4336  -0.0826 434 ARG C CA  
10131 C C   . ARG C 434 ? 1.2261 1.3859 1.4363 -0.0634 0.4658  -0.0866 434 ARG C C   
10132 O O   . ARG C 434 ? 1.2168 1.3935 1.4837 -0.0520 0.4777  -0.0904 434 ARG C O   
10133 C CB  . ARG C 434 ? 1.1834 1.3512 1.4080 -0.0520 0.4242  -0.0932 434 ARG C CB  
10134 C CG  . ARG C 434 ? 1.2261 1.3580 1.3995 -0.0454 0.4425  -0.1070 434 ARG C CG  
10135 C CD  . ARG C 434 ? 1.2863 1.4290 1.5133 -0.0286 0.4545  -0.1155 434 ARG C CD  
10136 N NE  . ARG C 434 ? 1.2703 1.4253 1.5295 -0.0178 0.4327  -0.1186 434 ARG C NE  
10137 C CZ  . ARG C 434 ? 1.2228 1.4108 1.5624 -0.0074 0.4236  -0.1150 434 ARG C CZ  
10138 N NH1 . ARG C 434 ? 1.1841 1.3969 1.5828 -0.0064 0.4335  -0.1083 434 ARG C NH1 
10139 N NH2 . ARG C 434 ? 1.0831 1.2783 1.4444 0.0019  0.4025  -0.1175 434 ARG C NH2 
10140 N N   . SER D 2   ? 1.2325 1.3397 0.9933 0.1368  -0.1690 0.2617  2   SER D N   
10141 C CA  . SER D 2   ? 1.1769 1.2414 0.9083 0.1341  -0.1310 0.2322  2   SER D CA  
10142 C C   . SER D 2   ? 1.1596 1.2007 0.8272 0.1071  -0.1344 0.2079  2   SER D C   
10143 O O   . SER D 2   ? 1.1621 1.2134 0.7979 0.0893  -0.1665 0.2142  2   SER D O   
10144 C CB  . SER D 2   ? 1.1391 1.2189 0.9325 0.1455  -0.1034 0.2133  2   SER D CB  
10145 O OG  . SER D 2   ? 1.1371 1.1779 0.9061 0.1430  -0.0696 0.1889  2   SER D OG  
10146 N N   . ASP D 3   ? 1.0053 1.0148 0.6561 0.1034  -0.1011 0.1805  3   ASP D N   
10147 C CA  . ASP D 3   ? 0.9502 0.9265 0.5362 0.0810  -0.0964 0.1596  3   ASP D CA  
10148 C C   . ASP D 3   ? 0.9346 0.9302 0.5370 0.0663  -0.0993 0.1352  3   ASP D C   
10149 O O   . ASP D 3   ? 0.9137 0.8853 0.4639 0.0461  -0.1003 0.1197  3   ASP D O   
10150 C CB  . ASP D 3   ? 0.8882 0.8173 0.4454 0.0842  -0.0584 0.1466  3   ASP D CB  
10151 C CG  . ASP D 3   ? 0.9124 0.8499 0.5280 0.0974  -0.0293 0.1317  3   ASP D CG  
10152 O OD1 . ASP D 3   ? 0.9053 0.8571 0.5458 0.0907  -0.0227 0.1102  3   ASP D OD1 
10153 O OD2 . ASP D 3   ? 0.9679 0.8961 0.6029 0.1141  -0.0141 0.1434  3   ASP D OD2 
10154 N N   . GLY D 4   ? 0.8194 0.8539 0.4897 0.0755  -0.0987 0.1317  4   GLY D N   
10155 C CA  . GLY D 4   ? 0.7087 0.7633 0.3940 0.0611  -0.1050 0.1126  4   GLY D CA  
10156 C C   . GLY D 4   ? 0.6670 0.6940 0.3359 0.0527  -0.0772 0.0841  4   GLY D C   
10157 O O   . GLY D 4   ? 0.6721 0.7058 0.3384 0.0376  -0.0826 0.0683  4   GLY D O   
10158 N N   . LEU D 5   ? 0.6877 0.6852 0.3505 0.0620  -0.0474 0.0780  5   LEU D N   
10159 C CA  . LEU D 5   ? 0.6095 0.5824 0.2615 0.0544  -0.0214 0.0539  5   LEU D CA  
10160 C C   . LEU D 5   ? 0.5865 0.5883 0.2887 0.0536  -0.0187 0.0393  5   LEU D C   
10161 O O   . LEU D 5   ? 0.6342 0.6257 0.3262 0.0418  -0.0103 0.0216  5   LEU D O   
10162 C CB  . LEU D 5   ? 0.6557 0.5999 0.3062 0.0654  0.0083  0.0531  5   LEU D CB  
10163 C CG  . LEU D 5   ? 0.6265 0.5466 0.2738 0.0595  0.0372  0.0320  5   LEU D CG  
10164 C CD1 . LEU D 5   ? 0.6728 0.5644 0.2650 0.0419  0.0387  0.0213  5   LEU D CD1 
10165 C CD2 . LEU D 5   ? 0.6215 0.5169 0.2714 0.0695  0.0635  0.0351  5   LEU D CD2 
10166 N N   . PHE D 6   ? 0.5124 0.5473 0.2675 0.0664  -0.0233 0.0471  6   PHE D N   
10167 C CA  . PHE D 6   ? 0.4694 0.5297 0.2693 0.0662  -0.0194 0.0350  6   PHE D CA  
10168 C C   . PHE D 6   ? 0.4892 0.5832 0.3059 0.0579  -0.0441 0.0379  6   PHE D C   
10169 O O   . PHE D 6   ? 0.4968 0.6137 0.3517 0.0583  -0.0416 0.0306  6   PHE D O   
10170 C CB  . PHE D 6   ? 0.4599 0.5304 0.3032 0.0831  -0.0049 0.0388  6   PHE D CB  
10171 C CG  . PHE D 6   ? 0.4658 0.5068 0.3023 0.0863  0.0211  0.0294  6   PHE D CG  
10172 C CD1 . PHE D 6   ? 0.4859 0.4989 0.2958 0.0918  0.0304  0.0382  6   PHE D CD1 
10173 C CD2 . PHE D 6   ? 0.4391 0.4808 0.2961 0.0825  0.0350  0.0132  6   PHE D CD2 
10174 C CE1 . PHE D 6   ? 0.5212 0.5083 0.3283 0.0931  0.0545  0.0301  6   PHE D CE1 
10175 C CE2 . PHE D 6   ? 0.4963 0.5138 0.3510 0.0834  0.0564  0.0061  6   PHE D CE2 
10176 C CZ  . PHE D 6   ? 0.5256 0.5166 0.3570 0.0885  0.0666  0.0142  6   PHE D CZ  
10177 N N   . ASP D 7   ? 0.5310 0.6268 0.3173 0.0478  -0.0678 0.0477  7   ASP D N   
10178 C CA  . ASP D 7   ? 0.5315 0.6631 0.3390 0.0387  -0.0940 0.0532  7   ASP D CA  
10179 C C   . ASP D 7   ? 0.5015 0.6361 0.3136 0.0239  -0.0907 0.0331  7   ASP D C   
10180 O O   . ASP D 7   ? 0.5127 0.6817 0.3642 0.0214  -0.1019 0.0348  7   ASP D O   
10181 C CB  . ASP D 7   ? 0.5885 0.7170 0.3548 0.0269  -0.1224 0.0672  7   ASP D CB  
10182 C CG  . ASP D 7   ? 0.6245 0.7761 0.4151 0.0422  -0.1382 0.0954  7   ASP D CG  
10183 O OD1 . ASP D 7   ? 0.6538 0.8099 0.4809 0.0631  -0.1199 0.1015  7   ASP D OD1 
10184 O OD2 . ASP D 7   ? 0.6889 0.8562 0.4671 0.0332  -0.1693 0.1118  7   ASP D OD2 
10185 N N   . GLN D 8   ? 0.5282 0.6271 0.3032 0.0143  -0.0744 0.0152  8   GLN D N   
10186 C CA  . GLN D 8   ? 0.5332 0.6332 0.3164 0.0022  -0.0692 -0.0022 8   GLN D CA  
10187 C C   . GLN D 8   ? 0.4813 0.6054 0.3192 0.0134  -0.0571 -0.0054 8   GLN D C   
10188 O O   . GLN D 8   ? 0.4404 0.5855 0.3031 0.0062  -0.0630 -0.0104 8   GLN D O   
10189 C CB  . GLN D 8   ? 0.5497 0.6056 0.2908 -0.0061 -0.0487 -0.0188 8   GLN D CB  
10190 C CG  . GLN D 8   ? 0.5235 0.5777 0.2771 -0.0160 -0.0402 -0.0351 8   GLN D CG  
10191 C CD  . GLN D 8   ? 0.5456 0.6047 0.2820 -0.0362 -0.0604 -0.0394 8   GLN D CD  
10192 O OE1 . GLN D 8   ? 0.6609 0.6872 0.3456 -0.0513 -0.0612 -0.0471 8   GLN D OE1 
10193 N NE2 . GLN D 8   ? 0.4981 0.5957 0.2773 -0.0377 -0.0748 -0.0354 8   GLN D NE2 
10194 N N   . PHE D 9   ? 0.4503 0.5691 0.3044 0.0292  -0.0394 -0.0032 9   PHE D N   
10195 C CA  . PHE D 9   ? 0.4107 0.5477 0.3085 0.0379  -0.0282 -0.0066 9   PHE D CA  
10196 C C   . PHE D 9   ? 0.3843 0.5590 0.3213 0.0438  -0.0410 0.0055  9   PHE D C   
10197 O O   . PHE D 9   ? 0.3597 0.5531 0.3267 0.0427  -0.0379 0.0009  9   PHE D O   
10198 C CB  . PHE D 9   ? 0.3948 0.5148 0.2973 0.0507  -0.0078 -0.0072 9   PHE D CB  
10199 C CG  . PHE D 9   ? 0.4247 0.5116 0.3006 0.0463  0.0084  -0.0177 9   PHE D CG  
10200 C CD1 . PHE D 9   ? 0.4219 0.5035 0.3063 0.0399  0.0184  -0.0303 9   PHE D CD1 
10201 C CD2 . PHE D 9   ? 0.4630 0.5239 0.3076 0.0493  0.0146  -0.0129 9   PHE D CD2 
10202 C CE1 . PHE D 9   ? 0.4361 0.4899 0.3047 0.0375  0.0350  -0.0375 9   PHE D CE1 
10203 C CE2 . PHE D 9   ? 0.4804 0.5111 0.3051 0.0457  0.0329  -0.0218 9   PHE D CE2 
10204 C CZ  . PHE D 9   ? 0.4423 0.4708 0.2816 0.0402  0.0432  -0.0338 9   PHE D CZ  
10205 N N   . LYS D 10  ? 0.4055 0.5916 0.3440 0.0503  -0.0548 0.0226  10  LYS D N   
10206 C CA  . LYS D 10  ? 0.3421 0.5666 0.3249 0.0570  -0.0664 0.0368  10  LYS D CA  
10207 C C   . LYS D 10  ? 0.4091 0.6576 0.4019 0.0405  -0.0847 0.0344  10  LYS D C   
10208 O O   . LYS D 10  ? 0.3585 0.6349 0.3930 0.0420  -0.0831 0.0357  10  LYS D O   
10209 C CB  . LYS D 10  ? 0.4697 0.7007 0.4519 0.0669  -0.0797 0.0584  10  LYS D CB  
10210 C CG  . LYS D 10  ? 0.4959 0.7001 0.4674 0.0825  -0.0603 0.0612  10  LYS D CG  
10211 C CD  . LYS D 10  ? 0.4839 0.6924 0.4556 0.0942  -0.0727 0.0854  10  LYS D CD  
10212 C CE  . LYS D 10  ? 0.5103 0.7570 0.5412 0.1085  -0.0774 0.1036  10  LYS D CE  
10213 N NZ  . LYS D 10  ? 0.5487 0.8370 0.6114 0.0986  -0.0997 0.1098  10  LYS D NZ  
10214 N N   . THR D 11  ? 0.3967 0.6317 0.3491 0.0234  -0.1007 0.0306  11  THR D N   
10215 C CA  . THR D 11  ? 0.4245 0.6746 0.3791 0.0039  -0.1169 0.0251  11  THR D CA  
10216 C C   . THR D 11  ? 0.3574 0.6049 0.3276 -0.0001 -0.0994 0.0084  11  THR D C   
10217 O O   . THR D 11  ? 0.3773 0.6522 0.3810 -0.0059 -0.1050 0.0094  11  THR D O   
10218 C CB  . THR D 11  ? 0.4369 0.6592 0.3325 -0.0155 -0.1313 0.0192  11  THR D CB  
10219 O OG1 . THR D 11  ? 0.4777 0.7049 0.3565 -0.0142 -0.1523 0.0374  11  THR D OG1 
10220 C CG2 . THR D 11  ? 0.4540 0.6851 0.3468 -0.0385 -0.1464 0.0107  11  THR D CG2 
10221 N N   . TRP D 12  ? 0.3435 0.5584 0.2909 0.0025  -0.0783 -0.0054 12  TRP D N   
10222 C CA  . TRP D 12  ? 0.3759 0.5883 0.3379 -0.0009 -0.0638 -0.0182 12  TRP D CA  
10223 C C   . TRP D 12  ? 0.3801 0.6202 0.3885 0.0105  -0.0562 -0.0125 12  TRP D C   
10224 O O   . TRP D 12  ? 0.3773 0.6300 0.4058 0.0041  -0.0537 -0.0170 12  TRP D O   
10225 C CB  . TRP D 12  ? 0.3489 0.5264 0.2873 0.0026  -0.0436 -0.0296 12  TRP D CB  
10226 C CG  . TRP D 12  ? 0.4057 0.5519 0.3034 -0.0114 -0.0426 -0.0404 12  TRP D CG  
10227 C CD1 . TRP D 12  ? 0.3946 0.5379 0.2747 -0.0290 -0.0554 -0.0452 12  TRP D CD1 
10228 C CD2 . TRP D 12  ? 0.4211 0.5320 0.2915 -0.0092 -0.0252 -0.0481 12  TRP D CD2 
10229 N NE1 . TRP D 12  ? 0.4228 0.5269 0.2621 -0.0376 -0.0449 -0.0566 12  TRP D NE1 
10230 C CE2 . TRP D 12  ? 0.4194 0.5047 0.2553 -0.0247 -0.0254 -0.0579 12  TRP D CE2 
10231 C CE3 . TRP D 12  ? 0.4012 0.4993 0.2762 0.0035  -0.0077 -0.0479 12  TRP D CE3 
10232 C CZ2 . TRP D 12  ? 0.5100 0.5565 0.3161 -0.0258 -0.0061 -0.0667 12  TRP D CZ2 
10233 C CZ3 . TRP D 12  ? 0.4108 0.4756 0.2613 0.0017  0.0086  -0.0555 12  TRP D CZ3 
10234 C CH2 . TRP D 12  ? 0.4545 0.4936 0.2718 -0.0118 0.0108  -0.0646 12  TRP D CH2 
10235 N N   . TYR D 13  ? 0.3371 0.5830 0.3604 0.0270  -0.0499 -0.0029 13  TYR D N   
10236 C CA  . TYR D 13  ? 0.3354 0.6011 0.3977 0.0377  -0.0383 0.0012  13  TYR D CA  
10237 C C   . TYR D 13  ? 0.3470 0.6504 0.4464 0.0350  -0.0514 0.0125  13  TYR D C   
10238 O O   . TYR D 13  ? 0.3133 0.6322 0.4387 0.0322  -0.0443 0.0100  13  TYR D O   
10239 C CB  . TYR D 13  ? 0.3096 0.5661 0.3759 0.0554  -0.0257 0.0076  13  TYR D CB  
10240 C CG  . TYR D 13  ? 0.3454 0.6183 0.4492 0.0681  -0.0118 0.0136  13  TYR D CG  
10241 C CD1 . TYR D 13  ? 0.3624 0.6265 0.4698 0.0677  0.0066  0.0027  13  TYR D CD1 
10242 C CD2 . TYR D 13  ? 0.3587 0.6530 0.4927 0.0806  -0.0158 0.0309  13  TYR D CD2 
10243 C CE1 . TYR D 13  ? 0.3405 0.6132 0.4760 0.0784  0.0233  0.0067  13  TYR D CE1 
10244 C CE2 . TYR D 13  ? 0.3959 0.7011 0.5652 0.0935  0.0019  0.0362  13  TYR D CE2 
10245 C CZ  . TYR D 13  ? 0.4343 0.7265 0.6014 0.0918  0.0229  0.0228  13  TYR D CZ  
10246 O OH  . TYR D 13  ? 0.4790 0.7770 0.6762 0.1040  0.0437  0.0271  13  TYR D OH  
10247 N N   . GLU D 14  ? 0.3057 0.6249 0.4084 0.0343  -0.0717 0.0263  14  GLU D N   
10248 C CA  . GLU D 14  ? 0.3201 0.6803 0.4662 0.0314  -0.0864 0.0400  14  GLU D CA  
10249 C C   . GLU D 14  ? 0.3432 0.7121 0.4882 0.0099  -0.0971 0.0312  14  GLU D C   
10250 O O   . GLU D 14  ? 0.3547 0.7552 0.5423 0.0068  -0.0988 0.0372  14  GLU D O   
10251 C CB  . GLU D 14  ? 0.3328 0.7091 0.4827 0.0346  -0.1098 0.0596  14  GLU D CB  
10252 C CG  . GLU D 14  ? 0.3729 0.7478 0.5407 0.0586  -0.0965 0.0725  14  GLU D CG  
10253 C CD  . GLU D 14  ? 0.4701 0.8454 0.6242 0.0636  -0.1162 0.0904  14  GLU D CD  
10254 O OE1 . GLU D 14  ? 0.5360 0.9136 0.6631 0.0469  -0.1430 0.0936  14  GLU D OE1 
10255 O OE2 . GLU D 14  ? 0.5146 0.8850 0.6821 0.0837  -0.1041 0.1017  14  GLU D OE2 
10256 N N   . LYS D 15  ? 0.3366 0.6763 0.4351 -0.0051 -0.1022 0.0173  15  LYS D N   
10257 C CA  . LYS D 15  ? 0.3384 0.6794 0.4294 -0.0272 -0.1127 0.0084  15  LYS D CA  
10258 C C   . LYS D 15  ? 0.3412 0.6552 0.4158 -0.0312 -0.0926 -0.0091 15  LYS D C   
10259 O O   . LYS D 15  ? 0.3440 0.6390 0.3926 -0.0480 -0.0964 -0.0202 15  LYS D O   
10260 C CB  . LYS D 15  ? 0.4406 0.7676 0.4895 -0.0441 -0.1360 0.0075  15  LYS D CB  
10261 C CG  . LYS D 15  ? 0.4220 0.7824 0.4908 -0.0441 -0.1633 0.0287  15  LYS D CG  
10262 C CD  . LYS D 15  ? 0.5102 0.8739 0.5543 -0.0709 -0.1942 0.0293  15  LYS D CD  
10263 C CE  . LYS D 15  ? 0.5708 0.9612 0.6507 -0.0880 -0.2011 0.0266  15  LYS D CE  
10264 N NZ  . LYS D 15  ? 0.5169 0.9436 0.6649 -0.0719 -0.1850 0.0353  15  LYS D NZ  
10265 N N   . ARG D 16  ? 0.3630 0.6741 0.4529 -0.0165 -0.0712 -0.0108 16  ARG D N   
10266 C CA  . ARG D 16  ? 0.3084 0.5939 0.3822 -0.0188 -0.0544 -0.0242 16  ARG D CA  
10267 C C   . ARG D 16  ? 0.2958 0.5864 0.3781 -0.0351 -0.0567 -0.0296 16  ARG D C   
10268 O O   . ARG D 16  ? 0.3260 0.5908 0.3859 -0.0431 -0.0507 -0.0401 16  ARG D O   
10269 C CB  . ARG D 16  ? 0.3271 0.6123 0.4162 -0.0033 -0.0350 -0.0233 16  ARG D CB  
10270 C CG  . ARG D 16  ? 0.3258 0.6409 0.4553 0.0007  -0.0297 -0.0152 16  ARG D CG  
10271 C CD  . ARG D 16  ? 0.2872 0.5920 0.4191 0.0109  -0.0084 -0.0185 16  ARG D CD  
10272 N NE  . ARG D 16  ? 0.2981 0.5814 0.4089 0.0024  -0.0024 -0.0287 16  ARG D NE  
10273 C CZ  . ARG D 16  ? 0.2906 0.5584 0.3918 0.0066  0.0116  -0.0330 16  ARG D CZ  
10274 N NH1 . ARG D 16  ? 0.2618 0.5289 0.3683 0.0181  0.0236  -0.0307 16  ARG D NH1 
10275 N NH2 . ARG D 16  ? 0.2574 0.5080 0.3422 -0.0012 0.0132  -0.0391 16  ARG D NH2 
10276 N N   . HIS D 17  ? 0.2539 0.5773 0.3716 -0.0401 -0.0638 -0.0215 17  HIS D N   
10277 C CA  . HIS D 17  ? 0.3047 0.6317 0.4323 -0.0559 -0.0634 -0.0262 17  HIS D CA  
10278 C C   . HIS D 17  ? 0.3327 0.6476 0.4356 -0.0763 -0.0805 -0.0326 17  HIS D C   
10279 O O   . HIS D 17  ? 0.3548 0.6476 0.4415 -0.0886 -0.0752 -0.0428 17  HIS D O   
10280 C CB  . HIS D 17  ? 0.2994 0.6651 0.4760 -0.0554 -0.0627 -0.0153 17  HIS D CB  
10281 C CG  . HIS D 17  ? 0.2812 0.6509 0.4756 -0.0384 -0.0407 -0.0120 17  HIS D CG  
10282 N ND1 . HIS D 17  ? 0.2562 0.5992 0.4288 -0.0345 -0.0236 -0.0204 17  HIS D ND1 
10283 C CD2 . HIS D 17  ? 0.2705 0.6651 0.5003 -0.0249 -0.0328 -0.0010 17  HIS D CD2 
10284 C CE1 . HIS D 17  ? 0.2707 0.6199 0.4587 -0.0217 -0.0068 -0.0163 17  HIS D CE1 
10285 N NE2 . HIS D 17  ? 0.2557 0.6345 0.4788 -0.0150 -0.0096 -0.0052 17  HIS D NE2 
10286 N N   . ASP D 18  ? 0.3270 0.6524 0.4230 -0.0806 -0.1008 -0.0266 18  ASP D N   
10287 C CA  . ASP D 18  ? 0.3620 0.6676 0.4212 -0.1016 -0.1171 -0.0345 18  ASP D CA  
10288 C C   . ASP D 18  ? 0.3807 0.6375 0.3904 -0.1012 -0.1035 -0.0489 18  ASP D C   
10289 O O   . ASP D 18  ? 0.4151 0.6444 0.3967 -0.1185 -0.1033 -0.0608 18  ASP D O   
10290 C CB  . ASP D 18  ? 0.3846 0.7101 0.4415 -0.1054 -0.1430 -0.0228 18  ASP D CB  
10291 C CG  . ASP D 18  ? 0.4409 0.8120 0.5441 -0.1172 -0.1629 -0.0105 18  ASP D CG  
10292 O OD1 . ASP D 18  ? 0.4616 0.8410 0.5869 -0.1295 -0.1583 -0.0150 18  ASP D OD1 
10293 O OD2 . ASP D 18  ? 0.4585 0.8591 0.5813 -0.1127 -0.1818 0.0058  18  ASP D OD2 
10294 N N   . TYR D 19  ? 0.3640 0.6081 0.3642 -0.0820 -0.0904 -0.0479 19  TYR D N   
10295 C CA  . TYR D 19  ? 0.4071 0.6080 0.3694 -0.0805 -0.0748 -0.0599 19  TYR D CA  
10296 C C   . TYR D 19  ? 0.3827 0.5682 0.3515 -0.0850 -0.0593 -0.0685 19  TYR D C   
10297 O O   . TYR D 19  ? 0.4001 0.5514 0.3404 -0.0949 -0.0521 -0.0793 19  TYR D O   
10298 C CB  . TYR D 19  ? 0.4116 0.6064 0.3723 -0.0598 -0.0626 -0.0562 19  TYR D CB  
10299 C CG  . TYR D 19  ? 0.3757 0.5315 0.3101 -0.0568 -0.0439 -0.0665 19  TYR D CG  
10300 C CD1 . TYR D 19  ? 0.3621 0.5126 0.3147 -0.0508 -0.0278 -0.0694 19  TYR D CD1 
10301 C CD2 . TYR D 19  ? 0.3955 0.5203 0.2888 -0.0603 -0.0419 -0.0720 19  TYR D CD2 
10302 C CE1 . TYR D 19  ? 0.3934 0.5130 0.3314 -0.0472 -0.0116 -0.0758 19  TYR D CE1 
10303 C CE2 . TYR D 19  ? 0.4134 0.5045 0.2901 -0.0566 -0.0219 -0.0801 19  TYR D CE2 
10304 C CZ  . TYR D 19  ? 0.4087 0.4993 0.3113 -0.0498 -0.0074 -0.0814 19  TYR D CZ  
10305 O OH  . TYR D 19  ? 0.4291 0.4890 0.3214 -0.0458 0.0118  -0.0870 19  TYR D OH  
10306 N N   . ALA D 20  ? 0.3050 0.5133 0.3101 -0.0780 -0.0529 -0.0629 20  ALA D N   
10307 C CA  . ALA D 20  ? 0.3271 0.5219 0.3393 -0.0800 -0.0386 -0.0674 20  ALA D CA  
10308 C C   . ALA D 20  ? 0.3458 0.5319 0.3535 -0.1005 -0.0432 -0.0735 20  ALA D C   
10309 O O   . ALA D 20  ? 0.3897 0.5446 0.3818 -0.1059 -0.0320 -0.0814 20  ALA D O   
10310 C CB  . ALA D 20  ? 0.2605 0.4803 0.3056 -0.0696 -0.0318 -0.0592 20  ALA D CB  
10311 N N   . ARG D 21  ? 0.3342 0.5473 0.3579 -0.1126 -0.0592 -0.0694 21  ARG D N   
10312 C CA  . ARG D 21  ? 0.3869 0.5909 0.4057 -0.1351 -0.0647 -0.0760 21  ARG D CA  
10313 C C   . ARG D 21  ? 0.4515 0.6142 0.4224 -0.1477 -0.0661 -0.0888 21  ARG D C   
10314 O O   . ARG D 21  ? 0.4923 0.6247 0.4479 -0.1610 -0.0575 -0.0987 21  ARG D O   
10315 C CB  . ARG D 21  ? 0.4036 0.6480 0.4517 -0.1470 -0.0846 -0.0677 21  ARG D CB  
10316 C CG  . ARG D 21  ? 0.3009 0.5801 0.3959 -0.1370 -0.0773 -0.0567 21  ARG D CG  
10317 C CD  . ARG D 21  ? 0.3647 0.6850 0.4962 -0.1500 -0.0951 -0.0477 21  ARG D CD  
10318 N NE  . ARG D 21  ? 0.4319 0.7795 0.5743 -0.1412 -0.1110 -0.0371 21  ARG D NE  
10319 C CZ  . ARG D 21  ? 0.4000 0.7809 0.5820 -0.1237 -0.1062 -0.0239 21  ARG D CZ  
10320 N NH1 . ARG D 21  ? 0.2993 0.6897 0.5095 -0.1149 -0.0859 -0.0210 21  ARG D NH1 
10321 N NH2 . ARG D 21  ? 0.3731 0.7757 0.5648 -0.1151 -0.1209 -0.0130 21  ARG D NH2 
10322 N N   . ASP D 22  ? 0.4364 0.5943 0.3810 -0.1446 -0.0755 -0.0888 22  ASP D N   
10323 C CA  . ASP D 22  ? 0.5260 0.6400 0.4176 -0.1574 -0.0744 -0.1016 22  ASP D CA  
10324 C C   . ASP D 22  ? 0.5416 0.6151 0.4175 -0.1466 -0.0470 -0.1098 22  ASP D C   
10325 O O   . ASP D 22  ? 0.5341 0.5655 0.3778 -0.1592 -0.0362 -0.1226 22  ASP D O   
10326 C CB  . ASP D 22  ? 0.5639 0.6812 0.4284 -0.1555 -0.0899 -0.0973 22  ASP D CB  
10327 C CG  . ASP D 22  ? 0.6165 0.6823 0.4175 -0.1690 -0.0855 -0.1113 22  ASP D CG  
10328 O OD1 . ASP D 22  ? 0.6432 0.6924 0.4156 -0.1944 -0.0971 -0.1201 22  ASP D OD1 
10329 O OD2 . ASP D 22  ? 0.6960 0.7354 0.4745 -0.1551 -0.0684 -0.1141 22  ASP D OD2 
10330 N N   . TRP D 23  ? 0.4778 0.5626 0.3770 -0.1239 -0.0352 -0.1023 23  TRP D N   
10331 C CA  . TRP D 23  ? 0.4748 0.5295 0.3714 -0.1126 -0.0112 -0.1063 23  TRP D CA  
10332 C C   . TRP D 23  ? 0.5021 0.5414 0.4104 -0.1211 -0.0005 -0.1102 23  TRP D C   
10333 O O   . TRP D 23  ? 0.5458 0.5460 0.4383 -0.1222 0.0178  -0.1177 23  TRP D O   
10334 C CB  . TRP D 23  ? 0.4465 0.5237 0.3716 -0.0904 -0.0059 -0.0957 23  TRP D CB  
10335 C CG  . TRP D 23  ? 0.4377 0.4903 0.3661 -0.0791 0.0148  -0.0968 23  TRP D CG  
10336 C CD1 . TRP D 23  ? 0.4544 0.4853 0.3670 -0.0700 0.0268  -0.0991 23  TRP D CD1 
10337 C CD2 . TRP D 23  ? 0.3883 0.4376 0.3415 -0.0755 0.0255  -0.0931 23  TRP D CD2 
10338 N NE1 . TRP D 23  ? 0.4973 0.5139 0.4282 -0.0609 0.0441  -0.0969 23  TRP D NE1 
10339 C CE2 . TRP D 23  ? 0.3982 0.4257 0.3530 -0.0641 0.0423  -0.0925 23  TRP D CE2 
10340 C CE3 . TRP D 23  ? 0.3954 0.4568 0.3693 -0.0816 0.0229  -0.0891 23  TRP D CE3 
10341 C CZ2 . TRP D 23  ? 0.3959 0.4167 0.3757 -0.0578 0.0536  -0.0862 23  TRP D CZ2 
10342 C CZ3 . TRP D 23  ? 0.4274 0.4781 0.4195 -0.0756 0.0351  -0.0836 23  TRP D CZ3 
10343 C CH2 . TRP D 23  ? 0.3556 0.3877 0.3518 -0.0634 0.0488  -0.0813 23  TRP D CH2 
10344 N N   . LYS D 24  ? 0.4359 0.5031 0.3716 -0.1280 -0.0101 -0.1047 24  LYS D N   
10345 C CA  . LYS D 24  ? 0.4996 0.5500 0.4452 -0.1367 0.0006  -0.1072 24  LYS D CA  
10346 C C   . LYS D 24  ? 0.5249 0.5374 0.4366 -0.1586 0.0025  -0.1214 24  LYS D C   
10347 O O   . LYS D 24  ? 0.5386 0.5145 0.4436 -0.1614 0.0210  -0.1272 24  LYS D O   
10348 C CB  . LYS D 24  ? 0.4674 0.5538 0.4477 -0.1407 -0.0080 -0.0983 24  LYS D CB  
10349 C CG  . LYS D 24  ? 0.3941 0.5067 0.4017 -0.1212 -0.0042 -0.0862 24  LYS D CG  
10350 C CD  . LYS D 24  ? 0.4249 0.5720 0.4630 -0.1253 -0.0102 -0.0778 24  LYS D CD  
10351 C CE  . LYS D 24  ? 0.4528 0.5863 0.5011 -0.1325 0.0007  -0.0758 24  LYS D CE  
10352 N NZ  . LYS D 24  ? 0.4337 0.5989 0.5093 -0.1411 -0.0043 -0.0691 24  LYS D NZ  
10353 N N   . VAL D 25  ? 0.5709 0.5905 0.4611 -0.1753 -0.0166 -0.1265 25  VAL D N   
10354 C CA  . VAL D 25  ? 0.6145 0.5939 0.4657 -0.1999 -0.0156 -0.1417 25  VAL D CA  
10355 C C   . VAL D 25  ? 0.6692 0.5968 0.4786 -0.1951 0.0053  -0.1528 25  VAL D C   
10356 O O   . VAL D 25  ? 0.7556 0.6360 0.5402 -0.2072 0.0225  -0.1654 25  VAL D O   
10357 C CB  . VAL D 25  ? 0.7116 0.7116 0.5475 -0.2222 -0.0451 -0.1433 25  VAL D CB  
10358 C CG1 . VAL D 25  ? 0.6037 0.6626 0.4908 -0.2206 -0.0634 -0.1287 25  VAL D CG1 
10359 C CG2 . VAL D 25  ? 0.7358 0.7323 0.5363 -0.2180 -0.0553 -0.1437 25  VAL D CG2 
10360 N N   . ARG D 26  ? 0.6491 0.5823 0.4517 -0.1773 0.0074  -0.1483 26  ARG D N   
10361 C CA  . ARG D 26  ? 0.7493 0.6343 0.5120 -0.1735 0.0286  -0.1584 26  ARG D CA  
10362 C C   . ARG D 26  ? 0.7182 0.5775 0.5028 -0.1583 0.0591  -0.1577 26  ARG D C   
10363 O O   . ARG D 26  ? 0.7697 0.5780 0.5257 -0.1615 0.0832  -0.1690 26  ARG D O   
10364 C CB  . ARG D 26  ? 0.6810 0.5812 0.4347 -0.1584 0.0229  -0.1518 26  ARG D CB  
10365 C CG  . ARG D 26  ? 0.7752 0.6786 0.4869 -0.1740 -0.0010 -0.1543 26  ARG D CG  
10366 C CD  . ARG D 26  ? 0.7635 0.6742 0.4650 -0.1569 -0.0011 -0.1469 26  ARG D CD  
10367 N NE  . ARG D 26  ? 0.6695 0.6279 0.4223 -0.1349 -0.0072 -0.1312 26  ARG D NE  
10368 C CZ  . ARG D 26  ? 0.7044 0.6624 0.4668 -0.1143 0.0068  -0.1257 26  ARG D CZ  
10369 N NH1 . ARG D 26  ? 0.7882 0.7045 0.5189 -0.1112 0.0287  -0.1332 26  ARG D NH1 
10370 N NH2 . ARG D 26  ? 0.5912 0.5894 0.3951 -0.0975 0.0002  -0.1129 26  ARG D NH2 
10371 N N   . THR D 27  ? 0.6474 0.5407 0.4822 -0.1412 0.0588  -0.1435 27  THR D N   
10372 C CA  . THR D 27  ? 0.5775 0.4563 0.4400 -0.1236 0.0825  -0.1374 27  THR D CA  
10373 C C   . THR D 27  ? 0.5839 0.4576 0.4719 -0.1278 0.0888  -0.1338 27  THR D C   
10374 O O   . THR D 27  ? 0.6685 0.5181 0.5733 -0.1174 0.1107  -0.1301 27  THR D O   
10375 C CB  . THR D 27  ? 0.5668 0.4840 0.4641 -0.1015 0.0773  -0.1224 27  THR D CB  
10376 O OG1 . THR D 27  ? 0.5311 0.4894 0.4586 -0.1012 0.0601  -0.1121 27  THR D OG1 
10377 C CG2 . THR D 27  ? 0.5405 0.4664 0.4161 -0.0967 0.0696  -0.1239 27  THR D CG2 
10378 N N   . GLY D 28  ? 0.5821 0.5464 0.4959 -0.0689 -0.0346 -0.0992 28  GLY D N   
10379 C CA  . GLY D 28  ? 0.5730 0.5311 0.4944 -0.0746 -0.0311 -0.0997 28  GLY D CA  
10380 C C   . GLY D 28  ? 0.5448 0.5028 0.4749 -0.0712 -0.0263 -0.0926 28  GLY D C   
10381 O O   . GLY D 28  ? 0.5528 0.5022 0.4866 -0.0746 -0.0222 -0.0924 28  GLY D O   
10382 N N   . GLY D 29  ? 0.5062 0.4727 0.4391 -0.0643 -0.0265 -0.0866 29  GLY D N   
10383 C CA  . GLY D 29  ? 0.4776 0.4437 0.4177 -0.0610 -0.0222 -0.0802 29  GLY D CA  
10384 C C   . GLY D 29  ? 0.4461 0.4242 0.3992 -0.0640 -0.0238 -0.0777 29  GLY D C   
10385 O O   . GLY D 29  ? 0.5052 0.4942 0.4631 -0.0684 -0.0285 -0.0806 29  GLY D O   
10386 N N   . GLN D 30  ? 0.4217 0.3974 0.3802 -0.0617 -0.0197 -0.0725 30  GLN D N   
10387 C CA  . GLN D 30  ? 0.4135 0.3987 0.3832 -0.0629 -0.0197 -0.0689 30  GLN D CA  
10388 C C   . GLN D 30  ? 0.4146 0.4103 0.3863 -0.0565 -0.0216 -0.0643 30  GLN D C   
10389 O O   . GLN D 30  ? 0.3976 0.3894 0.3630 -0.0507 -0.0204 -0.0619 30  GLN D O   
10390 C CB  . GLN D 30  ? 0.4633 0.4387 0.4356 -0.0629 -0.0141 -0.0655 30  GLN D CB  
10391 C CG  . GLN D 30  ? 0.5353 0.4997 0.5070 -0.0695 -0.0113 -0.0691 30  GLN D CG  
10392 C CD  . GLN D 30  ? 0.5952 0.5530 0.5708 -0.0689 -0.0064 -0.0645 30  GLN D CD  
10393 O OE1 . GLN D 30  ? 0.5320 0.4980 0.5154 -0.0691 -0.0061 -0.0611 30  GLN D OE1 
10394 N NE2 . GLN D 30  ? 0.6584 0.6010 0.6278 -0.0678 -0.0023 -0.0644 30  GLN D NE2 
10395 N N   . VAL D 31  ? 0.3473 0.3560 0.3281 -0.0577 -0.0240 -0.0629 31  VAL D N   
10396 C CA  . VAL D 31  ? 0.3389 0.3569 0.3225 -0.0517 -0.0253 -0.0581 31  VAL D CA  
10397 C C   . VAL D 31  ? 0.3396 0.3572 0.3304 -0.0510 -0.0214 -0.0535 31  VAL D C   
10398 O O   . VAL D 31  ? 0.3307 0.3479 0.3277 -0.0561 -0.0195 -0.0544 31  VAL D O   
10399 C CB  . VAL D 31  ? 0.3275 0.3609 0.3153 -0.0521 -0.0311 -0.0598 31  VAL D CB  
10400 C CG1 . VAL D 31  ? 0.2965 0.3381 0.2867 -0.0453 -0.0319 -0.0543 31  VAL D CG1 
10401 C CG2 . VAL D 31  ? 0.3658 0.3986 0.3442 -0.0523 -0.0354 -0.0644 31  VAL D CG2 
10402 N N   . VAL D 32  ? 0.2976 0.3149 0.2871 -0.0450 -0.0200 -0.0486 32  VAL D N   
10403 C CA  . VAL D 32  ? 0.3118 0.3275 0.3064 -0.0439 -0.0163 -0.0444 32  VAL D CA  
10404 C C   . VAL D 32  ? 0.3242 0.3492 0.3217 -0.0390 -0.0178 -0.0407 32  VAL D C   
10405 O O   . VAL D 32  ? 0.3108 0.3353 0.3028 -0.0341 -0.0188 -0.0389 32  VAL D O   
10406 C CB  . VAL D 32  ? 0.3471 0.3501 0.3366 -0.0416 -0.0122 -0.0421 32  VAL D CB  
10407 C CG1 . VAL D 32  ? 0.3957 0.3956 0.3777 -0.0367 -0.0127 -0.0411 32  VAL D CG1 
10408 C CG2 . VAL D 32  ? 0.3206 0.3227 0.3146 -0.0401 -0.0092 -0.0375 32  VAL D CG2 
10409 N N   . ALA D 33  ? 0.2739 0.3072 0.2797 -0.0405 -0.0178 -0.0398 33  ALA D N   
10410 C CA  . ALA D 33  ? 0.2719 0.3128 0.2805 -0.0354 -0.0185 -0.0360 33  ALA D CA  
10411 C C   . ALA D 33  ? 0.3103 0.3428 0.3159 -0.0317 -0.0147 -0.0316 33  ALA D C   
10412 O O   . ALA D 33  ? 0.3046 0.3308 0.3117 -0.0338 -0.0113 -0.0307 33  ALA D O   
10413 C CB  . ALA D 33  ? 0.2490 0.3012 0.2678 -0.0380 -0.0188 -0.0364 33  ALA D CB  
10414 N N   . THR D 34  ? 0.2841 0.3159 0.2850 -0.0262 -0.0154 -0.0289 34  THR D N   
10415 C CA  . THR D 34  ? 0.2793 0.3030 0.2770 -0.0233 -0.0122 -0.0253 34  THR D CA  
10416 C C   . THR D 34  ? 0.2952 0.3236 0.2953 -0.0194 -0.0120 -0.0220 34  THR D C   
10417 O O   . THR D 34  ? 0.3068 0.3439 0.3086 -0.0171 -0.0146 -0.0220 34  THR D O   
10418 C CB  . THR D 34  ? 0.2870 0.3040 0.2769 -0.0207 -0.0122 -0.0247 34  THR D CB  
10419 O OG1 . THR D 34  ? 0.3081 0.3298 0.2946 -0.0168 -0.0147 -0.0239 34  THR D OG1 
10420 C CG2 . THR D 34  ? 0.2872 0.2991 0.2739 -0.0240 -0.0122 -0.0284 34  THR D CG2 
10421 N N   . MET D 35  ? 0.2821 0.3048 0.2820 -0.0185 -0.0090 -0.0193 35  MET D N   
10422 C CA  . MET D 35  ? 0.2742 0.2993 0.2751 -0.0147 -0.0082 -0.0163 35  MET D CA  
10423 C C   . MET D 35  ? 0.3078 0.3241 0.3030 -0.0122 -0.0065 -0.0136 35  MET D C   
10424 O O   . MET D 35  ? 0.3323 0.3415 0.3258 -0.0141 -0.0048 -0.0136 35  MET D O   
10425 C CB  . MET D 35  ? 0.3125 0.3405 0.3193 -0.0165 -0.0061 -0.0159 35  MET D CB  
10426 C CG  . MET D 35  ? 0.3159 0.3554 0.3304 -0.0190 -0.0077 -0.0184 35  MET D CG  
10427 S SD  . MET D 35  ? 0.3186 0.3596 0.3401 -0.0231 -0.0039 -0.0184 35  MET D SD  
10428 C CE  . MET D 35  ? 0.3024 0.3574 0.3329 -0.0271 -0.0067 -0.0222 35  MET D CE  
10429 N N   . CYS D 36  ? 0.3122 0.3291 0.3048 -0.0079 -0.0067 -0.0113 36  CYS D N   
10430 C CA  . CYS D 36  ? 0.3523 0.3613 0.3392 -0.0056 -0.0054 -0.0088 36  CYS D CA  
10431 C C   . CYS D 36  ? 0.3683 0.3732 0.3506 -0.0059 -0.0059 -0.0093 36  CYS D C   
10432 O O   . CYS D 36  ? 0.3365 0.3406 0.3193 -0.0087 -0.0061 -0.0115 36  CYS D O   
10433 C CB  . CYS D 36  ? 0.3315 0.3344 0.3188 -0.0070 -0.0028 -0.0077 36  CYS D CB  
10434 S SG  . CYS D 36  ? 0.3173 0.3116 0.2986 -0.0048 -0.0015 -0.0050 36  CYS D SG  
10435 N N   . THR D 37  ? 0.3139 0.3156 0.2912 -0.0029 -0.0056 -0.0072 37  THR D N   
10436 C CA  . THR D 37  ? 0.2549 0.2528 0.2274 -0.0029 -0.0053 -0.0073 37  THR D CA  
10437 C C   . THR D 37  ? 0.3197 0.3120 0.2927 -0.0054 -0.0032 -0.0074 37  THR D C   
10438 O O   . THR D 37  ? 0.3121 0.3020 0.2823 -0.0057 -0.0025 -0.0077 37  THR D O   
10439 C CB  . THR D 37  ? 0.3293 0.3240 0.2961 0.0006  -0.0047 -0.0045 37  THR D CB  
10440 O OG1 . THR D 37  ? 0.3349 0.3251 0.3021 0.0010  -0.0029 -0.0025 37  THR D OG1 
10441 C CG2 . THR D 37  ? 0.3271 0.3277 0.2926 0.0041  -0.0071 -0.0042 37  THR D CG2 
10442 N N   . TYR D 38  ? 0.3407 0.3313 0.3171 -0.0071 -0.0023 -0.0072 38  TYR D N   
10443 C CA  . TYR D 38  ? 0.2410 0.2272 0.2182 -0.0090 -0.0010 -0.0073 38  TYR D CA  
10444 C C   . TYR D 38  ? 0.2839 0.2707 0.2632 -0.0112 -0.0012 -0.0098 38  TYR D C   
10445 O O   . TYR D 38  ? 0.3147 0.2980 0.2946 -0.0121 -0.0002 -0.0099 38  TYR D O   
10446 C CB  . TYR D 38  ? 0.2793 0.2627 0.2580 -0.0096 -0.0002 -0.0059 38  TYR D CB  
10447 C CG  . TYR D 38  ? 0.3120 0.2917 0.2878 -0.0083 0.0006  -0.0037 38  TYR D CG  
10448 C CD1 . TYR D 38  ? 0.2770 0.2541 0.2514 -0.0087 0.0014  -0.0031 38  TYR D CD1 
10449 C CD2 . TYR D 38  ? 0.3237 0.3023 0.2982 -0.0069 0.0008  -0.0025 38  TYR D CD2 
10450 C CE1 . TYR D 38  ? 0.2967 0.2701 0.2687 -0.0085 0.0023  -0.0013 38  TYR D CE1 
10451 C CE2 . TYR D 38  ? 0.3157 0.2895 0.2869 -0.0062 0.0017  -0.0008 38  TYR D CE2 
10452 C CZ  . TYR D 38  ? 0.3252 0.2964 0.2953 -0.0074 0.0023  -0.0003 38  TYR D CZ  
10453 O OH  . TYR D 38  ? 0.3109 0.2772 0.2780 -0.0076 0.0033  0.0012  38  TYR D OH  
10454 N N   . THR D 39  ? 0.2978 0.2886 0.2781 -0.0121 -0.0026 -0.0119 39  THR D N   
10455 C CA  . THR D 39  ? 0.3055 0.2955 0.2868 -0.0146 -0.0026 -0.0147 39  THR D CA  
10456 C C   . THR D 39  ? 0.2842 0.2705 0.2623 -0.0140 -0.0017 -0.0154 39  THR D C   
10457 O O   . THR D 39  ? 0.2780 0.2651 0.2525 -0.0122 -0.0018 -0.0150 39  THR D O   
10458 C CB  . THR D 39  ? 0.3250 0.3206 0.3075 -0.0159 -0.0047 -0.0172 39  THR D CB  
10459 O OG1 . THR D 39  ? 0.3311 0.3305 0.3181 -0.0170 -0.0049 -0.0169 39  THR D OG1 
10460 C CG2 . THR D 39  ? 0.2792 0.2723 0.2611 -0.0187 -0.0047 -0.0206 39  THR D CG2 
10461 N N   . PRO D 40  ? 0.3477 0.3298 0.3267 -0.0150 -0.0003 -0.0160 40  PRO D N   
10462 C CA  . PRO D 40  ? 0.3501 0.3293 0.3265 -0.0138 0.0011  -0.0165 40  PRO D CA  
10463 C C   . PRO D 40  ? 0.3099 0.2888 0.2832 -0.0147 0.0005  -0.0199 40  PRO D C   
10464 O O   . PRO D 40  ? 0.2961 0.2715 0.2694 -0.0162 0.0011  -0.0222 40  PRO D O   
10465 C CB  . PRO D 40  ? 0.3779 0.3530 0.3568 -0.0139 0.0025  -0.0156 40  PRO D CB  
10466 C CG  . PRO D 40  ? 0.3471 0.3215 0.3283 -0.0161 0.0019  -0.0161 40  PRO D CG  
10467 C CD  . PRO D 40  ? 0.3117 0.2910 0.2936 -0.0166 0.0004  -0.0157 40  PRO D CD  
10468 N N   . GLU D 41  ? 0.3306 0.3129 0.3005 -0.0137 -0.0008 -0.0204 41  GLU D N   
10469 C CA  . GLU D 41  ? 0.3500 0.3330 0.3168 -0.0150 -0.0023 -0.0240 41  GLU D CA  
10470 C C   . GLU D 41  ? 0.3133 0.2912 0.2759 -0.0146 -0.0003 -0.0261 41  GLU D C   
10471 O O   . GLU D 41  ? 0.3636 0.3400 0.3238 -0.0165 -0.0013 -0.0298 41  GLU D O   
10472 C CB  . GLU D 41  ? 0.4088 0.3973 0.3726 -0.0138 -0.0049 -0.0240 41  GLU D CB  
10473 C CG  . GLU D 41  ? 0.4101 0.3981 0.3697 -0.0106 -0.0038 -0.0214 41  GLU D CG  
10474 C CD  . GLU D 41  ? 0.4703 0.4632 0.4265 -0.0087 -0.0065 -0.0207 41  GLU D CD  
10475 O OE1 . GLU D 41  ? 0.5196 0.5173 0.4765 -0.0099 -0.0097 -0.0232 41  GLU D OE1 
10476 O OE2 . GLU D 41  ? 0.4625 0.4546 0.4157 -0.0060 -0.0056 -0.0177 41  GLU D OE2 
10477 N N   . GLU D 42  ? 0.2697 0.2447 0.2322 -0.0124 0.0025  -0.0241 42  GLU D N   
10478 C CA  . GLU D 42  ? 0.3090 0.2793 0.2683 -0.0114 0.0050  -0.0260 42  GLU D CA  
10479 C C   . GLU D 42  ? 0.3012 0.2664 0.2614 -0.0133 0.0053  -0.0288 42  GLU D C   
10480 O O   . GLU D 42  ? 0.3189 0.2797 0.2745 -0.0134 0.0064  -0.0320 42  GLU D O   
10481 C CB  . GLU D 42  ? 0.2804 0.2501 0.2422 -0.0090 0.0080  -0.0230 42  GLU D CB  
10482 C CG  . GLU D 42  ? 0.3130 0.2858 0.2726 -0.0074 0.0087  -0.0205 42  GLU D CG  
10483 C CD  . GLU D 42  ? 0.3670 0.3430 0.3300 -0.0079 0.0072  -0.0174 42  GLU D CD  
10484 O OE1 . GLU D 42  ? 0.3616 0.3384 0.3283 -0.0094 0.0052  -0.0174 42  GLU D OE1 
10485 O OE2 . GLU D 42  ? 0.3676 0.3446 0.3295 -0.0067 0.0085  -0.0149 42  GLU D OE2 
10486 N N   . LEU D 43  ? 0.3158 0.2807 0.2812 -0.0147 0.0049  -0.0273 43  LEU D N   
10487 C CA  . LEU D 43  ? 0.2968 0.2559 0.2630 -0.0166 0.0056  -0.0292 43  LEU D CA  
10488 C C   . LEU D 43  ? 0.3275 0.2862 0.2912 -0.0203 0.0037  -0.0332 43  LEU D C   
10489 O O   . LEU D 43  ? 0.3433 0.2955 0.3042 -0.0218 0.0047  -0.0363 43  LEU D O   
10490 C CB  . LEU D 43  ? 0.3066 0.2657 0.2780 -0.0174 0.0055  -0.0264 43  LEU D CB  
10491 C CG  . LEU D 43  ? 0.3795 0.3359 0.3530 -0.0146 0.0073  -0.0236 43  LEU D CG  
10492 C CD1 . LEU D 43  ? 0.3841 0.3445 0.3581 -0.0118 0.0079  -0.0218 43  LEU D CD1 
10493 C CD2 . LEU D 43  ? 0.3447 0.3015 0.3220 -0.0155 0.0066  -0.0210 43  LEU D CD2 
10494 N N   . LEU D 44  ? 0.3244 0.2902 0.2898 -0.0219 0.0009  -0.0331 44  LEU D N   
10495 C CA  . LEU D 44  ? 0.3604 0.3279 0.3248 -0.0257 -0.0015 -0.0370 44  LEU D CA  
10496 C C   . LEU D 44  ? 0.3701 0.3356 0.3273 -0.0254 -0.0021 -0.0407 44  LEU D C   
10497 O O   . LEU D 44  ? 0.3617 0.3231 0.3162 -0.0286 -0.0026 -0.0449 44  LEU D O   
10498 C CB  . LEU D 44  ? 0.3192 0.2962 0.2875 -0.0265 -0.0045 -0.0358 44  LEU D CB  
10499 C CG  . LEU D 44  ? 0.3274 0.3061 0.3018 -0.0266 -0.0036 -0.0323 44  LEU D CG  
10500 C CD1 . LEU D 44  ? 0.3530 0.3409 0.3307 -0.0261 -0.0060 -0.0309 44  LEU D CD1 
10501 C CD2 . LEU D 44  ? 0.3765 0.3511 0.3538 -0.0308 -0.0025 -0.0339 44  LEU D CD2 
10502 N N   . ILE D 45  ? 0.3376 0.3048 0.2909 -0.0216 -0.0017 -0.0391 45  ILE D N   
10503 C CA  . ILE D 45  ? 0.3479 0.3128 0.2930 -0.0206 -0.0018 -0.0422 45  ILE D CA  
10504 C C   . ILE D 45  ? 0.3589 0.3143 0.3007 -0.0204 0.0015  -0.0446 45  ILE D C   
10505 O O   . ILE D 45  ? 0.4108 0.3617 0.3469 -0.0224 0.0010  -0.0492 45  ILE D O   
10506 C CB  . ILE D 45  ? 0.3408 0.3089 0.2824 -0.0165 -0.0012 -0.0393 45  ILE D CB  
10507 C CG1 . ILE D 45  ? 0.3450 0.3216 0.2885 -0.0164 -0.0048 -0.0374 45  ILE D CG1 
10508 C CG2 . ILE D 45  ? 0.3821 0.3467 0.3141 -0.0148 -0.0002 -0.0420 45  ILE D CG2 
10509 C CD1 . ILE D 45  ? 0.3787 0.3574 0.3195 -0.0124 -0.0037 -0.0334 45  ILE D CD1 
10510 N N   . ALA D 46  ? 0.3568 0.3088 0.3020 -0.0180 0.0049  -0.0416 46  ALA D N   
10511 C CA  . ALA D 46  ? 0.4067 0.3497 0.3494 -0.0167 0.0084  -0.0433 46  ALA D CA  
10512 C C   . ALA D 46  ? 0.4042 0.3406 0.3467 -0.0208 0.0079  -0.0467 46  ALA D C   
10513 O O   . ALA D 46  ? 0.4238 0.3512 0.3611 -0.0208 0.0100  -0.0500 46  ALA D O   
10514 C CB  . ALA D 46  ? 0.3606 0.3034 0.3087 -0.0132 0.0112  -0.0390 46  ALA D CB  
10515 N N   . ALA D 47  ? 0.3807 0.3210 0.3285 -0.0245 0.0055  -0.0460 47  ALA D N   
10516 C CA  . ALA D 47  ? 0.4424 0.3772 0.3907 -0.0294 0.0052  -0.0491 47  ALA D CA  
10517 C C   . ALA D 47  ? 0.4228 0.3587 0.3667 -0.0336 0.0023  -0.0544 47  ALA D C   
10518 O O   . ALA D 47  ? 0.4643 0.3964 0.4088 -0.0387 0.0017  -0.0574 47  ALA D O   
10519 C CB  . ALA D 47  ? 0.4190 0.3578 0.3749 -0.0317 0.0044  -0.0460 47  ALA D CB  
10520 N N   . GLY D 48  ? 0.4152 0.3559 0.3542 -0.0316 0.0004  -0.0555 48  GLY D N   
10521 C CA  . GLY D 48  ? 0.4254 0.3683 0.3594 -0.0351 -0.0032 -0.0606 48  GLY D CA  
10522 C C   . GLY D 48  ? 0.4187 0.3731 0.3584 -0.0385 -0.0080 -0.0607 48  GLY D C   
10523 O O   . GLY D 48  ? 0.4079 0.3645 0.3460 -0.0430 -0.0113 -0.0654 48  GLY D O   
10524 N N   . MET D 49  ? 0.3826 0.3448 0.3291 -0.0365 -0.0084 -0.0558 49  MET D N   
10525 C CA  . MET D 49  ? 0.3604 0.3332 0.3141 -0.0392 -0.0119 -0.0552 49  MET D CA  
10526 C C   . MET D 49  ? 0.3691 0.3511 0.3214 -0.0352 -0.0147 -0.0530 49  MET D C   
10527 O O   . MET D 49  ? 0.3778 0.3574 0.3253 -0.0305 -0.0130 -0.0505 49  MET D O   
10528 C CB  . MET D 49  ? 0.3636 0.3362 0.3252 -0.0394 -0.0093 -0.0511 49  MET D CB  
10529 C CG  . MET D 49  ? 0.3345 0.2980 0.2973 -0.0436 -0.0067 -0.0531 49  MET D CG  
10530 S SD  . MET D 49  ? 0.4493 0.4152 0.4210 -0.0443 -0.0047 -0.0484 49  MET D SD  
10531 C CE  . MET D 49  ? 0.4043 0.3553 0.3740 -0.0470 -0.0004 -0.0494 49  MET D CE  
10532 N N   . LEU D 50  ? 0.3369 0.3294 0.2929 -0.0372 -0.0192 -0.0541 50  LEU D N   
10533 C CA  . LEU D 50  ? 0.3253 0.3270 0.2811 -0.0329 -0.0219 -0.0511 50  LEU D CA  
10534 C C   . LEU D 50  ? 0.3220 0.3293 0.2866 -0.0316 -0.0210 -0.0465 50  LEU D C   
10535 O O   . LEU D 50  ? 0.3441 0.3589 0.3163 -0.0348 -0.0229 -0.0473 50  LEU D O   
10536 C CB  . LEU D 50  ? 0.3369 0.3477 0.2917 -0.0348 -0.0277 -0.0548 50  LEU D CB  
10537 C CG  . LEU D 50  ? 0.3619 0.3821 0.3156 -0.0299 -0.0310 -0.0518 50  LEU D CG  
10538 C CD1 . LEU D 50  ? 0.3777 0.3924 0.3201 -0.0247 -0.0300 -0.0502 50  LEU D CD1 
10539 C CD2 . LEU D 50  ? 0.3825 0.4142 0.3390 -0.0326 -0.0372 -0.0555 50  LEU D CD2 
10540 N N   . PRO D 51  ? 0.3341 0.3390 0.2979 -0.0270 -0.0184 -0.0418 51  PRO D N   
10541 C CA  . PRO D 51  ? 0.3308 0.3411 0.3013 -0.0253 -0.0180 -0.0376 51  PRO D CA  
10542 C C   . PRO D 51  ? 0.3720 0.3926 0.3431 -0.0229 -0.0221 -0.0369 51  PRO D C   
10543 O O   . PRO D 51  ? 0.3532 0.3743 0.3173 -0.0194 -0.0237 -0.0365 51  PRO D O   
10544 C CB  . PRO D 51  ? 0.3647 0.3686 0.3325 -0.0214 -0.0144 -0.0335 51  PRO D CB  
10545 C CG  . PRO D 51  ? 0.3662 0.3627 0.3264 -0.0206 -0.0128 -0.0352 51  PRO D CG  
10546 C CD  . PRO D 51  ? 0.3720 0.3698 0.3282 -0.0233 -0.0158 -0.0402 51  PRO D CD  
10547 N N   . VAL D 52  ? 0.3298 0.3588 0.3091 -0.0242 -0.0236 -0.0366 52  VAL D N   
10548 C CA  . VAL D 52  ? 0.2993 0.3388 0.2801 -0.0208 -0.0272 -0.0353 52  VAL D CA  
10549 C C   . VAL D 52  ? 0.3043 0.3467 0.2914 -0.0185 -0.0252 -0.0312 52  VAL D C   
10550 O O   . VAL D 52  ? 0.2870 0.3318 0.2819 -0.0219 -0.0238 -0.0317 52  VAL D O   
10551 C CB  . VAL D 52  ? 0.3142 0.3644 0.2991 -0.0241 -0.0320 -0.0395 52  VAL D CB  
10552 C CG1 . VAL D 52  ? 0.3179 0.3643 0.2946 -0.0262 -0.0344 -0.0439 52  VAL D CG1 
10553 C CG2 . VAL D 52  ? 0.3095 0.3630 0.3046 -0.0303 -0.0308 -0.0416 52  VAL D CG2 
10554 N N   . ARG D 53  ? 0.3169 0.3581 0.3001 -0.0129 -0.0247 -0.0272 53  ARG D N   
10555 C CA  . ARG D 53  ? 0.3037 0.3460 0.2916 -0.0105 -0.0225 -0.0236 53  ARG D CA  
10556 C C   . ARG D 53  ? 0.3254 0.3802 0.3209 -0.0097 -0.0251 -0.0239 53  ARG D C   
10557 O O   . ARG D 53  ? 0.3405 0.4029 0.3347 -0.0068 -0.0291 -0.0242 53  ARG D O   
10558 C CB  . ARG D 53  ? 0.3346 0.3710 0.3156 -0.0051 -0.0211 -0.0195 53  ARG D CB  
10559 C CG  . ARG D 53  ? 0.4015 0.4378 0.3862 -0.0027 -0.0188 -0.0162 53  ARG D CG  
10560 C CD  . ARG D 53  ? 0.4316 0.4575 0.4108 -0.0007 -0.0154 -0.0129 53  ARG D CD  
10561 N NE  . ARG D 53  ? 0.4825 0.5088 0.4645 0.0018  -0.0138 -0.0103 53  ARG D NE  
10562 C CZ  . ARG D 53  ? 0.4335 0.4585 0.4119 0.0068  -0.0136 -0.0073 53  ARG D CZ  
10563 N NH1 . ARG D 53  ? 0.4240 0.4464 0.3951 0.0100  -0.0146 -0.0059 53  ARG D NH1 
10564 N NH2 . ARG D 53  ? 0.4623 0.4872 0.4437 0.0085  -0.0118 -0.0055 53  ARG D NH2 
10565 N N   . VAL D 54  ? 0.3008 0.3580 0.3042 -0.0119 -0.0228 -0.0234 54  VAL D N   
10566 C CA  . VAL D 54  ? 0.2702 0.3396 0.2819 -0.0108 -0.0243 -0.0233 54  VAL D CA  
10567 C C   . VAL D 54  ? 0.3348 0.4055 0.3437 -0.0034 -0.0245 -0.0193 54  VAL D C   
10568 O O   . VAL D 54  ? 0.3110 0.3721 0.3151 -0.0007 -0.0212 -0.0161 54  VAL D O   
10569 C CB  . VAL D 54  ? 0.3346 0.4046 0.3542 -0.0146 -0.0206 -0.0233 54  VAL D CB  
10570 C CG1 . VAL D 54  ? 0.3445 0.4281 0.3737 -0.0132 -0.0213 -0.0230 54  VAL D CG1 
10571 C CG2 . VAL D 54  ? 0.3232 0.3901 0.3446 -0.0220 -0.0201 -0.0271 54  VAL D CG2 
10572 N N   . LEU D 55  ? 0.3469 0.4291 0.3587 0.0000  -0.0283 -0.0195 55  LEU D N   
10573 C CA  . LEU D 55  ? 0.3609 0.4453 0.3707 0.0076  -0.0287 -0.0157 55  LEU D CA  
10574 C C   . LEU D 55  ? 0.3943 0.4945 0.4147 0.0092  -0.0308 -0.0162 55  LEU D C   
10575 O O   . LEU D 55  ? 0.3918 0.5026 0.4203 0.0044  -0.0333 -0.0199 55  LEU D O   
10576 C CB  . LEU D 55  ? 0.3598 0.4414 0.3595 0.0124  -0.0318 -0.0144 55  LEU D CB  
10577 C CG  . LEU D 55  ? 0.4272 0.4945 0.4167 0.0111  -0.0295 -0.0138 55  LEU D CG  
10578 C CD1 . LEU D 55  ? 0.4046 0.4711 0.3847 0.0147  -0.0329 -0.0135 55  LEU D CD1 
10579 C CD2 . LEU D 55  ? 0.3954 0.4514 0.3815 0.0132  -0.0246 -0.0101 55  LEU D CD2 
10580 N N   . GLY D 56  ? 0.4251 0.5268 0.4456 0.0160  -0.0297 -0.0127 56  GLY D N   
10581 C CA  . GLY D 56  ? 0.4444 0.5618 0.4751 0.0189  -0.0315 -0.0128 56  GLY D CA  
10582 C C   . GLY D 56  ? 0.3938 0.5225 0.4242 0.0229  -0.0379 -0.0134 56  GLY D C   
10583 O O   . GLY D 56  ? 0.4369 0.5601 0.4575 0.0243  -0.0408 -0.0134 56  GLY D O   
10584 N N   . ALA D 57  ? 0.3921 0.5376 0.4338 0.0247  -0.0402 -0.0141 57  ALA D N   
10585 C CA  . ALA D 57  ? 0.3522 0.5110 0.3950 0.0287  -0.0471 -0.0149 57  ALA D CA  
10586 C C   . ALA D 57  ? 0.3917 0.5547 0.4333 0.0396  -0.0477 -0.0105 57  ALA D C   
10587 O O   . ALA D 57  ? 0.4463 0.6190 0.4869 0.0447  -0.0536 -0.0102 57  ALA D O   
10588 C CB  . ALA D 57  ? 0.3992 0.5765 0.4565 0.0226  -0.0504 -0.0194 57  ALA D CB  
10589 N N   . HIS D 58  ? 0.3508 0.5061 0.3918 0.0435  -0.0420 -0.0070 58  HIS D N   
10590 C CA  . HIS D 58  ? 0.4324 0.5890 0.4715 0.0541  -0.0415 -0.0027 58  HIS D CA  
10591 C C   . HIS D 58  ? 0.4303 0.6094 0.4819 0.0583  -0.0461 -0.0034 58  HIS D C   
10592 O O   . HIS D 58  ? 0.4807 0.6652 0.5290 0.0669  -0.0502 -0.0010 58  HIS D O   
10593 C CB  . HIS D 58  ? 0.4326 0.5758 0.4557 0.0601  -0.0428 0.0006  58  HIS D CB  
10594 C CG  . HIS D 58  ? 0.4556 0.5781 0.4678 0.0562  -0.0379 0.0015  58  HIS D CG  
10595 N ND1 . HIS D 58  ? 0.4981 0.6080 0.5068 0.0583  -0.0319 0.0043  58  HIS D ND1 
10596 C CD2 . HIS D 58  ? 0.4746 0.5875 0.4793 0.0504  -0.0383 -0.0002 58  HIS D CD2 
10597 C CE1 . HIS D 58  ? 0.4643 0.5587 0.4644 0.0537  -0.0291 0.0042  58  HIS D CE1 
10598 N NE2 . HIS D 58  ? 0.4966 0.5926 0.4944 0.0491  -0.0327 0.0017  58  HIS D NE2 
10599 N N   . GLU D 59  ? 0.4424 0.6348 0.5088 0.0523  -0.0452 -0.0065 59  GLU D N   
10600 C CA  . GLU D 59  ? 0.4283 0.6443 0.5097 0.0548  -0.0489 -0.0077 59  GLU D CA  
10601 C C   . GLU D 59  ? 0.4335 0.6564 0.5282 0.0518  -0.0429 -0.0083 59  GLU D C   
10602 O O   . GLU D 59  ? 0.4033 0.6137 0.4958 0.0458  -0.0370 -0.0087 59  GLU D O   
10603 C CB  . GLU D 59  ? 0.4701 0.6991 0.5562 0.0484  -0.0563 -0.0125 59  GLU D CB  
10604 C CG  . GLU D 59  ? 0.4863 0.7150 0.5787 0.0357  -0.0544 -0.0172 59  GLU D CG  
10605 C CD  . GLU D 59  ? 0.5631 0.7991 0.6554 0.0295  -0.0617 -0.0220 59  GLU D CD  
10606 O OE1 . GLU D 59  ? 0.5522 0.7920 0.6379 0.0354  -0.0681 -0.0213 59  GLU D OE1 
10607 O OE2 . GLU D 59  ? 0.5802 0.8164 0.6774 0.0190  -0.0609 -0.0263 59  GLU D OE2 
10608 N N   . PRO D 60  ? 0.4022 0.6449 0.5106 0.0565  -0.0439 -0.0079 60  PRO D N   
10609 C CA  . PRO D 60  ? 0.4044 0.6543 0.5258 0.0538  -0.0375 -0.0083 60  PRO D CA  
10610 C C   . PRO D 60  ? 0.4557 0.7077 0.5847 0.0406  -0.0359 -0.0128 60  PRO D C   
10611 O O   . PRO D 60  ? 0.4134 0.6734 0.5458 0.0340  -0.0415 -0.0166 60  PRO D O   
10612 C CB  . PRO D 60  ? 0.4240 0.6984 0.5600 0.0609  -0.0407 -0.0077 60  PRO D CB  
10613 C CG  . PRO D 60  ? 0.4296 0.7018 0.5549 0.0714  -0.0466 -0.0048 60  PRO D CG  
10614 C CD  . PRO D 60  ? 0.4394 0.6979 0.5513 0.0658  -0.0505 -0.0065 60  PRO D CD  
10615 N N   . GLN D 61  ? 0.4336 0.6769 0.5638 0.0367  -0.0280 -0.0123 61  GLN D N   
10616 C CA  . GLN D 61  ? 0.4625 0.7060 0.5990 0.0246  -0.0255 -0.0159 61  GLN D CA  
10617 C C   . GLN D 61  ? 0.4746 0.7180 0.6180 0.0235  -0.0169 -0.0147 61  GLN D C   
10618 O O   . GLN D 61  ? 0.4522 0.6849 0.5886 0.0301  -0.0120 -0.0111 61  GLN D O   
10619 C CB  . GLN D 61  ? 0.4174 0.6401 0.5399 0.0183  -0.0255 -0.0171 61  GLN D CB  
10620 C CG  . GLN D 61  ? 0.3960 0.5964 0.5045 0.0215  -0.0200 -0.0137 61  GLN D CG  
10621 C CD  . GLN D 61  ? 0.4389 0.6327 0.5501 0.0162  -0.0123 -0.0136 61  GLN D CD  
10622 O OE1 . GLN D 61  ? 0.4092 0.6124 0.5313 0.0086  -0.0108 -0.0162 61  GLN D OE1 
10623 N NE2 . GLN D 61  ? 0.3980 0.5752 0.4988 0.0198  -0.0075 -0.0106 61  GLN D NE2 
10624 N N   A ASN D 62  ? 0.4702 0.7248 0.6265 0.0145  -0.0150 -0.0177 62  ASN D N   
10625 N N   B ASN D 62  ? 0.4703 0.7248 0.6266 0.0146  -0.0150 -0.0177 62  ASN D N   
10626 C CA  A ASN D 62  ? 0.5004 0.7564 0.6641 0.0125  -0.0067 -0.0168 62  ASN D CA  
10627 C CA  B ASN D 62  ? 0.5008 0.7559 0.6638 0.0126  -0.0065 -0.0166 62  ASN D CA  
10628 C C   A ASN D 62  ? 0.4898 0.7343 0.6514 0.0012  -0.0023 -0.0187 62  ASN D C   
10629 C C   B ASN D 62  ? 0.4896 0.7339 0.6510 0.0012  -0.0022 -0.0187 62  ASN D C   
10630 O O   A ASN D 62  ? 0.4903 0.7292 0.6524 0.0000  0.0054  -0.0172 62  ASN D O   
10631 O O   B ASN D 62  ? 0.4894 0.7284 0.6518 -0.0003 0.0055  -0.0173 62  ASN D O   
10632 C CB  A ASN D 62  ? 0.5263 0.8091 0.7100 0.0130  -0.0068 -0.0179 62  ASN D CB  
10633 C CB  B ASN D 62  ? 0.5271 0.8084 0.7099 0.0137  -0.0062 -0.0175 62  ASN D CB  
10634 C CG  A ASN D 62  ? 0.5324 0.8237 0.7189 0.0259  -0.0061 -0.0143 62  ASN D CG  
10635 C CG  B ASN D 62  ? 0.5020 0.8004 0.6969 0.0051  -0.0122 -0.0221 62  ASN D CG  
10636 O OD1 A ASN D 62  ? 0.5541 0.8371 0.7368 0.0310  0.0010  -0.0113 62  ASN D OD1 
10637 O OD1 B ASN D 62  ? 0.5098 0.7992 0.6977 -0.0020 -0.0160 -0.0248 62  ASN D OD1 
10638 N ND2 A ASN D 62  ? 0.5213 0.8283 0.7132 0.0316  -0.0136 -0.0147 62  ASN D ND2 
10639 N ND2 B ASN D 62  ? 0.4954 0.8186 0.7087 0.0054  -0.0130 -0.0233 62  ASN D ND2 
10640 N N   . VAL D 63  ? 0.4326 0.6724 0.5905 -0.0065 -0.0068 -0.0219 63  VAL D N   
10641 C CA  . VAL D 63  ? 0.3955 0.6266 0.5531 -0.0174 -0.0031 -0.0242 63  VAL D CA  
10642 C C   . VAL D 63  ? 0.3690 0.5775 0.5134 -0.0173 0.0032  -0.0215 63  VAL D C   
10643 O O   . VAL D 63  ? 0.3416 0.5432 0.4863 -0.0252 0.0075  -0.0225 63  VAL D O   
10644 C CB  . VAL D 63  ? 0.3696 0.5979 0.5238 -0.0246 -0.0094 -0.0282 63  VAL D CB  
10645 C CG1 . VAL D 63  ? 0.4633 0.7145 0.6330 -0.0292 -0.0146 -0.0322 63  VAL D CG1 
10646 C CG2 . VAL D 63  ? 0.3901 0.6071 0.5299 -0.0183 -0.0145 -0.0270 63  VAL D CG2 
10647 N N   . THR D 64  ? 0.3161 0.5125 0.4487 -0.0088 0.0037  -0.0182 64  THR D N   
10648 C CA  . THR D 64  ? 0.3669 0.5422 0.4869 -0.0098 0.0087  -0.0162 64  THR D CA  
10649 C C   . THR D 64  ? 0.3107 0.4839 0.4318 -0.0068 0.0165  -0.0135 64  THR D C   
10650 O O   . THR D 64  ? 0.3207 0.4771 0.4316 -0.0078 0.0207  -0.0120 64  THR D O   
10651 C CB  . THR D 64  ? 0.3633 0.5235 0.4683 -0.0040 0.0057  -0.0144 64  THR D CB  
10652 O OG1 . THR D 64  ? 0.3946 0.5590 0.4989 0.0059  0.0053  -0.0118 64  THR D OG1 
10653 C CG2 . THR D 64  ? 0.3290 0.4892 0.4311 -0.0070 -0.0013 -0.0170 64  THR D CG2 
10654 N N   . GLU D 65  ? 0.3964 0.5859 0.5289 -0.0025 0.0184  -0.0128 65  GLU D N   
10655 C CA  . GLU D 65  ? 0.3804 0.5673 0.5129 0.0011  0.0262  -0.0103 65  GLU D CA  
10656 C C   . GLU D 65  ? 0.3525 0.5322 0.4848 -0.0071 0.0328  -0.0106 65  GLU D C   
10657 O O   . GLU D 65  ? 0.3627 0.5291 0.4858 -0.0046 0.0384  -0.0083 65  GLU D O   
10658 C CB  . GLU D 65  ? 0.4226 0.6304 0.5690 0.0071  0.0271  -0.0097 65  GLU D CB  
10659 C CG  . GLU D 65  ? 0.5049 0.7171 0.6488 0.0168  0.0210  -0.0086 65  GLU D CG  
10660 C CD  . GLU D 65  ? 0.6739 0.8740 0.8067 0.0273  0.0242  -0.0050 65  GLU D CD  
10661 O OE1 . GLU D 65  ? 0.6268 0.8059 0.7440 0.0279  0.0254  -0.0038 65  GLU D OE1 
10662 O OE2 . GLU D 65  ? 0.7436 0.9560 0.8836 0.0353  0.0254  -0.0036 65  GLU D OE2 
10663 N N   . PRO D 66  ? 0.3462 0.5317 0.4865 -0.0167 0.0325  -0.0132 66  PRO D N   
10664 C CA  . PRO D 66  ? 0.3516 0.5266 0.4889 -0.0239 0.0392  -0.0129 66  PRO D CA  
10665 C C   . PRO D 66  ? 0.3162 0.4684 0.4371 -0.0258 0.0385  -0.0122 66  PRO D C   
10666 O O   . PRO D 66  ? 0.3359 0.4769 0.4516 -0.0304 0.0439  -0.0113 66  PRO D O   
10667 C CB  . PRO D 66  ? 0.3563 0.5449 0.5076 -0.0337 0.0386  -0.0162 66  PRO D CB  
10668 C CG  . PRO D 66  ? 0.3772 0.5866 0.5407 -0.0308 0.0323  -0.0181 66  PRO D CG  
10669 C CD  . PRO D 66  ? 0.3448 0.5469 0.4973 -0.0217 0.0267  -0.0167 66  PRO D CD  
10670 N N   . HIS D 67  ? 0.3165 0.4616 0.4288 -0.0223 0.0322  -0.0125 67  HIS D N   
10671 C CA  . HIS D 67  ? 0.3128 0.4386 0.4114 -0.0246 0.0309  -0.0122 67  HIS D CA  
10672 C C   . HIS D 67  ? 0.3545 0.4663 0.4397 -0.0175 0.0309  -0.0096 67  HIS D C   
10673 O O   . HIS D 67  ? 0.3388 0.4347 0.4136 -0.0193 0.0327  -0.0086 67  HIS D O   
10674 C CB  . HIS D 67  ? 0.2929 0.4196 0.3914 -0.0281 0.0239  -0.0151 67  HIS D CB  
10675 C CG  . HIS D 67  ? 0.3331 0.4710 0.4431 -0.0365 0.0234  -0.0183 67  HIS D CG  
10676 N ND1 . HIS D 67  ? 0.3315 0.4613 0.4406 -0.0446 0.0270  -0.0192 67  HIS D ND1 
10677 C CD2 . HIS D 67  ? 0.3460 0.5029 0.4692 -0.0381 0.0201  -0.0208 67  HIS D CD2 
10678 C CE1 . HIS D 67  ? 0.3124 0.4548 0.4332 -0.0515 0.0261  -0.0223 67  HIS D CE1 
10679 N NE2 . HIS D 67  ? 0.3276 0.4873 0.4575 -0.0479 0.0217  -0.0235 67  HIS D NE2 
10680 N N   . ILE D 68  ? 0.3377 0.4544 0.4226 -0.0096 0.0286  -0.0085 68  ILE D N   
10681 C CA  . ILE D 68  ? 0.3456 0.4488 0.4178 -0.0030 0.0282  -0.0063 68  ILE D CA  
10682 C C   . ILE D 68  ? 0.3407 0.4500 0.4153 0.0048  0.0312  -0.0045 68  ILE D C   
10683 O O   . ILE D 68  ? 0.3526 0.4772 0.4368 0.0083  0.0292  -0.0049 68  ILE D O   
10684 C CB  . ILE D 68  ? 0.3517 0.4510 0.4181 -0.0010 0.0215  -0.0068 68  ILE D CB  
10685 C CG1 . ILE D 68  ? 0.3131 0.4057 0.3765 -0.0081 0.0188  -0.0088 68  ILE D CG1 
10686 C CG2 . ILE D 68  ? 0.3383 0.4238 0.3922 0.0053  0.0217  -0.0045 68  ILE D CG2 
10687 C CD1 . ILE D 68  ? 0.3242 0.4137 0.3822 -0.0062 0.0129  -0.0094 68  ILE D CD1 
10688 N N   . PHE D 69  ? 0.3302 0.4278 0.3962 0.0075  0.0361  -0.0026 69  PHE D N   
10689 C CA  . PHE D 69  ? 0.3199 0.4202 0.3859 0.0152  0.0399  -0.0009 69  PHE D CA  
10690 C C   . PHE D 69  ? 0.3409 0.4404 0.4029 0.0230  0.0357  0.0000  69  PHE D C   
10691 O O   . PHE D 69  ? 0.3432 0.4324 0.3964 0.0228  0.0314  0.0000  69  PHE D O   
10692 C CB  . PHE D 69  ? 0.3777 0.4628 0.4327 0.0157  0.0456  0.0005  69  PHE D CB  
10693 C CG  . PHE D 69  ? 0.3440 0.4288 0.3968 0.0236  0.0503  0.0020  69  PHE D CG  
10694 C CD1 . PHE D 69  ? 0.3486 0.4502 0.4136 0.0279  0.0526  0.0022  69  PHE D CD1 
10695 C CD2 . PHE D 69  ? 0.3712 0.4386 0.4095 0.0266  0.0527  0.0031  69  PHE D CD2 
10696 C CE1 . PHE D 69  ? 0.3882 0.4884 0.4504 0.0357  0.0576  0.0036  69  PHE D CE1 
10697 C CE2 . PHE D 69  ? 0.3212 0.3861 0.3557 0.0337  0.0575  0.0042  69  PHE D CE2 
10698 C CZ  . PHE D 69  ? 0.3780 0.4592 0.4245 0.0386  0.0602  0.0045  69  PHE D CZ  
10699 N N   . GLY D 70  ? 0.3301 0.4409 0.3988 0.0299  0.0370  0.0009  70  GLY D N   
10700 C CA  . GLY D 70  ? 0.3495 0.4618 0.4159 0.0376  0.0329  0.0019  70  GLY D CA  
10701 C C   . GLY D 70  ? 0.3990 0.4923 0.4499 0.0425  0.0335  0.0036  70  GLY D C   
10702 O O   . GLY D 70  ? 0.4274 0.5194 0.4747 0.0492  0.0307  0.0049  70  GLY D O   
10703 N N   . MET D 71  ? 0.3617 0.4397 0.4028 0.0392  0.0369  0.0036  71  MET D N   
10704 C CA  . MET D 71  ? 0.3502 0.4100 0.3766 0.0426  0.0371  0.0048  71  MET D CA  
10705 C C   . MET D 71  ? 0.3784 0.4297 0.3983 0.0389  0.0316  0.0043  71  MET D C   
10706 O O   . MET D 71  ? 0.3448 0.3818 0.3533 0.0411  0.0312  0.0052  71  MET D O   
10707 C CB  . MET D 71  ? 0.3828 0.4297 0.4005 0.0408  0.0424  0.0048  71  MET D CB  
10708 C CG  . MET D 71  ? 0.3696 0.4103 0.3846 0.0319  0.0413  0.0037  71  MET D CG  
10709 S SD  . MET D 71  ? 0.3590 0.3855 0.3634 0.0300  0.0471  0.0039  71  MET D SD  
10710 C CE  . MET D 71  ? 0.2916 0.2989 0.2803 0.0314  0.0439  0.0040  71  MET D CE  
10711 N N   . PHE D 72  ? 0.3385 0.3977 0.3651 0.0331  0.0278  0.0029  72  PHE D N   
10712 C CA  . PHE D 72  ? 0.3184 0.3704 0.3395 0.0293  0.0231  0.0024  72  PHE D CA  
10713 C C   . PHE D 72  ? 0.3132 0.3726 0.3368 0.0330  0.0182  0.0027  72  PHE D C   
10714 O O   . PHE D 72  ? 0.3147 0.3869 0.3461 0.0376  0.0177  0.0030  72  PHE D O   
10715 C CB  . PHE D 72  ? 0.3187 0.3727 0.3439 0.0209  0.0226  0.0006  72  PHE D CB  
10716 C CG  . PHE D 72  ? 0.3369 0.3813 0.3571 0.0178  0.0271  0.0008  72  PHE D CG  
10717 C CD1 . PHE D 72  ? 0.3744 0.4029 0.3825 0.0182  0.0275  0.0015  72  PHE D CD1 
10718 C CD2 . PHE D 72  ? 0.2853 0.3363 0.3122 0.0150  0.0312  0.0003  72  PHE D CD2 
10719 C CE1 . PHE D 72  ? 0.3277 0.3472 0.3300 0.0160  0.0311  0.0017  72  PHE D CE1 
10720 C CE2 . PHE D 72  ? 0.3909 0.4320 0.4114 0.0128  0.0355  0.0008  72  PHE D CE2 
10721 C CZ  . PHE D 72  ? 0.3415 0.3669 0.3495 0.0135  0.0351  0.0015  72  PHE D CZ  
10722 N N   . CYS D 73  ? 0.3016 0.3527 0.3182 0.0314  0.0148  0.0027  73  CYS D N   
10723 C CA  . CYS D 73  ? 0.3282 0.3815 0.3428 0.0364  0.0110  0.0038  73  CYS D CA  
10724 C C   . CYS D 73  ? 0.3329 0.4032 0.3578 0.0359  0.0070  0.0025  73  CYS D C   
10725 O O   . CYS D 73  ? 0.2975 0.3756 0.3300 0.0297  0.0063  0.0002  73  CYS D O   
10726 C CB  . CYS D 73  ? 0.2652 0.3053 0.2697 0.0343  0.0089  0.0041  73  CYS D CB  
10727 S SG  . CYS D 73  ? 0.3062 0.3493 0.3142 0.0253  0.0056  0.0014  73  CYS D SG  
10728 N N   . PRO D 74  ? 0.3054 0.3816 0.3305 0.0425  0.0041  0.0038  74  PRO D N   
10729 C CA  . PRO D 74  ? 0.3297 0.4226 0.3640 0.0421  -0.0007 0.0024  74  PRO D CA  
10730 C C   . PRO D 74  ? 0.3130 0.4048 0.3460 0.0350  -0.0044 0.0000  74  PRO D C   
10731 O O   . PRO D 74  ? 0.3471 0.4520 0.3890 0.0313  -0.0074 -0.0024 74  PRO D O   
10732 C CB  . PRO D 74  ? 0.3910 0.4856 0.4213 0.0513  -0.0033 0.0049  74  PRO D CB  
10733 C CG  . PRO D 74  ? 0.3905 0.4739 0.4143 0.0571  0.0017  0.0075  74  PRO D CG  
10734 C CD  . PRO D 74  ? 0.3557 0.4240 0.3729 0.0510  0.0053  0.0067  74  PRO D CD  
10735 N N   . PHE D 75  ? 0.3055 0.3824 0.3279 0.0332  -0.0044 0.0006  75  PHE D N   
10736 C CA  . PHE D 75  ? 0.3589 0.4344 0.3792 0.0276  -0.0078 -0.0014 75  PHE D CA  
10737 C C   . PHE D 75  ? 0.3068 0.3844 0.3333 0.0195  -0.0065 -0.0042 75  PHE D C   
10738 O O   . PHE D 75  ? 0.3347 0.4190 0.3653 0.0149  -0.0096 -0.0069 75  PHE D O   
10739 C CB  . PHE D 75  ? 0.3459 0.4054 0.3541 0.0280  -0.0073 0.0001  75  PHE D CB  
10740 C CG  . PHE D 75  ? 0.3110 0.3679 0.3164 0.0228  -0.0099 -0.0018 75  PHE D CG  
10741 C CD1 . PHE D 75  ? 0.3649 0.4310 0.3721 0.0230  -0.0146 -0.0033 75  PHE D CD1 
10742 C CD2 . PHE D 75  ? 0.3952 0.4410 0.3962 0.0180  -0.0079 -0.0023 75  PHE D CD2 
10743 C CE1 . PHE D 75  ? 0.4016 0.4645 0.4052 0.0186  -0.0166 -0.0053 75  PHE D CE1 
10744 C CE2 . PHE D 75  ? 0.4111 0.4545 0.4095 0.0138  -0.0099 -0.0041 75  PHE D CE2 
10745 C CZ  . PHE D 75  ? 0.4105 0.4619 0.4099 0.0142  -0.0140 -0.0056 75  PHE D CZ  
10746 N N   . CYS D 76  ? 0.2873 0.3579 0.3132 0.0174  -0.0019 -0.0037 76  CYS D N   
10747 C CA  . CYS D 76  ? 0.2925 0.3638 0.3231 0.0100  -0.0004 -0.0060 76  CYS D CA  
10748 C C   . CYS D 76  ? 0.3181 0.4054 0.3610 0.0078  -0.0009 -0.0078 76  CYS D C   
10749 O O   . CYS D 76  ? 0.3204 0.4113 0.3680 0.0011  -0.0018 -0.0105 76  CYS D O   
10750 C CB  . CYS D 76  ? 0.3239 0.3839 0.3502 0.0087  0.0044  -0.0047 76  CYS D CB  
10751 S SG  . CYS D 76  ? 0.3106 0.3742 0.3413 0.0113  0.0098  -0.0034 76  CYS D SG  
10752 N N   . ARG D 77  ? 0.2906 0.3877 0.3388 0.0134  -0.0004 -0.0066 77  ARG D N   
10753 C CA  . ARG D 77  ? 0.2890 0.4034 0.3504 0.0117  -0.0008 -0.0083 77  ARG D CA  
10754 C C   . ARG D 77  ? 0.3200 0.4457 0.3856 0.0109  -0.0071 -0.0105 77  ARG D C   
10755 O O   . ARG D 77  ? 0.2892 0.4235 0.3626 0.0042  -0.0086 -0.0136 77  ARG D O   
10756 C CB  . ARG D 77  ? 0.3506 0.4718 0.4164 0.0186  0.0022  -0.0061 77  ARG D CB  
10757 C CG  . ARG D 77  ? 0.3711 0.4833 0.4345 0.0176  0.0090  -0.0049 77  ARG D CG  
10758 C CD  . ARG D 77  ? 0.3557 0.4744 0.4234 0.0247  0.0127  -0.0029 77  ARG D CD  
10759 N NE  . ARG D 77  ? 0.3927 0.5011 0.4500 0.0326  0.0126  -0.0004 77  ARG D NE  
10760 C CZ  . ARG D 77  ? 0.4248 0.5404 0.4840 0.0408  0.0111  0.0012  77  ARG D CZ  
10761 N NH1 . ARG D 77  ? 0.4502 0.5850 0.5220 0.0425  0.0090  0.0004  77  ARG D NH1 
10762 N NH2 . ARG D 77  ? 0.3987 0.5019 0.4470 0.0475  0.0119  0.0036  77  ARG D NH2 
10763 N N   . ASP D 78  ? 0.2491 0.3741 0.3086 0.0173  -0.0109 -0.0090 78  ASP D N   
10764 C CA  . ASP D 78  ? 0.3123 0.4465 0.3732 0.0172  -0.0174 -0.0109 78  ASP D CA  
10765 C C   . ASP D 78  ? 0.3037 0.4325 0.3619 0.0089  -0.0191 -0.0142 78  ASP D C   
10766 O O   . ASP D 78  ? 0.2908 0.4303 0.3553 0.0046  -0.0231 -0.0175 78  ASP D O   
10767 C CB  . ASP D 78  ? 0.3059 0.4343 0.3566 0.0253  -0.0201 -0.0081 78  ASP D CB  
10768 C CG  . ASP D 78  ? 0.3691 0.5089 0.4210 0.0275  -0.0269 -0.0094 78  ASP D CG  
10769 O OD1 . ASP D 78  ? 0.3688 0.5217 0.4296 0.0223  -0.0303 -0.0129 78  ASP D OD1 
10770 O OD2 . ASP D 78  ? 0.3803 0.5150 0.4231 0.0341  -0.0290 -0.0068 78  ASP D OD2 
10771 N N   . SER D 79  ? 0.2572 0.3694 0.3064 0.0065  -0.0162 -0.0134 79  SER D N   
10772 C CA  . SER D 79  ? 0.2642 0.3698 0.3099 -0.0004 -0.0173 -0.0162 79  SER D CA  
10773 C C   . SER D 79  ? 0.2886 0.4001 0.3437 -0.0081 -0.0157 -0.0192 79  SER D C   
10774 O O   . SER D 79  ? 0.2862 0.4016 0.3436 -0.0135 -0.0187 -0.0227 79  SER D O   
10775 C CB  . SER D 79  ? 0.3297 0.4176 0.3651 -0.0006 -0.0141 -0.0144 79  SER D CB  
10776 O OG  . SER D 79  ? 0.3271 0.4082 0.3531 0.0051  -0.0155 -0.0120 79  SER D OG  
10777 N N   . LEU D 80  ? 0.2857 0.3964 0.3452 -0.0090 -0.0106 -0.0178 80  LEU D N   
10778 C CA  . LEU D 80  ? 0.2555 0.3711 0.3236 -0.0166 -0.0084 -0.0203 80  LEU D CA  
10779 C C   . LEU D 80  ? 0.2652 0.3996 0.3450 -0.0185 -0.0120 -0.0231 80  LEU D C   
10780 O O   . LEU D 80  ? 0.2916 0.4300 0.3768 -0.0261 -0.0129 -0.0266 80  LEU D O   
10781 C CB  . LEU D 80  ? 0.2980 0.4104 0.3683 -0.0163 -0.0020 -0.0180 80  LEU D CB  
10782 C CG  . LEU D 80  ? 0.2611 0.3797 0.3410 -0.0237 0.0012  -0.0199 80  LEU D CG  
10783 C CD1 . LEU D 80  ? 0.2753 0.3831 0.3506 -0.0311 0.0012  -0.0222 80  LEU D CD1 
10784 C CD2 . LEU D 80  ? 0.2656 0.3821 0.3472 -0.0222 0.0079  -0.0172 80  LEU D CD2 
10785 N N   . ALA D 81  ? 0.2871 0.4334 0.3713 -0.0118 -0.0142 -0.0216 81  ALA D N   
10786 C CA  . ALA D 81  ? 0.3000 0.4661 0.3965 -0.0134 -0.0183 -0.0243 81  ALA D CA  
10787 C C   . ALA D 81  ? 0.2999 0.4675 0.3941 -0.0180 -0.0243 -0.0282 81  ALA D C   
10788 O O   . ALA D 81  ? 0.3270 0.5073 0.4309 -0.0240 -0.0269 -0.0320 81  ALA D O   
10789 C CB  . ALA D 81  ? 0.2555 0.4336 0.3557 -0.0039 -0.0204 -0.0218 81  ALA D CB  
10790 N N   . GLN D 82  ? 0.2926 0.4475 0.3738 -0.0156 -0.0265 -0.0277 82  GLN D N   
10791 C CA  . GLN D 82  ? 0.2864 0.4422 0.3640 -0.0193 -0.0322 -0.0315 82  GLN D CA  
10792 C C   . GLN D 82  ? 0.3002 0.4516 0.3804 -0.0295 -0.0305 -0.0354 82  GLN D C   
10793 O O   . GLN D 82  ? 0.3282 0.4871 0.4120 -0.0349 -0.0347 -0.0398 82  GLN D O   
10794 C CB  . GLN D 82  ? 0.3087 0.4510 0.3717 -0.0149 -0.0338 -0.0299 82  GLN D CB  
10795 C CG  . GLN D 82  ? 0.3383 0.4822 0.3969 -0.0048 -0.0350 -0.0257 82  GLN D CG  
10796 C CD  . GLN D 82  ? 0.3314 0.4944 0.3990 -0.0014 -0.0398 -0.0263 82  GLN D CD  
10797 O OE1 . GLN D 82  ? 0.3548 0.5261 0.4230 -0.0031 -0.0457 -0.0295 82  GLN D OE1 
10798 N NE2 . GLN D 82  ? 0.3691 0.5394 0.4433 0.0041  -0.0375 -0.0234 82  GLN D NE2 
10799 N N   . GLY D 83  ? 0.2885 0.4267 0.3656 -0.0321 -0.0244 -0.0338 83  GLY D N   
10800 C CA  . GLY D 83  ? 0.2893 0.4219 0.3685 -0.0412 -0.0219 -0.0369 83  GLY D CA  
10801 C C   . GLY D 83  ? 0.2880 0.4351 0.3816 -0.0471 -0.0208 -0.0391 83  GLY D C   
10802 O O   . GLY D 83  ? 0.2911 0.4418 0.3889 -0.0548 -0.0227 -0.0435 83  GLY D O   
10803 N N   . LEU D 84  ? 0.2893 0.4444 0.3906 -0.0437 -0.0173 -0.0361 84  LEU D N   
10804 C CA  . LEU D 84  ? 0.2745 0.4441 0.3904 -0.0490 -0.0152 -0.0377 84  LEU D CA  
10805 C C   . LEU D 84  ? 0.3089 0.4977 0.4345 -0.0509 -0.0219 -0.0415 84  LEU D C   
10806 O O   . LEU D 84  ? 0.3204 0.5195 0.4572 -0.0590 -0.0216 -0.0449 84  LEU D O   
10807 C CB  . LEU D 84  ? 0.3170 0.4919 0.4382 -0.0433 -0.0103 -0.0336 84  LEU D CB  
10808 C CG  . LEU D 84  ? 0.3203 0.4776 0.4325 -0.0417 -0.0037 -0.0299 84  LEU D CG  
10809 C CD1 . LEU D 84  ? 0.2464 0.4099 0.3629 -0.0351 0.0002  -0.0263 84  LEU D CD1 
10810 C CD2 . LEU D 84  ? 0.3065 0.4578 0.4212 -0.0510 0.0010  -0.0316 84  LEU D CD2 
10811 N N   . LEU D 85  ? 0.3015 0.4952 0.4227 -0.0440 -0.0281 -0.0412 85  LEU D N   
10812 C CA  . LEU D 85  ? 0.3013 0.5132 0.4301 -0.0446 -0.0355 -0.0446 85  LEU D CA  
10813 C C   . LEU D 85  ? 0.3287 0.5365 0.4528 -0.0522 -0.0402 -0.0500 85  LEU D C   
10814 O O   . LEU D 85  ? 0.2919 0.5147 0.4220 -0.0542 -0.0468 -0.0537 85  LEU D O   
10815 C CB  . LEU D 85  ? 0.2753 0.4924 0.3994 -0.0335 -0.0401 -0.0417 85  LEU D CB  
10816 C CG  . LEU D 85  ? 0.2701 0.4970 0.4023 -0.0263 -0.0367 -0.0375 85  LEU D CG  
10817 C CD1 . LEU D 85  ? 0.3665 0.5924 0.4904 -0.0144 -0.0399 -0.0336 85  LEU D CD1 
10818 C CD2 . LEU D 85  ? 0.3143 0.5655 0.4652 -0.0292 -0.0384 -0.0398 85  LEU D CD2 
10819 N N   . GLY D 86  ? 0.2829 0.4709 0.3961 -0.0561 -0.0370 -0.0505 86  GLY D N   
10820 C CA  . GLY D 86  ? 0.2993 0.4813 0.4074 -0.0635 -0.0404 -0.0558 86  GLY D CA  
10821 C C   . GLY D 86  ? 0.3333 0.5091 0.4282 -0.0582 -0.0458 -0.0562 86  GLY D C   
10822 O O   . GLY D 86  ? 0.3611 0.5336 0.4510 -0.0633 -0.0496 -0.0610 86  GLY D O   
10823 N N   . ARG D 87  ? 0.3125 0.4858 0.4009 -0.0483 -0.0460 -0.0515 87  ARG D N   
10824 C CA  . ARG D 87  ? 0.3665 0.5353 0.4426 -0.0431 -0.0511 -0.0517 87  ARG D CA  
10825 C C   . ARG D 87  ? 0.3281 0.4761 0.3905 -0.0445 -0.0484 -0.0519 87  ARG D C   
10826 O O   . ARG D 87  ? 0.3449 0.4883 0.3968 -0.0423 -0.0523 -0.0532 87  ARG D O   
10827 C CB  . ARG D 87  ? 0.3125 0.4855 0.3862 -0.0322 -0.0521 -0.0465 87  ARG D CB  
10828 C CG  . ARG D 87  ? 0.3815 0.5767 0.4684 -0.0300 -0.0561 -0.0468 87  ARG D CG  
10829 C CD  . ARG D 87  ? 0.3718 0.5707 0.4560 -0.0188 -0.0571 -0.0417 87  ARG D CD  
10830 N NE  . ARG D 87  ? 0.3891 0.6103 0.4868 -0.0162 -0.0609 -0.0420 87  ARG D NE  
10831 C CZ  . ARG D 87  ? 0.3977 0.6255 0.4978 -0.0067 -0.0606 -0.0375 87  ARG D CZ  
10832 N NH1 . ARG D 87  ? 0.3802 0.5936 0.4694 0.0007  -0.0570 -0.0326 87  ARG D NH1 
10833 N NH2 . ARG D 87  ? 0.4789 0.7284 0.5922 -0.0043 -0.0644 -0.0381 87  ARG D NH2 
10834 N N   . PHE D 88  ? 0.3374 0.4733 0.3995 -0.0480 -0.0419 -0.0507 88  PHE D N   
10835 C CA  . PHE D 88  ? 0.3444 0.4617 0.3950 -0.0497 -0.0393 -0.0513 88  PHE D CA  
10836 C C   . PHE D 88  ? 0.3278 0.4399 0.3809 -0.0594 -0.0375 -0.0558 88  PHE D C   
10837 O O   . PHE D 88  ? 0.3386 0.4353 0.3859 -0.0613 -0.0328 -0.0552 88  PHE D O   
10838 C CB  . PHE D 88  ? 0.3302 0.4353 0.3759 -0.0449 -0.0336 -0.0460 88  PHE D CB  
10839 C CG  . PHE D 88  ? 0.3053 0.4094 0.3439 -0.0361 -0.0351 -0.0422 88  PHE D CG  
10840 C CD1 . PHE D 88  ? 0.3332 0.4478 0.3770 -0.0302 -0.0359 -0.0390 88  PHE D CD1 
10841 C CD2 . PHE D 88  ? 0.3369 0.4290 0.3633 -0.0334 -0.0353 -0.0417 88  PHE D CD2 
10842 C CE1 . PHE D 88  ? 0.3205 0.4326 0.3567 -0.0219 -0.0371 -0.0353 88  PHE D CE1 
10843 C CE2 . PHE D 88  ? 0.3542 0.4445 0.3734 -0.0255 -0.0362 -0.0380 88  PHE D CE2 
10844 C CZ  . PHE D 88  ? 0.3556 0.4552 0.3794 -0.0200 -0.0371 -0.0348 88  PHE D CZ  
10845 N N   . ASP D 89  ? 0.3324 0.4576 0.3945 -0.0656 -0.0411 -0.0603 89  ASP D N   
10846 C CA  . ASP D 89  ? 0.3306 0.4512 0.3964 -0.0756 -0.0388 -0.0646 89  ASP D CA  
10847 C C   . ASP D 89  ? 0.3832 0.4878 0.4367 -0.0786 -0.0392 -0.0681 89  ASP D C   
10848 O O   . ASP D 89  ? 0.3996 0.4939 0.4528 -0.0856 -0.0355 -0.0704 89  ASP D O   
10849 C CB  . ASP D 89  ? 0.3662 0.5054 0.4452 -0.0822 -0.0429 -0.0689 89  ASP D CB  
10850 C CG  . ASP D 89  ? 0.4113 0.5620 0.4884 -0.0809 -0.0515 -0.0727 89  ASP D CG  
10851 O OD1 . ASP D 89  ? 0.4105 0.5547 0.4755 -0.0749 -0.0544 -0.0721 89  ASP D OD1 
10852 O OD2 . ASP D 89  ? 0.5043 0.6720 0.5928 -0.0859 -0.0556 -0.0764 89  ASP D OD2 
10853 N N   . TYR D 90  ? 0.3889 0.4899 0.4316 -0.0732 -0.0429 -0.0683 90  TYR D N   
10854 C CA  . TYR D 90  ? 0.3821 0.4676 0.4124 -0.0749 -0.0426 -0.0714 90  TYR D CA  
10855 C C   . TYR D 90  ? 0.3785 0.4463 0.4010 -0.0714 -0.0363 -0.0674 90  TYR D C   
10856 O O   . TYR D 90  ? 0.3942 0.4485 0.4069 -0.0724 -0.0352 -0.0697 90  TYR D O   
10857 C CB  . TYR D 90  ? 0.3666 0.4555 0.3880 -0.0700 -0.0486 -0.0728 90  TYR D CB  
10858 C CG  . TYR D 90  ? 0.3480 0.4414 0.3676 -0.0602 -0.0490 -0.0668 90  TYR D CG  
10859 C CD1 . TYR D 90  ? 0.3400 0.4204 0.3514 -0.0544 -0.0445 -0.0623 90  TYR D CD1 
10860 C CD2 . TYR D 90  ? 0.3406 0.4511 0.3666 -0.0566 -0.0539 -0.0657 90  TYR D CD2 
10861 C CE1 . TYR D 90  ? 0.3559 0.4393 0.3653 -0.0462 -0.0447 -0.0571 90  TYR D CE1 
10862 C CE2 . TYR D 90  ? 0.3286 0.4415 0.3520 -0.0476 -0.0540 -0.0603 90  TYR D CE2 
10863 C CZ  . TYR D 90  ? 0.3557 0.4544 0.3705 -0.0428 -0.0492 -0.0561 90  TYR D CZ  
10864 O OH  . TYR D 90  ? 0.3339 0.4336 0.3459 -0.0345 -0.0488 -0.0509 90  TYR D OH  
10865 N N   . ALA D 91  ? 0.3351 0.4030 0.3613 -0.0669 -0.0324 -0.0617 91  ALA D N   
10866 C CA  . ALA D 91  ? 0.3380 0.3908 0.3570 -0.0630 -0.0274 -0.0579 91  ALA D CA  
10867 C C   . ALA D 91  ? 0.3727 0.4164 0.3947 -0.0685 -0.0220 -0.0579 91  ALA D C   
10868 O O   . ALA D 91  ? 0.4307 0.4804 0.4617 -0.0705 -0.0198 -0.0561 91  ALA D O   
10869 C CB  . ALA D 91  ? 0.3270 0.3833 0.3467 -0.0553 -0.0263 -0.0520 91  ALA D CB  
10870 N N   . GLU D 92  ? 0.3874 0.4157 0.4013 -0.0699 -0.0194 -0.0592 92  GLU D N   
10871 C CA  . GLU D 92  ? 0.3632 0.3809 0.3784 -0.0746 -0.0143 -0.0589 92  GLU D CA  
10872 C C   . GLU D 92  ? 0.3620 0.3751 0.3777 -0.0699 -0.0099 -0.0529 92  GLU D C   
10873 O O   . GLU D 92  ? 0.3302 0.3396 0.3497 -0.0732 -0.0059 -0.0515 92  GLU D O   
10874 C CB  . GLU D 92  ? 0.4030 0.4051 0.4088 -0.0767 -0.0129 -0.0622 92  GLU D CB  
10875 C CG  . GLU D 92  ? 0.4893 0.4945 0.4957 -0.0839 -0.0163 -0.0688 92  GLU D CG  
10876 C CD  . GLU D 92  ? 0.5110 0.5204 0.5107 -0.0810 -0.0217 -0.0720 92  GLU D CD  
10877 O OE1 . GLU D 92  ? 0.4636 0.4681 0.4586 -0.0859 -0.0235 -0.0777 92  GLU D OE1 
10878 O OE2 . GLU D 92  ? 0.4297 0.4459 0.4276 -0.0738 -0.0240 -0.0689 92  GLU D OE2 
10879 N N   . GLY D 93  ? 0.3619 0.3743 0.3730 -0.0626 -0.0105 -0.0495 93  GLY D N   
10880 C CA  . GLY D 93  ? 0.3369 0.3431 0.3467 -0.0582 -0.0067 -0.0444 93  GLY D CA  
10881 C C   . GLY D 93  ? 0.3103 0.3268 0.3241 -0.0534 -0.0079 -0.0408 93  GLY D C   
10882 O O   . GLY D 93  ? 0.3029 0.3302 0.3188 -0.0520 -0.0117 -0.0419 93  GLY D O   
10883 N N   . VAL D 94  ? 0.2724 0.2853 0.2867 -0.0509 -0.0046 -0.0366 94  VAL D N   
10884 C CA  . VAL D 94  ? 0.2897 0.3087 0.3053 -0.0453 -0.0051 -0.0329 94  VAL D CA  
10885 C C   . VAL D 94  ? 0.3099 0.3187 0.3203 -0.0417 -0.0023 -0.0292 94  VAL D C   
10886 O O   . VAL D 94  ? 0.3260 0.3260 0.3349 -0.0438 0.0008  -0.0286 94  VAL D O   
10887 C CB  . VAL D 94  ? 0.2452 0.2747 0.2694 -0.0466 -0.0043 -0.0319 94  VAL D CB  
10888 C CG1 . VAL D 94  ? 0.2728 0.2963 0.2989 -0.0499 0.0004  -0.0306 94  VAL D CG1 
10889 C CG2 . VAL D 94  ? 0.2603 0.2960 0.2851 -0.0403 -0.0051 -0.0286 94  VAL D CG2 
10890 N N   . THR D 95  ? 0.2313 0.2410 0.2386 -0.0363 -0.0034 -0.0268 95  THR D N   
10891 C CA  . THR D 95  ? 0.2467 0.2477 0.2495 -0.0332 -0.0013 -0.0237 95  THR D CA  
10892 C C   . THR D 95  ? 0.3084 0.3131 0.3106 -0.0284 -0.0020 -0.0207 95  THR D C   
10893 O O   . THR D 95  ? 0.3110 0.3218 0.3129 -0.0261 -0.0044 -0.0211 95  THR D O   
10894 C CB  . THR D 95  ? 0.2935 0.2868 0.2905 -0.0324 -0.0015 -0.0247 95  THR D CB  
10895 O OG1 . THR D 95  ? 0.3032 0.2897 0.2974 -0.0297 0.0003  -0.0218 95  THR D OG1 
10896 C CG2 . THR D 95  ? 0.2788 0.2762 0.2730 -0.0300 -0.0043 -0.0259 95  THR D CG2 
10897 N N   . LEU D 96  ? 0.2647 0.2651 0.2660 -0.0270 0.0003  -0.0178 96  LEU D N   
10898 C CA  . LEU D 96  ? 0.2736 0.2746 0.2731 -0.0228 0.0002  -0.0150 96  LEU D CA  
10899 C C   . LEU D 96  ? 0.2696 0.2621 0.2645 -0.0213 0.0012  -0.0131 96  LEU D C   
10900 O O   . LEU D 96  ? 0.2850 0.2717 0.2791 -0.0229 0.0028  -0.0129 96  LEU D O   
10901 C CB  . LEU D 96  ? 0.2546 0.2594 0.2576 -0.0226 0.0019  -0.0136 96  LEU D CB  
10902 C CG  . LEU D 96  ? 0.2683 0.2703 0.2680 -0.0186 0.0026  -0.0107 96  LEU D CG  
10903 C CD1 . LEU D 96  ? 0.3703 0.3769 0.3690 -0.0152 0.0003  -0.0105 96  LEU D CD1 
10904 C CD2 . LEU D 96  ? 0.3607 0.3643 0.3625 -0.0183 0.0050  -0.0094 96  LEU D CD2 
10905 N N   . THR D 97  ? 0.2898 0.2816 0.2818 -0.0182 0.0004  -0.0117 97  THR D N   
10906 C CA  . THR D 97  ? 0.2638 0.2493 0.2526 -0.0169 0.0011  -0.0098 97  THR D CA  
10907 C C   . THR D 97  ? 0.3062 0.2916 0.2940 -0.0150 0.0017  -0.0077 97  THR D C   
10908 O O   . THR D 97  ? 0.3224 0.3117 0.3103 -0.0130 0.0011  -0.0073 97  THR D O   
10909 C CB  . THR D 97  ? 0.2853 0.2694 0.2717 -0.0156 0.0003  -0.0100 97  THR D CB  
10910 O OG1 . THR D 97  ? 0.2930 0.2756 0.2796 -0.0173 0.0003  -0.0121 97  THR D OG1 
10911 C CG2 . THR D 97  ? 0.2871 0.2666 0.2716 -0.0146 0.0008  -0.0081 97  THR D CG2 
10912 N N   . GLN D 98  ? 0.3006 0.2812 0.2870 -0.0153 0.0028  -0.0064 98  GLN D N   
10913 C CA  . GLN D 98  ? 0.2779 0.2572 0.2626 -0.0139 0.0037  -0.0048 98  GLN D CA  
10914 C C   . GLN D 98  ? 0.2816 0.2602 0.2636 -0.0115 0.0030  -0.0038 98  GLN D C   
10915 O O   . GLN D 98  ? 0.3109 0.2872 0.2912 -0.0113 0.0022  -0.0035 98  GLN D O   
10916 C CB  . GLN D 98  ? 0.3280 0.3011 0.3101 -0.0147 0.0043  -0.0039 98  GLN D CB  
10917 C CG  . GLN D 98  ? 0.3325 0.3017 0.3107 -0.0135 0.0047  -0.0024 98  GLN D CG  
10918 C CD  . GLN D 98  ? 0.3417 0.3058 0.3174 -0.0144 0.0050  -0.0017 98  GLN D CD  
10919 O OE1 . GLN D 98  ? 0.3333 0.2965 0.3091 -0.0154 0.0067  -0.0015 98  GLN D OE1 
10920 N NE2 . GLN D 98  ? 0.3355 0.2964 0.3092 -0.0141 0.0032  -0.0011 98  GLN D NE2 
10921 N N   A SER D 99  ? 0.2889 0.2697 0.2707 -0.0096 0.0038  -0.0032 99  SER D N   
10922 N N   B SER D 99  ? 0.2889 0.2691 0.2704 -0.0096 0.0039  -0.0031 99  SER D N   
10923 C CA  A SER D 99  ? 0.2883 0.2658 0.2661 -0.0071 0.0039  -0.0020 99  SER D CA  
10924 C CA  B SER D 99  ? 0.2881 0.2660 0.2661 -0.0070 0.0038  -0.0020 99  SER D CA  
10925 C C   A SER D 99  ? 0.3216 0.3004 0.2995 -0.0053 0.0056  -0.0014 99  SER D C   
10926 C C   B SER D 99  ? 0.3228 0.3004 0.2997 -0.0051 0.0055  -0.0013 99  SER D C   
10927 O O   A SER D 99  ? 0.2840 0.2610 0.2617 -0.0064 0.0071  -0.0014 99  SER D O   
10928 O O   B SER D 99  ? 0.3053 0.2789 0.2802 -0.0058 0.0068  -0.0010 99  SER D O   
10929 C CB  A SER D 99  ? 0.3012 0.2806 0.2783 -0.0054 0.0028  -0.0018 99  SER D CB  
10930 C CB  B SER D 99  ? 0.3009 0.2825 0.2793 -0.0055 0.0026  -0.0022 99  SER D CB  
10931 O OG  A SER D 99  ? 0.3234 0.2972 0.2957 -0.0039 0.0032  -0.0004 99  SER D OG  
10932 O OG  B SER D 99  ? 0.3158 0.3049 0.2982 -0.0048 0.0022  -0.0031 99  SER D OG  
10933 N N   . CYS D 100 ? 0.3036 0.2856 0.2817 -0.0021 0.0057  -0.0010 100 CYS D N   
10934 C CA  . CYS D 100 ? 0.3387 0.3218 0.3167 0.0005  0.0077  -0.0003 100 CYS D CA  
10935 C C   . CYS D 100 ? 0.2788 0.2664 0.2614 -0.0013 0.0094  -0.0010 100 CYS D C   
10936 O O   . CYS D 100 ? 0.3250 0.3188 0.3130 -0.0037 0.0086  -0.0022 100 CYS D O   
10937 C CB  . CYS D 100 ? 0.3378 0.3268 0.3176 0.0044  0.0071  0.0001  100 CYS D CB  
10938 S SG  . CYS D 100 ? 0.3441 0.3370 0.3256 0.0087  0.0097  0.0009  100 CYS D SG  
10939 N N   . ILE D 101 ? 0.2545 0.2387 0.2346 -0.0004 0.0121  -0.0004 101 ILE D N   
10940 C CA  . ILE D 101 ? 0.2736 0.2610 0.2574 -0.0026 0.0144  -0.0008 101 ILE D CA  
10941 C C   . ILE D 101 ? 0.2897 0.2883 0.2813 -0.0015 0.0152  -0.0013 101 ILE D C   
10942 O O   . ILE D 101 ? 0.3120 0.3157 0.3090 -0.0045 0.0166  -0.0020 101 ILE D O   
10943 C CB  . ILE D 101 ? 0.3008 0.2813 0.2791 -0.0021 0.0174  0.0000  101 ILE D CB  
10944 C CG1 . ILE D 101 ? 0.3125 0.2913 0.2874 0.0025  0.0192  0.0007  101 ILE D CG1 
10945 C CG2 . ILE D 101 ? 0.2933 0.2643 0.2648 -0.0038 0.0157  0.0003  101 ILE D CG2 
10946 C CD1 . ILE D 101 ? 0.3509 0.3241 0.3205 0.0033  0.0230  0.0012  101 ILE D CD1 
10947 N N   . GLN D 102 ? 0.2758 0.2784 0.2682 0.0029  0.0148  -0.0008 102 GLN D N   
10948 C CA  . GLN D 102 ? 0.2841 0.2990 0.2849 0.0043  0.0150  -0.0013 102 GLN D CA  
10949 C C   . GLN D 102 ? 0.2954 0.3178 0.3023 0.0006  0.0120  -0.0030 102 GLN D C   
10950 O O   . GLN D 102 ? 0.3205 0.3523 0.3353 -0.0017 0.0126  -0.0042 102 GLN D O   
10951 C CB  . GLN D 102 ? 0.3076 0.3250 0.3074 0.0106  0.0145  -0.0001 102 GLN D CB  
10952 C CG  . GLN D 102 ? 0.2980 0.3062 0.2906 0.0142  0.0176  0.0013  102 GLN D CG  
10953 C CD  . GLN D 102 ? 0.3685 0.3811 0.3621 0.0210  0.0185  0.0024  102 GLN D CD  
10954 O OE1 . GLN D 102 ? 0.3305 0.3554 0.3320 0.0229  0.0171  0.0022  102 GLN D OE1 
10955 N NE2 . GLN D 102 ? 0.3728 0.3752 0.3582 0.0248  0.0205  0.0035  102 GLN D NE2 
10956 N N   . TYR D 103 ? 0.3045 0.3230 0.3077 -0.0001 0.0089  -0.0034 103 TYR D N   
10957 C CA  . TYR D 103 ? 0.3135 0.3374 0.3207 -0.0033 0.0060  -0.0053 103 TYR D CA  
10958 C C   . TYR D 103 ? 0.3349 0.3574 0.3446 -0.0089 0.0074  -0.0067 103 TYR D C   
10959 O O   . TYR D 103 ? 0.3450 0.3738 0.3601 -0.0123 0.0061  -0.0087 103 TYR D O   
10960 C CB  . TYR D 103 ? 0.3413 0.3594 0.3425 -0.0023 0.0034  -0.0051 103 TYR D CB  
10961 C CG  . TYR D 103 ? 0.3760 0.4000 0.3786 -0.0022 0.0000  -0.0064 103 TYR D CG  
10962 C CD1 . TYR D 103 ? 0.3921 0.4251 0.4012 -0.0052 -0.0016 -0.0088 103 TYR D CD1 
10963 C CD2 . TYR D 103 ? 0.4577 0.4774 0.4542 0.0006  -0.0017 -0.0054 103 TYR D CD2 
10964 C CE1 . TYR D 103 ? 0.3973 0.4351 0.4064 -0.0051 -0.0052 -0.0103 103 TYR D CE1 
10965 C CE2 . TYR D 103 ? 0.4106 0.4346 0.4067 0.0009  -0.0047 -0.0065 103 TYR D CE2 
10966 C CZ  . TYR D 103 ? 0.4501 0.4831 0.4521 -0.0018 -0.0067 -0.0091 103 TYR D CZ  
10967 O OH  . TYR D 103 ? 0.4668 0.5034 0.4669 -0.0014 -0.0101 -0.0104 103 TYR D OH  
10968 N N   . ARG D 104 ? 0.3234 0.3374 0.3290 -0.0100 0.0100  -0.0056 104 ARG D N   
10969 C CA  . ARG D 104 ? 0.3215 0.3331 0.3287 -0.0149 0.0117  -0.0064 104 ARG D CA  
10970 C C   . ARG D 104 ? 0.3159 0.3363 0.3309 -0.0172 0.0139  -0.0073 104 ARG D C   
10971 O O   . ARG D 104 ? 0.3024 0.3236 0.3207 -0.0220 0.0145  -0.0087 104 ARG D O   
10972 C CB  . ARG D 104 ? 0.3240 0.3250 0.3245 -0.0149 0.0138  -0.0048 104 ARG D CB  
10973 C CG  . ARG D 104 ? 0.3211 0.3149 0.3154 -0.0133 0.0114  -0.0042 104 ARG D CG  
10974 C CD  . ARG D 104 ? 0.3132 0.2975 0.3009 -0.0132 0.0126  -0.0027 104 ARG D CD  
10975 N NE  . ARG D 104 ? 0.3173 0.2967 0.3001 -0.0112 0.0105  -0.0022 104 ARG D NE  
10976 C CZ  . ARG D 104 ? 0.3272 0.2990 0.3044 -0.0112 0.0103  -0.0013 104 ARG D CZ  
10977 N NH1 . ARG D 104 ? 0.3162 0.2839 0.2910 -0.0125 0.0119  -0.0006 104 ARG D NH1 
10978 N NH2 . ARG D 104 ? 0.3005 0.2689 0.2742 -0.0099 0.0085  -0.0009 104 ARG D NH2 
10979 N N   . GLN D 105 ? 0.3094 0.3370 0.3280 -0.0140 0.0153  -0.0066 105 GLN D N   
10980 C CA  . GLN D 105 ? 0.2829 0.3215 0.3108 -0.0161 0.0174  -0.0075 105 GLN D CA  
10981 C C   . GLN D 105 ? 0.3061 0.3551 0.3414 -0.0187 0.0139  -0.0101 105 GLN D C   
10982 O O   . GLN D 105 ? 0.3156 0.3712 0.3583 -0.0235 0.0151  -0.0117 105 GLN D O   
10983 C CB  . GLN D 105 ? 0.3284 0.3729 0.3586 -0.0110 0.0195  -0.0061 105 GLN D CB  
10984 C CG  . GLN D 105 ? 0.3203 0.3553 0.3434 -0.0087 0.0233  -0.0041 105 GLN D CG  
10985 C CD  . GLN D 105 ? 0.3229 0.3639 0.3482 -0.0029 0.0254  -0.0029 105 GLN D CD  
10986 O OE1 . GLN D 105 ? 0.3269 0.3714 0.3555 -0.0029 0.0299  -0.0024 105 GLN D OE1 
10987 N NE2 . GLN D 105 ? 0.3150 0.3568 0.3381 0.0023  0.0225  -0.0024 105 GLN D NE2 
10988 N N   . THR D 106 ? 0.2634 0.3146 0.2970 -0.0155 0.0096  -0.0105 106 THR D N   
10989 C CA  . THR D 106 ? 0.2939 0.3543 0.3328 -0.0177 0.0057  -0.0131 106 THR D CA  
10990 C C   . THR D 106 ? 0.2997 0.3549 0.3381 -0.0243 0.0056  -0.0153 106 THR D C   
10991 O O   . THR D 106 ? 0.3165 0.3791 0.3619 -0.0290 0.0051  -0.0178 106 THR D O   
10992 C CB  . THR D 106 ? 0.2797 0.3396 0.3136 -0.0131 0.0014  -0.0128 106 THR D CB  
10993 O OG1 . THR D 106 ? 0.2929 0.3554 0.3259 -0.0066 0.0019  -0.0104 106 THR D OG1 
10994 C CG2 . THR D 106 ? 0.2711 0.3395 0.3084 -0.0151 -0.0033 -0.0157 106 THR D CG2 
10995 N N   . PHE D 107 ? 0.2714 0.3137 0.3016 -0.0245 0.0062  -0.0144 107 PHE D N   
10996 C CA  . PHE D 107 ? 0.2656 0.3010 0.2939 -0.0296 0.0064  -0.0161 107 PHE D CA  
10997 C C   . PHE D 107 ? 0.2737 0.3086 0.3062 -0.0345 0.0104  -0.0164 107 PHE D C   
10998 O O   . PHE D 107 ? 0.2941 0.3303 0.3301 -0.0400 0.0103  -0.0189 107 PHE D O   
10999 C CB  . PHE D 107 ? 0.2846 0.3073 0.3040 -0.0277 0.0065  -0.0145 107 PHE D CB  
11000 C CG  . PHE D 107 ? 0.2886 0.3028 0.3054 -0.0320 0.0073  -0.0157 107 PHE D CG  
11001 C CD1 . PHE D 107 ? 0.2761 0.2898 0.2921 -0.0339 0.0047  -0.0184 107 PHE D CD1 
11002 C CD2 . PHE D 107 ? 0.2897 0.2960 0.3041 -0.0336 0.0108  -0.0142 107 PHE D CD2 
11003 C CE1 . PHE D 107 ? 0.2931 0.2978 0.3062 -0.0373 0.0059  -0.0195 107 PHE D CE1 
11004 C CE2 . PHE D 107 ? 0.3338 0.3313 0.3452 -0.0367 0.0117  -0.0150 107 PHE D CE2 
11005 C CZ  . PHE D 107 ? 0.3255 0.3223 0.3366 -0.0386 0.0093  -0.0178 107 PHE D CZ  
11006 N N   . GLY D 108 ? 0.2741 0.3060 0.3053 -0.0328 0.0143  -0.0137 108 GLY D N   
11007 C CA  . GLY D 108 ? 0.2736 0.3036 0.3074 -0.0374 0.0188  -0.0135 108 GLY D CA  
11008 C C   . GLY D 108 ? 0.3080 0.3513 0.3528 -0.0412 0.0197  -0.0155 108 GLY D C   
11009 O O   . GLY D 108 ? 0.3333 0.3758 0.3814 -0.0474 0.0217  -0.0170 108 GLY D O   
11010 N N   . SER D 109 ? 0.2684 0.3245 0.3195 -0.0377 0.0182  -0.0156 109 SER D N   
11011 C CA  . SER D 109 ? 0.2707 0.3415 0.3337 -0.0414 0.0185  -0.0177 109 SER D CA  
11012 C C   . SER D 109 ? 0.2932 0.3680 0.3593 -0.0461 0.0140  -0.0215 109 SER D C   
11013 O O   . SER D 109 ? 0.2855 0.3664 0.3594 -0.0527 0.0151  -0.0239 109 SER D O   
11014 C CB  . SER D 109 ? 0.3239 0.4080 0.3931 -0.0357 0.0177  -0.0168 109 SER D CB  
11015 O OG  . SER D 109 ? 0.3257 0.4064 0.3926 -0.0321 0.0226  -0.0138 109 SER D OG  
11016 N N   . TRP D 110 ? 0.2631 0.3342 0.3230 -0.0431 0.0092  -0.0222 110 TRP D N   
11017 C CA  . TRP D 110 ? 0.2711 0.3454 0.3324 -0.0470 0.0047  -0.0261 110 TRP D CA  
11018 C C   . TRP D 110 ? 0.3089 0.3735 0.3683 -0.0543 0.0069  -0.0281 110 TRP D C   
11019 O O   . TRP D 110 ? 0.3022 0.3729 0.3682 -0.0606 0.0062  -0.0315 110 TRP D O   
11020 C CB  . TRP D 110 ? 0.2625 0.3326 0.3159 -0.0420 0.0003  -0.0259 110 TRP D CB  
11021 C CG  . TRP D 110 ? 0.2572 0.3304 0.3100 -0.0444 -0.0047 -0.0297 110 TRP D CG  
11022 C CD1 . TRP D 110 ? 0.2831 0.3493 0.3334 -0.0504 -0.0050 -0.0329 110 TRP D CD1 
11023 C CD2 . TRP D 110 ? 0.2641 0.3456 0.3164 -0.0402 -0.0099 -0.0305 110 TRP D CD2 
11024 N NE1 . TRP D 110 ? 0.3068 0.3776 0.3555 -0.0503 -0.0103 -0.0361 110 TRP D NE1 
11025 C CE2 . TRP D 110 ? 0.2727 0.3529 0.3224 -0.0441 -0.0134 -0.0344 110 TRP D CE2 
11026 C CE3 . TRP D 110 ? 0.2875 0.3769 0.3406 -0.0333 -0.0118 -0.0282 110 TRP D CE3 
11027 C CZ2 . TRP D 110 ? 0.2524 0.3393 0.3001 -0.0414 -0.0189 -0.0361 110 TRP D CZ2 
11028 C CZ3 . TRP D 110 ? 0.2798 0.3757 0.3310 -0.0303 -0.0173 -0.0295 110 TRP D CZ3 
11029 C CH2 . TRP D 110 ? 0.2950 0.3897 0.3434 -0.0345 -0.0208 -0.0334 110 TRP D CH2 
11030 N N   A ARG D 111 ? 0.3082 0.3574 0.3587 -0.0535 0.0095  -0.0261 111 ARG D N   
11031 N N   B ARG D 111 ? 0.3080 0.3573 0.3586 -0.0534 0.0096  -0.0260 111 ARG D N   
11032 C CA  A ARG D 111 ? 0.3301 0.3690 0.3780 -0.0597 0.0117  -0.0277 111 ARG D CA  
11033 C CA  B ARG D 111 ? 0.3307 0.3692 0.3782 -0.0593 0.0117  -0.0275 111 ARG D CA  
11034 C C   A ARG D 111 ? 0.3336 0.3757 0.3888 -0.0658 0.0163  -0.0280 111 ARG D C   
11035 C C   B ARG D 111 ? 0.3338 0.3741 0.3877 -0.0654 0.0166  -0.0276 111 ARG D C   
11036 O O   A ARG D 111 ? 0.3273 0.3666 0.3843 -0.0727 0.0172  -0.0308 111 ARG D O   
11037 O O   B ARG D 111 ? 0.3323 0.3670 0.3863 -0.0719 0.0179  -0.0299 111 ARG D O   
11038 C CB  A ARG D 111 ? 0.3490 0.3718 0.3863 -0.0567 0.0135  -0.0250 111 ARG D CB  
11039 C CB  B ARG D 111 ? 0.3485 0.3711 0.3852 -0.0559 0.0131  -0.0249 111 ARG D CB  
11040 C CG  A ARG D 111 ? 0.3480 0.3670 0.3830 -0.0534 0.0176  -0.0208 111 ARG D CG  
11041 C CG  B ARG D 111 ? 0.3633 0.3788 0.3970 -0.0547 0.0182  -0.0210 111 ARG D CG  
11042 C CD  A ARG D 111 ? 0.4047 0.4077 0.4310 -0.0535 0.0204  -0.0187 111 ARG D CD  
11043 C CD  B ARG D 111 ? 0.3877 0.3871 0.4111 -0.0528 0.0192  -0.0190 111 ARG D CD  
11044 N NE  A ARG D 111 ? 0.4074 0.4054 0.4277 -0.0479 0.0213  -0.0151 111 ARG D NE  
11045 N NE  B ARG D 111 ? 0.4130 0.4070 0.4316 -0.0489 0.0218  -0.0151 111 ARG D NE  
11046 C CZ  A ARG D 111 ? 0.4259 0.4266 0.4470 -0.0460 0.0241  -0.0127 111 ARG D CZ  
11047 C CZ  B ARG D 111 ? 0.4052 0.3887 0.4157 -0.0455 0.0215  -0.0129 111 ARG D CZ  
11048 N NH1 A ARG D 111 ? 0.3737 0.3816 0.4018 -0.0493 0.0274  -0.0130 111 ARG D NH1 
11049 N NH1 B ARG D 111 ? 0.4294 0.4069 0.4359 -0.0448 0.0191  -0.0140 111 ARG D NH1 
11050 N NH2 A ARG D 111 ? 0.3604 0.3565 0.3754 -0.0407 0.0238  -0.0101 111 ARG D NH2 
11051 N NH2 B ARG D 111 ? 0.4175 0.3969 0.4237 -0.0426 0.0237  -0.0098 111 ARG D NH2 
11052 N N   . LEU D 112 ? 0.3110 0.3592 0.3705 -0.0637 0.0196  -0.0253 112 LEU D N   
11053 C CA  . LEU D 112 ? 0.3367 0.3877 0.4029 -0.0697 0.0249  -0.0253 112 LEU D CA  
11054 C C   . LEU D 112 ? 0.3104 0.3780 0.3893 -0.0749 0.0230  -0.0290 112 LEU D C   
11055 O O   . LEU D 112 ? 0.3579 0.4263 0.4423 -0.0827 0.0261  -0.0308 112 LEU D O   
11056 C CB  . LEU D 112 ? 0.3266 0.3796 0.3934 -0.0657 0.0295  -0.0214 112 LEU D CB  
11057 C CG  . LEU D 112 ? 0.4015 0.4381 0.4566 -0.0625 0.0327  -0.0177 112 LEU D CG  
11058 C CD1 . LEU D 112 ? 0.4007 0.4415 0.4565 -0.0578 0.0365  -0.0145 112 LEU D CD1 
11059 C CD2 . LEU D 112 ? 0.3931 0.4165 0.4439 -0.0687 0.0370  -0.0175 112 LEU D CD2 
11060 N N   . HIS D 113 ? 0.2956 0.3770 0.3796 -0.0708 0.0180  -0.0301 113 HIS D N   
11061 C CA  . HIS D 113 ? 0.2647 0.3654 0.3625 -0.0744 0.0160  -0.0330 113 HIS D CA  
11062 C C   . HIS D 113 ? 0.3148 0.4230 0.4146 -0.0761 0.0087  -0.0375 113 HIS D C   
11063 O O   . HIS D 113 ? 0.3013 0.4256 0.4128 -0.0802 0.0066  -0.0405 113 HIS D O   
11064 C CB  . HIS D 113 ? 0.2634 0.3774 0.3676 -0.0677 0.0167  -0.0304 113 HIS D CB  
11065 C CG  . HIS D 113 ? 0.2702 0.3798 0.3742 -0.0668 0.0241  -0.0268 113 HIS D CG  
11066 N ND1 . HIS D 113 ? 0.3193 0.4325 0.4311 -0.0738 0.0297  -0.0272 113 HIS D ND1 
11067 C CD2 . HIS D 113 ? 0.3309 0.4321 0.4269 -0.0601 0.0270  -0.0227 113 HIS D CD2 
11068 C CE1 . HIS D 113 ? 0.3155 0.4229 0.4238 -0.0708 0.0359  -0.0233 113 HIS D CE1 
11069 N NE2 . HIS D 113 ? 0.2856 0.3853 0.3840 -0.0626 0.0341  -0.0208 113 HIS D NE2 
11070 N N   . VAL D 114 ? 0.2938 0.3919 0.3831 -0.0731 0.0049  -0.0380 114 VAL D N   
11071 C CA  . VAL D 114 ? 0.2596 0.3638 0.3495 -0.0750 -0.0018 -0.0425 114 VAL D CA  
11072 C C   . VAL D 114 ? 0.3139 0.4086 0.4018 -0.0841 -0.0007 -0.0463 114 VAL D C   
11073 O O   . VAL D 114 ? 0.3150 0.3923 0.3924 -0.0841 0.0013  -0.0456 114 VAL D O   
11074 C CB  . VAL D 114 ? 0.2681 0.3672 0.3478 -0.0674 -0.0062 -0.0414 114 VAL D CB  
11075 C CG1 . VAL D 114 ? 0.2859 0.3904 0.3648 -0.0694 -0.0127 -0.0460 114 VAL D CG1 
11076 C CG2 . VAL D 114 ? 0.2797 0.3879 0.3616 -0.0588 -0.0069 -0.0377 114 VAL D CG2 
11077 N N   . PRO D 115 ? 0.3115 0.4173 0.4098 -0.0920 -0.0017 -0.0504 115 PRO D N   
11078 C CA  . PRO D 115 ? 0.3540 0.4494 0.4509 -0.1016 0.0007  -0.0539 115 PRO D CA  
11079 C C   . PRO D 115 ? 0.3627 0.4459 0.4487 -0.1025 -0.0030 -0.0572 115 PRO D C   
11080 O O   . PRO D 115 ? 0.3726 0.4414 0.4536 -0.1084 0.0000  -0.0590 115 PRO D O   
11081 C CB  . PRO D 115 ? 0.3651 0.4784 0.4768 -0.1096 -0.0007 -0.0579 115 PRO D CB  
11082 C CG  . PRO D 115 ? 0.3951 0.5285 0.5154 -0.1034 -0.0047 -0.0567 115 PRO D CG  
11083 C CD  . PRO D 115 ? 0.3251 0.4530 0.4356 -0.0922 -0.0063 -0.0526 115 PRO D CD  
11084 N N   . THR D 116 ? 0.3354 0.4229 0.4169 -0.0965 -0.0090 -0.0580 116 THR D N   
11085 C CA  . THR D 116 ? 0.3093 0.3854 0.3799 -0.0969 -0.0122 -0.0612 116 THR D CA  
11086 C C   . THR D 116 ? 0.3556 0.4131 0.4135 -0.0912 -0.0091 -0.0577 116 THR D C   
11087 O O   . THR D 116 ? 0.3790 0.4256 0.4275 -0.0912 -0.0106 -0.0601 116 THR D O   
11088 C CB  . THR D 116 ? 0.3553 0.4439 0.4257 -0.0930 -0.0198 -0.0636 116 THR D CB  
11089 O OG1 . THR D 116 ? 0.3357 0.4326 0.4077 -0.0841 -0.0206 -0.0588 116 THR D OG1 
11090 C CG2 . THR D 116 ? 0.3472 0.4526 0.4286 -0.1001 -0.0242 -0.0687 116 THR D CG2 
11091 N N   . VAL D 117 ? 0.3414 0.3956 0.3989 -0.0862 -0.0049 -0.0522 117 VAL D N   
11092 C CA  . VAL D 117 ? 0.3270 0.3648 0.3736 -0.0812 -0.0021 -0.0489 117 VAL D CA  
11093 C C   . VAL D 117 ? 0.3779 0.3995 0.4195 -0.0868 0.0020  -0.0502 117 VAL D C   
11094 O O   . VAL D 117 ? 0.3960 0.4159 0.4422 -0.0919 0.0064  -0.0496 117 VAL D O   
11095 C CB  . VAL D 117 ? 0.2977 0.3361 0.3450 -0.0753 0.0011  -0.0432 117 VAL D CB  
11096 C CG1 . VAL D 117 ? 0.3329 0.3547 0.3695 -0.0708 0.0037  -0.0399 117 VAL D CG1 
11097 C CG2 . VAL D 117 ? 0.3552 0.4079 0.4063 -0.0692 -0.0028 -0.0418 117 VAL D CG2 
11098 N N   . LYS D 118 ? 0.3815 0.3906 0.4133 -0.0853 0.0011  -0.0517 118 LYS D N   
11099 C CA  . LYS D 118 ? 0.3770 0.3686 0.4023 -0.0888 0.0052  -0.0524 118 LYS D CA  
11100 C C   . LYS D 118 ? 0.3985 0.3777 0.4163 -0.0825 0.0085  -0.0474 118 LYS D C   
11101 O O   . LYS D 118 ? 0.3817 0.3478 0.3958 -0.0845 0.0129  -0.0462 118 LYS D O   
11102 C CB  . LYS D 118 ? 0.3634 0.3478 0.3822 -0.0915 0.0027  -0.0577 118 LYS D CB  
11103 C CG  . LYS D 118 ? 0.4254 0.4223 0.4496 -0.0969 -0.0023 -0.0633 118 LYS D CG  
11104 C CD  . LYS D 118 ? 0.5461 0.5323 0.5652 -0.1039 -0.0024 -0.0692 118 LYS D CD  
11105 C CE  . LYS D 118 ? 0.6181 0.6182 0.6451 -0.1114 -0.0069 -0.0749 118 LYS D CE  
11106 N NZ  . LYS D 118 ? 0.6483 0.6552 0.6710 -0.1086 -0.0136 -0.0785 118 LYS D NZ  
11107 N N   . TRP D 119 ? 0.3432 0.3261 0.3587 -0.0749 0.0065  -0.0445 119 TRP D N   
11108 C CA  . TRP D 119 ? 0.3719 0.3453 0.3818 -0.0692 0.0092  -0.0398 119 TRP D CA  
11109 C C   . TRP D 119 ? 0.3028 0.2854 0.3144 -0.0628 0.0073  -0.0364 119 TRP D C   
11110 O O   . TRP D 119 ? 0.3407 0.3343 0.3552 -0.0614 0.0035  -0.0378 119 TRP D O   
11111 C CB  . TRP D 119 ? 0.3432 0.3038 0.3442 -0.0666 0.0093  -0.0407 119 TRP D CB  
11112 C CG  . TRP D 119 ? 0.3757 0.3410 0.3741 -0.0635 0.0051  -0.0430 119 TRP D CG  
11113 C CD1 . TRP D 119 ? 0.4038 0.3702 0.4008 -0.0670 0.0025  -0.0482 119 TRP D CD1 
11114 C CD2 . TRP D 119 ? 0.3643 0.3331 0.3604 -0.0566 0.0033  -0.0404 119 TRP D CD2 
11115 N NE1 . TRP D 119 ? 0.4637 0.4342 0.4571 -0.0620 -0.0007 -0.0486 119 TRP D NE1 
11116 C CE2 . TRP D 119 ? 0.4039 0.3757 0.3969 -0.0559 0.0000  -0.0437 119 TRP D CE2 
11117 C CE3 . TRP D 119 ? 0.3432 0.3125 0.3391 -0.0512 0.0043  -0.0356 119 TRP D CE3 
11118 C CZ2 . TRP D 119 ? 0.3829 0.3577 0.3727 -0.0499 -0.0018 -0.0420 119 TRP D CZ2 
11119 C CZ3 . TRP D 119 ? 0.3782 0.3506 0.3714 -0.0458 0.0022  -0.0343 119 TRP D CZ3 
11120 C CH2 . TRP D 119 ? 0.3969 0.3719 0.3872 -0.0452 -0.0006 -0.0373 119 TRP D CH2 
11121 N N   . ASP D 120 ? 0.3049 0.2818 0.3136 -0.0587 0.0098  -0.0320 120 ASP D N   
11122 C CA  . ASP D 120 ? 0.3058 0.2891 0.3150 -0.0528 0.0084  -0.0287 120 ASP D CA  
11123 C C   . ASP D 120 ? 0.3185 0.2919 0.3212 -0.0481 0.0096  -0.0255 120 ASP D C   
11124 O O   . ASP D 120 ? 0.3286 0.2910 0.3273 -0.0490 0.0121  -0.0248 120 ASP D O   
11125 C CB  . ASP D 120 ? 0.2946 0.2859 0.3099 -0.0536 0.0100  -0.0268 120 ASP D CB  
11126 C CG  . ASP D 120 ? 0.3720 0.3549 0.3857 -0.0552 0.0147  -0.0242 120 ASP D CG  
11127 O OD1 . ASP D 120 ? 0.3905 0.3680 0.3997 -0.0510 0.0159  -0.0207 120 ASP D OD1 
11128 O OD2 . ASP D 120 ? 0.4291 0.4100 0.4454 -0.0610 0.0172  -0.0257 120 ASP D OD2 
11129 N N   . TYR D 121 ? 0.2766 0.2537 0.2780 -0.0429 0.0078  -0.0234 121 TYR D N   
11130 C CA  . TYR D 121 ? 0.2784 0.2479 0.2748 -0.0387 0.0086  -0.0204 121 TYR D CA  
11131 C C   . TYR D 121 ? 0.2797 0.2548 0.2765 -0.0346 0.0073  -0.0179 121 TYR D C   
11132 O O   . TYR D 121 ? 0.2962 0.2782 0.2942 -0.0329 0.0049  -0.0187 121 TYR D O   
11133 C CB  . TYR D 121 ? 0.2942 0.2584 0.2864 -0.0370 0.0075  -0.0218 121 TYR D CB  
11134 C CG  . TYR D 121 ? 0.2968 0.2529 0.2849 -0.0334 0.0086  -0.0190 121 TYR D CG  
11135 C CD1 . TYR D 121 ? 0.3070 0.2655 0.2942 -0.0292 0.0074  -0.0166 121 TYR D CD1 
11136 C CD2 . TYR D 121 ? 0.3265 0.2724 0.3116 -0.0343 0.0110  -0.0187 121 TYR D CD2 
11137 C CE1 . TYR D 121 ? 0.3154 0.2683 0.2999 -0.0261 0.0079  -0.0143 121 TYR D CE1 
11138 C CE2 . TYR D 121 ? 0.3435 0.2831 0.3251 -0.0304 0.0115  -0.0160 121 TYR D CE2 
11139 C CZ  . TYR D 121 ? 0.3142 0.2580 0.2960 -0.0265 0.0097  -0.0139 121 TYR D CZ  
11140 O OH  . TYR D 121 ? 0.3065 0.2456 0.2859 -0.0228 0.0098  -0.0115 121 TYR D OH  
11141 N N   . TYR D 122 ? 0.2738 0.2449 0.2686 -0.0328 0.0090  -0.0148 122 TYR D N   
11142 C CA  . TYR D 122 ? 0.2815 0.2553 0.2754 -0.0291 0.0082  -0.0124 122 TYR D CA  
11143 C C   . TYR D 122 ? 0.2893 0.2573 0.2789 -0.0260 0.0073  -0.0109 122 TYR D C   
11144 O O   . TYR D 122 ? 0.2922 0.2531 0.2791 -0.0258 0.0085  -0.0097 122 TYR D O   
11145 C CB  . TYR D 122 ? 0.2875 0.2609 0.2818 -0.0296 0.0106  -0.0104 122 TYR D CB  
11146 C CG  . TYR D 122 ? 0.2964 0.2712 0.2888 -0.0261 0.0102  -0.0082 122 TYR D CG  
11147 C CD1 . TYR D 122 ? 0.2915 0.2599 0.2789 -0.0238 0.0099  -0.0062 122 TYR D CD1 
11148 C CD2 . TYR D 122 ? 0.4091 0.3913 0.4045 -0.0251 0.0101  -0.0082 122 TYR D CD2 
11149 C CE1 . TYR D 122 ? 0.3071 0.2757 0.2921 -0.0211 0.0095  -0.0045 122 TYR D CE1 
11150 C CE2 . TYR D 122 ? 0.3571 0.3388 0.3498 -0.0217 0.0101  -0.0063 122 TYR D CE2 
11151 C CZ  . TYR D 122 ? 0.3408 0.3154 0.3280 -0.0201 0.0097  -0.0047 122 TYR D CZ  
11152 O OH  . TYR D 122 ? 0.3585 0.3314 0.3422 -0.0174 0.0096  -0.0032 122 TYR D OH  
11153 N N   . VAL D 123 ? 0.2645 0.2357 0.2537 -0.0235 0.0054  -0.0108 123 VAL D N   
11154 C CA  . VAL D 123 ? 0.2679 0.2355 0.2545 -0.0209 0.0046  -0.0096 123 VAL D CA  
11155 C C   . VAL D 123 ? 0.2805 0.2481 0.2656 -0.0190 0.0043  -0.0072 123 VAL D C   
11156 O O   . VAL D 123 ? 0.2964 0.2681 0.2819 -0.0180 0.0035  -0.0070 123 VAL D O   
11157 C CB  . VAL D 123 ? 0.2920 0.2625 0.2787 -0.0198 0.0032  -0.0110 123 VAL D CB  
11158 C CG1 . VAL D 123 ? 0.3198 0.2875 0.3050 -0.0175 0.0029  -0.0095 123 VAL D CG1 
11159 C CG2 . VAL D 123 ? 0.2755 0.2456 0.2625 -0.0216 0.0034  -0.0137 123 VAL D CG2 
11160 N N   . PRO D 124 ? 0.2952 0.2578 0.2779 -0.0184 0.0047  -0.0054 124 PRO D N   
11161 C CA  . PRO D 124 ? 0.2843 0.2464 0.2646 -0.0169 0.0040  -0.0036 124 PRO D CA  
11162 C C   . PRO D 124 ? 0.3086 0.2714 0.2888 -0.0153 0.0022  -0.0032 124 PRO D C   
11163 O O   . PRO D 124 ? 0.3208 0.2810 0.2996 -0.0144 0.0012  -0.0021 124 PRO D O   
11164 C CB  . PRO D 124 ? 0.3419 0.2983 0.3190 -0.0170 0.0050  -0.0021 124 PRO D CB  
11165 C CG  . PRO D 124 ? 0.3701 0.3235 0.3481 -0.0185 0.0064  -0.0028 124 PRO D CG  
11166 C CD  . PRO D 124 ? 0.2826 0.2390 0.2636 -0.0189 0.0057  -0.0049 124 PRO D CD  
11167 N N   . MET D 125 ? 0.2896 0.2563 0.2713 -0.0150 0.0018  -0.0041 125 MET D N   
11168 C CA  . MET D 125 ? 0.2830 0.2505 0.2646 -0.0141 0.0008  -0.0036 125 MET D CA  
11169 C C   . MET D 125 ? 0.2657 0.2313 0.2449 -0.0138 0.0001  -0.0023 125 MET D C   
11170 O O   . MET D 125 ? 0.2765 0.2418 0.2539 -0.0136 0.0008  -0.0021 125 MET D O   
11171 C CB  . MET D 125 ? 0.2830 0.2541 0.2654 -0.0137 0.0009  -0.0045 125 MET D CB  
11172 C CG  . MET D 125 ? 0.3158 0.2875 0.2982 -0.0131 0.0006  -0.0039 125 MET D CG  
11173 S SD  . MET D 125 ? 0.2973 0.2712 0.2778 -0.0122 0.0010  -0.0039 125 MET D SD  
11174 C CE  . MET D 125 ? 0.3149 0.2871 0.2950 -0.0126 0.0013  -0.0025 125 MET D CE  
11175 N N   . PRO D 126 ? 0.2681 0.2326 0.2472 -0.0137 -0.0011 -0.0016 126 PRO D N   
11176 C CA  . PRO D 126 ? 0.2924 0.2547 0.2686 -0.0139 -0.0021 -0.0009 126 PRO D CA  
11177 C C   . PRO D 126 ? 0.2836 0.2459 0.2582 -0.0139 -0.0013 -0.0010 126 PRO D C   
11178 O O   . PRO D 126 ? 0.2901 0.2548 0.2662 -0.0136 -0.0006 -0.0012 126 PRO D O   
11179 C CB  . PRO D 126 ? 0.2865 0.2503 0.2651 -0.0143 -0.0038 -0.0007 126 PRO D CB  
11180 C CG  . PRO D 126 ? 0.3037 0.2688 0.2851 -0.0133 -0.0037 -0.0008 126 PRO D CG  
11181 C CD  . PRO D 126 ? 0.3067 0.2724 0.2886 -0.0132 -0.0018 -0.0017 126 PRO D CD  
11182 N N   . ASN D 127 ? 0.2866 0.2455 0.2572 -0.0137 -0.0010 -0.0006 127 ASN D N   
11183 C CA  . ASN D 127 ? 0.2818 0.2390 0.2499 -0.0131 -0.0002 -0.0005 127 ASN D CA  
11184 C C   . ASN D 127 ? 0.2981 0.2530 0.2650 -0.0146 -0.0013 -0.0004 127 ASN D C   
11185 O O   . ASN D 127 ? 0.2822 0.2363 0.2484 -0.0146 -0.0004 -0.0002 127 ASN D O   
11186 C CB  . ASN D 127 ? 0.2574 0.2111 0.2211 -0.0121 0.0009  -0.0003 127 ASN D CB  
11187 C CG  . ASN D 127 ? 0.3180 0.2751 0.2837 -0.0107 0.0026  -0.0004 127 ASN D CG  
11188 O OD1 . ASN D 127 ? 0.2954 0.2571 0.2648 -0.0104 0.0027  -0.0007 127 ASN D OD1 
11189 N ND2 . ASN D 127 ? 0.3223 0.2774 0.2855 -0.0100 0.0039  -0.0002 127 ASN D ND2 
11190 N N   . GLU D 128 ? 0.2816 0.2354 0.2483 -0.0160 -0.0032 -0.0006 128 GLU D N   
11191 C CA  . GLU D 128 ? 0.3078 0.2600 0.2739 -0.0182 -0.0045 -0.0008 128 GLU D CA  
11192 C C   . GLU D 128 ? 0.3044 0.2619 0.2766 -0.0193 -0.0048 -0.0008 128 GLU D C   
11193 O O   . GLU D 128 ? 0.2973 0.2577 0.2728 -0.0204 -0.0068 -0.0009 128 GLU D O   
11194 C CB  . GLU D 128 ? 0.2754 0.2246 0.2382 -0.0194 -0.0069 -0.0013 128 GLU D CB  
11195 C CG  . GLU D 128 ? 0.3048 0.2517 0.2663 -0.0222 -0.0082 -0.0021 128 GLU D CG  
11196 C CD  . GLU D 128 ? 0.3234 0.2661 0.2797 -0.0234 -0.0106 -0.0030 128 GLU D CD  
11197 O OE1 . GLU D 128 ? 0.3178 0.2590 0.2707 -0.0215 -0.0111 -0.0027 128 GLU D OE1 
11198 O OE2 . GLU D 128 ? 0.3469 0.2883 0.3027 -0.0265 -0.0123 -0.0041 128 GLU D OE2 
11199 N N   . VAL D 129 ? 0.2759 0.2348 0.2494 -0.0187 -0.0028 -0.0004 129 VAL D N   
11200 C CA  . VAL D 129 ? 0.2951 0.2585 0.2736 -0.0195 -0.0022 -0.0003 129 VAL D CA  
11201 C C   . VAL D 129 ? 0.3040 0.2675 0.2842 -0.0226 -0.0028 -0.0004 129 VAL D C   
11202 O O   . VAL D 129 ? 0.3095 0.2780 0.2951 -0.0236 -0.0026 -0.0003 129 VAL D O   
11203 C CB  . VAL D 129 ? 0.3047 0.2685 0.2823 -0.0181 0.0002  0.0001  129 VAL D CB  
11204 C CG1 . VAL D 129 ? 0.3037 0.2692 0.2813 -0.0158 0.0003  -0.0003 129 VAL D CG1 
11205 C CG2 . VAL D 129 ? 0.3161 0.2743 0.2883 -0.0181 0.0015  0.0008  129 VAL D CG2 
11206 N N   . GLN D 130 ? 0.2785 0.2365 0.2542 -0.0243 -0.0034 -0.0007 130 GLN D N   
11207 C CA  . GLN D 130 ? 0.2612 0.2192 0.2386 -0.0281 -0.0045 -0.0012 130 GLN D CA  
11208 C C   . GLN D 130 ? 0.3133 0.2760 0.2946 -0.0291 -0.0080 -0.0020 130 GLN D C   
11209 O O   . GLN D 130 ? 0.3112 0.2765 0.2961 -0.0325 -0.0094 -0.0026 130 GLN D O   
11210 C CB  . GLN D 130 ? 0.2810 0.2303 0.2512 -0.0297 -0.0041 -0.0017 130 GLN D CB  
11211 C CG  . GLN D 130 ? 0.3040 0.2486 0.2708 -0.0289 -0.0005 -0.0005 130 GLN D CG  
11212 C CD  . GLN D 130 ? 0.3049 0.2394 0.2635 -0.0292 0.0004  -0.0008 130 GLN D CD  
11213 O OE1 . GLN D 130 ? 0.3240 0.2545 0.2803 -0.0323 -0.0011 -0.0021 130 GLN D OE1 
11214 N NE2 . GLN D 130 ? 0.3230 0.2535 0.2771 -0.0257 0.0027  0.0003  130 GLN D NE2 
11215 N N   . SER D 131 ? 0.2832 0.2469 0.2637 -0.0264 -0.0096 -0.0019 131 SER D N   
11216 C CA  . SER D 131 ? 0.3010 0.2683 0.2840 -0.0265 -0.0132 -0.0022 131 SER D CA  
11217 C C   . SER D 131 ? 0.2888 0.2647 0.2805 -0.0260 -0.0134 -0.0018 131 SER D C   
11218 O O   . SER D 131 ? 0.2907 0.2684 0.2846 -0.0239 -0.0109 -0.0012 131 SER D O   
11219 C CB  . SER D 131 ? 0.3142 0.2791 0.2932 -0.0234 -0.0141 -0.0017 131 SER D CB  
11220 O OG  . SER D 131 ? 0.2983 0.2674 0.2801 -0.0226 -0.0173 -0.0015 131 SER D OG  
11221 N N   . PRO D 132 ? 0.3282 0.3097 0.3248 -0.0276 -0.0165 -0.0022 132 PRO D N   
11222 C CA  . PRO D 132 ? 0.2717 0.2622 0.2772 -0.0263 -0.0166 -0.0017 132 PRO D CA  
11223 C C   . PRO D 132 ? 0.2786 0.2697 0.2842 -0.0216 -0.0167 -0.0008 132 PRO D C   
11224 O O   . PRO D 132 ? 0.2962 0.2936 0.3085 -0.0197 -0.0160 -0.0004 132 PRO D O   
11225 C CB  . PRO D 132 ? 0.3174 0.3139 0.3277 -0.0288 -0.0208 -0.0025 132 PRO D CB  
11226 C CG  . PRO D 132 ? 0.3765 0.3659 0.3785 -0.0310 -0.0235 -0.0035 132 PRO D CG  
11227 C CD  . PRO D 132 ? 0.2877 0.2677 0.2821 -0.0312 -0.0198 -0.0035 132 PRO D CD  
11228 N N   . HIS D 133 ? 0.2724 0.2571 0.2709 -0.0198 -0.0173 -0.0005 133 HIS D N   
11229 C CA  . HIS D 133 ? 0.2629 0.2467 0.2606 -0.0158 -0.0172 0.0004  133 HIS D CA  
11230 C C   . HIS D 133 ? 0.2797 0.2593 0.2748 -0.0146 -0.0134 0.0005  133 HIS D C   
11231 O O   . HIS D 133 ? 0.2638 0.2420 0.2585 -0.0119 -0.0126 0.0010  133 HIS D O   
11232 C CB  . HIS D 133 ? 0.2799 0.2596 0.2715 -0.0149 -0.0204 0.0009  133 HIS D CB  
11233 C CG  . HIS D 133 ? 0.3042 0.2884 0.2980 -0.0162 -0.0249 0.0005  133 HIS D CG  
11234 N ND1 . HIS D 133 ? 0.3256 0.3179 0.3267 -0.0144 -0.0271 0.0010  133 HIS D ND1 
11235 C CD2 . HIS D 133 ? 0.3194 0.3018 0.3093 -0.0191 -0.0277 -0.0005 133 HIS D CD2 
11236 C CE1 . HIS D 133 ? 0.3083 0.3047 0.3108 -0.0164 -0.0315 0.0004  133 HIS D CE1 
11237 N NE2 . HIS D 133 ? 0.2972 0.2871 0.2924 -0.0196 -0.0319 -0.0008 133 HIS D NE2 
11238 N N   . ALA D 134 ? 0.2714 0.2490 0.2647 -0.0166 -0.0112 -0.0001 134 ALA D N   
11239 C CA  . ALA D 134 ? 0.2897 0.2639 0.2800 -0.0155 -0.0084 -0.0002 134 ALA D CA  
11240 C C   . ALA D 134 ? 0.3132 0.2905 0.3076 -0.0139 -0.0064 -0.0004 134 ALA D C   
11241 O O   . ALA D 134 ? 0.3008 0.2759 0.2936 -0.0125 -0.0051 -0.0007 134 ALA D O   
11242 C CB  . ALA D 134 ? 0.2884 0.2596 0.2752 -0.0173 -0.0070 -0.0005 134 ALA D CB  
11243 N N   . ARG D 135 ? 0.2737 0.2562 0.2734 -0.0144 -0.0059 -0.0005 135 ARG D N   
11244 C CA  . ARG D 135 ? 0.2723 0.2572 0.2749 -0.0127 -0.0033 -0.0009 135 ARG D CA  
11245 C C   . ARG D 135 ? 0.3040 0.2891 0.3082 -0.0096 -0.0038 -0.0008 135 ARG D C   
11246 O O   . ARG D 135 ? 0.3380 0.3211 0.3411 -0.0080 -0.0018 -0.0015 135 ARG D O   
11247 C CB  . ARG D 135 ? 0.2934 0.2837 0.3010 -0.0141 -0.0019 -0.0008 135 ARG D CB  
11248 C CG  . ARG D 135 ? 0.2997 0.2874 0.3037 -0.0162 0.0001  -0.0008 135 ARG D CG  
11249 C CD  . ARG D 135 ? 0.2992 0.2906 0.3070 -0.0188 0.0013  -0.0004 135 ARG D CD  
11250 N NE  . ARG D 135 ? 0.2930 0.2798 0.2957 -0.0206 0.0031  0.0000  135 ARG D NE  
11251 C CZ  . ARG D 135 ? 0.3286 0.3105 0.3268 -0.0221 0.0017  0.0001  135 ARG D CZ  
11252 N NH1 . ARG D 135 ? 0.3292 0.3100 0.3269 -0.0225 -0.0015 -0.0002 135 ARG D NH1 
11253 N NH2 . ARG D 135 ? 0.3401 0.3173 0.3332 -0.0227 0.0036  0.0007  135 ARG D NH2 
11254 N N   . LYS D 136 ? 0.2791 0.2660 0.2853 -0.0087 -0.0065 0.0000  136 LYS D N   
11255 C CA  . LYS D 136 ? 0.3105 0.2958 0.3168 -0.0052 -0.0071 0.0006  136 LYS D CA  
11256 C C   . LYS D 136 ? 0.3438 0.3213 0.3434 -0.0050 -0.0066 0.0006  136 LYS D C   
11257 O O   . LYS D 136 ? 0.2969 0.2710 0.2954 -0.0031 -0.0049 0.0003  136 LYS D O   
11258 C CB  . LYS D 136 ? 0.2601 0.2493 0.2693 -0.0040 -0.0107 0.0017  136 LYS D CB  
11259 C CG  . LYS D 136 ? 0.3381 0.3246 0.3462 0.0005  -0.0116 0.0029  136 LYS D CG  
11260 C CD  . LYS D 136 ? 0.3729 0.3607 0.3847 0.0037  -0.0089 0.0026  136 LYS D CD  
11261 C CE  . LYS D 136 ? 0.4687 0.4513 0.4776 0.0081  -0.0096 0.0039  136 LYS D CE  
11262 N NZ  . LYS D 136 ? 0.4774 0.4591 0.4885 0.0119  -0.0067 0.0035  136 LYS D NZ  
11263 N N   . ALA D 137 ? 0.2858 0.2601 0.2809 -0.0071 -0.0077 0.0008  137 ALA D N   
11264 C CA  . ALA D 137 ? 0.2628 0.2307 0.2525 -0.0073 -0.0065 0.0008  137 ALA D CA  
11265 C C   . ALA D 137 ? 0.2916 0.2586 0.2812 -0.0080 -0.0037 -0.0007 137 ALA D C   
11266 O O   . ALA D 137 ? 0.2841 0.2473 0.2721 -0.0074 -0.0023 -0.0011 137 ALA D O   
11267 C CB  . ALA D 137 ? 0.2780 0.2433 0.2632 -0.0091 -0.0076 0.0012  137 ALA D CB  
11268 N N   . HIS D 138 ? 0.3006 0.2710 0.2918 -0.0094 -0.0028 -0.0015 138 HIS D N   
11269 C CA  . HIS D 138 ? 0.2733 0.2432 0.2637 -0.0099 -0.0008 -0.0029 138 HIS D CA  
11270 C C   . HIS D 138 ? 0.2732 0.2433 0.2654 -0.0082 0.0007  -0.0039 138 HIS D C   
11271 O O   . HIS D 138 ? 0.2960 0.2635 0.2863 -0.0085 0.0020  -0.0053 138 HIS D O   
11272 C CB  . HIS D 138 ? 0.2551 0.2276 0.2452 -0.0113 -0.0002 -0.0032 138 HIS D CB  
11273 C CG  . HIS D 138 ? 0.2865 0.2585 0.2745 -0.0118 0.0010  -0.0045 138 HIS D CG  
11274 N ND1 . HIS D 138 ? 0.2909 0.2605 0.2772 -0.0124 0.0010  -0.0051 138 HIS D ND1 
11275 C CD2 . HIS D 138 ? 0.3066 0.2804 0.2938 -0.0118 0.0020  -0.0053 138 HIS D CD2 
11276 C CE1 . HIS D 138 ? 0.2842 0.2552 0.2696 -0.0129 0.0016  -0.0065 138 HIS D CE1 
11277 N NE2 . HIS D 138 ? 0.3036 0.2768 0.2890 -0.0123 0.0020  -0.0065 138 HIS D NE2 
11278 N N   . TYR D 139 ? 0.2710 0.2443 0.2669 -0.0065 0.0005  -0.0033 139 TYR D N   
11279 C CA  . TYR D 139 ? 0.2749 0.2476 0.2724 -0.0040 0.0022  -0.0041 139 TYR D CA  
11280 C C   . TYR D 139 ? 0.3077 0.2737 0.3019 -0.0031 0.0025  -0.0044 139 TYR D C   
11281 O O   . TYR D 139 ? 0.3026 0.2651 0.2949 -0.0028 0.0044  -0.0061 139 TYR D O   
11282 C CB  . TYR D 139 ? 0.3132 0.2910 0.3161 -0.0017 0.0015  -0.0029 139 TYR D CB  
11283 C CG  . TYR D 139 ? 0.2958 0.2736 0.3009 0.0018  0.0036  -0.0035 139 TYR D CG  
11284 C CD1 . TYR D 139 ? 0.3484 0.3213 0.3521 0.0048  0.0033  -0.0030 139 TYR D CD1 
11285 C CD2 . TYR D 139 ? 0.2795 0.2612 0.2871 0.0024  0.0062  -0.0045 139 TYR D CD2 
11286 C CE1 . TYR D 139 ? 0.3811 0.3530 0.3862 0.0087  0.0056  -0.0036 139 TYR D CE1 
11287 C CE2 . TYR D 139 ? 0.3118 0.2928 0.3208 0.0062  0.0087  -0.0053 139 TYR D CE2 
11288 C CZ  . TYR D 139 ? 0.3436 0.3198 0.3515 0.0093  0.0083  -0.0048 139 TYR D CZ  
11289 O OH  . TYR D 139 ? 0.3598 0.3345 0.3685 0.0135  0.0110  -0.0056 139 TYR D OH  
11290 N N   . GLU D 140 ? 0.2684 0.2318 0.2612 -0.0027 0.0007  -0.0027 140 GLU D N   
11291 C CA  . GLU D 140 ? 0.2578 0.2138 0.2469 -0.0019 0.0015  -0.0025 140 GLU D CA  
11292 C C   . GLU D 140 ? 0.2690 0.2214 0.2548 -0.0052 0.0027  -0.0040 140 GLU D C   
11293 O O   . GLU D 140 ? 0.3042 0.2508 0.2876 -0.0054 0.0044  -0.0050 140 GLU D O   
11294 C CB  . GLU D 140 ? 0.2970 0.2511 0.2847 -0.0003 -0.0007 -0.0001 140 GLU D CB  
11295 C CG  . GLU D 140 ? 0.3117 0.2704 0.3035 0.0033  -0.0025 0.0012  140 GLU D CG  
11296 C CD  . GLU D 140 ? 0.3910 0.3477 0.3843 0.0073  -0.0007 0.0010  140 GLU D CD  
11297 O OE1 . GLU D 140 ? 0.4022 0.3520 0.3921 0.0073  0.0019  -0.0002 140 GLU D OE1 
11298 O OE2 . GLU D 140 ? 0.3989 0.3612 0.3969 0.0106  -0.0020 0.0020  140 GLU D OE2 
11299 N N   . GLU D 141 ? 0.2811 0.2369 0.2669 -0.0077 0.0021  -0.0042 141 GLU D N   
11300 C CA  . GLU D 141 ? 0.2657 0.2201 0.2497 -0.0105 0.0032  -0.0057 141 GLU D CA  
11301 C C   . GLU D 141 ? 0.2756 0.2306 0.2599 -0.0111 0.0044  -0.0083 141 GLU D C   
11302 O O   . GLU D 141 ? 0.3091 0.2606 0.2919 -0.0130 0.0055  -0.0100 141 GLU D O   
11303 C CB  . GLU D 141 ? 0.2566 0.2150 0.2407 -0.0122 0.0023  -0.0053 141 GLU D CB  
11304 C CG  . GLU D 141 ? 0.3003 0.2572 0.2827 -0.0119 0.0012  -0.0032 141 GLU D CG  
11305 C CD  . GLU D 141 ? 0.3530 0.3044 0.3324 -0.0129 0.0024  -0.0026 141 GLU D CD  
11306 O OE1 . GLU D 141 ? 0.3426 0.2913 0.3219 -0.0143 0.0042  -0.0038 141 GLU D OE1 
11307 O OE2 . GLU D 141 ? 0.3399 0.2891 0.3167 -0.0123 0.0017  -0.0008 141 GLU D OE2 
11308 N N   . VAL D 142 ? 0.2853 0.2444 0.2713 -0.0099 0.0044  -0.0087 142 VAL D N   
11309 C CA  . VAL D 142 ? 0.2696 0.2288 0.2546 -0.0102 0.0056  -0.0113 142 VAL D CA  
11310 C C   . VAL D 142 ? 0.2791 0.2323 0.2626 -0.0089 0.0072  -0.0126 142 VAL D C   
11311 O O   . VAL D 142 ? 0.3006 0.2504 0.2817 -0.0106 0.0081  -0.0151 142 VAL D O   
11312 C CB  . VAL D 142 ? 0.3146 0.2790 0.3010 -0.0090 0.0058  -0.0110 142 VAL D CB  
11313 C CG1 . VAL D 142 ? 0.2907 0.2546 0.2749 -0.0086 0.0073  -0.0135 142 VAL D CG1 
11314 C CG2 . VAL D 142 ? 0.3040 0.2724 0.2904 -0.0105 0.0045  -0.0100 142 VAL D CG2 
11315 N N   . GLN D 143 ? 0.2919 0.2435 0.2768 -0.0059 0.0075  -0.0109 143 GLN D N   
11316 C CA  . GLN D 143 ? 0.3081 0.2525 0.2910 -0.0039 0.0092  -0.0117 143 GLN D CA  
11317 C C   . GLN D 143 ? 0.3464 0.2835 0.3259 -0.0065 0.0097  -0.0122 143 GLN D C   
11318 O O   . GLN D 143 ? 0.3175 0.2478 0.2940 -0.0072 0.0115  -0.0144 143 GLN D O   
11319 C CB  . GLN D 143 ? 0.2957 0.2405 0.2811 0.0005  0.0090  -0.0093 143 GLN D CB  
11320 C CG  . GLN D 143 ? 0.3367 0.2731 0.3195 0.0037  0.0109  -0.0095 143 GLN D CG  
11321 C CD  . GLN D 143 ? 0.3582 0.2913 0.3391 0.0046  0.0136  -0.0126 143 GLN D CD  
11322 O OE1 . GLN D 143 ? 0.3365 0.2746 0.3182 0.0036  0.0140  -0.0143 143 GLN D OE1 
11323 N NE2 . GLN D 143 ? 0.3798 0.3033 0.3571 0.0067  0.0155  -0.0132 143 GLN D NE2 
11324 N N   . ALA D 144 ? 0.2905 0.2280 0.2702 -0.0079 0.0085  -0.0101 144 ALA D N   
11325 C CA  . ALA D 144 ? 0.3082 0.2390 0.2849 -0.0108 0.0095  -0.0103 144 ALA D CA  
11326 C C   . ALA D 144 ? 0.3274 0.2590 0.3039 -0.0151 0.0102  -0.0136 144 ALA D C   
11327 O O   . ALA D 144 ? 0.3307 0.2555 0.3048 -0.0175 0.0119  -0.0153 144 ALA D O   
11328 C CB  . ALA D 144 ? 0.3164 0.2483 0.2929 -0.0116 0.0085  -0.0075 144 ALA D CB  
11329 N N   . PHE D 145 ? 0.3003 0.2400 0.2790 -0.0161 0.0087  -0.0146 145 PHE D N   
11330 C CA  . PHE D 145 ? 0.2968 0.2388 0.2755 -0.0198 0.0086  -0.0177 145 PHE D CA  
11331 C C   . PHE D 145 ? 0.3304 0.2680 0.3064 -0.0196 0.0096  -0.0209 145 PHE D C   
11332 O O   . PHE D 145 ? 0.3282 0.2628 0.3027 -0.0231 0.0101  -0.0239 145 PHE D O   
11333 C CB  . PHE D 145 ? 0.2828 0.2340 0.2636 -0.0198 0.0067  -0.0175 145 PHE D CB  
11334 C CG  . PHE D 145 ? 0.3097 0.2653 0.2914 -0.0232 0.0057  -0.0200 145 PHE D CG  
11335 C CD1 . PHE D 145 ? 0.3321 0.2849 0.3140 -0.0271 0.0064  -0.0221 145 PHE D CD1 
11336 C CD2 . PHE D 145 ? 0.3240 0.2871 0.3064 -0.0225 0.0039  -0.0201 145 PHE D CD2 
11337 C CE1 . PHE D 145 ? 0.3242 0.2829 0.3080 -0.0305 0.0050  -0.0246 145 PHE D CE1 
11338 C CE2 . PHE D 145 ? 0.3324 0.3009 0.3160 -0.0250 0.0025  -0.0222 145 PHE D CE2 
11339 C CZ  . PHE D 145 ? 0.3537 0.3209 0.3386 -0.0291 0.0028  -0.0246 145 PHE D CZ  
11340 N N   . ARG D 146 ? 0.3186 0.2559 0.2940 -0.0157 0.0102  -0.0204 146 ARG D N   
11341 C CA  . ARG D 146 ? 0.3161 0.2484 0.2882 -0.0147 0.0117  -0.0234 146 ARG D CA  
11342 C C   . ARG D 146 ? 0.3298 0.2513 0.2988 -0.0156 0.0137  -0.0244 146 ARG D C   
11343 O O   . ARG D 146 ? 0.3599 0.2761 0.3254 -0.0181 0.0146  -0.0281 146 ARG D O   
11344 C CB  . ARG D 146 ? 0.3642 0.2987 0.3372 -0.0099 0.0126  -0.0220 146 ARG D CB  
11345 C CG  . ARG D 146 ? 0.3885 0.3170 0.3575 -0.0081 0.0149  -0.0251 146 ARG D CG  
11346 C CD  . ARG D 146 ? 0.4251 0.3510 0.3954 -0.0029 0.0167  -0.0230 146 ARG D CD  
11347 N NE  . ARG D 146 ? 0.4285 0.3512 0.3959 0.0001  0.0194  -0.0253 146 ARG D NE  
11348 C CZ  . ARG D 146 ? 0.4466 0.3737 0.4172 0.0048  0.0207  -0.0236 146 ARG D CZ  
11349 N NH1 . ARG D 146 ? 0.3828 0.3176 0.3594 0.0062  0.0192  -0.0201 146 ARG D NH1 
11350 N NH2 . ARG D 146 ? 0.4383 0.3626 0.4061 0.0077  0.0237  -0.0258 146 ARG D NH2 
11351 N N   . VAL D 147 ? 0.3234 0.2407 0.2929 -0.0138 0.0143  -0.0212 147 VAL D N   
11352 C CA  . VAL D 147 ? 0.3768 0.2823 0.3424 -0.0143 0.0166  -0.0215 147 VAL D CA  
11353 C C   . VAL D 147 ? 0.3717 0.2746 0.3365 -0.0207 0.0169  -0.0236 147 VAL D C   
11354 O O   . VAL D 147 ? 0.3510 0.2450 0.3121 -0.0234 0.0188  -0.0265 147 VAL D O   
11355 C CB  . VAL D 147 ? 0.3820 0.2846 0.3479 -0.0106 0.0168  -0.0171 147 VAL D CB  
11356 C CG1 . VAL D 147 ? 0.4231 0.3132 0.3844 -0.0117 0.0191  -0.0165 147 VAL D CG1 
11357 C CG2 . VAL D 147 ? 0.3708 0.2755 0.3381 -0.0042 0.0167  -0.0157 147 VAL D CG2 
11358 N N   . PHE D 148 ? 0.3436 0.2545 0.3121 -0.0233 0.0153  -0.0223 148 PHE D N   
11359 C CA  . PHE D 148 ? 0.3407 0.2523 0.3103 -0.0295 0.0154  -0.0244 148 PHE D CA  
11360 C C   . PHE D 148 ? 0.3046 0.2169 0.2731 -0.0327 0.0148  -0.0294 148 PHE D C   
11361 O O   . PHE D 148 ? 0.3512 0.2576 0.3181 -0.0374 0.0160  -0.0322 148 PHE D O   
11362 C CB  . PHE D 148 ? 0.3152 0.2374 0.2894 -0.0306 0.0136  -0.0225 148 PHE D CB  
11363 C CG  . PHE D 148 ? 0.3220 0.2486 0.2992 -0.0366 0.0134  -0.0248 148 PHE D CG  
11364 C CD1 . PHE D 148 ? 0.3386 0.2734 0.3179 -0.0385 0.0111  -0.0280 148 PHE D CD1 
11365 C CD2 . PHE D 148 ? 0.3024 0.2255 0.2803 -0.0400 0.0155  -0.0236 148 PHE D CD2 
11366 C CE1 . PHE D 148 ? 0.3027 0.2433 0.2859 -0.0437 0.0104  -0.0302 148 PHE D CE1 
11367 C CE2 . PHE D 148 ? 0.3617 0.2905 0.3438 -0.0456 0.0156  -0.0257 148 PHE D CE2 
11368 C CZ  . PHE D 148 ? 0.3059 0.2442 0.2913 -0.0474 0.0127  -0.0291 148 PHE D CZ  
11369 N N   . LEU D 149 ? 0.3087 0.2286 0.2779 -0.0307 0.0127  -0.0305 149 LEU D N   
11370 C CA  . LEU D 149 ? 0.3344 0.2560 0.3018 -0.0336 0.0115  -0.0352 149 LEU D CA  
11371 C C   . LEU D 149 ? 0.3482 0.2582 0.3097 -0.0335 0.0137  -0.0383 149 LEU D C   
11372 O O   . LEU D 149 ? 0.3782 0.2851 0.3374 -0.0381 0.0135  -0.0427 149 LEU D O   
11373 C CB  . LEU D 149 ? 0.3339 0.2650 0.3019 -0.0306 0.0093  -0.0351 149 LEU D CB  
11374 C CG  . LEU D 149 ? 0.3162 0.2582 0.2891 -0.0310 0.0070  -0.0328 149 LEU D CG  
11375 C CD1 . LEU D 149 ? 0.3414 0.2897 0.3138 -0.0268 0.0058  -0.0314 149 LEU D CD1 
11376 C CD2 . LEU D 149 ? 0.3414 0.2887 0.3164 -0.0363 0.0050  -0.0359 149 LEU D CD2 
11377 N N   . GLN D 150 ? 0.3563 0.2598 0.3153 -0.0281 0.0159  -0.0363 150 GLN D N   
11378 C CA  . GLN D 150 ? 0.3724 0.2634 0.3255 -0.0269 0.0186  -0.0388 150 GLN D CA  
11379 C C   . GLN D 150 ? 0.3775 0.2582 0.3284 -0.0318 0.0204  -0.0402 150 GLN D C   
11380 O O   . GLN D 150 ? 0.4157 0.2867 0.3613 -0.0344 0.0219  -0.0444 150 GLN D O   
11381 C CB  . GLN D 150 ? 0.4475 0.3345 0.4002 -0.0199 0.0206  -0.0351 150 GLN D CB  
11382 C CG  . GLN D 150 ? 0.4753 0.3648 0.4267 -0.0155 0.0210  -0.0359 150 GLN D CG  
11383 C CD  . GLN D 150 ? 0.4799 0.3688 0.4332 -0.0086 0.0225  -0.0320 150 GLN D CD  
11384 O OE1 . GLN D 150 ? 0.5453 0.4296 0.4993 -0.0070 0.0231  -0.0288 150 GLN D OE1 
11385 N NE2 . GLN D 150 ? 0.4839 0.3778 0.4379 -0.0046 0.0230  -0.0322 150 GLN D NE2 
11386 N N   . THR D 151 ? 0.3707 0.2511 0.3245 -0.0325 0.0209  -0.0363 151 THR D N   
11387 C CA  . THR D 151 ? 0.3992 0.2690 0.3508 -0.0371 0.0234  -0.0368 151 THR D CA  
11388 C C   . THR D 151 ? 0.4223 0.2961 0.3758 -0.0451 0.0221  -0.0411 151 THR D C   
11389 O O   . THR D 151 ? 0.4090 0.2728 0.3589 -0.0499 0.0240  -0.0446 151 THR D O   
11390 C CB  . THR D 151 ? 0.4079 0.2778 0.3618 -0.0360 0.0242  -0.0316 151 THR D CB  
11391 O OG1 . THR D 151 ? 0.4157 0.2841 0.3684 -0.0284 0.0244  -0.0277 151 THR D OG1 
11392 C CG2 . THR D 151 ? 0.3871 0.2442 0.3374 -0.0403 0.0275  -0.0317 151 THR D CG2 
11393 N N   . LEU D 152 ? 0.3615 0.2501 0.3210 -0.0465 0.0189  -0.0410 152 LEU D N   
11394 C CA  . LEU D 152 ? 0.3525 0.2479 0.3157 -0.0537 0.0171  -0.0446 152 LEU D CA  
11395 C C   . LEU D 152 ? 0.4119 0.3039 0.3708 -0.0567 0.0160  -0.0506 152 LEU D C   
11396 O O   . LEU D 152 ? 0.4259 0.3145 0.3847 -0.0637 0.0163  -0.0545 152 LEU D O   
11397 C CB  . LEU D 152 ? 0.3830 0.2949 0.3526 -0.0525 0.0137  -0.0428 152 LEU D CB  
11398 C CG  . LEU D 152 ? 0.3911 0.3137 0.3657 -0.0584 0.0109  -0.0462 152 LEU D CG  
11399 C CD1 . LEU D 152 ? 0.4289 0.3512 0.4082 -0.0634 0.0131  -0.0449 152 LEU D CD1 
11400 C CD2 . LEU D 152 ? 0.3802 0.3170 0.3589 -0.0547 0.0076  -0.0441 152 LEU D CD2 
11401 N N   . THR D 153 ? 0.3950 0.2886 0.3502 -0.0518 0.0147  -0.0516 153 THR D N   
11402 C CA  . THR D 153 ? 0.4425 0.3331 0.3923 -0.0539 0.0135  -0.0574 153 THR D CA  
11403 C C   . THR D 153 ? 0.4522 0.3255 0.3942 -0.0535 0.0171  -0.0598 153 THR D C   
11404 O O   . THR D 153 ? 0.5019 0.3698 0.4384 -0.0568 0.0167  -0.0654 153 THR D O   
11405 C CB  . THR D 153 ? 0.4525 0.3510 0.4007 -0.0485 0.0113  -0.0573 153 THR D CB  
11406 O OG1 . THR D 153 ? 0.4727 0.3658 0.4187 -0.0414 0.0141  -0.0537 153 THR D OG1 
11407 C CG2 . THR D 153 ? 0.3765 0.2909 0.3317 -0.0483 0.0079  -0.0546 153 THR D CG2 
11408 N N   . GLY D 154 ? 0.4442 0.3085 0.3849 -0.0490 0.0206  -0.0557 154 GLY D N   
11409 C CA  . GLY D 154 ? 0.4935 0.3409 0.4264 -0.0467 0.0245  -0.0570 154 GLY D CA  
11410 C C   . GLY D 154 ? 0.5247 0.3701 0.4522 -0.0406 0.0249  -0.0587 154 GLY D C   
11411 O O   . GLY D 154 ? 0.5395 0.3709 0.4597 -0.0390 0.0280  -0.0613 154 GLY D O   
11412 N N   . LYS D 155 ? 0.4863 0.3448 0.4169 -0.0371 0.0224  -0.0575 155 LYS D N   
11413 C CA  . LYS D 155 ? 0.5143 0.3722 0.4402 -0.0314 0.0233  -0.0588 155 LYS D CA  
11414 C C   . LYS D 155 ? 0.4627 0.3285 0.3937 -0.0242 0.0238  -0.0531 155 LYS D C   
11415 O O   . LYS D 155 ? 0.4664 0.3439 0.4041 -0.0247 0.0213  -0.0497 155 LYS D O   
11416 C CB  . LYS D 155 ? 0.5436 0.4097 0.4672 -0.0342 0.0200  -0.0631 155 LYS D CB  
11417 C CG  . LYS D 155 ? 0.6547 0.5129 0.5720 -0.0409 0.0193  -0.0699 155 LYS D CG  
11418 C CD  . LYS D 155 ? 0.7030 0.5731 0.6243 -0.0477 0.0142  -0.0723 155 LYS D CD  
11419 C CE  . LYS D 155 ? 0.7206 0.5852 0.6345 -0.0536 0.0126  -0.0798 155 LYS D CE  
11420 N NZ  . LYS D 155 ? 0.8217 0.7002 0.7361 -0.0549 0.0074  -0.0818 155 LYS D NZ  
11421 N N   . GLU D 156 ? 0.4571 0.3164 0.3852 -0.0176 0.0271  -0.0520 156 GLU D N   
11422 C CA  . GLU D 156 ? 0.4503 0.3177 0.3836 -0.0110 0.0275  -0.0471 156 GLU D CA  
11423 C C   . GLU D 156 ? 0.4258 0.3071 0.3620 -0.0108 0.0250  -0.0467 156 GLU D C   
11424 O O   . GLU D 156 ? 0.4419 0.3236 0.3732 -0.0113 0.0250  -0.0504 156 GLU D O   
11425 C CB  . GLU D 156 ? 0.5011 0.3602 0.4307 -0.0040 0.0315  -0.0470 156 GLU D CB  
11426 C CG  . GLU D 156 ? 0.4974 0.3653 0.4339 0.0027  0.0320  -0.0418 156 GLU D CG  
11427 C CD  . GLU D 156 ? 0.6043 0.4674 0.5386 0.0101  0.0360  -0.0419 156 GLU D CD  
11428 O OE1 . GLU D 156 ? 0.6593 0.5126 0.5857 0.0105  0.0387  -0.0464 156 GLU D OE1 
11429 O OE2 . GLU D 156 ? 0.6077 0.4774 0.5481 0.0157  0.0365  -0.0378 156 GLU D OE2 
11430 N N   . ILE D 157 ? 0.4451 0.3370 0.3885 -0.0099 0.0231  -0.0423 157 ILE D N   
11431 C CA  . ILE D 157 ? 0.4357 0.3396 0.3816 -0.0091 0.0213  -0.0413 157 ILE D CA  
11432 C C   . ILE D 157 ? 0.4047 0.3115 0.3534 -0.0027 0.0237  -0.0383 157 ILE D C   
11433 O O   . ILE D 157 ? 0.4302 0.3409 0.3849 -0.0005 0.0233  -0.0341 157 ILE D O   
11434 C CB  . ILE D 157 ? 0.4229 0.3362 0.3745 -0.0124 0.0179  -0.0387 157 ILE D CB  
11435 C CG1 . ILE D 157 ? 0.4331 0.3451 0.3831 -0.0188 0.0157  -0.0419 157 ILE D CG1 
11436 C CG2 . ILE D 157 ? 0.3841 0.3085 0.3379 -0.0108 0.0165  -0.0370 157 ILE D CG2 
11437 C CD1 . ILE D 157 ? 0.4164 0.3362 0.3724 -0.0217 0.0131  -0.0392 157 ILE D CD1 
11438 N N   . THR D 158 ? 0.3915 0.2965 0.3359 0.0005  0.0264  -0.0404 158 THR D N   
11439 C CA  . THR D 158 ? 0.4058 0.3132 0.3533 0.0068  0.0295  -0.0380 158 THR D CA  
11440 C C   . THR D 158 ? 0.3928 0.3129 0.3459 0.0074  0.0285  -0.0349 158 THR D C   
11441 O O   . THR D 158 ? 0.3723 0.2976 0.3245 0.0038  0.0260  -0.0352 158 THR D O   
11442 C CB  . THR D 158 ? 0.4088 0.3097 0.3492 0.0099  0.0334  -0.0417 158 THR D CB  
11443 O OG1 . THR D 158 ? 0.4221 0.3272 0.3579 0.0074  0.0325  -0.0440 158 THR D OG1 
11444 C CG2 . THR D 158 ? 0.4163 0.3027 0.3496 0.0088  0.0347  -0.0455 158 THR D CG2 
11445 N N   . ASP D 159 ? 0.3530 0.2779 0.3117 0.0122  0.0307  -0.0320 159 ASP D N   
11446 C CA  . ASP D 159 ? 0.3942 0.3303 0.3580 0.0125  0.0304  -0.0292 159 ASP D CA  
11447 C C   . ASP D 159 ? 0.4235 0.3610 0.3813 0.0116  0.0319  -0.0316 159 ASP D C   
11448 O O   . ASP D 159 ? 0.3989 0.3431 0.3576 0.0094  0.0303  -0.0301 159 ASP D O   
11449 C CB  . ASP D 159 ? 0.4188 0.3599 0.3899 0.0177  0.0330  -0.0264 159 ASP D CB  
11450 C CG  . ASP D 159 ? 0.4961 0.4392 0.4741 0.0186  0.0305  -0.0231 159 ASP D CG  
11451 O OD1 . ASP D 159 ? 0.5184 0.4584 0.4952 0.0152  0.0273  -0.0228 159 ASP D OD1 
11452 O OD2 . ASP D 159 ? 0.5581 0.5057 0.5423 0.0230  0.0320  -0.0210 159 ASP D OD2 
11453 N N   . ALA D 160 ? 0.3982 0.3284 0.3488 0.0137  0.0350  -0.0351 160 ALA D N   
11454 C CA  . ALA D 160 ? 0.4152 0.3454 0.3581 0.0131  0.0364  -0.0376 160 ALA D CA  
11455 C C   . ALA D 160 ? 0.4087 0.3392 0.3470 0.0078  0.0319  -0.0393 160 ALA D C   
11456 O O   . ALA D 160 ? 0.4109 0.3462 0.3463 0.0068  0.0312  -0.0388 160 ALA D O   
11457 C CB  . ALA D 160 ? 0.4529 0.3738 0.3877 0.0160  0.0404  -0.0417 160 ALA D CB  
11458 N N   . MET D 161 ? 0.4031 0.3286 0.3409 0.0046  0.0290  -0.0409 161 MET D N   
11459 C CA  . MET D 161 ? 0.3899 0.3168 0.3248 -0.0003 0.0246  -0.0426 161 MET D CA  
11460 C C   . MET D 161 ? 0.4028 0.3396 0.3442 -0.0016 0.0219  -0.0384 161 MET D C   
11461 O O   . MET D 161 ? 0.3897 0.3309 0.3284 -0.0035 0.0195  -0.0386 161 MET D O   
11462 C CB  . MET D 161 ? 0.4300 0.3499 0.3647 -0.0036 0.0229  -0.0449 161 MET D CB  
11463 C CG  . MET D 161 ? 0.4069 0.3173 0.3321 -0.0055 0.0234  -0.0508 161 MET D CG  
11464 S SD  . MET D 161 ? 0.4562 0.3548 0.3822 -0.0071 0.0244  -0.0521 161 MET D SD  
11465 C CE  . MET D 161 ? 0.4410 0.3440 0.3686 -0.0147 0.0190  -0.0537 161 MET D CE  
11466 N N   . LEU D 162 ? 0.3347 0.2744 0.2842 -0.0003 0.0222  -0.0347 162 LEU D N   
11467 C CA  . LEU D 162 ? 0.3454 0.2933 0.3005 -0.0015 0.0200  -0.0309 162 LEU D CA  
11468 C C   . LEU D 162 ? 0.3705 0.3237 0.3247 0.0003  0.0218  -0.0292 162 LEU D C   
11469 O O   . LEU D 162 ? 0.3296 0.2875 0.2834 -0.0012 0.0198  -0.0277 162 LEU D O   
11470 C CB  . LEU D 162 ? 0.3640 0.3130 0.3268 -0.0004 0.0199  -0.0277 162 LEU D CB  
11471 C CG  . LEU D 162 ? 0.3578 0.3019 0.3210 -0.0030 0.0178  -0.0286 162 LEU D CG  
11472 C CD1 . LEU D 162 ? 0.3790 0.3219 0.3476 -0.0005 0.0186  -0.0259 162 LEU D CD1 
11473 C CD2 . LEU D 162 ? 0.3662 0.3147 0.3309 -0.0068 0.0143  -0.0278 162 LEU D CD2 
11474 N N   . SER D 163 ? 0.3452 0.2977 0.2989 0.0037  0.0259  -0.0293 163 SER D N   
11475 C CA  . SER D 163 ? 0.3822 0.3395 0.3350 0.0051  0.0284  -0.0275 163 SER D CA  
11476 C C   . SER D 163 ? 0.3775 0.3332 0.3205 0.0040  0.0277  -0.0295 163 SER D C   
11477 O O   . SER D 163 ? 0.3781 0.3379 0.3199 0.0036  0.0276  -0.0273 163 SER D O   
11478 C CB  . SER D 163 ? 0.4272 0.3844 0.3817 0.0091  0.0336  -0.0273 163 SER D CB  
11479 O OG  . SER D 163 ? 0.4715 0.4334 0.4362 0.0101  0.0337  -0.0242 163 SER D OG  
11480 N N   . ASP D 164 ? 0.3812 0.3307 0.3168 0.0038  0.0274  -0.0338 164 ASP D N   
11481 C CA  . ASP D 164 ? 0.4043 0.3526 0.3301 0.0027  0.0257  -0.0362 164 ASP D CA  
11482 C C   . ASP D 164 ? 0.4160 0.3689 0.3431 -0.0004 0.0205  -0.0349 164 ASP D C   
11483 O O   . ASP D 164 ? 0.4039 0.3597 0.3263 -0.0001 0.0195  -0.0337 164 ASP D O   
11484 C CB  . ASP D 164 ? 0.4291 0.3694 0.3470 0.0023  0.0257  -0.0416 164 ASP D CB  
11485 C CG  . ASP D 164 ? 0.5754 0.5102 0.4915 0.0061  0.0314  -0.0429 164 ASP D CG  
11486 O OD1 . ASP D 164 ? 0.6495 0.5880 0.5698 0.0092  0.0355  -0.0398 164 ASP D OD1 
11487 O OD2 . ASP D 164 ? 0.6353 0.5619 0.5459 0.0060  0.0320  -0.0473 164 ASP D OD2 
11488 N N   . ALA D 165 ? 0.3661 0.3196 0.2994 -0.0028 0.0175  -0.0349 165 ALA D N   
11489 C CA  . ALA D 165 ? 0.3928 0.3513 0.3284 -0.0052 0.0132  -0.0335 165 ALA D CA  
11490 C C   . ALA D 165 ? 0.3215 0.2852 0.2609 -0.0040 0.0138  -0.0288 165 ALA D C   
11491 O O   . ALA D 165 ? 0.3521 0.3192 0.2889 -0.0041 0.0116  -0.0274 165 ALA D O   
11492 C CB  . ALA D 165 ? 0.3595 0.3173 0.3014 -0.0080 0.0109  -0.0342 165 ALA D CB  
11493 N N   . LEU D 166 ? 0.3113 0.2756 0.2567 -0.0026 0.0167  -0.0262 166 LEU D N   
11494 C CA  . LEU D 166 ? 0.3273 0.2959 0.2761 -0.0022 0.0174  -0.0221 166 LEU D CA  
11495 C C   . LEU D 166 ? 0.3546 0.3232 0.2962 -0.0006 0.0197  -0.0213 166 LEU D C   
11496 O O   . LEU D 166 ? 0.3352 0.3059 0.2755 -0.0007 0.0191  -0.0186 166 LEU D O   
11497 C CB  . LEU D 166 ? 0.3263 0.2962 0.2831 -0.0014 0.0199  -0.0199 166 LEU D CB  
11498 C CG  . LEU D 166 ? 0.3579 0.3320 0.3193 -0.0016 0.0210  -0.0160 166 LEU D CG  
11499 C CD1 . LEU D 166 ? 0.3334 0.3088 0.2956 -0.0035 0.0174  -0.0144 166 LEU D CD1 
11500 C CD2 . LEU D 166 ? 0.3172 0.2935 0.2871 -0.0011 0.0225  -0.0146 166 LEU D CD2 
11501 N N   . ALA D 167 ? 0.3503 0.3157 0.2862 0.0011  0.0229  -0.0235 167 ALA D N   
11502 C CA  . ALA D 167 ? 0.3721 0.3369 0.3002 0.0028  0.0257  -0.0227 167 ALA D CA  
11503 C C   . ALA D 167 ? 0.3841 0.3487 0.3039 0.0025  0.0219  -0.0233 167 ALA D C   
11504 O O   . ALA D 167 ? 0.3982 0.3636 0.3136 0.0034  0.0225  -0.0206 167 ALA D O   
11505 C CB  . ALA D 167 ? 0.3686 0.3296 0.2918 0.0050  0.0300  -0.0254 167 ALA D CB  
11506 N N   . VAL D 168 ? 0.3597 0.3237 0.2780 0.0010  0.0176  -0.0267 168 VAL D N   
11507 C CA  . VAL D 168 ? 0.3979 0.3635 0.3098 0.0007  0.0131  -0.0274 168 VAL D CA  
11508 C C   . VAL D 168 ? 0.3814 0.3513 0.2982 0.0004  0.0108  -0.0236 168 VAL D C   
11509 O O   . VAL D 168 ? 0.3855 0.3564 0.2966 0.0020  0.0097  -0.0215 168 VAL D O   
11510 C CB  . VAL D 168 ? 0.4761 0.4410 0.3870 -0.0016 0.0091  -0.0323 168 VAL D CB  
11511 C CG1 . VAL D 168 ? 0.5210 0.4904 0.4291 -0.0022 0.0037  -0.0327 168 VAL D CG1 
11512 C CG2 . VAL D 168 ? 0.4437 0.4028 0.3462 -0.0009 0.0114  -0.0366 168 VAL D CG2 
11513 N N   . CYS D 169 ? 0.3335 0.3054 0.2601 -0.0014 0.0100  -0.0225 169 CYS D N   
11514 C CA  . CYS D 169 ? 0.3569 0.3319 0.2879 -0.0015 0.0082  -0.0191 169 CYS D CA  
11515 C C   . CYS D 169 ? 0.3636 0.3376 0.2932 0.0000  0.0117  -0.0149 169 CYS D C   
11516 O O   . CYS D 169 ? 0.3599 0.3344 0.2864 0.0011  0.0106  -0.0124 169 CYS D O   
11517 C CB  . CYS D 169 ? 0.3533 0.3296 0.2940 -0.0036 0.0074  -0.0189 169 CYS D CB  
11518 S SG  . CYS D 169 ? 0.3699 0.3476 0.3124 -0.0061 0.0033  -0.0231 169 CYS D SG  
11519 N N   . ASP D 170 ? 0.3243 0.2967 0.2562 0.0000  0.0162  -0.0142 170 ASP D N   
11520 C CA  . ASP D 170 ? 0.3831 0.3546 0.3139 0.0007  0.0199  -0.0105 170 ASP D CA  
11521 C C   . ASP D 170 ? 0.3956 0.3646 0.3151 0.0029  0.0211  -0.0096 170 ASP D C   
11522 O O   . ASP D 170 ? 0.3933 0.3608 0.3098 0.0035  0.0223  -0.0062 170 ASP D O   
11523 C CB  . ASP D 170 ? 0.3771 0.3490 0.3137 0.0003  0.0245  -0.0102 170 ASP D CB  
11524 C CG  . ASP D 170 ? 0.3860 0.3605 0.3332 -0.0015 0.0236  -0.0093 170 ASP D CG  
11525 O OD1 . ASP D 170 ? 0.3391 0.3143 0.2889 -0.0027 0.0205  -0.0081 170 ASP D OD1 
11526 O OD2 . ASP D 170 ? 0.3940 0.3700 0.3470 -0.0015 0.0260  -0.0098 170 ASP D OD2 
11527 N N   . GLU D 171 ? 0.3518 0.3192 0.2640 0.0041  0.0211  -0.0127 171 GLU D N   
11528 C CA  . GLU D 171 ? 0.3856 0.3503 0.2855 0.0065  0.0217  -0.0119 171 GLU D CA  
11529 C C   . GLU D 171 ? 0.4138 0.3798 0.3103 0.0075  0.0169  -0.0104 171 GLU D C   
11530 O O   . GLU D 171 ? 0.3983 0.3618 0.2875 0.0096  0.0180  -0.0070 171 GLU D O   
11531 C CB  . GLU D 171 ? 0.4123 0.3749 0.3041 0.0075  0.0217  -0.0161 171 GLU D CB  
11532 C CG  . GLU D 171 ? 0.3988 0.3582 0.2767 0.0103  0.0226  -0.0152 171 GLU D CG  
11533 C CD  . GLU D 171 ? 0.5560 0.5127 0.4241 0.0113  0.0221  -0.0198 171 GLU D CD  
11534 O OE1 . GLU D 171 ? 0.6152 0.5720 0.4870 0.0097  0.0209  -0.0241 171 GLU D OE1 
11535 O OE2 . GLU D 171 ? 0.6792 0.6327 0.5347 0.0137  0.0232  -0.0191 171 GLU D OE2 
11536 N N   . ASN D 172 ? 0.3799 0.3498 0.2818 0.0063  0.0117  -0.0125 172 ASN D N   
11537 C CA  . ASN D 172 ? 0.3747 0.3473 0.2749 0.0077  0.0071  -0.0112 172 ASN D CA  
11538 C C   . ASN D 172 ? 0.3867 0.3578 0.2899 0.0082  0.0088  -0.0065 172 ASN D C   
11539 O O   . ASN D 172 ? 0.4013 0.3709 0.2979 0.0109  0.0081  -0.0036 172 ASN D O   
11540 C CB  . ASN D 172 ? 0.3910 0.3688 0.2983 0.0056  0.0021  -0.0146 172 ASN D CB  
11541 C CG  . ASN D 172 ? 0.3899 0.3723 0.2955 0.0074  -0.0031 -0.0141 172 ASN D CG  
11542 O OD1 . ASN D 172 ? 0.4196 0.4048 0.3319 0.0073  -0.0046 -0.0123 172 ASN D OD1 
11543 N ND2 . ASN D 172 ? 0.4041 0.3876 0.3007 0.0093  -0.0060 -0.0157 172 ASN D ND2 
11544 N N   . ARG D 173 ? 0.3234 0.2945 0.2360 0.0057  0.0111  -0.0058 173 ARG D N   
11545 C CA  . ARG D 173 ? 0.3559 0.3250 0.2714 0.0055  0.0130  -0.0019 173 ARG D CA  
11546 C C   . ARG D 173 ? 0.3687 0.3325 0.2763 0.0068  0.0175  0.0014  173 ARG D C   
11547 O O   . ARG D 173 ? 0.3502 0.3105 0.2536 0.0083  0.0179  0.0049  173 ARG D O   
11548 C CB  . ARG D 173 ? 0.3741 0.3443 0.3002 0.0024  0.0144  -0.0022 173 ARG D CB  
11549 C CG  . ARG D 173 ? 0.3496 0.3238 0.2826 0.0012  0.0104  -0.0046 173 ARG D CG  
11550 C CD  . ARG D 173 ? 0.3485 0.3235 0.2904 -0.0014 0.0117  -0.0056 173 ARG D CD  
11551 N NE  . ARG D 173 ? 0.3086 0.2863 0.2558 -0.0026 0.0084  -0.0076 173 ARG D NE  
11552 C CZ  . ARG D 173 ? 0.3369 0.3151 0.2896 -0.0042 0.0086  -0.0095 173 ARG D CZ  
11553 N NH1 . ARG D 173 ? 0.3350 0.3121 0.2893 -0.0044 0.0117  -0.0097 173 ARG D NH1 
11554 N NH2 . ARG D 173 ? 0.3380 0.3180 0.2948 -0.0054 0.0059  -0.0111 173 ARG D NH2 
11555 N N   . ARG D 174 ? 0.3856 0.3481 0.2903 0.0065  0.0213  0.0005  174 ARG D N   
11556 C CA  . ARG D 174 ? 0.3994 0.3569 0.2969 0.0073  0.0265  0.0038  174 ARG D CA  
11557 C C   . ARG D 174 ? 0.4172 0.3714 0.3016 0.0111  0.0251  0.0052  174 ARG D C   
11558 O O   . ARG D 174 ? 0.3921 0.3411 0.2705 0.0123  0.0275  0.0093  174 ARG D O   
11559 C CB  . ARG D 174 ? 0.4357 0.3934 0.3343 0.0062  0.0315  0.0024  174 ARG D CB  
11560 C CG  . ARG D 174 ? 0.4675 0.4285 0.3789 0.0031  0.0334  0.0021  174 ARG D CG  
11561 C CD  . ARG D 174 ? 0.5208 0.4827 0.4336 0.0027  0.0388  0.0013  174 ARG D CD  
11562 N NE  . ARG D 174 ? 0.5677 0.5340 0.4934 0.0001  0.0400  0.0010  174 ARG D NE  
11563 C CZ  . ARG D 174 ? 0.5212 0.4912 0.4538 0.0001  0.0394  -0.0019 174 ARG D CZ  
11564 N NH1 . ARG D 174 ? 0.4765 0.4456 0.4044 0.0021  0.0380  -0.0052 174 ARG D NH1 
11565 N NH2 . ARG D 174 ? 0.5748 0.5489 0.5188 -0.0019 0.0401  -0.0015 174 ARG D NH2 
11566 N N   . LEU D 175 ? 0.4088 0.3656 0.2884 0.0129  0.0208  0.0020  175 LEU D N   
11567 C CA  . LEU D 175 ? 0.3765 0.3311 0.2433 0.0169  0.0184  0.0032  175 LEU D CA  
11568 C C   . LEU D 175 ? 0.3944 0.3493 0.2614 0.0190  0.0149  0.0062  175 LEU D C   
11569 O O   . LEU D 175 ? 0.4199 0.3700 0.2767 0.0225  0.0155  0.0097  175 LEU D O   
11570 C CB  . LEU D 175 ? 0.4252 0.3836 0.2878 0.0177  0.0139  -0.0014 175 LEU D CB  
11571 C CG  . LEU D 175 ? 0.4167 0.3729 0.2754 0.0168  0.0178  -0.0042 175 LEU D CG  
11572 C CD1 . LEU D 175 ? 0.4123 0.3723 0.2697 0.0163  0.0127  -0.0100 175 LEU D CD1 
11573 C CD2 . LEU D 175 ? 0.4116 0.3614 0.2563 0.0196  0.0225  -0.0014 175 LEU D CD2 
11574 N N   . LEU D 176 ? 0.3762 0.3360 0.2542 0.0173  0.0115  0.0049  176 LEU D N   
11575 C CA  . LEU D 176 ? 0.4197 0.3795 0.2983 0.0197  0.0088  0.0076  176 LEU D CA  
11576 C C   . LEU D 176 ? 0.4238 0.3758 0.3003 0.0196  0.0137  0.0123  176 LEU D C   
11577 O O   . LEU D 176 ? 0.4239 0.3717 0.2933 0.0233  0.0132  0.0158  176 LEU D O   
11578 C CB  . LEU D 176 ? 0.3888 0.3550 0.2794 0.0176  0.0051  0.0053  176 LEU D CB  
11579 C CG  . LEU D 176 ? 0.3684 0.3423 0.2606 0.0179  -0.0005 0.0012  176 LEU D CG  
11580 C CD1 . LEU D 176 ? 0.3428 0.3222 0.2475 0.0149  -0.0026 -0.0012 176 LEU D CD1 
11581 C CD2 . LEU D 176 ? 0.3750 0.3513 0.2597 0.0229  -0.0048 0.0026  176 LEU D CD2 
11582 N N   . ARG D 177 ? 0.3859 0.3358 0.2685 0.0155  0.0184  0.0124  177 ARG D N   
11583 C CA  . ARG D 177 ? 0.4052 0.3475 0.2855 0.0146  0.0234  0.0165  177 ARG D CA  
11584 C C   . ARG D 177 ? 0.4161 0.3515 0.2827 0.0175  0.0269  0.0197  177 ARG D C   
11585 O O   . ARG D 177 ? 0.4506 0.3782 0.3106 0.0191  0.0291  0.0239  177 ARG D O   
11586 C CB  . ARG D 177 ? 0.4417 0.3845 0.3313 0.0094  0.0277  0.0158  177 ARG D CB  
11587 C CG  . ARG D 177 ? 0.4514 0.3981 0.3534 0.0064  0.0255  0.0141  177 ARG D CG  
11588 C CD  . ARG D 177 ? 0.3989 0.3404 0.3003 0.0068  0.0251  0.0169  177 ARG D CD  
11589 N NE  . ARG D 177 ? 0.4745 0.4083 0.3736 0.0044  0.0303  0.0201  177 ARG D NE  
11590 C CZ  . ARG D 177 ? 0.4566 0.3907 0.3640 -0.0004 0.0325  0.0197  177 ARG D CZ  
11591 N NH1 . ARG D 177 ? 0.4488 0.3901 0.3667 -0.0028 0.0303  0.0166  177 ARG D NH1 
11592 N NH2 . ARG D 177 ? 0.5145 0.4413 0.4196 -0.0029 0.0369  0.0226  177 ARG D NH2 
11593 N N   . GLU D 178 ? 0.3975 0.3343 0.2588 0.0180  0.0279  0.0180  178 GLU D N   
11594 C CA  . GLU D 178 ? 0.4236 0.3536 0.2708 0.0208  0.0316  0.0210  178 GLU D CA  
11595 C C   . GLU D 178 ? 0.4173 0.3450 0.2536 0.0266  0.0271  0.0231  178 GLU D C   
11596 O O   . GLU D 178 ? 0.4881 0.4072 0.3134 0.0293  0.0301  0.0277  178 GLU D O   
11597 C CB  . GLU D 178 ? 0.4901 0.4227 0.3340 0.0205  0.0331  0.0178  178 GLU D CB  
11598 C CG  . GLU D 178 ? 0.5768 0.5032 0.4045 0.0240  0.0359  0.0201  178 GLU D CG  
11599 C CD  . GLU D 178 ? 0.5700 0.4969 0.3953 0.0226  0.0404  0.0177  178 GLU D CD  
11600 O OE1 . GLU D 178 ? 0.5554 0.4886 0.3910 0.0199  0.0395  0.0133  178 GLU D OE1 
11601 O OE2 . GLU D 178 ? 0.6672 0.5878 0.4795 0.0247  0.0448  0.0201  178 GLU D OE2 
11602 N N   . LEU D 179 ? 0.4610 0.3962 0.3008 0.0284  0.0201  0.0201  179 LEU D N   
11603 C CA  . LEU D 179 ? 0.4117 0.3470 0.2438 0.0341  0.0152  0.0220  179 LEU D CA  
11604 C C   . LEU D 179 ? 0.4274 0.3568 0.2608 0.0354  0.0166  0.0263  179 LEU D C   
11605 O O   . LEU D 179 ? 0.4781 0.4007 0.3002 0.0402  0.0169  0.0305  179 LEU D O   
11606 C CB  . LEU D 179 ? 0.4294 0.3756 0.2682 0.0347  0.0076  0.0175  179 LEU D CB  
11607 C CG  . LEU D 179 ? 0.5170 0.4667 0.3500 0.0407  0.0014  0.0188  179 LEU D CG  
11608 C CD1 . LEU D 179 ? 0.5066 0.4555 0.3247 0.0447  -0.0007 0.0187  179 LEU D CD1 
11609 C CD2 . LEU D 179 ? 0.4575 0.4187 0.3018 0.0399  -0.0051 0.0148  179 LEU D CD2 
11610 N N   . TYR D 180 ? 0.4354 0.3660 0.2811 0.0312  0.0178  0.0254  180 TYR D N   
11611 C CA  . TYR D 180 ? 0.4134 0.3375 0.2596 0.0322  0.0192  0.0290  180 TYR D CA  
11612 C C   . TYR D 180 ? 0.4603 0.3718 0.2969 0.0320  0.0259  0.0337  180 TYR D C   
11613 O O   . TYR D 180 ? 0.4826 0.3859 0.3137 0.0349  0.0270  0.0375  180 TYR D O   
11614 C CB  . TYR D 180 ? 0.4370 0.3641 0.2972 0.0274  0.0194  0.0269  180 TYR D CB  
11615 C CG  . TYR D 180 ? 0.4418 0.3769 0.3097 0.0292  0.0135  0.0246  180 TYR D CG  
11616 C CD1 . TYR D 180 ? 0.4196 0.3643 0.2884 0.0315  0.0080  0.0217  180 TYR D CD1 
11617 C CD2 . TYR D 180 ? 0.3946 0.3278 0.2690 0.0280  0.0138  0.0251  180 TYR D CD2 
11618 C CE1 . TYR D 180 ? 0.4435 0.3964 0.3204 0.0326  0.0031  0.0196  180 TYR D CE1 
11619 C CE2 . TYR D 180 ? 0.4336 0.3744 0.3154 0.0296  0.0091  0.0231  180 TYR D CE2 
11620 C CZ  . TYR D 180 ? 0.4451 0.3961 0.3284 0.0320  0.0040  0.0205  180 TYR D CZ  
11621 O OH  . TYR D 180 ? 0.4239 0.3830 0.3151 0.0332  -0.0001 0.0187  180 TYR D OH  
11622 N N   . GLU D 181 ? 0.4950 0.4045 0.3300 0.0284  0.0309  0.0335  181 GLU D N   
11623 C CA  . GLU D 181 ? 0.5107 0.4085 0.3374 0.0273  0.0380  0.0380  181 GLU D CA  
11624 C C   . GLU D 181 ? 0.5190 0.4081 0.3290 0.0340  0.0380  0.0426  181 GLU D C   
11625 O O   . GLU D 181 ? 0.5280 0.4052 0.3307 0.0343  0.0428  0.0472  181 GLU D O   
11626 C CB  . GLU D 181 ? 0.5334 0.4323 0.3613 0.0229  0.0434  0.0368  181 GLU D CB  
11627 C CG  . GLU D 181 ? 0.6446 0.5341 0.4706 0.0188  0.0516  0.0404  181 GLU D CG  
11628 C CD  . GLU D 181 ? 0.6293 0.5205 0.4698 0.0124  0.0531  0.0391  181 GLU D CD  
11629 O OE1 . GLU D 181 ? 0.6629 0.5624 0.5146 0.0113  0.0480  0.0355  181 GLU D OE1 
11630 O OE2 . GLU D 181 ? 0.7370 0.6210 0.5771 0.0083  0.0593  0.0417  181 GLU D OE2 
11631 N N   . TYR D 182 ? 0.4955 0.3901 0.2992 0.0396  0.0322  0.0415  182 TYR D N   
11632 C CA  . TYR D 182 ? 0.5133 0.4002 0.3002 0.0467  0.0316  0.0460  182 TYR D CA  
11633 C C   . TYR D 182 ? 0.5104 0.3923 0.2960 0.0512  0.0295  0.0493  182 TYR D C   
11634 O O   . TYR D 182 ? 0.5335 0.4046 0.3052 0.0564  0.0314  0.0544  182 TYR D O   
11635 C CB  . TYR D 182 ? 0.5187 0.4141 0.2999 0.0512  0.0252  0.0435  182 TYR D CB  
11636 C CG  . TYR D 182 ? 0.5173 0.4121 0.2911 0.0496  0.0285  0.0422  182 TYR D CG  
11637 C CD1 . TYR D 182 ? 0.5614 0.4644 0.3453 0.0443  0.0286  0.0369  182 TYR D CD1 
11638 C CD2 . TYR D 182 ? 0.5456 0.4305 0.3013 0.0535  0.0320  0.0465  182 TYR D CD2 
11639 C CE1 . TYR D 182 ? 0.5989 0.5011 0.3759 0.0432  0.0321  0.0355  182 TYR D CE1 
11640 C CE2 . TYR D 182 ? 0.5889 0.4732 0.3375 0.0522  0.0354  0.0451  182 TYR D CE2 
11641 C CZ  . TYR D 182 ? 0.5882 0.4811 0.3474 0.0471  0.0354  0.0396  182 TYR D CZ  
11642 O OH  . TYR D 182 ? 0.6745 0.5655 0.4247 0.0466  0.0394  0.0385  182 TYR D OH  
11643 N N   . ARG D 183 ? 0.5133 0.4015 0.3123 0.0493  0.0263  0.0466  183 ARG D N   
11644 C CA  . ARG D 183 ? 0.4944 0.3781 0.2928 0.0538  0.0246  0.0493  183 ARG D CA  
11645 C C   . ARG D 183 ? 0.5211 0.3892 0.3149 0.0516  0.0317  0.0535  183 ARG D C   
11646 O O   . ARG D 183 ? 0.5189 0.3791 0.3079 0.0562  0.0316  0.0568  183 ARG D O   
11647 C CB  . ARG D 183 ? 0.4471 0.3421 0.2609 0.0520  0.0198  0.0450  183 ARG D CB  
11648 C CG  . ARG D 183 ? 0.4903 0.4004 0.3098 0.0524  0.0135  0.0403  183 ARG D CG  
11649 C CD  . ARG D 183 ? 0.4733 0.3940 0.3091 0.0488  0.0102  0.0358  183 ARG D CD  
11650 N NE  . ARG D 183 ? 0.5010 0.4242 0.3394 0.0539  0.0066  0.0369  183 ARG D NE  
11651 C CZ  . ARG D 183 ? 0.5056 0.4358 0.3562 0.0521  0.0044  0.0341  183 ARG D CZ  
11652 N NH1 . ARG D 183 ? 0.4615 0.3974 0.3232 0.0453  0.0048  0.0301  183 ARG D NH1 
11653 N NH2 . ARG D 183 ? 0.4872 0.4189 0.3389 0.0575  0.0019  0.0356  183 ARG D NH2 
11654 N N   . LYS D 184 ? 0.5318 0.3957 0.3277 0.0445  0.0378  0.0533  184 LYS D N   
11655 C CA  . LYS D 184 ? 0.5418 0.3910 0.3335 0.0413  0.0448  0.0569  184 LYS D CA  
11656 C C   . LYS D 184 ? 0.5741 0.4091 0.3474 0.0465  0.0487  0.0630  184 LYS D C   
11657 O O   . LYS D 184 ? 0.6089 0.4296 0.3765 0.0458  0.0535  0.0667  184 LYS D O   
11658 C CB  . LYS D 184 ? 0.5572 0.4071 0.3569 0.0321  0.0504  0.0550  184 LYS D CB  
11659 C CG  . LYS D 184 ? 0.5007 0.3631 0.3178 0.0267  0.0474  0.0496  184 LYS D CG  
11660 C CD  . LYS D 184 ? 0.5549 0.4173 0.3789 0.0183  0.0534  0.0486  184 LYS D CD  
11661 C CE  . LYS D 184 ? 0.5761 0.4497 0.4166 0.0132  0.0505  0.0436  184 LYS D CE  
11662 N NZ  . LYS D 184 ? 0.6567 0.5315 0.5054 0.0054  0.0558  0.0426  184 LYS D NZ  
11663 N N   . ALA D 185 ? 0.5248 0.3624 0.2879 0.0515  0.0467  0.0641  185 ALA D N   
11664 C CA  . ALA D 185 ? 0.5986 0.4219 0.3429 0.0565  0.0509  0.0702  185 ALA D CA  
11665 C C   . ALA D 185 ? 0.6556 0.4701 0.3916 0.0644  0.0485  0.0743  185 ALA D C   
11666 O O   . ALA D 185 ? 0.6359 0.4581 0.3803 0.0674  0.0426  0.0720  185 ALA D O   
11667 C CB  . ALA D 185 ? 0.6564 0.4851 0.3908 0.0606  0.0485  0.0700  185 ALA D CB  
11668 N N   . ALA D 186 ? 0.6395 0.4369 0.3588 0.0679  0.0539  0.0805  186 ALA D N   
11669 C CA  . ALA D 186 ? 0.6526 0.4396 0.3617 0.0765  0.0524  0.0851  186 ALA D CA  
11670 C C   . ALA D 186 ? 0.6773 0.4761 0.3840 0.0862  0.0431  0.0845  186 ALA D C   
11671 O O   . ALA D 186 ? 0.6511 0.4512 0.3597 0.0925  0.0388  0.0852  186 ALA D O   
11672 C CB  . ALA D 186 ? 0.6496 0.4159 0.3392 0.0789  0.0598  0.0922  186 ALA D CB  
11673 N N   . ASP D 187 ? 0.6383 0.4462 0.3408 0.0876  0.0401  0.0831  187 ASP D N   
11674 C CA  . ASP D 187 ? 0.6394 0.4591 0.3386 0.0962  0.0310  0.0823  187 ASP D CA  
11675 C C   . ASP D 187 ? 0.6629 0.5015 0.3758 0.0908  0.0262  0.0751  187 ASP D C   
11676 O O   . ASP D 187 ? 0.6614 0.5034 0.3680 0.0899  0.0260  0.0738  187 ASP D O   
11677 C CB  . ASP D 187 ? 0.7158 0.5268 0.3935 0.1037  0.0314  0.0875  187 ASP D CB  
11678 C CG  . ASP D 187 ? 0.7916 0.5822 0.4540 0.1095  0.0365  0.0952  187 ASP D CG  
11679 O OD1 . ASP D 187 ? 0.7468 0.5336 0.4141 0.1121  0.0360  0.0963  187 ASP D OD1 
11680 O OD2 . ASP D 187 ? 0.8957 0.6734 0.5404 0.1117  0.0414  0.1000  187 ASP D OD2 
11681 N N   . PRO D 188 ? 0.6073 0.4574 0.3381 0.0875  0.0226  0.0703  188 PRO D N   
11682 C CA  . PRO D 188 ? 0.5564 0.4223 0.3011 0.0811  0.0193  0.0635  188 PRO D CA  
11683 C C   . PRO D 188 ? 0.5676 0.4447 0.3071 0.0853  0.0124  0.0612  188 PRO D C   
11684 O O   . PRO D 188 ? 0.5799 0.4632 0.3164 0.0929  0.0056  0.0620  188 PRO D O   
11685 C CB  . PRO D 188 ? 0.6022 0.4771 0.3638 0.0796  0.0156  0.0602  188 PRO D CB  
11686 C CG  . PRO D 188 ? 0.5993 0.4602 0.3577 0.0815  0.0202  0.0647  188 PRO D CG  
11687 C CD  . PRO D 188 ? 0.5726 0.4200 0.3107 0.0892  0.0222  0.0712  188 PRO D CD  
11688 N N   . LYS D 189 ? 0.5730 0.4539 0.3128 0.0800  0.0139  0.0578  189 LYS D N   
11689 C CA  . LYS D 189 ? 0.6123 0.5043 0.3486 0.0821  0.0074  0.0542  189 LYS D CA  
11690 C C   . LYS D 189 ? 0.5801 0.4893 0.3331 0.0797  0.0002  0.0478  189 LYS D C   
11691 O O   . LYS D 189 ? 0.6045 0.5235 0.3562 0.0801  -0.0053 0.0438  189 LYS D O   
11692 C CB  . LYS D 189 ? 0.6264 0.5144 0.3559 0.0775  0.0126  0.0529  189 LYS D CB  
11693 C CG  . LYS D 189 ? 0.6715 0.5447 0.3801 0.0823  0.0176  0.0592  189 LYS D CG  
11694 C CD  . LYS D 189 ? 0.7111 0.5805 0.4116 0.0785  0.0230  0.0581  189 LYS D CD  
11695 C CE  . LYS D 189 ? 0.7809 0.6333 0.4632 0.0808  0.0311  0.0649  189 LYS D CE  
11696 N NZ  . LYS D 189 ? 0.8019 0.6504 0.4863 0.0732  0.0400  0.0637  189 LYS D NZ  
11697 N N   . VAL D 190 ? 0.5779 0.4903 0.3459 0.0765  0.0006  0.0465  190 VAL D N   
11698 C CA  . VAL D 190 ? 0.4867 0.4140 0.2712 0.0737  -0.0051 0.0410  190 VAL D CA  
11699 C C   . VAL D 190 ? 0.5137 0.4406 0.3047 0.0772  -0.0060 0.0435  190 VAL D C   
11700 O O   . VAL D 190 ? 0.5104 0.4269 0.3026 0.0749  0.0000  0.0461  190 VAL D O   
11701 C CB  . VAL D 190 ? 0.5117 0.4415 0.3086 0.0644  -0.0015 0.0366  190 VAL D CB  
11702 C CG1 . VAL D 190 ? 0.5255 0.4692 0.3392 0.0615  -0.0066 0.0314  190 VAL D CG1 
11703 C CG2 . VAL D 190 ? 0.5982 0.5264 0.3884 0.0611  0.0011  0.0345  190 VAL D CG2 
11704 N N   . THR D 191 ? 0.4878 0.4256 0.2824 0.0826  -0.0131 0.0426  191 THR D N   
11705 C CA  . THR D 191 ? 0.4538 0.3928 0.2560 0.0860  -0.0139 0.0443  191 THR D CA  
11706 C C   . THR D 191 ? 0.5205 0.4678 0.3407 0.0790  -0.0138 0.0395  191 THR D C   
11707 O O   . THR D 191 ? 0.5002 0.4544 0.3274 0.0724  -0.0146 0.0347  191 THR D O   
11708 C CB  . THR D 191 ? 0.4926 0.4421 0.2936 0.0947  -0.0216 0.0451  191 THR D CB  
11709 O OG1 . THR D 191 ? 0.5149 0.4817 0.3256 0.0918  -0.0281 0.0392  191 THR D OG1 
11710 C CG2 . THR D 191 ? 0.5115 0.4530 0.2935 0.1026  -0.0224 0.0502  191 THR D CG2 
11711 N N   . GLY D 192 ? 0.4634 0.4093 0.2904 0.0807  -0.0128 0.0409  192 GLY D N   
11712 C CA  . GLY D 192 ? 0.4418 0.3957 0.2849 0.0749  -0.0130 0.0367  192 GLY D CA  
11713 C C   . GLY D 192 ? 0.4679 0.4399 0.3211 0.0741  -0.0199 0.0318  192 GLY D C   
11714 O O   . GLY D 192 ? 0.4466 0.4249 0.3106 0.0672  -0.0199 0.0273  192 GLY D O   
11715 N N   . VAL D 193 ? 0.4337 0.4143 0.2841 0.0811  -0.0257 0.0326  193 VAL D N   
11716 C CA  . VAL D 193 ? 0.4597 0.4580 0.3199 0.0796  -0.0324 0.0277  193 VAL D CA  
11717 C C   . VAL D 193 ? 0.4673 0.4675 0.3255 0.0732  -0.0333 0.0236  193 VAL D C   
11718 O O   . VAL D 193 ? 0.4537 0.4633 0.3230 0.0671  -0.0352 0.0185  193 VAL D O   
11719 C CB  . VAL D 193 ? 0.5056 0.5136 0.3628 0.0886  -0.0390 0.0295  193 VAL D CB  
11720 C CG1 . VAL D 193 ? 0.4851 0.5109 0.3496 0.0861  -0.0465 0.0240  193 VAL D CG1 
11721 C CG2 . VAL D 193 ? 0.4527 0.4636 0.3179 0.0935  -0.0386 0.0316  193 VAL D CG2 
11722 N N   . GLU D 194 ? 0.4449 0.4356 0.2886 0.0746  -0.0314 0.0257  194 GLU D N   
11723 C CA  . GLU D 194 ? 0.4535 0.4451 0.2942 0.0691  -0.0317 0.0217  194 GLU D CA  
11724 C C   . GLU D 194 ? 0.4689 0.4563 0.3180 0.0606  -0.0263 0.0191  194 GLU D C   
11725 O O   . GLU D 194 ? 0.4255 0.4196 0.2817 0.0549  -0.0279 0.0140  194 GLU D O   
11726 C CB  . GLU D 194 ? 0.4490 0.4300 0.2713 0.0729  -0.0299 0.0252  194 GLU D CB  
11727 C CG  . GLU D 194 ? 0.4810 0.4677 0.2946 0.0814  -0.0366 0.0272  194 GLU D CG  
11728 C CD  . GLU D 194 ? 0.5533 0.5283 0.3469 0.0863  -0.0346 0.0315  194 GLU D CD  
11729 O OE1 . GLU D 194 ? 0.5616 0.5218 0.3481 0.0851  -0.0270 0.0352  194 GLU D OE1 
11730 O OE2 . GLU D 194 ? 0.5937 0.5746 0.3787 0.0915  -0.0409 0.0314  194 GLU D OE2 
11731 N N   . ALA D 195 ? 0.4385 0.4145 0.2868 0.0598  -0.0199 0.0226  195 ALA D N   
11732 C CA  . ALA D 195 ? 0.4529 0.4259 0.3102 0.0523  -0.0152 0.0204  195 ALA D CA  
11733 C C   . ALA D 195 ? 0.4362 0.4204 0.3089 0.0487  -0.0183 0.0162  195 ALA D C   
11734 O O   . ALA D 195 ? 0.4080 0.3949 0.2877 0.0425  -0.0174 0.0123  195 ALA D O   
11735 C CB  . ALA D 195 ? 0.4435 0.4040 0.2986 0.0524  -0.0090 0.0248  195 ALA D CB  
11736 N N   . LEU D 196 ? 0.4288 0.4202 0.3066 0.0528  -0.0219 0.0169  196 LEU D N   
11737 C CA  . LEU D 196 ? 0.4206 0.4219 0.3128 0.0493  -0.0239 0.0134  196 LEU D CA  
11738 C C   . LEU D 196 ? 0.4089 0.4224 0.3060 0.0463  -0.0292 0.0082  196 LEU D C   
11739 O O   . LEU D 196 ? 0.4147 0.4327 0.3217 0.0404  -0.0290 0.0044  196 LEU D O   
11740 C CB  . LEU D 196 ? 0.4335 0.4383 0.3294 0.0550  -0.0252 0.0160  196 LEU D CB  
11741 C CG  . LEU D 196 ? 0.4420 0.4569 0.3525 0.0525  -0.0266 0.0132  196 LEU D CG  
11742 C CD1 . LEU D 196 ? 0.4500 0.4583 0.3659 0.0460  -0.0217 0.0121  196 LEU D CD1 
11743 C CD2 . LEU D 196 ? 0.4738 0.4903 0.3853 0.0597  -0.0271 0.0166  196 LEU D CD2 
11744 N N   . TYR D 197 ? 0.4086 0.4271 0.2985 0.0503  -0.0339 0.0080  197 TYR D N   
11745 C CA  . TYR D 197 ? 0.4305 0.4586 0.3230 0.0466  -0.0387 0.0027  197 TYR D CA  
11746 C C   . TYR D 197 ? 0.3963 0.4177 0.2874 0.0400  -0.0351 -0.0003 197 TYR D C   
11747 O O   . TYR D 197 ? 0.4198 0.4468 0.3188 0.0343  -0.0364 -0.0052 197 TYR D O   
11748 C CB  . TYR D 197 ? 0.4235 0.4554 0.3053 0.0521  -0.0440 0.0032  197 TYR D CB  
11749 C CG  . TYR D 197 ? 0.4636 0.5086 0.3504 0.0575  -0.0504 0.0037  197 TYR D CG  
11750 C CD1 . TYR D 197 ? 0.4775 0.5371 0.3780 0.0540  -0.0547 -0.0007 197 TYR D CD1 
11751 C CD2 . TYR D 197 ? 0.4804 0.5235 0.3579 0.0663  -0.0520 0.0087  197 TYR D CD2 
11752 C CE1 . TYR D 197 ? 0.5144 0.5878 0.4206 0.0589  -0.0605 -0.0004 197 TYR D CE1 
11753 C CE2 . TYR D 197 ? 0.5425 0.5990 0.4249 0.0720  -0.0582 0.0092  197 TYR D CE2 
11754 C CZ  . TYR D 197 ? 0.5105 0.5828 0.4078 0.0681  -0.0624 0.0045  197 TYR D CZ  
11755 O OH  . TYR D 197 ? 0.5451 0.6323 0.4489 0.0736  -0.0684 0.0048  197 TYR D OH  
11756 N N   . ALA D 198 ? 0.4196 0.4287 0.3009 0.0406  -0.0300 0.0026  198 ALA D N   
11757 C CA  . ALA D 198 ? 0.4189 0.4220 0.2992 0.0351  -0.0259 0.0001  198 ALA D CA  
11758 C C   . ALA D 198 ? 0.4039 0.4066 0.2966 0.0297  -0.0227 -0.0014 198 ALA D C   
11759 O O   . ALA D 198 ? 0.3990 0.4038 0.2967 0.0247  -0.0227 -0.0056 198 ALA D O   
11760 C CB  . ALA D 198 ? 0.4561 0.4471 0.3243 0.0370  -0.0207 0.0039  198 ALA D CB  
11761 N N   . SER D 199 ? 0.3887 0.3873 0.2853 0.0306  -0.0195 0.0022  199 SER D N   
11762 C CA  . SER D 199 ? 0.4208 0.4179 0.3275 0.0258  -0.0162 0.0012  199 SER D CA  
11763 C C   . SER D 199 ? 0.3576 0.3645 0.2758 0.0233  -0.0196 -0.0022 199 SER D C   
11764 O O   . SER D 199 ? 0.4107 0.4177 0.3362 0.0183  -0.0181 -0.0047 199 SER D O   
11765 C CB  . SER D 199 ? 0.4016 0.3911 0.3082 0.0274  -0.0122 0.0056  199 SER D CB  
11766 O OG  . SER D 199 ? 0.4162 0.4088 0.3234 0.0323  -0.0146 0.0078  199 SER D OG  
11767 N N   . LEU D 200 ? 0.3891 0.4045 0.3090 0.0266  -0.0242 -0.0022 200 LEU D N   
11768 C CA  . LEU D 200 ? 0.3842 0.4097 0.3158 0.0238  -0.0270 -0.0054 200 LEU D CA  
11769 C C   . LEU D 200 ? 0.3788 0.4092 0.3123 0.0190  -0.0296 -0.0106 200 LEU D C   
11770 O O   . LEU D 200 ? 0.4027 0.4350 0.3444 0.0139  -0.0289 -0.0135 200 LEU D O   
11771 C CB  . LEU D 200 ? 0.4196 0.4540 0.3537 0.0290  -0.0309 -0.0039 200 LEU D CB  
11772 C CG  . LEU D 200 ? 0.4679 0.5108 0.4144 0.0282  -0.0315 -0.0046 200 LEU D CG  
11773 C CD1 . LEU D 200 ? 0.4245 0.4609 0.3764 0.0245  -0.0265 -0.0041 200 LEU D CD1 
11774 C CD2 . LEU D 200 ? 0.5045 0.5520 0.4498 0.0357  -0.0335 -0.0012 200 LEU D CD2 
11775 N N   . THR D 201 ? 0.3451 0.3765 0.2700 0.0206  -0.0326 -0.0119 201 THR D N   
11776 C CA  . THR D 201 ? 0.3572 0.3924 0.2824 0.0161  -0.0354 -0.0173 201 THR D CA  
11777 C C   . THR D 201 ? 0.3563 0.3824 0.2803 0.0116  -0.0309 -0.0190 201 THR D C   
11778 O O   . THR D 201 ? 0.3610 0.3888 0.2879 0.0068  -0.0320 -0.0237 201 THR D O   
11779 C CB  . THR D 201 ? 0.3876 0.4251 0.3020 0.0193  -0.0399 -0.0183 201 THR D CB  
11780 O OG1 . THR D 201 ? 0.3736 0.4008 0.2756 0.0229  -0.0365 -0.0149 201 THR D OG1 
11781 C CG2 . THR D 201 ? 0.3872 0.4364 0.3044 0.0241  -0.0455 -0.0169 201 THR D CG2 
11782 N N   . ALA D 202 ? 0.3545 0.3711 0.2744 0.0129  -0.0257 -0.0155 202 ALA D N   
11783 C CA  . ALA D 202 ? 0.3875 0.3970 0.3084 0.0091  -0.0212 -0.0167 202 ALA D CA  
11784 C C   . ALA D 202 ? 0.3654 0.3774 0.2976 0.0045  -0.0207 -0.0190 202 ALA D C   
11785 O O   . ALA D 202 ? 0.3919 0.3997 0.3252 0.0010  -0.0185 -0.0214 202 ALA D O   
11786 C CB  . ALA D 202 ? 0.3667 0.3679 0.2841 0.0112  -0.0160 -0.0122 202 ALA D CB  
11787 N N   . GLN D 203 ? 0.3262 0.3446 0.2664 0.0047  -0.0226 -0.0182 203 GLN D N   
11788 C CA  . GLN D 203 ? 0.3299 0.3502 0.2803 0.0007  -0.0216 -0.0195 203 GLN D CA  
11789 C C   . GLN D 203 ? 0.3607 0.3883 0.3164 -0.0032 -0.0251 -0.0240 203 GLN D C   
11790 O O   . GLN D 203 ? 0.3586 0.3873 0.3223 -0.0069 -0.0240 -0.0252 203 GLN D O   
11791 C CB  . GLN D 203 ? 0.3206 0.3426 0.2759 0.0031  -0.0206 -0.0159 203 GLN D CB  
11792 C CG  . GLN D 203 ? 0.3216 0.3353 0.2709 0.0064  -0.0172 -0.0116 203 GLN D CG  
11793 C CD  . GLN D 203 ? 0.3692 0.3826 0.3220 0.0086  -0.0159 -0.0084 203 GLN D CD  
11794 O OE1 . GLN D 203 ? 0.3735 0.3892 0.3339 0.0063  -0.0153 -0.0091 203 GLN D OE1 
11795 N NE2 . GLN D 203 ? 0.3877 0.3973 0.3343 0.0131  -0.0151 -0.0048 203 GLN D NE2 
11796 N N   . PHE D 204 ? 0.3211 0.3533 0.2721 -0.0029 -0.0292 -0.0268 204 PHE D N   
11797 C CA  . PHE D 204 ? 0.3422 0.3805 0.2982 -0.0078 -0.0324 -0.0318 204 PHE D CA  
11798 C C   . PHE D 204 ? 0.3332 0.3712 0.2807 -0.0087 -0.0356 -0.0358 204 PHE D C   
11799 O O   . PHE D 204 ? 0.3858 0.4300 0.3364 -0.0126 -0.0394 -0.0403 204 PHE D O   
11800 C CB  . PHE D 204 ? 0.3255 0.3765 0.2904 -0.0075 -0.0361 -0.0318 204 PHE D CB  
11801 C CG  . PHE D 204 ? 0.3553 0.4120 0.3164 -0.0009 -0.0391 -0.0286 204 PHE D CG  
11802 C CD1 . PHE D 204 ? 0.3768 0.4375 0.3306 0.0011  -0.0438 -0.0304 204 PHE D CD1 
11803 C CD2 . PHE D 204 ? 0.3821 0.4401 0.3468 0.0033  -0.0373 -0.0242 204 PHE D CD2 
11804 C CE1 . PHE D 204 ? 0.4037 0.4694 0.3534 0.0076  -0.0468 -0.0274 204 PHE D CE1 
11805 C CE2 . PHE D 204 ? 0.3993 0.4617 0.3601 0.0099  -0.0400 -0.0211 204 PHE D CE2 
11806 C CZ  . PHE D 204 ? 0.3779 0.4441 0.3313 0.0122  -0.0447 -0.0225 204 PHE D CZ  
11807 N N   . ILE D 205 ? 0.3365 0.3671 0.2731 -0.0055 -0.0340 -0.0345 205 ILE D N   
11808 C CA  . ILE D 205 ? 0.3564 0.3838 0.2832 -0.0063 -0.0357 -0.0384 205 ILE D CA  
11809 C C   . ILE D 205 ? 0.3451 0.3611 0.2683 -0.0083 -0.0303 -0.0394 205 ILE D C   
11810 O O   . ILE D 205 ? 0.3968 0.4072 0.3219 -0.0069 -0.0255 -0.0358 205 ILE D O   
11811 C CB  . ILE D 205 ? 0.3478 0.3761 0.2639 -0.0004 -0.0379 -0.0358 205 ILE D CB  
11812 C CG1 . ILE D 205 ? 0.3912 0.4315 0.3117 0.0023  -0.0434 -0.0346 205 ILE D CG1 
11813 C CG2 . ILE D 205 ? 0.3911 0.4151 0.2946 -0.0002 -0.0392 -0.0392 205 ILE D CG2 
11814 C CD1 . ILE D 205 ? 0.4124 0.4634 0.3383 -0.0018 -0.0494 -0.0400 205 ILE D CD1 
11815 N N   . ASP D 206 ? 0.4260 0.4384 0.3439 -0.0113 -0.0311 -0.0445 206 ASP D N   
11816 C CA  . ASP D 206 ? 0.4345 0.4361 0.3484 -0.0123 -0.0259 -0.0456 206 ASP D CA  
11817 C C   . ASP D 206 ? 0.4627 0.4589 0.3692 -0.0073 -0.0219 -0.0413 206 ASP D C   
11818 O O   . ASP D 206 ? 0.4167 0.4137 0.3139 -0.0039 -0.0236 -0.0404 206 ASP D O   
11819 C CB  . ASP D 206 ? 0.4504 0.4484 0.3571 -0.0154 -0.0277 -0.0519 206 ASP D CB  
11820 C CG  . ASP D 206 ? 0.5198 0.5064 0.4232 -0.0163 -0.0221 -0.0535 206 ASP D CG  
11821 O OD1 . ASP D 206 ? 0.5377 0.5190 0.4360 -0.0125 -0.0176 -0.0505 206 ASP D OD1 
11822 O OD2 . ASP D 206 ? 0.5782 0.5612 0.4842 -0.0208 -0.0219 -0.0577 206 ASP D OD2 
11823 N N   . LYS D 207 ? 0.5046 0.3752 0.3605 -0.0609 0.0292  -0.0516 207 LYS D N   
11824 C CA  . LYS D 207 ? 0.4767 0.3568 0.3352 -0.0508 0.0232  -0.0445 207 LYS D CA  
11825 C C   . LYS D 207 ? 0.4899 0.3803 0.3502 -0.0482 0.0217  -0.0492 207 LYS D C   
11826 O O   . LYS D 207 ? 0.4806 0.3873 0.3446 -0.0429 0.0182  -0.0454 207 LYS D O   
11827 C CB  . LYS D 207 ? 0.5274 0.3867 0.3804 -0.0437 0.0218  -0.0369 207 LYS D CB  
11828 C CG  . LYS D 207 ? 0.5959 0.4490 0.4466 -0.0446 0.0225  -0.0312 207 LYS D CG  
11829 C CD  . LYS D 207 ? 0.5510 0.4009 0.4017 -0.0358 0.0176  -0.0230 207 LYS D CD  
11830 C CE  . LYS D 207 ? 0.5973 0.4456 0.4466 -0.0366 0.0180  -0.0178 207 LYS D CE  
11831 N NZ  . LYS D 207 ? 0.6127 0.4469 0.4545 -0.0442 0.0245  -0.0210 207 LYS D NZ  
11832 N N   . ARG D 208 ? 0.4457 0.3258 0.3022 -0.0519 0.0250  -0.0576 208 ARG D N   
11833 C CA  . ARG D 208 ? 0.4992 0.3922 0.3571 -0.0500 0.0240  -0.0633 208 ARG D CA  
11834 C C   . ARG D 208 ? 0.4746 0.3959 0.3372 -0.0528 0.0217  -0.0663 208 ARG D C   
11835 O O   . ARG D 208 ? 0.5028 0.4396 0.3659 -0.0474 0.0190  -0.0641 208 ARG D O   
11836 C CB  . ARG D 208 ? 0.5437 0.4207 0.3965 -0.0540 0.0283  -0.0734 208 ARG D CB  
11837 C CG  . ARG D 208 ? 0.6597 0.5054 0.5051 -0.0508 0.0306  -0.0704 208 ARG D CG  
11838 C CD  . ARG D 208 ? 0.7073 0.5339 0.5460 -0.0543 0.0354  -0.0803 208 ARG D CD  
11839 N NE  . ARG D 208 ? 0.8637 0.6714 0.6966 -0.0643 0.0415  -0.0834 208 ARG D NE  
11840 C CZ  . ARG D 208 ? 0.8623 0.6813 0.6994 -0.0766 0.0450  -0.0920 208 ARG D CZ  
11841 N NH1 . ARG D 208 ? 0.8255 0.6746 0.6712 -0.0790 0.0418  -0.0983 208 ARG D NH1 
11842 N NH2 . ARG D 208 ? 0.7927 0.5923 0.6249 -0.0865 0.0522  -0.0949 208 ARG D NH2 
11843 N N   . GLU D 209 ? 0.4638 0.3923 0.3292 -0.0610 0.0229  -0.0717 209 GLU D N   
11844 C CA  . GLU D 209 ? 0.4703 0.4279 0.3402 -0.0621 0.0193  -0.0756 209 GLU D CA  
11845 C C   . GLU D 209 ? 0.4488 0.4188 0.3202 -0.0540 0.0149  -0.0644 209 GLU D C   
11846 O O   . GLU D 209 ? 0.4578 0.4461 0.3277 -0.0487 0.0112  -0.0631 209 GLU D O   
11847 C CB  . GLU D 209 ? 0.4976 0.4620 0.3732 -0.0728 0.0218  -0.0850 209 GLU D CB  
11848 C CG  . GLU D 209 ? 0.5661 0.5177 0.4395 -0.0815 0.0268  -0.0971 209 GLU D CG  
11849 C CD  . GLU D 209 ? 0.6076 0.5601 0.4870 -0.0950 0.0319  -0.1075 209 GLU D CD  
11850 O OE1 . GLU D 209 ? 0.7428 0.6717 0.6177 -0.1026 0.0387  -0.1137 209 GLU D OE1 
11851 O OE2 . GLU D 209 ? 0.6156 0.5901 0.5039 -0.0980 0.0301  -0.1096 209 GLU D OE2 
11852 N N   . HIS D 210 ? 0.4364 0.3946 0.3091 -0.0526 0.0155  -0.0562 210 HIS D N   
11853 C CA  . HIS D 210 ? 0.4234 0.3901 0.2973 -0.0453 0.0119  -0.0459 210 HIS D CA  
11854 C C   . HIS D 210 ? 0.4340 0.3991 0.3043 -0.0375 0.0105  -0.0391 210 HIS D C   
11855 O O   . HIS D 210 ? 0.4354 0.4141 0.3043 -0.0321 0.0079  -0.0340 210 HIS D O   
11856 C CB  . HIS D 210 ? 0.3917 0.3433 0.2666 -0.0459 0.0135  -0.0400 210 HIS D CB  
11857 C CG  . HIS D 210 ? 0.4346 0.3966 0.3122 -0.0409 0.0105  -0.0326 210 HIS D CG  
11858 N ND1 . HIS D 210 ? 0.4176 0.3733 0.2935 -0.0336 0.0086  -0.0228 210 HIS D ND1 
11859 C CD2 . HIS D 210 ? 0.4025 0.3801 0.2851 -0.0419 0.0094  -0.0342 210 HIS D CD2 
11860 C CE1 . HIS D 210 ? 0.4238 0.3881 0.3017 -0.0301 0.0066  -0.0181 210 HIS D CE1 
11861 N NE2 . HIS D 210 ? 0.3994 0.3778 0.2815 -0.0343 0.0068  -0.0247 210 HIS D NE2 
11862 N N   . ASN D 211 ? 0.4200 0.3687 0.2886 -0.0367 0.0127  -0.0392 211 ASN D N   
11863 C CA  . ASN D 211 ? 0.4627 0.4118 0.3305 -0.0305 0.0126  -0.0345 211 ASN D CA  
11864 C C   . ASN D 211 ? 0.4658 0.4323 0.3299 -0.0292 0.0125  -0.0377 211 ASN D C   
11865 O O   . ASN D 211 ? 0.4347 0.4077 0.2965 -0.0243 0.0127  -0.0314 211 ASN D O   
11866 C CB  . ASN D 211 ? 0.4829 0.4150 0.3510 -0.0293 0.0145  -0.0369 211 ASN D CB  
11867 C CG  . ASN D 211 ? 0.4478 0.3626 0.3171 -0.0275 0.0135  -0.0317 211 ASN D CG  
11868 O OD1 . ASN D 211 ? 0.4540 0.3704 0.3247 -0.0268 0.0119  -0.0253 211 ASN D OD1 
11869 N ND2 . ASN D 211 ? 0.4807 0.3788 0.3484 -0.0257 0.0142  -0.0345 211 ASN D ND2 
11870 N N   . GLU D 212 ? 0.4659 0.4383 0.3281 -0.0338 0.0129  -0.0480 212 GLU D N   
11871 C CA  . GLU D 212 ? 0.4775 0.4673 0.3343 -0.0323 0.0121  -0.0524 212 GLU D CA  
11872 C C   . GLU D 212 ? 0.4862 0.4930 0.3400 -0.0282 0.0082  -0.0468 212 GLU D C   
11873 O O   . GLU D 212 ? 0.4518 0.4679 0.2979 -0.0226 0.0079  -0.0428 212 GLU D O   
11874 C CB  . GLU D 212 ? 0.4988 0.4913 0.3553 -0.0390 0.0128  -0.0660 212 GLU D CB  
11875 C CG  . GLU D 212 ? 0.5865 0.5976 0.4363 -0.0373 0.0112  -0.0720 212 GLU D CG  
11876 C CD  . GLU D 212 ? 0.6905 0.6948 0.5361 -0.0362 0.0151  -0.0768 212 GLU D CD  
11877 O OE1 . GLU D 212 ? 0.6826 0.6762 0.5291 -0.0318 0.0181  -0.0697 212 GLU D OE1 
11878 O OE2 . GLU D 212 ? 0.7209 0.7316 0.5633 -0.0398 0.0153  -0.0888 212 GLU D OE2 
11879 N N   . MET D 213 ? 0.4409 0.4514 0.2998 -0.0303 0.0057  -0.0464 213 MET D N   
11880 C CA  . MET D 213 ? 0.4836 0.5102 0.3401 -0.0246 0.0013  -0.0414 213 MET D CA  
11881 C C   . MET D 213 ? 0.4660 0.4844 0.3187 -0.0174 0.0021  -0.0277 213 MET D C   
11882 O O   . MET D 213 ? 0.4621 0.4899 0.3066 -0.0104 0.0001  -0.0221 213 MET D O   
11883 C CB  . MET D 213 ? 0.5090 0.5431 0.3737 -0.0285 -0.0010 -0.0455 213 MET D CB  
11884 C CG  . MET D 213 ? 0.4727 0.5299 0.3365 -0.0221 -0.0069 -0.0449 213 MET D CG  
11885 S SD  . MET D 213 ? 0.5978 0.6771 0.4508 -0.0164 -0.0118 -0.0504 213 MET D SD  
11886 C CE  . MET D 213 ? 0.5612 0.6431 0.4033 -0.0021 -0.0152 -0.0354 213 MET D CE  
11887 N N   . LEU D 214 ? 0.4155 0.4160 0.2732 -0.0189 0.0049  -0.0226 214 LEU D N   
11888 C CA  . LEU D 214 ? 0.4204 0.4127 0.2761 -0.0137 0.0063  -0.0114 214 LEU D CA  
11889 C C   . LEU D 214 ? 0.4185 0.4118 0.2673 -0.0111 0.0098  -0.0092 214 LEU D C   
11890 O O   . LEU D 214 ? 0.4032 0.3965 0.2453 -0.0062 0.0112  -0.0007 214 LEU D O   
11891 C CB  . LEU D 214 ? 0.3809 0.3556 0.2439 -0.0160 0.0079  -0.0087 214 LEU D CB  
11892 C CG  . LEU D 214 ? 0.4264 0.3965 0.2941 -0.0175 0.0059  -0.0077 214 LEU D CG  
11893 C CD1 . LEU D 214 ? 0.4072 0.3595 0.2788 -0.0194 0.0072  -0.0068 214 LEU D CD1 
11894 C CD2 . LEU D 214 ? 0.4203 0.3944 0.2857 -0.0118 0.0041  0.0006  214 LEU D CD2 
11895 N N   . LYS D 215 ? 0.4188 0.4115 0.2684 -0.0143 0.0121  -0.0167 215 LYS D N   
11896 C CA  . LYS D 215 ? 0.4509 0.4463 0.2939 -0.0121 0.0165  -0.0158 215 LYS D CA  
11897 C C   . LYS D 215 ? 0.4176 0.4268 0.2471 -0.0075 0.0152  -0.0141 215 LYS D C   
11898 O O   . LYS D 215 ? 0.4525 0.4608 0.2731 -0.0036 0.0191  -0.0067 215 LYS D O   
11899 C CB  . LYS D 215 ? 0.4506 0.4436 0.2971 -0.0156 0.0189  -0.0258 215 LYS D CB  
11900 C CG  . LYS D 215 ? 0.4943 0.4732 0.3511 -0.0163 0.0215  -0.0242 215 LYS D CG  
11901 C CD  . LYS D 215 ? 0.4910 0.4651 0.3515 -0.0175 0.0237  -0.0335 215 LYS D CD  
11902 C CE  . LYS D 215 ? 0.6000 0.5650 0.4626 -0.0209 0.0210  -0.0408 215 LYS D CE  
11903 N NZ  . LYS D 215 ? 0.6116 0.5665 0.4778 -0.0198 0.0232  -0.0477 215 LYS D NZ  
11904 N N   . LYS D 216 ? 0.4434 0.4655 0.2707 -0.0078 0.0099  -0.0212 216 LYS D N   
11905 C CA  . LYS D 216 ? 0.4787 0.5159 0.2922 -0.0017 0.0067  -0.0205 216 LYS D CA  
11906 C C   . LYS D 216 ? 0.4762 0.5109 0.2830 0.0057  0.0054  -0.0078 216 LYS D C   
11907 O O   . LYS D 216 ? 0.4903 0.5279 0.2812 0.0128  0.0063  -0.0016 216 LYS D O   
11908 C CB  . LYS D 216 ? 0.4983 0.5522 0.3145 -0.0040 0.0003  -0.0323 216 LYS D CB  
11909 C CG  . LYS D 216 ? 0.5616 0.6325 0.3690 0.0042  -0.0065 -0.0301 216 LYS D CG  
11910 C CD  . LYS D 216 ? 0.5568 0.6490 0.3684 0.0014  -0.0131 -0.0445 216 LYS D CD  
11911 C CE  . LYS D 216 ? 0.6260 0.7381 0.4251 0.0124  -0.0206 -0.0433 216 LYS D CE  
11912 N NZ  . LYS D 216 ? 0.5823 0.7186 0.3858 0.0096  -0.0273 -0.0595 216 LYS D NZ  
11913 N N   . THR D 217 ? 0.4629 0.4906 0.2799 0.0047  0.0038  -0.0040 217 THR D N   
11914 C CA  . THR D 217 ? 0.4376 0.4611 0.2494 0.0119  0.0025  0.0071  217 THR D CA  
11915 C C   . THR D 217 ? 0.4482 0.4558 0.2529 0.0136  0.0097  0.0179  217 THR D C   
11916 O O   . THR D 217 ? 0.5025 0.5081 0.2917 0.0210  0.0110  0.0265  217 THR D O   
11917 C CB  . THR D 217 ? 0.4774 0.4965 0.3031 0.0090  0.0000  0.0067  217 THR D CB  
11918 O OG1 . THR D 217 ? 0.4663 0.5010 0.2990 0.0058  -0.0050 -0.0043 217 THR D OG1 
11919 C CG2 . THR D 217 ? 0.4943 0.5078 0.3158 0.0166  -0.0013 0.0172  217 THR D CG2 
11920 N N   . LEU D 218 ? 0.4980 0.4946 0.3131 0.0068  0.0149  0.0167  218 LEU D N   
11921 C CA  . LEU D 218 ? 0.5161 0.4997 0.3286 0.0063  0.0227  0.0247  218 LEU D CA  
11922 C C   . LEU D 218 ? 0.4998 0.4869 0.2973 0.0085  0.0282  0.0264  218 LEU D C   
11923 O O   . LEU D 218 ? 0.5741 0.5512 0.3637 0.0096  0.0354  0.0351  218 LEU D O   
11924 C CB  . LEU D 218 ? 0.4857 0.4616 0.3145 -0.0007 0.0256  0.0205  218 LEU D CB  
11925 C CG  . LEU D 218 ? 0.4846 0.4528 0.3254 -0.0025 0.0217  0.0208  218 LEU D CG  
11926 C CD1 . LEU D 218 ? 0.4823 0.4452 0.3366 -0.0076 0.0226  0.0146  218 LEU D CD1 
11927 C CD2 . LEU D 218 ? 0.3984 0.3563 0.2363 0.0008  0.0227  0.0311  218 LEU D CD2 
11928 N N   . ALA D 219 ? 0.4962 0.4965 0.2888 0.0086  0.0260  0.0177  219 ALA D N   
11929 C CA  . ALA D 219 ? 0.5202 0.5242 0.2959 0.0114  0.0313  0.0190  219 ALA D CA  
11930 C C   . ALA D 219 ? 0.5313 0.5373 0.2851 0.0212  0.0289  0.0275  219 ALA D C   
11931 O O   . ALA D 219 ? 0.5471 0.5482 0.2828 0.0246  0.0357  0.0341  219 ALA D O   
11932 C CB  . ALA D 219 ? 0.5378 0.5547 0.3147 0.0087  0.0292  0.0059  219 ALA D CB  
11933 N N   . ALA D 220 ? 0.5267 0.5393 0.2814 0.0262  0.0197  0.0276  220 ALA D N   
11934 C CA  . ALA D 220 ? 0.5717 0.5872 0.3069 0.0378  0.0153  0.0350  220 ALA D CA  
11935 C C   . ALA D 220 ? 0.5677 0.5641 0.2975 0.0423  0.0190  0.0491  220 ALA D C   
11936 O O   . ALA D 220 ? 0.6346 0.6255 0.3424 0.0526  0.0192  0.0586  220 ALA D O   
11937 C CB  . ALA D 220 ? 0.5378 0.5727 0.2793 0.0415  0.0033  0.0265  220 ALA D CB  
11938 N N   . LEU D 221 ? 0.5825 0.5675 0.3302 0.0354  0.0217  0.0504  221 LEU D N   
11939 C CA  . LEU D 221 ? 0.5827 0.5503 0.3275 0.0393  0.0239  0.0617  221 LEU D CA  
11940 C C   . LEU D 221 ? 0.6570 0.6057 0.3830 0.0414  0.0346  0.0737  221 LEU D C   
11941 O O   . LEU D 221 ? 0.6240 0.5612 0.3335 0.0508  0.0345  0.0840  221 LEU D O   
11942 C CB  . LEU D 221 ? 0.5503 0.5101 0.3181 0.0306  0.0249  0.0591  221 LEU D CB  
11943 C CG  . LEU D 221 ? 0.5196 0.4899 0.3027 0.0301  0.0159  0.0517  221 LEU D CG  
11944 C CD1 . LEU D 221 ? 0.4506 0.4109 0.2542 0.0211  0.0177  0.0490  221 LEU D CD1 
11945 C CD2 . LEU D 221 ? 0.5918 0.5646 0.3657 0.0413  0.0098  0.0570  221 LEU D CD2 
11946 N N   . PRO D 222 ? 0.6458 0.5892 0.3733 0.0331  0.0448  0.0729  222 PRO D N   
11947 C CA  . PRO D 222 ? 0.7266 0.6509 0.4355 0.0338  0.0571  0.0844  222 PRO D CA  
11948 C C   . PRO D 222 ? 0.7617 0.6820 0.4385 0.0469  0.0562  0.0936  222 PRO D C   
11949 O O   . PRO D 222 ? 0.7742 0.6725 0.4332 0.0506  0.0642  0.1062  222 PRO D O   
11950 C CB  . PRO D 222 ? 0.7738 0.7033 0.4893 0.0241  0.0661  0.0780  222 PRO D CB  
11951 C CG  . PRO D 222 ? 0.6804 0.6224 0.4239 0.0167  0.0602  0.0658  222 PRO D CG  
11952 C CD  . PRO D 222 ? 0.6160 0.5693 0.3624 0.0229  0.0466  0.0616  222 PRO D CD  
11953 N N   . ASN D 223 ? 0.6609 0.6008 0.3287 0.0545  0.0465  0.0876  223 ASN D N   
11954 C CA  . ASN D 223 ? 0.7593 0.6961 0.3947 0.0689  0.0444  0.0962  223 ASN D CA  
11955 C C   . ASN D 223 ? 0.7264 0.6750 0.3596 0.0817  0.0298  0.0952  223 ASN D C   
11956 O O   . ASN D 223 ? 0.6636 0.6171 0.2720 0.0955  0.0242  0.0989  223 ASN D O   
11957 C CB  . ASN D 223 ? 0.7729 0.7224 0.3932 0.0696  0.0462  0.0910  223 ASN D CB  
11958 C CG  . ASN D 223 ? 0.8303 0.7735 0.4586 0.0564  0.0600  0.0888  223 ASN D CG  
11959 O OD1 . ASN D 223 ? 0.8734 0.7946 0.4939 0.0526  0.0732  0.0991  223 ASN D OD1 
11960 N ND2 . ASN D 223 ? 0.8201 0.7818 0.4660 0.0486  0.0577  0.0748  223 ASN D ND2 
11961 N N   . ARG D 224 ? 0.6780 0.6315 0.3360 0.0779  0.0237  0.0902  224 ARG D N   
11962 C CA  . ARG D 224 ? 0.6582 0.6235 0.3175 0.0894  0.0111  0.0888  224 ARG D CA  
11963 C C   . ARG D 224 ? 0.7193 0.6615 0.3573 0.1020  0.0134  0.1040  224 ARG D C   
11964 O O   . ARG D 224 ? 0.7420 0.6590 0.3818 0.0966  0.0232  0.1125  224 ARG D O   
11965 C CB  . ARG D 224 ? 0.6508 0.6247 0.3418 0.0806  0.0065  0.0797  224 ARG D CB  
11966 C CG  . ARG D 224 ? 0.6466 0.6424 0.3450 0.0891  -0.0066 0.0728  224 ARG D CG  
11967 C CD  . ARG D 224 ? 0.5571 0.5554 0.2839 0.0807  -0.0086 0.0665  224 ARG D CD  
11968 N NE  . ARG D 224 ? 0.6170 0.6415 0.3530 0.0865  -0.0200 0.0569  224 ARG D NE  
11969 C CZ  . ARG D 224 ? 0.5996 0.6312 0.3557 0.0834  -0.0234 0.0512  224 ARG D CZ  
11970 N NH1 . ARG D 224 ? 0.6209 0.6346 0.3891 0.0752  -0.0175 0.0543  224 ARG D NH1 
11971 N NH2 . ARG D 224 ? 0.5859 0.6439 0.3497 0.0892  -0.0330 0.0419  224 ARG D NH2 
11972 N N   . LYS D 225 ? 0.7052 0.6558 0.3228 0.1191  0.0043  0.1069  225 LYS D N   
11973 C CA  . LYS D 225 ? 0.8024 0.7311 0.3985 0.1342  0.0046  0.1210  225 LYS D CA  
11974 C C   . LYS D 225 ? 0.7823 0.7160 0.3986 0.1377  -0.0031 0.1180  225 LYS D C   
11975 O O   . LYS D 225 ? 0.8162 0.7795 0.4513 0.1386  -0.0144 0.1054  225 LYS D O   
11976 C CB  . LYS D 225 ? 0.8590 0.7951 0.4232 0.1534  -0.0030 0.1252  225 LYS D CB  
11977 C CG  . LYS D 225 ? 1.0357 0.9425 0.5659 0.1565  0.0096  0.1396  225 LYS D CG  
11978 C CD  . LYS D 225 ? 1.1071 1.0256 0.6321 0.1470  0.0147  0.1332  225 LYS D CD  
11979 C CE  . LYS D 225 ? 1.0711 0.9734 0.5676 0.1526  0.0214  0.1419  225 LYS D CE  
11980 N NZ  . LYS D 225 ? 1.1672 1.0323 0.6567 0.1440  0.0393  0.1551  225 LYS D NZ  
11981 N N   . VAL D 226 ? 0.7593 0.6639 0.3726 0.1388  0.0039  0.1287  226 VAL D N   
11982 C CA  . VAL D 226 ? 0.7545 0.6610 0.3840 0.1436  -0.0025 0.1267  226 VAL D CA  
11983 C C   . VAL D 226 ? 0.8349 0.7311 0.4383 0.1663  -0.0079 0.1370  226 VAL D C   
11984 O O   . VAL D 226 ? 0.8361 0.7042 0.4094 0.1737  -0.0003 0.1508  226 VAL D O   
11985 C CB  . VAL D 226 ? 0.7681 0.6506 0.4136 0.1301  0.0076  0.1296  226 VAL D CB  
11986 C CG1 . VAL D 226 ? 0.7892 0.6694 0.4461 0.1374  0.0020  0.1291  226 VAL D CG1 
11987 C CG2 . VAL D 226 ? 0.7545 0.6505 0.4266 0.1105  0.0104  0.1182  226 VAL D CG2 
11988 N N   . GLU D 227 ? 0.8361 0.7555 0.4499 0.1779  -0.0208 0.1300  227 GLU D N   
11989 C CA  . GLU D 227 ? 0.8921 0.8039 0.4833 0.2016  -0.0274 0.1386  227 GLU D CA  
11990 C C   . GLU D 227 ? 0.7958 0.6991 0.3999 0.2075  -0.0293 0.1396  227 GLU D C   
11991 O O   . GLU D 227 ? 0.7807 0.6650 0.3701 0.2220  -0.0294 0.1477  227 GLU D O   
11992 C CB  . GLU D 227 ? 0.9107 0.8596 0.4988 0.2154  -0.0423 0.1293  227 GLU D CB  
11993 C CG  . GLU D 227 ? 0.9759 0.9132 0.5423 0.2332  -0.0449 0.1362  227 GLU D CG  
11994 C CD  . GLU D 227 ? 1.0263 0.9466 0.5682 0.2305  -0.0370 0.1435  227 GLU D CD  
11995 O OE1 . GLU D 227 ? 1.1047 1.0497 0.6432 0.2300  -0.0427 0.1358  227 GLU D OE1 
11996 O OE2 . GLU D 227 ? 1.0562 0.9382 0.5818 0.2291  -0.0248 0.1565  227 GLU D OE2 
11997 N N   . ARG D 228 ? 0.7941 0.7109 0.4311 0.1933  -0.0295 0.1287  228 ARG D N   
11998 C CA  . ARG D 228 ? 0.7038 0.6121 0.3535 0.1975  -0.0301 0.1288  228 ARG D CA  
11999 C C   . ARG D 228 ? 0.7446 0.6079 0.3834 0.1920  -0.0168 0.1414  228 ARG D C   
12000 O O   . ARG D 228 ? 0.7099 0.5541 0.3427 0.1782  -0.0060 0.1463  228 ARG D O   
12001 C CB  . ARG D 228 ? 0.6891 0.6244 0.3748 0.1830  -0.0332 0.1134  228 ARG D CB  
12002 C CG  . ARG D 228 ? 0.6846 0.6125 0.3849 0.1596  -0.0240 0.1101  228 ARG D CG  
12003 C CD  . ARG D 228 ? 0.6498 0.6062 0.3811 0.1469  -0.0280 0.0948  228 ARG D CD  
12004 N NE  . ARG D 228 ? 0.6520 0.6065 0.3973 0.1495  -0.0290 0.0923  228 ARG D NE  
12005 C CZ  . ARG D 228 ? 0.6470 0.5762 0.3973 0.1413  -0.0213 0.0961  228 ARG D CZ  
12006 N NH1 . ARG D 228 ? 0.6420 0.5469 0.3865 0.1297  -0.0121 0.1021  228 ARG D NH1 
12007 N NH2 . ARG D 228 ? 0.6477 0.5771 0.4093 0.1450  -0.0228 0.0930  228 ARG D NH2 
12008 N N   . LYS D 229 ? 0.7366 0.5828 0.3730 0.2031  -0.0171 0.1460  229 LYS D N   
12009 C CA  . LYS D 229 ? 0.8005 0.6056 0.4315 0.1955  -0.0045 0.1550  229 LYS D CA  
12010 C C   . LYS D 229 ? 0.7475 0.5585 0.4102 0.1775  -0.0019 0.1448  229 LYS D C   
12011 O O   . LYS D 229 ? 0.7048 0.5450 0.3892 0.1777  -0.0102 0.1334  229 LYS D O   
12012 C CB  . LYS D 229 ? 0.9015 0.6818 0.5160 0.2135  -0.0044 0.1634  229 LYS D CB  
12013 C CG  . LYS D 229 ? 0.9140 0.6894 0.5049 0.2259  -0.0054 0.1694  229 LYS D CG  
12014 C CD  . LYS D 229 ? 1.0350 0.7784 0.6091 0.2135  0.0091  0.1789  229 LYS D CD  
12015 C CE  . LYS D 229 ? 1.1435 0.8497 0.7213 0.1995  0.0231  0.1836  229 LYS D CE  
12016 N NZ  . LYS D 229 ? 1.1154 0.8051 0.6974 0.2079  0.0224  0.1837  229 LYS D NZ  
12017 N N   . THR D 230 ? 0.7219 0.5063 0.3870 0.1612  0.0100  0.1482  230 THR D N   
12018 C CA  . THR D 230 ? 0.6947 0.4860 0.3881 0.1436  0.0119  0.1380  230 THR D CA  
12019 C C   . THR D 230 ? 0.6520 0.4378 0.3545 0.1505  0.0090  0.1352  230 THR D C   
12020 O O   . THR D 230 ? 0.6363 0.4431 0.3617 0.1442  0.0045  0.1242  230 THR D O   
12021 C CB  . THR D 230 ? 0.6985 0.4652 0.3930 0.1256  0.0244  0.1412  230 THR D CB  
12022 O OG1 . THR D 230 ? 0.6847 0.4574 0.3706 0.1197  0.0279  0.1434  230 THR D OG1 
12023 C CG2 . THR D 230 ? 0.6442 0.4206 0.3670 0.1087  0.0247  0.1299  230 THR D CG2 
12024 N N   . GLY D 231 ? 0.7447 0.5012 0.4278 0.1643  0.0120  0.1451  231 GLY D N   
12025 C CA  . GLY D 231 ? 0.7161 0.4655 0.4089 0.1692  0.0105  0.1415  231 GLY D CA  
12026 C C   . GLY D 231 ? 0.6733 0.4117 0.3843 0.1495  0.0173  0.1355  231 GLY D C   
12027 O O   . GLY D 231 ? 0.7206 0.4499 0.4342 0.1331  0.0247  0.1361  231 GLY D O   
12028 N N   . ALA D 232 ? 0.6985 0.4410 0.4233 0.1514  0.0143  0.1283  232 ALA D N   
12029 C CA  . ALA D 232 ? 0.6634 0.3963 0.4040 0.1347  0.0193  0.1218  232 ALA D CA  
12030 C C   . ALA D 232 ? 0.6209 0.3788 0.3798 0.1181  0.0176  0.1132  232 ALA D C   
12031 O O   . ALA D 232 ? 0.6324 0.4212 0.3990 0.1202  0.0106  0.1080  232 ALA D O   
12032 C CB  . ALA D 232 ? 0.6590 0.3938 0.4094 0.1409  0.0160  0.1151  232 ALA D CB  
12033 N N   . ARG D 233 ? 0.6117 0.3561 0.3782 0.1018  0.0238  0.1109  233 ARG D N   
12034 C CA  . ARG D 233 ? 0.5600 0.3237 0.3427 0.0866  0.0226  0.1030  233 ARG D CA  
12035 C C   . ARG D 233 ? 0.5728 0.3466 0.3718 0.0821  0.0188  0.0929  233 ARG D C   
12036 O O   . ARG D 233 ? 0.6036 0.3593 0.4061 0.0769  0.0221  0.0905  233 ARG D O   
12037 C CB  . ARG D 233 ? 0.6038 0.3499 0.3864 0.0727  0.0310  0.1052  233 ARG D CB  
12038 C CG  . ARG D 233 ? 0.6142 0.3467 0.3776 0.0764  0.0372  0.1161  233 ARG D CG  
12039 C CD  . ARG D 233 ? 0.6282 0.3451 0.3942 0.0607  0.0473  0.1169  233 ARG D CD  
12040 N NE  . ARG D 233 ? 0.6209 0.3606 0.4044 0.0482  0.0451  0.1083  233 ARG D NE  
12041 C CZ  . ARG D 233 ? 0.6023 0.3588 0.3840 0.0466  0.0445  0.1089  233 ARG D CZ  
12042 N NH1 . ARG D 233 ? 0.6283 0.3829 0.3910 0.0562  0.0457  0.1175  233 ARG D NH1 
12043 N NH2 . ARG D 233 ? 0.5825 0.3578 0.3805 0.0361  0.0423  0.1003  233 ARG D NH2 
12044 N N   . PHE D 234 ? 0.5127 0.3143 0.3206 0.0841  0.0123  0.0867  234 PHE D N   
12045 C CA  . PHE D 234 ? 0.5025 0.3132 0.3230 0.0806  0.0097  0.0778  234 PHE D CA  
12046 C C   . PHE D 234 ? 0.5380 0.3595 0.3700 0.0662  0.0091  0.0711  234 PHE D C   
12047 O O   . PHE D 234 ? 0.5005 0.3315 0.3334 0.0607  0.0090  0.0717  234 PHE D O   
12048 C CB  . PHE D 234 ? 0.5200 0.3543 0.3442 0.0910  0.0043  0.0739  234 PHE D CB  
12049 C CG  . PHE D 234 ? 0.5654 0.3912 0.3820 0.1067  0.0037  0.0773  234 PHE D CG  
12050 C CD1 . PHE D 234 ? 0.5724 0.3676 0.3802 0.1096  0.0082  0.0820  234 PHE D CD1 
12051 C CD2 . PHE D 234 ? 0.5668 0.4158 0.3857 0.1189  -0.0015 0.0748  234 PHE D CD2 
12052 C CE1 . PHE D 234 ? 0.6099 0.3954 0.4096 0.1253  0.0076  0.0851  234 PHE D CE1 
12053 C CE2 . PHE D 234 ? 0.6385 0.4810 0.4509 0.1354  -0.0028 0.0773  234 PHE D CE2 
12054 C CZ  . PHE D 234 ? 0.6689 0.4784 0.4708 0.1390  0.0019  0.0829  234 PHE D CZ  
12055 N N   . MET D 235 ? 0.4805 0.2997 0.3199 0.0610  0.0087  0.0646  235 MET D N   
12056 C CA  . MET D 235 ? 0.4572 0.2881 0.3054 0.0507  0.0070  0.0581  235 MET D CA  
12057 C C   . MET D 235 ? 0.4706 0.3149 0.3233 0.0534  0.0048  0.0521  235 MET D C   
12058 O O   . MET D 235 ? 0.5063 0.3448 0.3570 0.0604  0.0053  0.0515  235 MET D O   
12059 C CB  . MET D 235 ? 0.5106 0.3255 0.3618 0.0416  0.0087  0.0555  235 MET D CB  
12060 C CG  . MET D 235 ? 0.4739 0.2962 0.3318 0.0338  0.0061  0.0482  235 MET D CG  
12061 S SD  . MET D 235 ? 0.5151 0.3190 0.3763 0.0259  0.0068  0.0447  235 MET D SD  
12062 C CE  . MET D 235 ? 0.4443 0.2597 0.3115 0.0182  0.0032  0.0390  235 MET D CE  
12063 N N   . THR D 236 ? 0.4493 0.3104 0.3075 0.0477  0.0033  0.0474  236 THR D N   
12064 C CA  . THR D 236 ? 0.4310 0.3024 0.2931 0.0476  0.0033  0.0413  236 THR D CA  
12065 C C   . THR D 236 ? 0.4773 0.3409 0.3400 0.0384  0.0038  0.0369  236 THR D C   
12066 O O   . THR D 236 ? 0.4538 0.3144 0.3172 0.0316  0.0030  0.0370  236 THR D O   
12067 C CB  . THR D 236 ? 0.4077 0.3045 0.2753 0.0485  0.0022  0.0381  236 THR D CB  
12068 O OG1 . THR D 236 ? 0.4239 0.3267 0.2928 0.0413  0.0014  0.0380  236 THR D OG1 
12069 C CG2 . THR D 236 ? 0.4585 0.3657 0.3248 0.0607  0.0001  0.0413  236 THR D CG2 
12070 N N   . ILE D 237 ? 0.3996 0.2597 0.2610 0.0393  0.0051  0.0330  237 ILE D N   
12071 C CA  . ILE D 237 ? 0.4194 0.2692 0.2775 0.0329  0.0052  0.0293  237 ILE D CA  
12072 C C   . ILE D 237 ? 0.4371 0.2957 0.2945 0.0316  0.0082  0.0246  237 ILE D C   
12073 O O   . ILE D 237 ? 0.4456 0.3118 0.3047 0.0372  0.0105  0.0230  237 ILE D O   
12074 C CB  . ILE D 237 ? 0.4327 0.2634 0.2865 0.0348  0.0045  0.0288  237 ILE D CB  
12075 C CG1 . ILE D 237 ? 0.4418 0.2632 0.2974 0.0341  0.0033  0.0328  237 ILE D CG1 
12076 C CG2 . ILE D 237 ? 0.4467 0.2684 0.2956 0.0296  0.0030  0.0244  237 ILE D CG2 
12077 C CD1 . ILE D 237 ? 0.4742 0.2766 0.3271 0.0363  0.0036  0.0320  237 ILE D CD1 
12078 N N   . GLY D 238 ? 0.4346 0.2917 0.2890 0.0245  0.0089  0.0223  238 GLY D N   
12079 C CA  . GLY D 238 ? 0.4080 0.2711 0.2601 0.0219  0.0137  0.0183  238 GLY D CA  
12080 C C   . GLY D 238 ? 0.4459 0.3028 0.2920 0.0142  0.0149  0.0170  238 GLY D C   
12081 O O   . GLY D 238 ? 0.4293 0.2776 0.2732 0.0120  0.0110  0.0187  238 GLY D O   
12082 N N   . SER D 239 ? 0.4217 0.2830 0.2652 0.0102  0.0210  0.0137  239 SER D N   
12083 C CA  . SER D 239 ? 0.4614 0.3147 0.2973 0.0029  0.0237  0.0127  239 SER D CA  
12084 C C   . SER D 239 ? 0.4569 0.3236 0.3020 -0.0020 0.0236  0.0120  239 SER D C   
12085 O O   . SER D 239 ? 0.4357 0.2980 0.2811 -0.0023 0.0188  0.0143  239 SER D O   
12086 C CB  . SER D 239 ? 0.4350 0.2843 0.2625 -0.0005 0.0321  0.0097  239 SER D CB  
12087 O OG  . SER D 239 ? 0.4159 0.2863 0.2551 -0.0023 0.0378  0.0057  239 SER D OG  
12088 N N   . GLU D 240 ? 0.4337 0.3181 0.2870 -0.0059 0.0289  0.0079  240 GLU D N   
12089 C CA  . GLU D 240 ? 0.4538 0.3512 0.3153 -0.0110 0.0286  0.0058  240 GLU D CA  
12090 C C   . GLU D 240 ? 0.4801 0.3973 0.3535 -0.0049 0.0233  0.0064  240 GLU D C   
12091 O O   . GLU D 240 ? 0.4697 0.3873 0.3443 -0.0040 0.0185  0.0089  240 GLU D O   
12092 C CB  . GLU D 240 ? 0.5005 0.4051 0.3640 -0.0204 0.0373  -0.0004 240 GLU D CB  
12093 C CG  . GLU D 240 ? 0.5375 0.4636 0.4139 -0.0248 0.0366  -0.0051 240 GLU D CG  
12094 C CD  . GLU D 240 ? 0.5589 0.4737 0.4302 -0.0288 0.0341  -0.0037 240 GLU D CD  
12095 O OE1 . GLU D 240 ? 0.5919 0.4828 0.4504 -0.0284 0.0333  0.0006  240 GLU D OE1 
12096 O OE2 . GLU D 240 ? 0.5695 0.5001 0.4496 -0.0314 0.0322  -0.0073 240 GLU D OE2 
12097 N N   . ASN D 241 ? 0.4419 0.3744 0.3225 0.0006  0.0241  0.0044  241 ASN D N   
12098 C CA  . ASN D 241 ? 0.4123 0.3621 0.3013 0.0090  0.0189  0.0055  241 ASN D CA  
12099 C C   . ASN D 241 ? 0.4370 0.4047 0.3332 0.0050  0.0171  0.0021  241 ASN D C   
12100 O O   . ASN D 241 ? 0.4680 0.4362 0.3631 0.0082  0.0120  0.0058  241 ASN D O   
12101 C CB  . ASN D 241 ? 0.4241 0.3587 0.3069 0.0164  0.0134  0.0131  241 ASN D CB  
12102 C CG  . ASN D 241 ? 0.4510 0.3728 0.3289 0.0225  0.0142  0.0151  241 ASN D CG  
12103 O OD1 . ASN D 241 ? 0.4411 0.3685 0.3209 0.0229  0.0185  0.0109  241 ASN D OD1 
12104 N ND2 . ASN D 241 ? 0.4823 0.3882 0.3551 0.0271  0.0106  0.0206  241 ASN D ND2 
12105 N N   . ASP D 242 ? 0.4870 0.4691 0.3904 -0.0029 0.0221  -0.0058 242 ASP D N   
12106 C CA  . ASP D 242 ? 0.5145 0.5141 0.4253 -0.0078 0.0206  -0.0110 242 ASP D CA  
12107 C C   . ASP D 242 ? 0.4983 0.5301 0.4229 -0.0029 0.0184  -0.0177 242 ASP D C   
12108 O O   . ASP D 242 ? 0.5061 0.5566 0.4388 -0.0083 0.0178  -0.0250 242 ASP D O   
12109 C CB  . ASP D 242 ? 0.4578 0.4513 0.3677 -0.0217 0.0276  -0.0167 242 ASP D CB  
12110 C CG  . ASP D 242 ? 0.5314 0.5287 0.4451 -0.0280 0.0366  -0.0225 242 ASP D CG  
12111 O OD1 . ASP D 242 ? 0.5422 0.5457 0.4588 -0.0212 0.0372  -0.0220 242 ASP D OD1 
12112 O OD2 . ASP D 242 ? 0.6036 0.5994 0.5183 -0.0401 0.0439  -0.0285 242 ASP D OD2 
12113 N N   . ASP D 243 ? 0.4751 0.5144 0.4028 0.0075  0.0169  -0.0165 243 ASP D N   
12114 C CA  . ASP D 243 ? 0.5214 0.5933 0.4625 0.0150  0.0132  -0.0231 243 ASP D CA  
12115 C C   . ASP D 243 ? 0.4645 0.5414 0.4012 0.0266  0.0036  -0.0176 243 ASP D C   
12116 O O   . ASP D 243 ? 0.4534 0.5230 0.3840 0.0395  -0.0003 -0.0104 243 ASP D O   
12117 C CB  . ASP D 243 ? 0.4930 0.5715 0.4393 0.0226  0.0157  -0.0248 243 ASP D CB  
12118 C CG  . ASP D 243 ? 0.5305 0.6473 0.4942 0.0291  0.0129  -0.0348 243 ASP D CG  
12119 O OD1 . ASP D 243 ? 0.4964 0.6332 0.4653 0.0317  0.0063  -0.0382 243 ASP D OD1 
12120 O OD2 . ASP D 243 ? 0.6214 0.7495 0.5936 0.0324  0.0171  -0.0397 243 ASP D OD2 
12121 N N   . ILE D 244 ? 0.4742 0.5943 0.4586 0.0641  -0.0821 0.0036  244 ILE D N   
12122 C CA  . ILE D 244 ? 0.4722 0.5850 0.4361 0.0723  -0.0858 0.0074  244 ILE D CA  
12123 C C   . ILE D 244 ? 0.4927 0.6137 0.4544 0.0857  -0.0913 0.0114  244 ILE D C   
12124 O O   . ILE D 244 ? 0.5086 0.6166 0.4525 0.0949  -0.0898 0.0184  244 ILE D O   
12125 C CB  . ILE D 244 ? 0.5488 0.6683 0.5073 0.0683  -0.0927 0.0010  244 ILE D CB  
12126 C CG1 . ILE D 244 ? 0.5466 0.6630 0.5119 0.0550  -0.0885 -0.0046 244 ILE D CG1 
12127 C CG2 . ILE D 244 ? 0.5411 0.6475 0.4745 0.0759  -0.0942 0.0057  244 ILE D CG2 
12128 C CD1 . ILE D 244 ? 0.5660 0.6610 0.5193 0.0513  -0.0795 -0.0003 244 ILE D CD1 
12129 N N   . ALA D 245 ? 0.4999 0.6429 0.4793 0.0873  -0.0978 0.0070  245 ALA D N   
12130 C CA  . ALA D 245 ? 0.4779 0.6313 0.4559 0.1009  -0.1043 0.0102  245 ALA D CA  
12131 C C   . ALA D 245 ? 0.5003 0.6407 0.4747 0.1085  -0.0967 0.0189  245 ALA D C   
12132 O O   . ALA D 245 ? 0.4967 0.6326 0.4580 0.1213  -0.0985 0.0252  245 ALA D O   
12133 C CB  . ALA D 245 ? 0.5215 0.7028 0.5222 0.1002  -0.1125 0.0029  245 ALA D CB  
12134 N N   . PHE D 246 ? 0.4915 0.6248 0.4762 0.1013  -0.0878 0.0194  246 PHE D N   
12135 C CA  . PHE D 246 ? 0.4791 0.5966 0.4580 0.1072  -0.0796 0.0272  246 PHE D CA  
12136 C C   . PHE D 246 ? 0.4821 0.5760 0.4371 0.1104  -0.0746 0.0335  246 PHE D C   
12137 O O   . PHE D 246 ? 0.5029 0.5866 0.4460 0.1212  -0.0723 0.0406  246 PHE D O   
12138 C CB  . PHE D 246 ? 0.4867 0.5997 0.4792 0.0979  -0.0711 0.0258  246 PHE D CB  
12139 C CG  . PHE D 246 ? 0.4533 0.5490 0.4395 0.1029  -0.0624 0.0328  246 PHE D CG  
12140 C CD1 . PHE D 246 ? 0.5486 0.6509 0.5433 0.1111  -0.0618 0.0355  246 PHE D CD1 
12141 C CD2 . PHE D 246 ? 0.4872 0.5601 0.4589 0.0997  -0.0547 0.0366  246 PHE D CD2 
12142 C CE1 . PHE D 246 ? 0.5363 0.6217 0.5244 0.1157  -0.0535 0.0417  246 PHE D CE1 
12143 C CE2 . PHE D 246 ? 0.5000 0.5568 0.4659 0.1038  -0.0467 0.0424  246 PHE D CE2 
12144 C CZ  . PHE D 246 ? 0.5567 0.6191 0.5301 0.1118  -0.0461 0.0449  246 PHE D CZ  
12145 N N   . MET D 247 ? 0.4655 0.5505 0.4133 0.1014  -0.0727 0.0311  247 MET D N   
12146 C CA  . MET D 247 ? 0.4827 0.5453 0.4098 0.1030  -0.0667 0.0366  247 MET D CA  
12147 C C   . MET D 247 ? 0.4937 0.5547 0.4028 0.1153  -0.0720 0.0407  247 MET D C   
12148 O O   . MET D 247 ? 0.5192 0.5618 0.4115 0.1222  -0.0662 0.0479  247 MET D O   
12149 C CB  . MET D 247 ? 0.4443 0.5004 0.3682 0.0916  -0.0644 0.0325  247 MET D CB  
12150 C CG  . MET D 247 ? 0.5064 0.5626 0.4456 0.0800  -0.0590 0.0287  247 MET D CG  
12151 S SD  . MET D 247 ? 0.5065 0.5454 0.4460 0.0803  -0.0481 0.0344  247 MET D SD  
12152 C CE  . MET D 247 ? 0.4341 0.4762 0.3890 0.0661  -0.0448 0.0280  247 MET D CE  
12153 N N   . GLY D 248 ? 0.5053 0.5852 0.4173 0.1181  -0.0830 0.0359  248 GLY D N   
12154 C CA  . GLY D 248 ? 0.4889 0.5693 0.3835 0.1309  -0.0895 0.0394  248 GLY D CA  
12155 C C   . GLY D 248 ? 0.5163 0.5960 0.4084 0.1447  -0.0891 0.0462  248 GLY D C   
12156 O O   . GLY D 248 ? 0.5310 0.5996 0.4028 0.1564  -0.0891 0.0527  248 GLY D O   
12157 N N   . MET D 249 ? 0.5277 0.6179 0.4395 0.1439  -0.0880 0.0452  249 MET D N   
12158 C CA  . MET D 249 ? 0.5638 0.6529 0.4738 0.1573  -0.0868 0.0519  249 MET D CA  
12159 C C   . MET D 249 ? 0.5562 0.6163 0.4505 0.1595  -0.0742 0.0602  249 MET D C   
12160 O O   . MET D 249 ? 0.5756 0.6244 0.4537 0.1725  -0.0724 0.0677  249 MET D O   
12161 C CB  . MET D 249 ? 0.5262 0.6329 0.4617 0.1552  -0.0876 0.0485  249 MET D CB  
12162 C CG  . MET D 249 ? 0.5907 0.6904 0.5255 0.1668  -0.0821 0.0560  249 MET D CG  
12163 S SD  . MET D 249 ? 0.5658 0.6364 0.4948 0.1623  -0.0660 0.0619  249 MET D SD  
12164 C CE  . MET D 249 ? 0.5682 0.6504 0.5243 0.1492  -0.0628 0.0551  249 MET D CE  
12165 N N   . VAL D 250 ? 0.5334 0.5810 0.4317 0.1467  -0.0655 0.0586  250 VAL D N   
12166 C CA  . VAL D 250 ? 0.5964 0.6170 0.4814 0.1462  -0.0534 0.0648  250 VAL D CA  
12167 C C   . VAL D 250 ? 0.5799 0.5838 0.4396 0.1533  -0.0517 0.0703  250 VAL D C   
12168 O O   . VAL D 250 ? 0.6453 0.6321 0.4907 0.1628  -0.0454 0.0780  250 VAL D O   
12169 C CB  . VAL D 250 ? 0.5591 0.5725 0.4529 0.1306  -0.0465 0.0607  250 VAL D CB  
12170 C CG1 . VAL D 250 ? 0.5839 0.5705 0.4641 0.1294  -0.0347 0.0661  250 VAL D CG1 
12171 C CG2 . VAL D 250 ? 0.5183 0.5433 0.4339 0.1251  -0.0458 0.0568  250 VAL D CG2 
12172 N N   . GLU D 251 ? 0.5680 0.5761 0.4210 0.1495  -0.0571 0.0667  251 GLU D N   
12173 C CA  . GLU D 251 ? 0.5280 0.5193 0.3560 0.1557  -0.0548 0.0717  251 GLU D CA  
12174 C C   . GLU D 251 ? 0.6331 0.6284 0.4467 0.1725  -0.0618 0.0764  251 GLU D C   
12175 O O   . GLU D 251 ? 0.7693 0.7491 0.5596 0.1796  -0.0595 0.0814  251 GLU D O   
12176 C CB  . GLU D 251 ? 0.5321 0.5257 0.3566 0.1463  -0.0579 0.0661  251 GLU D CB  
12177 C CG  . GLU D 251 ? 0.5240 0.5098 0.3586 0.1311  -0.0496 0.0627  251 GLU D CG  
12178 C CD  . GLU D 251 ? 0.5447 0.5250 0.3706 0.1235  -0.0490 0.0596  251 GLU D CD  
12179 O OE1 . GLU D 251 ? 0.5201 0.5147 0.3458 0.1233  -0.0585 0.0546  251 GLU D OE1 
12180 O OE2 . GLU D 251 ? 0.5327 0.4955 0.3539 0.1170  -0.0389 0.0615  251 GLU D OE2 
12181 N N   . SER D 252 ? 0.6135 0.6296 0.4400 0.1795  -0.0705 0.0747  252 SER D N   
12182 C CA  . SER D 252 ? 0.6187 0.6399 0.4321 0.1969  -0.0777 0.0793  252 SER D CA  
12183 C C   . SER D 252 ? 0.6222 0.6300 0.4297 0.2086  -0.0703 0.0881  252 SER D C   
12184 O O   . SER D 252 ? 0.6667 0.6739 0.4597 0.2247  -0.0743 0.0937  252 SER D O   
12185 C CB  . SER D 252 ? 0.6543 0.7081 0.4851 0.1993  -0.0924 0.0722  252 SER D CB  
12186 O OG  . SER D 252 ? 0.6497 0.7164 0.5043 0.1971  -0.0917 0.0703  252 SER D OG  
12187 N N   . VAL D 253 ? 0.6435 0.6407 0.4616 0.2013  -0.0598 0.0892  253 VAL D N   
12188 C CA  . VAL D 253 ? 0.6953 0.6770 0.5070 0.2117  -0.0514 0.0973  253 VAL D CA  
12189 C C   . VAL D 253 ? 0.6517 0.6018 0.4368 0.2167  -0.0401 0.1056  253 VAL D C   
12190 O O   . VAL D 253 ? 0.7016 0.6369 0.4754 0.2287  -0.0339 0.1134  253 VAL D O   
12191 C CB  . VAL D 253 ? 0.6227 0.6036 0.4543 0.2022  -0.0440 0.0951  253 VAL D CB  
12192 C CG1 . VAL D 253 ? 0.6531 0.6621 0.5109 0.1937  -0.0528 0.0862  253 VAL D CG1 
12193 C CG2 . VAL D 253 ? 0.6755 0.6337 0.5030 0.1893  -0.0319 0.0950  253 VAL D CG2 
12194 N N   . GLY D 254 ? 0.6256 0.5644 0.4003 0.2083  -0.0369 0.1042  254 GLY D N   
12195 C CA  . GLY D 254 ? 0.6713 0.5796 0.4227 0.2111  -0.0247 0.1114  254 GLY D CA  
12196 C C   . GLY D 254 ? 0.6651 0.5596 0.4222 0.1944  -0.0142 0.1083  254 GLY D C   
12197 O O   . GLY D 254 ? 0.6645 0.5360 0.4155 0.1926  -0.0012 0.1127  254 GLY D O   
12198 N N   . ALA D 255 ? 0.6533 0.5621 0.4226 0.1818  -0.0198 0.1004  255 ALA D N   
12199 C CA  . ALA D 255 ? 0.5577 0.4579 0.3365 0.1659  -0.0115 0.0966  255 ALA D CA  
12200 C C   . ALA D 255 ? 0.5950 0.5060 0.3766 0.1567  -0.0175 0.0902  255 ALA D C   
12201 O O   . ALA D 255 ? 0.5925 0.5205 0.3730 0.1609  -0.0289 0.0873  255 ALA D O   
12202 C CB  . ALA D 255 ? 0.5933 0.5026 0.3952 0.1584  -0.0105 0.0925  255 ALA D CB  
12203 N N   . THR D 256 ? 0.5424 0.4435 0.3277 0.1440  -0.0098 0.0876  256 THR D N   
12204 C CA  . THR D 256 ? 0.5305 0.4414 0.3213 0.1336  -0.0142 0.0810  256 THR D CA  
12205 C C   . THR D 256 ? 0.5396 0.4531 0.3500 0.1194  -0.0100 0.0757  256 THR D C   
12206 O O   . THR D 256 ? 0.5451 0.4428 0.3561 0.1155  0.0004  0.0779  256 THR D O   
12207 C CB  . THR D 256 ? 0.5720 0.4658 0.3424 0.1341  -0.0085 0.0839  256 THR D CB  
12208 O OG1 . THR D 256 ? 0.5856 0.4741 0.3347 0.1488  -0.0115 0.0898  256 THR D OG1 
12209 C CG2 . THR D 256 ? 0.5444 0.4484 0.3196 0.1243  -0.0133 0.0771  256 THR D CG2 
12210 N N   . ILE D 257 ? 0.4890 0.4217 0.3150 0.1116  -0.0178 0.0684  257 ILE D N   
12211 C CA  . ILE D 257 ? 0.4570 0.3918 0.2994 0.0984  -0.0142 0.0633  257 ILE D CA  
12212 C C   . ILE D 257 ? 0.4738 0.3985 0.3091 0.0911  -0.0092 0.0621  257 ILE D C   
12213 O O   . ILE D 257 ? 0.4807 0.4129 0.3122 0.0897  -0.0148 0.0590  257 ILE D O   
12214 C CB  . ILE D 257 ? 0.4663 0.4238 0.3272 0.0934  -0.0233 0.0565  257 ILE D CB  
12215 C CG1 . ILE D 257 ? 0.4916 0.4595 0.3604 0.1012  -0.0276 0.0578  257 ILE D CG1 
12216 C CG2 . ILE D 257 ? 0.4445 0.4018 0.3189 0.0808  -0.0191 0.0518  257 ILE D CG2 
12217 C CD1 . ILE D 257 ? 0.4946 0.4867 0.3788 0.0993  -0.0378 0.0516  257 ILE D CD1 
12218 N N   . VAL D 258 ? 0.4623 0.3703 0.2960 0.0864  0.0016  0.0642  258 VAL D N   
12219 C CA  . VAL D 258 ? 0.4570 0.3546 0.2835 0.0805  0.0075  0.0637  258 VAL D CA  
12220 C C   . VAL D 258 ? 0.5022 0.4054 0.3445 0.0678  0.0089  0.0576  258 VAL D C   
12221 O O   . VAL D 258 ? 0.4380 0.3361 0.2767 0.0626  0.0126  0.0563  258 VAL D O   
12222 C CB  . VAL D 258 ? 0.4925 0.3666 0.3050 0.0838  0.0195  0.0700  258 VAL D CB  
12223 C CG1 . VAL D 258 ? 0.5369 0.4025 0.3294 0.0979  0.0189  0.0770  258 VAL D CG1 
12224 C CG2 . VAL D 258 ? 0.4883 0.3558 0.3120 0.0795  0.0264  0.0700  258 VAL D CG2 
12225 N N   . ILE D 259 ? 0.4200 0.3332 0.2788 0.0633  0.0064  0.0540  259 ILE D N   
12226 C CA  . ILE D 259 ? 0.4202 0.3394 0.2933 0.0524  0.0069  0.0483  259 ILE D CA  
12227 C C   . ILE D 259 ? 0.4100 0.3424 0.2977 0.0512  0.0016  0.0452  259 ILE D C   
12228 O O   . ILE D 259 ? 0.3844 0.3193 0.2719 0.0581  -0.0007 0.0477  259 ILE D O   
12229 C CB  . ILE D 259 ? 0.4368 0.3418 0.3110 0.0465  0.0171  0.0489  259 ILE D CB  
12230 C CG1 . ILE D 259 ? 0.3839 0.2951 0.2702 0.0363  0.0173  0.0432  259 ILE D CG1 
12231 C CG2 . ILE D 259 ? 0.4382 0.3351 0.3151 0.0484  0.0219  0.0512  259 ILE D CG2 
12232 C CD1 . ILE D 259 ? 0.4225 0.3421 0.3069 0.0344  0.0124  0.0405  259 ILE D CD1 
12233 N N   . ASP D 260 ? 0.3755 0.3165 0.2757 0.0430  -0.0002 0.0399  260 ASP D N   
12234 C CA  . ASP D 260 ? 0.4123 0.3660 0.3255 0.0416  -0.0050 0.0367  260 ASP D CA  
12235 C C   . ASP D 260 ? 0.3621 0.3165 0.2858 0.0326  -0.0024 0.0325  260 ASP D C   
12236 O O   . ASP D 260 ? 0.3661 0.3161 0.2883 0.0275  0.0006  0.0311  260 ASP D O   
12237 C CB  . ASP D 260 ? 0.3825 0.3515 0.2981 0.0433  -0.0137 0.0340  260 ASP D CB  
12238 C CG  . ASP D 260 ? 0.4078 0.3799 0.3228 0.0371  -0.0151 0.0301  260 ASP D CG  
12239 O OD1 . ASP D 260 ? 0.4257 0.4040 0.3513 0.0304  -0.0157 0.0258  260 ASP D OD1 
12240 O OD2 . ASP D 260 ? 0.4271 0.3940 0.3303 0.0390  -0.0149 0.0316  260 ASP D OD2 
12241 N N   . ASP D 261 ? 0.3649 0.3249 0.2991 0.0311  -0.0034 0.0305  261 ASP D N   
12242 C CA  . ASP D 261 ? 0.3434 0.3067 0.2876 0.0238  -0.0026 0.0261  261 ASP D CA  
12243 C C   . ASP D 261 ? 0.3327 0.3094 0.2858 0.0238  -0.0080 0.0234  261 ASP D C   
12244 O O   . ASP D 261 ? 0.3011 0.2801 0.2598 0.0258  -0.0079 0.0236  261 ASP D O   
12245 C CB  . ASP D 261 ? 0.3342 0.2885 0.2810 0.0223  0.0027  0.0265  261 ASP D CB  
12246 C CG  . ASP D 261 ? 0.3425 0.3006 0.2984 0.0159  0.0027  0.0219  261 ASP D CG  
12247 O OD1 . ASP D 261 ? 0.3703 0.3300 0.3272 0.0112  0.0025  0.0196  261 ASP D OD1 
12248 O OD2 . ASP D 261 ? 0.3568 0.3165 0.3181 0.0160  0.0027  0.0208  261 ASP D OD2 
12249 N N   . GLN D 262 ? 0.3163 0.3014 0.2709 0.0212  -0.0120 0.0205  262 GLN D N   
12250 C CA  . GLN D 262 ? 0.3233 0.3212 0.2868 0.0207  -0.0166 0.0175  262 GLN D CA  
12251 C C   . GLN D 262 ? 0.3007 0.3036 0.2651 0.0156  -0.0188 0.0137  262 GLN D C   
12252 O O   . GLN D 262 ? 0.3000 0.2981 0.2565 0.0146  -0.0182 0.0141  262 GLN D O   
12253 C CB  . GLN D 262 ? 0.3293 0.3352 0.2924 0.0275  -0.0212 0.0191  262 GLN D CB  
12254 C CG  . GLN D 262 ? 0.3591 0.3654 0.3118 0.0307  -0.0248 0.0202  262 GLN D CG  
12255 C CD  . GLN D 262 ? 0.3678 0.3748 0.3142 0.0400  -0.0274 0.0243  262 GLN D CD  
12256 O OE1 . GLN D 262 ? 0.3790 0.3810 0.3254 0.0445  -0.0244 0.0278  262 GLN D OE1 
12257 N NE2 . GLN D 262 ? 0.3664 0.3784 0.3057 0.0435  -0.0326 0.0240  262 GLN D NE2 
12258 N N   . CYS D 263 ? 0.3230 0.3352 0.2970 0.0125  -0.0207 0.0100  263 CYS D N   
12259 C CA  . CYS D 263 ? 0.3367 0.3522 0.3119 0.0071  -0.0218 0.0060  263 CYS D CA  
12260 C C   . CYS D 263 ? 0.3445 0.3678 0.3171 0.0082  -0.0272 0.0040  263 CYS D C   
12261 O O   . CYS D 263 ? 0.3129 0.3371 0.2841 0.0039  -0.0278 0.0007  263 CYS D O   
12262 C CB  . CYS D 263 ? 0.3028 0.3226 0.2883 0.0029  -0.0203 0.0028  263 CYS D CB  
12263 S SG  . CYS D 263 ? 0.2897 0.2992 0.2742 -0.0001 -0.0148 0.0034  263 CYS D SG  
12264 N N   . SER D 264 ? 0.3070 0.3361 0.2785 0.0140  -0.0313 0.0056  264 SER D N   
12265 C CA  . SER D 264 ? 0.3520 0.3870 0.3178 0.0158  -0.0369 0.0039  264 SER D CA  
12266 C C   . SER D 264 ? 0.3843 0.4083 0.3352 0.0176  -0.0353 0.0068  264 SER D C   
12267 O O   . SER D 264 ? 0.3447 0.3709 0.2881 0.0183  -0.0391 0.0050  264 SER D O   
12268 C CB  . SER D 264 ? 0.3785 0.4234 0.3465 0.0228  -0.0423 0.0050  264 SER D CB  
12269 O OG  . SER D 264 ? 0.3447 0.3807 0.3054 0.0295  -0.0396 0.0111  264 SER D OG  
12270 N N   . GLY D 265 ? 0.3696 0.3817 0.3164 0.0180  -0.0293 0.0106  265 GLY D N   
12271 C CA  . GLY D 265 ? 0.3355 0.3358 0.2691 0.0207  -0.0262 0.0145  265 GLY D CA  
12272 C C   . GLY D 265 ? 0.3417 0.3321 0.2754 0.0156  -0.0195 0.0148  265 GLY D C   
12273 O O   . GLY D 265 ? 0.3578 0.3500 0.2957 0.0099  -0.0188 0.0113  265 GLY D O   
12274 N N   . SER D 266 ? 0.3203 0.3004 0.2501 0.0174  -0.0144 0.0187  266 SER D N   
12275 C CA  . SER D 266 ? 0.3170 0.2884 0.2465 0.0129  -0.0082 0.0187  266 SER D CA  
12276 C C   . SER D 266 ? 0.3639 0.3394 0.3044 0.0069  -0.0075 0.0150  266 SER D C   
12277 O O   . SER D 266 ? 0.3384 0.3110 0.2790 0.0029  -0.0047 0.0134  266 SER D O   
12278 C CB  . SER D 266 ? 0.3408 0.3015 0.2673 0.0151  -0.0027 0.0227  266 SER D CB  
12279 O OG  . SER D 266 ? 0.3392 0.3028 0.2736 0.0159  -0.0034 0.0226  266 SER D OG  
12280 N N   . ARG D 267 ? 0.3274 0.3087 0.2768 0.0066  -0.0093 0.0137  267 ARG D N   
12281 C CA  . ARG D 267 ? 0.2860 0.2692 0.2438 0.0019  -0.0080 0.0108  267 ARG D CA  
12282 C C   . ARG D 267 ? 0.3233 0.3118 0.2829 -0.0017 -0.0099 0.0072  267 ARG D C   
12283 O O   . ARG D 267 ? 0.3633 0.3511 0.3270 -0.0051 -0.0079 0.0052  267 ARG D O   
12284 C CB  . ARG D 267 ? 0.2696 0.2564 0.2348 0.0030  -0.0088 0.0105  267 ARG D CB  
12285 C CG  . ARG D 267 ? 0.3135 0.2978 0.2839 -0.0004 -0.0060 0.0087  267 ARG D CG  
12286 C CD  . ARG D 267 ? 0.3285 0.3152 0.3047 0.0008  -0.0063 0.0083  267 ARG D CD  
12287 N NE  . ARG D 267 ? 0.2749 0.2579 0.2495 0.0048  -0.0053 0.0112  267 ARG D NE  
12288 C CZ  . ARG D 267 ? 0.3230 0.3105 0.2991 0.0089  -0.0073 0.0126  267 ARG D CZ  
12289 N NH1 . ARG D 267 ? 0.2978 0.2948 0.2781 0.0090  -0.0107 0.0110  267 ARG D NH1 
12290 N NH2 . ARG D 267 ? 0.2828 0.2653 0.2565 0.0130  -0.0056 0.0155  267 ARG D NH2 
12291 N N   . TYR D 268 ? 0.2964 0.2898 0.2528 -0.0007 -0.0136 0.0061  268 TYR D N   
12292 C CA  . TYR D 268 ? 0.2998 0.2967 0.2570 -0.0046 -0.0147 0.0023  268 TYR D CA  
12293 C C   . TYR D 268 ? 0.3516 0.3414 0.3024 -0.0065 -0.0113 0.0024  268 TYR D C   
12294 O O   . TYR D 268 ? 0.3338 0.3226 0.2875 -0.0100 -0.0091 0.0003  268 TYR D O   
12295 C CB  . TYR D 268 ? 0.3020 0.3065 0.2575 -0.0032 -0.0200 0.0004  268 TYR D CB  
12296 C CG  . TYR D 268 ? 0.3276 0.3333 0.2808 -0.0071 -0.0208 -0.0036 268 TYR D CG  
12297 C CD1 . TYR D 268 ? 0.3267 0.3344 0.2869 -0.0118 -0.0192 -0.0071 268 TYR D CD1 
12298 C CD2 . TYR D 268 ? 0.3550 0.3591 0.2980 -0.0057 -0.0229 -0.0039 268 TYR D CD2 
12299 C CE1 . TYR D 268 ? 0.3459 0.3534 0.3035 -0.0156 -0.0193 -0.0111 268 TYR D CE1 
12300 C CE2 . TYR D 268 ? 0.3698 0.3744 0.3098 -0.0094 -0.0236 -0.0082 268 TYR D CE2 
12301 C CZ  . TYR D 268 ? 0.3787 0.3850 0.3266 -0.0145 -0.0217 -0.0118 268 TYR D CZ  
12302 O OH  . TYR D 268 ? 0.3985 0.4038 0.3424 -0.0181 -0.0218 -0.0161 268 TYR D OH  
12303 N N   . PHE D 269 ? 0.3169 0.3010 0.2588 -0.0038 -0.0101 0.0052  269 PHE D N   
12304 C CA  . PHE D 269 ? 0.3105 0.2890 0.2450 -0.0051 -0.0073 0.0049  269 PHE D CA  
12305 C C   . PHE D 269 ? 0.3455 0.3157 0.2785 -0.0052 -0.0014 0.0076  269 PHE D C   
12306 O O   . PHE D 269 ? 0.3580 0.3236 0.2862 -0.0064 0.0019  0.0075  269 PHE D O   
12307 C CB  . PHE D 269 ? 0.3293 0.3074 0.2527 -0.0019 -0.0104 0.0054  269 PHE D CB  
12308 C CG  . PHE D 269 ? 0.3103 0.2831 0.2260 0.0035  -0.0096 0.0101  269 PHE D CG  
12309 C CD1 . PHE D 269 ? 0.3457 0.3081 0.2541 0.0045  -0.0037 0.0133  269 PHE D CD1 
12310 C CD2 . PHE D 269 ? 0.3541 0.3322 0.2693 0.0080  -0.0146 0.0112  269 PHE D CD2 
12311 C CE1 . PHE D 269 ? 0.3807 0.3363 0.2804 0.0098  -0.0021 0.0179  269 PHE D CE1 
12312 C CE2 . PHE D 269 ? 0.3624 0.3344 0.2691 0.0140  -0.0135 0.0160  269 PHE D CE2 
12313 C CZ  . PHE D 269 ? 0.3615 0.3217 0.2598 0.0149  -0.0072 0.0193  269 PHE D CZ  
12314 N N   . TRP D 270 ? 0.3311 0.2993 0.2681 -0.0041 0.0003  0.0099  270 TRP D N   
12315 C CA  . TRP D 270 ? 0.3295 0.2892 0.2635 -0.0036 0.0059  0.0127  270 TRP D CA  
12316 C C   . TRP D 270 ? 0.3532 0.3101 0.2885 -0.0069 0.0105  0.0114  270 TRP D C   
12317 O O   . TRP D 270 ? 0.3758 0.3258 0.3041 -0.0062 0.0148  0.0133  270 TRP D O   
12318 C CB  . TRP D 270 ? 0.3438 0.3025 0.2850 -0.0038 0.0073  0.0135  270 TRP D CB  
12319 C CG  . TRP D 270 ? 0.3511 0.3001 0.2881 -0.0025 0.0129  0.0167  270 TRP D CG  
12320 C CD1 . TRP D 270 ? 0.3284 0.2734 0.2711 -0.0056 0.0180  0.0161  270 TRP D CD1 
12321 C CD2 . TRP D 270 ? 0.3822 0.3245 0.3086 0.0023  0.0141  0.0207  270 TRP D CD2 
12322 N NE1 . TRP D 270 ? 0.3743 0.3094 0.3110 -0.0038 0.0232  0.0194  270 TRP D NE1 
12323 C CE2 . TRP D 270 ? 0.4249 0.3575 0.3507 0.0016  0.0211  0.0227  270 TRP D CE2 
12324 C CE3 . TRP D 270 ? 0.4118 0.3553 0.3289 0.0075  0.0099  0.0227  270 TRP D CE3 
12325 C CZ2 . TRP D 270 ? 0.4240 0.3463 0.3390 0.0061  0.0250  0.0273  270 TRP D CZ2 
12326 C CZ3 . TRP D 270 ? 0.4452 0.3794 0.3510 0.0128  0.0128  0.0273  270 TRP D CZ3 
12327 C CH2 . TRP D 270 ? 0.4529 0.3757 0.3572 0.0121  0.0207  0.0298  270 TRP D CH2 
12328 N N   . ASN D 271 ? 0.3139 0.2756 0.2580 -0.0101 0.0101  0.0084  271 ASN D N   
12329 C CA  . ASN D 271 ? 0.3062 0.2665 0.2535 -0.0126 0.0144  0.0072  271 ASN D CA  
12330 C C   . ASN D 271 ? 0.3381 0.3002 0.2825 -0.0135 0.0136  0.0051  271 ASN D C   
12331 O O   . ASN D 271 ? 0.3548 0.3214 0.3002 -0.0138 0.0096  0.0032  271 ASN D O   
12332 C CB  . ASN D 271 ? 0.3221 0.2858 0.2804 -0.0147 0.0150  0.0054  271 ASN D CB  
12333 C CG  . ASN D 271 ? 0.3139 0.2837 0.2767 -0.0149 0.0105  0.0032  271 ASN D CG  
12334 O OD1 . ASN D 271 ? 0.3111 0.2829 0.2722 -0.0136 0.0069  0.0035  271 ASN D OD1 
12335 N ND2 . ASN D 271 ? 0.3279 0.3007 0.2960 -0.0161 0.0111  0.0010  271 ASN D ND2 
12336 N N   . ALA D 272 ? 0.3225 0.2803 0.2628 -0.0139 0.0180  0.0055  272 ALA D N   
12337 C CA  . ALA D 272 ? 0.3712 0.3296 0.3096 -0.0149 0.0186  0.0032  272 ALA D CA  
12338 C C   . ALA D 272 ? 0.3269 0.2891 0.2757 -0.0165 0.0204  0.0015  272 ALA D C   
12339 O O   . ALA D 272 ? 0.3618 0.3256 0.3184 -0.0170 0.0220  0.0019  272 ALA D O   
12340 C CB  . ALA D 272 ? 0.4071 0.3587 0.3360 -0.0142 0.0231  0.0044  272 ALA D CB  
12341 N N   . SER D 273 ? 0.3160 0.2794 0.2647 -0.0169 0.0203  -0.0006 273 SER D N   
12342 C CA  . SER D 273 ? 0.2796 0.2466 0.2372 -0.0171 0.0218  -0.0019 273 SER D CA  
12343 C C   . SER D 273 ? 0.3256 0.2919 0.2873 -0.0171 0.0271  -0.0013 273 SER D C   
12344 O O   . SER D 273 ? 0.3641 0.3254 0.3203 -0.0172 0.0309  0.0002  273 SER D O   
12345 C CB  . SER D 273 ? 0.3118 0.2783 0.2671 -0.0169 0.0217  -0.0039 273 SER D CB  
12346 O OG  . SER D 273 ? 0.3466 0.3081 0.2952 -0.0168 0.0258  -0.0039 273 SER D OG  
12347 N N   . LYS D 274 ? 0.3128 0.2841 0.2840 -0.0169 0.0275  -0.0025 274 LYS D N   
12348 C CA  . LYS D 274 ? 0.2999 0.2728 0.2776 -0.0170 0.0325  -0.0027 274 LYS D CA  
12349 C C   . LYS D 274 ? 0.3499 0.3212 0.3248 -0.0156 0.0357  -0.0032 274 LYS D C   
12350 O O   . LYS D 274 ? 0.3548 0.3263 0.3272 -0.0142 0.0334  -0.0042 274 LYS D O   
12351 C CB  . LYS D 274 ? 0.3226 0.3036 0.3133 -0.0170 0.0308  -0.0045 274 LYS D CB  
12352 C CG  . LYS D 274 ? 0.3666 0.3486 0.3607 -0.0187 0.0282  -0.0045 274 LYS D CG  
12353 C CD  . LYS D 274 ? 0.4350 0.4121 0.4283 -0.0208 0.0332  -0.0030 274 LYS D CD  
12354 C CE  . LYS D 274 ? 0.5002 0.4760 0.4952 -0.0223 0.0315  -0.0027 274 LYS D CE  
12355 N NZ  . LYS D 274 ? 0.4889 0.4574 0.4802 -0.0236 0.0375  -0.0004 274 LYS D NZ  
12356 N N   . PRO D 275 ? 0.3597 0.3291 0.3355 -0.0157 0.0418  -0.0026 275 PRO D N   
12357 C CA  . PRO D 275 ? 0.3520 0.3200 0.3261 -0.0138 0.0457  -0.0032 275 PRO D CA  
12358 C C   . PRO D 275 ? 0.3591 0.3351 0.3434 -0.0116 0.0437  -0.0048 275 PRO D C   
12359 O O   . PRO D 275 ? 0.3336 0.3175 0.3295 -0.0118 0.0420  -0.0058 275 PRO D O   
12360 C CB  . PRO D 275 ? 0.3679 0.3338 0.3441 -0.0146 0.0531  -0.0022 275 PRO D CB  
12361 C CG  . PRO D 275 ? 0.3387 0.3091 0.3249 -0.0169 0.0528  -0.0021 275 PRO D CG  
12362 C CD  . PRO D 275 ? 0.3164 0.2854 0.2970 -0.0175 0.0461  -0.0017 275 PRO D CD  
12363 N N   . GLU D 276 ? 0.3379 0.3114 0.3171 -0.0093 0.0435  -0.0053 276 GLU D N   
12364 C CA  . GLU D 276 ? 0.3451 0.3242 0.3305 -0.0061 0.0408  -0.0063 276 GLU D CA  
12365 C C   . GLU D 276 ? 0.3614 0.3342 0.3387 -0.0035 0.0433  -0.0063 276 GLU D C   
12366 O O   . GLU D 276 ? 0.4131 0.3776 0.3792 -0.0054 0.0437  -0.0064 276 GLU D O   
12367 C CB  . GLU D 276 ? 0.3816 0.3630 0.3675 -0.0069 0.0344  -0.0066 276 GLU D CB  
12368 C CG  . GLU D 276 ? 0.3765 0.3595 0.3627 -0.0032 0.0317  -0.0071 276 GLU D CG  
12369 C CD  . GLU D 276 ? 0.4056 0.3973 0.4023 0.0006  0.0313  -0.0080 276 GLU D CD  
12370 O OE1 . GLU D 276 ? 0.4121 0.4114 0.4187 -0.0008 0.0301  -0.0090 276 GLU D OE1 
12371 O OE2 . GLU D 276 ? 0.4212 0.4124 0.4166 0.0053  0.0324  -0.0078 276 GLU D OE2 
12372 N N   . GLY D 277 ? 0.3268 0.3032 0.3096 0.0008  0.0453  -0.0065 277 GLY D N   
12373 C CA  . GLY D 277 ? 0.3403 0.3090 0.3149 0.0036  0.0492  -0.0064 277 GLY D CA  
12374 C C   . GLY D 277 ? 0.3607 0.3248 0.3289 0.0049  0.0464  -0.0065 277 GLY D C   
12375 O O   . GLY D 277 ? 0.4197 0.3744 0.3786 0.0054  0.0498  -0.0068 277 GLY D O   
12376 N N   . ASP D 278 ? 0.3153 0.2849 0.2882 0.0055  0.0411  -0.0066 278 ASP D N   
12377 C CA  . ASP D 278 ? 0.3435 0.3081 0.3103 0.0067  0.0393  -0.0065 278 ASP D CA  
12378 C C   . ASP D 278 ? 0.3466 0.3077 0.3083 0.0010  0.0367  -0.0072 278 ASP D C   
12379 O O   . ASP D 278 ? 0.3312 0.2977 0.2975 -0.0009 0.0324  -0.0072 278 ASP D O   
12380 C CB  . ASP D 278 ? 0.3625 0.3342 0.3356 0.0110  0.0351  -0.0061 278 ASP D CB  
12381 C CG  . ASP D 278 ? 0.3680 0.3330 0.3336 0.0129  0.0345  -0.0056 278 ASP D CG  
12382 O OD1 . ASP D 278 ? 0.3495 0.3073 0.3084 0.0087  0.0351  -0.0061 278 ASP D OD1 
12383 O OD2 . ASP D 278 ? 0.3680 0.3348 0.3345 0.0187  0.0334  -0.0048 278 ASP D OD2 
12384 N N   . VAL D 279 ? 0.3189 0.2710 0.2714 -0.0015 0.0393  -0.0081 279 VAL D N   
12385 C CA  . VAL D 279 ? 0.3401 0.2907 0.2887 -0.0067 0.0365  -0.0092 279 VAL D CA  
12386 C C   . VAL D 279 ? 0.3410 0.2943 0.2922 -0.0073 0.0322  -0.0092 279 VAL D C   
12387 O O   . VAL D 279 ? 0.3094 0.2661 0.2621 -0.0102 0.0286  -0.0094 279 VAL D O   
12388 C CB  . VAL D 279 ? 0.3819 0.3236 0.3209 -0.0096 0.0395  -0.0112 279 VAL D CB  
12389 C CG1 . VAL D 279 ? 0.3534 0.2877 0.2880 -0.0088 0.0423  -0.0123 279 VAL D CG1 
12390 C CG2 . VAL D 279 ? 0.3746 0.3171 0.3103 -0.0145 0.0357  -0.0127 279 VAL D CG2 
12391 N N   . ILE D 280 ? 0.2919 0.2428 0.2426 -0.0042 0.0331  -0.0088 280 ILE D N   
12392 C CA  . ILE D 280 ? 0.2987 0.2514 0.2512 -0.0046 0.0298  -0.0086 280 ILE D CA  
12393 C C   . ILE D 280 ? 0.3201 0.2818 0.2800 -0.0037 0.0252  -0.0077 280 ILE D C   
12394 O O   . ILE D 280 ? 0.3311 0.2953 0.2928 -0.0060 0.0219  -0.0078 280 ILE D O   
12395 C CB  . ILE D 280 ? 0.3311 0.2784 0.2804 -0.0003 0.0325  -0.0078 280 ILE D CB  
12396 C CG1 . ILE D 280 ? 0.3434 0.2802 0.2851 -0.0023 0.0377  -0.0091 280 ILE D CG1 
12397 C CG2 . ILE D 280 ? 0.3406 0.2897 0.2914 0.0006  0.0295  -0.0072 280 ILE D CG2 
12398 C CD1 . ILE D 280 ? 0.3621 0.2974 0.3027 -0.0087 0.0366  -0.0114 280 ILE D CD1 
12399 N N   . LYS D 281 ? 0.2934 0.2601 0.2584 -0.0004 0.0252  -0.0071 281 LYS D N   
12400 C CA  . LYS D 281 ? 0.3097 0.2848 0.2826 -0.0005 0.0212  -0.0071 281 LYS D CA  
12401 C C   . LYS D 281 ? 0.3272 0.3034 0.3011 -0.0052 0.0204  -0.0072 281 LYS D C   
12402 O O   . LYS D 281 ? 0.2853 0.2648 0.2623 -0.0067 0.0171  -0.0072 281 LYS D O   
12403 C CB  . LYS D 281 ? 0.3002 0.2816 0.2800 0.0034  0.0217  -0.0073 281 LYS D CB  
12404 C CG  . LYS D 281 ? 0.3317 0.3220 0.3209 0.0022  0.0182  -0.0083 281 LYS D CG  
12405 C CD  . LYS D 281 ? 0.3410 0.3394 0.3387 0.0062  0.0183  -0.0092 281 LYS D CD  
12406 C CE  . LYS D 281 ? 0.4404 0.4482 0.4486 0.0049  0.0148  -0.0113 281 LYS D CE  
12407 N NZ  . LYS D 281 ? 0.4172 0.4251 0.4294 -0.0005 0.0174  -0.0114 281 LYS D NZ  
12408 N N   . ALA D 282 ? 0.2988 0.2716 0.2691 -0.0070 0.0235  -0.0072 282 ALA D N   
12409 C CA  . ALA D 282 ? 0.2781 0.2510 0.2475 -0.0105 0.0231  -0.0069 282 ALA D CA  
12410 C C   . ALA D 282 ? 0.3117 0.2832 0.2775 -0.0128 0.0198  -0.0070 282 ALA D C   
12411 O O   . ALA D 282 ? 0.3284 0.3024 0.2963 -0.0141 0.0174  -0.0063 282 ALA D O   
12412 C CB  . ALA D 282 ? 0.2879 0.2556 0.2512 -0.0113 0.0274  -0.0069 282 ALA D CB  
12413 N N   . ILE D 283 ? 0.3044 0.2722 0.2657 -0.0131 0.0200  -0.0080 283 ILE D N   
12414 C CA  . ILE D 283 ? 0.2863 0.2541 0.2459 -0.0155 0.0171  -0.0087 283 ILE D CA  
12415 C C   . ILE D 283 ? 0.3117 0.2833 0.2764 -0.0143 0.0143  -0.0080 283 ILE D C   
12416 O O   . ILE D 283 ? 0.3302 0.3045 0.2966 -0.0155 0.0116  -0.0075 283 ILE D O   
12417 C CB  . ILE D 283 ? 0.2992 0.2620 0.2540 -0.0170 0.0190  -0.0106 283 ILE D CB  
12418 C CG1 . ILE D 283 ? 0.2827 0.2413 0.2310 -0.0188 0.0211  -0.0120 283 ILE D CG1 
12419 C CG2 . ILE D 283 ? 0.2996 0.2643 0.2553 -0.0196 0.0161  -0.0117 283 ILE D CG2 
12420 C CD1 . ILE D 283 ? 0.2833 0.2352 0.2273 -0.0201 0.0246  -0.0143 283 ILE D CD1 
12421 N N   . ALA D 284 ? 0.2894 0.2608 0.2559 -0.0115 0.0150  -0.0078 284 ALA D N   
12422 C CA  . ALA D 284 ? 0.2937 0.2675 0.2632 -0.0101 0.0125  -0.0074 284 ALA D CA  
12423 C C   . ALA D 284 ? 0.2893 0.2680 0.2638 -0.0103 0.0099  -0.0069 284 ALA D C   
12424 O O   . ALA D 284 ? 0.3257 0.3059 0.3017 -0.0110 0.0076  -0.0067 284 ALA D O   
12425 C CB  . ALA D 284 ? 0.2957 0.2677 0.2642 -0.0060 0.0136  -0.0072 284 ALA D CB  
12426 N N   . GLU D 285 ? 0.2876 0.2686 0.2652 -0.0098 0.0108  -0.0069 285 GLU D N   
12427 C CA  . GLU D 285 ? 0.3151 0.3001 0.2982 -0.0106 0.0092  -0.0070 285 GLU D CA  
12428 C C   . GLU D 285 ? 0.3138 0.2971 0.2951 -0.0133 0.0092  -0.0059 285 GLU D C   
12429 O O   . GLU D 285 ? 0.2855 0.2701 0.2698 -0.0139 0.0079  -0.0057 285 GLU D O   
12430 C CB  . GLU D 285 ? 0.2682 0.2570 0.2571 -0.0097 0.0108  -0.0078 285 GLU D CB  
12431 C CG  . GLU D 285 ? 0.3060 0.2973 0.2964 -0.0057 0.0097  -0.0087 285 GLU D CG  
12432 C CD  . GLU D 285 ? 0.3800 0.3781 0.3786 -0.0041 0.0098  -0.0102 285 GLU D CD  
12433 O OE1 . GLU D 285 ? 0.3822 0.3821 0.3854 -0.0065 0.0123  -0.0104 285 GLU D OE1 
12434 O OE2 . GLU D 285 ? 0.3470 0.3489 0.3476 -0.0001 0.0075  -0.0112 285 GLU D OE2 
12435 N N   . ARG D 286 ? 0.3165 0.2966 0.2922 -0.0145 0.0108  -0.0054 286 ARG D N   
12436 C CA  . ARG D 286 ? 0.2975 0.2760 0.2697 -0.0159 0.0101  -0.0042 286 ARG D CA  
12437 C C   . ARG D 286 ? 0.3532 0.3332 0.3266 -0.0157 0.0069  -0.0039 286 ARG D C   
12438 O O   . ARG D 286 ? 0.3280 0.3079 0.3020 -0.0157 0.0062  -0.0027 286 ARG D O   
12439 C CB  . ARG D 286 ? 0.3513 0.3267 0.3163 -0.0168 0.0109  -0.0044 286 ARG D CB  
12440 C CG  . ARG D 286 ? 0.3161 0.2902 0.2763 -0.0171 0.0098  -0.0030 286 ARG D CG  
12441 C CD  . ARG D 286 ? 0.2977 0.2741 0.2571 -0.0172 0.0059  -0.0035 286 ARG D CD  
12442 N NE  . ARG D 286 ? 0.3419 0.3179 0.2975 -0.0161 0.0043  -0.0016 286 ARG D NE  
12443 C CZ  . ARG D 286 ? 0.3151 0.2941 0.2705 -0.0153 0.0007  -0.0015 286 ARG D CZ  
12444 N NH1 . ARG D 286 ? 0.3164 0.2994 0.2759 -0.0163 -0.0013 -0.0035 286 ARG D NH1 
12445 N NH2 . ARG D 286 ? 0.2822 0.2601 0.2337 -0.0132 -0.0003 0.0008  286 ARG D NH2 
12446 N N   . TYR D 287 ? 0.3071 0.2878 0.2806 -0.0154 0.0057  -0.0049 287 TYR D N   
12447 C CA  . TYR D 287 ? 0.2514 0.2335 0.2263 -0.0151 0.0034  -0.0047 287 TYR D CA  
12448 C C   . TYR D 287 ? 0.2789 0.2619 0.2578 -0.0137 0.0026  -0.0045 287 TYR D C   
12449 O O   . TYR D 287 ? 0.3040 0.2874 0.2840 -0.0134 0.0013  -0.0037 287 TYR D O   
12450 C CB  . TYR D 287 ? 0.2692 0.2511 0.2433 -0.0156 0.0036  -0.0059 287 TYR D CB  
12451 C CG  . TYR D 287 ? 0.2963 0.2779 0.2669 -0.0176 0.0036  -0.0070 287 TYR D CG  
12452 C CD1 . TYR D 287 ? 0.3079 0.2927 0.2786 -0.0183 0.0010  -0.0070 287 TYR D CD1 
12453 C CD2 . TYR D 287 ? 0.3383 0.3170 0.3056 -0.0186 0.0059  -0.0082 287 TYR D CD2 
12454 C CE1 . TYR D 287 ? 0.3107 0.2963 0.2780 -0.0201 0.0000  -0.0086 287 TYR D CE1 
12455 C CE2 . TYR D 287 ? 0.3511 0.3292 0.3145 -0.0207 0.0056  -0.0098 287 TYR D CE2 
12456 C CZ  . TYR D 287 ? 0.3062 0.2881 0.2697 -0.0216 0.0024  -0.0103 287 TYR D CZ  
12457 O OH  . TYR D 287 ? 0.3004 0.2828 0.2598 -0.0236 0.0012  -0.0126 287 TYR D OH  
12458 N N   . CYS D 288 ? 0.2742 0.2577 0.2551 -0.0127 0.0033  -0.0055 288 CYS D N   
12459 C CA  . CYS D 288 ? 0.3253 0.3102 0.3098 -0.0116 0.0018  -0.0062 288 CYS D CA  
12460 C C   . CYS D 288 ? 0.3054 0.2903 0.2926 -0.0132 0.0022  -0.0058 288 CYS D C   
12461 O O   . CYS D 288 ? 0.3104 0.2950 0.2995 -0.0131 0.0012  -0.0063 288 CYS D O   
12462 C CB  . CYS D 288 ? 0.3140 0.3010 0.3006 -0.0096 0.0016  -0.0077 288 CYS D CB  
12463 S SG  . CYS D 288 ? 0.3228 0.3071 0.3044 -0.0067 0.0020  -0.0076 288 CYS D SG  
12464 N N   . ASP D 289 ? 0.2781 0.2625 0.2651 -0.0145 0.0044  -0.0052 289 ASP D N   
12465 C CA  . ASP D 289 ? 0.2637 0.2467 0.2529 -0.0161 0.0063  -0.0047 289 ASP D CA  
12466 C C   . ASP D 289 ? 0.3139 0.2929 0.2984 -0.0161 0.0067  -0.0023 289 ASP D C   
12467 O O   . ASP D 289 ? 0.3149 0.2907 0.2999 -0.0169 0.0089  -0.0014 289 ASP D O   
12468 C CB  . ASP D 289 ? 0.3494 0.3327 0.3401 -0.0171 0.0096  -0.0049 289 ASP D CB  
12469 C CG  . ASP D 289 ? 0.3256 0.3141 0.3229 -0.0166 0.0093  -0.0074 289 ASP D CG  
12470 O OD1 . ASP D 289 ? 0.3615 0.3531 0.3622 -0.0156 0.0064  -0.0092 289 ASP D OD1 
12471 O OD2 . ASP D 289 ? 0.3208 0.3107 0.3200 -0.0167 0.0120  -0.0076 289 ASP D OD2 
12472 N N   . ARG D 290 ? 0.3017 0.2809 0.2819 -0.0150 0.0048  -0.0013 290 ARG D N   
12473 C CA  . ARG D 290 ? 0.3267 0.3038 0.3023 -0.0139 0.0042  0.0009  290 ARG D CA  
12474 C C   . ARG D 290 ? 0.2991 0.2746 0.2765 -0.0130 0.0038  0.0017  290 ARG D C   
12475 O O   . ARG D 290 ? 0.2886 0.2654 0.2699 -0.0130 0.0028  0.0000  290 ARG D O   
12476 C CB  . ARG D 290 ? 0.2921 0.2721 0.2655 -0.0133 0.0015  0.0005  290 ARG D CB  
12477 C CG  . ARG D 290 ? 0.3308 0.3108 0.2994 -0.0118 -0.0001 0.0023  290 ARG D CG  
12478 C CD  . ARG D 290 ? 0.3105 0.2956 0.2808 -0.0115 -0.0032 0.0011  290 ARG D CD  
12479 N NE  . ARG D 290 ? 0.3082 0.2945 0.2826 -0.0100 -0.0039 0.0017  290 ARG D NE  
12480 C CZ  . ARG D 290 ? 0.2826 0.2734 0.2601 -0.0095 -0.0058 0.0009  290 ARG D CZ  
12481 N NH1 . ARG D 290 ? 0.3163 0.3112 0.2940 -0.0110 -0.0072 -0.0010 290 ARG D NH1 
12482 N NH2 . ARG D 290 ? 0.2984 0.2896 0.2791 -0.0077 -0.0058 0.0017  290 ARG D NH2 
12483 N N   . PRO D 291 ? 0.3193 0.2908 0.2929 -0.0116 0.0048  0.0041  291 PRO D N   
12484 C CA  . PRO D 291 ? 0.3024 0.2717 0.2771 -0.0101 0.0047  0.0050  291 PRO D CA  
12485 C C   . PRO D 291 ? 0.3232 0.2970 0.3003 -0.0090 0.0016  0.0039  291 PRO D C   
12486 O O   . PRO D 291 ? 0.3171 0.2951 0.2934 -0.0083 -0.0005 0.0040  291 PRO D O   
12487 C CB  . PRO D 291 ? 0.3250 0.2901 0.2933 -0.0073 0.0056  0.0085  291 PRO D CB  
12488 C CG  . PRO D 291 ? 0.3772 0.3413 0.3405 -0.0077 0.0067  0.0093  291 PRO D CG  
12489 C CD  . PRO D 291 ? 0.3452 0.3130 0.3123 -0.0107 0.0067  0.0065  291 PRO D CD  
12490 N N   . ALA D 292 ? 0.2843 0.2571 0.2645 -0.0089 0.0017  0.0027  292 ALA D N   
12491 C CA  . ALA D 292 ? 0.2904 0.2664 0.2727 -0.0081 -0.0001 0.0013  292 ALA D CA  
12492 C C   . ALA D 292 ? 0.3061 0.2830 0.2881 -0.0054 -0.0009 0.0031  292 ALA D C   
12493 O O   . ALA D 292 ? 0.3319 0.3052 0.3124 -0.0035 0.0002  0.0049  292 ALA D O   
12494 C CB  . ALA D 292 ? 0.3099 0.2839 0.2942 -0.0088 0.0003  -0.0010 292 ALA D CB  
12495 N N   . CYS D 293 ? 0.3064 0.2880 0.2903 -0.0050 -0.0022 0.0024  293 CYS D N   
12496 C CA  . CYS D 293 ? 0.2942 0.2778 0.2803 -0.0027 -0.0024 0.0030  293 CYS D CA  
12497 C C   . CYS D 293 ? 0.3064 0.2848 0.2921 -0.0016 -0.0008 0.0026  293 CYS D C   
12498 O O   . CYS D 293 ? 0.2874 0.2632 0.2723 -0.0031 -0.0004 0.0007  293 CYS D O   
12499 C CB  . CYS D 293 ? 0.3145 0.3026 0.3037 -0.0038 -0.0025 0.0014  293 CYS D CB  
12500 S SG  . CYS D 293 ? 0.3624 0.3547 0.3565 -0.0014 -0.0018 0.0018  293 CYS D SG  
12501 N N   . PRO D 294 ? 0.3263 0.3033 0.3123 0.0013  0.0000  0.0042  294 PRO D N   
12502 C CA  . PRO D 294 ? 0.2975 0.2690 0.2825 0.0023  0.0018  0.0033  294 PRO D CA  
12503 C C   . PRO D 294 ? 0.2754 0.2470 0.2603 0.0014  0.0021  0.0008  294 PRO D C   
12504 O O   . PRO D 294 ? 0.3115 0.2783 0.2937 0.0011  0.0025  -0.0011 294 PRO D O   
12505 C CB  . PRO D 294 ? 0.3205 0.2927 0.3069 0.0061  0.0028  0.0055  294 PRO D CB  
12506 C CG  . PRO D 294 ? 0.3153 0.2901 0.3014 0.0074  0.0014  0.0080  294 PRO D CG  
12507 C CD  . PRO D 294 ? 0.2955 0.2757 0.2825 0.0043  -0.0008 0.0068  294 PRO D CD  
12508 N N   . THR D 295 ? 0.2593 0.2357 0.2464 0.0012  0.0020  0.0008  295 THR D N   
12509 C CA  . THR D 295 ? 0.3213 0.2964 0.3069 0.0011  0.0031  -0.0009 295 THR D CA  
12510 C C   . THR D 295 ? 0.2769 0.2501 0.2594 -0.0004 0.0018  -0.0027 295 THR D C   
12511 O O   . THR D 295 ? 0.2919 0.2616 0.2707 0.0007  0.0022  -0.0042 295 THR D O   
12512 C CB  . THR D 295 ? 0.3191 0.2993 0.3084 0.0003  0.0041  -0.0007 295 THR D CB  
12513 O OG1 . THR D 295 ? 0.3953 0.3786 0.3890 0.0021  0.0055  0.0004  295 THR D OG1 
12514 C CG2 . THR D 295 ? 0.3245 0.3019 0.3109 0.0000  0.0063  -0.0020 295 THR D CG2 
12515 N N   . LYS D 296 ? 0.2819 0.2572 0.2655 -0.0025 0.0004  -0.0026 296 LYS D N   
12516 C CA  . LYS D 296 ? 0.2816 0.2566 0.2639 -0.0038 -0.0007 -0.0043 296 LYS D CA  
12517 C C   . LYS D 296 ? 0.2776 0.2504 0.2603 -0.0048 -0.0014 -0.0055 296 LYS D C   
12518 O O   . LYS D 296 ? 0.2829 0.2570 0.2665 -0.0063 -0.0023 -0.0071 296 LYS D O   
12519 C CB  . LYS D 296 ? 0.2599 0.2384 0.2433 -0.0057 -0.0010 -0.0038 296 LYS D CB  
12520 C CG  . LYS D 296 ? 0.2696 0.2498 0.2531 -0.0056 0.0001  -0.0035 296 LYS D CG  
12521 C CD  . LYS D 296 ? 0.2534 0.2353 0.2367 -0.0075 0.0001  -0.0039 296 LYS D CD  
12522 C CE  . LYS D 296 ? 0.3116 0.2946 0.2955 -0.0084 0.0018  -0.0042 296 LYS D CE  
12523 N NZ  . LYS D 296 ? 0.2612 0.2402 0.2423 -0.0068 0.0044  -0.0048 296 LYS D NZ  
12524 N N   . ASP D 297 ? 0.3037 0.2730 0.2860 -0.0040 -0.0006 -0.0051 297 ASP D N   
12525 C CA  . ASP D 297 ? 0.3025 0.2684 0.2854 -0.0057 -0.0002 -0.0063 297 ASP D CA  
12526 C C   . ASP D 297 ? 0.3411 0.3030 0.3221 -0.0051 -0.0005 -0.0093 297 ASP D C   
12527 O O   . ASP D 297 ? 0.3408 0.2977 0.3200 -0.0039 0.0012  -0.0089 297 ASP D O   
12528 C CB  . ASP D 297 ? 0.3112 0.2746 0.2941 -0.0053 0.0017  -0.0034 297 ASP D CB  
12529 C CG  . ASP D 297 ? 0.3319 0.2921 0.3159 -0.0079 0.0032  -0.0040 297 ASP D CG  
12530 O OD1 . ASP D 297 ? 0.3229 0.2858 0.3095 -0.0105 0.0026  -0.0061 297 ASP D OD1 
12531 O OD2 . ASP D 297 ? 0.3219 0.2763 0.3043 -0.0072 0.0057  -0.0024 297 ASP D OD2 
12532 N N   . TYR D 298 ? 0.3028 0.2668 0.2834 -0.0054 -0.0027 -0.0125 298 TYR D N   
12533 C CA  . TYR D 298 ? 0.2834 0.2446 0.2615 -0.0049 -0.0041 -0.0163 298 TYR D CA  
12534 C C   . TYR D 298 ? 0.2751 0.2415 0.2553 -0.0058 -0.0074 -0.0197 298 TYR D C   
12535 O O   . TYR D 298 ? 0.2676 0.2386 0.2491 -0.0054 -0.0079 -0.0183 298 TYR D O   
12536 C CB  . TYR D 298 ? 0.2729 0.2309 0.2450 -0.0011 -0.0036 -0.0156 298 TYR D CB  
12537 C CG  . TYR D 298 ? 0.2579 0.2188 0.2277 0.0011  -0.0042 -0.0144 298 TYR D CG  
12538 C CD1 . TYR D 298 ? 0.2890 0.2508 0.2551 0.0029  -0.0068 -0.0170 298 TYR D CD1 
12539 C CD2 . TYR D 298 ? 0.2854 0.2479 0.2566 0.0015  -0.0020 -0.0109 298 TYR D CD2 
12540 C CE1 . TYR D 298 ? 0.2851 0.2477 0.2478 0.0055  -0.0062 -0.0154 298 TYR D CE1 
12541 C CE2 . TYR D 298 ? 0.2726 0.2362 0.2415 0.0032  -0.0013 -0.0099 298 TYR D CE2 
12542 C CZ  . TYR D 298 ? 0.2759 0.2388 0.2402 0.0052  -0.0031 -0.0119 298 TYR D CZ  
12543 O OH  . TYR D 298 ? 0.2878 0.2498 0.2485 0.0074  -0.0014 -0.0105 298 TYR D OH  
12544 N N   . PRO D 299 ? 0.2942 0.2604 0.2748 -0.0068 -0.0096 -0.0246 299 PRO D N   
12545 C CA  . PRO D 299 ? 0.3002 0.2600 0.2786 -0.0078 -0.0088 -0.0272 299 PRO D CA  
12546 C C   . PRO D 299 ? 0.3241 0.2799 0.3067 -0.0114 -0.0051 -0.0261 299 PRO D C   
12547 O O   . PRO D 299 ? 0.3139 0.2623 0.2936 -0.0113 -0.0026 -0.0261 299 PRO D O   
12548 C CB  . PRO D 299 ? 0.3057 0.2690 0.2853 -0.0088 -0.0131 -0.0336 299 PRO D CB  
12549 C CG  . PRO D 299 ? 0.3022 0.2744 0.2884 -0.0099 -0.0150 -0.0339 299 PRO D CG  
12550 C CD  . PRO D 299 ? 0.3099 0.2827 0.2929 -0.0068 -0.0136 -0.0284 299 PRO D CD  
12551 N N   . ALA D 300 ? 0.3228 0.2825 0.3116 -0.0142 -0.0041 -0.0251 300 ALA D N   
12552 C CA  . ALA D 300 ? 0.2871 0.2418 0.2790 -0.0175 0.0001  -0.0242 300 ALA D CA  
12553 C C   . ALA D 300 ? 0.3338 0.2851 0.3223 -0.0151 0.0031  -0.0180 300 ALA D C   
12554 O O   . ALA D 300 ? 0.3108 0.2668 0.2985 -0.0129 0.0018  -0.0149 300 ALA D O   
12555 C CB  . ALA D 300 ? 0.3564 0.3160 0.3561 -0.0217 0.0006  -0.0264 300 ALA D CB  
12556 N N   . HIS D 301 ? 0.3161 0.2593 0.3027 -0.0152 0.0070  -0.0163 301 HIS D N   
12557 C CA  . HIS D 301 ? 0.2829 0.2237 0.2665 -0.0122 0.0093  -0.0105 301 HIS D CA  
12558 C C   . HIS D 301 ? 0.3144 0.2555 0.3002 -0.0144 0.0116  -0.0085 301 HIS D C   
12559 O O   . HIS D 301 ? 0.3224 0.2559 0.3065 -0.0149 0.0160  -0.0066 301 HIS D O   
12560 C CB  . HIS D 301 ? 0.3125 0.2437 0.2920 -0.0101 0.0129  -0.0088 301 HIS D CB  
12561 C CG  . HIS D 301 ? 0.3799 0.3100 0.3561 -0.0065 0.0118  -0.0090 301 HIS D CG  
12562 N ND1 . HIS D 301 ? 0.3861 0.3211 0.3613 -0.0026 0.0104  -0.0057 301 HIS D ND1 
12563 C CD2 . HIS D 301 ? 0.3847 0.3085 0.3581 -0.0064 0.0128  -0.0121 301 HIS D CD2 
12564 C CE1 . HIS D 301 ? 0.4021 0.3340 0.3744 0.0000  0.0109  -0.0064 301 HIS D CE1 
12565 N NE2 . HIS D 301 ? 0.3510 0.2756 0.3214 -0.0020 0.0123  -0.0102 301 HIS D NE2 
12566 N N   . THR D 302 ? 0.3149 0.2637 0.3037 -0.0155 0.0093  -0.0089 302 THR D N   
12567 C CA  . THR D 302 ? 0.3276 0.2761 0.3177 -0.0174 0.0121  -0.0071 302 THR D CA  
12568 C C   . THR D 302 ? 0.3262 0.2705 0.3105 -0.0141 0.0142  -0.0016 302 THR D C   
12569 O O   . THR D 302 ? 0.3413 0.2807 0.3238 -0.0149 0.0181  0.0005  302 THR D O   
12570 C CB  . THR D 302 ? 0.3351 0.2922 0.3284 -0.0184 0.0095  -0.0081 302 THR D CB  
12571 O OG1 . THR D 302 ? 0.3441 0.3045 0.3337 -0.0151 0.0072  -0.0051 302 THR D OG1 
12572 C CG2 . THR D 302 ? 0.3450 0.3078 0.3431 -0.0198 0.0062  -0.0131 302 THR D CG2 
12573 N N   . ARG D 303 ? 0.3157 0.2617 0.2968 -0.0102 0.0118  0.0006  303 ARG D N   
12574 C CA  . ARG D 303 ? 0.3215 0.2656 0.2977 -0.0061 0.0125  0.0054  303 ARG D CA  
12575 C C   . ARG D 303 ? 0.3405 0.2740 0.3126 -0.0049 0.0174  0.0077  303 ARG D C   
12576 O O   . ARG D 303 ? 0.3599 0.2898 0.3269 -0.0024 0.0193  0.0116  303 ARG D O   
12577 C CB  . ARG D 303 ? 0.3264 0.2751 0.3023 -0.0025 0.0094  0.0063  303 ARG D CB  
12578 C CG  . ARG D 303 ? 0.3623 0.3116 0.3345 0.0024  0.0090  0.0107  303 ARG D CG  
12579 C CD  . ARG D 303 ? 0.3429 0.3000 0.3179 0.0049  0.0057  0.0107  303 ARG D CD  
12580 N NE  . ARG D 303 ? 0.3775 0.3364 0.3501 0.0097  0.0048  0.0143  303 ARG D NE  
12581 C CZ  . ARG D 303 ? 0.3716 0.3301 0.3445 0.0142  0.0053  0.0161  303 ARG D CZ  
12582 N NH1 . ARG D 303 ? 0.3257 0.2818 0.3010 0.0141  0.0068  0.0146  303 ARG D NH1 
12583 N NH2 . ARG D 303 ? 0.3328 0.2937 0.3035 0.0192  0.0040  0.0195  303 ARG D NH2 
12584 N N   . PHE D 304 ? 0.3235 0.2509 0.2968 -0.0064 0.0197  0.0053  304 PHE D N   
12585 C CA  . PHE D 304 ? 0.3206 0.2361 0.2893 -0.0050 0.0252  0.0075  304 PHE D CA  
12586 C C   . PHE D 304 ? 0.3595 0.2694 0.3269 -0.0076 0.0299  0.0087  304 PHE D C   
12587 O O   . PHE D 304 ? 0.4113 0.3125 0.3719 -0.0042 0.0341  0.0133  304 PHE D O   
12588 C CB  . PHE D 304 ? 0.3587 0.2678 0.3292 -0.0074 0.0273  0.0036  304 PHE D CB  
12589 C CG  . PHE D 304 ? 0.3844 0.2958 0.3541 -0.0040 0.0244  0.0031  304 PHE D CG  
12590 C CD1 . PHE D 304 ? 0.3972 0.3173 0.3669 0.0000  0.0202  0.0056  304 PHE D CD1 
12591 C CD2 . PHE D 304 ? 0.4081 0.3124 0.3773 -0.0052 0.0263  -0.0003 304 PHE D CD2 
12592 C CE1 . PHE D 304 ? 0.4296 0.3517 0.3994 0.0029  0.0185  0.0050  304 PHE D CE1 
12593 C CE2 . PHE D 304 ? 0.4193 0.3248 0.3870 -0.0018 0.0244  -0.0007 304 PHE D CE2 
12594 C CZ  . PHE D 304 ? 0.4290 0.3433 0.3972 0.0024  0.0209  0.0023  304 PHE D CZ  
12595 N N   . ASP D 305 ? 0.3655 0.2798 0.3392 -0.0132 0.0298  0.0048  305 ASP D N   
12596 C CA  . ASP D 305 ? 0.4003 0.3096 0.3740 -0.0162 0.0353  0.0055  305 ASP D CA  
12597 C C   . ASP D 305 ? 0.3731 0.2847 0.3410 -0.0127 0.0345  0.0102  305 ASP D C   
12598 O O   . ASP D 305 ? 0.3716 0.2749 0.3339 -0.0119 0.0400  0.0135  305 ASP D O   
12599 C CB  . ASP D 305 ? 0.4423 0.3579 0.4261 -0.0228 0.0349  -0.0003 305 ASP D CB  
12600 C CG  . ASP D 305 ? 0.5555 0.4698 0.5454 -0.0269 0.0351  -0.0061 305 ASP D CG  
12601 O OD1 . ASP D 305 ? 0.5036 0.4069 0.4908 -0.0274 0.0400  -0.0060 305 ASP D OD1 
12602 O OD2 . ASP D 305 ? 0.5950 0.5193 0.5918 -0.0291 0.0300  -0.0110 305 ASP D OD2 
12603 N N   . HIS D 306 ? 0.3592 0.2815 0.3282 -0.0111 0.0282  0.0100  306 HIS D N   
12604 C CA  . HIS D 306 ? 0.3650 0.2903 0.3282 -0.0078 0.0264  0.0135  306 HIS D CA  
12605 C C   . HIS D 306 ? 0.3811 0.2998 0.3348 -0.0016 0.0275  0.0187  306 HIS D C   
12606 O O   . HIS D 306 ? 0.3685 0.2819 0.3144 0.0008  0.0303  0.0223  306 HIS D O   
12607 C CB  . HIS D 306 ? 0.3029 0.2400 0.2694 -0.0075 0.0197  0.0117  306 HIS D CB  
12608 C CG  . HIS D 306 ? 0.3278 0.2684 0.2885 -0.0044 0.0172  0.0144  306 HIS D CG  
12609 N ND1 . HIS D 306 ? 0.3721 0.3109 0.3290 -0.0053 0.0195  0.0155  306 HIS D ND1 
12610 C CD2 . HIS D 306 ? 0.3294 0.2754 0.2875 -0.0005 0.0127  0.0159  306 HIS D CD2 
12611 C CE1 . HIS D 306 ? 0.3355 0.2781 0.2868 -0.0021 0.0160  0.0172  306 HIS D CE1 
12612 N NE2 . HIS D 306 ? 0.3523 0.3001 0.3051 0.0006  0.0116  0.0172  306 HIS D NE2 
12613 N N   . VAL D 307 ? 0.3621 0.2806 0.3156 0.0017  0.0256  0.0194  307 VAL D N   
12614 C CA  . VAL D 307 ? 0.3935 0.3075 0.3387 0.0088  0.0259  0.0244  307 VAL D CA  
12615 C C   . VAL D 307 ? 0.4059 0.3046 0.3440 0.0101  0.0337  0.0276  307 VAL D C   
12616 O O   . VAL D 307 ? 0.4101 0.3032 0.3384 0.0151  0.0356  0.0324  307 VAL D O   
12617 C CB  . VAL D 307 ? 0.3539 0.2720 0.3020 0.0122  0.0225  0.0242  307 VAL D CB  
12618 C CG1 . VAL D 307 ? 0.3819 0.2951 0.3221 0.0204  0.0233  0.0296  307 VAL D CG1 
12619 C CG2 . VAL D 307 ? 0.3746 0.3068 0.3289 0.0114  0.0158  0.0217  307 VAL D CG2 
12620 N N   . LEU D 308 ? 0.3768 0.2681 0.3190 0.0054  0.0387  0.0248  308 LEU D N   
12621 C CA  . LEU D 308 ? 0.3870 0.2623 0.3228 0.0058  0.0475  0.0275  308 LEU D CA  
12622 C C   . LEU D 308 ? 0.4277 0.2992 0.3597 0.0040  0.0517  0.0291  308 LEU D C   
12623 O O   . LEU D 308 ? 0.4285 0.2881 0.3496 0.0084  0.0573  0.0342  308 LEU D O   
12624 C CB  . LEU D 308 ? 0.4018 0.2707 0.3444 -0.0002 0.0519  0.0228  308 LEU D CB  
12625 C CG  . LEU D 308 ? 0.4456 0.2963 0.3818 -0.0004 0.0623  0.0253  308 LEU D CG  
12626 C CD1 . LEU D 308 ? 0.4536 0.2948 0.3777 0.0090  0.0642  0.0320  308 LEU D CD1 
12627 C CD2 . LEU D 308 ? 0.4716 0.3165 0.4154 -0.0076 0.0667  0.0194  308 LEU D CD2 
12628 N N   . GLY D 309 ? 0.4277 0.3087 0.3673 -0.0015 0.0492  0.0252  309 GLY D N   
12629 C CA  . GLY D 309 ? 0.4204 0.2982 0.3569 -0.0032 0.0536  0.0265  309 GLY D CA  
12630 C C   . GLY D 309 ? 0.4548 0.3317 0.3787 0.0038  0.0517  0.0320  309 GLY D C   
12631 O O   . GLY D 309 ? 0.4586 0.3243 0.3728 0.0060  0.0582  0.0359  309 GLY D O   
12632 N N   . MET D 310 ? 0.4299 0.3183 0.3535 0.0075  0.0429  0.0320  310 MET D N   
12633 C CA  . MET D 310 ? 0.4648 0.3536 0.3767 0.0145  0.0399  0.0365  310 MET D CA  
12634 C C   . MET D 310 ? 0.4785 0.3552 0.3788 0.0220  0.0437  0.0421  310 MET D C   
12635 O O   . MET D 310 ? 0.4501 0.3193 0.3373 0.0274  0.0460  0.0467  310 MET D O   
12636 C CB  . MET D 310 ? 0.4477 0.3516 0.3634 0.0164  0.0301  0.0346  310 MET D CB  
12637 C CG  . MET D 310 ? 0.4616 0.3747 0.3820 0.0116  0.0270  0.0310  310 MET D CG  
12638 S SD  . MET D 310 ? 0.4375 0.3664 0.3617 0.0132  0.0169  0.0287  310 MET D SD  
12639 C CE  . MET D 310 ? 0.4089 0.3410 0.3421 0.0135  0.0152  0.0274  310 MET D CE  
12640 N N   . ALA D 311 ? 0.4087 0.2822 0.3125 0.0231  0.0446  0.0421  311 ALA D N   
12641 C CA  . ALA D 311 ? 0.4583 0.3197 0.3510 0.0310  0.0484  0.0478  311 ALA D CA  
12642 C C   . ALA D 311 ? 0.4721 0.3155 0.3556 0.0307  0.0592  0.0510  311 ALA D C   
12643 O O   . ALA D 311 ? 0.4770 0.3103 0.3459 0.0387  0.0621  0.0570  311 ALA D O   
12644 C CB  . ALA D 311 ? 0.4613 0.3212 0.3600 0.0313  0.0488  0.0466  311 ALA D CB  
12645 N N   . LYS D 312 ? 0.4703 0.3092 0.3621 0.0218  0.0654  0.0471  312 LYS D N   
12646 C CA  . LYS D 312 ? 0.5001 0.3215 0.3850 0.0203  0.0770  0.0496  312 LYS D CA  
12647 C C   . LYS D 312 ? 0.4944 0.3140 0.3702 0.0220  0.0787  0.0524  312 LYS D C   
12648 O O   . LYS D 312 ? 0.5193 0.3233 0.3807 0.0270  0.0864  0.0580  312 LYS D O   
12649 C CB  . LYS D 312 ? 0.5093 0.3286 0.4079 0.0098  0.0826  0.0436  312 LYS D CB  
12650 C CG  . LYS D 312 ? 0.5244 0.3412 0.4286 0.0088  0.0826  0.0412  312 LYS D CG  
12651 C CD  . LYS D 312 ? 0.6465 0.4417 0.5397 0.0127  0.0932  0.0459  312 LYS D CD  
12652 C CE  . LYS D 312 ? 0.6047 0.3945 0.5057 0.0082  0.0961  0.0415  312 LYS D CE  
12653 N NZ  . LYS D 312 ? 0.6653 0.4386 0.5547 0.0158  0.1018  0.0468  312 LYS D NZ  
12654 N N   . GLU D 313 ? 0.4914 0.3261 0.3740 0.0186  0.0717  0.0488  313 GLU D N   
12655 C CA  . GLU D 313 ? 0.5276 0.3614 0.4025 0.0193  0.0732  0.0504  313 GLU D CA  
12656 C C   . GLU D 313 ? 0.5018 0.3319 0.3587 0.0298  0.0700  0.0564  313 GLU D C   
12657 O O   . GLU D 313 ? 0.5703 0.3899 0.4139 0.0330  0.0756  0.0603  313 GLU D O   
12658 C CB  . GLU D 313 ? 0.4839 0.3347 0.3705 0.0134  0.0662  0.0448  313 GLU D CB  
12659 C CG  . GLU D 313 ? 0.5810 0.4323 0.4606 0.0137  0.0671  0.0457  313 GLU D CG  
12660 C CD  . GLU D 313 ? 0.6468 0.5145 0.5377 0.0086  0.0600  0.0402  313 GLU D CD  
12661 O OE1 . GLU D 313 ? 0.6551 0.5343 0.5588 0.0053  0.0539  0.0360  313 GLU D OE1 
12662 O OE2 . GLU D 313 ? 0.7010 0.5691 0.5867 0.0085  0.0610  0.0404  313 GLU D OE2 
12663 N N   . TYR D 314 ? 0.4994 0.3378 0.3555 0.0357  0.0614  0.0572  314 TYR D N   
12664 C CA  . TYR D 314 ? 0.5078 0.3459 0.3485 0.0463  0.0566  0.0621  314 TYR D CA  
12665 C C   . TYR D 314 ? 0.5457 0.3699 0.3752 0.0549  0.0612  0.0682  314 TYR D C   
12666 O O   . TYR D 314 ? 0.5396 0.3651 0.3573 0.0650  0.0560  0.0723  314 TYR D O   
12667 C CB  . TYR D 314 ? 0.4612 0.3194 0.3089 0.0475  0.0437  0.0588  314 TYR D CB  
12668 C CG  . TYR D 314 ? 0.4814 0.3503 0.3344 0.0415  0.0396  0.0542  314 TYR D CG  
12669 C CD1 . TYR D 314 ? 0.4635 0.3383 0.3320 0.0316  0.0409  0.0488  314 TYR D CD1 
12670 C CD2 . TYR D 314 ? 0.4552 0.3278 0.2970 0.0461  0.0346  0.0552  314 TYR D CD2 
12671 C CE1 . TYR D 314 ? 0.4905 0.3747 0.3633 0.0267  0.0374  0.0448  314 TYR D CE1 
12672 C CE2 . TYR D 314 ? 0.4796 0.3600 0.3248 0.0409  0.0318  0.0511  314 TYR D CE2 
12673 C CZ  . TYR D 314 ? 0.4823 0.3684 0.3430 0.0314  0.0333  0.0462  314 TYR D CZ  
12674 O OH  . TYR D 314 ? 0.4977 0.3908 0.3598 0.0277  0.0306  0.0427  314 TYR D OH  
12675 N N   A ASN D 315 ? 0.5168 0.3275 0.3495 0.0513  0.0709  0.0686  315 ASN D N   
12676 N N   B ASN D 315 ? 0.5172 0.3280 0.3499 0.0513  0.0709  0.0686  315 ASN D N   
12677 C CA  A ASN D 315 ? 0.5550 0.3480 0.3754 0.0590  0.0782  0.0748  315 ASN D CA  
12678 C CA  B ASN D 315 ? 0.5550 0.3482 0.3753 0.0592  0.0780  0.0748  315 ASN D CA  
12679 C C   A ASN D 315 ? 0.5687 0.3699 0.3879 0.0680  0.0698  0.0769  315 ASN D C   
12680 C C   B ASN D 315 ? 0.5683 0.3699 0.3875 0.0681  0.0695  0.0768  315 ASN D C   
12681 O O   A ASN D 315 ? 0.5553 0.3494 0.3591 0.0795  0.0696  0.0832  315 ASN D O   
12682 O O   B ASN D 315 ? 0.5550 0.3504 0.3589 0.0795  0.0688  0.0830  315 ASN D O   
12683 C CB  A ASN D 315 ? 0.5947 0.3705 0.3944 0.0657  0.0859  0.0814  315 ASN D CB  
12684 C CB  B ASN D 315 ? 0.5940 0.3707 0.3936 0.0660  0.0853  0.0814  315 ASN D CB  
12685 C CG  A ASN D 315 ? 0.6141 0.3736 0.4144 0.0577  0.1000  0.0809  315 ASN D CG  
12686 C CG  B ASN D 315 ? 0.5947 0.3494 0.3807 0.0734  0.0954  0.0880  315 ASN D CG  
12687 O OD1 A ASN D 315 ? 0.6496 0.3978 0.4558 0.0531  0.1088  0.0801  315 ASN D OD1 
12688 O OD1 B ASN D 315 ? 0.5959 0.3435 0.3898 0.0695  0.1011  0.0867  315 ASN D OD1 
12689 N ND2 A ASN D 315 ? 0.6477 0.4049 0.4413 0.0564  0.1027  0.0815  315 ASN D ND2 
12690 N ND2 B ASN D 315 ? 0.6360 0.3793 0.4005 0.0846  0.0975  0.0952  315 ASN D ND2 
12691 N N   . VAL D 316 ? 0.5214 0.3380 0.3572 0.0630  0.0627  0.0714  316 VAL D N   
12692 C CA  . VAL D 316 ? 0.4848 0.3116 0.3231 0.0702  0.0548  0.0723  316 VAL D CA  
12693 C C   . VAL D 316 ? 0.5628 0.3741 0.3952 0.0761  0.0620  0.0767  316 VAL D C   
12694 O O   . VAL D 316 ? 0.5261 0.3249 0.3624 0.0699  0.0709  0.0752  316 VAL D O   
12695 C CB  . VAL D 316 ? 0.5175 0.3625 0.3748 0.0623  0.0474  0.0652  316 VAL D CB  
12696 C CG1 . VAL D 316 ? 0.4954 0.3487 0.3579 0.0680  0.0420  0.0656  316 VAL D CG1 
12697 C CG2 . VAL D 316 ? 0.4950 0.3553 0.3556 0.0592  0.0396  0.0620  316 VAL D CG2 
12698 N N   . GLU D 317 ? 0.5054 0.3179 0.3289 0.0882  0.0580  0.0818  317 GLU D N   
12699 C CA  . GLU D 317 ? 0.5330 0.3307 0.3506 0.0949  0.0649  0.0862  317 GLU D CA  
12700 C C   . GLU D 317 ? 0.5562 0.3659 0.3871 0.0954  0.0594  0.0834  317 GLU D C   
12701 O O   . GLU D 317 ? 0.5771 0.3744 0.4080 0.0963  0.0664  0.0844  317 GLU D O   
12702 C CB  . GLU D 317 ? 0.5787 0.3663 0.3761 0.1096  0.0661  0.0947  317 GLU D CB  
12703 C CG  . GLU D 317 ? 0.6502 0.4192 0.4320 0.1091  0.0754  0.0984  317 GLU D CG  
12704 C CD  . GLU D 317 ? 0.6981 0.4605 0.4578 0.1232  0.0741  0.1061  317 GLU D CD  
12705 O OE1 . GLU D 317 ? 0.6711 0.4466 0.4276 0.1338  0.0639  0.1081  317 GLU D OE1 
12706 O OE2 . GLU D 317 ? 0.7592 0.5028 0.5044 0.1237  0.0839  0.1099  317 GLU D OE2 
12707 N N   . GLY D 318 ? 0.5096 0.3421 0.3516 0.0944  0.0480  0.0795  318 GLY D N   
12708 C CA  . GLY D 318 ? 0.4758 0.3200 0.3311 0.0940  0.0434  0.0764  318 GLY D CA  
12709 C C   . GLY D 318 ? 0.4650 0.3320 0.3342 0.0879  0.0333  0.0704  318 GLY D C   
12710 O O   . GLY D 318 ? 0.4802 0.3567 0.3468 0.0884  0.0273  0.0699  318 GLY D O   
12711 N N   . ALA D 319 ? 0.4399 0.3143 0.3229 0.0819  0.0321  0.0656  319 ALA D N   
12712 C CA  . ALA D 319 ? 0.4452 0.3389 0.3413 0.0753  0.0240  0.0597  319 ALA D CA  
12713 C C   . ALA D 319 ? 0.4322 0.3403 0.3381 0.0798  0.0183  0.0588  319 ALA D C   
12714 O O   . ALA D 319 ? 0.4464 0.3485 0.3540 0.0828  0.0222  0.0600  319 ALA D O   
12715 C CB  . ALA D 319 ? 0.4393 0.3310 0.3441 0.0633  0.0270  0.0541  319 ALA D CB  
12716 N N   . ILE D 320 ? 0.3881 0.3147 0.3006 0.0799  0.0095  0.0564  320 ILE D N   
12717 C CA  . ILE D 320 ? 0.3926 0.3353 0.3158 0.0840  0.0038  0.0552  320 ILE D CA  
12718 C C   . ILE D 320 ? 0.3926 0.3470 0.3295 0.0741  0.0008  0.0487  320 ILE D C   
12719 O O   . ILE D 320 ? 0.3731 0.3348 0.3119 0.0683  -0.0030 0.0455  320 ILE D O   
12720 C CB  . ILE D 320 ? 0.4380 0.3936 0.3584 0.0926  -0.0040 0.0573  320 ILE D CB  
12721 C CG1 . ILE D 320 ? 0.4606 0.4023 0.3639 0.1035  -0.0008 0.0645  320 ILE D CG1 
12722 C CG2 . ILE D 320 ? 0.4493 0.4220 0.3829 0.0968  -0.0091 0.0558  320 ILE D CG2 
12723 C CD1 . ILE D 320 ? 0.5080 0.4612 0.4058 0.1125  -0.0090 0.0665  320 ILE D CD1 
12724 N N   . PHE D 321 ? 0.3532 0.3076 0.2984 0.0721  0.0036  0.0469  321 PHE D N   
12725 C CA  . PHE D 321 ? 0.3535 0.3188 0.3111 0.0646  0.0012  0.0414  321 PHE D CA  
12726 C C   . PHE D 321 ? 0.3853 0.3692 0.3530 0.0687  -0.0049 0.0404  321 PHE D C   
12727 O O   . PHE D 321 ? 0.3847 0.3714 0.3552 0.0760  -0.0045 0.0428  321 PHE D O   
12728 C CB  . PHE D 321 ? 0.3702 0.3272 0.3312 0.0614  0.0069  0.0398  321 PHE D CB  
12729 C CG  . PHE D 321 ? 0.4110 0.3525 0.3656 0.0554  0.0124  0.0388  321 PHE D CG  
12730 C CD1 . PHE D 321 ? 0.4611 0.3862 0.4061 0.0588  0.0184  0.0423  321 PHE D CD1 
12731 C CD2 . PHE D 321 ? 0.3842 0.3275 0.3428 0.0465  0.0117  0.0341  321 PHE D CD2 
12732 C CE1 . PHE D 321 ? 0.4920 0.4036 0.4329 0.0522  0.0237  0.0405  321 PHE D CE1 
12733 C CE2 . PHE D 321 ? 0.4184 0.3495 0.3730 0.0407  0.0162  0.0324  321 PHE D CE2 
12734 C CZ  . PHE D 321 ? 0.4326 0.3481 0.3790 0.0431  0.0223  0.0353  321 PHE D CZ  
12735 N N   . LEU D 322 ? 0.3344 0.3311 0.3083 0.0636  -0.0103 0.0365  322 LEU D N   
12736 C CA  . LEU D 322 ? 0.3796 0.3950 0.3653 0.0654  -0.0159 0.0340  322 LEU D CA  
12737 C C   . LEU D 322 ? 0.3591 0.3780 0.3551 0.0572  -0.0139 0.0294  322 LEU D C   
12738 O O   . LEU D 322 ? 0.3702 0.3859 0.3647 0.0496  -0.0135 0.0266  322 LEU D O   
12739 C CB  . LEU D 322 ? 0.3634 0.3899 0.3478 0.0656  -0.0232 0.0325  322 LEU D CB  
12740 C CG  . LEU D 322 ? 0.4225 0.4461 0.3942 0.0739  -0.0263 0.0368  322 LEU D CG  
12741 C CD1 . LEU D 322 ? 0.4788 0.4829 0.4363 0.0733  -0.0205 0.0404  322 LEU D CD1 
12742 C CD2 . LEU D 322 ? 0.4827 0.5176 0.4538 0.0719  -0.0335 0.0336  322 LEU D CD2 
12743 N N   A GLN D 323 ? 0.3764 0.4004 0.3817 0.0593  -0.0120 0.0290  323 GLN D N   
12744 N N   B GLN D 323 ? 0.3766 0.4005 0.3819 0.0592  -0.0120 0.0289  323 GLN D N   
12745 C CA  A GLN D 323 ? 0.3823 0.4069 0.3952 0.0525  -0.0089 0.0252  323 GLN D CA  
12746 C CA  B GLN D 323 ? 0.3826 0.4066 0.3951 0.0523  -0.0087 0.0252  323 GLN D CA  
12747 C C   A GLN D 323 ? 0.3729 0.4152 0.4004 0.0519  -0.0117 0.0221  323 GLN D C   
12748 C C   B GLN D 323 ? 0.3735 0.4150 0.4007 0.0518  -0.0113 0.0221  323 GLN D C   
12749 O O   A GLN D 323 ? 0.3563 0.4083 0.3907 0.0585  -0.0133 0.0234  323 GLN D O   
12750 O O   B GLN D 323 ? 0.3595 0.4098 0.3935 0.0585  -0.0124 0.0236  323 GLN D O   
12751 C CB  A GLN D 323 ? 0.4000 0.4128 0.4107 0.0543  -0.0024 0.0268  323 GLN D CB  
12752 C CB  B GLN D 323 ? 0.4014 0.4123 0.4107 0.0537  -0.0021 0.0268  323 GLN D CB  
12753 C CG  A GLN D 323 ? 0.4237 0.4316 0.4360 0.0469  0.0011  0.0233  323 GLN D CG  
12754 C CG  B GLN D 323 ? 0.4233 0.4305 0.4354 0.0465  0.0014  0.0231  323 GLN D CG  
12755 C CD  A GLN D 323 ? 0.4013 0.3994 0.4120 0.0490  0.0070  0.0241  323 GLN D CD  
12756 C CD  B GLN D 323 ? 0.4017 0.3921 0.4037 0.0433  0.0054  0.0232  323 GLN D CD  
12757 O OE1 A GLN D 323 ? 0.4449 0.4288 0.4465 0.0483  0.0102  0.0249  323 GLN D OE1 
12758 O OE1 B GLN D 323 ? 0.4231 0.4055 0.4236 0.0442  0.0099  0.0231  323 GLN D OE1 
12759 N NE2 A GLN D 323 ? 0.4469 0.4522 0.4667 0.0509  0.0089  0.0233  323 GLN D NE2 
12760 N NE2 B GLN D 323 ? 0.4233 0.4087 0.4185 0.0400  0.0040  0.0231  323 GLN D NE2 
12761 N N   . GLN D 324 ? 0.3491 0.3956 0.3817 0.0441  -0.0119 0.0178  324 GLN D N   
12762 C CA  . GLN D 324 ? 0.3710 0.4316 0.4183 0.0422  -0.0122 0.0143  324 GLN D CA  
12763 C C   . GLN D 324 ? 0.3230 0.3791 0.3746 0.0438  -0.0057 0.0151  324 GLN D C   
12764 O O   . GLN D 324 ? 0.3402 0.3821 0.3839 0.0418  -0.0010 0.0159  324 GLN D O   
12765 C CB  . GLN D 324 ? 0.3664 0.4297 0.4166 0.0334  -0.0127 0.0098  324 GLN D CB  
12766 C CG  . GLN D 324 ? 0.3678 0.4362 0.4144 0.0313  -0.0189 0.0081  324 GLN D CG  
12767 C CD  . GLN D 324 ? 0.4130 0.5000 0.4706 0.0340  -0.0247 0.0059  324 GLN D CD  
12768 O OE1 . GLN D 324 ? 0.4073 0.5056 0.4786 0.0307  -0.0240 0.0020  324 GLN D OE1 
12769 N NE2 . GLN D 324 ? 0.4274 0.5176 0.4791 0.0404  -0.0302 0.0083  324 GLN D NE2 
12770 N N   . LYS D 325 ? 0.3116 0.3804 0.3759 0.0476  -0.0056 0.0147  325 LYS D N   
12771 C CA  . LYS D 325 ? 0.3288 0.3945 0.3984 0.0486  0.0013  0.0149  325 LYS D CA  
12772 C C   . LYS D 325 ? 0.3012 0.3592 0.3690 0.0406  0.0057  0.0120  325 LYS D C   
12773 O O   . LYS D 325 ? 0.3018 0.3644 0.3719 0.0343  0.0036  0.0087  325 LYS D O   
12774 C CB  . LYS D 325 ? 0.3683 0.4523 0.4555 0.0518  0.0007  0.0134  325 LYS D CB  
12775 C CG  . LYS D 325 ? 0.4346 0.5161 0.5280 0.0538  0.0086  0.0139  325 LYS D CG  
12776 C CD  . LYS D 325 ? 0.5036 0.5989 0.6096 0.0621  0.0080  0.0154  325 LYS D CD  
12777 C CE  . LYS D 325 ? 0.5605 0.6459 0.6650 0.0672  0.0162  0.0183  325 LYS D CE  
12778 N NZ  . LYS D 325 ? 0.4638 0.5257 0.5494 0.0666  0.0204  0.0207  325 LYS D NZ  
12779 N N   . PHE D 326 ? 0.3128 0.3577 0.3743 0.0412  0.0118  0.0132  326 PHE D N   
12780 C CA  . PHE D 326 ? 0.3158 0.3525 0.3741 0.0356  0.0166  0.0110  326 PHE D CA  
12781 C C   . PHE D 326 ? 0.3342 0.3620 0.3817 0.0303  0.0143  0.0099  326 PHE D C   
12782 O O   . PHE D 326 ? 0.3175 0.3397 0.3622 0.0260  0.0174  0.0081  326 PHE D O   
12783 C CB  . PHE D 326 ? 0.2950 0.3429 0.3668 0.0319  0.0192  0.0078  326 PHE D CB  
12784 C CG  . PHE D 326 ? 0.3399 0.3985 0.4250 0.0368  0.0218  0.0083  326 PHE D CG  
12785 C CD1 . PHE D 326 ? 0.3420 0.3921 0.4237 0.0420  0.0274  0.0109  326 PHE D CD1 
12786 C CD2 . PHE D 326 ? 0.3646 0.4418 0.4660 0.0359  0.0191  0.0058  326 PHE D CD2 
12787 C CE1 . PHE D 326 ? 0.3942 0.4540 0.4885 0.0471  0.0306  0.0116  326 PHE D CE1 
12788 C CE2 . PHE D 326 ? 0.3471 0.4356 0.4625 0.0407  0.0219  0.0061  326 PHE D CE2 
12789 C CZ  . PHE D 326 ? 0.3960 0.4757 0.5078 0.0466  0.0278  0.0093  326 PHE D CZ  
12790 N N   . CYS D 327 ? 0.2891 0.3154 0.3301 0.0308  0.0093  0.0112  327 CYS D N   
12791 C CA  . CYS D 327 ? 0.3111 0.3310 0.3438 0.0256  0.0073  0.0100  327 CYS D CA  
12792 C C   . CYS D 327 ? 0.3234 0.3282 0.3453 0.0248  0.0105  0.0103  327 CYS D C   
12793 O O   . CYS D 327 ? 0.3072 0.3042 0.3220 0.0270  0.0100  0.0122  327 CYS D O   
12794 C CB  . CYS D 327 ? 0.3060 0.3290 0.3355 0.0267  0.0018  0.0112  327 CYS D CB  
12795 S SG  . CYS D 327 ? 0.2908 0.3066 0.3109 0.0211  -0.0003 0.0100  327 CYS D SG  
12796 N N   . ASP D 328 ? 0.3008 0.3356 0.3563 -0.0160 -0.0018 0.0508  328 ASP D N   
12797 C CA  . ASP D 328 ? 0.2971 0.3274 0.3271 -0.0106 0.0110  0.0440  328 ASP D CA  
12798 C C   . ASP D 328 ? 0.2958 0.2981 0.3003 -0.0099 0.0065  0.0268  328 ASP D C   
12799 O O   . ASP D 328 ? 0.2984 0.2939 0.2815 -0.0028 0.0164  0.0161  328 ASP D O   
12800 C CB  . ASP D 328 ? 0.3184 0.3646 0.3553 -0.0169 0.0144  0.0588  328 ASP D CB  
12801 C CG  . ASP D 328 ? 0.3317 0.4120 0.3909 -0.0156 0.0237  0.0770  328 ASP D CG  
12802 O OD1 . ASP D 328 ? 0.3598 0.4556 0.4087 -0.0034 0.0399  0.0753  328 ASP D OD1 
12803 O OD2 . ASP D 328 ? 0.3118 0.4043 0.4002 -0.0263 0.0143  0.0931  328 ASP D OD2 
12804 N N   . PRO D 329 ? 0.3202 0.3058 0.3260 -0.0162 -0.0083 0.0230  329 PRO D N   
12805 C CA  . PRO D 329 ? 0.3110 0.2765 0.2938 -0.0138 -0.0105 0.0080  329 PRO D CA  
12806 C C   . PRO D 329 ? 0.3021 0.2596 0.2726 -0.0066 -0.0058 -0.0029 329 PRO D C   
12807 O O   . PRO D 329 ? 0.3377 0.2874 0.2892 -0.0038 0.0012  -0.0119 329 PRO D O   
12808 C CB  . PRO D 329 ? 0.2986 0.2502 0.2879 -0.0188 -0.0280 0.0064  329 PRO D CB  
12809 C CG  . PRO D 329 ? 0.3282 0.2905 0.3421 -0.0273 -0.0340 0.0230  329 PRO D CG  
12810 C CD  . PRO D 329 ? 0.3108 0.2954 0.3389 -0.0256 -0.0241 0.0323  329 PRO D CD  
12811 N N   . HIS D 330 ? 0.3102 0.2704 0.2922 -0.0042 -0.0099 -0.0008 330 HIS D N   
12812 C CA  . HIS D 330 ? 0.3377 0.2890 0.3080 0.0028  -0.0064 -0.0088 330 HIS D CA  
12813 C C   . HIS D 330 ? 0.3229 0.2797 0.2889 0.0098  0.0083  -0.0080 330 HIS D C   
12814 O O   . HIS D 330 ? 0.3527 0.2964 0.3029 0.0143  0.0141  -0.0159 330 HIS D O   
12815 C CB  . HIS D 330 ? 0.3104 0.2623 0.2920 0.0041  -0.0180 -0.0073 330 HIS D CB  
12816 C CG  . HIS D 330 ? 0.3124 0.2532 0.2905 0.0006  -0.0328 -0.0131 330 HIS D CG  
12817 N ND1 . HIS D 330 ? 0.3537 0.2831 0.3150 0.0055  -0.0363 -0.0224 330 HIS D ND1 
12818 C CD2 . HIS D 330 ? 0.3075 0.2455 0.2947 -0.0060 -0.0444 -0.0112 330 HIS D CD2 
12819 C CE1 . HIS D 330 ? 0.3322 0.2540 0.2916 0.0040  -0.0495 -0.0276 330 HIS D CE1 
12820 N NE2 . HIS D 330 ? 0.3587 0.2827 0.3337 -0.0032 -0.0556 -0.0216 330 HIS D NE2 
12821 N N   . GLU D 331 ? 0.3106 0.2864 0.2907 0.0112  0.0143  0.0017  331 GLU D N   
12822 C CA  . GLU D 331 ? 0.3253 0.3063 0.2977 0.0209  0.0291  0.0004  331 GLU D CA  
12823 C C   . GLU D 331 ? 0.3523 0.3208 0.3008 0.0207  0.0358  -0.0099 331 GLU D C   
12824 O O   . GLU D 331 ? 0.3947 0.3523 0.3282 0.0284  0.0441  -0.0183 331 GLU D O   
12825 C CB  . GLU D 331 ? 0.3207 0.3304 0.3124 0.0231  0.0352  0.0141  331 GLU D CB  
12826 C CG  . GLU D 331 ? 0.3053 0.3322 0.3224 0.0265  0.0315  0.0241  331 GLU D CG  
12827 C CD  . GLU D 331 ? 0.3216 0.3826 0.3624 0.0258  0.0369  0.0409  331 GLU D CD  
12828 O OE1 . GLU D 331 ? 0.3252 0.3947 0.3666 0.0185  0.0387  0.0475  331 GLU D OE1 
12829 O OE2 . GLU D 331 ? 0.3345 0.4171 0.3949 0.0328  0.0397  0.0496  331 GLU D OE2 
12830 N N   . GLY D 332 ? 0.3305 0.3000 0.2754 0.0123  0.0315  -0.0092 332 GLY D N   
12831 C CA  . GLY D 332 ? 0.3835 0.3442 0.3065 0.0117  0.0362  -0.0187 332 GLY D CA  
12832 C C   . GLY D 332 ? 0.3731 0.3118 0.2812 0.0101  0.0335  -0.0310 332 GLY D C   
12833 O O   . GLY D 332 ? 0.4307 0.3597 0.3217 0.0112  0.0384  -0.0403 332 GLY D O   
12834 N N   . ASP D 333 ? 0.3581 0.2896 0.2720 0.0069  0.0248  -0.0308 333 ASP D N   
12835 C CA  . ASP D 333 ? 0.3835 0.2992 0.2863 0.0051  0.0228  -0.0386 333 ASP D CA  
12836 C C   . ASP D 333 ? 0.4027 0.3068 0.3028 0.0114  0.0278  -0.0402 333 ASP D C   
12837 O O   . ASP D 333 ? 0.4422 0.3314 0.3317 0.0093  0.0288  -0.0456 333 ASP D O   
12838 C CB  . ASP D 333 ? 0.3849 0.3009 0.2935 0.0025  0.0125  -0.0369 333 ASP D CB  
12839 C CG  . ASP D 333 ? 0.3882 0.3074 0.2934 -0.0027 0.0070  -0.0390 333 ASP D CG  
12840 O OD1 . ASP D 333 ? 0.4228 0.3466 0.3235 -0.0053 0.0106  -0.0394 333 ASP D OD1 
12841 O OD2 . ASP D 333 ? 0.4141 0.3318 0.3202 -0.0024 -0.0011 -0.0402 333 ASP D OD2 
12842 N N   . TYR D 334 ? 0.3984 0.3100 0.3102 0.0188  0.0300  -0.0340 334 TYR D N   
12843 C CA  . TYR D 334 ? 0.3898 0.2915 0.3025 0.0259  0.0314  -0.0328 334 TYR D CA  
12844 C C   . TYR D 334 ? 0.4164 0.2974 0.3146 0.0297  0.0385  -0.0400 334 TYR D C   
12845 O O   . TYR D 334 ? 0.4212 0.2864 0.3144 0.0290  0.0367  -0.0401 334 TYR D O   
12846 C CB  . TYR D 334 ? 0.4218 0.3399 0.3520 0.0342  0.0326  -0.0242 334 TYR D CB  
12847 C CG  . TYR D 334 ? 0.4122 0.3206 0.3423 0.0446  0.0358  -0.0228 334 TYR D CG  
12848 C CD1 . TYR D 334 ? 0.4211 0.3223 0.3513 0.0445  0.0288  -0.0200 334 TYR D CD1 
12849 C CD2 . TYR D 334 ? 0.3710 0.2776 0.2995 0.0563  0.0456  -0.0242 334 TYR D CD2 
12850 C CE1 . TYR D 334 ? 0.4791 0.3710 0.4091 0.0545  0.0309  -0.0167 334 TYR D CE1 
12851 C CE2 . TYR D 334 ? 0.4320 0.3273 0.3607 0.0674  0.0477  -0.0223 334 TYR D CE2 
12852 C CZ  . TYR D 334 ? 0.4559 0.3434 0.3859 0.0657  0.0400  -0.0177 334 TYR D CZ  
12853 O OH  . TYR D 334 ? 0.5192 0.3951 0.4493 0.0777  0.0421  -0.0141 334 TYR D OH  
12854 N N   . PRO D 335 ? 0.3993 0.2783 0.2899 0.0345  0.0461  -0.0456 335 PRO D N   
12855 C CA  . PRO D 335 ? 0.4077 0.2611 0.2840 0.0394  0.0506  -0.0543 335 PRO D CA  
12856 C C   . PRO D 335 ? 0.4731 0.3075 0.3391 0.0274  0.0458  -0.0595 335 PRO D C   
12857 O O   . PRO D 335 ? 0.4879 0.3010 0.3507 0.0276  0.0451  -0.0592 335 PRO D O   
12858 C CB  . PRO D 335 ? 0.4192 0.2775 0.2860 0.0464  0.0579  -0.0615 335 PRO D CB  
12859 C CG  . PRO D 335 ? 0.4064 0.2969 0.2902 0.0508  0.0604  -0.0505 335 PRO D CG  
12860 C CD  . PRO D 335 ? 0.3907 0.2909 0.2858 0.0385  0.0512  -0.0433 335 PRO D CD  
12861 N N   . ASP D 336 ? 0.4255 0.2692 0.2885 0.0166  0.0421  -0.0619 336 ASP D N   
12862 C CA  . ASP D 336 ? 0.4541 0.2853 0.3105 0.0049  0.0378  -0.0654 336 ASP D CA  
12863 C C   . ASP D 336 ? 0.4355 0.2721 0.2999 0.0006  0.0335  -0.0564 336 ASP D C   
12864 O O   . ASP D 336 ? 0.4633 0.2871 0.3248 -0.0059 0.0323  -0.0550 336 ASP D O   
12865 C CB  . ASP D 336 ? 0.4510 0.2916 0.3006 -0.0034 0.0355  -0.0718 336 ASP D CB  
12866 C CG  . ASP D 336 ? 0.5226 0.3504 0.3572 -0.0008 0.0383  -0.0839 336 ASP D CG  
12867 O OD1 . ASP D 336 ? 0.5535 0.3664 0.3828 0.0098  0.0431  -0.0880 336 ASP D OD1 
12868 O OD2 . ASP D 336 ? 0.5512 0.3830 0.3776 -0.0082 0.0350  -0.0904 336 ASP D OD2 
12869 N N   . LEU D 337 ? 0.3848 0.2391 0.2587 0.0042  0.0306  -0.0500 337 LEU D N   
12870 C CA  . LEU D 337 ? 0.3870 0.2447 0.2640 0.0033  0.0265  -0.0432 337 LEU D CA  
12871 C C   . LEU D 337 ? 0.4323 0.2753 0.3091 0.0092  0.0288  -0.0377 337 LEU D C   
12872 O O   . LEU D 337 ? 0.4372 0.2742 0.3107 0.0056  0.0282  -0.0325 337 LEU D O   
12873 C CB  . LEU D 337 ? 0.3953 0.2707 0.2807 0.0070  0.0207  -0.0399 337 LEU D CB  
12874 C CG  . LEU D 337 ? 0.3916 0.2719 0.2763 0.0089  0.0155  -0.0352 337 LEU D CG  
12875 C CD1 . LEU D 337 ? 0.3810 0.2632 0.2581 0.0026  0.0159  -0.0356 337 LEU D CD1 
12876 C CD2 . LEU D 337 ? 0.4213 0.3151 0.3132 0.0119  0.0069  -0.0355 337 LEU D CD2 
12877 N N   . LYS D 338 ? 0.4212 0.2596 0.3018 0.0189  0.0320  -0.0372 338 LYS D N   
12878 C CA  . LYS D 338 ? 0.4460 0.2674 0.3258 0.0262  0.0342  -0.0319 338 LYS D CA  
12879 C C   . LYS D 338 ? 0.5008 0.2968 0.3712 0.0190  0.0361  -0.0341 338 LYS D C   
12880 O O   . LYS D 338 ? 0.5268 0.3127 0.3962 0.0171  0.0351  -0.0256 338 LYS D O   
12881 C CB  . LYS D 338 ? 0.5036 0.3246 0.3888 0.0393  0.0386  -0.0328 338 LYS D CB  
12882 C CG  . LYS D 338 ? 0.5570 0.3585 0.4415 0.0499  0.0409  -0.0279 338 LYS D CG  
12883 C CD  . LYS D 338 ? 0.5515 0.3461 0.4356 0.0631  0.0476  -0.0339 338 LYS D CD  
12884 C CE  . LYS D 338 ? 0.5796 0.3517 0.4630 0.0763  0.0494  -0.0293 338 LYS D CE  
12885 N NZ  . LYS D 338 ? 0.7438 0.5141 0.6271 0.0929  0.0565  -0.0358 338 LYS D NZ  
12886 N N   . ARG D 339 ? 0.4634 0.2486 0.3270 0.0147  0.0381  -0.0449 339 ARG D N   
12887 C CA  . ARG D 339 ? 0.5462 0.3040 0.4022 0.0062  0.0374  -0.0484 339 ARG D CA  
12888 C C   . ARG D 339 ? 0.5650 0.3294 0.4233 -0.0082 0.0340  -0.0410 339 ARG D C   
12889 O O   . ARG D 339 ? 0.5235 0.2694 0.3818 -0.0143 0.0333  -0.0339 339 ARG D O   
12890 C CB  . ARG D 339 ? 0.5454 0.2945 0.3918 0.0031  0.0377  -0.0633 339 ARG D CB  
12891 C CG  . ARG D 339 ? 0.6027 0.3397 0.4430 0.0191  0.0425  -0.0715 339 ARG D CG  
12892 C CD  . ARG D 339 ? 0.6195 0.3503 0.4462 0.0184  0.0427  -0.0872 339 ARG D CD  
12893 N NE  . ARG D 339 ? 0.5882 0.2907 0.4058 0.0057  0.0366  -0.0955 339 ARG D NE  
12894 C CZ  . ARG D 339 ? 0.5930 0.2890 0.3976 0.0009  0.0333  -0.1100 339 ARG D CZ  
12895 N NH1 . ARG D 339 ? 0.6194 0.3358 0.4162 0.0086  0.0369  -0.1173 339 ARG D NH1 
12896 N NH2 . ARG D 339 ? 0.7054 0.3724 0.5041 -0.0117 0.0257  -0.1171 339 ARG D NH2 
12897 N N   . HIS D 340 ? 0.5121 0.3038 0.3733 -0.0131 0.0322  -0.0412 340 HIS D N   
12898 C CA  . HIS D 340 ? 0.4847 0.2893 0.3485 -0.0242 0.0301  -0.0343 340 HIS D CA  
12899 C C   . HIS D 340 ? 0.5086 0.3141 0.3746 -0.0208 0.0311  -0.0201 340 HIS D C   
12900 O O   . HIS D 340 ? 0.5083 0.3108 0.3757 -0.0302 0.0316  -0.0109 340 HIS D O   
12901 C CB  . HIS D 340 ? 0.4829 0.3161 0.3487 -0.0245 0.0278  -0.0376 340 HIS D CB  
12902 C CG  . HIS D 340 ? 0.4907 0.3412 0.3588 -0.0340 0.0265  -0.0330 340 HIS D CG  
12903 N ND1 . HIS D 340 ? 0.5179 0.3640 0.3876 -0.0479 0.0257  -0.0336 340 HIS D ND1 
12904 C CD2 . HIS D 340 ? 0.4676 0.3422 0.3374 -0.0307 0.0253  -0.0285 340 HIS D CD2 
12905 C CE1 . HIS D 340 ? 0.5208 0.3913 0.3952 -0.0528 0.0254  -0.0274 340 HIS D CE1 
12906 N NE2 . HIS D 340 ? 0.4822 0.3697 0.3551 -0.0412 0.0256  -0.0252 340 HIS D NE2 
12907 N N   . LEU D 341 ? 0.4896 0.3015 0.3565 -0.0078 0.0309  -0.0168 341 LEU D N   
12908 C CA  . LEU D 341 ? 0.4763 0.2909 0.3427 -0.0027 0.0310  -0.0035 341 LEU D CA  
12909 C C   . LEU D 341 ? 0.4959 0.2811 0.3616 -0.0025 0.0333  0.0038  341 LEU D C   
12910 O O   . LEU D 341 ? 0.4888 0.2704 0.3538 -0.0067 0.0343  0.0176  341 LEU D O   
12911 C CB  . LEU D 341 ? 0.4529 0.2814 0.3210 0.0106  0.0279  -0.0030 341 LEU D CB  
12912 C CG  . LEU D 341 ? 0.4183 0.2714 0.2870 0.0109  0.0234  -0.0096 341 LEU D CG  
12913 C CD1 . LEU D 341 ? 0.4728 0.3345 0.3459 0.0219  0.0182  -0.0099 341 LEU D CD1 
12914 C CD2 . LEU D 341 ? 0.4972 0.3659 0.3605 0.0074  0.0230  -0.0044 341 LEU D CD2 
12915 N N   . GLU D 342 ? 0.4946 0.2584 0.3600 0.0031  0.0343  -0.0044 342 GLU D N   
12916 C CA  . GLU D 342 ? 0.4909 0.2222 0.3550 0.0060  0.0354  0.0019  342 GLU D CA  
12917 C C   . GLU D 342 ? 0.5140 0.2238 0.3771 -0.0107 0.0343  0.0036  342 GLU D C   
12918 O O   . GLU D 342 ? 0.5534 0.2423 0.4176 -0.0138 0.0341  0.0164  342 GLU D O   
12919 C CB  . GLU D 342 ? 0.5749 0.2896 0.4379 0.0196  0.0371  -0.0083 342 GLU D CB  
12920 C CG  . GLU D 342 ? 0.5703 0.3047 0.4388 0.0356  0.0374  -0.0037 342 GLU D CG  
12921 C CD  . GLU D 342 ? 0.7114 0.4380 0.5817 0.0513  0.0406  -0.0115 342 GLU D CD  
12922 O OE1 . GLU D 342 ? 0.7436 0.4511 0.6078 0.0516  0.0431  -0.0238 342 GLU D OE1 
12923 O OE2 . GLU D 342 ? 0.7425 0.4844 0.6205 0.0645  0.0403  -0.0050 342 GLU D OE2 
12924 N N   . GLU D 343 ? 0.5685 0.2829 0.4309 -0.0223 0.0328  -0.0079 343 GLU D N   
12925 C CA  . GLU D 343 ? 0.5636 0.2616 0.4281 -0.0408 0.0298  -0.0062 343 GLU D CA  
12926 C C   . GLU D 343 ? 0.5448 0.2633 0.4164 -0.0516 0.0308  0.0125  343 GLU D C   
12927 O O   . GLU D 343 ? 0.5576 0.2613 0.4348 -0.0668 0.0288  0.0217  343 GLU D O   
12928 C CB  . GLU D 343 ? 0.5804 0.2841 0.4422 -0.0492 0.0268  -0.0231 343 GLU D CB  
12929 C CG  . GLU D 343 ? 0.5744 0.2534 0.4265 -0.0380 0.0265  -0.0402 343 GLU D CG  
12930 C CD  . GLU D 343 ? 0.6467 0.3363 0.4925 -0.0411 0.0245  -0.0571 343 GLU D CD  
12931 O OE1 . GLU D 343 ? 0.6663 0.3820 0.5166 -0.0524 0.0225  -0.0560 343 GLU D OE1 
12932 O OE2 . GLU D 343 ? 0.6744 0.3448 0.5096 -0.0316 0.0247  -0.0715 343 GLU D OE2 
12933 N N   . ASN D 344 ? 0.5156 0.2679 0.3870 -0.0438 0.0336  0.0186  344 ASN D N   
12934 C CA  . ASN D 344 ? 0.5429 0.3202 0.4181 -0.0500 0.0360  0.0356  344 ASN D CA  
12935 C C   . ASN D 344 ? 0.5689 0.3451 0.4407 -0.0391 0.0383  0.0522  344 ASN D C   
12936 O O   . ASN D 344 ? 0.6533 0.4587 0.5230 -0.0362 0.0409  0.0640  344 ASN D O   
12937 C CB  . ASN D 344 ? 0.4972 0.3134 0.3716 -0.0474 0.0364  0.0293  344 ASN D CB  
12938 C CG  . ASN D 344 ? 0.5295 0.3530 0.4095 -0.0619 0.0343  0.0205  344 ASN D CG  
12939 O OD1 . ASN D 344 ? 0.5613 0.3975 0.4491 -0.0755 0.0352  0.0308  344 ASN D OD1 
12940 N ND2 . ASN D 344 ? 0.5282 0.3449 0.4051 -0.0595 0.0313  0.0030  344 ASN D ND2 
12941 N N   . GLY D 345 ? 0.5512 0.2961 0.4209 -0.0307 0.0374  0.0529  345 GLY D N   
12942 C CA  . GLY D 345 ? 0.6234 0.3620 0.4907 -0.0218 0.0387  0.0711  345 GLY D CA  
12943 C C   . GLY D 345 ? 0.6356 0.3946 0.4969 -0.0027 0.0380  0.0710  345 GLY D C   
12944 O O   . GLY D 345 ? 0.6742 0.4378 0.5316 0.0047  0.0386  0.0878  345 GLY D O   
12945 N N   . ILE D 346 ? 0.5836 0.3553 0.4445 0.0050  0.0359  0.0539  346 ILE D N   
12946 C CA  . ILE D 346 ? 0.5995 0.3904 0.4576 0.0209  0.0329  0.0528  346 ILE D CA  
12947 C C   . ILE D 346 ? 0.5518 0.3275 0.4147 0.0314  0.0316  0.0428  346 ILE D C   
12948 O O   . ILE D 346 ? 0.5645 0.3437 0.4307 0.0302  0.0314  0.0278  346 ILE D O   
12949 C CB  . ILE D 346 ? 0.5518 0.3753 0.4074 0.0209  0.0303  0.0438  346 ILE D CB  
12950 C CG1 . ILE D 346 ? 0.6387 0.4826 0.4887 0.0145  0.0327  0.0538  346 ILE D CG1 
12951 C CG2 . ILE D 346 ? 0.5292 0.3682 0.3844 0.0352  0.0240  0.0390  346 ILE D CG2 
12952 C CD1 . ILE D 346 ? 0.5410 0.3990 0.3933 0.0046  0.0336  0.0437  346 ILE D CD1 
12953 N N   . PRO D 347 ? 0.5554 0.3185 0.4191 0.0435  0.0309  0.0520  347 PRO D N   
12954 C CA  . PRO D 347 ? 0.5559 0.3131 0.4259 0.0566  0.0303  0.0439  347 PRO D CA  
12955 C C   . PRO D 347 ? 0.5509 0.3400 0.4260 0.0623  0.0260  0.0364  347 PRO D C   
12956 O O   . PRO D 347 ? 0.5591 0.3713 0.4308 0.0615  0.0213  0.0397  347 PRO D O   
12957 C CB  . PRO D 347 ? 0.6216 0.3636 0.4916 0.0694  0.0297  0.0587  347 PRO D CB  
12958 C CG  . PRO D 347 ? 0.6719 0.4093 0.5348 0.0614  0.0301  0.0754  347 PRO D CG  
12959 C CD  . PRO D 347 ? 0.5879 0.3456 0.4470 0.0470  0.0309  0.0722  347 PRO D CD  
12960 N N   . THR D 348 ? 0.5327 0.3226 0.4159 0.0680  0.0273  0.0261  348 THR D N   
12961 C CA  . THR D 348 ? 0.4638 0.2818 0.3558 0.0703  0.0231  0.0196  348 THR D CA  
12962 C C   . THR D 348 ? 0.4740 0.2998 0.3788 0.0851  0.0227  0.0216  348 THR D C   
12963 O O   . THR D 348 ? 0.4898 0.2975 0.3959 0.0950  0.0279  0.0232  348 THR D O   
12964 C CB  . THR D 348 ? 0.5345 0.3562 0.4265 0.0598  0.0255  0.0066  348 THR D CB  
12965 O OG1 . THR D 348 ? 0.5652 0.3702 0.4580 0.0633  0.0322  -0.0004 348 THR D OG1 
12966 C CG2 . THR D 348 ? 0.5183 0.3367 0.4003 0.0459  0.0257  0.0052  348 THR D CG2 
12967 N N   . LEU D 349 ? 0.4817 0.3357 0.3972 0.0867  0.0157  0.0215  349 LEU D N   
12968 C CA  . LEU D 349 ? 0.4699 0.3416 0.4025 0.0983  0.0137  0.0250  349 LEU D CA  
12969 C C   . LEU D 349 ? 0.4384 0.3331 0.3835 0.0910  0.0110  0.0184  349 LEU D C   
12970 O O   . LEU D 349 ? 0.4354 0.3361 0.3762 0.0802  0.0048  0.0141  349 LEU D O   
12971 C CB  . LEU D 349 ? 0.4622 0.3480 0.3985 0.1060  0.0039  0.0354  349 LEU D CB  
12972 C CG  . LEU D 349 ? 0.4826 0.3933 0.4406 0.1169  -0.0005 0.0406  349 LEU D CG  
12973 C CD1 . LEU D 349 ? 0.5121 0.4109 0.4751 0.1320  0.0094  0.0445  349 LEU D CD1 
12974 C CD2 . LEU D 349 ? 0.4860 0.4132 0.4455 0.1214  -0.0138 0.0489  349 LEU D CD2 
12975 N N   . PHE D 350 ? 0.4263 0.3343 0.3870 0.0980  0.0158  0.0188  350 PHE D N   
12976 C CA  . PHE D 350 ? 0.4007 0.3322 0.3763 0.0910  0.0143  0.0163  350 PHE D CA  
12977 C C   . PHE D 350 ? 0.4246 0.3867 0.4251 0.0971  0.0075  0.0257  350 PHE D C   
12978 O O   . PHE D 350 ? 0.4215 0.3909 0.4318 0.1114  0.0128  0.0317  350 PHE D O   
12979 C CB  . PHE D 350 ? 0.4138 0.3404 0.3868 0.0929  0.0274  0.0101  350 PHE D CB  
12980 C CG  . PHE D 350 ? 0.4320 0.3843 0.4202 0.0863  0.0276  0.0110  350 PHE D CG  
12981 C CD1 . PHE D 350 ? 0.4570 0.4070 0.4389 0.0714  0.0238  0.0056  350 PHE D CD1 
12982 C CD2 . PHE D 350 ? 0.4143 0.3939 0.4232 0.0953  0.0325  0.0185  350 PHE D CD2 
12983 C CE1 . PHE D 350 ? 0.4541 0.4258 0.4502 0.0648  0.0237  0.0087  350 PHE D CE1 
12984 C CE2 . PHE D 350 ? 0.4401 0.4455 0.4648 0.0878  0.0331  0.0227  350 PHE D CE2 
12985 C CZ  . PHE D 350 ? 0.4429 0.4424 0.4606 0.0722  0.0287  0.0181  350 PHE D CZ  
12986 N N   . LEU D 351 ? 0.3895 0.3698 0.4017 0.0867  -0.0049 0.0268  351 LEU D N   
12987 C CA  . LEU D 351 ? 0.3479 0.3596 0.3877 0.0888  -0.0139 0.0362  351 LEU D CA  
12988 C C   . LEU D 351 ? 0.3494 0.3783 0.4058 0.0749  -0.0178 0.0364  351 LEU D C   
12989 O O   . LEU D 351 ? 0.3648 0.3802 0.4095 0.0633  -0.0220 0.0289  351 LEU D O   
12990 C CB  . LEU D 351 ? 0.3539 0.3692 0.3927 0.0891  -0.0308 0.0385  351 LEU D CB  
12991 C CG  . LEU D 351 ? 0.3696 0.3679 0.3903 0.1017  -0.0285 0.0411  351 LEU D CG  
12992 C CD1 . LEU D 351 ? 0.4282 0.4318 0.4424 0.1005  -0.0464 0.0419  351 LEU D CD1 
12993 C CD2 . LEU D 351 ? 0.4224 0.4328 0.4586 0.1173  -0.0211 0.0503  351 LEU D CD2 
12994 N N   . GLU D 352 ? 0.3467 0.4060 0.4309 0.0769  -0.0154 0.0465  352 GLU D N   
12995 C CA  . GLU D 352 ? 0.3244 0.4030 0.4283 0.0635  -0.0177 0.0512  352 GLU D CA  
12996 C C   . GLU D 352 ? 0.3694 0.4764 0.5051 0.0558  -0.0351 0.0615  352 GLU D C   
12997 O O   . GLU D 352 ? 0.3345 0.4630 0.4873 0.0654  -0.0375 0.0698  352 GLU D O   
12998 C CB  . GLU D 352 ? 0.3846 0.4809 0.4971 0.0706  0.0009  0.0571  352 GLU D CB  
12999 C CG  . GLU D 352 ? 0.4144 0.5217 0.5368 0.0559  0.0016  0.0612  352 GLU D CG  
13000 C CD  . GLU D 352 ? 0.4871 0.6155 0.6144 0.0643  0.0212  0.0675  352 GLU D CD  
13001 O OE1 . GLU D 352 ? 0.4619 0.6170 0.6058 0.0782  0.0295  0.0762  352 GLU D OE1 
13002 O OE2 . GLU D 352 ? 0.5080 0.6276 0.6217 0.0581  0.0279  0.0637  352 GLU D OE2 
13003 N N   . PHE D 353 ? 0.3313 0.4386 0.4765 0.0384  -0.0481 0.0614  353 PHE D N   
13004 C CA  . PHE D 353 ? 0.4138 0.5393 0.5861 0.0275  -0.0699 0.0678  353 PHE D CA  
13005 C C   . PHE D 353 ? 0.3890 0.5392 0.5943 0.0122  -0.0728 0.0811  353 PHE D C   
13006 O O   . PHE D 353 ? 0.3775 0.5182 0.5767 0.0046  -0.0653 0.0807  353 PHE D O   
13007 C CB  . PHE D 353 ? 0.3934 0.4906 0.5458 0.0202  -0.0896 0.0539  353 PHE D CB  
13008 C CG  . PHE D 353 ? 0.4402 0.5193 0.5635 0.0339  -0.0885 0.0447  353 PHE D CG  
13009 C CD1 . PHE D 353 ? 0.4102 0.4638 0.5022 0.0408  -0.0733 0.0361  353 PHE D CD1 
13010 C CD2 . PHE D 353 ? 0.4416 0.5327 0.5711 0.0401  -0.1021 0.0471  353 PHE D CD2 
13011 C CE1 . PHE D 353 ? 0.4226 0.4616 0.4906 0.0525  -0.0715 0.0313  353 PHE D CE1 
13012 C CE2 . PHE D 353 ? 0.4845 0.5611 0.5871 0.0536  -0.1001 0.0419  353 PHE D CE2 
13013 C CZ  . PHE D 353 ? 0.4534 0.5034 0.5257 0.0593  -0.0845 0.0347  353 PHE D CZ  
13014 N N   . ASP D 354 ? 0.4002 0.5829 0.6417 0.0068  -0.0853 0.0941  354 ASP D N   
13015 C CA  . ASP D 354 ? 0.3771 0.5828 0.6548 -0.0122 -0.0944 0.1087  354 ASP D CA  
13016 C C   . ASP D 354 ? 0.4360 0.6260 0.7210 -0.0285 -0.1253 0.1022  354 ASP D C   
13017 O O   . ASP D 354 ? 0.4352 0.5942 0.6903 -0.0237 -0.1361 0.0844  354 ASP D O   
13018 C CB  . ASP D 354 ? 0.4474 0.7048 0.7646 -0.0082 -0.0862 0.1298  354 ASP D CB  
13019 C CG  . ASP D 354 ? 0.5096 0.7934 0.8540 -0.0207 -0.0771 0.1481  354 ASP D CG  
13020 O OD1 . ASP D 354 ? 0.4680 0.7433 0.8269 -0.0424 -0.0936 0.1522  354 ASP D OD1 
13021 O OD2 . ASP D 354 ? 0.5637 0.8762 0.9139 -0.0079 -0.0536 0.1586  354 ASP D OD2 
13022 N N   . ILE D 355 ? 0.4388 0.6500 0.7631 -0.0478 -0.1400 0.1167  355 ILE D N   
13023 C CA  . ILE D 355 ? 0.4535 0.6459 0.7849 -0.0638 -0.1721 0.1088  355 ILE D CA  
13024 C C   . ILE D 355 ? 0.4789 0.6766 0.8060 -0.0544 -0.1875 0.1004  355 ILE D C   
13025 O O   . ILE D 355 ? 0.4913 0.6566 0.7888 -0.0513 -0.2031 0.0809  355 ILE D O   
13026 C CB  . ILE D 355 ? 0.4320 0.6469 0.8113 -0.0882 -0.1868 0.1283  355 ILE D CB  
13027 C CG1 . ILE D 355 ? 0.4377 0.6389 0.8160 -0.0989 -0.1762 0.1353  355 ILE D CG1 
13028 C CG2 . ILE D 355 ? 0.4433 0.6375 0.8310 -0.1039 -0.2238 0.1180  355 ILE D CG2 
13029 C CD1 . ILE D 355 ? 0.3786 0.5846 0.7982 -0.1268 -0.1984 0.1511  355 ILE D CD1 
13030 N N   . THR D 356 ? 0.4440 0.6843 0.7983 -0.0473 -0.1817 0.1153  356 THR D N   
13031 C CA  . THR D 356 ? 0.4820 0.7319 0.8309 -0.0342 -0.1919 0.1102  356 THR D CA  
13032 C C   . THR D 356 ? 0.5235 0.7893 0.8613 -0.0099 -0.1645 0.1153  356 THR D C   
13033 O O   . THR D 356 ? 0.5125 0.8024 0.8664 -0.0055 -0.1421 0.1290  356 THR D O   
13034 C CB  . THR D 356 ? 0.4880 0.7767 0.8839 -0.0472 -0.2155 0.1239  356 THR D CB  
13035 O OG1 . THR D 356 ? 0.5001 0.8374 0.9384 -0.0493 -0.1995 0.1488  356 THR D OG1 
13036 C CG2 . THR D 356 ? 0.4384 0.7079 0.8473 -0.0724 -0.2447 0.1188  356 THR D CG2 
13037 N N   . ASN D 357 ? 0.5771 0.8300 0.8874 0.0069  -0.1668 0.1049  357 ASN D N   
13038 C CA  . ASN D 357 ? 0.5612 0.8240 0.8609 0.0310  -0.1431 0.1098  357 ASN D CA  
13039 C C   . ASN D 357 ? 0.5665 0.8389 0.8629 0.0439  -0.1565 0.1093  357 ASN D C   
13040 O O   . ASN D 357 ? 0.5669 0.8137 0.8367 0.0426  -0.1737 0.0955  357 ASN D O   
13041 C CB  . ASN D 357 ? 0.5559 0.7781 0.8113 0.0413  -0.1227 0.0966  357 ASN D CB  
13042 C CG  . ASN D 357 ? 0.5071 0.7192 0.7617 0.0302  -0.1098 0.0962  357 ASN D CG  
13043 O OD1 . ASN D 357 ? 0.4885 0.6740 0.7289 0.0172  -0.1199 0.0859  357 ASN D OD1 
13044 N ND2 . ASN D 357 ? 0.4938 0.7271 0.7613 0.0374  -0.0875 0.1072  357 ASN D ND2 
13045 N N   . PRO D 358 ? 0.5439 0.8536 0.8651 0.0579  -0.1493 0.1241  358 PRO D N   
13046 C CA  . PRO D 358 ? 0.5065 0.8225 0.8194 0.0743  -0.1591 0.1246  358 PRO D CA  
13047 C C   . PRO D 358 ? 0.5111 0.7824 0.7730 0.0889  -0.1491 0.1112  358 PRO D C   
13048 O O   . PRO D 358 ? 0.5222 0.7730 0.7651 0.0987  -0.1250 0.1090  358 PRO D O   
13049 C CB  . PRO D 358 ? 0.4874 0.8474 0.8329 0.0907  -0.1447 0.1432  358 PRO D CB  
13050 C CG  . PRO D 358 ? 0.4543 0.8431 0.8353 0.0776  -0.1345 0.1546  358 PRO D CG  
13051 C CD  . PRO D 358 ? 0.4829 0.8405 0.8508 0.0543  -0.1411 0.1436  358 PRO D CD  
13052 N N   . ILE D 359 ? 0.5296 0.7871 0.7694 0.0903  -0.1686 0.1028  359 ILE D N   
13053 C CA  . ILE D 359 ? 0.5919 0.8088 0.7839 0.1006  -0.1606 0.0916  359 ILE D CA  
13054 C C   . ILE D 359 ? 0.5456 0.7604 0.7263 0.1246  -0.1440 0.1006  359 ILE D C   
13055 O O   . ILE D 359 ? 0.5280 0.7086 0.6754 0.1320  -0.1288 0.0950  359 ILE D O   
13056 C CB  . ILE D 359 ? 0.6157 0.8200 0.7851 0.0946  -0.1863 0.0793  359 ILE D CB  
13057 C CG1 . ILE D 359 ? 0.6594 0.8221 0.7809 0.0994  -0.1764 0.0667  359 ILE D CG1 
13058 C CG2 . ILE D 359 ? 0.5402 0.7709 0.7175 0.1052  -0.2049 0.0869  359 ILE D CG2 
13059 C CD1 . ILE D 359 ? 0.5743 0.7165 0.6757 0.0861  -0.1930 0.0492  359 ILE D CD1 
13060 N N   . GLY D 360 ? 0.4939 0.7444 0.7036 0.1367  -0.1462 0.1151  360 GLY D N   
13061 C CA  . GLY D 360 ? 0.5117 0.7603 0.7141 0.1611  -0.1322 0.1247  360 GLY D CA  
13062 C C   . GLY D 360 ? 0.5512 0.7676 0.7337 0.1711  -0.1044 0.1219  360 GLY D C   
13063 O O   . GLY D 360 ? 0.5295 0.7139 0.6808 0.1826  -0.0972 0.1205  360 GLY D O   
13064 N N   . PRO D 361 ? 0.5400 0.7648 0.7401 0.1672  -0.0889 0.1220  361 PRO D N   
13065 C CA  . PRO D 361 ? 0.5060 0.6998 0.6859 0.1778  -0.0642 0.1175  361 PRO D CA  
13066 C C   . PRO D 361 ? 0.5296 0.6774 0.6712 0.1671  -0.0605 0.1035  361 PRO D C   
13067 O O   . PRO D 361 ? 0.5504 0.6652 0.6680 0.1774  -0.0461 0.1005  361 PRO D O   
13068 C CB  . PRO D 361 ? 0.5077 0.7276 0.7148 0.1739  -0.0517 0.1203  361 PRO D CB  
13069 C CG  . PRO D 361 ? 0.4917 0.7630 0.7403 0.1689  -0.0667 0.1328  361 PRO D CG  
13070 C CD  . PRO D 361 ? 0.4905 0.7574 0.7319 0.1558  -0.0926 0.1290  361 PRO D CD  
13071 N N   . PHE D 362 ? 0.5061 0.6503 0.6422 0.1469  -0.0734 0.0950  362 PHE D N   
13072 C CA  . PHE D 362 ? 0.5073 0.6124 0.6076 0.1387  -0.0706 0.0828  362 PHE D CA  
13073 C C   . PHE D 362 ? 0.4980 0.5852 0.5720 0.1488  -0.0760 0.0848  362 PHE D C   
13074 O O   . PHE D 362 ? 0.4917 0.5463 0.5383 0.1515  -0.0648 0.0814  362 PHE D O   
13075 C CB  . PHE D 362 ? 0.4989 0.6051 0.5996 0.1180  -0.0842 0.0732  362 PHE D CB  
13076 C CG  . PHE D 362 ? 0.5015 0.6234 0.6270 0.1061  -0.0791 0.0736  362 PHE D CG  
13077 C CD1 . PHE D 362 ? 0.4864 0.5888 0.5999 0.1021  -0.0622 0.0674  362 PHE D CD1 
13078 C CD2 . PHE D 362 ? 0.5599 0.7184 0.7218 0.0990  -0.0914 0.0820  362 PHE D CD2 
13079 C CE1 . PHE D 362 ? 0.5101 0.6285 0.6443 0.0919  -0.0571 0.0696  362 PHE D CE1 
13080 C CE2 . PHE D 362 ? 0.5770 0.7522 0.7628 0.0873  -0.0859 0.0858  362 PHE D CE2 
13081 C CZ  . PHE D 362 ? 0.5247 0.6798 0.6954 0.0844  -0.0683 0.0798  362 PHE D CZ  
13082 N N   . ARG D 363 ? 0.4662 0.5757 0.5485 0.1544  -0.0932 0.0918  363 ARG D N   
13083 C CA  . ARG D 363 ? 0.5169 0.6125 0.5734 0.1659  -0.0975 0.0966  363 ARG D CA  
13084 C C   . ARG D 363 ? 0.5399 0.6165 0.5897 0.1835  -0.0799 0.1061  363 ARG D C   
13085 O O   . ARG D 363 ? 0.5769 0.6244 0.5986 0.1875  -0.0740 0.1078  363 ARG D O   
13086 C CB  . ARG D 363 ? 0.5833 0.7096 0.6507 0.1710  -0.1197 0.1033  363 ARG D CB  
13087 C CG  . ARG D 363 ? 0.6000 0.7136 0.6350 0.1804  -0.1265 0.1071  363 ARG D CG  
13088 C CD  . ARG D 363 ? 0.6551 0.8009 0.6997 0.1880  -0.1492 0.1143  363 ARG D CD  
13089 N NE  . ARG D 363 ? 0.7667 0.9390 0.8351 0.1732  -0.1688 0.1058  363 ARG D NE  
13090 C CZ  . ARG D 363 ? 0.7882 0.9958 0.8965 0.1727  -0.1771 0.1132  363 ARG D CZ  
13091 N NH1 . ARG D 363 ? 0.7290 0.9530 0.8579 0.1891  -0.1672 0.1285  363 ARG D NH1 
13092 N NH2 . ARG D 363 ? 0.7554 0.9829 0.8849 0.1556  -0.1963 0.1057  363 ARG D NH2 
13093 N N   . ILE D 364 ? 0.5025 0.5951 0.5783 0.1949  -0.0716 0.1131  364 ILE D N   
13094 C CA  . ILE D 364 ? 0.5725 0.6417 0.6405 0.2137  -0.0560 0.1201  364 ILE D CA  
13095 C C   . ILE D 364 ? 0.5645 0.5917 0.6085 0.2062  -0.0402 0.1099  364 ILE D C   
13096 O O   . ILE D 364 ? 0.5765 0.5698 0.5988 0.2132  -0.0333 0.1135  364 ILE D O   
13097 C CB  . ILE D 364 ? 0.5269 0.6225 0.6264 0.2296  -0.0486 0.1271  364 ILE D CB  
13098 C CG1 . ILE D 364 ? 0.4880 0.6264 0.6127 0.2391  -0.0649 0.1401  364 ILE D CG1 
13099 C CG2 . ILE D 364 ? 0.6063 0.6703 0.6951 0.2493  -0.0317 0.1299  364 ILE D CG2 
13100 C CD1 . ILE D 364 ? 0.4919 0.6659 0.6525 0.2554  -0.0576 0.1487  364 ILE D CD1 
13101 N N   . ARG D 365 ? 0.4934 0.5230 0.5421 0.1910  -0.0353 0.0982  365 ARG D N   
13102 C CA  . ARG D 365 ? 0.5206 0.5147 0.5485 0.1825  -0.0220 0.0877  365 ARG D CA  
13103 C C   . ARG D 365 ? 0.5483 0.5172 0.5474 0.1726  -0.0259 0.0854  365 ARG D C   
13104 O O   . ARG D 365 ? 0.5491 0.4838 0.5293 0.1727  -0.0157 0.0842  365 ARG D O   
13105 C CB  . ARG D 365 ? 0.5238 0.5309 0.5630 0.1683  -0.0183 0.0774  365 ARG D CB  
13106 C CG  . ARG D 365 ? 0.5253 0.5572 0.5907 0.1793  -0.0096 0.0810  365 ARG D CG  
13107 C CD  . ARG D 365 ? 0.5709 0.5728 0.6228 0.1917  0.0082  0.0760  365 ARG D CD  
13108 N NE  . ARG D 365 ? 0.6017 0.5721 0.6304 0.1774  0.0146  0.0634  365 ARG D NE  
13109 C CZ  . ARG D 365 ? 0.6338 0.6130 0.6657 0.1653  0.0192  0.0552  365 ARG D CZ  
13110 N NH1 . ARG D 365 ? 0.6702 0.6878 0.7277 0.1639  0.0184  0.0594  365 ARG D NH1 
13111 N NH2 . ARG D 365 ? 0.6858 0.6363 0.6960 0.1537  0.0242  0.0444  365 ARG D NH2 
13112 N N   . ILE D 366 ? 0.5385 0.5242 0.5339 0.1640  -0.0409 0.0845  366 ILE D N   
13113 C CA  . ILE D 366 ? 0.5167 0.4845 0.4839 0.1570  -0.0436 0.0831  366 ILE D CA  
13114 C C   . ILE D 366 ? 0.5317 0.4841 0.4844 0.1705  -0.0417 0.0975  366 ILE D C   
13115 O O   . ILE D 366 ? 0.5609 0.4872 0.4928 0.1669  -0.0343 0.0999  366 ILE D O   
13116 C CB  . ILE D 366 ? 0.5585 0.5480 0.5226 0.1485  -0.0612 0.0772  366 ILE D CB  
13117 C CG1 . ILE D 366 ? 0.5005 0.4995 0.4778 0.1333  -0.0642 0.0639  366 ILE D CG1 
13118 C CG2 . ILE D 366 ? 0.5476 0.5234 0.4807 0.1463  -0.0628 0.0774  366 ILE D CG2 
13119 C CD1 . ILE D 366 ? 0.5478 0.5251 0.5098 0.1218  -0.0541 0.0539  366 ILE D CD1 
13120 N N   . GLU D 367 ? 0.5359 0.5059 0.5008 0.1857  -0.0491 0.1090  367 GLU D N   
13121 C CA  . GLU D 367 ? 0.5692 0.5240 0.5212 0.2000  -0.0478 0.1252  367 GLU D CA  
13122 C C   . GLU D 367 ? 0.5921 0.5087 0.5399 0.2046  -0.0314 0.1279  367 GLU D C   
13123 O O   . GLU D 367 ? 0.6509 0.5412 0.5807 0.2069  -0.0274 0.1385  367 GLU D O   
13124 C CB  . GLU D 367 ? 0.6099 0.5927 0.5794 0.2169  -0.0588 0.1367  367 GLU D CB  
13125 C CG  . GLU D 367 ? 0.6696 0.6902 0.6468 0.2105  -0.0778 0.1316  367 GLU D CG  
13126 C CD  . GLU D 367 ? 0.6875 0.7399 0.6828 0.2256  -0.0914 0.1433  367 GLU D CD  
13127 O OE1 . GLU D 367 ? 0.7280 0.7980 0.7530 0.2329  -0.0887 0.1456  367 GLU D OE1 
13128 O OE2 . GLU D 367 ? 0.7360 0.7994 0.7163 0.2306  -0.1049 0.1503  367 GLU D OE2 
13129 N N   . ALA D 368 ? 0.5901 0.5031 0.5540 0.2065  -0.0224 0.1190  368 ALA D N   
13130 C CA  . ALA D 368 ? 0.6636 0.5368 0.6210 0.2112  -0.0085 0.1176  368 ALA D CA  
13131 C C   . ALA D 368 ? 0.6562 0.5018 0.5940 0.1921  -0.0024 0.1095  368 ALA D C   
13132 O O   . ALA D 368 ? 0.6377 0.4464 0.5626 0.1921  0.0038  0.1147  368 ALA D O   
13133 C CB  . ALA D 368 ? 0.6730 0.5533 0.6496 0.2200  -0.0003 0.1083  368 ALA D CB  
13134 N N   . PHE D 369 ? 0.5899 0.4532 0.5268 0.1756  -0.0051 0.0979  369 PHE D N   
13135 C CA  . PHE D 369 ? 0.5937 0.4375 0.5139 0.1580  -0.0001 0.0908  369 PHE D CA  
13136 C C   . PHE D 369 ? 0.6614 0.4955 0.5630 0.1551  -0.0027 0.1041  369 PHE D C   
13137 O O   . PHE D 369 ? 0.7034 0.5095 0.5936 0.1469  0.0043  0.1070  369 PHE D O   
13138 C CB  . PHE D 369 ? 0.5633 0.4309 0.4873 0.1440  -0.0041 0.0771  369 PHE D CB  
13139 C CG  . PHE D 369 ? 0.5636 0.4166 0.4732 0.1271  0.0008  0.0690  369 PHE D CG  
13140 C CD1 . PHE D 369 ? 0.5418 0.3651 0.4464 0.1218  0.0112  0.0643  369 PHE D CD1 
13141 C CD2 . PHE D 369 ? 0.5489 0.4191 0.4500 0.1175  -0.0061 0.0652  369 PHE D CD2 
13142 C CE1 . PHE D 369 ? 0.5220 0.3370 0.4159 0.1055  0.0144  0.0576  369 PHE D CE1 
13143 C CE2 . PHE D 369 ? 0.5628 0.4245 0.4525 0.1037  -0.0016 0.0585  369 PHE D CE2 
13144 C CZ  . PHE D 369 ? 0.5345 0.3707 0.4219 0.0971  0.0085  0.0556  369 PHE D CZ  
13145 N N   . LEU D 370 ? 0.6305 0.4897 0.5291 0.1615  -0.0133 0.1130  370 LEU D N   
13146 C CA  . LEU D 370 ? 0.6601 0.5155 0.5396 0.1623  -0.0154 0.1286  370 LEU D CA  
13147 C C   . LEU D 370 ? 0.7250 0.5462 0.6015 0.1695  -0.0081 0.1445  370 LEU D C   
13148 O O   . LEU D 370 ? 0.7914 0.5935 0.6545 0.1614  -0.0029 0.1548  370 LEU D O   
13149 C CB  . LEU D 370 ? 0.6790 0.5667 0.5561 0.1730  -0.0293 0.1355  370 LEU D CB  
13150 C CG  . LEU D 370 ? 0.7468 0.6518 0.6011 0.1716  -0.0361 0.1420  370 LEU D CG  
13151 C CD1 . LEU D 370 ? 0.7247 0.6388 0.5701 0.1570  -0.0361 0.1257  370 LEU D CD1 
13152 C CD2 . LEU D 370 ? 0.6922 0.6267 0.5471 0.1853  -0.0519 0.1471  370 LEU D CD2 
13153 N N   . GLU D 371 ? 0.7419 0.5554 0.6322 0.1853  -0.0081 0.1478  371 GLU D N   
13154 C CA  . GLU D 371 ? 0.7715 0.5487 0.6592 0.1952  -0.0032 0.1630  371 GLU D CA  
13155 C C   . GLU D 371 ? 0.8637 0.6000 0.7481 0.1829  0.0069  0.1553  371 GLU D C   
13156 O O   . GLU D 371 ? 0.9605 0.6627 0.8372 0.1810  0.0100  0.1689  371 GLU D O   
13157 C CB  . GLU D 371 ? 0.7891 0.5715 0.6933 0.2177  -0.0059 0.1660  371 GLU D CB  
13158 C CG  . GLU D 371 ? 0.8533 0.6756 0.7601 0.2289  -0.0183 0.1771  371 GLU D CG  
13159 C CD  . GLU D 371 ? 0.9002 0.7382 0.8276 0.2511  -0.0224 0.1808  371 GLU D CD  
13160 O OE1 . GLU D 371 ? 0.8610 0.7139 0.8068 0.2528  -0.0198 0.1664  371 GLU D OE1 
13161 O OE2 . GLU D 371 ? 0.9795 0.8184 0.9051 0.2672  -0.0280 0.1996  371 GLU D OE2 
13162 N N   . THR D 372 ? 0.7754 0.5152 0.6655 0.1733  0.0109  0.1344  372 THR D N   
13163 C CA  . THR D 372 ? 0.8801 0.5856 0.7653 0.1594  0.0184  0.1247  372 THR D CA  
13164 C C   . THR D 372 ? 0.9011 0.6019 0.7736 0.1399  0.0194  0.1330  372 THR D C   
13165 O O   . THR D 372 ? 0.9544 0.6193 0.8225 0.1310  0.0231  0.1386  372 THR D O   
13166 C CB  . THR D 372 ? 0.8510 0.5691 0.7437 0.1544  0.0217  0.1018  372 THR D CB  
13167 O OG1 . THR D 372 ? 0.8656 0.5796 0.7695 0.1732  0.0241  0.0961  372 THR D OG1 
13168 C CG2 . THR D 372 ? 0.8920 0.5841 0.7773 0.1363  0.0271  0.0902  372 THR D CG2 
13169 N N   . LEU D 373 ? 0.8481 0.5851 0.7151 0.1335  0.0156  0.1342  373 LEU D N   
13170 C CA  . LEU D 373 ? 0.8861 0.6256 0.7413 0.1178  0.0179  0.1431  373 LEU D CA  
13171 C C   . LEU D 373 ? 0.9458 0.6654 0.7943 0.1205  0.0189  0.1691  373 LEU D C   
13172 O O   . LEU D 373 ? 1.0217 0.7291 0.8652 0.1056  0.0233  0.1794  373 LEU D O   
13173 C CB  . LEU D 373 ? 0.7581 0.5407 0.6060 0.1159  0.0128  0.1390  373 LEU D CB  
13174 C CG  . LEU D 373 ? 0.7585 0.5588 0.6132 0.1100  0.0112  0.1152  373 LEU D CG  
13175 C CD1 . LEU D 373 ? 0.6575 0.4953 0.5050 0.1105  0.0035  0.1094  373 LEU D CD1 
13176 C CD2 . LEU D 373 ? 0.7103 0.4934 0.5666 0.0935  0.0183  0.1041  373 LEU D CD2 
13177 N N   . SER D 374 ? 1.0047 0.7214 0.8547 0.1390  0.0146  0.1816  374 SER D N   
13178 C CA  . SER D 374 ? 1.0735 0.7721 0.9166 0.1430  0.0149  0.2093  374 SER D CA  
13179 C C   . SER D 374 ? 1.1311 0.7764 0.9792 0.1365  0.0193  0.2152  374 SER D C   
13180 O O   . SER D 374 ? 1.2161 0.8427 1.0596 0.1326  0.0203  0.2397  374 SER D O   
13181 C CB  . SER D 374 ? 1.0717 0.7822 0.9155 0.1663  0.0079  0.2213  374 SER D CB  
13182 O OG  . SER D 374 ? 1.0664 0.8232 0.9010 0.1704  0.0016  0.2224  374 SER D OG  
13183 N N   . GLU D 375 ? 1.2945 0.9146 1.1512 0.1354  0.0212  0.1939  375 GLU D N   
13184 C CA  . GLU D 375 ? 1.3695 0.9339 1.2295 0.1315  0.0229  0.1949  375 GLU D CA  
13185 C C   . GLU D 375 ? 1.3825 0.9303 1.2424 0.1058  0.0260  0.1856  375 GLU D C   
13186 O O   . GLU D 375 ? 1.4387 0.9382 1.3011 0.1001  0.0253  0.1826  375 GLU D O   
13187 C CB  . GLU D 375 ? 1.3219 0.8657 1.1889 0.1508  0.0224  0.1769  375 GLU D CB  
13188 C CG  . GLU D 375 ? 1.2916 0.8619 1.1633 0.1763  0.0193  0.1817  375 GLU D CG  
13189 C CD  . GLU D 375 ? 1.3491 0.9221 1.2300 0.1918  0.0212  0.1591  375 GLU D CD  
13190 O OE1 . GLU D 375 ? 1.2813 0.8545 1.1625 0.1808  0.0249  0.1374  375 GLU D OE1 
13191 O OE2 . GLU D 375 ? 1.4201 0.9975 1.3080 0.2156  0.0192  0.1642  375 GLU D OE2 
13192 N N   . GLU D 376 ? 1.2661 0.8516 1.1234 0.0910  0.0282  0.1800  376 GLU D N   
13193 C CA  . GLU D 376 ? 1.2893 0.8651 1.1481 0.0662  0.0306  0.1748  376 GLU D CA  
13194 C C   . GLU D 376 ? 1.3169 0.9029 1.1734 0.0513  0.0327  0.2023  376 GLU D C   
13195 O O   . GLU D 376 ? 1.3296 0.9109 1.1903 0.0294  0.0347  0.2042  376 GLU D O   
13196 C CB  . GLU D 376 ? 1.2711 0.8805 1.1301 0.0595  0.0322  0.1506  376 GLU D CB  
13197 C CG  . GLU D 376 ? 1.2548 0.9169 1.1090 0.0671  0.0317  0.1498  376 GLU D CG  
13198 C CD  . GLU D 376 ? 1.3150 1.0063 1.1622 0.0566  0.0339  0.1671  376 GLU D CD  
13199 O OE1 . GLU D 376 ? 1.3624 1.0394 1.2116 0.0404  0.0371  0.1812  376 GLU D OE1 
13200 O OE2 . GLU D 376 ? 1.2111 0.9414 1.0512 0.0648  0.0322  0.1662  376 GLU D OE2 
# 
