data_9KT5
# 
_entry.id   9KT5 
# 
_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   9KT5         pdb_00009kt5 10.2210/pdb9kt5/pdb 
WWPDB D_1300054228 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-26 ? 
2 'Structure model' 1 1 2025-04-02 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.page_last'               
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9KT5 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'F393H mutant, oxidized state'              8YAZ unspecified 
PDB 'F393H mutant, reduced state'               8YB1 unspecified 
PDB 'F393H mutant, oxygen-bound state'          8YB3 unspecified 
PDB 'F87A and F393H mutant, oxidized state'     8YAY unspecified 
PDB 'F87A and F393H mutant, reduced state'      8YB0 unspecified 
PDB 'F87A and F393H mutant, oxygen-bound state' 8YB2 unspecified 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 sugimoto@spring8.or.jp   Hiroshi Sugimoto ? 'principal investigator/group leader' 0000-0002-3140-8362 
4 minoru@sci.u-hyogo.ac.jp Minoru  Kubo     ? 'principal investigator/group leader' 0000-0002-1470-942X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Nagao, S.'       1  ? 
'Kuwano, W.'      2  ? 
'Tosha, T.'       3  ? 
'Yamashita, K.'   4  ? 
'Stanfield, J.K.' 5  ? 
'Kasai, C.'       6  ? 
'Ariyasu, S.'     7  ? 
'Shoji, O.'       8  ? 
'Sugimoto, H.'    9  ? 
'Kubo, M.'        10 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Chem' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3669 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                63 
_citation.page_last                 63 
_citation.title                     
'XFEL crystallography reveals catalytic cycle dynamics during non-native substrate oxidation by cytochrome P450BM3.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42004-025-01440-2 
_citation.pdbx_database_id_PubMed   40075209 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nagao, S.'       1  ? 
primary 'Kuwano, W.'      2  ? 
primary 'Tosha, T.'       3  ? 
primary 'Yamashita, K.'   4  ? 
primary 'Stanfield, J.K.' 5  ? 
primary 'Kasai, C.'       6  ? 
primary 'Ariyasu, S.'     7  ? 
primary 'Hirata, K.'      8  ? 
primary 'Ueno, G.'        9  ? 
primary 'Murakami, H.'    10 ? 
primary 'Ago, H.'         11 ? 
primary 'Yamamoto, M.'    12 ? 
primary 'Shoji, O.'       13 ? 
primary 'Sugimoto, H.'    14 ? 
primary 'Kubo, M.'        15 ? 
# 
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 'Bifunctional cytochrome P450/NADPH--P450 reductase'                           52215.535 2   1.14.14.1,1.6.2.4 
F87A,F393H ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                              616.487   2   ?                 ? 
? ? 
3 non-polymer syn ethenylbenzene                                                                 104.149   2   ?                 ? 
? ? 
4 non-polymer syn 'OXYGEN MOLECULE'                                                              31.999    2   ?                 ? 
? ? 
5 non-polymer syn '(2S)-2-[[(2S)-1-heptylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid' 360.490   2   ?                 ? 
? ? 
6 non-polymer syn GLYCEROL                                                                       92.094    4   ?                 ? 
? ? 
7 water       nat water                                                                          18.015    880 ?                 ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytochrome P450(BM-3),Cytochrome P450BM-3,Fatty acid monooxygenase,Flavocytochrome P450 BM3' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MTIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVR
DFAGDGLATSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFN
YRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLN
GKDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLN
EALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPHGNGQRA
CIGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVR
DFAGDGLATSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFN
YRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLN
GKDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLN
EALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPHGNGQRA
CIGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'                                              HEM 
3 ethenylbenzene                                                                 SYN 
4 'OXYGEN MOLECULE'                                                              OXY 
5 '(2S)-2-[[(2S)-1-heptylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid' D0L 
6 GLYCEROL                                                                       GOL 
7 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   THR n 
1 3   ILE n 
1 4   LYS n 
1 5   GLU n 
1 6   MET n 
1 7   PRO n 
1 8   GLN n 
1 9   PRO n 
1 10  LYS n 
1 11  THR n 
1 12  PHE n 
1 13  GLY n 
1 14  GLU n 
1 15  LEU n 
1 16  LYS n 
1 17  ASN n 
1 18  LEU n 
1 19  PRO n 
1 20  LEU n 
1 21  LEU n 
1 22  ASN n 
1 23  THR n 
1 24  ASP n 
1 25  LYS n 
1 26  PRO n 
1 27  VAL n 
1 28  GLN n 
1 29  ALA n 
1 30  LEU n 
1 31  MET n 
1 32  LYS n 
1 33  ILE n 
1 34  ALA n 
1 35  ASP n 
1 36  GLU n 
1 37  LEU n 
1 38  GLY n 
1 39  GLU n 
1 40  ILE n 
1 41  PHE n 
1 42  LYS n 
1 43  PHE n 
1 44  GLU n 
1 45  ALA n 
1 46  PRO n 
1 47  GLY n 
1 48  ARG n 
1 49  VAL n 
1 50  THR n 
1 51  ARG n 
1 52  TYR n 
1 53  LEU n 
1 54  SER n 
1 55  SER n 
1 56  GLN n 
1 57  ARG n 
1 58  LEU n 
1 59  ILE n 
1 60  LYS n 
1 61  GLU n 
1 62  ALA n 
1 63  CYS n 
1 64  ASP n 
1 65  GLU n 
1 66  SER n 
1 67  ARG n 
1 68  PHE n 
1 69  ASP n 
1 70  LYS n 
1 71  ASN n 
1 72  LEU n 
1 73  SER n 
1 74  GLN n 
1 75  ALA n 
1 76  LEU n 
1 77  LYS n 
1 78  PHE n 
1 79  VAL n 
1 80  ARG n 
1 81  ASP n 
1 82  PHE n 
1 83  ALA n 
1 84  GLY n 
1 85  ASP n 
1 86  GLY n 
1 87  LEU n 
1 88  ALA n 
1 89  THR n 
1 90  SER n 
1 91  TRP n 
1 92  THR n 
1 93  HIS n 
1 94  GLU n 
1 95  LYS n 
1 96  ASN n 
1 97  TRP n 
1 98  LYS n 
1 99  LYS n 
1 100 ALA n 
1 101 HIS n 
1 102 ASN n 
1 103 ILE n 
1 104 LEU n 
1 105 LEU n 
1 106 PRO n 
1 107 SER n 
1 108 PHE n 
1 109 SER n 
1 110 GLN n 
1 111 GLN n 
1 112 ALA n 
1 113 MET n 
1 114 LYS n 
1 115 GLY n 
1 116 TYR n 
1 117 HIS n 
1 118 ALA n 
1 119 MET n 
1 120 MET n 
1 121 VAL n 
1 122 ASP n 
1 123 ILE n 
1 124 ALA n 
1 125 VAL n 
1 126 GLN n 
1 127 LEU n 
1 128 VAL n 
1 129 GLN n 
1 130 LYS n 
1 131 TRP n 
1 132 GLU n 
1 133 ARG n 
1 134 LEU n 
1 135 ASN n 
1 136 ALA n 
1 137 ASP n 
1 138 GLU n 
1 139 HIS n 
1 140 ILE n 
1 141 GLU n 
1 142 VAL n 
1 143 PRO n 
1 144 GLU n 
1 145 ASP n 
1 146 MET n 
1 147 THR n 
1 148 ARG n 
1 149 LEU n 
1 150 THR n 
1 151 LEU n 
1 152 ASP n 
1 153 THR n 
1 154 ILE n 
1 155 GLY n 
1 156 LEU n 
1 157 CYS n 
1 158 GLY n 
1 159 PHE n 
1 160 ASN n 
1 161 TYR n 
1 162 ARG n 
1 163 PHE n 
1 164 ASN n 
1 165 SER n 
1 166 PHE n 
1 167 TYR n 
1 168 ARG n 
1 169 ASP n 
1 170 GLN n 
1 171 PRO n 
1 172 HIS n 
1 173 PRO n 
1 174 PHE n 
1 175 ILE n 
1 176 THR n 
1 177 SER n 
1 178 MET n 
1 179 VAL n 
1 180 ARG n 
1 181 ALA n 
1 182 LEU n 
1 183 ASP n 
1 184 GLU n 
1 185 ALA n 
1 186 MET n 
1 187 ASN n 
1 188 LYS n 
1 189 LEU n 
1 190 GLN n 
1 191 ARG n 
1 192 ALA n 
1 193 ASN n 
1 194 PRO n 
1 195 ASP n 
1 196 ASP n 
1 197 PRO n 
1 198 ALA n 
1 199 TYR n 
1 200 ASP n 
1 201 GLU n 
1 202 ASN n 
1 203 LYS n 
1 204 ARG n 
1 205 GLN n 
1 206 PHE n 
1 207 GLN n 
1 208 GLU n 
1 209 ASP n 
1 210 ILE n 
1 211 LYS n 
1 212 VAL n 
1 213 MET n 
1 214 ASN n 
1 215 ASP n 
1 216 LEU n 
1 217 VAL n 
1 218 ASP n 
1 219 LYS n 
1 220 ILE n 
1 221 ILE n 
1 222 ALA n 
1 223 ASP n 
1 224 ARG n 
1 225 LYS n 
1 226 ALA n 
1 227 SER n 
1 228 GLY n 
1 229 GLU n 
1 230 GLN n 
1 231 SER n 
1 232 ASP n 
1 233 ASP n 
1 234 LEU n 
1 235 LEU n 
1 236 THR n 
1 237 HIS n 
1 238 MET n 
1 239 LEU n 
1 240 ASN n 
1 241 GLY n 
1 242 LYS n 
1 243 ASP n 
1 244 PRO n 
1 245 GLU n 
1 246 THR n 
1 247 GLY n 
1 248 GLU n 
1 249 PRO n 
1 250 LEU n 
1 251 ASP n 
1 252 ASP n 
1 253 GLU n 
1 254 ASN n 
1 255 ILE n 
1 256 ARG n 
1 257 TYR n 
1 258 GLN n 
1 259 ILE n 
1 260 ILE n 
1 261 THR n 
1 262 PHE n 
1 263 LEU n 
1 264 ILE n 
1 265 ALA n 
1 266 GLY n 
1 267 HIS n 
1 268 GLU n 
1 269 THR n 
1 270 THR n 
1 271 SER n 
1 272 GLY n 
1 273 LEU n 
1 274 LEU n 
1 275 SER n 
1 276 PHE n 
1 277 ALA n 
1 278 LEU n 
1 279 TYR n 
1 280 PHE n 
1 281 LEU n 
1 282 VAL n 
1 283 LYS n 
1 284 ASN n 
1 285 PRO n 
1 286 HIS n 
1 287 VAL n 
1 288 LEU n 
1 289 GLN n 
1 290 LYS n 
1 291 ALA n 
1 292 ALA n 
1 293 GLU n 
1 294 GLU n 
1 295 ALA n 
1 296 ALA n 
1 297 ARG n 
1 298 VAL n 
1 299 LEU n 
1 300 VAL n 
1 301 ASP n 
1 302 PRO n 
1 303 VAL n 
1 304 PRO n 
1 305 SER n 
1 306 TYR n 
1 307 LYS n 
1 308 GLN n 
1 309 VAL n 
1 310 LYS n 
1 311 GLN n 
1 312 LEU n 
1 313 LYS n 
1 314 TYR n 
1 315 VAL n 
1 316 GLY n 
1 317 MET n 
1 318 VAL n 
1 319 LEU n 
1 320 ASN n 
1 321 GLU n 
1 322 ALA n 
1 323 LEU n 
1 324 ARG n 
1 325 LEU n 
1 326 TRP n 
1 327 PRO n 
1 328 THR n 
1 329 ALA n 
1 330 PRO n 
1 331 ALA n 
1 332 PHE n 
1 333 SER n 
1 334 LEU n 
1 335 TYR n 
1 336 ALA n 
1 337 LYS n 
1 338 GLU n 
1 339 ASP n 
1 340 THR n 
1 341 VAL n 
1 342 LEU n 
1 343 GLY n 
1 344 GLY n 
1 345 GLU n 
1 346 TYR n 
1 347 PRO n 
1 348 LEU n 
1 349 GLU n 
1 350 LYS n 
1 351 GLY n 
1 352 ASP n 
1 353 GLU n 
1 354 LEU n 
1 355 MET n 
1 356 VAL n 
1 357 LEU n 
1 358 ILE n 
1 359 PRO n 
1 360 GLN n 
1 361 LEU n 
1 362 HIS n 
1 363 ARG n 
1 364 ASP n 
1 365 LYS n 
1 366 THR n 
1 367 ILE n 
1 368 TRP n 
1 369 GLY n 
1 370 ASP n 
1 371 ASP n 
1 372 VAL n 
1 373 GLU n 
1 374 GLU n 
1 375 PHE n 
1 376 ARG n 
1 377 PRO n 
1 378 GLU n 
1 379 ARG n 
1 380 PHE n 
1 381 GLU n 
1 382 ASN n 
1 383 PRO n 
1 384 SER n 
1 385 ALA n 
1 386 ILE n 
1 387 PRO n 
1 388 GLN n 
1 389 HIS n 
1 390 ALA n 
1 391 PHE n 
1 392 LYS n 
1 393 PRO n 
1 394 HIS n 
1 395 GLY n 
1 396 ASN n 
1 397 GLY n 
1 398 GLN n 
1 399 ARG n 
1 400 ALA n 
1 401 CYS n 
1 402 ILE n 
1 403 GLY n 
1 404 GLN n 
1 405 GLN n 
1 406 PHE n 
1 407 ALA n 
1 408 LEU n 
1 409 HIS n 
1 410 GLU n 
1 411 ALA n 
1 412 THR n 
1 413 LEU n 
1 414 VAL n 
1 415 LEU n 
1 416 GLY n 
1 417 MET n 
1 418 MET n 
1 419 LEU n 
1 420 LYS n 
1 421 HIS n 
1 422 PHE n 
1 423 ASP n 
1 424 PHE n 
1 425 GLU n 
1 426 ASP n 
1 427 HIS n 
1 428 THR n 
1 429 ASN n 
1 430 TYR n 
1 431 GLU n 
1 432 LEU n 
1 433 ASP n 
1 434 ILE n 
1 435 LYS n 
1 436 GLU n 
1 437 THR n 
1 438 LEU n 
1 439 THR n 
1 440 LEU n 
1 441 LYS n 
1 442 PRO n 
1 443 GLU n 
1 444 GLY n 
1 445 PHE n 
1 446 VAL n 
1 447 VAL n 
1 448 LYS n 
1 449 ALA n 
1 450 LYS n 
1 451 SER n 
1 452 LYS n 
1 453 LYS n 
1 454 ILE n 
1 455 PRO n 
1 456 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   456 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'cyp102A1, cyp102, BG04_163' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    'ATCC 14581/NBRC 15308' 
_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      'Priestia megaterium NBRC 15308 = ATCC 14581' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1348623 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                        ? 'C3 H7 N O2'       
89.093  
ARG 'L-peptide linking' y ARGININE                                                                       ? 'C6 H15 N4 O2 1'   
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                     ? 'C4 H8 N2 O3'      
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                ? 'C4 H7 N O4'       
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                       ? 'C3 H7 N O2 S'     
121.158 
D0L non-polymer         . '(2S)-2-[[(2S)-1-heptylpyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic acid' ? 'C21 H32 N2 O3'    
360.490 
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  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                              HEME 'C34 H32 Fe N4 O4' 
616.487 
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 
OXY non-polymer         . 'OXYGEN MOLECULE'                                                              ? O2                 
31.999  
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 
SYN non-polymer         . ethenylbenzene                                                                 styrene 'C8 H8' 104.149 
THR 'L-peptide linking' y THREONINE                                                                      ? 'C4 H9 N O3'       
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                     ? 'C11 H12 N2 O2'    
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                       ? 'C9 H11 N O3'      
181.189 
VAL 'L-peptide linking' y VALINE                                                                         ? 'C5 H11 N O2'      
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   A . n 
A 1 2   THR 2   1   1   THR THR A . n 
A 1 3   ILE 3   2   2   ILE ILE A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   GLU 5   4   4   GLU GLU A . n 
A 1 6   MET 6   5   5   MET MET A . n 
A 1 7   PRO 7   6   6   PRO PRO A . n 
A 1 8   GLN 8   7   7   GLN GLN A . n 
A 1 9   PRO 9   8   8   PRO PRO A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  THR 11  10  10  THR THR A . n 
A 1 12  PHE 12  11  11  PHE PHE A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  GLU 14  13  13  GLU GLU A . n 
A 1 15  LEU 15  14  14  LEU LEU A . n 
A 1 16  LYS 16  15  15  LYS LYS A . n 
A 1 17  ASN 17  16  16  ASN ASN A . n 
A 1 18  LEU 18  17  17  LEU LEU A . n 
A 1 19  PRO 19  18  18  PRO PRO A . n 
A 1 20  LEU 20  19  19  LEU LEU A . n 
A 1 21  LEU 21  20  20  LEU LEU A . n 
A 1 22  ASN 22  21  21  ASN ASN A . n 
A 1 23  THR 23  22  22  THR THR A . n 
A 1 24  ASP 24  23  23  ASP ASP A . n 
A 1 25  LYS 25  24  24  LYS LYS A . n 
A 1 26  PRO 26  25  25  PRO PRO A . n 
A 1 27  VAL 27  26  26  VAL VAL A . n 
A 1 28  GLN 28  27  27  GLN GLN A . n 
A 1 29  ALA 29  28  28  ALA ALA A . n 
A 1 30  LEU 30  29  29  LEU LEU A . n 
A 1 31  MET 31  30  30  MET MET A . n 
A 1 32  LYS 32  31  31  LYS LYS A . n 
A 1 33  ILE 33  32  32  ILE ILE A . n 
A 1 34  ALA 34  33  33  ALA ALA A . n 
A 1 35  ASP 35  34  34  ASP ASP A . n 
A 1 36  GLU 36  35  35  GLU GLU A . n 
A 1 37  LEU 37  36  36  LEU LEU A . n 
A 1 38  GLY 38  37  37  GLY GLY A . n 
A 1 39  GLU 39  38  38  GLU GLU A . n 
A 1 40  ILE 40  39  39  ILE ILE A . n 
A 1 41  PHE 41  40  40  PHE PHE A . n 
A 1 42  LYS 42  41  41  LYS LYS A . n 
A 1 43  PHE 43  42  42  PHE PHE A . n 
A 1 44  GLU 44  43  43  GLU GLU A . n 
A 1 45  ALA 45  44  44  ALA ALA A . n 
A 1 46  PRO 46  45  45  PRO PRO A . n 
A 1 47  GLY 47  46  46  GLY GLY A . n 
A 1 48  ARG 48  47  47  ARG ARG A . n 
A 1 49  VAL 49  48  48  VAL VAL A . n 
A 1 50  THR 50  49  49  THR THR A . n 
A 1 51  ARG 51  50  50  ARG ARG A . n 
A 1 52  TYR 52  51  51  TYR TYR A . n 
A 1 53  LEU 53  52  52  LEU LEU A . n 
A 1 54  SER 54  53  53  SER SER A . n 
A 1 55  SER 55  54  54  SER SER A . n 
A 1 56  GLN 56  55  55  GLN GLN A . n 
A 1 57  ARG 57  56  56  ARG ARG A . n 
A 1 58  LEU 58  57  57  LEU LEU A . n 
A 1 59  ILE 59  58  58  ILE ILE A . n 
A 1 60  LYS 60  59  59  LYS LYS A . n 
A 1 61  GLU 61  60  60  GLU GLU A . n 
A 1 62  ALA 62  61  61  ALA ALA A . n 
A 1 63  CYS 63  62  62  CYS CYS A . n 
A 1 64  ASP 64  63  63  ASP ASP A . n 
A 1 65  GLU 65  64  64  GLU GLU A . n 
A 1 66  SER 66  65  65  SER SER A . n 
A 1 67  ARG 67  66  66  ARG ARG A . n 
A 1 68  PHE 68  67  67  PHE PHE A . n 
A 1 69  ASP 69  68  68  ASP ASP A . n 
A 1 70  LYS 70  69  69  LYS LYS A . n 
A 1 71  ASN 71  70  70  ASN ASN A . n 
A 1 72  LEU 72  71  71  LEU LEU A . n 
A 1 73  SER 73  72  72  SER SER A . n 
A 1 74  GLN 74  73  73  GLN GLN A . n 
A 1 75  ALA 75  74  74  ALA ALA A . n 
A 1 76  LEU 76  75  75  LEU LEU A . n 
A 1 77  LYS 77  76  76  LYS LYS A . n 
A 1 78  PHE 78  77  77  PHE PHE A . n 
A 1 79  VAL 79  78  78  VAL VAL A . n 
A 1 80  ARG 80  79  79  ARG ARG A . n 
A 1 81  ASP 81  80  80  ASP ASP A . n 
A 1 82  PHE 82  81  81  PHE PHE A . n 
A 1 83  ALA 83  82  82  ALA ALA A . n 
A 1 84  GLY 84  83  83  GLY GLY A . n 
A 1 85  ASP 85  84  84  ASP ASP A . n 
A 1 86  GLY 86  85  85  GLY GLY A . n 
A 1 87  LEU 87  86  86  LEU LEU A . n 
A 1 88  ALA 88  87  87  ALA ALA A . n 
A 1 89  THR 89  88  88  THR THR A . n 
A 1 90  SER 90  89  89  SER SER A . n 
A 1 91  TRP 91  90  90  TRP TRP A . n 
A 1 92  THR 92  91  91  THR THR A . n 
A 1 93  HIS 93  92  92  HIS HIS A . n 
A 1 94  GLU 94  93  93  GLU GLU A . n 
A 1 95  LYS 95  94  94  LYS LYS A . n 
A 1 96  ASN 96  95  95  ASN ASN A . n 
A 1 97  TRP 97  96  96  TRP TRP A . n 
A 1 98  LYS 98  97  97  LYS LYS A . n 
A 1 99  LYS 99  98  98  LYS LYS A . n 
A 1 100 ALA 100 99  99  ALA ALA A . n 
A 1 101 HIS 101 100 100 HIS HIS A . n 
A 1 102 ASN 102 101 101 ASN ASN A . n 
A 1 103 ILE 103 102 102 ILE ILE A . n 
A 1 104 LEU 104 103 103 LEU LEU A . n 
A 1 105 LEU 105 104 104 LEU LEU A . n 
A 1 106 PRO 106 105 105 PRO PRO A . n 
A 1 107 SER 107 106 106 SER SER A . n 
A 1 108 PHE 108 107 107 PHE PHE A . n 
A 1 109 SER 109 108 108 SER SER A . n 
A 1 110 GLN 110 109 109 GLN GLN A . n 
A 1 111 GLN 111 110 110 GLN GLN A . n 
A 1 112 ALA 112 111 111 ALA ALA A . n 
A 1 113 MET 113 112 112 MET MET A . n 
A 1 114 LYS 114 113 113 LYS LYS A . n 
A 1 115 GLY 115 114 114 GLY GLY A . n 
A 1 116 TYR 116 115 115 TYR TYR A . n 
A 1 117 HIS 117 116 116 HIS HIS A . n 
A 1 118 ALA 118 117 117 ALA ALA A . n 
A 1 119 MET 119 118 118 MET MET A . n 
A 1 120 MET 120 119 119 MET MET A . n 
A 1 121 VAL 121 120 120 VAL VAL A . n 
A 1 122 ASP 122 121 121 ASP ASP A . n 
A 1 123 ILE 123 122 122 ILE ILE A . n 
A 1 124 ALA 124 123 123 ALA ALA A . n 
A 1 125 VAL 125 124 124 VAL VAL A . n 
A 1 126 GLN 126 125 125 GLN GLN A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 VAL 128 127 127 VAL VAL A . n 
A 1 129 GLN 129 128 128 GLN GLN A . n 
A 1 130 LYS 130 129 129 LYS LYS A . n 
A 1 131 TRP 131 130 130 TRP TRP A . n 
A 1 132 GLU 132 131 131 GLU GLU A . n 
A 1 133 ARG 133 132 132 ARG ARG A . n 
A 1 134 LEU 134 133 133 LEU LEU A . n 
A 1 135 ASN 135 134 134 ASN ASN A . n 
A 1 136 ALA 136 135 135 ALA ALA A . n 
A 1 137 ASP 137 136 136 ASP ASP A . n 
A 1 138 GLU 138 137 137 GLU GLU A . n 
A 1 139 HIS 139 138 138 HIS HIS A . n 
A 1 140 ILE 140 139 139 ILE ILE A . n 
A 1 141 GLU 141 140 140 GLU GLU A . n 
A 1 142 VAL 142 141 141 VAL VAL A . n 
A 1 143 PRO 143 142 142 PRO PRO A . n 
A 1 144 GLU 144 143 143 GLU GLU A . n 
A 1 145 ASP 145 144 144 ASP ASP A . n 
A 1 146 MET 146 145 145 MET MET A . n 
A 1 147 THR 147 146 146 THR THR A . n 
A 1 148 ARG 148 147 147 ARG ARG A . n 
A 1 149 LEU 149 148 148 LEU LEU A . n 
A 1 150 THR 150 149 149 THR THR A . n 
A 1 151 LEU 151 150 150 LEU LEU A . n 
A 1 152 ASP 152 151 151 ASP ASP A . n 
A 1 153 THR 153 152 152 THR THR A . n 
A 1 154 ILE 154 153 153 ILE ILE A . n 
A 1 155 GLY 155 154 154 GLY GLY A . n 
A 1 156 LEU 156 155 155 LEU LEU A . n 
A 1 157 CYS 157 156 156 CYS CYS A . n 
A 1 158 GLY 158 157 157 GLY GLY A . n 
A 1 159 PHE 159 158 158 PHE PHE A . n 
A 1 160 ASN 160 159 159 ASN ASN A . n 
A 1 161 TYR 161 160 160 TYR TYR A . n 
A 1 162 ARG 162 161 161 ARG ARG A . n 
A 1 163 PHE 163 162 162 PHE PHE A . n 
A 1 164 ASN 164 163 163 ASN ASN A . n 
A 1 165 SER 165 164 164 SER SER A . n 
A 1 166 PHE 166 165 165 PHE PHE A . n 
A 1 167 TYR 167 166 166 TYR TYR A . n 
A 1 168 ARG 168 167 167 ARG ARG A . n 
A 1 169 ASP 169 168 168 ASP ASP A . n 
A 1 170 GLN 170 169 169 GLN GLN A . n 
A 1 171 PRO 171 170 170 PRO PRO A . n 
A 1 172 HIS 172 171 171 HIS HIS A . n 
A 1 173 PRO 173 172 172 PRO PRO A . n 
A 1 174 PHE 174 173 173 PHE PHE A . n 
A 1 175 ILE 175 174 174 ILE ILE A . n 
A 1 176 THR 176 175 175 THR THR A . n 
A 1 177 SER 177 176 176 SER SER A . n 
A 1 178 MET 178 177 177 MET MET A . n 
A 1 179 VAL 179 178 178 VAL VAL A . n 
A 1 180 ARG 180 179 179 ARG ARG A . n 
A 1 181 ALA 181 180 180 ALA ALA A . n 
A 1 182 LEU 182 181 181 LEU LEU A . n 
A 1 183 ASP 183 182 182 ASP ASP A . n 
A 1 184 GLU 184 183 183 GLU GLU A . n 
A 1 185 ALA 185 184 184 ALA ALA A . n 
A 1 186 MET 186 185 185 MET MET A . n 
A 1 187 ASN 187 186 186 ASN ASN A . n 
A 1 188 LYS 188 187 187 LYS LYS A . n 
A 1 189 LEU 189 188 188 LEU LEU A . n 
A 1 190 GLN 190 189 189 GLN GLN A . n 
A 1 191 ARG 191 190 190 ARG ARG A . n 
A 1 192 ALA 192 191 191 ALA ALA A . n 
A 1 193 ASN 193 192 192 ASN ASN A . n 
A 1 194 PRO 194 193 193 PRO PRO A . n 
A 1 195 ASP 195 194 194 ASP ASP A . n 
A 1 196 ASP 196 195 195 ASP ASP A . n 
A 1 197 PRO 197 196 196 PRO PRO A . n 
A 1 198 ALA 198 197 197 ALA ALA A . n 
A 1 199 TYR 199 198 198 TYR TYR A . n 
A 1 200 ASP 200 199 199 ASP ASP A . n 
A 1 201 GLU 201 200 200 GLU GLU A . n 
A 1 202 ASN 202 201 201 ASN ASN A . n 
A 1 203 LYS 203 202 202 LYS LYS A . n 
A 1 204 ARG 204 203 203 ARG ARG A . n 
A 1 205 GLN 205 204 204 GLN GLN A . n 
A 1 206 PHE 206 205 205 PHE PHE A . n 
A 1 207 GLN 207 206 206 GLN GLN A . n 
A 1 208 GLU 208 207 207 GLU GLU A . n 
A 1 209 ASP 209 208 208 ASP ASP A . n 
A 1 210 ILE 210 209 209 ILE ILE A . n 
A 1 211 LYS 211 210 210 LYS LYS A . n 
A 1 212 VAL 212 211 211 VAL VAL A . n 
A 1 213 MET 213 212 212 MET MET A . n 
A 1 214 ASN 214 213 213 ASN ASN A . n 
A 1 215 ASP 215 214 214 ASP ASP A . n 
A 1 216 LEU 216 215 215 LEU LEU A . n 
A 1 217 VAL 217 216 216 VAL VAL A . n 
A 1 218 ASP 218 217 217 ASP ASP A . n 
A 1 219 LYS 219 218 218 LYS LYS A . n 
A 1 220 ILE 220 219 219 ILE ILE A . n 
A 1 221 ILE 221 220 220 ILE ILE A . n 
A 1 222 ALA 222 221 221 ALA ALA A . n 
A 1 223 ASP 223 222 222 ASP ASP A . n 
A 1 224 ARG 224 223 223 ARG ARG A . n 
A 1 225 LYS 225 224 224 LYS LYS A . n 
A 1 226 ALA 226 225 225 ALA ALA A . n 
A 1 227 SER 227 226 226 SER SER A . n 
A 1 228 GLY 228 227 227 GLY GLY A . n 
A 1 229 GLU 229 228 228 GLU GLU A . n 
A 1 230 GLN 230 229 229 GLN GLN A . n 
A 1 231 SER 231 230 230 SER SER A . n 
A 1 232 ASP 232 231 231 ASP ASP A . n 
A 1 233 ASP 233 232 232 ASP ASP A . n 
A 1 234 LEU 234 233 233 LEU LEU A . n 
A 1 235 LEU 235 234 234 LEU LEU A . n 
A 1 236 THR 236 235 235 THR THR A . n 
A 1 237 HIS 237 236 236 HIS HIS A . n 
A 1 238 MET 238 237 237 MET MET A . n 
A 1 239 LEU 239 238 238 LEU LEU A . n 
A 1 240 ASN 240 239 239 ASN ASN A . n 
A 1 241 GLY 241 240 240 GLY GLY A . n 
A 1 242 LYS 242 241 241 LYS LYS A . n 
A 1 243 ASP 243 242 242 ASP ASP A . n 
A 1 244 PRO 244 243 243 PRO PRO A . n 
A 1 245 GLU 245 244 244 GLU GLU A . n 
A 1 246 THR 246 245 245 THR THR A . n 
A 1 247 GLY 247 246 246 GLY GLY A . n 
A 1 248 GLU 248 247 247 GLU GLU A . n 
A 1 249 PRO 249 248 248 PRO PRO A . n 
A 1 250 LEU 250 249 249 LEU LEU A . n 
A 1 251 ASP 251 250 250 ASP ASP A . n 
A 1 252 ASP 252 251 251 ASP ASP A . n 
A 1 253 GLU 253 252 252 GLU GLU A . n 
A 1 254 ASN 254 253 253 ASN ASN A . n 
A 1 255 ILE 255 254 254 ILE ILE A . n 
A 1 256 ARG 256 255 255 ARG ARG A . n 
A 1 257 TYR 257 256 256 TYR TYR A . n 
A 1 258 GLN 258 257 257 GLN GLN A . n 
A 1 259 ILE 259 258 258 ILE ILE A . n 
A 1 260 ILE 260 259 259 ILE ILE A . n 
A 1 261 THR 261 260 260 THR THR A . n 
A 1 262 PHE 262 261 261 PHE PHE A . n 
A 1 263 LEU 263 262 262 LEU LEU A . n 
A 1 264 ILE 264 263 263 ILE ILE A . n 
A 1 265 ALA 265 264 264 ALA ALA A . n 
A 1 266 GLY 266 265 265 GLY GLY A . n 
A 1 267 HIS 267 266 266 HIS HIS A . n 
A 1 268 GLU 268 267 267 GLU GLU A . n 
A 1 269 THR 269 268 268 THR THR A . n 
A 1 270 THR 270 269 269 THR THR A . n 
A 1 271 SER 271 270 270 SER SER A . n 
A 1 272 GLY 272 271 271 GLY GLY A . n 
A 1 273 LEU 273 272 272 LEU LEU A . n 
A 1 274 LEU 274 273 273 LEU LEU A . n 
A 1 275 SER 275 274 274 SER SER A . n 
A 1 276 PHE 276 275 275 PHE PHE A . n 
A 1 277 ALA 277 276 276 ALA ALA A . n 
A 1 278 LEU 278 277 277 LEU LEU A . n 
A 1 279 TYR 279 278 278 TYR TYR A . n 
A 1 280 PHE 280 279 279 PHE PHE A . n 
A 1 281 LEU 281 280 280 LEU LEU A . n 
A 1 282 VAL 282 281 281 VAL VAL A . n 
A 1 283 LYS 283 282 282 LYS LYS A . n 
A 1 284 ASN 284 283 283 ASN ASN A . n 
A 1 285 PRO 285 284 284 PRO PRO A . n 
A 1 286 HIS 286 285 285 HIS HIS A . n 
A 1 287 VAL 287 286 286 VAL VAL A . n 
A 1 288 LEU 288 287 287 LEU LEU A . n 
A 1 289 GLN 289 288 288 GLN GLN A . n 
A 1 290 LYS 290 289 289 LYS LYS A . n 
A 1 291 ALA 291 290 290 ALA ALA A . n 
A 1 292 ALA 292 291 291 ALA ALA A . n 
A 1 293 GLU 293 292 292 GLU GLU A . n 
A 1 294 GLU 294 293 293 GLU GLU A . n 
A 1 295 ALA 295 294 294 ALA ALA A . n 
A 1 296 ALA 296 295 295 ALA ALA A . n 
A 1 297 ARG 297 296 296 ARG ARG A . n 
A 1 298 VAL 298 297 297 VAL VAL A . n 
A 1 299 LEU 299 298 298 LEU LEU A . n 
A 1 300 VAL 300 299 299 VAL VAL A . n 
A 1 301 ASP 301 300 300 ASP ASP A . n 
A 1 302 PRO 302 301 301 PRO PRO A . n 
A 1 303 VAL 303 302 302 VAL VAL A . n 
A 1 304 PRO 304 303 303 PRO PRO A . n 
A 1 305 SER 305 304 304 SER SER A . n 
A 1 306 TYR 306 305 305 TYR TYR A . n 
A 1 307 LYS 307 306 306 LYS LYS A . n 
A 1 308 GLN 308 307 307 GLN GLN A . n 
A 1 309 VAL 309 308 308 VAL VAL A . n 
A 1 310 LYS 310 309 309 LYS LYS A . n 
A 1 311 GLN 311 310 310 GLN GLN A . n 
A 1 312 LEU 312 311 311 LEU LEU A . n 
A 1 313 LYS 313 312 312 LYS LYS A . n 
A 1 314 TYR 314 313 313 TYR TYR A . n 
A 1 315 VAL 315 314 314 VAL VAL A . n 
A 1 316 GLY 316 315 315 GLY GLY A . n 
A 1 317 MET 317 316 316 MET MET A . n 
A 1 318 VAL 318 317 317 VAL VAL A . n 
A 1 319 LEU 319 318 318 LEU LEU A . n 
A 1 320 ASN 320 319 319 ASN ASN A . n 
A 1 321 GLU 321 320 320 GLU GLU A . n 
A 1 322 ALA 322 321 321 ALA ALA A . n 
A 1 323 LEU 323 322 322 LEU LEU A . n 
A 1 324 ARG 324 323 323 ARG ARG A . n 
A 1 325 LEU 325 324 324 LEU LEU A . n 
A 1 326 TRP 326 325 325 TRP TRP A . n 
A 1 327 PRO 327 326 326 PRO PRO A . n 
A 1 328 THR 328 327 327 THR THR A . n 
A 1 329 ALA 329 328 328 ALA ALA A . n 
A 1 330 PRO 330 329 329 PRO PRO A . n 
A 1 331 ALA 331 330 330 ALA ALA A . n 
A 1 332 PHE 332 331 331 PHE PHE A . n 
A 1 333 SER 333 332 332 SER SER A . n 
A 1 334 LEU 334 333 333 LEU LEU A . n 
A 1 335 TYR 335 334 334 TYR TYR A . n 
A 1 336 ALA 336 335 335 ALA ALA A . n 
A 1 337 LYS 337 336 336 LYS LYS A . n 
A 1 338 GLU 338 337 337 GLU GLU A . n 
A 1 339 ASP 339 338 338 ASP ASP A . n 
A 1 340 THR 340 339 339 THR THR A . n 
A 1 341 VAL 341 340 340 VAL VAL A . n 
A 1 342 LEU 342 341 341 LEU LEU A . n 
A 1 343 GLY 343 342 342 GLY GLY A . n 
A 1 344 GLY 344 343 343 GLY GLY A . n 
A 1 345 GLU 345 344 344 GLU GLU A . n 
A 1 346 TYR 346 345 345 TYR TYR A . n 
A 1 347 PRO 347 346 346 PRO PRO A . n 
A 1 348 LEU 348 347 347 LEU LEU A . n 
A 1 349 GLU 349 348 348 GLU GLU A . n 
A 1 350 LYS 350 349 349 LYS LYS A . n 
A 1 351 GLY 351 350 350 GLY GLY A . n 
A 1 352 ASP 352 351 351 ASP ASP A . n 
A 1 353 GLU 353 352 352 GLU GLU A . n 
A 1 354 LEU 354 353 353 LEU LEU A . n 
A 1 355 MET 355 354 354 MET MET A . n 
A 1 356 VAL 356 355 355 VAL VAL A . n 
A 1 357 LEU 357 356 356 LEU LEU A . n 
A 1 358 ILE 358 357 357 ILE ILE A . n 
A 1 359 PRO 359 358 358 PRO PRO A . n 
A 1 360 GLN 360 359 359 GLN GLN A . n 
A 1 361 LEU 361 360 360 LEU LEU A . n 
A 1 362 HIS 362 361 361 HIS HIS A . n 
A 1 363 ARG 363 362 362 ARG ARG A . n 
A 1 364 ASP 364 363 363 ASP ASP A . n 
A 1 365 LYS 365 364 364 LYS LYS A . n 
A 1 366 THR 366 365 365 THR THR A . n 
A 1 367 ILE 367 366 366 ILE ILE A . n 
A 1 368 TRP 368 367 367 TRP TRP A . n 
A 1 369 GLY 369 368 368 GLY GLY A . n 
A 1 370 ASP 370 369 369 ASP ASP A . n 
A 1 371 ASP 371 370 370 ASP ASP A . n 
A 1 372 VAL 372 371 371 VAL VAL A . n 
A 1 373 GLU 373 372 372 GLU GLU A . n 
A 1 374 GLU 374 373 373 GLU GLU A . n 
A 1 375 PHE 375 374 374 PHE PHE A . n 
A 1 376 ARG 376 375 375 ARG ARG A . n 
A 1 377 PRO 377 376 376 PRO PRO A . n 
A 1 378 GLU 378 377 377 GLU GLU A . n 
A 1 379 ARG 379 378 378 ARG ARG A . n 
A 1 380 PHE 380 379 379 PHE PHE A . n 
A 1 381 GLU 381 380 380 GLU GLU A . n 
A 1 382 ASN 382 381 381 ASN ASN A . n 
A 1 383 PRO 383 382 382 PRO PRO A . n 
A 1 384 SER 384 383 383 SER SER A . n 
A 1 385 ALA 385 384 384 ALA ALA A . n 
A 1 386 ILE 386 385 385 ILE ILE A . n 
A 1 387 PRO 387 386 386 PRO PRO A . n 
A 1 388 GLN 388 387 387 GLN GLN A . n 
A 1 389 HIS 389 388 388 HIS HIS A . n 
A 1 390 ALA 390 389 389 ALA ALA A . n 
A 1 391 PHE 391 390 390 PHE PHE A . n 
A 1 392 LYS 392 391 391 LYS LYS A . n 
A 1 393 PRO 393 392 392 PRO PRO A . n 
A 1 394 HIS 394 393 393 HIS HIS A . n 
A 1 395 GLY 395 394 394 GLY GLY A . n 
A 1 396 ASN 396 395 395 ASN ASN A . n 
A 1 397 GLY 397 396 396 GLY GLY A . n 
A 1 398 GLN 398 397 397 GLN GLN A . n 
A 1 399 ARG 399 398 398 ARG ARG A . n 
A 1 400 ALA 400 399 399 ALA ALA A . n 
A 1 401 CYS 401 400 400 CYS CYS A . n 
A 1 402 ILE 402 401 401 ILE ILE A . n 
A 1 403 GLY 403 402 402 GLY GLY A . n 
A 1 404 GLN 404 403 403 GLN GLN A . n 
A 1 405 GLN 405 404 404 GLN GLN A . n 
A 1 406 PHE 406 405 405 PHE PHE A . n 
A 1 407 ALA 407 406 406 ALA ALA A . n 
A 1 408 LEU 408 407 407 LEU LEU A . n 
A 1 409 HIS 409 408 408 HIS HIS A . n 
A 1 410 GLU 410 409 409 GLU GLU A . n 
A 1 411 ALA 411 410 410 ALA ALA A . n 
A 1 412 THR 412 411 411 THR THR A . n 
A 1 413 LEU 413 412 412 LEU LEU A . n 
A 1 414 VAL 414 413 413 VAL VAL A . n 
A 1 415 LEU 415 414 414 LEU LEU A . n 
A 1 416 GLY 416 415 415 GLY GLY A . n 
A 1 417 MET 417 416 416 MET MET A . n 
A 1 418 MET 418 417 417 MET MET A . n 
A 1 419 LEU 419 418 418 LEU LEU A . n 
A 1 420 LYS 420 419 419 LYS LYS A . n 
A 1 421 HIS 421 420 420 HIS HIS A . n 
A 1 422 PHE 422 421 421 PHE PHE A . n 
A 1 423 ASP 423 422 422 ASP ASP A . n 
A 1 424 PHE 424 423 423 PHE PHE A . n 
A 1 425 GLU 425 424 424 GLU GLU A . n 
A 1 426 ASP 426 425 425 ASP ASP A . n 
A 1 427 HIS 427 426 426 HIS HIS A . n 
A 1 428 THR 428 427 427 THR THR A . n 
A 1 429 ASN 429 428 428 ASN ASN A . n 
A 1 430 TYR 430 429 429 TYR TYR A . n 
A 1 431 GLU 431 430 430 GLU GLU A . n 
A 1 432 LEU 432 431 431 LEU LEU A . n 
A 1 433 ASP 433 432 432 ASP ASP A . n 
A 1 434 ILE 434 433 433 ILE ILE A . n 
A 1 435 LYS 435 434 434 LYS LYS A . n 
A 1 436 GLU 436 435 435 GLU GLU A . n 
A 1 437 THR 437 436 436 THR THR A . n 
A 1 438 LEU 438 437 437 LEU LEU A . n 
A 1 439 THR 439 438 438 THR THR A . n 
A 1 440 LEU 440 439 439 LEU LEU A . n 
A 1 441 LYS 441 440 440 LYS LYS A . n 
A 1 442 PRO 442 441 441 PRO PRO A . n 
A 1 443 GLU 443 442 442 GLU GLU A . n 
A 1 444 GLY 444 443 443 GLY GLY A . n 
A 1 445 PHE 445 444 444 PHE PHE A . n 
A 1 446 VAL 446 445 445 VAL VAL A . n 
A 1 447 VAL 447 446 446 VAL VAL A . n 
A 1 448 LYS 448 447 447 LYS LYS A . n 
A 1 449 ALA 449 448 448 ALA ALA A . n 
A 1 450 LYS 450 449 449 LYS LYS A . n 
A 1 451 SER 451 450 450 SER SER A . n 
A 1 452 LYS 452 451 451 LYS LYS A . n 
A 1 453 LYS 453 452 452 LYS LYS A . n 
A 1 454 ILE 454 453 453 ILE ILE A . n 
A 1 455 PRO 455 454 454 PRO PRO A . n 
A 1 456 LEU 456 455 455 LEU LEU A . n 
B 1 1   MET 1   0   ?   ?   ?   B . n 
B 1 2   THR 2   1   1   THR THR B . n 
B 1 3   ILE 3   2   2   ILE ILE B . n 
B 1 4   LYS 4   3   3   LYS LYS B . n 
B 1 5   GLU 5   4   4   GLU GLU B . n 
B 1 6   MET 6   5   5   MET MET B . n 
B 1 7   PRO 7   6   6   PRO PRO B . n 
B 1 8   GLN 8   7   7   GLN GLN B . n 
B 1 9   PRO 9   8   8   PRO PRO B . n 
B 1 10  LYS 10  9   9   LYS LYS B . n 
B 1 11  THR 11  10  10  THR THR B . n 
B 1 12  PHE 12  11  11  PHE PHE B . n 
B 1 13  GLY 13  12  12  GLY GLY B . n 
B 1 14  GLU 14  13  13  GLU GLU B . n 
B 1 15  LEU 15  14  14  LEU LEU B . n 
B 1 16  LYS 16  15  15  LYS LYS B . n 
B 1 17  ASN 17  16  16  ASN ASN B . n 
B 1 18  LEU 18  17  17  LEU LEU B . n 
B 1 19  PRO 19  18  18  PRO PRO B . n 
B 1 20  LEU 20  19  19  LEU LEU B . n 
B 1 21  LEU 21  20  20  LEU LEU B . n 
B 1 22  ASN 22  21  21  ASN ASN B . n 
B 1 23  THR 23  22  22  THR THR B . n 
B 1 24  ASP 24  23  23  ASP ASP B . n 
B 1 25  LYS 25  24  24  LYS LYS B . n 
B 1 26  PRO 26  25  25  PRO PRO B . n 
B 1 27  VAL 27  26  26  VAL VAL B . n 
B 1 28  GLN 28  27  27  GLN GLN B . n 
B 1 29  ALA 29  28  28  ALA ALA B . n 
B 1 30  LEU 30  29  29  LEU LEU B . n 
B 1 31  MET 31  30  30  MET MET B . n 
B 1 32  LYS 32  31  31  LYS LYS B . n 
B 1 33  ILE 33  32  32  ILE ILE B . n 
B 1 34  ALA 34  33  33  ALA ALA B . n 
B 1 35  ASP 35  34  34  ASP ASP B . n 
B 1 36  GLU 36  35  35  GLU GLU B . n 
B 1 37  LEU 37  36  36  LEU LEU B . n 
B 1 38  GLY 38  37  37  GLY GLY B . n 
B 1 39  GLU 39  38  38  GLU GLU B . n 
B 1 40  ILE 40  39  39  ILE ILE B . n 
B 1 41  PHE 41  40  40  PHE PHE B . n 
B 1 42  LYS 42  41  41  LYS LYS B . n 
B 1 43  PHE 43  42  42  PHE PHE B . n 
B 1 44  GLU 44  43  43  GLU GLU B . n 
B 1 45  ALA 45  44  44  ALA ALA B . n 
B 1 46  PRO 46  45  45  PRO PRO B . n 
B 1 47  GLY 47  46  46  GLY GLY B . n 
B 1 48  ARG 48  47  47  ARG ARG B . n 
B 1 49  VAL 49  48  48  VAL VAL B . n 
B 1 50  THR 50  49  49  THR THR B . n 
B 1 51  ARG 51  50  50  ARG ARG B . n 
B 1 52  TYR 52  51  51  TYR TYR B . n 
B 1 53  LEU 53  52  52  LEU LEU B . n 
B 1 54  SER 54  53  53  SER SER B . n 
B 1 55  SER 55  54  54  SER SER B . n 
B 1 56  GLN 56  55  55  GLN GLN B . n 
B 1 57  ARG 57  56  56  ARG ARG B . n 
B 1 58  LEU 58  57  57  LEU LEU B . n 
B 1 59  ILE 59  58  58  ILE ILE B . n 
B 1 60  LYS 60  59  59  LYS LYS B . n 
B 1 61  GLU 61  60  60  GLU GLU B . n 
B 1 62  ALA 62  61  61  ALA ALA B . n 
B 1 63  CYS 63  62  62  CYS CYS B . n 
B 1 64  ASP 64  63  63  ASP ASP B . n 
B 1 65  GLU 65  64  64  GLU GLU B . n 
B 1 66  SER 66  65  65  SER SER B . n 
B 1 67  ARG 67  66  66  ARG ARG B . n 
B 1 68  PHE 68  67  67  PHE PHE B . n 
B 1 69  ASP 69  68  68  ASP ASP B . n 
B 1 70  LYS 70  69  69  LYS LYS B . n 
B 1 71  ASN 71  70  70  ASN ASN B . n 
B 1 72  LEU 72  71  71  LEU LEU B . n 
B 1 73  SER 73  72  72  SER SER B . n 
B 1 74  GLN 74  73  73  GLN GLN B . n 
B 1 75  ALA 75  74  74  ALA ALA B . n 
B 1 76  LEU 76  75  75  LEU LEU B . n 
B 1 77  LYS 77  76  76  LYS LYS B . n 
B 1 78  PHE 78  77  77  PHE PHE B . n 
B 1 79  VAL 79  78  78  VAL VAL B . n 
B 1 80  ARG 80  79  79  ARG ARG B . n 
B 1 81  ASP 81  80  80  ASP ASP B . n 
B 1 82  PHE 82  81  81  PHE PHE B . n 
B 1 83  ALA 83  82  82  ALA ALA B . n 
B 1 84  GLY 84  83  83  GLY GLY B . n 
B 1 85  ASP 85  84  84  ASP ASP B . n 
B 1 86  GLY 86  85  85  GLY GLY B . n 
B 1 87  LEU 87  86  86  LEU LEU B . n 
B 1 88  ALA 88  87  87  ALA ALA B . n 
B 1 89  THR 89  88  88  THR THR B . n 
B 1 90  SER 90  89  89  SER SER B . n 
B 1 91  TRP 91  90  90  TRP TRP B . n 
B 1 92  THR 92  91  91  THR THR B . n 
B 1 93  HIS 93  92  92  HIS HIS B . n 
B 1 94  GLU 94  93  93  GLU GLU B . n 
B 1 95  LYS 95  94  94  LYS LYS B . n 
B 1 96  ASN 96  95  95  ASN ASN B . n 
B 1 97  TRP 97  96  96  TRP TRP B . n 
B 1 98  LYS 98  97  97  LYS LYS B . n 
B 1 99  LYS 99  98  98  LYS LYS B . n 
B 1 100 ALA 100 99  99  ALA ALA B . n 
B 1 101 HIS 101 100 100 HIS HIS B . n 
B 1 102 ASN 102 101 101 ASN ASN B . n 
B 1 103 ILE 103 102 102 ILE ILE B . n 
B 1 104 LEU 104 103 103 LEU LEU B . n 
B 1 105 LEU 105 104 104 LEU LEU B . n 
B 1 106 PRO 106 105 105 PRO PRO B . n 
B 1 107 SER 107 106 106 SER SER B . n 
B 1 108 PHE 108 107 107 PHE PHE B . n 
B 1 109 SER 109 108 108 SER SER B . n 
B 1 110 GLN 110 109 109 GLN GLN B . n 
B 1 111 GLN 111 110 110 GLN GLN B . n 
B 1 112 ALA 112 111 111 ALA ALA B . n 
B 1 113 MET 113 112 112 MET MET B . n 
B 1 114 LYS 114 113 113 LYS LYS B . n 
B 1 115 GLY 115 114 114 GLY GLY B . n 
B 1 116 TYR 116 115 115 TYR TYR B . n 
B 1 117 HIS 117 116 116 HIS HIS B . n 
B 1 118 ALA 118 117 117 ALA ALA B . n 
B 1 119 MET 119 118 118 MET MET B . n 
B 1 120 MET 120 119 119 MET MET B . n 
B 1 121 VAL 121 120 120 VAL VAL B . n 
B 1 122 ASP 122 121 121 ASP ASP B . n 
B 1 123 ILE 123 122 122 ILE ILE B . n 
B 1 124 ALA 124 123 123 ALA ALA B . n 
B 1 125 VAL 125 124 124 VAL VAL B . n 
B 1 126 GLN 126 125 125 GLN GLN B . n 
B 1 127 LEU 127 126 126 LEU LEU B . n 
B 1 128 VAL 128 127 127 VAL VAL B . n 
B 1 129 GLN 129 128 128 GLN GLN B . n 
B 1 130 LYS 130 129 129 LYS LYS B . n 
B 1 131 TRP 131 130 130 TRP TRP B . n 
B 1 132 GLU 132 131 131 GLU GLU B . n 
B 1 133 ARG 133 132 132 ARG ARG B . n 
B 1 134 LEU 134 133 133 LEU LEU B . n 
B 1 135 ASN 135 134 134 ASN ASN B . n 
B 1 136 ALA 136 135 135 ALA ALA B . n 
B 1 137 ASP 137 136 136 ASP ASP B . n 
B 1 138 GLU 138 137 137 GLU GLU B . n 
B 1 139 HIS 139 138 138 HIS HIS B . n 
B 1 140 ILE 140 139 139 ILE ILE B . n 
B 1 141 GLU 141 140 140 GLU GLU B . n 
B 1 142 VAL 142 141 141 VAL VAL B . n 
B 1 143 PRO 143 142 142 PRO PRO B . n 
B 1 144 GLU 144 143 143 GLU GLU B . n 
B 1 145 ASP 145 144 144 ASP ASP B . n 
B 1 146 MET 146 145 145 MET MET B . n 
B 1 147 THR 147 146 146 THR THR B . n 
B 1 148 ARG 148 147 147 ARG ARG B . n 
B 1 149 LEU 149 148 148 LEU LEU B . n 
B 1 150 THR 150 149 149 THR THR B . n 
B 1 151 LEU 151 150 150 LEU LEU B . n 
B 1 152 ASP 152 151 151 ASP ASP B . n 
B 1 153 THR 153 152 152 THR THR B . n 
B 1 154 ILE 154 153 153 ILE ILE B . n 
B 1 155 GLY 155 154 154 GLY GLY B . n 
B 1 156 LEU 156 155 155 LEU LEU B . n 
B 1 157 CYS 157 156 156 CYS CYS B . n 
B 1 158 GLY 158 157 157 GLY GLY B . n 
B 1 159 PHE 159 158 158 PHE PHE B . n 
B 1 160 ASN 160 159 159 ASN ASN B . n 
B 1 161 TYR 161 160 160 TYR TYR B . n 
B 1 162 ARG 162 161 161 ARG ARG B . n 
B 1 163 PHE 163 162 162 PHE PHE B . n 
B 1 164 ASN 164 163 163 ASN ASN B . n 
B 1 165 SER 165 164 164 SER SER B . n 
B 1 166 PHE 166 165 165 PHE PHE B . n 
B 1 167 TYR 167 166 166 TYR TYR B . n 
B 1 168 ARG 168 167 167 ARG ARG B . n 
B 1 169 ASP 169 168 168 ASP ASP B . n 
B 1 170 GLN 170 169 169 GLN GLN B . n 
B 1 171 PRO 171 170 170 PRO PRO B . n 
B 1 172 HIS 172 171 171 HIS HIS B . n 
B 1 173 PRO 173 172 172 PRO PRO B . n 
B 1 174 PHE 174 173 173 PHE PHE B . n 
B 1 175 ILE 175 174 174 ILE ILE B . n 
B 1 176 THR 176 175 175 THR THR B . n 
B 1 177 SER 177 176 176 SER SER B . n 
B 1 178 MET 178 177 177 MET MET B . n 
B 1 179 VAL 179 178 178 VAL VAL B . n 
B 1 180 ARG 180 179 179 ARG ARG B . n 
B 1 181 ALA 181 180 180 ALA ALA B . n 
B 1 182 LEU 182 181 181 LEU LEU B . n 
B 1 183 ASP 183 182 182 ASP ASP B . n 
B 1 184 GLU 184 183 183 GLU GLU B . n 
B 1 185 ALA 185 184 184 ALA ALA B . n 
B 1 186 MET 186 185 185 MET MET B . n 
B 1 187 ASN 187 186 186 ASN ASN B . n 
B 1 188 LYS 188 187 187 LYS LYS B . n 
B 1 189 LEU 189 188 188 LEU LEU B . n 
B 1 190 GLN 190 189 189 GLN GLN B . n 
B 1 191 ARG 191 190 190 ARG ARG B . n 
B 1 192 ALA 192 191 191 ALA ALA B . n 
B 1 193 ASN 193 192 192 ASN ASN B . n 
B 1 194 PRO 194 193 193 PRO PRO B . n 
B 1 195 ASP 195 194 194 ASP ASP B . n 
B 1 196 ASP 196 195 195 ASP ASP B . n 
B 1 197 PRO 197 196 196 PRO PRO B . n 
B 1 198 ALA 198 197 197 ALA ALA B . n 
B 1 199 TYR 199 198 198 TYR TYR B . n 
B 1 200 ASP 200 199 199 ASP ASP B . n 
B 1 201 GLU 201 200 200 GLU GLU B . n 
B 1 202 ASN 202 201 201 ASN ASN B . n 
B 1 203 LYS 203 202 202 LYS LYS B . n 
B 1 204 ARG 204 203 203 ARG ARG B . n 
B 1 205 GLN 205 204 204 GLN GLN B . n 
B 1 206 PHE 206 205 205 PHE PHE B . n 
B 1 207 GLN 207 206 206 GLN GLN B . n 
B 1 208 GLU 208 207 207 GLU GLU B . n 
B 1 209 ASP 209 208 208 ASP ASP B . n 
B 1 210 ILE 210 209 209 ILE ILE B . n 
B 1 211 LYS 211 210 210 LYS LYS B . n 
B 1 212 VAL 212 211 211 VAL VAL B . n 
B 1 213 MET 213 212 212 MET MET B . n 
B 1 214 ASN 214 213 213 ASN ASN B . n 
B 1 215 ASP 215 214 214 ASP ASP B . n 
B 1 216 LEU 216 215 215 LEU LEU B . n 
B 1 217 VAL 217 216 216 VAL VAL B . n 
B 1 218 ASP 218 217 217 ASP ASP B . n 
B 1 219 LYS 219 218 218 LYS LYS B . n 
B 1 220 ILE 220 219 219 ILE ILE B . n 
B 1 221 ILE 221 220 220 ILE ILE B . n 
B 1 222 ALA 222 221 221 ALA ALA B . n 
B 1 223 ASP 223 222 222 ASP ASP B . n 
B 1 224 ARG 224 223 223 ARG ARG B . n 
B 1 225 LYS 225 224 224 LYS LYS B . n 
B 1 226 ALA 226 225 225 ALA ALA B . n 
B 1 227 SER 227 226 226 SER SER B . n 
B 1 228 GLY 228 227 227 GLY GLY B . n 
B 1 229 GLU 229 228 228 GLU GLU B . n 
B 1 230 GLN 230 229 229 GLN GLN B . n 
B 1 231 SER 231 230 230 SER SER B . n 
B 1 232 ASP 232 231 231 ASP ASP B . n 
B 1 233 ASP 233 232 232 ASP ASP B . n 
B 1 234 LEU 234 233 233 LEU LEU B . n 
B 1 235 LEU 235 234 234 LEU LEU B . n 
B 1 236 THR 236 235 235 THR THR B . n 
B 1 237 HIS 237 236 236 HIS HIS B . n 
B 1 238 MET 238 237 237 MET MET B . n 
B 1 239 LEU 239 238 238 LEU LEU B . n 
B 1 240 ASN 240 239 239 ASN ASN B . n 
B 1 241 GLY 241 240 240 GLY GLY B . n 
B 1 242 LYS 242 241 241 LYS LYS B . n 
B 1 243 ASP 243 242 242 ASP ASP B . n 
B 1 244 PRO 244 243 243 PRO PRO B . n 
B 1 245 GLU 245 244 244 GLU GLU B . n 
B 1 246 THR 246 245 245 THR THR B . n 
B 1 247 GLY 247 246 246 GLY GLY B . n 
B 1 248 GLU 248 247 247 GLU GLU B . n 
B 1 249 PRO 249 248 248 PRO PRO B . n 
B 1 250 LEU 250 249 249 LEU LEU B . n 
B 1 251 ASP 251 250 250 ASP ASP B . n 
B 1 252 ASP 252 251 251 ASP ASP B . n 
B 1 253 GLU 253 252 252 GLU GLU B . n 
B 1 254 ASN 254 253 253 ASN ASN B . n 
B 1 255 ILE 255 254 254 ILE ILE B . n 
B 1 256 ARG 256 255 255 ARG ARG B . n 
B 1 257 TYR 257 256 256 TYR TYR B . n 
B 1 258 GLN 258 257 257 GLN GLN B . n 
B 1 259 ILE 259 258 258 ILE ILE B . n 
B 1 260 ILE 260 259 259 ILE ILE B . n 
B 1 261 THR 261 260 260 THR THR B . n 
B 1 262 PHE 262 261 261 PHE PHE B . n 
B 1 263 LEU 263 262 262 LEU LEU B . n 
B 1 264 ILE 264 263 263 ILE ILE B . n 
B 1 265 ALA 265 264 264 ALA ALA B . n 
B 1 266 GLY 266 265 265 GLY GLY B . n 
B 1 267 HIS 267 266 266 HIS HIS B . n 
B 1 268 GLU 268 267 267 GLU GLU B . n 
B 1 269 THR 269 268 268 THR THR B . n 
B 1 270 THR 270 269 269 THR THR B . n 
B 1 271 SER 271 270 270 SER SER B . n 
B 1 272 GLY 272 271 271 GLY GLY B . n 
B 1 273 LEU 273 272 272 LEU LEU B . n 
B 1 274 LEU 274 273 273 LEU LEU B . n 
B 1 275 SER 275 274 274 SER SER B . n 
B 1 276 PHE 276 275 275 PHE PHE B . n 
B 1 277 ALA 277 276 276 ALA ALA B . n 
B 1 278 LEU 278 277 277 LEU LEU B . n 
B 1 279 TYR 279 278 278 TYR TYR B . n 
B 1 280 PHE 280 279 279 PHE PHE B . n 
B 1 281 LEU 281 280 280 LEU LEU B . n 
B 1 282 VAL 282 281 281 VAL VAL B . n 
B 1 283 LYS 283 282 282 LYS LYS B . n 
B 1 284 ASN 284 283 283 ASN ASN B . n 
B 1 285 PRO 285 284 284 PRO PRO B . n 
B 1 286 HIS 286 285 285 HIS HIS B . n 
B 1 287 VAL 287 286 286 VAL VAL B . n 
B 1 288 LEU 288 287 287 LEU LEU B . n 
B 1 289 GLN 289 288 288 GLN GLN B . n 
B 1 290 LYS 290 289 289 LYS LYS B . n 
B 1 291 ALA 291 290 290 ALA ALA B . n 
B 1 292 ALA 292 291 291 ALA ALA B . n 
B 1 293 GLU 293 292 292 GLU GLU B . n 
B 1 294 GLU 294 293 293 GLU GLU B . n 
B 1 295 ALA 295 294 294 ALA ALA B . n 
B 1 296 ALA 296 295 295 ALA ALA B . n 
B 1 297 ARG 297 296 296 ARG ARG B . n 
B 1 298 VAL 298 297 297 VAL VAL B . n 
B 1 299 LEU 299 298 298 LEU LEU B . n 
B 1 300 VAL 300 299 299 VAL VAL B . n 
B 1 301 ASP 301 300 300 ASP ASP B . n 
B 1 302 PRO 302 301 301 PRO PRO B . n 
B 1 303 VAL 303 302 302 VAL VAL B . n 
B 1 304 PRO 304 303 303 PRO PRO B . n 
B 1 305 SER 305 304 304 SER SER B . n 
B 1 306 TYR 306 305 305 TYR TYR B . n 
B 1 307 LYS 307 306 306 LYS LYS B . n 
B 1 308 GLN 308 307 307 GLN GLN B . n 
B 1 309 VAL 309 308 308 VAL VAL B . n 
B 1 310 LYS 310 309 309 LYS LYS B . n 
B 1 311 GLN 311 310 310 GLN GLN B . n 
B 1 312 LEU 312 311 311 LEU LEU B . n 
B 1 313 LYS 313 312 312 LYS LYS B . n 
B 1 314 TYR 314 313 313 TYR TYR B . n 
B 1 315 VAL 315 314 314 VAL VAL B . n 
B 1 316 GLY 316 315 315 GLY GLY B . n 
B 1 317 MET 317 316 316 MET MET B . n 
B 1 318 VAL 318 317 317 VAL VAL B . n 
B 1 319 LEU 319 318 318 LEU LEU B . n 
B 1 320 ASN 320 319 319 ASN ASN B . n 
B 1 321 GLU 321 320 320 GLU GLU B . n 
B 1 322 ALA 322 321 321 ALA ALA B . n 
B 1 323 LEU 323 322 322 LEU LEU B . n 
B 1 324 ARG 324 323 323 ARG ARG B . n 
B 1 325 LEU 325 324 324 LEU LEU B . n 
B 1 326 TRP 326 325 325 TRP TRP B . n 
B 1 327 PRO 327 326 326 PRO PRO B . n 
B 1 328 THR 328 327 327 THR THR B . n 
B 1 329 ALA 329 328 328 ALA ALA B . n 
B 1 330 PRO 330 329 329 PRO PRO B . n 
B 1 331 ALA 331 330 330 ALA ALA B . n 
B 1 332 PHE 332 331 331 PHE PHE B . n 
B 1 333 SER 333 332 332 SER SER B . n 
B 1 334 LEU 334 333 333 LEU LEU B . n 
B 1 335 TYR 335 334 334 TYR TYR B . n 
B 1 336 ALA 336 335 335 ALA ALA B . n 
B 1 337 LYS 337 336 336 LYS LYS B . n 
B 1 338 GLU 338 337 337 GLU GLU B . n 
B 1 339 ASP 339 338 338 ASP ASP B . n 
B 1 340 THR 340 339 339 THR THR B . n 
B 1 341 VAL 341 340 340 VAL VAL B . n 
B 1 342 LEU 342 341 341 LEU LEU B . n 
B 1 343 GLY 343 342 342 GLY GLY B . n 
B 1 344 GLY 344 343 343 GLY GLY B . n 
B 1 345 GLU 345 344 344 GLU GLU B . n 
B 1 346 TYR 346 345 345 TYR TYR B . n 
B 1 347 PRO 347 346 346 PRO PRO B . n 
B 1 348 LEU 348 347 347 LEU LEU B . n 
B 1 349 GLU 349 348 348 GLU GLU B . n 
B 1 350 LYS 350 349 349 LYS LYS B . n 
B 1 351 GLY 351 350 350 GLY GLY B . n 
B 1 352 ASP 352 351 351 ASP ASP B . n 
B 1 353 GLU 353 352 352 GLU GLU B . n 
B 1 354 LEU 354 353 353 LEU LEU B . n 
B 1 355 MET 355 354 354 MET MET B . n 
B 1 356 VAL 356 355 355 VAL VAL B . n 
B 1 357 LEU 357 356 356 LEU LEU B . n 
B 1 358 ILE 358 357 357 ILE ILE B . n 
B 1 359 PRO 359 358 358 PRO PRO B . n 
B 1 360 GLN 360 359 359 GLN GLN B . n 
B 1 361 LEU 361 360 360 LEU LEU B . n 
B 1 362 HIS 362 361 361 HIS HIS B . n 
B 1 363 ARG 363 362 362 ARG ARG B . n 
B 1 364 ASP 364 363 363 ASP ASP B . n 
B 1 365 LYS 365 364 364 LYS LYS B . n 
B 1 366 THR 366 365 365 THR THR B . n 
B 1 367 ILE 367 366 366 ILE ILE B . n 
B 1 368 TRP 368 367 367 TRP TRP B . n 
B 1 369 GLY 369 368 368 GLY GLY B . n 
B 1 370 ASP 370 369 369 ASP ASP B . n 
B 1 371 ASP 371 370 370 ASP ASP B . n 
B 1 372 VAL 372 371 371 VAL VAL B . n 
B 1 373 GLU 373 372 372 GLU GLU B . n 
B 1 374 GLU 374 373 373 GLU GLU B . n 
B 1 375 PHE 375 374 374 PHE PHE B . n 
B 1 376 ARG 376 375 375 ARG ARG B . n 
B 1 377 PRO 377 376 376 PRO PRO B . n 
B 1 378 GLU 378 377 377 GLU GLU B . n 
B 1 379 ARG 379 378 378 ARG ARG B . n 
B 1 380 PHE 380 379 379 PHE PHE B . n 
B 1 381 GLU 381 380 380 GLU GLU B . n 
B 1 382 ASN 382 381 381 ASN ASN B . n 
B 1 383 PRO 383 382 382 PRO PRO B . n 
B 1 384 SER 384 383 383 SER SER B . n 
B 1 385 ALA 385 384 384 ALA ALA B . n 
B 1 386 ILE 386 385 385 ILE ILE B . n 
B 1 387 PRO 387 386 386 PRO PRO B . n 
B 1 388 GLN 388 387 387 GLN GLN B . n 
B 1 389 HIS 389 388 388 HIS HIS B . n 
B 1 390 ALA 390 389 389 ALA ALA B . n 
B 1 391 PHE 391 390 390 PHE PHE B . n 
B 1 392 LYS 392 391 391 LYS LYS B . n 
B 1 393 PRO 393 392 392 PRO PRO B . n 
B 1 394 HIS 394 393 393 HIS HIS B . n 
B 1 395 GLY 395 394 394 GLY GLY B . n 
B 1 396 ASN 396 395 395 ASN ASN B . n 
B 1 397 GLY 397 396 396 GLY GLY B . n 
B 1 398 GLN 398 397 397 GLN GLN B . n 
B 1 399 ARG 399 398 398 ARG ARG B . n 
B 1 400 ALA 400 399 399 ALA ALA B . n 
B 1 401 CYS 401 400 400 CYS CYS B . n 
B 1 402 ILE 402 401 401 ILE ILE B . n 
B 1 403 GLY 403 402 402 GLY GLY B . n 
B 1 404 GLN 404 403 403 GLN GLN B . n 
B 1 405 GLN 405 404 404 GLN GLN B . n 
B 1 406 PHE 406 405 405 PHE PHE B . n 
B 1 407 ALA 407 406 406 ALA ALA B . n 
B 1 408 LEU 408 407 407 LEU LEU B . n 
B 1 409 HIS 409 408 408 HIS HIS B . n 
B 1 410 GLU 410 409 409 GLU GLU B . n 
B 1 411 ALA 411 410 410 ALA ALA B . n 
B 1 412 THR 412 411 411 THR THR B . n 
B 1 413 LEU 413 412 412 LEU LEU B . n 
B 1 414 VAL 414 413 413 VAL VAL B . n 
B 1 415 LEU 415 414 414 LEU LEU B . n 
B 1 416 GLY 416 415 415 GLY GLY B . n 
B 1 417 MET 417 416 416 MET MET B . n 
B 1 418 MET 418 417 417 MET MET B . n 
B 1 419 LEU 419 418 418 LEU LEU B . n 
B 1 420 LYS 420 419 419 LYS LYS B . n 
B 1 421 HIS 421 420 420 HIS HIS B . n 
B 1 422 PHE 422 421 421 PHE PHE B . n 
B 1 423 ASP 423 422 422 ASP ASP B . n 
B 1 424 PHE 424 423 423 PHE PHE B . n 
B 1 425 GLU 425 424 424 GLU GLU B . n 
B 1 426 ASP 426 425 425 ASP ASP B . n 
B 1 427 HIS 427 426 426 HIS HIS B . n 
B 1 428 THR 428 427 427 THR THR B . n 
B 1 429 ASN 429 428 428 ASN ASN B . n 
B 1 430 TYR 430 429 429 TYR TYR B . n 
B 1 431 GLU 431 430 430 GLU GLU B . n 
B 1 432 LEU 432 431 431 LEU LEU B . n 
B 1 433 ASP 433 432 432 ASP ASP B . n 
B 1 434 ILE 434 433 433 ILE ILE B . n 
B 1 435 LYS 435 434 434 LYS LYS B . n 
B 1 436 GLU 436 435 435 GLU GLU B . n 
B 1 437 THR 437 436 436 THR THR B . n 
B 1 438 LEU 438 437 437 LEU LEU B . n 
B 1 439 THR 439 438 438 THR THR B . n 
B 1 440 LEU 440 439 439 LEU LEU B . n 
B 1 441 LYS 441 440 440 LYS LYS B . n 
B 1 442 PRO 442 441 441 PRO PRO B . n 
B 1 443 GLU 443 442 442 GLU GLU B . n 
B 1 444 GLY 444 443 443 GLY GLY B . n 
B 1 445 PHE 445 444 444 PHE PHE B . n 
B 1 446 VAL 446 445 445 VAL VAL B . n 
B 1 447 VAL 447 446 446 VAL VAL B . n 
B 1 448 LYS 448 447 447 LYS LYS B . n 
B 1 449 ALA 449 448 448 ALA ALA B . n 
B 1 450 LYS 450 449 449 LYS LYS B . n 
B 1 451 SER 451 450 450 SER SER B . n 
B 1 452 LYS 452 451 451 LYS LYS B . n 
B 1 453 LYS 453 452 452 LYS LYS B . n 
B 1 454 ILE 454 453 453 ILE ILE B . n 
B 1 455 PRO 455 454 454 PRO PRO B . n 
B 1 456 LEU 456 455 455 LEU LEU B . 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 OXY ? ? OXY ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SYN ? ? SYN ? ? 'SUBJECT OF INVESTIGATION' ? 
3 HEM ? ? HEM ? ? 'SUBJECT OF INVESTIGATION' ? 
4 D0L ? ? D0L ? ? '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 
C 2 HEM 1   501  501  HEM HEM A . 
D 3 SYN 1   502  502  SYN SYN A . 
E 4 OXY 1   503  503  OXY OXY A . 
F 5 D0L 1   504  504  D0L D0L A . 
G 6 GOL 1   505  505  GOL GOL A . 
H 2 HEM 1   501  501  HEM HEM B . 
I 3 SYN 1   502  502  SYN SYN B . 
J 4 OXY 1   503  503  OXY OXY B . 
K 5 D0L 1   504  504  D0L D0L B . 
L 6 GOL 1   505  505  GOL GOL B . 
M 6 GOL 1   506  506  GOL GOL B . 
N 6 GOL 1   507  507  GOL GOL B . 
O 7 HOH 1   601  818  HOH HOH A . 
O 7 HOH 2   602  980  HOH HOH A . 
O 7 HOH 3   603  976  HOH HOH A . 
O 7 HOH 4   604  961  HOH HOH A . 
O 7 HOH 5   605  981  HOH HOH A . 
O 7 HOH 6   606  941  HOH HOH A . 
O 7 HOH 7   607  855  HOH HOH A . 
O 7 HOH 8   608  601  HOH HOH A . 
O 7 HOH 9   609  692  HOH HOH A . 
O 7 HOH 10  610  862  HOH HOH A . 
O 7 HOH 11  611  999  HOH HOH A . 
O 7 HOH 12  612  685  HOH HOH A . 
O 7 HOH 13  613  876  HOH HOH A . 
O 7 HOH 14  614  635  HOH HOH A . 
O 7 HOH 15  615  1011 HOH HOH A . 
O 7 HOH 16  616  988  HOH HOH A . 
O 7 HOH 17  617  982  HOH HOH A . 
O 7 HOH 18  618  901  HOH HOH A . 
O 7 HOH 19  619  996  HOH HOH A . 
O 7 HOH 20  620  604  HOH HOH A . 
O 7 HOH 21  621  791  HOH HOH A . 
O 7 HOH 22  622  858  HOH HOH A . 
O 7 HOH 23  623  655  HOH HOH A . 
O 7 HOH 24  624  811  HOH HOH A . 
O 7 HOH 25  625  837  HOH HOH A . 
O 7 HOH 26  626  801  HOH HOH A . 
O 7 HOH 27  627  636  HOH HOH A . 
O 7 HOH 28  628  814  HOH HOH A . 
O 7 HOH 29  629  707  HOH HOH A . 
O 7 HOH 30  630  937  HOH HOH A . 
O 7 HOH 31  631  823  HOH HOH A . 
O 7 HOH 32  632  728  HOH HOH A . 
O 7 HOH 33  633  884  HOH HOH A . 
O 7 HOH 34  634  991  HOH HOH A . 
O 7 HOH 35  635  806  HOH HOH A . 
O 7 HOH 36  636  626  HOH HOH A . 
O 7 HOH 37  637  926  HOH HOH A . 
O 7 HOH 38  638  782  HOH HOH A . 
O 7 HOH 39  639  716  HOH HOH A . 
O 7 HOH 40  640  668  HOH HOH A . 
O 7 HOH 41  641  612  HOH HOH A . 
O 7 HOH 42  642  755  HOH HOH A . 
O 7 HOH 43  643  784  HOH HOH A . 
O 7 HOH 44  644  628  HOH HOH A . 
O 7 HOH 45  645  950  HOH HOH A . 
O 7 HOH 46  646  978  HOH HOH A . 
O 7 HOH 47  647  761  HOH HOH A . 
O 7 HOH 48  648  672  HOH HOH A . 
O 7 HOH 49  649  872  HOH HOH A . 
O 7 HOH 50  650  797  HOH HOH A . 
O 7 HOH 51  651  878  HOH HOH A . 
O 7 HOH 52  652  724  HOH HOH A . 
O 7 HOH 53  653  642  HOH HOH A . 
O 7 HOH 54  654  890  HOH HOH A . 
O 7 HOH 55  655  711  HOH HOH A . 
O 7 HOH 56  656  995  HOH HOH A . 
O 7 HOH 57  657  706  HOH HOH A . 
O 7 HOH 58  658  611  HOH HOH A . 
O 7 HOH 59  659  744  HOH HOH A . 
O 7 HOH 60  660  631  HOH HOH A . 
O 7 HOH 61  661  684  HOH HOH A . 
O 7 HOH 62  662  737  HOH HOH A . 
O 7 HOH 63  663  913  HOH HOH A . 
O 7 HOH 64  664  678  HOH HOH A . 
O 7 HOH 65  665  758  HOH HOH A . 
O 7 HOH 66  666  893  HOH HOH A . 
O 7 HOH 67  667  865  HOH HOH A . 
O 7 HOH 68  668  840  HOH HOH A . 
O 7 HOH 69  669  828  HOH HOH A . 
O 7 HOH 70  670  623  HOH HOH A . 
O 7 HOH 71  671  740  HOH HOH A . 
O 7 HOH 72  672  621  HOH HOH A . 
O 7 HOH 73  673  664  HOH HOH A . 
O 7 HOH 74  674  643  HOH HOH A . 
O 7 HOH 75  675  813  HOH HOH A . 
O 7 HOH 76  676  633  HOH HOH A . 
O 7 HOH 77  677  627  HOH HOH A . 
O 7 HOH 78  678  617  HOH HOH A . 
O 7 HOH 79  679  900  HOH HOH A . 
O 7 HOH 80  680  804  HOH HOH A . 
O 7 HOH 81  681  748  HOH HOH A . 
O 7 HOH 82  682  916  HOH HOH A . 
O 7 HOH 83  683  756  HOH HOH A . 
O 7 HOH 84  684  793  HOH HOH A . 
O 7 HOH 85  685  634  HOH HOH A . 
O 7 HOH 86  686  754  HOH HOH A . 
O 7 HOH 87  687  889  HOH HOH A . 
O 7 HOH 88  688  687  HOH HOH A . 
O 7 HOH 89  689  680  HOH HOH A . 
O 7 HOH 90  690  842  HOH HOH A . 
O 7 HOH 91  691  922  HOH HOH A . 
O 7 HOH 92  692  925  HOH HOH A . 
O 7 HOH 93  693  1005 HOH HOH A . 
O 7 HOH 94  694  638  HOH HOH A . 
O 7 HOH 95  695  802  HOH HOH A . 
O 7 HOH 96  696  618  HOH HOH A . 
O 7 HOH 97  697  779  HOH HOH A . 
O 7 HOH 98  698  852  HOH HOH A . 
O 7 HOH 99  699  1006 HOH HOH A . 
O 7 HOH 100 700  875  HOH HOH A . 
O 7 HOH 101 701  812  HOH HOH A . 
O 7 HOH 102 702  815  HOH HOH A . 
O 7 HOH 103 703  968  HOH HOH A . 
O 7 HOH 104 704  752  HOH HOH A . 
O 7 HOH 105 705  864  HOH HOH A . 
O 7 HOH 106 706  831  HOH HOH A . 
O 7 HOH 107 707  1002 HOH HOH A . 
O 7 HOH 108 708  681  HOH HOH A . 
O 7 HOH 109 709  753  HOH HOH A . 
O 7 HOH 110 710  835  HOH HOH A . 
O 7 HOH 111 711  719  HOH HOH A . 
O 7 HOH 112 712  606  HOH HOH A . 
O 7 HOH 113 713  746  HOH HOH A . 
O 7 HOH 114 714  675  HOH HOH A . 
O 7 HOH 115 715  741  HOH HOH A . 
O 7 HOH 116 716  749  HOH HOH A . 
O 7 HOH 117 717  699  HOH HOH A . 
O 7 HOH 118 718  700  HOH HOH A . 
O 7 HOH 119 719  727  HOH HOH A . 
O 7 HOH 120 720  824  HOH HOH A . 
O 7 HOH 121 721  923  HOH HOH A . 
O 7 HOH 122 722  952  HOH HOH A . 
O 7 HOH 123 723  721  HOH HOH A . 
O 7 HOH 124 724  770  HOH HOH A . 
O 7 HOH 125 725  765  HOH HOH A . 
O 7 HOH 126 726  630  HOH HOH A . 
O 7 HOH 127 727  602  HOH HOH A . 
O 7 HOH 128 728  669  HOH HOH A . 
O 7 HOH 129 729  641  HOH HOH A . 
O 7 HOH 130 730  686  HOH HOH A . 
O 7 HOH 131 731  644  HOH HOH A . 
O 7 HOH 132 732  646  HOH HOH A . 
O 7 HOH 133 733  939  HOH HOH A . 
O 7 HOH 134 734  663  HOH HOH A . 
O 7 HOH 135 735  674  HOH HOH A . 
O 7 HOH 136 736  637  HOH HOH A . 
O 7 HOH 137 737  817  HOH HOH A . 
O 7 HOH 138 738  659  HOH HOH A . 
O 7 HOH 139 739  715  HOH HOH A . 
O 7 HOH 140 740  739  HOH HOH A . 
O 7 HOH 141 741  808  HOH HOH A . 
O 7 HOH 142 742  909  HOH HOH A . 
O 7 HOH 143 743  652  HOH HOH A . 
O 7 HOH 144 744  932  HOH HOH A . 
O 7 HOH 145 745  605  HOH HOH A . 
O 7 HOH 146 746  899  HOH HOH A . 
O 7 HOH 147 747  670  HOH HOH A . 
O 7 HOH 148 748  645  HOH HOH A . 
O 7 HOH 149 749  667  HOH HOH A . 
O 7 HOH 150 750  629  HOH HOH A . 
O 7 HOH 151 751  665  HOH HOH A . 
O 7 HOH 152 752  614  HOH HOH A . 
O 7 HOH 153 753  622  HOH HOH A . 
O 7 HOH 154 754  712  HOH HOH A . 
O 7 HOH 155 755  640  HOH HOH A . 
O 7 HOH 156 756  834  HOH HOH A . 
O 7 HOH 157 757  648  HOH HOH A . 
O 7 HOH 158 758  942  HOH HOH A . 
O 7 HOH 159 759  608  HOH HOH A . 
O 7 HOH 160 760  849  HOH HOH A . 
O 7 HOH 161 761  874  HOH HOH A . 
O 7 HOH 162 762  763  HOH HOH A . 
O 7 HOH 163 763  704  HOH HOH A . 
O 7 HOH 164 764  701  HOH HOH A . 
O 7 HOH 165 765  1013 HOH HOH A . 
O 7 HOH 166 766  660  HOH HOH A . 
O 7 HOH 167 767  743  HOH HOH A . 
O 7 HOH 168 768  725  HOH HOH A . 
O 7 HOH 169 769  691  HOH HOH A . 
O 7 HOH 170 770  938  HOH HOH A . 
O 7 HOH 171 771  718  HOH HOH A . 
O 7 HOH 172 772  632  HOH HOH A . 
O 7 HOH 173 773  745  HOH HOH A . 
O 7 HOH 174 774  661  HOH HOH A . 
O 7 HOH 175 775  726  HOH HOH A . 
O 7 HOH 176 776  695  HOH HOH A . 
O 7 HOH 177 777  709  HOH HOH A . 
O 7 HOH 178 778  830  HOH HOH A . 
O 7 HOH 179 779  656  HOH HOH A . 
O 7 HOH 180 780  877  HOH HOH A . 
O 7 HOH 181 781  832  HOH HOH A . 
O 7 HOH 182 782  920  HOH HOH A . 
O 7 HOH 183 783  984  HOH HOH A . 
O 7 HOH 184 784  690  HOH HOH A . 
O 7 HOH 185 785  676  HOH HOH A . 
O 7 HOH 186 786  895  HOH HOH A . 
O 7 HOH 187 787  973  HOH HOH A . 
O 7 HOH 188 788  921  HOH HOH A . 
O 7 HOH 189 789  736  HOH HOH A . 
O 7 HOH 190 790  654  HOH HOH A . 
O 7 HOH 191 791  609  HOH HOH A . 
O 7 HOH 192 792  679  HOH HOH A . 
O 7 HOH 193 793  720  HOH HOH A . 
O 7 HOH 194 794  935  HOH HOH A . 
O 7 HOH 195 795  649  HOH HOH A . 
O 7 HOH 196 796  616  HOH HOH A . 
O 7 HOH 197 797  829  HOH HOH A . 
O 7 HOH 198 798  615  HOH HOH A . 
O 7 HOH 199 799  853  HOH HOH A . 
O 7 HOH 200 800  610  HOH HOH A . 
O 7 HOH 201 801  1001 HOH HOH A . 
O 7 HOH 202 802  683  HOH HOH A . 
O 7 HOH 203 803  894  HOH HOH A . 
O 7 HOH 204 804  603  HOH HOH A . 
O 7 HOH 205 805  619  HOH HOH A . 
O 7 HOH 206 806  613  HOH HOH A . 
O 7 HOH 207 807  990  HOH HOH A . 
O 7 HOH 208 808  910  HOH HOH A . 
O 7 HOH 209 809  1009 HOH HOH A . 
O 7 HOH 210 810  956  HOH HOH A . 
O 7 HOH 211 811  953  HOH HOH A . 
O 7 HOH 212 812  966  HOH HOH A . 
O 7 HOH 213 813  971  HOH HOH A . 
O 7 HOH 214 814  671  HOH HOH A . 
O 7 HOH 215 815  662  HOH HOH A . 
O 7 HOH 216 816  825  HOH HOH A . 
O 7 HOH 217 817  738  HOH HOH A . 
O 7 HOH 218 818  768  HOH HOH A . 
O 7 HOH 219 819  682  HOH HOH A . 
O 7 HOH 220 820  927  HOH HOH A . 
O 7 HOH 221 821  780  HOH HOH A . 
O 7 HOH 222 822  710  HOH HOH A . 
O 7 HOH 223 823  881  HOH HOH A . 
O 7 HOH 224 824  827  HOH HOH A . 
O 7 HOH 225 825  723  HOH HOH A . 
O 7 HOH 226 826  757  HOH HOH A . 
O 7 HOH 227 827  747  HOH HOH A . 
O 7 HOH 228 828  688  HOH HOH A . 
O 7 HOH 229 829  773  HOH HOH A . 
O 7 HOH 230 830  693  HOH HOH A . 
O 7 HOH 231 831  1000 HOH HOH A . 
O 7 HOH 232 832  798  HOH HOH A . 
O 7 HOH 233 833  911  HOH HOH A . 
O 7 HOH 234 834  868  HOH HOH A . 
O 7 HOH 235 835  859  HOH HOH A . 
O 7 HOH 236 836  651  HOH HOH A . 
O 7 HOH 237 837  833  HOH HOH A . 
O 7 HOH 238 838  751  HOH HOH A . 
O 7 HOH 239 839  790  HOH HOH A . 
O 7 HOH 240 840  677  HOH HOH A . 
O 7 HOH 241 841  917  HOH HOH A . 
O 7 HOH 242 842  892  HOH HOH A . 
O 7 HOH 243 843  785  HOH HOH A . 
O 7 HOH 244 844  914  HOH HOH A . 
O 7 HOH 245 845  869  HOH HOH A . 
O 7 HOH 246 846  764  HOH HOH A . 
O 7 HOH 247 847  987  HOH HOH A . 
O 7 HOH 248 848  789  HOH HOH A . 
O 7 HOH 249 849  933  HOH HOH A . 
O 7 HOH 250 850  714  HOH HOH A . 
O 7 HOH 251 851  863  HOH HOH A . 
O 7 HOH 252 852  1012 HOH HOH A . 
O 7 HOH 253 853  796  HOH HOH A . 
O 7 HOH 254 854  866  HOH HOH A . 
O 7 HOH 255 855  983  HOH HOH A . 
O 7 HOH 256 856  624  HOH HOH A . 
O 7 HOH 257 857  974  HOH HOH A . 
O 7 HOH 258 858  620  HOH HOH A . 
O 7 HOH 259 859  787  HOH HOH A . 
O 7 HOH 260 860  653  HOH HOH A . 
O 7 HOH 261 861  931  HOH HOH A . 
O 7 HOH 262 862  883  HOH HOH A . 
O 7 HOH 263 863  625  HOH HOH A . 
O 7 HOH 264 864  689  HOH HOH A . 
O 7 HOH 265 865  731  HOH HOH A . 
O 7 HOH 266 866  713  HOH HOH A . 
O 7 HOH 267 867  698  HOH HOH A . 
O 7 HOH 268 868  992  HOH HOH A . 
O 7 HOH 269 869  732  HOH HOH A . 
O 7 HOH 270 870  846  HOH HOH A . 
O 7 HOH 271 871  722  HOH HOH A . 
O 7 HOH 272 872  848  HOH HOH A . 
O 7 HOH 273 873  650  HOH HOH A . 
O 7 HOH 274 874  775  HOH HOH A . 
O 7 HOH 275 875  896  HOH HOH A . 
O 7 HOH 276 876  838  HOH HOH A . 
O 7 HOH 277 877  1007 HOH HOH A . 
O 7 HOH 278 878  639  HOH HOH A . 
O 7 HOH 279 879  972  HOH HOH A . 
O 7 HOH 280 880  994  HOH HOH A . 
O 7 HOH 281 881  885  HOH HOH A . 
O 7 HOH 282 882  819  HOH HOH A . 
O 7 HOH 283 883  897  HOH HOH A . 
O 7 HOH 284 884  934  HOH HOH A . 
O 7 HOH 285 885  975  HOH HOH A . 
O 7 HOH 286 886  742  HOH HOH A . 
O 7 HOH 287 887  717  HOH HOH A . 
O 7 HOH 288 888  703  HOH HOH A . 
O 7 HOH 289 889  860  HOH HOH A . 
O 7 HOH 290 890  856  HOH HOH A . 
O 7 HOH 291 891  861  HOH HOH A . 
O 7 HOH 292 892  977  HOH HOH A . 
O 7 HOH 293 893  666  HOH HOH A . 
O 7 HOH 294 894  943  HOH HOH A . 
O 7 HOH 295 895  908  HOH HOH A . 
O 7 HOH 296 896  841  HOH HOH A . 
O 7 HOH 297 897  708  HOH HOH A . 
O 7 HOH 298 898  772  HOH HOH A . 
O 7 HOH 299 899  857  HOH HOH A . 
O 7 HOH 300 900  766  HOH HOH A . 
O 7 HOH 301 901  960  HOH HOH A . 
O 7 HOH 302 902  658  HOH HOH A . 
O 7 HOH 303 903  697  HOH HOH A . 
O 7 HOH 304 904  788  HOH HOH A . 
O 7 HOH 305 905  771  HOH HOH A . 
O 7 HOH 306 906  759  HOH HOH A . 
O 7 HOH 307 907  979  HOH HOH A . 
O 7 HOH 308 908  958  HOH HOH A . 
O 7 HOH 309 909  696  HOH HOH A . 
O 7 HOH 310 910  839  HOH HOH A . 
O 7 HOH 311 911  803  HOH HOH A . 
O 7 HOH 312 912  799  HOH HOH A . 
O 7 HOH 313 913  843  HOH HOH A . 
O 7 HOH 314 914  944  HOH HOH A . 
O 7 HOH 315 915  776  HOH HOH A . 
O 7 HOH 316 916  854  HOH HOH A . 
O 7 HOH 317 917  928  HOH HOH A . 
O 7 HOH 318 918  647  HOH HOH A . 
O 7 HOH 319 919  845  HOH HOH A . 
O 7 HOH 320 920  970  HOH HOH A . 
O 7 HOH 321 921  850  HOH HOH A . 
O 7 HOH 322 922  760  HOH HOH A . 
O 7 HOH 323 923  1004 HOH HOH A . 
O 7 HOH 324 924  959  HOH HOH A . 
O 7 HOH 325 925  949  HOH HOH A . 
O 7 HOH 326 926  847  HOH HOH A . 
O 7 HOH 327 927  903  HOH HOH A . 
O 7 HOH 328 928  805  HOH HOH A . 
O 7 HOH 329 929  867  HOH HOH A . 
O 7 HOH 330 930  930  HOH HOH A . 
O 7 HOH 331 931  985  HOH HOH A . 
O 7 HOH 332 932  1003 HOH HOH A . 
O 7 HOH 333 933  729  HOH HOH A . 
O 7 HOH 334 934  769  HOH HOH A . 
O 7 HOH 335 935  762  HOH HOH A . 
O 7 HOH 336 936  794  HOH HOH A . 
O 7 HOH 337 937  800  HOH HOH A . 
O 7 HOH 338 938  783  HOH HOH A . 
O 7 HOH 339 939  786  HOH HOH A . 
O 7 HOH 340 940  993  HOH HOH A . 
O 7 HOH 341 941  989  HOH HOH A . 
O 7 HOH 342 942  750  HOH HOH A . 
O 7 HOH 343 943  607  HOH HOH A . 
O 7 HOH 344 944  915  HOH HOH A . 
O 7 HOH 345 945  946  HOH HOH A . 
O 7 HOH 346 946  730  HOH HOH A . 
O 7 HOH 347 947  929  HOH HOH A . 
O 7 HOH 348 948  826  HOH HOH A . 
O 7 HOH 349 949  962  HOH HOH A . 
O 7 HOH 350 950  912  HOH HOH A . 
O 7 HOH 351 951  792  HOH HOH A . 
O 7 HOH 352 952  821  HOH HOH A . 
O 7 HOH 353 953  964  HOH HOH A . 
O 7 HOH 354 954  873  HOH HOH A . 
O 7 HOH 355 955  879  HOH HOH A . 
O 7 HOH 356 956  902  HOH HOH A . 
O 7 HOH 357 957  948  HOH HOH A . 
O 7 HOH 358 958  851  HOH HOH A . 
O 7 HOH 359 959  809  HOH HOH A . 
O 7 HOH 360 960  673  HOH HOH A . 
O 7 HOH 361 961  919  HOH HOH A . 
O 7 HOH 362 962  997  HOH HOH A . 
O 7 HOH 363 963  945  HOH HOH A . 
O 7 HOH 364 964  807  HOH HOH A . 
O 7 HOH 365 965  904  HOH HOH A . 
O 7 HOH 366 966  887  HOH HOH A . 
O 7 HOH 367 967  967  HOH HOH A . 
O 7 HOH 368 968  810  HOH HOH A . 
O 7 HOH 369 969  947  HOH HOH A . 
O 7 HOH 370 970  882  HOH HOH A . 
O 7 HOH 371 971  816  HOH HOH A . 
O 7 HOH 372 972  822  HOH HOH A . 
O 7 HOH 373 973  1008 HOH HOH A . 
O 7 HOH 374 974  820  HOH HOH A . 
O 7 HOH 375 975  886  HOH HOH A . 
O 7 HOH 376 976  918  HOH HOH A . 
O 7 HOH 377 977  905  HOH HOH A . 
O 7 HOH 378 978  951  HOH HOH A . 
O 7 HOH 379 979  694  HOH HOH A . 
O 7 HOH 380 980  781  HOH HOH A . 
O 7 HOH 381 981  924  HOH HOH A . 
O 7 HOH 382 982  955  HOH HOH A . 
O 7 HOH 383 983  936  HOH HOH A . 
O 7 HOH 384 984  733  HOH HOH A . 
O 7 HOH 385 985  777  HOH HOH A . 
O 7 HOH 386 986  888  HOH HOH A . 
O 7 HOH 387 987  870  HOH HOH A . 
O 7 HOH 388 988  767  HOH HOH A . 
O 7 HOH 389 989  778  HOH HOH A . 
O 7 HOH 390 990  965  HOH HOH A . 
O 7 HOH 391 991  871  HOH HOH A . 
O 7 HOH 392 992  735  HOH HOH A . 
O 7 HOH 393 993  969  HOH HOH A . 
O 7 HOH 394 994  891  HOH HOH A . 
O 7 HOH 395 995  998  HOH HOH A . 
O 7 HOH 396 996  906  HOH HOH A . 
O 7 HOH 397 997  657  HOH HOH A . 
O 7 HOH 398 998  907  HOH HOH A . 
O 7 HOH 399 999  734  HOH HOH A . 
O 7 HOH 400 1000 954  HOH HOH A . 
O 7 HOH 401 1001 795  HOH HOH A . 
O 7 HOH 402 1002 957  HOH HOH A . 
O 7 HOH 403 1003 774  HOH HOH A . 
O 7 HOH 404 1004 1010 HOH HOH A . 
O 7 HOH 405 1005 844  HOH HOH A . 
O 7 HOH 406 1006 963  HOH HOH A . 
O 7 HOH 407 1007 898  HOH HOH A . 
O 7 HOH 408 1008 705  HOH HOH A . 
O 7 HOH 409 1009 940  HOH HOH A . 
O 7 HOH 410 1010 836  HOH HOH A . 
O 7 HOH 411 1011 702  HOH HOH A . 
P 7 HOH 1   601  1047 HOH HOH B . 
P 7 HOH 2   602  601  HOH HOH B . 
P 7 HOH 3   603  887  HOH HOH B . 
P 7 HOH 4   604  994  HOH HOH B . 
P 7 HOH 5   605  978  HOH HOH B . 
P 7 HOH 6   606  1037 HOH HOH B . 
P 7 HOH 7   607  879  HOH HOH B . 
P 7 HOH 8   608  1043 HOH HOH B . 
P 7 HOH 9   609  864  HOH HOH B . 
P 7 HOH 10  610  780  HOH HOH B . 
P 7 HOH 11  611  990  HOH HOH B . 
P 7 HOH 12  612  956  HOH HOH B . 
P 7 HOH 13  613  844  HOH HOH B . 
P 7 HOH 14  614  963  HOH HOH B . 
P 7 HOH 15  615  738  HOH HOH B . 
P 7 HOH 16  616  882  HOH HOH B . 
P 7 HOH 17  617  691  HOH HOH B . 
P 7 HOH 18  618  787  HOH HOH B . 
P 7 HOH 19  619  1040 HOH HOH B . 
P 7 HOH 20  620  781  HOH HOH B . 
P 7 HOH 21  621  803  HOH HOH B . 
P 7 HOH 22  622  1059 HOH HOH B . 
P 7 HOH 23  623  632  HOH HOH B . 
P 7 HOH 24  624  701  HOH HOH B . 
P 7 HOH 25  625  959  HOH HOH B . 
P 7 HOH 26  626  827  HOH HOH B . 
P 7 HOH 27  627  901  HOH HOH B . 
P 7 HOH 28  628  1033 HOH HOH B . 
P 7 HOH 29  629  801  HOH HOH B . 
P 7 HOH 30  630  964  HOH HOH B . 
P 7 HOH 31  631  986  HOH HOH B . 
P 7 HOH 32  632  903  HOH HOH B . 
P 7 HOH 33  633  1046 HOH HOH B . 
P 7 HOH 34  634  811  HOH HOH B . 
P 7 HOH 35  635  868  HOH HOH B . 
P 7 HOH 36  636  989  HOH HOH B . 
P 7 HOH 37  637  812  HOH HOH B . 
P 7 HOH 38  638  997  HOH HOH B . 
P 7 HOH 39  639  653  HOH HOH B . 
P 7 HOH 40  640  863  HOH HOH B . 
P 7 HOH 41  641  629  HOH HOH B . 
P 7 HOH 42  642  872  HOH HOH B . 
P 7 HOH 43  643  960  HOH HOH B . 
P 7 HOH 44  644  967  HOH HOH B . 
P 7 HOH 45  645  828  HOH HOH B . 
P 7 HOH 46  646  654  HOH HOH B . 
P 7 HOH 47  647  644  HOH HOH B . 
P 7 HOH 48  648  662  HOH HOH B . 
P 7 HOH 49  649  606  HOH HOH B . 
P 7 HOH 50  650  878  HOH HOH B . 
P 7 HOH 51  651  614  HOH HOH B . 
P 7 HOH 52  652  768  HOH HOH B . 
P 7 HOH 53  653  612  HOH HOH B . 
P 7 HOH 54  654  839  HOH HOH B . 
P 7 HOH 55  655  832  HOH HOH B . 
P 7 HOH 56  656  1035 HOH HOH B . 
P 7 HOH 57  657  676  HOH HOH B . 
P 7 HOH 58  658  747  HOH HOH B . 
P 7 HOH 59  659  774  HOH HOH B . 
P 7 HOH 60  660  645  HOH HOH B . 
P 7 HOH 61  661  905  HOH HOH B . 
P 7 HOH 62  662  1005 HOH HOH B . 
P 7 HOH 63  663  742  HOH HOH B . 
P 7 HOH 64  664  663  HOH HOH B . 
P 7 HOH 65  665  948  HOH HOH B . 
P 7 HOH 66  666  702  HOH HOH B . 
P 7 HOH 67  667  775  HOH HOH B . 
P 7 HOH 68  668  696  HOH HOH B . 
P 7 HOH 69  669  870  HOH HOH B . 
P 7 HOH 70  670  639  HOH HOH B . 
P 7 HOH 71  671  902  HOH HOH B . 
P 7 HOH 72  672  692  HOH HOH B . 
P 7 HOH 73  673  924  HOH HOH B . 
P 7 HOH 74  674  734  HOH HOH B . 
P 7 HOH 75  675  941  HOH HOH B . 
P 7 HOH 76  676  761  HOH HOH B . 
P 7 HOH 77  677  848  HOH HOH B . 
P 7 HOH 78  678  689  HOH HOH B . 
P 7 HOH 79  679  995  HOH HOH B . 
P 7 HOH 80  680  623  HOH HOH B . 
P 7 HOH 81  681  996  HOH HOH B . 
P 7 HOH 82  682  829  HOH HOH B . 
P 7 HOH 83  683  633  HOH HOH B . 
P 7 HOH 84  684  741  HOH HOH B . 
P 7 HOH 85  685  846  HOH HOH B . 
P 7 HOH 86  686  667  HOH HOH B . 
P 7 HOH 87  687  673  HOH HOH B . 
P 7 HOH 88  688  637  HOH HOH B . 
P 7 HOH 89  689  671  HOH HOH B . 
P 7 HOH 90  690  823  HOH HOH B . 
P 7 HOH 91  691  694  HOH HOH B . 
P 7 HOH 92  692  706  HOH HOH B . 
P 7 HOH 93  693  975  HOH HOH B . 
P 7 HOH 94  694  646  HOH HOH B . 
P 7 HOH 95  695  759  HOH HOH B . 
P 7 HOH 96  696  763  HOH HOH B . 
P 7 HOH 97  697  619  HOH HOH B . 
P 7 HOH 98  698  720  HOH HOH B . 
P 7 HOH 99  699  1031 HOH HOH B . 
P 7 HOH 100 700  985  HOH HOH B . 
P 7 HOH 101 701  745  HOH HOH B . 
P 7 HOH 102 702  769  HOH HOH B . 
P 7 HOH 103 703  613  HOH HOH B . 
P 7 HOH 104 704  707  HOH HOH B . 
P 7 HOH 105 705  771  HOH HOH B . 
P 7 HOH 106 706  984  HOH HOH B . 
P 7 HOH 107 707  782  HOH HOH B . 
P 7 HOH 108 708  732  HOH HOH B . 
P 7 HOH 109 709  899  HOH HOH B . 
P 7 HOH 110 710  940  HOH HOH B . 
P 7 HOH 111 711  1066 HOH HOH B . 
P 7 HOH 112 712  650  HOH HOH B . 
P 7 HOH 113 713  873  HOH HOH B . 
P 7 HOH 114 714  658  HOH HOH B . 
P 7 HOH 115 715  631  HOH HOH B . 
P 7 HOH 116 716  744  HOH HOH B . 
P 7 HOH 117 717  824  HOH HOH B . 
P 7 HOH 118 718  729  HOH HOH B . 
P 7 HOH 119 719  753  HOH HOH B . 
P 7 HOH 120 720  625  HOH HOH B . 
P 7 HOH 121 721  957  HOH HOH B . 
P 7 HOH 122 722  862  HOH HOH B . 
P 7 HOH 123 723  703  HOH HOH B . 
P 7 HOH 124 724  668  HOH HOH B . 
P 7 HOH 125 725  764  HOH HOH B . 
P 7 HOH 126 726  721  HOH HOH B . 
P 7 HOH 127 727  1010 HOH HOH B . 
P 7 HOH 128 728  617  HOH HOH B . 
P 7 HOH 129 729  723  HOH HOH B . 
P 7 HOH 130 730  605  HOH HOH B . 
P 7 HOH 131 731  622  HOH HOH B . 
P 7 HOH 132 732  884  HOH HOH B . 
P 7 HOH 133 733  814  HOH HOH B . 
P 7 HOH 134 734  749  HOH HOH B . 
P 7 HOH 135 735  708  HOH HOH B . 
P 7 HOH 136 736  752  HOH HOH B . 
P 7 HOH 137 737  945  HOH HOH B . 
P 7 HOH 138 738  849  HOH HOH B . 
P 7 HOH 139 739  670  HOH HOH B . 
P 7 HOH 140 740  733  HOH HOH B . 
P 7 HOH 141 741  604  HOH HOH B . 
P 7 HOH 142 742  784  HOH HOH B . 
P 7 HOH 143 743  609  HOH HOH B . 
P 7 HOH 144 744  790  HOH HOH B . 
P 7 HOH 145 745  709  HOH HOH B . 
P 7 HOH 146 746  859  HOH HOH B . 
P 7 HOH 147 747  659  HOH HOH B . 
P 7 HOH 148 748  640  HOH HOH B . 
P 7 HOH 149 749  820  HOH HOH B . 
P 7 HOH 150 750  651  HOH HOH B . 
P 7 HOH 151 751  664  HOH HOH B . 
P 7 HOH 152 752  746  HOH HOH B . 
P 7 HOH 153 753  851  HOH HOH B . 
P 7 HOH 154 754  751  HOH HOH B . 
P 7 HOH 155 755  643  HOH HOH B . 
P 7 HOH 156 756  822  HOH HOH B . 
P 7 HOH 157 757  1048 HOH HOH B . 
P 7 HOH 158 758  930  HOH HOH B . 
P 7 HOH 159 759  630  HOH HOH B . 
P 7 HOH 160 760  641  HOH HOH B . 
P 7 HOH 161 761  845  HOH HOH B . 
P 7 HOH 162 762  777  HOH HOH B . 
P 7 HOH 163 763  743  HOH HOH B . 
P 7 HOH 164 764  603  HOH HOH B . 
P 7 HOH 165 765  1051 HOH HOH B . 
P 7 HOH 166 766  799  HOH HOH B . 
P 7 HOH 167 767  953  HOH HOH B . 
P 7 HOH 168 768  638  HOH HOH B . 
P 7 HOH 169 769  816  HOH HOH B . 
P 7 HOH 170 770  677  HOH HOH B . 
P 7 HOH 171 771  657  HOH HOH B . 
P 7 HOH 172 772  718  HOH HOH B . 
P 7 HOH 173 773  875  HOH HOH B . 
P 7 HOH 174 774  776  HOH HOH B . 
P 7 HOH 175 775  1021 HOH HOH B . 
P 7 HOH 176 776  1009 HOH HOH B . 
P 7 HOH 177 777  610  HOH HOH B . 
P 7 HOH 178 778  621  HOH HOH B . 
P 7 HOH 179 779  969  HOH HOH B . 
P 7 HOH 180 780  1006 HOH HOH B . 
P 7 HOH 181 781  608  HOH HOH B . 
P 7 HOH 182 782  686  HOH HOH B . 
P 7 HOH 183 783  757  HOH HOH B . 
P 7 HOH 184 784  952  HOH HOH B . 
P 7 HOH 185 785  736  HOH HOH B . 
P 7 HOH 186 786  635  HOH HOH B . 
P 7 HOH 187 787  661  HOH HOH B . 
P 7 HOH 188 788  652  HOH HOH B . 
P 7 HOH 189 789  1003 HOH HOH B . 
P 7 HOH 190 790  1060 HOH HOH B . 
P 7 HOH 191 791  705  HOH HOH B . 
P 7 HOH 192 792  772  HOH HOH B . 
P 7 HOH 193 793  917  HOH HOH B . 
P 7 HOH 194 794  634  HOH HOH B . 
P 7 HOH 195 795  965  HOH HOH B . 
P 7 HOH 196 796  680  HOH HOH B . 
P 7 HOH 197 797  789  HOH HOH B . 
P 7 HOH 198 798  697  HOH HOH B . 
P 7 HOH 199 799  647  HOH HOH B . 
P 7 HOH 200 800  750  HOH HOH B . 
P 7 HOH 201 801  624  HOH HOH B . 
P 7 HOH 202 802  699  HOH HOH B . 
P 7 HOH 203 803  754  HOH HOH B . 
P 7 HOH 204 804  934  HOH HOH B . 
P 7 HOH 205 805  932  HOH HOH B . 
P 7 HOH 206 806  700  HOH HOH B . 
P 7 HOH 207 807  616  HOH HOH B . 
P 7 HOH 208 808  674  HOH HOH B . 
P 7 HOH 209 809  1034 HOH HOH B . 
P 7 HOH 210 810  802  HOH HOH B . 
P 7 HOH 211 811  955  HOH HOH B . 
P 7 HOH 212 812  602  HOH HOH B . 
P 7 HOH 213 813  788  HOH HOH B . 
P 7 HOH 214 814  880  HOH HOH B . 
P 7 HOH 215 815  711  HOH HOH B . 
P 7 HOH 216 816  611  HOH HOH B . 
P 7 HOH 217 817  626  HOH HOH B . 
P 7 HOH 218 818  1019 HOH HOH B . 
P 7 HOH 219 819  1052 HOH HOH B . 
P 7 HOH 220 820  672  HOH HOH B . 
P 7 HOH 221 821  1041 HOH HOH B . 
P 7 HOH 222 822  1004 HOH HOH B . 
P 7 HOH 223 823  1063 HOH HOH B . 
P 7 HOH 224 824  607  HOH HOH B . 
P 7 HOH 225 825  618  HOH HOH B . 
P 7 HOH 226 826  993  HOH HOH B . 
P 7 HOH 227 827  727  HOH HOH B . 
P 7 HOH 228 828  958  HOH HOH B . 
P 7 HOH 229 829  779  HOH HOH B . 
P 7 HOH 230 830  987  HOH HOH B . 
P 7 HOH 231 831  683  HOH HOH B . 
P 7 HOH 232 832  642  HOH HOH B . 
P 7 HOH 233 833  907  HOH HOH B . 
P 7 HOH 234 834  687  HOH HOH B . 
P 7 HOH 235 835  766  HOH HOH B . 
P 7 HOH 236 836  693  HOH HOH B . 
P 7 HOH 237 837  675  HOH HOH B . 
P 7 HOH 238 838  889  HOH HOH B . 
P 7 HOH 239 839  918  HOH HOH B . 
P 7 HOH 240 840  911  HOH HOH B . 
P 7 HOH 241 841  1039 HOH HOH B . 
P 7 HOH 242 842  831  HOH HOH B . 
P 7 HOH 243 843  880  HOH HOH B . 
P 7 HOH 244 844  867  HOH HOH B . 
P 7 HOH 245 845  961  HOH HOH B . 
P 7 HOH 246 846  1065 HOH HOH B . 
P 7 HOH 247 847  946  HOH HOH B . 
P 7 HOH 248 848  756  HOH HOH B . 
P 7 HOH 249 849  972  HOH HOH B . 
P 7 HOH 250 850  1032 HOH HOH B . 
P 7 HOH 251 851  976  HOH HOH B . 
P 7 HOH 252 852  833  HOH HOH B . 
P 7 HOH 253 853  786  HOH HOH B . 
P 7 HOH 254 854  722  HOH HOH B . 
P 7 HOH 255 855  853  HOH HOH B . 
P 7 HOH 256 856  682  HOH HOH B . 
P 7 HOH 257 857  628  HOH HOH B . 
P 7 HOH 258 858  798  HOH HOH B . 
P 7 HOH 259 859  695  HOH HOH B . 
P 7 HOH 260 860  944  HOH HOH B . 
P 7 HOH 261 861  726  HOH HOH B . 
P 7 HOH 262 862  1002 HOH HOH B . 
P 7 HOH 263 863  690  HOH HOH B . 
P 7 HOH 264 864  627  HOH HOH B . 
P 7 HOH 265 865  770  HOH HOH B . 
P 7 HOH 266 866  660  HOH HOH B . 
P 7 HOH 267 867  835  HOH HOH B . 
P 7 HOH 268 868  688  HOH HOH B . 
P 7 HOH 269 869  765  HOH HOH B . 
P 7 HOH 270 870  760  HOH HOH B . 
P 7 HOH 271 871  785  HOH HOH B . 
P 7 HOH 272 872  805  HOH HOH B . 
P 7 HOH 273 873  648  HOH HOH B . 
P 7 HOH 274 874  679  HOH HOH B . 
P 7 HOH 275 875  854  HOH HOH B . 
P 7 HOH 276 876  876  HOH HOH B . 
P 7 HOH 277 877  730  HOH HOH B . 
P 7 HOH 278 878  809  HOH HOH B . 
P 7 HOH 279 879  740  HOH HOH B . 
P 7 HOH 280 880  762  HOH HOH B . 
P 7 HOH 281 881  710  HOH HOH B . 
P 7 HOH 282 882  719  HOH HOH B . 
P 7 HOH 283 883  877  HOH HOH B . 
P 7 HOH 284 884  914  HOH HOH B . 
P 7 HOH 285 885  717  HOH HOH B . 
P 7 HOH 286 886  856  HOH HOH B . 
P 7 HOH 287 887  886  HOH HOH B . 
P 7 HOH 288 888  819  HOH HOH B . 
P 7 HOH 289 889  791  HOH HOH B . 
P 7 HOH 290 890  796  HOH HOH B . 
P 7 HOH 291 891  1025 HOH HOH B . 
P 7 HOH 292 892  712  HOH HOH B . 
P 7 HOH 293 893  850  HOH HOH B . 
P 7 HOH 294 894  656  HOH HOH B . 
P 7 HOH 295 895  704  HOH HOH B . 
P 7 HOH 296 896  892  HOH HOH B . 
P 7 HOH 297 897  861  HOH HOH B . 
P 7 HOH 298 898  685  HOH HOH B . 
P 7 HOH 299 899  1038 HOH HOH B . 
P 7 HOH 300 900  636  HOH HOH B . 
P 7 HOH 301 901  847  HOH HOH B . 
P 7 HOH 302 902  669  HOH HOH B . 
P 7 HOH 303 903  891  HOH HOH B . 
P 7 HOH 304 904  842  HOH HOH B . 
P 7 HOH 305 905  909  HOH HOH B . 
P 7 HOH 306 906  724  HOH HOH B . 
P 7 HOH 307 907  739  HOH HOH B . 
P 7 HOH 308 908  755  HOH HOH B . 
P 7 HOH 309 909  767  HOH HOH B . 
P 7 HOH 310 910  615  HOH HOH B . 
P 7 HOH 311 911  883  HOH HOH B . 
P 7 HOH 312 912  666  HOH HOH B . 
P 7 HOH 313 913  1030 HOH HOH B . 
P 7 HOH 314 914  966  HOH HOH B . 
P 7 HOH 315 915  773  HOH HOH B . 
P 7 HOH 316 916  748  HOH HOH B . 
P 7 HOH 317 917  855  HOH HOH B . 
P 7 HOH 318 918  912  HOH HOH B . 
P 7 HOH 319 919  1015 HOH HOH B . 
P 7 HOH 320 920  865  HOH HOH B . 
P 7 HOH 321 921  728  HOH HOH B . 
P 7 HOH 322 922  665  HOH HOH B . 
P 7 HOH 323 923  1050 HOH HOH B . 
P 7 HOH 324 924  929  HOH HOH B . 
P 7 HOH 325 925  1027 HOH HOH B . 
P 7 HOH 326 926  792  HOH HOH B . 
P 7 HOH 327 927  793  HOH HOH B . 
P 7 HOH 328 928  810  HOH HOH B . 
P 7 HOH 329 929  1062 HOH HOH B . 
P 7 HOH 330 930  900  HOH HOH B . 
P 7 HOH 331 931  991  HOH HOH B . 
P 7 HOH 332 932  1020 HOH HOH B . 
P 7 HOH 333 933  913  HOH HOH B . 
P 7 HOH 334 934  977  HOH HOH B . 
P 7 HOH 335 935  860  HOH HOH B . 
P 7 HOH 336 936  698  HOH HOH B . 
P 7 HOH 337 937  1067 HOH HOH B . 
P 7 HOH 338 938  830  HOH HOH B . 
P 7 HOH 339 939  897  HOH HOH B . 
P 7 HOH 340 940  684  HOH HOH B . 
P 7 HOH 341 941  881  HOH HOH B . 
P 7 HOH 342 942  942  HOH HOH B . 
P 7 HOH 343 943  925  HOH HOH B . 
P 7 HOH 344 944  866  HOH HOH B . 
P 7 HOH 345 945  937  HOH HOH B . 
P 7 HOH 346 946  983  HOH HOH B . 
P 7 HOH 347 947  649  HOH HOH B . 
P 7 HOH 348 948  971  HOH HOH B . 
P 7 HOH 349 949  834  HOH HOH B . 
P 7 HOH 350 950  1018 HOH HOH B . 
P 7 HOH 351 951  725  HOH HOH B . 
P 7 HOH 352 952  896  HOH HOH B . 
P 7 HOH 353 953  806  HOH HOH B . 
P 7 HOH 354 954  1042 HOH HOH B . 
P 7 HOH 355 955  813  HOH HOH B . 
P 7 HOH 356 956  1029 HOH HOH B . 
P 7 HOH 357 957  1008 HOH HOH B . 
P 7 HOH 358 958  713  HOH HOH B . 
P 7 HOH 359 959  821  HOH HOH B . 
P 7 HOH 360 960  1023 HOH HOH B . 
P 7 HOH 361 961  1055 HOH HOH B . 
P 7 HOH 362 962  919  HOH HOH B . 
P 7 HOH 363 963  1045 HOH HOH B . 
P 7 HOH 364 964  1007 HOH HOH B . 
P 7 HOH 365 965  1044 HOH HOH B . 
P 7 HOH 366 966  815  HOH HOH B . 
P 7 HOH 367 967  998  HOH HOH B . 
P 7 HOH 368 968  778  HOH HOH B . 
P 7 HOH 369 969  1000 HOH HOH B . 
P 7 HOH 370 970  921  HOH HOH B . 
P 7 HOH 371 971  857  HOH HOH B . 
P 7 HOH 372 972  936  HOH HOH B . 
P 7 HOH 373 973  1058 HOH HOH B . 
P 7 HOH 374 974  986  HOH HOH B . 
P 7 HOH 375 975  982  HOH HOH B . 
P 7 HOH 376 976  1014 HOH HOH B . 
P 7 HOH 377 977  939  HOH HOH B . 
P 7 HOH 378 978  1057 HOH HOH B . 
P 7 HOH 379 979  818  HOH HOH B . 
P 7 HOH 380 980  843  HOH HOH B . 
P 7 HOH 381 981  817  HOH HOH B . 
P 7 HOH 382 982  800  HOH HOH B . 
P 7 HOH 383 983  885  HOH HOH B . 
P 7 HOH 384 984  938  HOH HOH B . 
P 7 HOH 385 985  973  HOH HOH B . 
P 7 HOH 386 986  1022 HOH HOH B . 
P 7 HOH 387 987  1049 HOH HOH B . 
P 7 HOH 388 988  962  HOH HOH B . 
P 7 HOH 389 989  620  HOH HOH B . 
P 7 HOH 390 990  949  HOH HOH B . 
P 7 HOH 391 991  804  HOH HOH B . 
P 7 HOH 392 992  1054 HOH HOH B . 
P 7 HOH 393 993  871  HOH HOH B . 
P 7 HOH 394 994  825  HOH HOH B . 
P 7 HOH 395 995  951  HOH HOH B . 
P 7 HOH 396 996  1056 HOH HOH B . 
P 7 HOH 397 997  935  HOH HOH B . 
P 7 HOH 398 998  716  HOH HOH B . 
P 7 HOH 399 999  1017 HOH HOH B . 
P 7 HOH 400 1000 895  HOH HOH B . 
P 7 HOH 401 1001 808  HOH HOH B . 
P 7 HOH 402 1002 922  HOH HOH B . 
P 7 HOH 403 1003 928  HOH HOH B . 
P 7 HOH 404 1004 837  HOH HOH B . 
P 7 HOH 405 1005 836  HOH HOH B . 
P 7 HOH 406 1006 927  HOH HOH B . 
P 7 HOH 407 1007 906  HOH HOH B . 
P 7 HOH 408 1008 858  HOH HOH B . 
P 7 HOH 409 1009 795  HOH HOH B . 
P 7 HOH 410 1010 888  HOH HOH B . 
P 7 HOH 411 1011 1036 HOH HOH B . 
P 7 HOH 412 1012 1028 HOH HOH B . 
P 7 HOH 413 1013 1053 HOH HOH B . 
P 7 HOH 414 1014 797  HOH HOH B . 
P 7 HOH 415 1015 737  HOH HOH B . 
P 7 HOH 416 1016 970  HOH HOH B . 
P 7 HOH 417 1017 920  HOH HOH B . 
P 7 HOH 418 1018 731  HOH HOH B . 
P 7 HOH 419 1019 908  HOH HOH B . 
P 7 HOH 420 1020 1013 HOH HOH B . 
P 7 HOH 421 1021 874  HOH HOH B . 
P 7 HOH 422 1022 714  HOH HOH B . 
P 7 HOH 423 1023 840  HOH HOH B . 
P 7 HOH 424 1024 890  HOH HOH B . 
P 7 HOH 425 1025 1016 HOH HOH B . 
P 7 HOH 426 1026 678  HOH HOH B . 
P 7 HOH 427 1027 807  HOH HOH B . 
P 7 HOH 428 1028 783  HOH HOH B . 
P 7 HOH 429 1029 992  HOH HOH B . 
P 7 HOH 430 1030 894  HOH HOH B . 
P 7 HOH 431 1031 910  HOH HOH B . 
P 7 HOH 432 1032 1012 HOH HOH B . 
P 7 HOH 433 1033 926  HOH HOH B . 
P 7 HOH 434 1034 981  HOH HOH B . 
P 7 HOH 435 1035 869  HOH HOH B . 
P 7 HOH 436 1036 904  HOH HOH B . 
P 7 HOH 437 1037 681  HOH HOH B . 
P 7 HOH 438 1038 758  HOH HOH B . 
P 7 HOH 439 1039 931  HOH HOH B . 
P 7 HOH 440 1040 950  HOH HOH B . 
P 7 HOH 441 1041 933  HOH HOH B . 
P 7 HOH 442 1042 794  HOH HOH B . 
P 7 HOH 443 1043 923  HOH HOH B . 
P 7 HOH 444 1044 898  HOH HOH B . 
P 7 HOH 445 1045 735  HOH HOH B . 
P 7 HOH 446 1046 1024 HOH HOH B . 
P 7 HOH 447 1047 988  HOH HOH B . 
P 7 HOH 448 1048 915  HOH HOH B . 
P 7 HOH 449 1049 943  HOH HOH B . 
P 7 HOH 450 1050 954  HOH HOH B . 
P 7 HOH 451 1051 841  HOH HOH B . 
P 7 HOH 452 1052 1001 HOH HOH B . 
P 7 HOH 453 1053 980  HOH HOH B . 
P 7 HOH 454 1054 715  HOH HOH B . 
P 7 HOH 455 1055 947  HOH HOH B . 
P 7 HOH 456 1056 826  HOH HOH B . 
P 7 HOH 457 1057 1064 HOH HOH B . 
P 7 HOH 458 1058 999  HOH HOH B . 
P 7 HOH 459 1059 852  HOH HOH B . 
P 7 HOH 460 1060 916  HOH HOH B . 
P 7 HOH 461 1061 968  HOH HOH B . 
P 7 HOH 462 1062 838  HOH HOH B . 
P 7 HOH 463 1063 974  HOH HOH B . 
P 7 HOH 464 1064 893  HOH HOH B . 
P 7 HOH 465 1065 655  HOH HOH B . 
P 7 HOH 466 1066 1011 HOH HOH B . 
P 7 HOH 467 1067 979  HOH HOH B . 
P 7 HOH 468 1068 1026 HOH HOH B . 
P 7 HOH 469 1069 1061 HOH HOH B . 
# 
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 ? ? ? 'Jan 10, 2022  BUILT=20220220' 2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487                    3 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? 0.9.8.7                        4 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? 'Jan 10, 2022  BUILT=20220220' 5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KT5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     59.130 
_cell.length_a_esd                 ? 
_cell.length_b                     129.340 
_cell.length_b_esd                 ? 
_cell.length_c                     150.150 
_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                         9KT5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9KT5 
_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             2.76 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.5 
_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          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.4 
_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    
'50 mM Tris-HCl buffer, 120 mM MgCl2, 16-18% PEG 8000, 0.2 mM N-Enanthyl-L-Prolyl-L-Phenylalanine, 1%(v/v) styrene' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-07-20 
_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                    Si 
_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   1.00 
_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                        'SPRING-8 BEAMLINE BL32XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL32XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9KT5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.6 
_reflns.d_resolution_low                               43.64 
_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                                     152182 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                19.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.85 
_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                                0.311 
_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                                   0.987 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.303 
_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   ? 1.13  ? ? ? ? 24982 ? ? ? ? ? ? ? ? ? ? ? 18.2  ? ? ? ?     ? ? 1 1 0.564 ? ? 100.0 ? 2.883 ? ? ? ? ? ? ? ? ? 
1.70 1.81  ? 2.15  ? ? ? ? 21560 ? ? ? ? ? ? ? ? ? ? ? 18.7  ? ? ? ?     ? ? 2 1 0.814 ? ? 100.0 ? 1.461 ? ? ? ? ? ? ? ? ? 
1.81 1.96  ? 3.89  ? ? ? ? 22191 ? ? ? ? ? ? ? ? ? ? ? 20.6  ? ? ? 0.887 ? ? 3 1 0.922 ? ? 100.0 ? 0.866 ? ? ? ? ? ? ? ? ? 
1.96 2.15  ? 6.71  ? ? ? ? 19959 ? ? ? ? ? ? ? ? ? ? ? 20.49 ? ? ? 0.535 ? ? 4 1 0.961 ? ? 100.0 ? 0.522 ? ? ? ? ? ? ? ? ? 
2.15 2.4   ? 10.14 ? ? ? ? 17597 ? ? ? ? ? ? ? ? ? ? ? 20.2  ? ? ? 0.355 ? ? 5 1 0.973 ? ? 100.0 ? 0.346 ? ? ? ? ? ? ? ? ? 
2.40 2.77  ? 13.43 ? ? ? ? 15803 ? ? ? ? ? ? ? ? ? ? ? 19.4  ? ? ? 0.269 ? ? 6 1 0.981 ? ? 100.0 ? 0.262 ? ? ? ? ? ? ? ? ? 
2.77 3.39  ? 17.29 ? ? ? ? 13461 ? ? ? ? ? ? ? ? ? ? ? 17.9  ? ? ? 0.208 ? ? 7 1 0.986 ? ? 100.0 ? 0.202 ? ? ? ? ? ? ? ? ? 
3.39 4.8   ? 25.69 ? ? ? ? 10598 ? ? ? ? ? ? ? ? ? ? ? 21.0  ? ? ? 0.171 ? ? 8 1 0.981 ? ? 100.0 ? 0.167 ? ? ? ? ? ? ? ? ? 
4.80 43.64 ? 25.89 ? ? ? ? 6031  ? ? ? ? ? ? ? ? ? ? ? 20.2  ? ? ? 0.158 ? ? 9 1 0.984 ? ? 99.8  ? 0.153 ? ? ? ? ? ? ? ? ? 
# 
_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                                 9KT5 
_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                             43.64 
_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                     147863 
_refine.ls_number_reflns_R_free                  7420 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.75 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1515 
_refine.ls_R_factor_R_free                       0.2003 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1490 
_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                          1.33 
_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            'Random selection' 
_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                 18.12 
_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                            0.21 
_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.pdbx_number_atoms_protein        7328 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         182 
_refine_hist.number_atoms_solvent             880 
_refine_hist.number_atoms_total               8390 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        43.64 
# 
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' ? 0.006  ? 7775  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.820  ? 10552 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.332 ? 2981  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.049  ? 1115  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 1385  ? 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  . . 93  1849 39.00  . . . . 0.3308 . . . . . . . . . . . 0.4070 
'X-RAY DIFFRACTION' 1.62 1.64  . . 236 4418 93.00  . . . . 0.3063 . . . . . . . . . . . 0.3878 
'X-RAY DIFFRACTION' 1.64 1.66  . . 245 4710 100.00 . . . . 0.2724 . . . . . . . . . . . 0.3532 
'X-RAY DIFFRACTION' 1.66 1.68  . . 266 4756 100.00 . . . . 0.2611 . . . . . . . . . . . 0.3039 
'X-RAY DIFFRACTION' 1.68 1.70  . . 249 4705 100.00 . . . . 0.2259 . . . . . . . . . . . 0.3132 
'X-RAY DIFFRACTION' 1.70 1.73  . . 249 4746 100.00 . . . . 0.1924 . . . . . . . . . . . 0.2872 
'X-RAY DIFFRACTION' 1.73 1.75  . . 279 4742 100.00 . . . . 0.1759 . . . . . . . . . . . 0.2442 
'X-RAY DIFFRACTION' 1.75 1.78  . . 228 4734 100.00 . . . . 0.1689 . . . . . . . . . . . 0.2465 
'X-RAY DIFFRACTION' 1.78 1.81  . . 273 4752 100.00 . . . . 0.1502 . . . . . . . . . . . 0.2307 
'X-RAY DIFFRACTION' 1.81 1.84  . . 244 4753 100.00 . . . . 0.1344 . . . . . . . . . . . 0.2053 
'X-RAY DIFFRACTION' 1.84 1.87  . . 262 4718 100.00 . . . . 0.1344 . . . . . . . . . . . 0.2245 
'X-RAY DIFFRACTION' 1.87 1.90  . . 268 4754 100.00 . . . . 0.1442 . . . . . . . . . . . 0.2038 
'X-RAY DIFFRACTION' 1.90 1.94  . . 261 4718 100.00 . . . . 0.1456 . . . . . . . . . . . 0.2210 
'X-RAY DIFFRACTION' 1.94 1.98  . . 243 4798 100.00 . . . . 0.1552 . . . . . . . . . . . 0.2235 
'X-RAY DIFFRACTION' 1.98 2.02  . . 230 4779 100.00 . . . . 0.1600 . . . . . . . . . . . 0.2053 
'X-RAY DIFFRACTION' 2.02 2.07  . . 264 4739 100.00 . . . . 0.1316 . . . . . . . . . . . 0.1975 
'X-RAY DIFFRACTION' 2.07 2.12  . . 269 4775 100.00 . . . . 0.1263 . . . . . . . . . . . 0.1837 
'X-RAY DIFFRACTION' 2.12 2.18  . . 257 4766 100.00 . . . . 0.1271 . . . . . . . . . . . 0.1885 
'X-RAY DIFFRACTION' 2.18 2.24  . . 265 4744 100.00 . . . . 0.1270 . . . . . . . . . . . 0.1855 
'X-RAY DIFFRACTION' 2.24 2.31  . . 232 4787 100.00 . . . . 0.1279 . . . . . . . . . . . 0.1915 
'X-RAY DIFFRACTION' 2.31 2.40  . . 221 4823 100.00 . . . . 0.1260 . . . . . . . . . . . 0.1904 
'X-RAY DIFFRACTION' 2.40 2.49  . . 270 4793 100.00 . . . . 0.1260 . . . . . . . . . . . 0.1708 
'X-RAY DIFFRACTION' 2.49 2.60  . . 254 4776 100.00 . . . . 0.1313 . . . . . . . . . . . 0.1781 
'X-RAY DIFFRACTION' 2.60 2.74  . . 219 4860 100.00 . . . . 0.1442 . . . . . . . . . . . 0.1950 
'X-RAY DIFFRACTION' 2.74 2.91  . . 279 4780 100.00 . . . . 0.1446 . . . . . . . . . . . 0.1969 
'X-RAY DIFFRACTION' 2.91 3.14  . . 244 4849 100.00 . . . . 0.1524 . . . . . . . . . . . 0.1881 
'X-RAY DIFFRACTION' 3.14 3.45  . . 252 4865 100.00 . . . . 0.1468 . . . . . . . . . . . 0.1999 
'X-RAY DIFFRACTION' 3.45 3.95  . . 241 4905 100.00 . . . . 0.1374 . . . . . . . . . . . 0.1699 
'X-RAY DIFFRACTION' 3.95 4.98  . . 245 4934 100.00 . . . . 0.1351 . . . . . . . . . . . 0.1599 
'X-RAY DIFFRACTION' 4.98 43.64 . . 282 5115 100.00 . . . . 0.1738 . . . . . . . . . . . 0.2007 
# 
_struct.entry_id                     9KT5 
_struct.title                        
;Synchrotron X-ray crystal structure of oxygen-bound F87A/F393H P450BM3 with decoy C7ProPhe (N-enanthyl-L-prolyl-L-phenylalanine) and substrate styrene at 2 MGy X-ray dose
;
_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        9KT5 
_struct_keywords.text            'Cytochrome P450, heme enzyme, 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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 6 ? 
M N N 6 ? 
N N N 6 ? 
O N N 7 ? 
P N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CPXB_PRIM2 
_struct_ref.pdbx_db_accession          P14779 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVR
DFAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFN
YRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLN
GKDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLN
EALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRA
CIGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
;
_struct_ref.pdbx_align_begin           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 9KT5 A 1 ? 456 ? P14779 1 ? 456 ? 0 455 
2 1 9KT5 B 1 ? 456 ? P14779 1 ? 456 ? 0 455 
# 
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 9KT5 ALA A 88  ? UNP P14779 PHE 88  'engineered mutation' 87  1 
1 9KT5 HIS A 394 ? UNP P14779 PHE 394 'engineered mutation' 393 2 
2 9KT5 ALA B 88  ? UNP P14779 PHE 88  'engineered mutation' 87  3 
2 9KT5 HIS B 394 ? UNP P14779 PHE 394 'engineered mutation' 393 4 
# 
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 ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
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)' 0     ? 
1 MORE         0     ? 
1 'SSA (A^2)'  19840 ? 
2 'ABSA (A^2)' 230   ? 
2 MORE         0     ? 
2 'SSA (A^2)'  19770 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,O     
2 1 B,H,I,J,K,L,M,N,P 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 'gel filtration' ? 
2 2 'gel filtration' ? 
# 
_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 PHE A 12  ? LYS A 16  ? PHE A 11  LYS A 15  5 ? 5  
HELX_P HELX_P2  AA2 ASN A 17  ? ASN A 22  ? ASN A 16  ASN A 21  5 ? 6  
HELX_P HELX_P3  AA3 LYS A 25  ? GLY A 38  ? LYS A 24  GLY A 37  1 ? 14 
HELX_P HELX_P4  AA4 SER A 55  ? CYS A 63  ? SER A 54  CYS A 62  1 ? 9  
HELX_P HELX_P5  AA5 SER A 73  ? GLY A 84  ? SER A 72  GLY A 83  1 ? 12 
HELX_P HELX_P6  AA6 GLU A 94  ? LEU A 105 ? GLU A 93  LEU A 104 1 ? 12 
HELX_P HELX_P7  AA7 PRO A 106 ? PHE A 108 ? PRO A 105 PHE A 107 5 ? 3  
HELX_P HELX_P8  AA8 SER A 109 ? ARG A 133 ? SER A 108 ARG A 132 1 ? 25 
HELX_P HELX_P9  AA9 VAL A 142 ? ASN A 160 ? VAL A 141 ASN A 159 1 ? 19 
HELX_P HELX_P10 AB1 ASN A 164 ? ARG A 168 ? ASN A 163 ARG A 167 5 ? 5  
HELX_P HELX_P11 AB2 HIS A 172 ? LEU A 189 ? HIS A 171 LEU A 188 1 ? 18 
HELX_P HELX_P12 AB3 ASP A 196 ? ALA A 198 ? ASP A 195 ALA A 197 5 ? 3  
HELX_P HELX_P13 AB4 TYR A 199 ? SER A 227 ? TYR A 198 SER A 226 1 ? 29 
HELX_P HELX_P14 AB5 ASP A 233 ? GLY A 241 ? ASP A 232 GLY A 240 1 ? 9  
HELX_P HELX_P15 AB6 ASP A 251 ? GLY A 266 ? ASP A 250 GLY A 265 1 ? 16 
HELX_P HELX_P16 AB7 HIS A 267 ? ASN A 284 ? HIS A 266 ASN A 283 1 ? 18 
HELX_P HELX_P17 AB8 ASN A 284 ? LEU A 299 ? ASN A 283 LEU A 298 1 ? 16 
HELX_P HELX_P18 AB9 SER A 305 ? LYS A 310 ? SER A 304 LYS A 309 1 ? 6  
HELX_P HELX_P19 AC1 LEU A 312 ? TRP A 326 ? LEU A 311 TRP A 325 1 ? 15 
HELX_P HELX_P20 AC2 ILE A 358 ? HIS A 362 ? ILE A 357 HIS A 361 1 ? 5  
HELX_P HELX_P21 AC3 ASP A 364 ? GLY A 369 ? ASP A 363 GLY A 368 1 ? 6  
HELX_P HELX_P22 AC4 ARG A 376 ? GLU A 381 ? ARG A 375 GLU A 380 5 ? 6  
HELX_P HELX_P23 AC5 ASN A 382 ? ILE A 386 ? ASN A 381 ILE A 385 5 ? 5  
HELX_P HELX_P24 AC6 ASN A 396 ? ALA A 400 ? ASN A 395 ALA A 399 5 ? 5  
HELX_P HELX_P25 AC7 GLY A 403 ? HIS A 421 ? GLY A 402 HIS A 420 1 ? 19 
HELX_P HELX_P26 AC8 PHE B 12  ? LYS B 16  ? PHE B 11  LYS B 15  5 ? 5  
HELX_P HELX_P27 AC9 ASN B 17  ? ASN B 22  ? ASN B 16  ASN B 21  5 ? 6  
HELX_P HELX_P28 AD1 LYS B 25  ? GLY B 38  ? LYS B 24  GLY B 37  1 ? 14 
HELX_P HELX_P29 AD2 SER B 55  ? CYS B 63  ? SER B 54  CYS B 62  1 ? 9  
HELX_P HELX_P30 AD3 SER B 73  ? GLY B 84  ? SER B 72  GLY B 83  1 ? 12 
HELX_P HELX_P31 AD4 GLU B 94  ? LEU B 105 ? GLU B 93  LEU B 104 1 ? 12 
HELX_P HELX_P32 AD5 PRO B 106 ? PHE B 108 ? PRO B 105 PHE B 107 5 ? 3  
HELX_P HELX_P33 AD6 SER B 109 ? ARG B 133 ? SER B 108 ARG B 132 1 ? 25 
HELX_P HELX_P34 AD7 VAL B 142 ? ASN B 160 ? VAL B 141 ASN B 159 1 ? 19 
HELX_P HELX_P35 AD8 ASN B 164 ? ARG B 168 ? ASN B 163 ARG B 167 5 ? 5  
HELX_P HELX_P36 AD9 HIS B 172 ? LEU B 189 ? HIS B 171 LEU B 188 1 ? 18 
HELX_P HELX_P37 AE1 ASP B 196 ? ALA B 198 ? ASP B 195 ALA B 197 5 ? 3  
HELX_P HELX_P38 AE2 TYR B 199 ? SER B 227 ? TYR B 198 SER B 226 1 ? 29 
HELX_P HELX_P39 AE3 ASP B 233 ? GLY B 241 ? ASP B 232 GLY B 240 1 ? 9  
HELX_P HELX_P40 AE4 ASP B 251 ? GLY B 266 ? ASP B 250 GLY B 265 1 ? 16 
HELX_P HELX_P41 AE5 HIS B 267 ? ASN B 284 ? HIS B 266 ASN B 283 1 ? 18 
HELX_P HELX_P42 AE6 ASN B 284 ? LEU B 299 ? ASN B 283 LEU B 298 1 ? 16 
HELX_P HELX_P43 AE7 SER B 305 ? GLN B 311 ? SER B 304 GLN B 310 1 ? 7  
HELX_P HELX_P44 AE8 LEU B 312 ? TRP B 326 ? LEU B 311 TRP B 325 1 ? 15 
HELX_P HELX_P45 AE9 GLY B 343 ? GLU B 345 ? GLY B 342 GLU B 344 5 ? 3  
HELX_P HELX_P46 AF1 ILE B 358 ? HIS B 362 ? ILE B 357 HIS B 361 1 ? 5  
HELX_P HELX_P47 AF2 ASP B 364 ? GLY B 369 ? ASP B 363 GLY B 368 1 ? 6  
HELX_P HELX_P48 AF3 ARG B 376 ? GLU B 381 ? ARG B 375 GLU B 380 5 ? 6  
HELX_P HELX_P49 AF4 ASN B 382 ? ILE B 386 ? ASN B 381 ILE B 385 5 ? 5  
HELX_P HELX_P50 AF5 ASN B 396 ? ALA B 400 ? ASN B 395 ALA B 399 5 ? 5  
HELX_P HELX_P51 AF6 GLY B 403 ? HIS B 421 ? GLY B 402 HIS B 420 1 ? 19 
# 
_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 401 SG ? ? ? 1_555 C HEM . FE A ? A CYS 400 A HEM 501 1_555 ? ? ? ? ? ? ? 2.425 ? ? 
metalc2 metalc ? ? A CYS 401 SG ? ? ? 1_555 C HEM . FE B ? A CYS 400 A HEM 501 1_555 ? ? ? ? ? ? ? 2.368 ? ? 
metalc3 metalc ? ? C HEM .   FE A ? ? 1_555 E OXY . O1 A ? A HEM 501 A OXY 503 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
metalc4 metalc ? ? B CYS 401 SG ? ? ? 1_555 H HEM . FE A ? B CYS 400 B HEM 501 1_555 ? ? ? ? ? ? ? 2.428 ? ? 
metalc5 metalc ? ? B CYS 401 SG ? ? ? 1_555 H HEM . FE B ? B CYS 400 B HEM 501 1_555 ? ? ? ? ? ? ? 2.367 ? ? 
metalc6 metalc ? ? H HEM .   FE A ? ? 1_555 J OXY . O1 A ? B HEM 501 B OXY 503 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
# 
_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 401 ? A CYS 400 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 NA ? C HEM . ? A HEM 501 ? 1_555 97.7  ? 
2  SG ? A CYS 401 ? A CYS 400 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 88.2  ? 
3  NA ? C HEM .   ? A HEM 501 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 88.4  ? 
4  SG ? A CYS 401 ? A CYS 400 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 83.5  ? 
5  NA ? C HEM .   ? A HEM 501 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 176.6 ? 
6  NB ? C HEM .   ? A HEM 501 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 88.5  ? 
7  SG ? A CYS 401 ? A CYS 400 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 92.9  ? 
8  NA ? C HEM .   ? A HEM 501 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 91.5  ? 
9  NB ? C HEM .   ? A HEM 501 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 178.8 ? 
10 NC ? C HEM .   ? A HEM 501 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 91.6  ? 
11 SG ? A CYS 401 ? A CYS 400 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 O1 A E OXY . ? A OXY 503 ? 1_555 177.0 ? 
12 NA ? C HEM .   ? A HEM 501 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 O1 A E OXY . ? A OXY 503 ? 1_555 84.4  ? 
13 NB ? C HEM .   ? A HEM 501 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 O1 A E OXY . ? A OXY 503 ? 1_555 89.6  ? 
14 NC ? C HEM .   ? A HEM 501 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 O1 A E OXY . ? A OXY 503 ? 1_555 94.3  ? 
15 ND ? C HEM .   ? A HEM 501 ? 1_555 FE A C HEM . ? A HEM 501 ? 1_555 O1 A E OXY . ? A OXY 503 ? 1_555 89.3  ? 
16 SG ? A CYS 401 ? A CYS 400 ? 1_555 FE B C HEM . ? A HEM 501 ? 1_555 NA ? C HEM . ? A HEM 501 ? 1_555 99.5  ? 
17 SG ? A CYS 401 ? A CYS 400 ? 1_555 FE B C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 89.2  ? 
18 NA ? C HEM .   ? A HEM 501 ? 1_555 FE B C HEM . ? A HEM 501 ? 1_555 NB ? C HEM . ? A HEM 501 ? 1_555 87.8  ? 
19 SG ? A CYS 401 ? A CYS 400 ? 1_555 FE B C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 84.8  ? 
20 NA ? C HEM .   ? A HEM 501 ? 1_555 FE B C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 173.6 ? 
21 NB ? C HEM .   ? A HEM 501 ? 1_555 FE B C HEM . ? A HEM 501 ? 1_555 NC ? C HEM . ? A HEM 501 ? 1_555 87.7  ? 
22 SG ? A CYS 401 ? A CYS 400 ? 1_555 FE B C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 95.2  ? 
23 NA ? C HEM .   ? A HEM 501 ? 1_555 FE B C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 92.2  ? 
24 NB ? C HEM .   ? A HEM 501 ? 1_555 FE B C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 175.5 ? 
25 NC ? C HEM .   ? A HEM 501 ? 1_555 FE B C HEM . ? A HEM 501 ? 1_555 ND ? C HEM . ? A HEM 501 ? 1_555 92.0  ? 
26 SG ? B CYS 401 ? B CYS 400 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 NA ? H HEM . ? B HEM 501 ? 1_555 97.4  ? 
27 SG ? B CYS 401 ? B CYS 400 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 NB ? H HEM . ? B HEM 501 ? 1_555 87.7  ? 
28 NA ? H HEM .   ? B HEM 501 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 NB ? H HEM . ? B HEM 501 ? 1_555 88.1  ? 
29 SG ? B CYS 401 ? B CYS 400 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 83.4  ? 
30 NA ? H HEM .   ? B HEM 501 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 176.7 ? 
31 NB ? H HEM .   ? B HEM 501 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 88.7  ? 
32 SG ? B CYS 401 ? B CYS 400 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 93.4  ? 
33 NA ? H HEM .   ? B HEM 501 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 91.6  ? 
34 NB ? H HEM .   ? B HEM 501 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 178.9 ? 
35 NC ? H HEM .   ? B HEM 501 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 91.5  ? 
36 SG ? B CYS 401 ? B CYS 400 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 O1 A J OXY . ? B OXY 503 ? 1_555 176.9 ? 
37 NA ? H HEM .   ? B HEM 501 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 O1 A J OXY . ? B OXY 503 ? 1_555 85.1  ? 
38 NB ? H HEM .   ? B HEM 501 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 O1 A J OXY . ? B OXY 503 ? 1_555 90.6  ? 
39 NC ? H HEM .   ? B HEM 501 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 O1 A J OXY . ? B OXY 503 ? 1_555 94.0  ? 
40 ND ? H HEM .   ? B HEM 501 ? 1_555 FE A H HEM . ? B HEM 501 ? 1_555 O1 A J OXY . ? B OXY 503 ? 1_555 88.3  ? 
41 SG ? B CYS 401 ? B CYS 400 ? 1_555 FE B H HEM . ? B HEM 501 ? 1_555 NA ? H HEM . ? B HEM 501 ? 1_555 99.4  ? 
42 SG ? B CYS 401 ? B CYS 400 ? 1_555 FE B H HEM . ? B HEM 501 ? 1_555 NB ? H HEM . ? B HEM 501 ? 1_555 88.8  ? 
43 NA ? H HEM .   ? B HEM 501 ? 1_555 FE B H HEM . ? B HEM 501 ? 1_555 NB ? H HEM . ? B HEM 501 ? 1_555 87.5  ? 
44 SG ? B CYS 401 ? B CYS 400 ? 1_555 FE B H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 84.8  ? 
45 NA ? H HEM .   ? B HEM 501 ? 1_555 FE B H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 173.7 ? 
46 NB ? H HEM .   ? B HEM 501 ? 1_555 FE B H HEM . ? B HEM 501 ? 1_555 NC ? H HEM . ? B HEM 501 ? 1_555 87.9  ? 
47 SG ? B CYS 401 ? B CYS 400 ? 1_555 FE B H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 95.7  ? 
48 NA ? H HEM .   ? B HEM 501 ? 1_555 FE B H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 92.3  ? 
49 NB ? H HEM .   ? B HEM 501 ? 1_555 FE B H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 175.4 ? 
50 NC ? H HEM .   ? B HEM 501 ? 1_555 FE B H HEM . ? B HEM 501 ? 1_555 ND ? H HEM . ? B HEM 501 ? 1_555 91.9  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 40  ? ALA A 45  ? ILE A 39  ALA A 44  
AA1 2 ARG A 48  ? LEU A 53  ? ARG A 47  LEU A 52  
AA1 3 GLU A 353 ? LEU A 357 ? GLU A 352 LEU A 356 
AA1 4 ALA A 331 ? ALA A 336 ? ALA A 330 ALA A 335 
AA1 5 PHE A 68  ? ASN A 71  ? PHE A 67  ASN A 70  
AA2 1 ILE A 140 ? GLU A 141 ? ILE A 139 GLU A 140 
AA2 2 VAL A 446 ? SER A 451 ? VAL A 445 SER A 450 
AA2 3 PHE A 422 ? GLU A 425 ? PHE A 421 GLU A 424 
AA3 1 THR A 340 ? LEU A 342 ? THR A 339 LEU A 341 
AA3 2 TYR A 346 ? LEU A 348 ? TYR A 345 LEU A 347 
AA4 1 ILE A 434 ? GLU A 436 ? ILE A 433 GLU A 435 
AA4 2 LEU A 440 ? PRO A 442 ? LEU A 439 PRO A 441 
AA5 1 ILE B 40  ? ALA B 45  ? ILE B 39  ALA B 44  
AA5 2 ARG B 48  ? LEU B 53  ? ARG B 47  LEU B 52  
AA5 3 GLU B 353 ? LEU B 357 ? GLU B 352 LEU B 356 
AA5 4 ALA B 331 ? ALA B 336 ? ALA B 330 ALA B 335 
AA5 5 PHE B 68  ? ASN B 71  ? PHE B 67  ASN B 70  
AA6 1 ILE B 140 ? GLU B 141 ? ILE B 139 GLU B 140 
AA6 2 VAL B 446 ? SER B 451 ? VAL B 445 SER B 450 
AA6 3 PHE B 422 ? GLU B 425 ? PHE B 421 GLU B 424 
AA7 1 THR B 340 ? LEU B 342 ? THR B 339 LEU B 341 
AA7 2 TYR B 346 ? LEU B 348 ? TYR B 345 LEU B 347 
AA8 1 ILE B 434 ? GLU B 436 ? ILE B 433 GLU B 435 
AA8 2 LEU B 440 ? PRO B 442 ? LEU B 439 PRO B 441 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 43  ? N PHE A 42  O THR A 50  ? O THR A 49  
AA1 2 3 N LEU A 53  ? N LEU A 52  O MET A 355 ? O MET A 354 
AA1 3 4 O VAL A 356 ? O VAL A 355 N PHE A 332 ? N PHE A 331 
AA1 4 5 O SER A 333 ? O SER A 332 N ASN A 71  ? N ASN A 70  
AA2 1 2 N ILE A 140 ? N ILE A 139 O VAL A 447 ? O VAL A 446 
AA2 2 3 O LYS A 450 ? O LYS A 449 N ASP A 423 ? N ASP A 422 
AA3 1 2 N THR A 340 ? N THR A 339 O LEU A 348 ? O LEU A 347 
AA4 1 2 N LYS A 435 ? N LYS A 434 O LYS A 441 ? O LYS A 440 
AA5 1 2 N PHE B 43  ? N PHE B 42  O THR B 50  ? O THR B 49  
AA5 2 3 N LEU B 53  ? N LEU B 52  O MET B 355 ? O MET B 354 
AA5 3 4 O VAL B 356 ? O VAL B 355 N PHE B 332 ? N PHE B 331 
AA5 4 5 O SER B 333 ? O SER B 332 N ASN B 71  ? N ASN B 70  
AA6 1 2 N ILE B 140 ? N ILE B 139 O VAL B 447 ? O VAL B 446 
AA6 2 3 O LYS B 450 ? O LYS B 449 N ASP B 423 ? N ASP B 422 
AA7 1 2 N THR B 340 ? N THR B 339 O LEU B 348 ? O LEU B 347 
AA8 1 2 N LYS B 435 ? N LYS B 434 O LYS B 441 ? O LYS B 440 
# 
_pdbx_entry_details.entry_id                   9KT5 
_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 
# 
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 LYS A 15  ? ? 57.72   -126.55 
2  1 ASP A 84  ? ? -98.32  36.59   
3  1 HIS A 266 ? ? -137.04 -31.73  
4  1 ASP A 370 ? ? -84.43  33.03   
5  1 LEU A 437 ? ? 68.97   -60.42  
6  1 LYS B 15  ? ? 57.56   -126.79 
7  1 ASP B 84  ? ? -98.83  38.64   
8  1 ASP B 232 ? ? -124.53 -166.76 
9  1 HIS B 266 ? ? -139.70 -32.42  
10 1 ASP B 370 ? ? -92.97  37.52   
11 1 LEU B 437 ? ? 72.04   -61.02  
# 
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 0 ? A MET 1 
2 1 Y 1 B MET 0 ? B MET 1 
# 
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  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
D0L C1   C  Y N 88  
D0L C2   C  Y N 89  
D0L C15  C  N N 90  
D0L C14  C  N N 91  
D0L C7   C  N N 92  
D0L C12  C  N N 93  
D0L C10  C  N N 94  
D0L C3   C  Y N 95  
D0L C13  C  N N 96  
D0L C11  C  N S 97  
D0L C6   C  Y N 98  
D0L C8   C  N S 99  
D0L C5   C  Y N 100 
D0L C9   C  N N 101 
D0L C4   C  Y N 102 
D0L O2   O  N N 103 
D0L O3   O  N N 104 
D0L O1   O  N N 105 
D0L N2   N  N N 106 
D0L C16  C  N N 107 
D0L C17  C  N N 108 
D0L C18  C  N N 109 
D0L C19  C  N N 110 
D0L C20  C  N N 111 
D0L C21  C  N N 112 
D0L N1   N  N N 113 
D0L H1   H  N N 114 
D0L H2   H  N N 115 
D0L H3   H  N N 116 
D0L H4   H  N N 117 
D0L H5   H  N N 118 
D0L H6   H  N N 119 
D0L H7   H  N N 120 
D0L H8   H  N N 121 
D0L H9   H  N N 122 
D0L H10  H  N N 123 
D0L H11  H  N N 124 
D0L H12  H  N N 125 
D0L H13  H  N N 126 
D0L H14  H  N N 127 
D0L H15  H  N N 128 
D0L H16  H  N N 129 
D0L H17  H  N N 130 
D0L H18  H  N N 131 
D0L H20  H  N N 132 
D0L H21  H  N N 133 
D0L H22  H  N N 134 
D0L H23  H  N N 135 
D0L H24  H  N N 136 
D0L H25  H  N N 137 
D0L H26  H  N N 138 
D0L H27  H  N N 139 
D0L H28  H  N N 140 
D0L H29  H  N N 141 
D0L H30  H  N N 142 
D0L H31  H  N N 143 
D0L H32  H  N N 144 
D0L H33  H  N N 145 
GLN N    N  N N 146 
GLN CA   C  N S 147 
GLN C    C  N N 148 
GLN O    O  N N 149 
GLN CB   C  N N 150 
GLN CG   C  N N 151 
GLN CD   C  N N 152 
GLN OE1  O  N N 153 
GLN NE2  N  N N 154 
GLN OXT  O  N N 155 
GLN H    H  N N 156 
GLN H2   H  N N 157 
GLN HA   H  N N 158 
GLN HB2  H  N N 159 
GLN HB3  H  N N 160 
GLN HG2  H  N N 161 
GLN HG3  H  N N 162 
GLN HE21 H  N N 163 
GLN HE22 H  N N 164 
GLN HXT  H  N N 165 
GLU N    N  N N 166 
GLU CA   C  N S 167 
GLU C    C  N N 168 
GLU O    O  N N 169 
GLU CB   C  N N 170 
GLU CG   C  N N 171 
GLU CD   C  N N 172 
GLU OE1  O  N N 173 
GLU OE2  O  N N 174 
GLU OXT  O  N N 175 
GLU H    H  N N 176 
GLU H2   H  N N 177 
GLU HA   H  N N 178 
GLU HB2  H  N N 179 
GLU HB3  H  N N 180 
GLU HG2  H  N N 181 
GLU HG3  H  N N 182 
GLU HE2  H  N N 183 
GLU HXT  H  N N 184 
GLY N    N  N N 185 
GLY CA   C  N N 186 
GLY C    C  N N 187 
GLY O    O  N N 188 
GLY OXT  O  N N 189 
GLY H    H  N N 190 
GLY H2   H  N N 191 
GLY HA2  H  N N 192 
GLY HA3  H  N N 193 
GLY HXT  H  N N 194 
GOL C1   C  N N 195 
GOL O1   O  N N 196 
GOL C2   C  N N 197 
GOL O2   O  N N 198 
GOL C3   C  N N 199 
GOL O3   O  N N 200 
GOL H11  H  N N 201 
GOL H12  H  N N 202 
GOL HO1  H  N N 203 
GOL H2   H  N N 204 
GOL HO2  H  N N 205 
GOL H31  H  N N 206 
GOL H32  H  N N 207 
GOL HO3  H  N N 208 
HEM CHA  C  N N 209 
HEM CHB  C  N N 210 
HEM CHC  C  N N 211 
HEM CHD  C  N N 212 
HEM C1A  C  Y N 213 
HEM C2A  C  Y N 214 
HEM C3A  C  Y N 215 
HEM C4A  C  Y N 216 
HEM CMA  C  N N 217 
HEM CAA  C  N N 218 
HEM CBA  C  N N 219 
HEM CGA  C  N N 220 
HEM O1A  O  N N 221 
HEM O2A  O  N N 222 
HEM C1B  C  N N 223 
HEM C2B  C  N N 224 
HEM C3B  C  N N 225 
HEM C4B  C  N N 226 
HEM CMB  C  N N 227 
HEM CAB  C  N N 228 
HEM CBB  C  N N 229 
HEM C1C  C  Y N 230 
HEM C2C  C  Y N 231 
HEM C3C  C  Y N 232 
HEM C4C  C  Y N 233 
HEM CMC  C  N N 234 
HEM CAC  C  N N 235 
HEM CBC  C  N N 236 
HEM C1D  C  N N 237 
HEM C2D  C  N N 238 
HEM C3D  C  N N 239 
HEM C4D  C  N N 240 
HEM CMD  C  N N 241 
HEM CAD  C  N N 242 
HEM CBD  C  N N 243 
HEM CGD  C  N N 244 
HEM O1D  O  N N 245 
HEM O2D  O  N N 246 
HEM NA   N  Y N 247 
HEM NB   N  N N 248 
HEM NC   N  Y N 249 
HEM ND   N  N N 250 
HEM FE   FE N N 251 
HEM HHB  H  N N 252 
HEM HHC  H  N N 253 
HEM HHD  H  N N 254 
HEM HMA  H  N N 255 
HEM HMAA H  N N 256 
HEM HMAB H  N N 257 
HEM HAA  H  N N 258 
HEM HAAA H  N N 259 
HEM HBA  H  N N 260 
HEM HBAA H  N N 261 
HEM HMB  H  N N 262 
HEM HMBA H  N N 263 
HEM HMBB H  N N 264 
HEM HAB  H  N N 265 
HEM HBB  H  N N 266 
HEM HBBA H  N N 267 
HEM HMC  H  N N 268 
HEM HMCA H  N N 269 
HEM HMCB H  N N 270 
HEM HAC  H  N N 271 
HEM HBC  H  N N 272 
HEM HBCA H  N N 273 
HEM HMD  H  N N 274 
HEM HMDA H  N N 275 
HEM HMDB H  N N 276 
HEM HAD  H  N N 277 
HEM HADA H  N N 278 
HEM HBD  H  N N 279 
HEM HBDA H  N N 280 
HEM H2A  H  N N 281 
HEM H2D  H  N N 282 
HEM HHA  H  N N 283 
HIS N    N  N N 284 
HIS CA   C  N S 285 
HIS C    C  N N 286 
HIS O    O  N N 287 
HIS CB   C  N N 288 
HIS CG   C  Y N 289 
HIS ND1  N  Y N 290 
HIS CD2  C  Y N 291 
HIS CE1  C  Y N 292 
HIS NE2  N  Y N 293 
HIS OXT  O  N N 294 
HIS H    H  N N 295 
HIS H2   H  N N 296 
HIS HA   H  N N 297 
HIS HB2  H  N N 298 
HIS HB3  H  N N 299 
HIS HD1  H  N N 300 
HIS HD2  H  N N 301 
HIS HE1  H  N N 302 
HIS HE2  H  N N 303 
HIS HXT  H  N N 304 
HOH O    O  N N 305 
HOH H1   H  N N 306 
HOH H2   H  N N 307 
ILE N    N  N N 308 
ILE CA   C  N S 309 
ILE C    C  N N 310 
ILE O    O  N N 311 
ILE CB   C  N S 312 
ILE CG1  C  N N 313 
ILE CG2  C  N N 314 
ILE CD1  C  N N 315 
ILE OXT  O  N N 316 
ILE H    H  N N 317 
ILE H2   H  N N 318 
ILE HA   H  N N 319 
ILE HB   H  N N 320 
ILE HG12 H  N N 321 
ILE HG13 H  N N 322 
ILE HG21 H  N N 323 
ILE HG22 H  N N 324 
ILE HG23 H  N N 325 
ILE HD11 H  N N 326 
ILE HD12 H  N N 327 
ILE HD13 H  N N 328 
ILE HXT  H  N N 329 
LEU N    N  N N 330 
LEU CA   C  N S 331 
LEU C    C  N N 332 
LEU O    O  N N 333 
LEU CB   C  N N 334 
LEU CG   C  N N 335 
LEU CD1  C  N N 336 
LEU CD2  C  N N 337 
LEU OXT  O  N N 338 
LEU H    H  N N 339 
LEU H2   H  N N 340 
LEU HA   H  N N 341 
LEU HB2  H  N N 342 
LEU HB3  H  N N 343 
LEU HG   H  N N 344 
LEU HD11 H  N N 345 
LEU HD12 H  N N 346 
LEU HD13 H  N N 347 
LEU HD21 H  N N 348 
LEU HD22 H  N N 349 
LEU HD23 H  N N 350 
LEU HXT  H  N N 351 
LYS N    N  N N 352 
LYS CA   C  N S 353 
LYS C    C  N N 354 
LYS O    O  N N 355 
LYS CB   C  N N 356 
LYS CG   C  N N 357 
LYS CD   C  N N 358 
LYS CE   C  N N 359 
LYS NZ   N  N N 360 
LYS OXT  O  N N 361 
LYS H    H  N N 362 
LYS H2   H  N N 363 
LYS HA   H  N N 364 
LYS HB2  H  N N 365 
LYS HB3  H  N N 366 
LYS HG2  H  N N 367 
LYS HG3  H  N N 368 
LYS HD2  H  N N 369 
LYS HD3  H  N N 370 
LYS HE2  H  N N 371 
LYS HE3  H  N N 372 
LYS HZ1  H  N N 373 
LYS HZ2  H  N N 374 
LYS HZ3  H  N N 375 
LYS HXT  H  N N 376 
MET N    N  N N 377 
MET CA   C  N S 378 
MET C    C  N N 379 
MET O    O  N N 380 
MET CB   C  N N 381 
MET CG   C  N N 382 
MET SD   S  N N 383 
MET CE   C  N N 384 
MET OXT  O  N N 385 
MET H    H  N N 386 
MET H2   H  N N 387 
MET HA   H  N N 388 
MET HB2  H  N N 389 
MET HB3  H  N N 390 
MET HG2  H  N N 391 
MET HG3  H  N N 392 
MET HE1  H  N N 393 
MET HE2  H  N N 394 
MET HE3  H  N N 395 
MET HXT  H  N N 396 
OXY O1   O  N N 397 
OXY O2   O  N N 398 
PHE N    N  N N 399 
PHE CA   C  N S 400 
PHE C    C  N N 401 
PHE O    O  N N 402 
PHE CB   C  N N 403 
PHE CG   C  Y N 404 
PHE CD1  C  Y N 405 
PHE CD2  C  Y N 406 
PHE CE1  C  Y N 407 
PHE CE2  C  Y N 408 
PHE CZ   C  Y N 409 
PHE OXT  O  N N 410 
PHE H    H  N N 411 
PHE H2   H  N N 412 
PHE HA   H  N N 413 
PHE HB2  H  N N 414 
PHE HB3  H  N N 415 
PHE HD1  H  N N 416 
PHE HD2  H  N N 417 
PHE HE1  H  N N 418 
PHE HE2  H  N N 419 
PHE HZ   H  N N 420 
PHE HXT  H  N N 421 
PRO N    N  N N 422 
PRO CA   C  N S 423 
PRO C    C  N N 424 
PRO O    O  N N 425 
PRO CB   C  N N 426 
PRO CG   C  N N 427 
PRO CD   C  N N 428 
PRO OXT  O  N N 429 
PRO H    H  N N 430 
PRO HA   H  N N 431 
PRO HB2  H  N N 432 
PRO HB3  H  N N 433 
PRO HG2  H  N N 434 
PRO HG3  H  N N 435 
PRO HD2  H  N N 436 
PRO HD3  H  N N 437 
PRO HXT  H  N N 438 
SER N    N  N N 439 
SER CA   C  N S 440 
SER C    C  N N 441 
SER O    O  N N 442 
SER CB   C  N N 443 
SER OG   O  N N 444 
SER OXT  O  N N 445 
SER H    H  N N 446 
SER H2   H  N N 447 
SER HA   H  N N 448 
SER HB2  H  N N 449 
SER HB3  H  N N 450 
SER HG   H  N N 451 
SER HXT  H  N N 452 
SYN CAF  C  Y N 453 
SYN CAD  C  Y N 454 
SYN CAC  C  Y N 455 
SYN CAE  C  Y N 456 
SYN CAG  C  Y N 457 
SYN CAH  C  Y N 458 
SYN CAB  C  N N 459 
SYN CAA  C  N N 460 
SYN H1   H  N N 461 
SYN H2   H  N N 462 
SYN H3   H  N N 463 
SYN H4   H  N N 464 
SYN H5   H  N N 465 
SYN H6   H  N N 466 
SYN H8   H  N N 467 
SYN H9   H  N N 468 
THR N    N  N N 469 
THR CA   C  N S 470 
THR C    C  N N 471 
THR O    O  N N 472 
THR CB   C  N R 473 
THR OG1  O  N N 474 
THR CG2  C  N N 475 
THR OXT  O  N N 476 
THR H    H  N N 477 
THR H2   H  N N 478 
THR HA   H  N N 479 
THR HB   H  N N 480 
THR HG1  H  N N 481 
THR HG21 H  N N 482 
THR HG22 H  N N 483 
THR HG23 H  N N 484 
THR HXT  H  N N 485 
TRP N    N  N N 486 
TRP CA   C  N S 487 
TRP C    C  N N 488 
TRP O    O  N N 489 
TRP CB   C  N N 490 
TRP CG   C  Y N 491 
TRP CD1  C  Y N 492 
TRP CD2  C  Y N 493 
TRP NE1  N  Y N 494 
TRP CE2  C  Y N 495 
TRP CE3  C  Y N 496 
TRP CZ2  C  Y N 497 
TRP CZ3  C  Y N 498 
TRP CH2  C  Y N 499 
TRP OXT  O  N N 500 
TRP H    H  N N 501 
TRP H2   H  N N 502 
TRP HA   H  N N 503 
TRP HB2  H  N N 504 
TRP HB3  H  N N 505 
TRP HD1  H  N N 506 
TRP HE1  H  N N 507 
TRP HE3  H  N N 508 
TRP HZ2  H  N N 509 
TRP HZ3  H  N N 510 
TRP HH2  H  N N 511 
TRP HXT  H  N N 512 
TYR N    N  N N 513 
TYR CA   C  N S 514 
TYR C    C  N N 515 
TYR O    O  N N 516 
TYR CB   C  N N 517 
TYR CG   C  Y N 518 
TYR CD1  C  Y N 519 
TYR CD2  C  Y N 520 
TYR CE1  C  Y N 521 
TYR CE2  C  Y N 522 
TYR CZ   C  Y N 523 
TYR OH   O  N N 524 
TYR OXT  O  N N 525 
TYR H    H  N N 526 
TYR H2   H  N N 527 
TYR HA   H  N N 528 
TYR HB2  H  N N 529 
TYR HB3  H  N N 530 
TYR HD1  H  N N 531 
TYR HD2  H  N N 532 
TYR HE1  H  N N 533 
TYR HE2  H  N N 534 
TYR HH   H  N N 535 
TYR HXT  H  N N 536 
VAL N    N  N N 537 
VAL CA   C  N S 538 
VAL C    C  N N 539 
VAL O    O  N N 540 
VAL CB   C  N N 541 
VAL CG1  C  N N 542 
VAL CG2  C  N N 543 
VAL OXT  O  N N 544 
VAL H    H  N N 545 
VAL H2   H  N N 546 
VAL HA   H  N N 547 
VAL HB   H  N N 548 
VAL HG11 H  N N 549 
VAL HG12 H  N N 550 
VAL HG13 H  N N 551 
VAL HG21 H  N N 552 
VAL HG22 H  N N 553 
VAL HG23 H  N N 554 
VAL HXT  H  N N 555 
# 
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  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
D0L C21 C20  sing N N 83  
D0L C20 C19  sing N N 84  
D0L C19 C18  sing N N 85  
D0L C18 C17  sing N N 86  
D0L C14 N2   sing N N 87  
D0L C14 C13  sing N N 88  
D0L C17 C16  sing N N 89  
D0L C15 N2   sing N N 90  
D0L C15 C16  sing N N 91  
D0L N2  C11  sing N N 92  
D0L C13 C12  sing N N 93  
D0L O2  C9   doub N N 94  
D0L C11 C12  sing N N 95  
D0L C11 C10  sing N N 96  
D0L C5  C4   doub Y N 97  
D0L C5  C6   sing Y N 98  
D0L C4  C3   sing Y N 99  
D0L C6  C1   doub Y N 100 
D0L N1  C10  sing N N 101 
D0L N1  C8   sing N N 102 
D0L C9  O1   sing N N 103 
D0L C9  C8   sing N N 104 
D0L C10 O3   doub N N 105 
D0L C3  C2   doub Y N 106 
D0L C1  C2   sing Y N 107 
D0L C8  C7   sing N N 108 
D0L C2  C7   sing N N 109 
D0L C1  H1   sing N N 110 
D0L C15 H2   sing N N 111 
D0L C15 H3   sing N N 112 
D0L C14 H4   sing N N 113 
D0L C14 H5   sing N N 114 
D0L C7  H6   sing N N 115 
D0L C7  H7   sing N N 116 
D0L C12 H8   sing N N 117 
D0L C12 H9   sing N N 118 
D0L C3  H10  sing N N 119 
D0L C13 H11  sing N N 120 
D0L C13 H12  sing N N 121 
D0L C11 H13  sing N N 122 
D0L C6  H14  sing N N 123 
D0L C8  H15  sing N N 124 
D0L C5  H16  sing N N 125 
D0L C4  H17  sing N N 126 
D0L O1  H18  sing N N 127 
D0L C16 H20  sing N N 128 
D0L C16 H21  sing N N 129 
D0L C17 H22  sing N N 130 
D0L C17 H23  sing N N 131 
D0L C18 H24  sing N N 132 
D0L C18 H25  sing N N 133 
D0L C19 H26  sing N N 134 
D0L C19 H27  sing N N 135 
D0L C20 H28  sing N N 136 
D0L C20 H29  sing N N 137 
D0L C21 H30  sing N N 138 
D0L C21 H31  sing N N 139 
D0L C21 H32  sing N N 140 
D0L N1  H33  sing N N 141 
GLN N   CA   sing N N 142 
GLN N   H    sing N N 143 
GLN N   H2   sing N N 144 
GLN CA  C    sing N N 145 
GLN CA  CB   sing N N 146 
GLN CA  HA   sing N N 147 
GLN C   O    doub N N 148 
GLN C   OXT  sing N N 149 
GLN CB  CG   sing N N 150 
GLN CB  HB2  sing N N 151 
GLN CB  HB3  sing N N 152 
GLN CG  CD   sing N N 153 
GLN CG  HG2  sing N N 154 
GLN CG  HG3  sing N N 155 
GLN CD  OE1  doub N N 156 
GLN CD  NE2  sing N N 157 
GLN NE2 HE21 sing N N 158 
GLN NE2 HE22 sing N N 159 
GLN OXT HXT  sing N N 160 
GLU N   CA   sing N N 161 
GLU N   H    sing N N 162 
GLU N   H2   sing N N 163 
GLU CA  C    sing N N 164 
GLU CA  CB   sing N N 165 
GLU CA  HA   sing N N 166 
GLU C   O    doub N N 167 
GLU C   OXT  sing N N 168 
GLU CB  CG   sing N N 169 
GLU CB  HB2  sing N N 170 
GLU CB  HB3  sing N N 171 
GLU CG  CD   sing N N 172 
GLU CG  HG2  sing N N 173 
GLU CG  HG3  sing N N 174 
GLU CD  OE1  doub N N 175 
GLU CD  OE2  sing N N 176 
GLU OE2 HE2  sing N N 177 
GLU OXT HXT  sing N N 178 
GLY N   CA   sing N N 179 
GLY N   H    sing N N 180 
GLY N   H2   sing N N 181 
GLY CA  C    sing N N 182 
GLY CA  HA2  sing N N 183 
GLY CA  HA3  sing N N 184 
GLY C   O    doub N N 185 
GLY C   OXT  sing N N 186 
GLY OXT HXT  sing N N 187 
GOL C1  O1   sing N N 188 
GOL C1  C2   sing N N 189 
GOL C1  H11  sing N N 190 
GOL C1  H12  sing N N 191 
GOL O1  HO1  sing N N 192 
GOL C2  O2   sing N N 193 
GOL C2  C3   sing N N 194 
GOL C2  H2   sing N N 195 
GOL O2  HO2  sing N N 196 
GOL C3  O3   sing N N 197 
GOL C3  H31  sing N N 198 
GOL C3  H32  sing N N 199 
GOL O3  HO3  sing N N 200 
HEM CHA C1A  sing N N 201 
HEM CHA C4D  doub N N 202 
HEM CHA HHA  sing N N 203 
HEM CHB C4A  sing N N 204 
HEM CHB C1B  doub N N 205 
HEM CHB HHB  sing N N 206 
HEM CHC C4B  sing N N 207 
HEM CHC C1C  doub N N 208 
HEM CHC HHC  sing N N 209 
HEM CHD C4C  doub N N 210 
HEM CHD C1D  sing N N 211 
HEM CHD HHD  sing N N 212 
HEM C1A C2A  doub Y N 213 
HEM C1A NA   sing Y N 214 
HEM C2A C3A  sing Y N 215 
HEM C2A CAA  sing N N 216 
HEM C3A C4A  doub Y N 217 
HEM C3A CMA  sing N N 218 
HEM C4A NA   sing Y N 219 
HEM CMA HMA  sing N N 220 
HEM CMA HMAA sing N N 221 
HEM CMA HMAB sing N N 222 
HEM CAA CBA  sing N N 223 
HEM CAA HAA  sing N N 224 
HEM CAA HAAA sing N N 225 
HEM CBA CGA  sing N N 226 
HEM CBA HBA  sing N N 227 
HEM CBA HBAA sing N N 228 
HEM CGA O1A  doub N N 229 
HEM CGA O2A  sing N N 230 
HEM C1B C2B  sing N N 231 
HEM C1B NB   sing N N 232 
HEM C2B C3B  doub N N 233 
HEM C2B CMB  sing N N 234 
HEM C3B C4B  sing N N 235 
HEM C3B CAB  sing N N 236 
HEM C4B NB   doub N N 237 
HEM CMB HMB  sing N N 238 
HEM CMB HMBA sing N N 239 
HEM CMB HMBB sing N N 240 
HEM CAB CBB  doub N N 241 
HEM CAB HAB  sing N N 242 
HEM CBB HBB  sing N N 243 
HEM CBB HBBA sing N N 244 
HEM C1C C2C  sing Y N 245 
HEM C1C NC   sing Y N 246 
HEM C2C C3C  doub Y N 247 
HEM C2C CMC  sing N N 248 
HEM C3C C4C  sing Y N 249 
HEM C3C CAC  sing N N 250 
HEM C4C NC   sing Y N 251 
HEM CMC HMC  sing N N 252 
HEM CMC HMCA sing N N 253 
HEM CMC HMCB sing N N 254 
HEM CAC CBC  doub N N 255 
HEM CAC HAC  sing N N 256 
HEM CBC HBC  sing N N 257 
HEM CBC HBCA sing N N 258 
HEM C1D C2D  sing N N 259 
HEM C1D ND   doub N N 260 
HEM C2D C3D  doub N N 261 
HEM C2D CMD  sing N N 262 
HEM C3D C4D  sing N N 263 
HEM C3D CAD  sing N N 264 
HEM C4D ND   sing N N 265 
HEM CMD HMD  sing N N 266 
HEM CMD HMDA sing N N 267 
HEM CMD HMDB sing N N 268 
HEM CAD CBD  sing N N 269 
HEM CAD HAD  sing N N 270 
HEM CAD HADA sing N N 271 
HEM CBD CGD  sing N N 272 
HEM CBD HBD  sing N N 273 
HEM CBD HBDA sing N N 274 
HEM CGD O1D  doub N N 275 
HEM CGD O2D  sing N N 276 
HEM O2A H2A  sing N N 277 
HEM O2D H2D  sing N N 278 
HEM FE  NA   sing N N 279 
HEM FE  NB   sing N N 280 
HEM FE  NC   sing N N 281 
HEM FE  ND   sing N N 282 
HIS N   CA   sing N N 283 
HIS N   H    sing N N 284 
HIS N   H2   sing N N 285 
HIS CA  C    sing N N 286 
HIS CA  CB   sing N N 287 
HIS CA  HA   sing N N 288 
HIS C   O    doub N N 289 
HIS C   OXT  sing N N 290 
HIS CB  CG   sing N N 291 
HIS CB  HB2  sing N N 292 
HIS CB  HB3  sing N N 293 
HIS CG  ND1  sing Y N 294 
HIS CG  CD2  doub Y N 295 
HIS ND1 CE1  doub Y N 296 
HIS ND1 HD1  sing N N 297 
HIS CD2 NE2  sing Y N 298 
HIS CD2 HD2  sing N N 299 
HIS CE1 NE2  sing Y N 300 
HIS CE1 HE1  sing N N 301 
HIS NE2 HE2  sing N N 302 
HIS OXT HXT  sing N N 303 
HOH O   H1   sing N N 304 
HOH O   H2   sing N N 305 
ILE N   CA   sing N N 306 
ILE N   H    sing N N 307 
ILE N   H2   sing N N 308 
ILE CA  C    sing N N 309 
ILE CA  CB   sing N N 310 
ILE CA  HA   sing N N 311 
ILE C   O    doub N N 312 
ILE C   OXT  sing N N 313 
ILE CB  CG1  sing N N 314 
ILE CB  CG2  sing N N 315 
ILE CB  HB   sing N N 316 
ILE CG1 CD1  sing N N 317 
ILE CG1 HG12 sing N N 318 
ILE CG1 HG13 sing N N 319 
ILE CG2 HG21 sing N N 320 
ILE CG2 HG22 sing N N 321 
ILE CG2 HG23 sing N N 322 
ILE CD1 HD11 sing N N 323 
ILE CD1 HD12 sing N N 324 
ILE CD1 HD13 sing N N 325 
ILE OXT HXT  sing N N 326 
LEU N   CA   sing N N 327 
LEU N   H    sing N N 328 
LEU N   H2   sing N N 329 
LEU CA  C    sing N N 330 
LEU CA  CB   sing N N 331 
LEU CA  HA   sing N N 332 
LEU C   O    doub N N 333 
LEU C   OXT  sing N N 334 
LEU CB  CG   sing N N 335 
LEU CB  HB2  sing N N 336 
LEU CB  HB3  sing N N 337 
LEU CG  CD1  sing N N 338 
LEU CG  CD2  sing N N 339 
LEU CG  HG   sing N N 340 
LEU CD1 HD11 sing N N 341 
LEU CD1 HD12 sing N N 342 
LEU CD1 HD13 sing N N 343 
LEU CD2 HD21 sing N N 344 
LEU CD2 HD22 sing N N 345 
LEU CD2 HD23 sing N N 346 
LEU OXT HXT  sing N N 347 
LYS N   CA   sing N N 348 
LYS N   H    sing N N 349 
LYS N   H2   sing N N 350 
LYS CA  C    sing N N 351 
LYS CA  CB   sing N N 352 
LYS CA  HA   sing N N 353 
LYS C   O    doub N N 354 
LYS C   OXT  sing N N 355 
LYS CB  CG   sing N N 356 
LYS CB  HB2  sing N N 357 
LYS CB  HB3  sing N N 358 
LYS CG  CD   sing N N 359 
LYS CG  HG2  sing N N 360 
LYS CG  HG3  sing N N 361 
LYS CD  CE   sing N N 362 
LYS CD  HD2  sing N N 363 
LYS CD  HD3  sing N N 364 
LYS CE  NZ   sing N N 365 
LYS CE  HE2  sing N N 366 
LYS CE  HE3  sing N N 367 
LYS NZ  HZ1  sing N N 368 
LYS NZ  HZ2  sing N N 369 
LYS NZ  HZ3  sing N N 370 
LYS OXT HXT  sing N N 371 
MET N   CA   sing N N 372 
MET N   H    sing N N 373 
MET N   H2   sing N N 374 
MET CA  C    sing N N 375 
MET CA  CB   sing N N 376 
MET CA  HA   sing N N 377 
MET C   O    doub N N 378 
MET C   OXT  sing N N 379 
MET CB  CG   sing N N 380 
MET CB  HB2  sing N N 381 
MET CB  HB3  sing N N 382 
MET CG  SD   sing N N 383 
MET CG  HG2  sing N N 384 
MET CG  HG3  sing N N 385 
MET SD  CE   sing N N 386 
MET CE  HE1  sing N N 387 
MET CE  HE2  sing N N 388 
MET CE  HE3  sing N N 389 
MET OXT HXT  sing N N 390 
OXY O1  O2   doub N N 391 
PHE N   CA   sing N N 392 
PHE N   H    sing N N 393 
PHE N   H2   sing N N 394 
PHE CA  C    sing N N 395 
PHE CA  CB   sing N N 396 
PHE CA  HA   sing N N 397 
PHE C   O    doub N N 398 
PHE C   OXT  sing N N 399 
PHE CB  CG   sing N N 400 
PHE CB  HB2  sing N N 401 
PHE CB  HB3  sing N N 402 
PHE CG  CD1  doub Y N 403 
PHE CG  CD2  sing Y N 404 
PHE CD1 CE1  sing Y N 405 
PHE CD1 HD1  sing N N 406 
PHE CD2 CE2  doub Y N 407 
PHE CD2 HD2  sing N N 408 
PHE CE1 CZ   doub Y N 409 
PHE CE1 HE1  sing N N 410 
PHE CE2 CZ   sing Y N 411 
PHE CE2 HE2  sing N N 412 
PHE CZ  HZ   sing N N 413 
PHE OXT HXT  sing N N 414 
PRO N   CA   sing N N 415 
PRO N   CD   sing N N 416 
PRO N   H    sing N N 417 
PRO CA  C    sing N N 418 
PRO CA  CB   sing N N 419 
PRO CA  HA   sing N N 420 
PRO C   O    doub N N 421 
PRO C   OXT  sing N N 422 
PRO CB  CG   sing N N 423 
PRO CB  HB2  sing N N 424 
PRO CB  HB3  sing N N 425 
PRO CG  CD   sing N N 426 
PRO CG  HG2  sing N N 427 
PRO CG  HG3  sing N N 428 
PRO CD  HD2  sing N N 429 
PRO CD  HD3  sing N N 430 
PRO OXT HXT  sing N N 431 
SER N   CA   sing N N 432 
SER N   H    sing N N 433 
SER N   H2   sing N N 434 
SER CA  C    sing N N 435 
SER CA  CB   sing N N 436 
SER CA  HA   sing N N 437 
SER C   O    doub N N 438 
SER C   OXT  sing N N 439 
SER CB  OG   sing N N 440 
SER CB  HB2  sing N N 441 
SER CB  HB3  sing N N 442 
SER OG  HG   sing N N 443 
SER OXT HXT  sing N N 444 
SYN CAC CAE  doub Y N 445 
SYN CAC CAD  sing Y N 446 
SYN CAE CAG  sing Y N 447 
SYN CAD CAF  doub Y N 448 
SYN CAG CAH  doub Y N 449 
SYN CAF CAH  sing Y N 450 
SYN CAH CAB  sing N N 451 
SYN CAB CAA  doub N N 452 
SYN CAF H1   sing N N 453 
SYN CAD H2   sing N N 454 
SYN CAC H3   sing N N 455 
SYN CAE H4   sing N N 456 
SYN CAG H5   sing N N 457 
SYN CAB H6   sing N N 458 
SYN CAA H8   sing N N 459 
SYN CAA H9   sing N N 460 
THR N   CA   sing N N 461 
THR N   H    sing N N 462 
THR N   H2   sing N N 463 
THR CA  C    sing N N 464 
THR CA  CB   sing N N 465 
THR CA  HA   sing N N 466 
THR C   O    doub N N 467 
THR C   OXT  sing N N 468 
THR CB  OG1  sing N N 469 
THR CB  CG2  sing N N 470 
THR CB  HB   sing N N 471 
THR OG1 HG1  sing N N 472 
THR CG2 HG21 sing N N 473 
THR CG2 HG22 sing N N 474 
THR CG2 HG23 sing N N 475 
THR OXT HXT  sing N N 476 
TRP N   CA   sing N N 477 
TRP N   H    sing N N 478 
TRP N   H2   sing N N 479 
TRP CA  C    sing N N 480 
TRP CA  CB   sing N N 481 
TRP CA  HA   sing N N 482 
TRP C   O    doub N N 483 
TRP C   OXT  sing N N 484 
TRP CB  CG   sing N N 485 
TRP CB  HB2  sing N N 486 
TRP CB  HB3  sing N N 487 
TRP CG  CD1  doub Y N 488 
TRP CG  CD2  sing Y N 489 
TRP CD1 NE1  sing Y N 490 
TRP CD1 HD1  sing N N 491 
TRP CD2 CE2  doub Y N 492 
TRP CD2 CE3  sing Y N 493 
TRP NE1 CE2  sing Y N 494 
TRP NE1 HE1  sing N N 495 
TRP CE2 CZ2  sing Y N 496 
TRP CE3 CZ3  doub Y N 497 
TRP CE3 HE3  sing N N 498 
TRP CZ2 CH2  doub Y N 499 
TRP CZ2 HZ2  sing N N 500 
TRP CZ3 CH2  sing Y N 501 
TRP CZ3 HZ3  sing N N 502 
TRP CH2 HH2  sing N N 503 
TRP OXT HXT  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 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Japan Science and Technology'                      Japan JPMJCR15P3 1 
'Japan Society for the Promotion of Science (JSPS)' Japan JP19H05784 2 
'Japan Society for the Promotion of Science (JSPS)' Japan JP18KK0397 3 
'Japan Society for the Promotion of Science (JSPS)' Japan JP19K22403 4 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8YB3 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9KT5 
_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]   0.016912 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007732 
_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]   0.006660 
_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 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . THR A 1 2   ? -11.461 -23.591 -24.743 1.00 61.99 ? 1    THR A N   1 
ATOM   2    C  CA  . THR A 1 2   ? -10.196 -23.685 -24.022 1.00 62.58 ? 1    THR A CA  1 
ATOM   3    C  C   . THR A 1 2   ? -10.384 -24.386 -22.678 1.00 58.67 ? 1    THR A C   1 
ATOM   4    O  O   . THR A 1 2   ? -9.821  -23.970 -21.665 1.00 57.95 ? 1    THR A O   1 
ATOM   5    C  CB  . THR A 1 2   ? -9.574  -22.294 -23.788 1.00 66.04 ? 1    THR A CB  1 
ATOM   6    O  OG1 . THR A 1 2   ? -10.507 -21.457 -23.094 1.00 68.01 ? 1    THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 2   ? -9.208  -21.641 -25.113 1.00 67.56 ? 1    THR A CG2 1 
ATOM   8    N  N   . ILE A 1 3   ? -11.178 -25.456 -22.680 1.00 56.12 ? 2    ILE A N   1 
ATOM   9    C  CA  . ILE A 1 3   ? -11.451 -26.207 -21.458 1.00 52.87 ? 2    ILE A CA  1 
ATOM   10   C  C   . ILE A 1 3   ? -10.177 -26.917 -21.013 1.00 50.64 ? 2    ILE A C   1 
ATOM   11   O  O   . ILE A 1 3   ? -9.576  -27.684 -21.775 1.00 50.20 ? 2    ILE A O   1 
ATOM   12   C  CB  . ILE A 1 3   ? -12.598 -27.205 -21.673 1.00 50.84 ? 2    ILE A CB  1 
ATOM   13   C  CG1 . ILE A 1 3   ? -13.877 -26.470 -22.080 1.00 51.21 ? 2    ILE A CG1 1 
ATOM   14   C  CG2 . ILE A 1 3   ? -12.833 -28.037 -20.420 1.00 49.89 ? 2    ILE A CG2 1 
ATOM   15   C  CD1 . ILE A 1 3   ? -15.055 -27.390 -22.331 1.00 51.94 ? 2    ILE A CD1 1 
ATOM   16   N  N   . LYS A 1 4   ? -9.760  -26.662 -19.775 1.00 46.56 ? 3    LYS A N   1 
ATOM   17   C  CA  . LYS A 1 4   ? -8.628  -27.340 -19.164 1.00 44.42 ? 3    LYS A CA  1 
ATOM   18   C  C   . LYS A 1 4   ? -9.111  -28.433 -18.216 1.00 44.38 ? 3    LYS A C   1 
ATOM   19   O  O   . LYS A 1 4   ? -10.255 -28.432 -17.753 1.00 43.58 ? 3    LYS A O   1 
ATOM   20   C  CB  . LYS A 1 4   ? -7.741  -26.356 -18.391 1.00 41.67 ? 3    LYS A CB  1 
ATOM   21   C  CG  . LYS A 1 4   ? -6.750  -25.563 -19.220 1.00 42.76 ? 3    LYS A CG  1 
ATOM   22   C  CD  . LYS A 1 4   ? -5.671  -24.978 -18.312 1.00 44.74 ? 3    LYS A CD  1 
ATOM   23   C  CE  . LYS A 1 4   ? -4.522  -24.366 -19.102 1.00 48.00 ? 3    LYS A CE  1 
ATOM   24   N  NZ  . LYS A 1 4   ? -4.897  -23.080 -19.752 1.00 50.02 ? 3    LYS A NZ  1 
ATOM   25   N  N   . GLU A 1 5   ? -8.210  -29.370 -17.931 1.00 43.49 ? 4    GLU A N   1 
ATOM   26   C  CA  . GLU A 1 5   ? -8.412  -30.391 -16.911 1.00 41.49 ? 4    GLU A CA  1 
ATOM   27   C  C   . GLU A 1 5   ? -7.654  -29.965 -15.660 1.00 35.80 ? 4    GLU A C   1 
ATOM   28   O  O   . GLU A 1 5   ? -6.445  -29.723 -15.721 1.00 36.98 ? 4    GLU A O   1 
ATOM   29   C  CB  . GLU A 1 5   ? -7.915  -31.750 -17.401 1.00 46.49 ? 4    GLU A CB  1 
ATOM   30   C  CG  . GLU A 1 5   ? -8.434  -32.933 -16.607 1.00 51.50 ? 4    GLU A CG  1 
ATOM   31   C  CD  . GLU A 1 5   ? -9.883  -33.244 -16.928 1.00 57.50 ? 4    GLU A CD  1 
ATOM   32   O  OE1 . GLU A 1 5   ? -10.468 -32.533 -17.779 1.00 59.24 ? 4    GLU A OE1 1 
ATOM   33   O  OE2 . GLU A 1 5   ? -10.433 -34.197 -16.334 1.00 58.49 ? 4    GLU A OE2 1 
ATOM   34   N  N   . MET A 1 6   ? -8.368  -29.867 -14.518 1.00 30.41 ? 5    MET A N   1 
ATOM   35   C  CA  . MET A 1 6   ? -7.537  -29.400 -13.415 1.00 26.83 ? 5    MET A CA  1 
ATOM   36   C  C   . MET A 1 6   ? -6.816  -30.569 -12.746 1.00 22.66 ? 5    MET A C   1 
ATOM   37   O  O   . MET A 1 6   ? -7.296  -31.707 -12.773 1.00 23.00 ? 5    MET A O   1 
ATOM   38   C  CB  . MET A 1 6   ? -8.385  -28.658 -12.379 1.00 25.72 ? 5    MET A CB  1 
ATOM   39   C  CG  . MET A 1 6   ? -9.342  -29.542 -11.614 1.00 23.95 ? 5    MET A CG  1 
ATOM   40   S  SD  . MET A 1 6   ? -10.510 -28.612 -10.606 1.00 22.95 ? 5    MET A SD  1 
ATOM   41   C  CE  . MET A 1 6   ? -11.449 -27.745 -11.876 1.00 21.80 ? 5    MET A CE  1 
ATOM   42   N  N   . PRO A 1 7   ? -5.655  -30.309 -12.150 1.00 20.63 ? 6    PRO A N   1 
ATOM   43   C  CA  . PRO A 1 7   ? -4.937  -31.364 -11.426 1.00 19.43 ? 6    PRO A CA  1 
ATOM   44   C  C   . PRO A 1 7   ? -5.666  -31.763 -10.152 1.00 20.60 ? 6    PRO A C   1 
ATOM   45   O  O   . PRO A 1 7   ? -6.604  -31.103 -9.695  1.00 19.12 ? 6    PRO A O   1 
ATOM   46   C  CB  . PRO A 1 7   ? -3.587  -30.719 -11.105 1.00 23.34 ? 6    PRO A CB  1 
ATOM   47   C  CG  . PRO A 1 7   ? -3.877  -29.260 -11.072 1.00 21.73 ? 6    PRO A CG  1 
ATOM   48   C  CD  . PRO A 1 7   ? -4.918  -29.033 -12.142 1.00 22.49 ? 6    PRO A CD  1 
ATOM   49   N  N   . GLN A 1 8   ? -5.194  -32.872 -9.572  1.00 19.46 ? 7    GLN A N   1 
ATOM   50   C  CA  . GLN A 1 8   ? -5.753  -33.431 -8.355  1.00 19.38 ? 7    GLN A CA  1 
ATOM   51   C  C   . GLN A 1 8   ? -4.633  -34.085 -7.560  1.00 18.48 ? 7    GLN A C   1 
ATOM   52   O  O   . GLN A 1 8   ? -3.792  -34.781 -8.154  1.00 19.44 ? 7    GLN A O   1 
ATOM   53   C  CB  . GLN A 1 8   ? -6.842  -34.459 -8.670  1.00 17.91 ? 7    GLN A CB  1 
ATOM   54   C  CG  . GLN A 1 8   ? -7.466  -35.116 -7.446  1.00 20.43 ? 7    GLN A CG  1 
ATOM   55   C  CD  . GLN A 1 8   ? -8.589  -36.066 -7.819  1.00 23.45 ? 7    GLN A CD  1 
ATOM   56   O  OE1 . GLN A 1 8   ? -8.791  -36.376 -8.998  1.00 25.03 ? 7    GLN A OE1 1 
ATOM   57   N  NE2 . GLN A 1 8   ? -9.335  -36.525 -6.818  1.00 24.11 ? 7    GLN A NE2 1 
ATOM   58   N  N   . PRO A 1 9   ? -4.583  -33.885 -6.229  1.00 16.73 ? 8    PRO A N   1 
ATOM   59   C  CA  . PRO A 1 9   ? -3.526  -34.528 -5.438  1.00 15.71 ? 8    PRO A CA  1 
ATOM   60   C  C   . PRO A 1 9   ? -3.758  -36.024 -5.284  1.00 15.85 ? 8    PRO A C   1 
ATOM   61   O  O   . PRO A 1 9   ? -4.776  -36.560 -5.741  1.00 17.49 ? 8    PRO A O   1 
ATOM   62   C  CB  . PRO A 1 9   ? -3.593  -33.788 -4.091  1.00 14.04 ? 8    PRO A CB  1 
ATOM   63   C  CG  . PRO A 1 9   ? -5.018  -33.347 -3.976  1.00 14.28 ? 8    PRO A CG  1 
ATOM   64   C  CD  . PRO A 1 9   ? -5.421  -32.989 -5.408  1.00 16.80 ? 8    PRO A CD  1 
ATOM   65   N  N   . LYS A 1 10  ? -2.807  -36.702 -4.645  1.00 16.83 ? 9    LYS A N   1 
ATOM   66   C  CA  . LYS A 1 10  ? -2.800  -38.160 -4.614  1.00 17.21 ? 9    LYS A CA  1 
ATOM   67   C  C   . LYS A 1 10  ? -4.025  -38.710 -3.887  1.00 17.92 ? 9    LYS A C   1 
ATOM   68   O  O   . LYS A 1 10  ? -4.510  -38.138 -2.906  1.00 18.04 ? 9    LYS A O   1 
ATOM   69   C  CB  . LYS A 1 10  ? -1.516  -38.661 -3.948  1.00 17.64 ? 9    LYS A CB  1 
ATOM   70   C  CG  . LYS A 1 10  ? -1.335  -38.167 -2.503  1.00 17.13 ? 9    LYS A CG  1 
ATOM   71   C  CD  . LYS A 1 10  ? 0.073   -38.449 -2.000  1.00 17.59 ? 9    LYS A CD  1 
ATOM   72   C  CE  . LYS A 1 10  ? 0.257   -37.944 -0.578  1.00 21.41 ? 9    LYS A CE  1 
ATOM   73   N  NZ  . LYS A 1 10  ? 1.666   -38.061 -0.080  1.00 23.52 ? 9    LYS A NZ  1 
ATOM   74   N  N   . THR A 1 11  ? -4.497  -39.860 -4.366  1.00 17.49 ? 10   THR A N   1 
ATOM   75   C  CA  . THR A 1 11  ? -5.710  -40.505 -3.888  1.00 17.23 ? 10   THR A CA  1 
ATOM   76   C  C   . THR A 1 11  ? -5.397  -41.802 -3.147  1.00 16.57 ? 10   THR A C   1 
ATOM   77   O  O   . THR A 1 11  ? -4.311  -42.386 -3.269  1.00 15.14 ? 10   THR A O   1 
ATOM   78   C  CB  . THR A 1 11  ? -6.673  -40.797 -5.051  1.00 18.34 ? 10   THR A CB  1 
ATOM   79   O  OG1 . THR A 1 11  ? -6.004  -41.584 -6.056  1.00 19.57 ? 10   THR A OG1 1 
ATOM   80   C  CG2 . THR A 1 11  ? -7.186  -39.490 -5.664  1.00 16.15 ? 10   THR A CG2 1 
ATOM   81   N  N   . PHE A 1 12  ? -6.405  -42.263 -2.400  1.00 16.72 ? 11   PHE A N   1 
ATOM   82   C  CA  . PHE A 1 12  ? -6.300  -43.393 -1.479  1.00 18.52 ? 11   PHE A CA  1 
ATOM   83   C  C   . PHE A 1 12  ? -7.453  -44.372 -1.732  1.00 21.59 ? 11   PHE A C   1 
ATOM   84   O  O   . PHE A 1 12  ? -8.230  -44.702 -0.835  1.00 23.75 ? 11   PHE A O   1 
ATOM   85   C  CB  . PHE A 1 12  ? -6.320  -42.909 -0.025  1.00 16.14 ? 11   PHE A CB  1 
ATOM   86   C  CG  . PHE A 1 12  ? -5.130  -42.081 0.362   1.00 16.82 ? 11   PHE A CG  1 
ATOM   87   C  CD1 . PHE A 1 12  ? -5.031  -40.754 -0.030  1.00 16.87 ? 11   PHE A CD1 1 
ATOM   88   C  CD2 . PHE A 1 12  ? -4.120  -42.618 1.151   1.00 16.90 ? 11   PHE A CD2 1 
ATOM   89   C  CE1 . PHE A 1 12  ? -3.939  -39.984 0.338   1.00 16.67 ? 11   PHE A CE1 1 
ATOM   90   C  CE2 . PHE A 1 12  ? -3.025  -41.846 1.530   1.00 16.41 ? 11   PHE A CE2 1 
ATOM   91   C  CZ  . PHE A 1 12  ? -2.929  -40.538 1.118   1.00 16.18 ? 11   PHE A CZ  1 
ATOM   92   N  N   . GLY A 1 13  ? -7.570  -44.840 -2.972  1.00 20.83 ? 12   GLY A N   1 
ATOM   93   C  CA  . GLY A 1 13  ? -8.641  -45.777 -3.290  1.00 20.89 ? 12   GLY A CA  1 
ATOM   94   C  C   . GLY A 1 13  ? -10.016 -45.179 -3.037  1.00 21.87 ? 12   GLY A C   1 
ATOM   95   O  O   . GLY A 1 13  ? -10.301 -44.033 -3.408  1.00 22.45 ? 12   GLY A O   1 
ATOM   96   N  N   . GLU A 1 14  ? -10.887 -45.960 -2.391  1.00 22.40 ? 13   GLU A N   1 
ATOM   97   C  CA  . GLU A 1 14  ? -12.257 -45.511 -2.158  1.00 26.96 ? 13   GLU A CA  1 
ATOM   98   C  C   . GLU A 1 14  ? -12.327 -44.309 -1.228  1.00 24.45 ? 13   GLU A C   1 
ATOM   99   O  O   . GLU A 1 14  ? -13.367 -43.639 -1.182  1.00 25.32 ? 13   GLU A O   1 
ATOM   100  C  CB  . GLU A 1 14  ? -13.112 -46.650 -1.588  1.00 34.68 ? 13   GLU A CB  1 
ATOM   101  C  CG  . GLU A 1 14  ? -13.253 -47.851 -2.517  1.00 44.04 ? 13   GLU A CG  1 
ATOM   102  C  CD  . GLU A 1 14  ? -14.202 -48.906 -1.975  1.00 52.87 ? 13   GLU A CD  1 
ATOM   103  O  OE1 . GLU A 1 14  ? -15.390 -48.585 -1.757  1.00 57.65 ? 13   GLU A OE1 1 
ATOM   104  O  OE2 . GLU A 1 14  ? -13.760 -50.055 -1.756  1.00 56.38 ? 13   GLU A OE2 1 
ATOM   105  N  N   . LEU A 1 15  ? -11.263 -44.024 -0.478  1.00 23.09 ? 14   LEU A N   1 
ATOM   106  C  CA  . LEU A 1 15  ? -11.260 -42.835 0.368   1.00 21.13 ? 14   LEU A CA  1 
ATOM   107  C  C   . LEU A 1 15  ? -10.934 -41.563 -0.408  1.00 20.58 ? 14   LEU A C   1 
ATOM   108  O  O   . LEU A 1 15  ? -11.037 -40.470 0.157   1.00 21.58 ? 14   LEU A O   1 
ATOM   109  C  CB  . LEU A 1 15  ? -10.268 -43.006 1.521   1.00 21.94 ? 14   LEU A CB  1 
ATOM   110  C  CG  . LEU A 1 15  ? -10.551 -44.212 2.424   1.00 25.29 ? 14   LEU A CG  1 
ATOM   111  C  CD1 . LEU A 1 15  ? -9.503  -44.348 3.525   1.00 27.45 ? 14   LEU A CD1 1 
ATOM   112  C  CD2 . LEU A 1 15  ? -11.948 -44.126 3.026   1.00 28.06 ? 14   LEU A CD2 1 
ATOM   113  N  N   . LYS A 1 16  ? -10.525 -41.686 -1.669  1.00 18.12 ? 15   LYS A N   1 
ATOM   114  C  CA  . LYS A 1 16  ? -10.229 -40.548 -2.554  1.00 20.28 ? 15   LYS A CA  1 
ATOM   115  C  C   . LYS A 1 16  ? -9.147  -39.691 -1.895  1.00 21.25 ? 15   LYS A C   1 
ATOM   116  O  O   . LYS A 1 16  ? -8.082  -40.231 -1.554  1.00 20.00 ? 15   LYS A O   1 
ATOM   117  C  CB  . LYS A 1 16  ? -11.543 -39.854 -2.881  1.00 22.88 ? 15   LYS A CB  1 
ATOM   118  C  CG  . LYS A 1 16  ? -12.581 -40.843 -3.400  1.00 29.47 ? 15   LYS A CG  1 
ATOM   119  C  CD  . LYS A 1 16  ? -13.753 -40.185 -4.101  1.00 35.26 ? 15   LYS A CD  1 
ATOM   120  C  CE  . LYS A 1 16  ? -14.778 -41.246 -4.501  1.00 39.55 ? 15   LYS A CE  1 
ATOM   121  N  NZ  . LYS A 1 16  ? -15.901 -40.705 -5.312  1.00 41.67 ? 15   LYS A NZ  1 
ATOM   122  N  N   . ASN A 1 17  ? -9.345  -38.380 -1.716  1.00 19.15 ? 16   ASN A N   1 
ATOM   123  C  CA  . ASN A 1 17  ? -8.318  -37.526 -1.122  1.00 18.01 ? 16   ASN A CA  1 
ATOM   124  C  C   . ASN A 1 17  ? -8.458  -37.359 0.388   1.00 17.75 ? 16   ASN A C   1 
ATOM   125  O  O   . ASN A 1 17  ? -7.650  -36.642 0.991   1.00 18.39 ? 16   ASN A O   1 
ATOM   126  C  CB  . ASN A 1 17  ? -8.329  -36.128 -1.755  1.00 18.66 ? 16   ASN A CB  1 
ATOM   127  C  CG  . ASN A 1 17  ? -8.006  -36.141 -3.236  1.00 18.49 ? 16   ASN A CG  1 
ATOM   128  O  OD1 . ASN A 1 17  ? -8.811  -35.700 -4.057  1.00 18.39 ? 16   ASN A OD1 1 
ATOM   129  N  ND2 . ASN A 1 17  ? -6.814  -36.606 -3.582  1.00 18.14 ? 16   ASN A ND2 1 
ATOM   130  N  N   . LEU A 1 18  ? -9.459  -37.978 1.009   1.00 17.33 ? 17   LEU A N   1 
ATOM   131  C  CA  . LEU A 1 18  ? -9.752  -37.685 2.409   1.00 19.53 ? 17   LEU A CA  1 
ATOM   132  C  C   . LEU A 1 18  ? -8.556  -37.872 3.337   1.00 20.21 ? 17   LEU A C   1 
ATOM   133  O  O   . LEU A 1 18  ? -8.373  -37.033 4.237   1.00 19.90 ? 17   LEU A O   1 
ATOM   134  C  CB  . LEU A 1 18  ? -10.940 -38.544 2.864   1.00 23.63 ? 17   LEU A CB  1 
ATOM   135  C  CG  . LEU A 1 18  ? -11.721 -38.054 4.074   1.00 27.10 ? 17   LEU A CG  1 
ATOM   136  C  CD1 . LEU A 1 18  ? -12.190 -36.600 3.857   1.00 26.73 ? 17   LEU A CD1 1 
ATOM   137  C  CD2 . LEU A 1 18  ? -12.894 -38.987 4.323   1.00 27.91 ? 17   LEU A CD2 1 
ATOM   138  N  N   . PRO A 1 19  ? -7.722  -38.904 3.190   1.00 18.98 ? 18   PRO A N   1 
ATOM   139  C  CA  . PRO A 1 19  ? -6.599  -39.074 4.130   1.00 16.67 ? 18   PRO A CA  1 
ATOM   140  C  C   . PRO A 1 19  ? -5.588  -37.939 4.091   1.00 17.09 ? 18   PRO A C   1 
ATOM   141  O  O   . PRO A 1 19  ? -4.764  -37.834 5.013   1.00 17.72 ? 18   PRO A O   1 
ATOM   142  C  CB  . PRO A 1 19  ? -5.975  -40.411 3.698   1.00 19.23 ? 18   PRO A CB  1 
ATOM   143  C  CG  . PRO A 1 19  ? -7.139  -41.169 3.094   1.00 19.83 ? 18   PRO A CG  1 
ATOM   144  C  CD  . PRO A 1 19  ? -7.922  -40.098 2.351   1.00 17.64 ? 18   PRO A CD  1 
ATOM   145  N  N   . LEU A 1 20  ? -5.621  -37.079 3.068   1.00 15.71 ? 19   LEU A N   1 
ATOM   146  C  CA  . LEU A 1 20  ? -4.740  -35.914 3.064   1.00 16.65 ? 19   LEU A CA  1 
ATOM   147  C  C   . LEU A 1 20  ? -5.064  -34.954 4.205   1.00 16.93 ? 19   LEU A C   1 
ATOM   148  O  O   . LEU A 1 20  ? -4.217  -34.131 4.569   1.00 18.77 ? 19   LEU A O   1 
ATOM   149  C  CB  . LEU A 1 20  ? -4.825  -35.189 1.715   1.00 15.65 ? 19   LEU A CB  1 
ATOM   150  C  CG  . LEU A 1 20  ? -4.314  -36.015 0.525   1.00 15.91 ? 19   LEU A CG  1 
ATOM   151  C  CD1 . LEU A 1 20  ? -4.542  -35.306 -0.806  1.00 18.91 ? 19   LEU A CD1 1 
ATOM   152  C  CD2 . LEU A 1 20  ? -2.838  -36.386 0.677   1.00 17.88 ? 19   LEU A CD2 1 
ATOM   153  N  N   . LEU A 1 21  ? -6.267  -35.041 4.772   1.00 17.99 ? 20   LEU A N   1 
ATOM   154  C  CA  . LEU A 1 21  ? -6.676  -34.230 5.913   1.00 18.50 ? 20   LEU A CA  1 
ATOM   155  C  C   . LEU A 1 21  ? -6.367  -34.892 7.248   1.00 19.48 ? 20   LEU A C   1 
ATOM   156  O  O   . LEU A 1 21  ? -6.674  -34.310 8.302   1.00 20.36 ? 20   LEU A O   1 
ATOM   157  C  CB  . LEU A 1 21  ? -8.176  -33.927 5.834   1.00 18.60 ? 20   LEU A CB  1 
ATOM   158  C  CG  . LEU A 1 21  ? -8.635  -33.232 4.547   1.00 22.17 ? 20   LEU A CG  1 
ATOM   159  C  CD1 . LEU A 1 21  ? -10.145 -33.020 4.534   1.00 22.46 ? 20   LEU A CD1 1 
ATOM   160  C  CD2 . LEU A 1 21  ? -7.900  -31.914 4.360   1.00 21.48 ? 20   LEU A CD2 1 
ATOM   161  N  N   . ASN A 1 22  ? -5.786  -36.098 7.237   1.00 20.08 ? 21   ASN A N   1 
ATOM   162  C  CA  . ASN A 1 22  ? -5.410  -36.780 8.479   1.00 22.28 ? 21   ASN A CA  1 
ATOM   163  C  C   . ASN A 1 22  ? -4.075  -36.211 8.959   1.00 20.51 ? 21   ASN A C   1 
ATOM   164  O  O   . ASN A 1 22  ? -3.016  -36.832 8.856   1.00 25.26 ? 21   ASN A O   1 
ATOM   165  C  CB  . ASN A 1 22  ? -5.346  -38.289 8.275   1.00 25.51 ? 21   ASN A CB  1 
ATOM   166  C  CG  . ASN A 1 22  ? -5.189  -39.056 9.587   1.00 31.63 ? 21   ASN A CG  1 
ATOM   167  O  OD1 . ASN A 1 22  ? -5.220  -38.471 10.669  1.00 34.59 ? 21   ASN A OD1 1 
ATOM   168  N  ND2 . ASN A 1 22  ? -5.035  -40.370 9.491   1.00 33.76 ? 21   ASN A ND2 1 
ATOM   169  N  N   . THR A 1 23  ? -4.150  -34.987 9.477   1.00 21.15 ? 22   THR A N   1 
ATOM   170  C  CA  . THR A 1 23  ? -2.999  -34.257 9.993   1.00 20.49 ? 22   THR A CA  1 
ATOM   171  C  C   . THR A 1 23  ? -3.508  -33.179 10.940  1.00 20.31 ? 22   THR A C   1 
ATOM   172  O  O   . THR A 1 23  ? -4.651  -32.732 10.840  1.00 20.75 ? 22   THR A O   1 
ATOM   173  C  CB  . THR A 1 23  ? -2.160  -33.633 8.863   1.00 22.65 ? 22   THR A CB  1 
ATOM   174  O  OG1 . THR A 1 23  ? -1.183  -32.742 9.422   1.00 26.57 ? 22   THR A OG1 1 
ATOM   175  C  CG2 . THR A 1 23  ? -3.041  -32.860 7.874   1.00 21.37 ? 22   THR A CG2 1 
ATOM   176  N  N   . ASP A 1 24  ? -2.653  -32.770 11.873  1.00 22.12 ? 23   ASP A N   1 
ATOM   177  C  CA  . ASP A 1 24  ? -3.058  -31.697 12.768  1.00 22.61 ? 23   ASP A CA  1 
ATOM   178  C  C   . ASP A 1 24  ? -2.971  -30.323 12.115  1.00 19.32 ? 23   ASP A C   1 
ATOM   179  O  O   . ASP A 1 24  ? -3.427  -29.346 12.713  1.00 18.79 ? 23   ASP A O   1 
ATOM   180  C  CB  . ASP A 1 24  ? -2.209  -31.719 14.043  1.00 31.17 ? 23   ASP A CB  1 
ATOM   181  C  CG  . ASP A 1 24  ? -0.736  -31.521 13.762  1.00 41.58 ? 23   ASP A CG  1 
ATOM   182  O  OD1 . ASP A 1 24  ? -0.300  -31.813 12.625  1.00 44.93 ? 23   ASP A OD1 1 
ATOM   183  O  OD2 . ASP A 1 24  ? -0.013  -31.076 14.679  1.00 47.83 ? 23   ASP A OD2 1 
ATOM   184  N  N   . LYS A 1 25  ? -2.424  -30.221 10.903  1.00 17.88 ? 24   LYS A N   1 
ATOM   185  C  CA  . LYS A 1 25  ? -2.244  -28.937 10.220  1.00 15.72 ? 24   LYS A CA  1 
ATOM   186  C  C   . LYS A 1 25  ? -2.788  -29.029 8.798   1.00 17.07 ? 24   LYS A C   1 
ATOM   187  O  O   . LYS A 1 25  ? -2.050  -28.877 7.818   1.00 16.93 ? 24   LYS A O   1 
ATOM   188  C  CB  . LYS A 1 25  ? -0.772  -28.522 10.224  1.00 15.72 ? 24   LYS A CB  1 
ATOM   189  C  CG  . LYS A 1 25  ? -0.217  -28.215 11.618  1.00 17.92 ? 24   LYS A CG  1 
ATOM   190  C  CD  . LYS A 1 25  ? 1.251   -27.758 11.594  1.00 19.60 ? 24   LYS A CD  1 
ATOM   191  C  CE  . LYS A 1 25  ? 1.749   -27.494 13.016  1.00 19.88 ? 24   LYS A CE  1 
ATOM   192  N  NZ  . LYS A 1 25  ? 3.155   -27.007 13.096  1.00 23.04 ? 24   LYS A NZ  1 
ATOM   193  N  N   . PRO A 1 26  ? -4.095  -29.259 8.651   1.00 15.14 ? 25   PRO A N   1 
ATOM   194  C  CA  . PRO A 1 26  ? -4.635  -29.488 7.301   1.00 14.74 ? 25   PRO A CA  1 
ATOM   195  C  C   . PRO A 1 26  ? -4.590  -28.271 6.384   1.00 15.62 ? 25   PRO A C   1 
ATOM   196  O  O   . PRO A 1 26  ? -4.369  -28.446 5.180   1.00 16.57 ? 25   PRO A O   1 
ATOM   197  C  CB  . PRO A 1 26  ? -6.074  -29.948 7.579   1.00 14.63 ? 25   PRO A CB  1 
ATOM   198  C  CG  . PRO A 1 26  ? -6.405  -29.367 8.915   1.00 14.80 ? 25   PRO A CG  1 
ATOM   199  C  CD  . PRO A 1 26  ? -5.117  -29.434 9.696   1.00 14.77 ? 25   PRO A CD  1 
ATOM   200  N  N   . VAL A 1 27  ? -4.825  -27.052 6.888   1.00 15.63 ? 26   VAL A N   1 
ATOM   201  C  CA  . VAL A 1 27  ? -4.741  -25.881 6.011   1.00 13.57 ? 26   VAL A CA  1 
ATOM   202  C  C   . VAL A 1 27  ? -3.333  -25.734 5.458   1.00 16.00 ? 26   VAL A C   1 
ATOM   203  O  O   . VAL A 1 27  ? -3.138  -25.453 4.264   1.00 15.28 ? 26   VAL A O   1 
ATOM   204  C  CB  . VAL A 1 27  ? -5.175  -24.603 6.753   1.00 15.50 ? 26   VAL A CB  1 
ATOM   205  C  CG1 . VAL A 1 27  ? -4.786  -23.358 5.934   1.00 14.96 ? 26   VAL A CG1 1 
ATOM   206  C  CG2 . VAL A 1 27  ? -6.668  -24.621 7.005   1.00 16.07 ? 26   VAL A CG2 1 
ATOM   207  N  N   . GLN A 1 28  ? -2.328  -25.905 6.318   1.00 15.63 ? 27   GLN A N   1 
ATOM   208  C  CA  . GLN A 1 28  ? -0.953  -25.799 5.853   1.00 14.30 ? 27   GLN A CA  1 
ATOM   209  C  C   . GLN A 1 28  ? -0.610  -26.920 4.877   1.00 17.26 ? 27   GLN A C   1 
ATOM   210  O  O   . GLN A 1 28  ? 0.147   -26.697 3.923   1.00 16.86 ? 27   GLN A O   1 
ATOM   211  C  CB  . GLN A 1 28  ? -0.011  -25.763 7.060   1.00 15.33 ? 27   GLN A CB  1 
ATOM   212  C  CG  . GLN A 1 28  ? -0.171  -24.466 7.868   1.00 16.29 ? 27   GLN A CG  1 
ATOM   213  C  CD  . GLN A 1 28  ? 0.422   -24.525 9.258   1.00 15.95 ? 27   GLN A CD  1 
ATOM   214  O  OE1 . GLN A 1 28  ? 1.614   -24.286 9.446   1.00 18.59 ? 27   GLN A OE1 1 
ATOM   215  N  NE2 . GLN A 1 28  ? -0.421  -24.822 10.253  1.00 17.84 ? 27   GLN A NE2 1 
ATOM   216  N  N   . ALA A 1 29  ? -1.190  -28.110 5.059   1.00 15.82 ? 28   ALA A N   1 
ATOM   217  C  CA  . ALA A 1 29  ? -0.980  -29.177 4.079   1.00 15.20 ? 28   ALA A CA  1 
ATOM   218  C  C   . ALA A 1 29  ? -1.621  -28.832 2.738   1.00 17.68 ? 28   ALA A C   1 
ATOM   219  O  O   . ALA A 1 29  ? -1.059  -29.149 1.678   1.00 19.28 ? 28   ALA A O   1 
ATOM   220  C  CB  . ALA A 1 29  ? -1.523  -30.503 4.610   1.00 15.79 ? 28   ALA A CB  1 
ATOM   221  N  N   . LEU A 1 30  ? -2.801  -28.197 2.759   1.00 14.01 ? 29   LEU A N   1 
ATOM   222  C  CA  . LEU A 1 30  ? -3.431  -27.787 1.504   1.00 15.22 ? 29   LEU A CA  1 
ATOM   223  C  C   . LEU A 1 30  ? -2.641  -26.676 0.820   1.00 17.04 ? 29   LEU A C   1 
ATOM   224  O  O   . LEU A 1 30  ? -2.583  -26.631 -0.417  1.00 16.75 ? 29   LEU A O   1 
ATOM   225  C  CB  . LEU A 1 30  ? -4.881  -27.353 1.752   1.00 15.80 ? 29   LEU A CB  1 
ATOM   226  C  CG  . LEU A 1 30  ? -5.866  -28.493 2.055   1.00 14.19 ? 29   LEU A CG  1 
ATOM   227  C  CD1 . LEU A 1 30  ? -7.080  -28.016 2.861   1.00 14.54 ? 29   LEU A CD1 1 
ATOM   228  C  CD2 . LEU A 1 30  ? -6.314  -29.193 0.765   1.00 14.76 ? 29   LEU A CD2 1 
ATOM   229  N  N   . MET A 1 31  ? -2.023  -25.781 1.599   1.00 18.01 ? 30   MET A N   1 
ATOM   230  C  CA  . MET A 1 31  ? -1.143  -24.769 1.013   1.00 16.26 ? 30   MET A CA  1 
ATOM   231  C  C   . MET A 1 31  ? 0.021   -25.413 0.270   1.00 17.72 ? 30   MET A C   1 
ATOM   232  O  O   . MET A 1 31  ? 0.402   -24.966 -0.822  1.00 19.28 ? 30   MET A O   1 
ATOM   233  C  CB  . MET A 1 31  ? -0.621  -23.826 2.101   1.00 13.26 ? 30   MET A CB  1 
ATOM   234  C  CG  . MET A 1 31  ? -1.691  -22.912 2.671   1.00 14.63 ? 30   MET A CG  1 
ATOM   235  S  SD  . MET A 1 31  ? -1.137  -21.923 4.084   1.00 17.62 ? 30   MET A SD  1 
ATOM   236  C  CE  . MET A 1 31  ? 0.096   -20.862 3.316   1.00 17.26 ? 30   MET A CE  1 
ATOM   237  N  N   . LYS A 1 32  ? 0.603   -26.463 0.846   1.00 16.67 ? 31   LYS A N   1 
ATOM   238  C  CA  . LYS A 1 32  ? 1.720   -27.137 0.189   1.00 18.65 ? 31   LYS A CA  1 
ATOM   239  C  C   . LYS A 1 32  ? 1.265   -27.839 -1.091  1.00 18.50 ? 31   LYS A C   1 
ATOM   240  O  O   . LYS A 1 32  ? 1.992   -27.845 -2.095  1.00 18.62 ? 31   LYS A O   1 
ATOM   241  C  CB  . LYS A 1 32  ? 2.369   -28.113 1.169   1.00 23.58 ? 31   LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 32  ? 3.742   -28.623 0.754   1.00 30.34 ? 31   LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 32  ? 4.556   -29.039 1.979   1.00 37.98 ? 31   LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 32  ? 5.872   -29.686 1.584   1.00 43.23 ? 31   LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 32  ? 6.404   -30.556 2.685   1.00 46.00 ? 31   LYS A NZ  1 
ATOM   246  N  N   . ILE A 1 33  ? 0.056   -28.411 -1.087  1.00 16.59 ? 32   ILE A N   1 
ATOM   247  C  CA  . ILE A 1 33  ? -0.503  -28.960 -2.322  1.00 16.44 ? 32   ILE A CA  1 
ATOM   248  C  C   . ILE A 1 33  ? -0.685  -27.859 -3.364  1.00 18.38 ? 32   ILE A C   1 
ATOM   249  O  O   . ILE A 1 33  ? -0.369  -28.043 -4.549  1.00 16.73 ? 32   ILE A O   1 
ATOM   250  C  CB  . ILE A 1 33  ? -1.826  -29.695 -2.037  1.00 17.12 ? 32   ILE A CB  1 
ATOM   251  C  CG1 . ILE A 1 33  ? -1.572  -30.924 -1.154  1.00 16.25 ? 32   ILE A CG1 1 
ATOM   252  C  CG2 . ILE A 1 33  ? -2.504  -30.100 -3.371  1.00 17.35 ? 32   ILE A CG2 1 
ATOM   253  C  CD1 . ILE A 1 33  ? -2.838  -31.555 -0.581  1.00 14.47 ? 32   ILE A CD1 1 
ATOM   254  N  N   . ALA A 1 34  ? -1.199  -26.698 -2.946  1.00 18.79 ? 33   ALA A N   1 
ATOM   255  C  CA  . ALA A 1 34  ? -1.359  -25.585 -3.882  1.00 17.41 ? 33   ALA A CA  1 
ATOM   256  C  C   . ALA A 1 34  ? -0.015  -25.154 -4.466  1.00 19.67 ? 33   ALA A C   1 
ATOM   257  O  O   . ALA A 1 34  ? 0.073   -24.818 -5.655  1.00 19.80 ? 33   ALA A O   1 
ATOM   258  C  CB  . ALA A 1 34  ? -2.059  -24.411 -3.186  1.00 16.86 ? 33   ALA A CB  1 
ATOM   259  N  N   . ASP A 1 35  ? 1.046   -25.158 -3.648  1.00 18.46 ? 34   ASP A N   1 
ATOM   260  C  CA  . ASP A 1 35  ? 2.382   -24.864 -4.167  1.00 20.38 ? 34   ASP A CA  1 
ATOM   261  C  C   . ASP A 1 35  ? 2.747   -25.803 -5.305  1.00 20.75 ? 34   ASP A C   1 
ATOM   262  O  O   . ASP A 1 35  ? 3.381   -25.393 -6.286  1.00 25.24 ? 34   ASP A O   1 
ATOM   263  C  CB  . ASP A 1 35  ? 3.438   -24.989 -3.068  1.00 24.45 ? 34   ASP A CB  1 
ATOM   264  C  CG  . ASP A 1 35  ? 3.431   -23.831 -2.102  1.00 29.54 ? 34   ASP A CG  1 
ATOM   265  O  OD1 . ASP A 1 35  ? 2.921   -22.749 -2.455  1.00 32.36 ? 34   ASP A OD1 1 
ATOM   266  O  OD2 . ASP A 1 35  ? 3.956   -24.007 -0.983  1.00 33.56 ? 34   ASP A OD2 1 
ATOM   267  N  N   . GLU A 1 36  ? 2.373   -27.071 -5.181  1.00 21.68 ? 35   GLU A N   1 
ATOM   268  C  CA  . GLU A 1 36  ? 2.790   -28.065 -6.160  1.00 22.75 ? 35   GLU A CA  1 
ATOM   269  C  C   . GLU A 1 36  ? 1.878   -28.072 -7.383  1.00 22.22 ? 35   GLU A C   1 
ATOM   270  O  O   . GLU A 1 36  ? 2.353   -28.263 -8.508  1.00 25.46 ? 35   GLU A O   1 
ATOM   271  C  CB  . GLU A 1 36  ? 2.824   -29.452 -5.512  1.00 27.22 ? 35   GLU A CB  1 
ATOM   272  C  CG  . GLU A 1 36  ? 3.219   -30.560 -6.489  1.00 33.92 ? 35   GLU A CG  1 
ATOM   273  C  CD  . GLU A 1 36  ? 3.111   -31.960 -5.906  1.00 42.80 ? 35   GLU A CD  1 
ATOM   274  O  OE1 . GLU A 1 36  ? 3.153   -32.109 -4.664  1.00 43.89 ? 35   GLU A OE1 1 
ATOM   275  O  OE2 . GLU A 1 36  ? 2.985   -32.918 -6.706  1.00 46.68 ? 35   GLU A OE2 1 
ATOM   276  N  N   . LEU A 1 37  ? 0.574   -27.857 -7.190  1.00 19.13 ? 36   LEU A N   1 
ATOM   277  C  CA  . LEU A 1 37  ? -0.391  -28.052 -8.267  1.00 20.15 ? 36   LEU A CA  1 
ATOM   278  C  C   . LEU A 1 37  ? -0.871  -26.765 -8.926  1.00 20.05 ? 36   LEU A C   1 
ATOM   279  O  O   . LEU A 1 37  ? -1.334  -26.821 -10.070 1.00 20.71 ? 36   LEU A O   1 
ATOM   280  C  CB  . LEU A 1 37  ? -1.608  -28.826 -7.754  1.00 19.19 ? 36   LEU A CB  1 
ATOM   281  C  CG  . LEU A 1 37  ? -1.358  -30.264 -7.301  1.00 20.90 ? 36   LEU A CG  1 
ATOM   282  C  CD1 . LEU A 1 37  ? -2.694  -30.942 -7.027  1.00 21.26 ? 36   LEU A CD1 1 
ATOM   283  C  CD2 . LEU A 1 37  ? -0.530  -31.041 -8.339  1.00 21.89 ? 36   LEU A CD2 1 
ATOM   284  N  N   . GLY A 1 38  ? -0.798  -25.625 -8.251  1.00 18.12 ? 37   GLY A N   1 
ATOM   285  C  CA  . GLY A 1 38  ? -1.111  -24.344 -8.863  1.00 18.58 ? 37   GLY A CA  1 
ATOM   286  C  C   . GLY A 1 38  ? -2.418  -23.735 -8.383  1.00 18.54 ? 37   GLY A C   1 
ATOM   287  O  O   . GLY A 1 38  ? -2.912  -24.011 -7.282  1.00 19.11 ? 37   GLY A O   1 
ATOM   288  N  N   . GLU A 1 39  ? -3.001  -22.900 -9.255  1.00 16.79 ? 38   GLU A N   1 
ATOM   289  C  CA  . GLU A 1 39  ? -4.091  -22.013 -8.852  1.00 17.08 ? 38   GLU A CA  1 
ATOM   290  C  C   . GLU A 1 39  ? -5.417  -22.735 -8.618  1.00 16.70 ? 38   GLU A C   1 
ATOM   291  O  O   . GLU A 1 39  ? -6.321  -22.143 -8.014  1.00 15.23 ? 38   GLU A O   1 
ATOM   292  C  CB  . GLU A 1 39  ? -4.283  -20.920 -9.912  1.00 18.69 ? 38   GLU A CB  1 
ATOM   293  C  CG  . GLU A 1 39  ? -4.798  -21.459 -11.241 1.00 20.41 ? 38   GLU A CG  1 
ATOM   294  C  CD  . GLU A 1 39  ? -4.953  -20.382 -12.300 1.00 23.95 ? 38   GLU A CD  1 
ATOM   295  O  OE1 . GLU A 1 39  ? -5.016  -19.183 -11.940 1.00 21.68 ? 38   GLU A OE1 1 
ATOM   296  O  OE2 . GLU A 1 39  ? -5.001  -20.740 -13.500 1.00 26.47 ? 38   GLU A OE2 1 
ATOM   297  N  N   . ILE A 1 40  ? -5.569  -23.980 -9.071  1.00 16.07 ? 39   ILE A N   1 
ATOM   298  C  CA  . ILE A 1 40  ? -6.830  -24.696 -8.897  1.00 14.07 ? 39   ILE A CA  1 
ATOM   299  C  C   . ILE A 1 40  ? -6.556  -26.195 -8.864  1.00 17.29 ? 39   ILE A C   1 
ATOM   300  O  O   . ILE A 1 40  ? -5.832  -26.721 -9.716  1.00 19.13 ? 39   ILE A O   1 
ATOM   301  C  CB  . ILE A 1 40  ? -7.839  -24.342 -10.013 1.00 15.34 ? 39   ILE A CB  1 
ATOM   302  C  CG1 . ILE A 1 40  ? -9.196  -25.007 -9.753  1.00 16.59 ? 39   ILE A CG1 1 
ATOM   303  C  CG2 . ILE A 1 40  ? -7.286  -24.739 -11.388 1.00 19.42 ? 39   ILE A CG2 1 
ATOM   304  C  CD1 . ILE A 1 40  ? -10.306 -24.468 -10.649 1.00 17.63 ? 39   ILE A CD1 1 
ATOM   305  N  N   . PHE A 1 41  ? -7.127  -26.896 -7.878  1.00 15.02 ? 40   PHE A N   1 
ATOM   306  C  CA  . PHE A 1 41  ? -7.060  -28.351 -7.905  1.00 15.45 ? 40   PHE A CA  1 
ATOM   307  C  C   . PHE A 1 41  ? -8.353  -28.963 -7.380  1.00 15.72 ? 40   PHE A C   1 
ATOM   308  O  O   . PHE A 1 41  ? -9.051  -28.381 -6.543  1.00 15.03 ? 40   PHE A O   1 
ATOM   309  C  CB  . PHE A 1 41  ? -5.838  -28.900 -7.139  1.00 15.90 ? 40   PHE A CB  1 
ATOM   310  C  CG  . PHE A 1 41  ? -5.783  -28.534 -5.669  1.00 15.12 ? 40   PHE A CG  1 
ATOM   311  C  CD1 . PHE A 1 41  ? -5.097  -27.407 -5.246  1.00 16.86 ? 40   PHE A CD1 1 
ATOM   312  C  CD2 . PHE A 1 41  ? -6.356  -29.361 -4.711  1.00 15.75 ? 40   PHE A CD2 1 
ATOM   313  C  CE1 . PHE A 1 41  ? -5.016  -27.084 -3.896  1.00 15.69 ? 40   PHE A CE1 1 
ATOM   314  C  CE2 . PHE A 1 41  ? -6.280  -29.048 -3.358  1.00 14.01 ? 40   PHE A CE2 1 
ATOM   315  C  CZ  . PHE A 1 41  ? -5.609  -27.908 -2.950  1.00 15.65 ? 40   PHE A CZ  1 
ATOM   316  N  N   . LYS A 1 42  ? -8.673  -30.140 -7.918  1.00 17.61 ? 41   LYS A N   1 
ATOM   317  C  CA  . LYS A 1 42  ? -9.839  -30.905 -7.500  1.00 18.44 ? 41   LYS A CA  1 
ATOM   318  C  C   . LYS A 1 42  ? -9.540  -31.668 -6.212  1.00 16.41 ? 41   LYS A C   1 
ATOM   319  O  O   . LYS A 1 42  ? -8.424  -32.152 -6.013  1.00 18.73 ? 41   LYS A O   1 
ATOM   320  C  CB  . LYS A 1 42  ? -10.241 -31.876 -8.612  1.00 21.30 ? 41   LYS A CB  1 
ATOM   321  C  CG  . LYS A 1 42  ? -11.411 -32.771 -8.284  1.00 23.98 ? 41   LYS A CG  1 
ATOM   322  C  CD  . LYS A 1 42  ? -11.871 -33.521 -9.527  1.00 29.44 ? 41   LYS A CD  1 
ATOM   323  C  CE  . LYS A 1 42  ? -12.993 -34.490 -9.204  1.00 35.20 ? 41   LYS A CE  1 
ATOM   324  N  NZ  . LYS A 1 42  ? -13.623 -35.039 -10.440 1.00 38.52 ? 41   LYS A NZ  1 
ATOM   325  N  N   . PHE A 1 43  ? -10.536 -31.760 -5.323  1.00 16.17 ? 42   PHE A N   1 
ATOM   326  C  CA  . PHE A 1 43  ? -10.386 -32.508 -4.076  1.00 16.21 ? 42   PHE A CA  1 
ATOM   327  C  C   . PHE A 1 43  ? -11.654 -33.317 -3.839  1.00 15.50 ? 42   PHE A C   1 
ATOM   328  O  O   . PHE A 1 43  ? -12.747 -32.745 -3.757  1.00 17.69 ? 42   PHE A O   1 
ATOM   329  C  CB  . PHE A 1 43  ? -10.118 -31.559 -2.898  1.00 17.88 ? 42   PHE A CB  1 
ATOM   330  C  CG  . PHE A 1 43  ? -9.672  -32.251 -1.628  1.00 20.27 ? 42   PHE A CG  1 
ATOM   331  C  CD1 . PHE A 1 43  ? -10.595 -32.842 -0.776  1.00 20.87 ? 42   PHE A CD1 1 
ATOM   332  C  CD2 . PHE A 1 43  ? -8.329  -32.283 -1.275  1.00 21.30 ? 42   PHE A CD2 1 
ATOM   333  C  CE1 . PHE A 1 43  ? -10.183 -33.458 0.409   1.00 22.78 ? 42   PHE A CE1 1 
ATOM   334  C  CE2 . PHE A 1 43  ? -7.912  -32.898 -0.097  1.00 21.58 ? 42   PHE A CE2 1 
ATOM   335  C  CZ  . PHE A 1 43  ? -8.841  -33.483 0.744   1.00 22.47 ? 42   PHE A CZ  1 
ATOM   336  N  N   . GLU A 1 44  ? -11.510 -34.639 -3.724  1.00 19.01 ? 43   GLU A N   1 
ATOM   337  C  CA  . GLU A 1 44  ? -12.638 -35.550 -3.591  1.00 19.68 ? 43   GLU A CA  1 
ATOM   338  C  C   . GLU A 1 44  ? -12.607 -36.283 -2.255  1.00 19.29 ? 43   GLU A C   1 
ATOM   339  O  O   . GLU A 1 44  ? -11.543 -36.616 -1.726  1.00 20.20 ? 43   GLU A O   1 
ATOM   340  C  CB  . GLU A 1 44  ? -12.663 -36.593 -4.717  1.00 23.81 ? 43   GLU A CB  1 
ATOM   341  C  CG  . GLU A 1 44  ? -13.051 -36.051 -6.080  1.00 26.98 ? 43   GLU A CG  1 
ATOM   342  C  CD  . GLU A 1 44  ? -13.048 -37.126 -7.148  1.00 31.84 ? 43   GLU A CD  1 
ATOM   343  O  OE1 . GLU A 1 44  ? -12.072 -37.906 -7.218  1.00 31.70 ? 43   GLU A OE1 1 
ATOM   344  O  OE2 . GLU A 1 44  ? -14.027 -37.197 -7.916  1.00 35.77 ? 43   GLU A OE2 1 
ATOM   345  N  N   . ALA A 1 45  ? -13.795 -36.539 -1.730  1.00 18.20 ? 44   ALA A N   1 
ATOM   346  C  CA  . ALA A 1 45  ? -14.037 -37.452 -0.626  1.00 22.02 ? 44   ALA A CA  1 
ATOM   347  C  C   . ALA A 1 45  ? -15.235 -38.302 -1.007  1.00 24.20 ? 44   ALA A C   1 
ATOM   348  O  O   . ALA A 1 45  ? -15.954 -37.976 -1.957  1.00 25.60 ? 44   ALA A O   1 
ATOM   349  C  CB  . ALA A 1 45  ? -14.313 -36.701 0.686   1.00 25.54 ? 44   ALA A CB  1 
ATOM   350  N  N   . PRO A 1 46  ? -15.475 -39.404 -0.301  1.00 25.66 ? 45   PRO A N   1 
ATOM   351  C  CA  . PRO A 1 46  ? -16.694 -40.173 -0.577  1.00 27.16 ? 45   PRO A CA  1 
ATOM   352  C  C   . PRO A 1 46  ? -17.924 -39.278 -0.567  1.00 30.22 ? 45   PRO A C   1 
ATOM   353  O  O   . PRO A 1 46  ? -18.214 -38.620 0.436   1.00 29.59 ? 45   PRO A O   1 
ATOM   354  C  CB  . PRO A 1 46  ? -16.713 -41.211 0.553   1.00 25.67 ? 45   PRO A CB  1 
ATOM   355  C  CG  . PRO A 1 46  ? -15.241 -41.429 0.851   1.00 24.45 ? 45   PRO A CG  1 
ATOM   356  C  CD  . PRO A 1 46  ? -14.624 -40.056 0.712   1.00 24.73 ? 45   PRO A CD  1 
ATOM   357  N  N   . GLY A 1 47  ? -18.617 -39.211 -1.704  1.00 33.40 ? 46   GLY A N   1 
ATOM   358  C  CA  . GLY A 1 47  ? -19.843 -38.446 -1.808  1.00 32.78 ? 46   GLY A CA  1 
ATOM   359  C  C   . GLY A 1 47  ? -19.685 -36.948 -1.940  1.00 31.32 ? 46   GLY A C   1 
ATOM   360  O  O   . GLY A 1 47  ? -20.674 -36.224 -1.792  1.00 35.20 ? 46   GLY A O   1 
ATOM   361  N  N   . ARG A 1 48  ? -18.482 -36.448 -2.217  1.00 27.66 ? 47   ARG A N   1 
ATOM   362  C  CA  . ARG A 1 48  ? -18.303 -35.003 -2.274  1.00 25.42 ? 47   ARG A CA  1 
ATOM   363  C  C   . ARG A 1 48  ? -17.135 -34.646 -3.182  1.00 26.15 ? 47   ARG A C   1 
ATOM   364  O  O   . ARG A 1 48  ? -16.135 -35.369 -3.250  1.00 25.49 ? 47   ARG A O   1 
ATOM   365  C  CB  . ARG A 1 48  ? -18.084 -34.407 -0.876  1.00 28.15 ? 47   ARG A CB  1 
ATOM   366  C  CG  . ARG A 1 48  ? -17.458 -33.009 -0.899  1.00 31.94 ? 47   ARG A CG  1 
ATOM   367  C  CD  . ARG A 1 48  ? -18.012 -32.089 0.183   1.00 28.60 ? 47   ARG A CD  1 
ATOM   368  N  NE  . ARG A 1 48  ? -17.400 -30.762 0.151   1.00 25.27 ? 47   ARG A NE  1 
ATOM   369  C  CZ  . ARG A 1 48  ? -16.723 -30.227 1.161   1.00 26.72 ? 47   ARG A CZ  1 
ATOM   370  N  NH1 . ARG A 1 48  ? -16.541 -30.886 2.297   1.00 28.73 ? 47   ARG A NH1 1 
ATOM   371  N  NH2 . ARG A 1 48  ? -16.223 -28.998 1.035   1.00 24.16 ? 47   ARG A NH2 1 
ATOM   372  N  N   . VAL A 1 49  ? -17.276 -33.512 -3.867  1.00 22.10 ? 48   VAL A N   1 
ATOM   373  C  CA  . VAL A 1 49  ? -16.219 -32.923 -4.684  1.00 22.53 ? 48   VAL A CA  1 
ATOM   374  C  C   . VAL A 1 49  ? -16.167 -31.428 -4.396  1.00 21.92 ? 48   VAL A C   1 
ATOM   375  O  O   . VAL A 1 49  ? -17.208 -30.775 -4.266  1.00 23.04 ? 48   VAL A O   1 
ATOM   376  C  CB  . VAL A 1 49  ? -16.452 -33.164 -6.193  1.00 23.14 ? 48   VAL A CB  1 
ATOM   377  C  CG1 . VAL A 1 49  ? -15.346 -32.507 -7.016  1.00 21.39 ? 48   VAL A CG1 1 
ATOM   378  C  CG2 . VAL A 1 49  ? -16.552 -34.651 -6.504  1.00 27.83 ? 48   VAL A CG2 1 
ATOM   379  N  N   . THR A 1 50  ? -14.956 -30.880 -4.301  1.00 16.70 ? 49   THR A N   1 
ATOM   380  C  CA  . THR A 1 50  ? -14.779 -29.435 -4.261  1.00 14.40 ? 49   THR A CA  1 
ATOM   381  C  C   . THR A 1 50  ? -13.524 -29.086 -5.048  1.00 16.32 ? 49   THR A C   1 
ATOM   382  O  O   . THR A 1 50  ? -12.793 -29.965 -5.515  1.00 19.77 ? 49   THR A O   1 
ATOM   383  C  CB  . THR A 1 50  ? -14.731 -28.905 -2.812  1.00 16.23 ? 49   THR A CB  1 
ATOM   384  O  OG1 . THR A 1 50  ? -14.886 -27.481 -2.808  1.00 17.73 ? 49   THR A OG1 1 
ATOM   385  C  CG2 . THR A 1 50  ? -13.424 -29.269 -2.133  1.00 16.33 ? 49   THR A CG2 1 
ATOM   386  N  N   . ARG A 1 51  ? -13.302 -27.787 -5.235  1.00 14.06 ? 50   ARG A N   1 
ATOM   387  C  CA  . ARG A 1 51  ? -12.166 -27.270 -5.993  1.00 14.72 ? 50   ARG A CA  1 
ATOM   388  C  C   . ARG A 1 51  ? -11.511 -26.152 -5.196  1.00 15.94 ? 50   ARG A C   1 
ATOM   389  O  O   . ARG A 1 51  ? -12.175 -25.165 -4.855  1.00 16.45 ? 50   ARG A O   1 
ATOM   390  C  CB  . ARG A 1 51  ? -12.615 -26.755 -7.370  1.00 18.45 ? 50   ARG A CB  1 
ATOM   391  C  CG  . ARG A 1 51  ? -13.346 -27.806 -8.208  1.00 19.56 ? 50   ARG A CG  1 
ATOM   392  C  CD  . ARG A 1 51  ? -14.614 -27.259 -8.840  1.00 20.20 ? 50   ARG A CD  1 
ATOM   393  N  NE  . ARG A 1 51  ? -15.383 -28.319 -9.481  1.00 21.10 ? 50   ARG A NE  1 
ATOM   394  C  CZ  . ARG A 1 51  ? -16.357 -29.006 -8.897  1.00 20.80 ? 50   ARG A CZ  1 
ATOM   395  N  NH1 . ARG A 1 51  ? -16.778 -28.710 -7.673  1.00 20.58 ? 50   ARG A NH1 1 
ATOM   396  N  NH2 . ARG A 1 51  ? -16.938 -30.003 -9.565  1.00 19.76 ? 50   ARG A NH2 1 
ATOM   397  N  N   . TYR A 1 52  ? -10.208 -26.286 -4.925  1.00 14.40 ? 51   TYR A N   1 
ATOM   398  C  CA  . TYR A 1 52  ? -9.470  -25.292 -4.145  1.00 12.73 ? 51   TYR A CA  1 
ATOM   399  C  C   . TYR A 1 52  ? -8.878  -24.232 -5.064  1.00 14.39 ? 51   TYR A C   1 
ATOM   400  O  O   . TYR A 1 52  ? -8.087  -24.553 -5.958  1.00 16.26 ? 51   TYR A O   1 
ATOM   401  C  CB  . TYR A 1 52  ? -8.368  -25.958 -3.320  1.00 10.68 ? 51   TYR A CB  1 
ATOM   402  C  CG  . TYR A 1 52  ? -8.914  -26.643 -2.093  1.00 12.65 ? 51   TYR A CG  1 
ATOM   403  C  CD1 . TYR A 1 52  ? -9.406  -27.945 -2.155  1.00 13.65 ? 51   TYR A CD1 1 
ATOM   404  C  CD2 . TYR A 1 52  ? -8.956  -25.981 -0.873  1.00 14.12 ? 51   TYR A CD2 1 
ATOM   405  C  CE1 . TYR A 1 52  ? -9.924  -28.573 -1.024  1.00 15.36 ? 51   TYR A CE1 1 
ATOM   406  C  CE2 . TYR A 1 52  ? -9.473  -26.596 0.265   1.00 13.78 ? 51   TYR A CE2 1 
ATOM   407  C  CZ  . TYR A 1 52  ? -9.952  -27.884 0.184   1.00 15.96 ? 51   TYR A CZ  1 
ATOM   408  O  OH  . TYR A 1 52  ? -10.465 -28.487 1.315   1.00 14.77 ? 51   TYR A OH  1 
ATOM   409  N  N   . LEU A 1 53  ? -9.250  -22.972 -4.830  1.00 14.43 ? 52   LEU A N   1 
ATOM   410  C  CA  . LEU A 1 53  ? -8.753  -21.831 -5.594  1.00 14.50 ? 52   LEU A CA  1 
ATOM   411  C  C   . LEU A 1 53  ? -7.702  -21.050 -4.806  1.00 12.11 ? 52   LEU A C   1 
ATOM   412  O  O   . LEU A 1 53  ? -7.886  -20.757 -3.618  1.00 14.15 ? 52   LEU A O   1 
ATOM   413  C  CB  . LEU A 1 53  ? -9.897  -20.891 -5.970  1.00 14.91 ? 52   LEU A CB  1 
ATOM   414  C  CG  . LEU A 1 53  ? -11.098 -21.433 -6.736  1.00 16.42 ? 52   LEU A CG  1 
ATOM   415  C  CD1 . LEU A 1 53  ? -12.041 -20.279 -7.069  1.00 16.23 ? 52   LEU A CD1 1 
ATOM   416  C  CD2 . LEU A 1 53  ? -10.653 -22.168 -8.002  1.00 17.81 ? 52   LEU A CD2 1 
ATOM   417  N  N   . SER A 1 54  ? -6.620  -20.667 -5.494  1.00 13.19 ? 53   SER A N   1 
ATOM   418  C  CA  . SER A 1 54  ? -5.484  -20.004 -4.867  1.00 14.27 ? 53   SER A CA  1 
ATOM   419  C  C   . SER A 1 54  ? -5.025  -18.727 -5.564  1.00 14.33 ? 53   SER A C   1 
ATOM   420  O  O   . SER A 1 54  ? -4.162  -18.035 -5.011  1.00 16.24 ? 53   SER A O   1 
ATOM   421  C  CB  . SER A 1 54  ? -4.279  -20.963 -4.782  1.00 16.96 ? 53   SER A CB  1 
ATOM   422  O  OG  . SER A 1 54  ? -4.490  -21.992 -3.827  1.00 22.40 ? 53   SER A OG  1 
ATOM   423  N  N   . SER A 1 55  ? -5.545  -18.392 -6.743  1.00 15.09 ? 54   SER A N   1 
ATOM   424  C  CA  . SER A 1 55  ? -5.067  -17.227 -7.479  1.00 16.01 ? 54   SER A CA  1 
ATOM   425  C  C   . SER A 1 55  ? -6.115  -16.119 -7.477  1.00 14.83 ? 54   SER A C   1 
ATOM   426  O  O   . SER A 1 55  ? -7.321  -16.379 -7.451  1.00 14.71 ? 54   SER A O   1 
ATOM   427  C  CB  . SER A 1 55  ? -4.712  -17.587 -8.932  1.00 17.55 ? 54   SER A CB  1 
ATOM   428  O  OG  . SER A 1 55  ? -5.879  -17.887 -9.686  1.00 16.53 ? 54   SER A OG  1 
ATOM   429  N  N   . GLN A 1 56  ? -5.645  -14.868 -7.505  1.00 13.65 ? 55   GLN A N   1 
ATOM   430  C  CA  . GLN A 1 56  ? -6.583  -13.757 -7.620  1.00 14.05 ? 55   GLN A CA  1 
ATOM   431  C  C   . GLN A 1 56  ? -7.326  -13.805 -8.954  1.00 13.41 ? 55   GLN A C   1 
ATOM   432  O  O   . GLN A 1 56  ? -8.486  -13.380 -9.036  1.00 13.52 ? 55   GLN A O   1 
ATOM   433  C  CB  . GLN A 1 56  ? -5.842  -12.427 -7.435  1.00 14.50 ? 55   GLN A CB  1 
ATOM   434  C  CG  . GLN A 1 56  ? -6.712  -11.165 -7.489  1.00 13.59 ? 55   GLN A CG  1 
ATOM   435  C  CD  . GLN A 1 56  ? -6.811  -10.578 -8.891  1.00 13.36 ? 55   GLN A CD  1 
ATOM   436  O  OE1 . GLN A 1 56  ? -6.195  -11.077 -9.835  1.00 16.02 ? 55   GLN A OE1 1 
ATOM   437  N  NE2 . GLN A 1 56  ? -7.596  -9.509  -9.030  1.00 13.83 ? 55   GLN A NE2 1 
ATOM   438  N  N   . ARG A 1 57  ? -6.685  -14.347 -9.995  1.00 15.39 ? 56   ARG A N   1 
ATOM   439  C  CA  . ARG A 1 57  ? -7.318  -14.439 -11.307 1.00 15.42 ? 56   ARG A CA  1 
ATOM   440  C  C   . ARG A 1 57  ? -8.648  -15.180 -11.233 1.00 14.87 ? 56   ARG A C   1 
ATOM   441  O  O   . ARG A 1 57  ? -9.648  -14.744 -11.820 1.00 16.73 ? 56   ARG A O   1 
ATOM   442  C  CB  . ARG A 1 57  ? -6.365  -15.126 -12.294 1.00 18.18 ? 56   ARG A CB  1 
ATOM   443  C  CG  . ARG A 1 57  ? -6.940  -15.366 -13.690 1.00 24.66 ? 56   ARG A CG  1 
ATOM   444  C  CD  . ARG A 1 57  ? -5.973  -16.176 -14.572 1.00 28.59 ? 56   ARG A CD  1 
ATOM   445  N  NE  . ARG A 1 57  ? -6.179  -17.617 -14.468 1.00 29.99 ? 56   ARG A NE  1 
ATOM   446  C  CZ  . ARG A 1 57  ? -6.928  -18.330 -15.302 1.00 31.02 ? 56   ARG A CZ  1 
ATOM   447  N  NH1 . ARG A 1 57  ? -7.592  -17.763 -16.298 1.00 30.54 ? 56   ARG A NH1 1 
ATOM   448  N  NH2 . ARG A 1 57  ? -7.008  -19.649 -15.137 1.00 30.80 ? 56   ARG A NH2 1 
ATOM   449  N  N   . LEU A 1 58  ? -8.686  -16.307 -10.516 1.00 14.79 ? 57   LEU A N   1 
ATOM   450  C  CA  . LEU A 1 58  ? -9.930  -17.058 -10.405 1.00 15.35 ? 57   LEU A CA  1 
ATOM   451  C  C   . LEU A 1 58  ? -10.794 -16.591 -9.243  1.00 15.33 ? 57   LEU A C   1 
ATOM   452  O  O   . LEU A 1 58  ? -12.028 -16.604 -9.344  1.00 14.37 ? 57   LEU A O   1 
ATOM   453  C  CB  . LEU A 1 58  ? -9.635  -18.555 -10.263 1.00 14.92 ? 57   LEU A CB  1 
ATOM   454  C  CG  . LEU A 1 58  ? -8.910  -19.184 -11.466 1.00 14.97 ? 57   LEU A CG  1 
ATOM   455  C  CD1 . LEU A 1 58  ? -8.578  -20.650 -11.197 1.00 18.14 ? 57   LEU A CD1 1 
ATOM   456  C  CD2 . LEU A 1 58  ? -9.739  -19.039 -12.753 1.00 17.46 ? 57   LEU A CD2 1 
ATOM   457  N  N   . ILE A 1 59  ? -10.187 -16.171 -8.138  1.00 13.60 ? 58   ILE A N   1 
ATOM   458  C  CA  . ILE A 1 59  ? -11.007 -15.824 -6.982  1.00 13.43 ? 58   ILE A CA  1 
ATOM   459  C  C   . ILE A 1 59  ? -11.809 -14.544 -7.244  1.00 13.46 ? 58   ILE A C   1 
ATOM   460  O  O   . ILE A 1 59  ? -12.925 -14.390 -6.730  1.00 14.86 ? 58   ILE A O   1 
ATOM   461  C  CB  . ILE A 1 59  ? -10.110 -15.746 -5.732  1.00 11.60 ? 58   ILE A CB  1 
ATOM   462  C  CG1 . ILE A 1 59  ? -9.729  -17.179 -5.317  1.00 14.27 ? 58   ILE A CG1 1 
ATOM   463  C  CG2 . ILE A 1 59  ? -10.821 -15.002 -4.588  1.00 13.05 ? 58   ILE A CG2 1 
ATOM   464  C  CD1 . ILE A 1 59  ? -8.503  -17.286 -4.399  1.00 15.38 ? 58   ILE A CD1 1 
ATOM   465  N  N   . LYS A 1 60  ? -11.298 -13.628 -8.081  1.00 13.61 ? 59   LYS A N   1 
ATOM   466  C  CA  . LYS A 1 60  ? -12.082 -12.433 -8.381  1.00 14.57 ? 59   LYS A CA  1 
ATOM   467  C  C   . LYS A 1 60  ? -13.390 -12.785 -9.089  1.00 14.70 ? 59   LYS A C   1 
ATOM   468  O  O   . LYS A 1 60  ? -14.387 -12.068 -8.939  1.00 18.02 ? 59   LYS A O   1 
ATOM   469  C  CB  . LYS A 1 60  ? -11.266 -11.431 -9.211  1.00 13.29 ? 59   LYS A CB  1 
ATOM   470  C  CG  . LYS A 1 60  ? -10.977 -11.838 -10.648 1.00 14.30 ? 59   LYS A CG  1 
ATOM   471  C  CD  . LYS A 1 60  ? -9.973  -10.873 -11.304 1.00 16.83 ? 59   LYS A CD  1 
ATOM   472  C  CE  . LYS A 1 60  ? -9.577  -11.347 -12.697 1.00 20.62 ? 59   LYS A CE  1 
ATOM   473  N  NZ  . LYS A 1 60  ? -8.580  -10.449 -13.361 1.00 24.66 ? 59   LYS A NZ  1 
ATOM   474  N  N   . GLU A 1 61  ? -13.408 -13.880 -9.858  1.00 15.27 ? 60   GLU A N   1 
ATOM   475  C  CA  . GLU A 1 61  ? -14.658 -14.359 -10.448 1.00 14.40 ? 60   GLU A CA  1 
ATOM   476  C  C   . GLU A 1 61  ? -15.526 -15.066 -9.413  1.00 14.05 ? 60   GLU A C   1 
ATOM   477  O  O   . GLU A 1 61  ? -16.752 -14.895 -9.402  1.00 15.22 ? 60   GLU A O   1 
ATOM   478  C  CB  . GLU A 1 61  ? -14.370 -15.295 -11.632 1.00 14.52 ? 60   GLU A CB  1 
ATOM   479  C  CG  . GLU A 1 61  ? -13.612 -14.629 -12.766 1.00 17.16 ? 60   GLU A CG  1 
ATOM   480  C  CD  . GLU A 1 61  ? -13.624 -15.436 -14.065 1.00 22.68 ? 60   GLU A CD  1 
ATOM   481  O  OE1 . GLU A 1 61  ? -14.530 -16.274 -14.259 1.00 23.04 ? 60   GLU A OE1 1 
ATOM   482  O  OE2 . GLU A 1 61  ? -12.725 -15.216 -14.903 1.00 25.91 ? 60   GLU A OE2 1 
ATOM   483  N  N   . ALA A 1 62  ? -14.910 -15.871 -8.539  1.00 14.12 ? 61   ALA A N   1 
ATOM   484  C  CA  . ALA A 1 62  ? -15.674 -16.547 -7.499  1.00 13.98 ? 61   ALA A CA  1 
ATOM   485  C  C   . ALA A 1 62  ? -16.416 -15.559 -6.601  1.00 13.97 ? 61   ALA A C   1 
ATOM   486  O  O   . ALA A 1 62  ? -17.451 -15.910 -6.017  1.00 16.71 ? 61   ALA A O   1 
ATOM   487  C  CB  . ALA A 1 62  ? -14.742 -17.433 -6.663  1.00 15.48 ? 61   ALA A CB  1 
ATOM   488  N  N   . CYS A 1 63  ? -15.910 -14.331 -6.472  1.00 13.07 ? 62   CYS A N   1 
ATOM   489  C  CA  . CYS A 1 63  ? -16.511 -13.329 -5.592  1.00 12.38 ? 62   CYS A CA  1 
ATOM   490  C  C   . CYS A 1 63  ? -17.669 -12.575 -6.234  1.00 11.09 ? 62   CYS A C   1 
ATOM   491  O  O   . CYS A 1 63  ? -18.204 -11.645 -5.613  1.00 12.29 ? 62   CYS A O   1 
ATOM   492  C  CB  . CYS A 1 63  ? -15.435 -12.350 -5.115  1.00 13.25 ? 62   CYS A CB  1 
ATOM   493  S  SG  . CYS A 1 63  ? -14.306 -13.084 -3.873  1.00 14.51 ? 62   CYS A SG  1 
ATOM   494  N  N   . ASP A 1 64  ? -18.056 -12.936 -7.458  1.00 13.61 ? 63   ASP A N   1 
ATOM   495  C  CA  . ASP A 1 64  ? -19.208 -12.351 -8.136  1.00 15.32 ? 63   ASP A CA  1 
ATOM   496  C  C   . ASP A 1 64  ? -20.478 -12.938 -7.526  1.00 13.89 ? 63   ASP A C   1 
ATOM   497  O  O   . ASP A 1 64  ? -20.812 -14.103 -7.774  1.00 16.44 ? 63   ASP A O   1 
ATOM   498  C  CB  . ASP A 1 64  ? -19.097 -12.643 -9.632  1.00 17.02 ? 63   ASP A CB  1 
ATOM   499  C  CG  . ASP A 1 64  ? -20.272 -12.117 -10.445 1.00 20.04 ? 63   ASP A CG  1 
ATOM   500  O  OD1 . ASP A 1 64  ? -21.297 -11.694 -9.876  1.00 20.69 ? 63   ASP A OD1 1 
ATOM   501  O  OD2 . ASP A 1 64  ? -20.154 -12.134 -11.687 1.00 23.57 ? 63   ASP A OD2 1 
ATOM   502  N  N   . GLU A 1 65  ? -21.185 -12.141 -6.715  1.00 12.43 ? 64   GLU A N   1 
ATOM   503  C  CA  . GLU A 1 65  ? -22.349 -12.657 -5.995  1.00 13.30 ? 64   GLU A CA  1 
ATOM   504  C  C   . GLU A 1 65  ? -23.501 -13.027 -6.917  1.00 15.80 ? 64   GLU A C   1 
ATOM   505  O  O   . GLU A 1 65  ? -24.440 -13.706 -6.478  1.00 17.14 ? 64   GLU A O   1 
ATOM   506  C  CB  . GLU A 1 65  ? -22.835 -11.637 -4.966  1.00 16.39 ? 64   GLU A CB  1 
ATOM   507  C  CG  . GLU A 1 65  ? -21.816 -11.303 -3.906  1.00 15.45 ? 64   GLU A CG  1 
ATOM   508  C  CD  . GLU A 1 65  ? -22.349 -10.320 -2.896  1.00 18.06 ? 64   GLU A CD  1 
ATOM   509  O  OE1 . GLU A 1 65  ? -22.289 -9.098  -3.162  1.00 22.32 ? 64   GLU A OE1 1 
ATOM   510  O  OE2 . GLU A 1 65  ? -22.846 -10.770 -1.843  1.00 15.53 ? 64   GLU A OE2 1 
ATOM   511  N  N   . SER A 1 66  ? -23.475 -12.583 -8.171  1.00 15.79 ? 65   SER A N   1 
ATOM   512  C  CA  . SER A 1 66  ? -24.525 -13.006 -9.082  1.00 17.01 ? 65   SER A CA  1 
ATOM   513  C  C   . SER A 1 66  ? -24.299 -14.425 -9.571  1.00 18.11 ? 65   SER A C   1 
ATOM   514  O  O   . SER A 1 66  ? -25.239 -15.055 -10.061 1.00 21.22 ? 65   SER A O   1 
ATOM   515  C  CB  . SER A 1 66  ? -24.635 -12.037 -10.269 1.00 18.12 ? 65   SER A CB  1 
ATOM   516  O  OG  . SER A 1 66  ? -23.570 -12.203 -11.192 1.00 20.26 ? 65   SER A OG  1 
ATOM   517  N  N   . ARG A 1 67  ? -23.081 -14.945 -9.420  1.00 16.70 ? 66   ARG A N   1 
ATOM   518  C  CA  . ARG A 1 67  ? -22.718 -16.272 -9.899  1.00 17.26 ? 66   ARG A CA  1 
ATOM   519  C  C   . ARG A 1 67  ? -22.498 -17.286 -8.789  1.00 16.37 ? 66   ARG A C   1 
ATOM   520  O  O   . ARG A 1 67  ? -22.722 -18.475 -9.015  1.00 17.45 ? 66   ARG A O   1 
ATOM   521  C  CB  . ARG A 1 67  ? -21.443 -16.203 -10.754 1.00 18.30 ? 66   ARG A CB  1 
ATOM   522  C  CG  . ARG A 1 67  ? -21.573 -15.391 -12.040 1.00 19.66 ? 66   ARG A CG  1 
ATOM   523  C  CD  . ARG A 1 67  ? -20.194 -15.020 -12.629 1.00 22.48 ? 66   ARG A CD  1 
ATOM   524  N  NE  . ARG A 1 67  ? -19.484 -16.170 -13.170 1.00 24.96 ? 66   ARG A NE  1 
ATOM   525  C  CZ  . ARG A 1 67  ? -18.212 -16.155 -13.551 1.00 26.67 ? 66   ARG A CZ  1 
ATOM   526  N  NH1 . ARG A 1 67  ? -17.458 -15.072 -13.408 1.00 24.55 ? 66   ARG A NH1 1 
ATOM   527  N  NH2 . ARG A 1 67  ? -17.683 -17.252 -14.088 1.00 28.13 ? 66   ARG A NH2 1 
ATOM   528  N  N   . PHE A 1 68  ? -22.061 -16.851 -7.604  1.00 15.12 ? 67   PHE A N   1 
ATOM   529  C  CA  . PHE A 1 68  ? -21.706 -17.754 -6.517  1.00 13.61 ? 67   PHE A CA  1 
ATOM   530  C  C   . PHE A 1 68  ? -22.250 -17.229 -5.194  1.00 13.23 ? 67   PHE A C   1 
ATOM   531  O  O   . PHE A 1 68  ? -22.204 -16.026 -4.926  1.00 14.68 ? 67   PHE A O   1 
ATOM   532  C  CB  . PHE A 1 68  ? -20.184 -17.922 -6.413  1.00 13.53 ? 67   PHE A CB  1 
ATOM   533  C  CG  . PHE A 1 68  ? -19.551 -18.476 -7.655  1.00 15.26 ? 67   PHE A CG  1 
ATOM   534  C  CD1 . PHE A 1 68  ? -19.456 -19.842 -7.844  1.00 17.42 ? 67   PHE A CD1 1 
ATOM   535  C  CD2 . PHE A 1 68  ? -19.056 -17.630 -8.630  1.00 16.55 ? 67   PHE A CD2 1 
ATOM   536  C  CE1 . PHE A 1 68  ? -18.885 -20.361 -8.989  1.00 17.79 ? 67   PHE A CE1 1 
ATOM   537  C  CE2 . PHE A 1 68  ? -18.482 -18.137 -9.779  1.00 16.32 ? 67   PHE A CE2 1 
ATOM   538  C  CZ  . PHE A 1 68  ? -18.393 -19.504 -9.961  1.00 18.42 ? 67   PHE A CZ  1 
ATOM   539  N  N   . ASP A 1 69  ? -22.756 -18.140 -4.367  1.00 12.50 ? 68   ASP A N   1 
ATOM   540  C  CA  . ASP A 1 69  ? -23.262 -17.821 -3.037  1.00 13.40 ? 68   ASP A CA  1 
ATOM   541  C  C   . ASP A 1 69  ? -22.444 -18.592 -1.997  1.00 13.49 ? 68   ASP A C   1 
ATOM   542  O  O   . ASP A 1 69  ? -21.746 -19.564 -2.318  1.00 13.00 ? 68   ASP A O   1 
ATOM   543  C  CB  . ASP A 1 69  ? -24.768 -18.168 -2.964  1.00 14.29 ? 68   ASP A CB  1 
ATOM   544  C  CG  . ASP A 1 69  ? -25.410 -17.876 -1.611  1.00 13.31 ? 68   ASP A CG  1 
ATOM   545  O  OD1 . ASP A 1 69  ? -24.994 -16.944 -0.887  1.00 13.60 ? 68   ASP A OD1 1 
ATOM   546  O  OD2 . ASP A 1 69  ? -26.371 -18.605 -1.286  1.00 14.37 ? 68   ASP A OD2 1 
ATOM   547  N  N   . LYS A 1 70  ? -22.505 -18.131 -0.747  1.00 11.17 ? 69   LYS A N   1 
ATOM   548  C  CA  . LYS A 1 70  ? -21.813 -18.825 0.343   1.00 9.95  ? 69   LYS A CA  1 
ATOM   549  C  C   . LYS A 1 70  ? -22.295 -20.271 0.481   1.00 11.79 ? 69   LYS A C   1 
ATOM   550  O  O   . LYS A 1 70  ? -23.498 -20.535 0.526   1.00 14.12 ? 69   LYS A O   1 
ATOM   551  C  CB  . LYS A 1 70  ? -22.020 -18.094 1.677   1.00 9.41  ? 69   LYS A CB  1 
ATOM   552  C  CG  . LYS A 1 70  ? -21.669 -18.965 2.891   1.00 10.11 ? 69   LYS A CG  1 
ATOM   553  C  CD  . LYS A 1 70  ? -21.338 -18.143 4.147   1.00 12.03 ? 69   LYS A CD  1 
ATOM   554  C  CE  . LYS A 1 70  ? -21.259 -19.053 5.391   1.00 10.23 ? 69   LYS A CE  1 
ATOM   555  N  NZ  . LYS A 1 70  ? -20.510 -18.423 6.524   1.00 8.98  ? 69   LYS A NZ  1 
ATOM   556  N  N   . ASN A 1 71  ? -21.348 -21.203 0.571   1.00 10.15 ? 70   ASN A N   1 
ATOM   557  C  CA  . ASN A 1 71  ? -21.613 -22.606 0.855   1.00 12.12 ? 70   ASN A CA  1 
ATOM   558  C  C   . ASN A 1 71  ? -21.160 -22.937 2.275   1.00 13.26 ? 70   ASN A C   1 
ATOM   559  O  O   . ASN A 1 71  ? -20.215 -22.338 2.791   1.00 14.42 ? 70   ASN A O   1 
ATOM   560  C  CB  . ASN A 1 71  ? -20.888 -23.503 -0.159  1.00 12.01 ? 70   ASN A CB  1 
ATOM   561  C  CG  . ASN A 1 71  ? -21.132 -24.978 0.073   1.00 14.84 ? 70   ASN A CG  1 
ATOM   562  O  OD1 . ASN A 1 71  ? -22.277 -25.442 0.059   1.00 16.74 ? 70   ASN A OD1 1 
ATOM   563  N  ND2 . ASN A 1 71  ? -20.048 -25.740 0.244   1.00 15.88 ? 70   ASN A ND2 1 
ATOM   564  N  N   . LEU A 1 72  ? -21.846 -23.881 2.919   1.00 13.33 ? 71   LEU A N   1 
ATOM   565  C  CA  . LEU A 1 72  ? -21.364 -24.411 4.196   1.00 12.06 ? 71   LEU A CA  1 
ATOM   566  C  C   . LEU A 1 72  ? -20.361 -25.519 3.901   1.00 12.18 ? 71   LEU A C   1 
ATOM   567  O  O   . LEU A 1 72  ? -20.731 -26.583 3.395   1.00 15.81 ? 71   LEU A O   1 
ATOM   568  C  CB  . LEU A 1 72  ? -22.511 -24.931 5.060   1.00 12.26 ? 71   LEU A CB  1 
ATOM   569  C  CG  . LEU A 1 72  ? -23.626 -23.951 5.453   1.00 12.90 ? 71   LEU A CG  1 
ATOM   570  C  CD1 . LEU A 1 72  ? -24.532 -24.588 6.483   1.00 14.07 ? 71   LEU A CD1 1 
ATOM   571  C  CD2 . LEU A 1 72  ? -23.078 -22.617 5.974   1.00 14.50 ? 71   LEU A CD2 1 
ATOM   572  N  N   . SER A 1 73  ? -19.090 -25.267 4.197   1.00 12.73 ? 72   SER A N   1 
ATOM   573  C  CA  . SER A 1 73  ? -18.089 -26.322 4.166   1.00 12.82 ? 72   SER A CA  1 
ATOM   574  C  C   . SER A 1 73  ? -18.452 -27.418 5.168   1.00 13.42 ? 72   SER A C   1 
ATOM   575  O  O   . SER A 1 73  ? -19.317 -27.249 6.034   1.00 14.92 ? 72   SER A O   1 
ATOM   576  C  CB  . SER A 1 73  ? -16.715 -25.752 4.500   1.00 15.37 ? 72   SER A CB  1 
ATOM   577  O  OG  . SER A 1 73  ? -16.767 -25.072 5.744   1.00 13.47 ? 72   SER A OG  1 
ATOM   578  N  N   . GLN A 1 74  ? -17.784 -28.565 5.045   1.00 12.64 ? 73   GLN A N   1 
ATOM   579  C  CA  . GLN A 1 74  ? -18.007 -29.605 6.045   1.00 15.84 ? 73   GLN A CA  1 
ATOM   580  C  C   . GLN A 1 74  ? -17.709 -29.075 7.442   1.00 14.51 ? 73   GLN A C   1 
ATOM   581  O  O   . GLN A 1 74  ? -18.431 -29.378 8.403   1.00 15.64 ? 73   GLN A O   1 
ATOM   582  C  CB  . GLN A 1 74  ? -17.151 -30.836 5.753   1.00 18.69 ? 73   GLN A CB  1 
ATOM   583  C  CG  . GLN A 1 74  ? -17.626 -32.074 6.502   1.00 23.42 ? 73   GLN A CG  1 
ATOM   584  C  CD  . GLN A 1 74  ? -19.086 -32.380 6.211   1.00 26.33 ? 73   GLN A CD  1 
ATOM   585  O  OE1 . GLN A 1 74  ? -19.475 -32.568 5.056   1.00 28.38 ? 73   GLN A OE1 1 
ATOM   586  N  NE2 . GLN A 1 74  ? -19.906 -32.402 7.256   1.00 27.33 ? 73   GLN A NE2 1 
ATOM   587  N  N   . ALA A 1 75  ? -16.653 -28.267 7.565   1.00 14.13 ? 74   ALA A N   1 
ATOM   588  C  CA  . ALA A 1 75  ? -16.298 -27.689 8.855   1.00 13.84 ? 74   ALA A CA  1 
ATOM   589  C  C   . ALA A 1 75  ? -17.453 -26.877 9.432   1.00 13.53 ? 74   ALA A C   1 
ATOM   590  O  O   . ALA A 1 75  ? -17.803 -27.025 10.609  1.00 14.96 ? 74   ALA A O   1 
ATOM   591  C  CB  . ALA A 1 75  ? -15.045 -26.823 8.712   1.00 15.43 ? 74   ALA A CB  1 
ATOM   592  N  N   . LEU A 1 76  ? -18.058 -26.004 8.619   1.00 12.01 ? 75   LEU A N   1 
ATOM   593  C  CA  . LEU A 1 76  ? -19.173 -25.214 9.130   1.00 13.36 ? 75   LEU A CA  1 
ATOM   594  C  C   . LEU A 1 76  ? -20.398 -26.077 9.412   1.00 12.95 ? 75   LEU A C   1 
ATOM   595  O  O   . LEU A 1 76  ? -21.164 -25.769 10.334  1.00 14.83 ? 75   LEU A O   1 
ATOM   596  C  CB  . LEU A 1 76  ? -19.525 -24.076 8.164   1.00 13.83 ? 75   LEU A CB  1 
ATOM   597  C  CG  . LEU A 1 76  ? -18.519 -22.917 8.029   1.00 12.96 ? 75   LEU A CG  1 
ATOM   598  C  CD1 . LEU A 1 76  ? -19.036 -21.849 7.058   1.00 13.45 ? 75   LEU A CD1 1 
ATOM   599  C  CD2 . LEU A 1 76  ? -18.201 -22.279 9.381   1.00 14.87 ? 75   LEU A CD2 1 
ATOM   600  N  N   . LYS A 1 77  ? -20.619 -27.147 8.638   1.00 13.55 ? 76   LYS A N   1 
ATOM   601  C  CA  . LYS A 1 77  ? -21.717 -28.053 8.973   1.00 14.26 ? 76   LYS A CA  1 
ATOM   602  C  C   . LYS A 1 77  ? -21.507 -28.691 10.342  1.00 14.55 ? 76   LYS A C   1 
ATOM   603  O  O   . LYS A 1 77  ? -22.471 -28.914 11.086  1.00 16.03 ? 76   LYS A O   1 
ATOM   604  C  CB  . LYS A 1 77  ? -21.882 -29.125 7.894   1.00 16.21 ? 76   LYS A CB  1 
ATOM   605  C  CG  . LYS A 1 77  ? -22.459 -28.574 6.604   1.00 15.92 ? 76   LYS A CG  1 
ATOM   606  C  CD  . LYS A 1 77  ? -22.549 -29.634 5.531   1.00 20.80 ? 76   LYS A CD  1 
ATOM   607  C  CE  . LYS A 1 77  ? -22.938 -29.015 4.194   1.00 24.08 ? 76   LYS A CE  1 
ATOM   608  N  NZ  . LYS A 1 77  ? -23.107 -30.053 3.158   1.00 30.95 ? 76   LYS A NZ  1 
ATOM   609  N  N   . PHE A 1 78  ? -20.255 -28.991 10.697  1.00 14.47 ? 77   PHE A N   1 
ATOM   610  C  CA  . PHE A 1 78  ? -19.998 -29.562 12.017  1.00 17.04 ? 77   PHE A CA  1 
ATOM   611  C  C   . PHE A 1 78  ? -20.157 -28.508 13.108  1.00 17.31 ? 77   PHE A C   1 
ATOM   612  O  O   . PHE A 1 78  ? -20.718 -28.790 14.176  1.00 17.67 ? 77   PHE A O   1 
ATOM   613  C  CB  . PHE A 1 78  ? -18.603 -30.194 12.060  1.00 20.89 ? 77   PHE A CB  1 
ATOM   614  C  CG  . PHE A 1 78  ? -18.476 -31.461 11.251  1.00 24.11 ? 77   PHE A CG  1 
ATOM   615  C  CD1 . PHE A 1 78  ? -19.593 -32.229 10.945  1.00 25.20 ? 77   PHE A CD1 1 
ATOM   616  C  CD2 . PHE A 1 78  ? -17.230 -31.896 10.808  1.00 22.74 ? 77   PHE A CD2 1 
ATOM   617  C  CE1 . PHE A 1 78  ? -19.472 -33.400 10.213  1.00 28.57 ? 77   PHE A CE1 1 
ATOM   618  C  CE2 . PHE A 1 78  ? -17.106 -33.065 10.071  1.00 26.72 ? 77   PHE A CE2 1 
ATOM   619  C  CZ  . PHE A 1 78  ? -18.228 -33.817 9.774   1.00 28.00 ? 77   PHE A CZ  1 
ATOM   620  N  N   . VAL A 1 79  ? -19.684 -27.283 12.855  1.00 15.05 ? 78   VAL A N   1 
ATOM   621  C  CA  . VAL A 1 79  ? -19.888 -26.191 13.810  1.00 14.42 ? 78   VAL A CA  1 
ATOM   622  C  C   . VAL A 1 79  ? -21.370 -25.917 14.012  1.00 14.18 ? 78   VAL A C   1 
ATOM   623  O  O   . VAL A 1 79  ? -21.801 -25.539 15.113  1.00 16.42 ? 78   VAL A O   1 
ATOM   624  C  CB  . VAL A 1 79  ? -19.141 -24.924 13.345  1.00 13.69 ? 78   VAL A CB  1 
ATOM   625  C  CG1 . VAL A 1 79  ? -19.501 -23.720 14.233  1.00 18.34 ? 78   VAL A CG1 1 
ATOM   626  C  CG2 . VAL A 1 79  ? -17.631 -25.168 13.343  1.00 15.06 ? 78   VAL A CG2 1 
ATOM   627  N  N   . ARG A 1 80  ? -22.176 -26.099 12.963  1.00 15.13 ? 79   ARG A N   1 
ATOM   628  C  CA  . ARG A 1 80  ? -23.613 -25.882 13.077  1.00 15.11 ? 79   ARG A CA  1 
ATOM   629  C  C   . ARG A 1 80  ? -24.258 -26.799 14.111  1.00 16.52 ? 79   ARG A C   1 
ATOM   630  O  O   . ARG A 1 80  ? -25.348 -26.489 14.601  1.00 16.36 ? 79   ARG A O   1 
ATOM   631  C  CB  . ARG A 1 80  ? -24.276 -26.075 11.708  1.00 16.84 ? 79   ARG A CB  1 
ATOM   632  C  CG  . ARG A 1 80  ? -25.774 -25.827 11.709  1.00 15.92 ? 79   ARG A CG  1 
ATOM   633  C  CD  . ARG A 1 80  ? -26.311 -25.505 10.317  1.00 15.92 ? 79   ARG A CD  1 
ATOM   634  N  NE  . ARG A 1 80  ? -27.772 -25.466 10.307  1.00 18.34 ? 79   ARG A NE  1 
ATOM   635  C  CZ  . ARG A 1 80  ? -28.510 -24.633 9.582   1.00 17.49 ? 79   ARG A CZ  1 
ATOM   636  N  NH1 . ARG A 1 80  ? -27.960 -23.689 8.827   1.00 14.93 ? 79   ARG A NH1 1 
ATOM   637  N  NH2 . ARG A 1 80  ? -29.837 -24.730 9.638   1.00 17.75 ? 79   ARG A NH2 1 
ATOM   638  N  N   . ASP A 1 81  ? -23.615 -27.915 14.461  1.00 16.67 ? 80   ASP A N   1 
ATOM   639  C  CA  . ASP A 1 81  ? -24.158 -28.759 15.519  1.00 20.54 ? 80   ASP A CA  1 
ATOM   640  C  C   . ASP A 1 81  ? -24.306 -28.003 16.837  1.00 20.37 ? 80   ASP A C   1 
ATOM   641  O  O   . ASP A 1 81  ? -25.150 -28.379 17.663  1.00 24.70 ? 80   ASP A O   1 
ATOM   642  C  CB  . ASP A 1 81  ? -23.296 -30.008 15.705  1.00 21.38 ? 80   ASP A CB  1 
ATOM   643  C  CG  . ASP A 1 81  ? -23.548 -31.054 14.625  1.00 26.37 ? 80   ASP A CG  1 
ATOM   644  O  OD1 . ASP A 1 81  ? -24.633 -31.028 14.009  1.00 27.85 ? 80   ASP A OD1 1 
ATOM   645  O  OD2 . ASP A 1 81  ? -22.661 -31.906 14.393  1.00 31.90 ? 80   ASP A OD2 1 
ATOM   646  N  N   . PHE A 1 82  ? -23.521 -26.942 17.064  1.00 18.89 ? 81   PHE A N   1 
ATOM   647  C  CA  . PHE A 1 82  ? -23.768 -26.089 18.219  1.00 17.25 ? 81   PHE A CA  1 
ATOM   648  C  C   . PHE A 1 82  ? -24.071 -24.631 17.884  1.00 17.82 ? 81   PHE A C   1 
ATOM   649  O  O   . PHE A 1 82  ? -24.665 -23.949 18.724  1.00 18.57 ? 81   PHE A O   1 
ATOM   650  C  CB  . PHE A 1 82  ? -22.605 -26.154 19.236  1.00 19.01 ? 81   PHE A CB  1 
ATOM   651  C  CG  . PHE A 1 82  ? -21.226 -25.976 18.647  1.00 19.79 ? 81   PHE A CG  1 
ATOM   652  C  CD1 . PHE A 1 82  ? -20.644 -24.719 18.568  1.00 21.43 ? 81   PHE A CD1 1 
ATOM   653  C  CD2 . PHE A 1 82  ? -20.490 -27.077 18.224  1.00 20.76 ? 81   PHE A CD2 1 
ATOM   654  C  CE1 . PHE A 1 82  ? -19.366 -24.557 18.039  1.00 22.67 ? 81   PHE A CE1 1 
ATOM   655  C  CE2 . PHE A 1 82  ? -19.212 -26.922 17.694  1.00 22.82 ? 81   PHE A CE2 1 
ATOM   656  C  CZ  . PHE A 1 82  ? -18.649 -25.663 17.607  1.00 22.62 ? 81   PHE A CZ  1 
ATOM   657  N  N   . ALA A 1 83  ? -23.751 -24.148 16.677  1.00 17.11 ? 82   ALA A N   1 
ATOM   658  C  CA  . ALA A 1 83  ? -24.081 -22.774 16.300  1.00 15.35 ? 82   ALA A CA  1 
ATOM   659  C  C   . ALA A 1 83  ? -25.372 -22.654 15.486  1.00 15.63 ? 82   ALA A C   1 
ATOM   660  O  O   . ALA A 1 83  ? -25.804 -21.527 15.200  1.00 15.23 ? 82   ALA A O   1 
ATOM   661  C  CB  . ALA A 1 83  ? -22.921 -22.140 15.522  1.00 16.44 ? 82   ALA A CB  1 
ATOM   662  N  N   . GLY A 1 84  ? -25.989 -23.775 15.114  1.00 15.64 ? 83   GLY A N   1 
ATOM   663  C  CA  . GLY A 1 84  ? -27.326 -23.764 14.530  1.00 15.52 ? 83   GLY A CA  1 
ATOM   664  C  C   . GLY A 1 84  ? -27.431 -22.841 13.340  1.00 14.32 ? 83   GLY A C   1 
ATOM   665  O  O   . GLY A 1 84  ? -26.528 -22.780 12.497  1.00 16.06 ? 83   GLY A O   1 
ATOM   666  N  N   . ASP A 1 85  ? -28.549 -22.115 13.251  1.00 15.51 ? 84   ASP A N   1 
ATOM   667  C  CA  . ASP A 1 85  ? -28.730 -21.126 12.184  1.00 13.97 ? 84   ASP A CA  1 
ATOM   668  C  C   . ASP A 1 85  ? -28.411 -19.707 12.658  1.00 15.24 ? 84   ASP A C   1 
ATOM   669  O  O   . ASP A 1 85  ? -29.059 -18.736 12.250  1.00 13.89 ? 84   ASP A O   1 
ATOM   670  C  CB  . ASP A 1 85  ? -30.135 -21.217 11.562  1.00 14.37 ? 84   ASP A CB  1 
ATOM   671  C  CG  . ASP A 1 85  ? -31.279 -21.007 12.567  1.00 16.37 ? 84   ASP A CG  1 
ATOM   672  O  OD1 . ASP A 1 85  ? -31.039 -20.896 13.787  1.00 16.61 ? 84   ASP A OD1 1 
ATOM   673  O  OD2 . ASP A 1 85  ? -32.450 -20.950 12.112  1.00 18.93 ? 84   ASP A OD2 1 
ATOM   674  N  N   . GLY A 1 86  ? -27.400 -19.565 13.521  1.00 14.18 ? 85   GLY A N   1 
ATOM   675  C  CA  . GLY A 1 86  ? -26.752 -18.277 13.720  1.00 13.03 ? 85   GLY A CA  1 
ATOM   676  C  C   . GLY A 1 86  ? -26.162 -17.744 12.417  1.00 11.86 ? 85   GLY A C   1 
ATOM   677  O  O   . GLY A 1 86  ? -26.156 -18.409 11.381  1.00 12.97 ? 85   GLY A O   1 
ATOM   678  N  N   . LEU A 1 87  ? -25.651 -16.506 12.480  1.00 10.00 ? 86   LEU A N   1 
ATOM   679  C  CA  . LEU A 1 87  ? -25.279 -15.801 11.250  1.00 11.62 ? 86   LEU A CA  1 
ATOM   680  C  C   . LEU A 1 87  ? -24.218 -16.546 10.452  1.00 12.95 ? 86   LEU A C   1 
ATOM   681  O  O   . LEU A 1 87  ? -24.262 -16.548 9.217   1.00 14.66 ? 86   LEU A O   1 
ATOM   682  C  CB  . LEU A 1 87  ? -24.793 -14.381 11.561  1.00 10.48 ? 86   LEU A CB  1 
ATOM   683  C  CG  . LEU A 1 87  ? -25.881 -13.329 11.784  1.00 12.42 ? 86   LEU A CG  1 
ATOM   684  C  CD1 . LEU A 1 87  ? -25.246 -12.009 12.225  1.00 14.10 ? 86   LEU A CD1 1 
ATOM   685  C  CD2 . LEU A 1 87  ? -26.726 -13.120 10.515  1.00 11.89 ? 86   LEU A CD2 1 
ATOM   686  N  N   . ALA A 1 88  ? -23.228 -17.147 11.126  1.00 12.40 ? 87   ALA A N   1 
ATOM   687  C  CA  . ALA A 1 88  ? -22.083 -17.697 10.410  1.00 11.02 ? 87   ALA A CA  1 
ATOM   688  C  C   . ALA A 1 88  ? -22.357 -19.067 9.802   1.00 11.85 ? 87   ALA A C   1 
ATOM   689  O  O   . ALA A 1 88  ? -21.684 -19.449 8.840   1.00 13.23 ? 87   ALA A O   1 
ATOM   690  C  CB  . ALA A 1 88  ? -20.863 -17.803 11.339  1.00 10.78 ? 87   ALA A CB  1 
ATOM   691  N  N   . THR A 1 89  ? -23.318 -19.818 10.336  1.00 11.50 ? 88   THR A N   1 
ATOM   692  C  CA  . THR A 1 89  ? -23.571 -21.174 9.862   1.00 11.30 ? 88   THR A CA  1 
ATOM   693  C  C   . THR A 1 89  ? -24.948 -21.333 9.214   1.00 12.07 ? 88   THR A C   1 
ATOM   694  O  O   . THR A 1 89  ? -25.403 -22.463 9.001   1.00 14.37 ? 88   THR A O   1 
ATOM   695  C  CB  . THR A 1 89  ? -23.384 -22.182 11.003  1.00 14.21 ? 88   THR A CB  1 
ATOM   696  O  OG1 . THR A 1 89  ? -24.114 -21.762 12.165  1.00 14.20 ? 88   THR A OG1 1 
ATOM   697  C  CG2 . THR A 1 89  ? -21.911 -22.303 11.360  1.00 12.29 ? 88   THR A CG2 1 
ATOM   698  N  N   . SER A 1 90  ? -25.611 -20.239 8.862   1.00 11.74 ? 89   SER A N   1 
ATOM   699  C  CA  . SER A 1 90  ? -26.865 -20.320 8.126   1.00 13.75 ? 89   SER A CA  1 
ATOM   700  C  C   . SER A 1 90  ? -26.637 -20.133 6.621   1.00 11.58 ? 89   SER A C   1 
ATOM   701  O  O   . SER A 1 90  ? -25.695 -19.458 6.192   1.00 12.56 ? 89   SER A O   1 
ATOM   702  C  CB  . SER A 1 90  ? -27.853 -19.277 8.656   1.00 16.95 ? 89   SER A CB  1 
ATOM   703  O  OG  . SER A 1 90  ? -27.259 -17.994 8.675   1.00 22.72 ? 89   SER A OG  1 
ATOM   704  N  N   . TRP A 1 91  ? -27.513 -20.741 5.821   1.00 13.55 ? 90   TRP A N   1 
ATOM   705  C  CA  . TRP A 1 91  ? -27.502 -20.496 4.381   1.00 12.93 ? 90   TRP A CA  1 
ATOM   706  C  C   . TRP A 1 91  ? -28.132 -19.136 4.085   1.00 12.63 ? 90   TRP A C   1 
ATOM   707  O  O   . TRP A 1 91  ? -29.023 -18.671 4.804   1.00 13.01 ? 90   TRP A O   1 
ATOM   708  C  CB  . TRP A 1 91  ? -28.265 -21.589 3.619   1.00 12.43 ? 90   TRP A CB  1 
ATOM   709  C  CG  . TRP A 1 91  ? -27.756 -22.991 3.810   1.00 15.12 ? 90   TRP A CG  1 
ATOM   710  C  CD1 . TRP A 1 91  ? -28.165 -23.892 4.761   1.00 15.02 ? 90   TRP A CD1 1 
ATOM   711  C  CD2 . TRP A 1 91  ? -26.762 -23.664 3.023   1.00 13.73 ? 90   TRP A CD2 1 
ATOM   712  N  NE1 . TRP A 1 91  ? -27.478 -25.076 4.618   1.00 14.15 ? 90   TRP A NE1 1 
ATOM   713  C  CE2 . TRP A 1 91  ? -26.617 -24.968 3.557   1.00 14.29 ? 90   TRP A CE2 1 
ATOM   714  C  CE3 . TRP A 1 91  ? -25.978 -23.290 1.920   1.00 12.55 ? 90   TRP A CE3 1 
ATOM   715  C  CZ2 . TRP A 1 91  ? -25.718 -25.900 3.030   1.00 14.37 ? 90   TRP A CZ2 1 
ATOM   716  C  CZ3 . TRP A 1 91  ? -25.086 -24.223 1.389   1.00 14.70 ? 90   TRP A CZ3 1 
ATOM   717  C  CH2 . TRP A 1 91  ? -24.968 -25.517 1.944   1.00 13.74 ? 90   TRP A CH2 1 
ATOM   718  N  N   . THR A 1 92  ? -27.676 -18.504 2.999   1.00 11.06 ? 91   THR A N   1 
ATOM   719  C  CA  . THR A 1 92  ? -28.169 -17.170 2.672   1.00 12.62 ? 91   THR A CA  1 
ATOM   720  C  C   . THR A 1 92  ? -29.679 -17.170 2.468   1.00 14.43 ? 91   THR A C   1 
ATOM   721  O  O   . THR A 1 92  ? -30.340 -16.153 2.715   1.00 13.26 ? 91   THR A O   1 
ATOM   722  C  CB  . THR A 1 92  ? -27.452 -16.645 1.422   1.00 11.53 ? 91   THR A CB  1 
ATOM   723  O  OG1 . THR A 1 92  ? -26.037 -16.650 1.644   1.00 11.15 ? 91   THR A OG1 1 
ATOM   724  C  CG2 . THR A 1 92  ? -27.893 -15.230 1.076   1.00 15.35 ? 91   THR A CG2 1 
ATOM   725  N  N   . HIS A 1 93  ? -30.241 -18.304 2.045   1.00 12.94 ? 92   HIS A N   1 
ATOM   726  C  CA  . HIS A 1 93  ? -31.662 -18.402 1.745   1.00 12.48 ? 92   HIS A CA  1 
ATOM   727  C  C   . HIS A 1 93  ? -32.516 -18.796 2.943   1.00 13.75 ? 92   HIS A C   1 
ATOM   728  O  O   . HIS A 1 93  ? -33.749 -18.807 2.822   1.00 13.11 ? 92   HIS A O   1 
ATOM   729  C  CB  . HIS A 1 93  ? -31.895 -19.395 0.601   1.00 15.24 ? 92   HIS A CB  1 
ATOM   730  C  CG  . HIS A 1 93  ? -31.171 -20.696 0.754   1.00 16.79 ? 92   HIS A CG  1 
ATOM   731  N  ND1 . HIS A 1 93  ? -31.608 -21.701 1.594   1.00 15.63 ? 92   HIS A ND1 1 
ATOM   732  C  CD2 . HIS A 1 93  ? -30.059 -21.173 0.143   1.00 16.68 ? 92   HIS A CD2 1 
ATOM   733  C  CE1 . HIS A 1 93  ? -30.787 -22.733 1.505   1.00 18.60 ? 92   HIS A CE1 1 
ATOM   734  N  NE2 . HIS A 1 93  ? -29.844 -22.443 0.626   1.00 17.44 ? 92   HIS A NE2 1 
ATOM   735  N  N   . GLU A 1 94  ? -31.911 -19.126 4.084   1.00 13.61 ? 93   GLU A N   1 
ATOM   736  C  CA  . GLU A 1 94  ? -32.703 -19.382 5.278   1.00 15.00 ? 93   GLU A CA  1 
ATOM   737  C  C   . GLU A 1 94  ? -33.232 -18.069 5.833   1.00 14.60 ? 93   GLU A C   1 
ATOM   738  O  O   . GLU A 1 94  ? -32.501 -17.074 5.921   1.00 15.20 ? 93   GLU A O   1 
ATOM   739  C  CB  . GLU A 1 94  ? -31.875 -20.101 6.344   1.00 14.58 ? 93   GLU A CB  1 
ATOM   740  C  CG  . GLU A 1 94  ? -31.579 -21.578 6.051   1.00 14.40 ? 93   GLU A CG  1 
ATOM   741  C  CD  . GLU A 1 94  ? -30.760 -22.223 7.159   1.00 14.67 ? 93   GLU A CD  1 
ATOM   742  O  OE1 . GLU A 1 94  ? -29.537 -21.968 7.217   1.00 14.30 ? 93   GLU A OE1 1 
ATOM   743  O  OE2 . GLU A 1 94  ? -31.349 -22.963 7.993   1.00 17.18 ? 93   GLU A OE2 1 
ATOM   744  N  N   . LYS A 1 95  ? -34.512 -18.075 6.220   1.00 15.41 ? 94   LYS A N   1 
ATOM   745  C  CA  . LYS A 1 95  ? -35.153 -16.853 6.694   1.00 15.69 ? 94   LYS A CA  1 
ATOM   746  C  C   . LYS A 1 95  ? -34.330 -16.173 7.781   1.00 15.66 ? 94   LYS A C   1 
ATOM   747  O  O   . LYS A 1 95  ? -34.176 -14.945 7.781   1.00 16.43 ? 94   LYS A O   1 
ATOM   748  C  CB  . LYS A 1 95  ? -36.559 -17.168 7.210   1.00 18.22 ? 94   LYS A CB  1 
ATOM   749  C  CG  . LYS A 1 95  ? -37.285 -15.988 7.843   1.00 20.76 ? 94   LYS A CG  1 
ATOM   750  C  CD  . LYS A 1 95  ? -38.629 -16.430 8.395   1.00 21.69 ? 94   LYS A CD  1 
ATOM   751  C  CE  . LYS A 1 95  ? -39.362 -15.288 9.057   1.00 27.19 ? 94   LYS A CE  1 
ATOM   752  N  NZ  . LYS A 1 95  ? -40.663 -15.741 9.636   1.00 31.69 ? 94   LYS A NZ  1 
ATOM   753  N  N   . ASN A 1 96  ? -33.783 -16.955 8.716   1.00 15.27 ? 95   ASN A N   1 
ATOM   754  C  CA  . ASN A 1 96  ? -33.098 -16.350 9.849   1.00 16.53 ? 95   ASN A CA  1 
ATOM   755  C  C   . ASN A 1 96  ? -31.777 -15.677 9.481   1.00 13.84 ? 95   ASN A C   1 
ATOM   756  O  O   . ASN A 1 96  ? -31.259 -14.907 10.302  1.00 13.83 ? 95   ASN A O   1 
ATOM   757  C  CB  . ASN A 1 96  ? -32.871 -17.393 10.949  1.00 16.53 ? 95   ASN A CB  1 
ATOM   758  C  CG  . ASN A 1 96  ? -34.063 -17.526 11.870  1.00 19.55 ? 95   ASN A CG  1 
ATOM   759  O  OD1 . ASN A 1 96  ? -34.881 -16.605 11.967  1.00 21.65 ? 95   ASN A OD1 1 
ATOM   760  N  ND2 . ASN A 1 96  ? -34.170 -18.665 12.562  1.00 18.77 ? 95   ASN A ND2 1 
ATOM   761  N  N   . TRP A 1 97  ? -31.212 -15.910 8.288   1.00 12.72 ? 96   TRP A N   1 
ATOM   762  C  CA  . TRP A 1 97  ? -29.982 -15.191 7.964   1.00 13.52 ? 96   TRP A CA  1 
ATOM   763  C  C   . TRP A 1 97  ? -30.255 -13.701 7.756   1.00 12.84 ? 96   TRP A C   1 
ATOM   764  O  O   . TRP A 1 97  ? -29.729 -12.855 8.490   1.00 14.82 ? 96   TRP A O   1 
ATOM   765  C  CB  . TRP A 1 97  ? -29.244 -15.774 6.740   1.00 13.28 ? 96   TRP A CB  1 
ATOM   766  C  CG  . TRP A 1 97  ? -28.055 -14.880 6.532   1.00 14.86 ? 96   TRP A CG  1 
ATOM   767  C  CD1 . TRP A 1 97  ? -26.931 -14.817 7.322   1.00 14.83 ? 96   TRP A CD1 1 
ATOM   768  C  CD2 . TRP A 1 97  ? -27.940 -13.806 5.590   1.00 14.35 ? 96   TRP A CD2 1 
ATOM   769  N  NE1 . TRP A 1 97  ? -26.113 -13.798 6.901   1.00 13.39 ? 96   TRP A NE1 1 
ATOM   770  C  CE2 . TRP A 1 97  ? -26.706 -13.164 5.837   1.00 15.13 ? 96   TRP A CE2 1 
ATOM   771  C  CE3 . TRP A 1 97  ? -28.750 -13.341 4.545   1.00 14.94 ? 96   TRP A CE3 1 
ATOM   772  C  CZ2 . TRP A 1 97  ? -26.259 -12.085 5.073   1.00 15.66 ? 96   TRP A CZ2 1 
ATOM   773  C  CZ3 . TRP A 1 97  ? -28.302 -12.259 3.783   1.00 13.41 ? 96   TRP A CZ3 1 
ATOM   774  C  CH2 . TRP A 1 97  ? -27.066 -11.649 4.054   1.00 15.56 ? 96   TRP A CH2 1 
ATOM   775  N  N   . LYS A 1 98  ? -31.075 -13.354 6.756   1.00 14.09 ? 97   LYS A N   1 
ATOM   776  C  CA  . LYS A 1 98  ? -31.317 -11.940 6.476   1.00 14.20 ? 97   LYS A CA  1 
ATOM   777  C  C   . LYS A 1 98  ? -31.997 -11.256 7.657   1.00 14.80 ? 97   LYS A C   1 
ATOM   778  O  O   . LYS A 1 98  ? -31.726 -10.086 7.955   1.00 14.46 ? 97   LYS A O   1 
ATOM   779  C  CB  . LYS A 1 98  ? -32.164 -11.782 5.207   1.00 16.13 ? 97   LYS A CB  1 
ATOM   780  C  CG  . LYS A 1 98  ? -32.295 -10.330 4.734   1.00 20.79 ? 97   LYS A CG  1 
ATOM   781  C  CD  . LYS A 1 98  ? -30.913 -9.710  4.552   1.00 24.43 ? 97   LYS A CD  1 
ATOM   782  C  CE  . LYS A 1 98  ? -30.979 -8.277  4.051   1.00 29.06 ? 97   LYS A CE  1 
ATOM   783  N  NZ  . LYS A 1 98  ? -31.150 -8.223  2.578   1.00 33.43 ? 97   LYS A NZ  1 
ATOM   784  N  N   . LYS A 1 99  ? -32.886 -11.972 8.342   1.00 13.61 ? 98   LYS A N   1 
ATOM   785  C  CA  . LYS A 1 99  ? -33.573 -11.397 9.494   1.00 13.95 ? 98   LYS A CA  1 
ATOM   786  C  C   . LYS A 1 99  ? -32.578 -10.979 10.579  1.00 15.51 ? 98   LYS A C   1 
ATOM   787  O  O   . LYS A 1 99  ? -32.582 -9.829  11.038  1.00 15.25 ? 98   LYS A O   1 
ATOM   788  C  CB  . LYS A 1 99  ? -34.583 -12.414 10.022  1.00 17.76 ? 98   LYS A CB  1 
ATOM   789  C  CG  . LYS A 1 99  ? -35.432 -11.969 11.188  1.00 19.74 ? 98   LYS A CG  1 
ATOM   790  C  CD  . LYS A 1 99  ? -36.475 -13.053 11.507  1.00 22.85 ? 98   LYS A CD  1 
ATOM   791  C  CE  . LYS A 1 99  ? -37.082 -12.887 12.891  1.00 22.29 ? 98   LYS A CE  1 
ATOM   792  N  NZ  . LYS A 1 99  ? -38.058 -13.981 13.198  1.00 22.36 ? 98   LYS A NZ  1 
ATOM   793  N  N   . ALA A 1 100 ? -31.710 -11.902 10.999  1.00 14.53 ? 99   ALA A N   1 
ATOM   794  C  CA  . ALA A 1 100 ? -30.713 -11.574 12.019  1.00 13.65 ? 99   ALA A CA  1 
ATOM   795  C  C   . ALA A 1 100 ? -29.687 -10.572 11.498  1.00 13.24 ? 99   ALA A C   1 
ATOM   796  O  O   . ALA A 1 100 ? -29.218 -9.708  12.249  1.00 14.07 ? 99   ALA A O   1 
ATOM   797  C  CB  . ALA A 1 100 ? -30.016 -12.844 12.504  1.00 13.63 ? 99   ALA A CB  1 
ATOM   798  N  N   . HIS A 1 101 ? -29.322 -10.670 10.215  1.00 13.86 ? 100  HIS A N   1 
ATOM   799  C  CA  . HIS A 1 101 ? -28.430 -9.675  9.624   1.00 15.44 ? 100  HIS A CA  1 
ATOM   800  C  C   . HIS A 1 101 ? -29.012 -8.267  9.749   1.00 15.98 ? 100  HIS A C   1 
ATOM   801  O  O   . HIS A 1 101 ? -28.324 -7.330  10.185  1.00 15.10 ? 100  HIS A O   1 
ATOM   802  C  CB  . HIS A 1 101 ? -28.165 -10.030 8.158   1.00 16.35 ? 100  HIS A CB  1 
ATOM   803  C  CG  . HIS A 1 101 ? -27.380 -8.996  7.413   1.00 22.17 ? 100  HIS A CG  1 
ATOM   804  N  ND1 . HIS A 1 101 ? -26.004 -8.927  7.462   1.00 25.07 ? 100  HIS A ND1 1 
ATOM   805  C  CD2 . HIS A 1 101 ? -27.778 -7.996  6.590   1.00 26.86 ? 100  HIS A CD2 1 
ATOM   806  C  CE1 . HIS A 1 101 ? -25.588 -7.920  6.716   1.00 27.40 ? 100  HIS A CE1 1 
ATOM   807  N  NE2 . HIS A 1 101 ? -26.644 -7.343  6.169   1.00 30.76 ? 100  HIS A NE2 1 
ATOM   808  N  N   . ASN A 1 102 ? -30.285 -8.094  9.367   1.00 15.59 ? 101  ASN A N   1 
ATOM   809  C  CA  . ASN A 1 102 ? -30.907 -6.775  9.462   1.00 14.80 ? 101  ASN A CA  1 
ATOM   810  C  C   . ASN A 1 102 ? -30.955 -6.291  10.903  1.00 16.89 ? 101  ASN A C   1 
ATOM   811  O  O   . ASN A 1 102 ? -30.754 -5.101  11.175  1.00 19.14 ? 101  ASN A O   1 
ATOM   812  C  CB  . ASN A 1 102 ? -32.322 -6.800  8.877   1.00 14.58 ? 101  ASN A CB  1 
ATOM   813  C  CG  . ASN A 1 102 ? -32.325 -6.852  7.358   1.00 16.39 ? 101  ASN A CG  1 
ATOM   814  O  OD1 . ASN A 1 102 ? -31.312 -6.582  6.718   1.00 18.22 ? 101  ASN A OD1 1 
ATOM   815  N  ND2 . ASN A 1 102 ? -33.474 -7.188  6.777   1.00 18.74 ? 101  ASN A ND2 1 
ATOM   816  N  N   . ILE A 1 103 ? -31.230 -7.202  11.837  1.00 15.16 ? 102  ILE A N   1 
ATOM   817  C  CA  . ILE A 1 103 ? -31.413 -6.820  13.236  1.00 15.74 ? 102  ILE A CA  1 
ATOM   818  C  C   . ILE A 1 103 ? -30.080 -6.452  13.878  1.00 14.23 ? 102  ILE A C   1 
ATOM   819  O  O   . ILE A 1 103 ? -30.010 -5.528  14.701  1.00 17.85 ? 102  ILE A O   1 
ATOM   820  C  CB  . ILE A 1 103 ? -32.128 -7.957  13.995  1.00 15.44 ? 102  ILE A CB  1 
ATOM   821  C  CG1 . ILE A 1 103 ? -33.605 -8.023  13.575  1.00 15.28 ? 102  ILE A CG1 1 
ATOM   822  C  CG2 . ILE A 1 103 ? -31.964 -7.799  15.511  1.00 16.19 ? 102  ILE A CG2 1 
ATOM   823  C  CD1 . ILE A 1 103 ? -34.357 -9.276  14.049  1.00 15.99 ? 102  ILE A CD1 1 
ATOM   824  N  N   . LEU A 1 104 ? -28.997 -7.150  13.510  1.00 12.96 ? 103  LEU A N   1 
ATOM   825  C  CA  . LEU A 1 104 ? -27.727 -6.994  14.215  1.00 14.18 ? 103  LEU A CA  1 
ATOM   826  C  C   . LEU A 1 104 ? -26.741 -6.053  13.527  1.00 14.45 ? 103  LEU A C   1 
ATOM   827  O  O   . LEU A 1 104 ? -25.809 -5.578  14.187  1.00 15.96 ? 103  LEU A O   1 
ATOM   828  C  CB  . LEU A 1 104 ? -27.069 -8.368  14.432  1.00 13.71 ? 103  LEU A CB  1 
ATOM   829  C  CG  . LEU A 1 104 ? -27.898 -9.334  15.295  1.00 13.66 ? 103  LEU A CG  1 
ATOM   830  C  CD1 . LEU A 1 104 ? -27.255 -10.725 15.368  1.00 14.54 ? 103  LEU A CD1 1 
ATOM   831  C  CD2 . LEU A 1 104 ? -28.152 -8.768  16.695  1.00 19.04 ? 103  LEU A CD2 1 
ATOM   832  N  N   . LEU A 1 105 ? -26.916 -5.745  12.244  1.00 15.19 ? 104  LEU A N   1 
ATOM   833  C  CA  . LEU A 1 105 ? -26.008 -4.797  11.598  1.00 15.06 ? 104  LEU A CA  1 
ATOM   834  C  C   . LEU A 1 105 ? -25.863 -3.475  12.353  1.00 17.31 ? 104  LEU A C   1 
ATOM   835  O  O   . LEU A 1 105 ? -24.733 -2.961  12.430  1.00 17.50 ? 104  LEU A O   1 
ATOM   836  C  CB  . LEU A 1 105 ? -26.467 -4.542  10.155  1.00 18.26 ? 104  LEU A CB  1 
ATOM   837  C  CG  . LEU A 1 105 ? -25.456 -3.885  9.215   1.00 22.12 ? 104  LEU A CG  1 
ATOM   838  C  CD1 . LEU A 1 105 ? -24.237 -4.785  9.029   1.00 22.19 ? 104  LEU A CD1 1 
ATOM   839  C  CD2 . LEU A 1 105 ? -26.106 -3.581  7.871   1.00 23.96 ? 104  LEU A CD2 1 
ATOM   840  N  N   . PRO A 1 106 ? -26.919 -2.873  12.910  1.00 17.26 ? 105  PRO A N   1 
ATOM   841  C  CA  . PRO A 1 106 ? -26.731 -1.613  13.654  1.00 18.75 ? 105  PRO A CA  1 
ATOM   842  C  C   . PRO A 1 106 ? -25.839 -1.753  14.876  1.00 19.15 ? 105  PRO A C   1 
ATOM   843  O  O   . PRO A 1 106 ? -25.301 -0.741  15.350  1.00 21.30 ? 105  PRO A O   1 
ATOM   844  C  CB  . PRO A 1 106 ? -28.162 -1.214  14.044  1.00 21.11 ? 105  PRO A CB  1 
ATOM   845  C  CG  . PRO A 1 106 ? -29.016 -1.857  12.993  1.00 19.05 ? 105  PRO A CG  1 
ATOM   846  C  CD  . PRO A 1 106 ? -28.344 -3.171  12.687  1.00 18.26 ? 105  PRO A CD  1 
ATOM   847  N  N   . SER A 1 107 ? -25.664 -2.967  15.401  1.00 14.04 ? 106  SER A N   1 
ATOM   848  C  CA  . SER A 1 107 ? -24.760 -3.205  16.522  1.00 17.14 ? 106  SER A CA  1 
ATOM   849  C  C   . SER A 1 107 ? -23.296 -3.091  16.133  1.00 15.54 ? 106  SER A C   1 
ATOM   850  O  O   . SER A 1 107 ? -22.429 -3.197  17.011  1.00 15.88 ? 106  SER A O   1 
ATOM   851  C  CB  . SER A 1 107 ? -25.019 -4.590  17.125  1.00 20.50 ? 106  SER A CB  1 
ATOM   852  O  OG  . SER A 1 107 ? -26.277 -4.634  17.763  1.00 25.94 ? 106  SER A OG  1 
ATOM   853  N  N   . PHE A 1 108 ? -22.992 -2.891  14.848  1.00 17.03 ? 107  PHE A N   1 
ATOM   854  C  CA  . PHE A 1 108 ? -21.620 -2.677  14.401  1.00 20.03 ? 107  PHE A CA  1 
ATOM   855  C  C   . PHE A 1 108 ? -21.466 -1.382  13.611  1.00 22.22 ? 107  PHE A C   1 
ATOM   856  O  O   . PHE A 1 108 ? -20.517 -1.231  12.835  1.00 27.14 ? 107  PHE A O   1 
ATOM   857  C  CB  . PHE A 1 108 ? -21.146 -3.897  13.616  1.00 22.17 ? 107  PHE A CB  1 
ATOM   858  C  CG  . PHE A 1 108 ? -21.168 -5.146  14.445  1.00 20.69 ? 107  PHE A CG  1 
ATOM   859  C  CD1 . PHE A 1 108 ? -20.115 -5.435  15.294  1.00 20.34 ? 107  PHE A CD1 1 
ATOM   860  C  CD2 . PHE A 1 108 ? -22.279 -5.972  14.461  1.00 20.65 ? 107  PHE A CD2 1 
ATOM   861  C  CE1 . PHE A 1 108 ? -20.145 -6.569  16.108  1.00 23.78 ? 107  PHE A CE1 1 
ATOM   862  C  CE2 . PHE A 1 108 ? -22.322 -7.095  15.276  1.00 19.71 ? 107  PHE A CE2 1 
ATOM   863  C  CZ  . PHE A 1 108 ? -21.253 -7.395  16.099  1.00 22.06 ? 107  PHE A CZ  1 
ATOM   864  N  N   . SER A 1 109 ? -22.356 -0.423  13.834  1.00 24.37 ? 108  SER A N   1 
ATOM   865  C  CA  . SER A 1 109 ? -22.224 0.889   13.223  1.00 26.03 ? 108  SER A CA  1 
ATOM   866  C  C   . SER A 1 109 ? -21.133 1.695   13.928  1.00 28.95 ? 108  SER A C   1 
ATOM   867  O  O   . SER A 1 109 ? -20.649 1.330   15.007  1.00 28.81 ? 108  SER A O   1 
ATOM   868  C  CB  . SER A 1 109 ? -23.546 1.642   13.303  1.00 28.69 ? 108  SER A CB  1 
ATOM   869  O  OG  . SER A 1 109 ? -23.876 1.890   14.663  1.00 29.95 ? 108  SER A OG  1 
ATOM   870  N  N   . GLN A 1 110 ? -20.750 2.815   13.301  1.00 30.74 ? 109  GLN A N   1 
ATOM   871  C  CA  . GLN A 1 110 ? -19.835 3.757   13.941  1.00 32.80 ? 109  GLN A CA  1 
ATOM   872  C  C   . GLN A 1 110 ? -20.334 4.135   15.331  1.00 33.01 ? 109  GLN A C   1 
ATOM   873  O  O   . GLN A 1 110 ? -19.579 4.106   16.312  1.00 34.66 ? 109  GLN A O   1 
ATOM   874  C  CB  . GLN A 1 110 ? -19.679 5.020   13.083  1.00 38.68 ? 109  GLN A CB  1 
ATOM   875  C  CG  . GLN A 1 110 ? -19.092 4.818   11.685  1.00 44.03 ? 109  GLN A CG  1 
ATOM   876  C  CD  . GLN A 1 110 ? -19.176 6.080   10.828  1.00 46.91 ? 109  GLN A CD  1 
ATOM   877  O  OE1 . GLN A 1 110 ? -19.634 7.127   11.288  1.00 49.68 ? 109  GLN A OE1 1 
ATOM   878  N  NE2 . GLN A 1 110 ? -18.738 5.982   9.573   1.00 44.71 ? 109  GLN A NE2 1 
ATOM   879  N  N   . GLN A 1 111 ? -21.613 4.505   15.427  1.00 32.69 ? 110  GLN A N   1 
ATOM   880  C  CA  . GLN A 1 111 ? -22.171 4.908   16.713  1.00 33.23 ? 110  GLN A CA  1 
ATOM   881  C  C   . GLN A 1 111 ? -22.090 3.777   17.731  1.00 30.34 ? 110  GLN A C   1 
ATOM   882  O  O   . GLN A 1 111 ? -21.867 4.018   18.926  1.00 27.61 ? 110  GLN A O   1 
ATOM   883  C  CB  . GLN A 1 111 ? -23.619 5.367   16.535  1.00 37.90 ? 110  GLN A CB  1 
ATOM   884  C  CG  . GLN A 1 111 ? -24.237 5.932   17.801  1.00 42.89 ? 110  GLN A CG  1 
ATOM   885  C  CD  . GLN A 1 111 ? -23.484 7.148   18.309  1.00 49.32 ? 110  GLN A CD  1 
ATOM   886  O  OE1 . GLN A 1 111 ? -23.111 8.031   17.533  1.00 50.77 ? 110  GLN A OE1 1 
ATOM   887  N  NE2 . GLN A 1 111 ? -23.244 7.194   19.617  1.00 52.65 ? 110  GLN A NE2 1 
ATOM   888  N  N   . ALA A 1 112 ? -22.281 2.535   17.277  1.00 27.73 ? 111  ALA A N   1 
ATOM   889  C  CA  . ALA A 1 112 ? -22.152 1.396   18.176  1.00 23.07 ? 111  ALA A CA  1 
ATOM   890  C  C   . ALA A 1 112 ? -20.720 1.244   18.670  1.00 22.25 ? 111  ALA A C   1 
ATOM   891  O  O   . ALA A 1 112 ? -20.497 0.958   19.852  1.00 21.84 ? 111  ALA A O   1 
ATOM   892  C  CB  . ALA A 1 112 ? -22.619 0.119   17.476  1.00 20.30 ? 111  ALA A CB  1 
ATOM   893  N  N   . MET A 1 113 ? -19.735 1.427   17.784  1.00 20.73 ? 112  MET A N   1 
ATOM   894  C  CA  . MET A 1 113 ? -18.342 1.248   18.188  1.00 19.43 ? 112  MET A CA  1 
ATOM   895  C  C   . MET A 1 113 ? -17.928 2.296   19.215  1.00 18.16 ? 112  MET A C   1 
ATOM   896  O  O   . MET A 1 113 ? -17.191 1.994   20.164  1.00 18.86 ? 112  MET A O   1 
ATOM   897  C  CB  . MET A 1 113 ? -17.422 1.306   16.971  1.00 24.14 ? 112  MET A CB  1 
ATOM   898  C  CG  . MET A 1 113 ? -17.577 0.141   15.998  1.00 27.25 ? 112  MET A CG  1 
ATOM   899  S  SD  . MET A 1 113 ? -17.183 -1.441  16.756  1.00 25.83 ? 112  MET A SD  1 
ATOM   900  C  CE  . MET A 1 113 ? -15.475 -1.173  17.201  1.00 32.88 ? 112  MET A CE  1 
ATOM   901  N  N   . LYS A 1 114 ? -18.382 3.537   19.035  1.00 16.75 ? 113  LYS A N   1 
ATOM   902  C  CA  . LYS A 1 114 ? -18.143 4.556   20.047  1.00 16.00 ? 113  LYS A CA  1 
ATOM   903  C  C   . LYS A 1 114 ? -18.692 4.123   21.396  1.00 18.68 ? 113  LYS A C   1 
ATOM   904  O  O   . LYS A 1 114 ? -18.106 4.445   22.438  1.00 20.64 ? 113  LYS A O   1 
ATOM   905  C  CB  . LYS A 1 114 ? -18.769 5.881   19.608  1.00 16.34 ? 113  LYS A CB  1 
ATOM   906  C  CG  . LYS A 1 114 ? -18.166 6.445   18.332  1.00 19.42 ? 113  LYS A CG  1 
ATOM   907  C  CD  . LYS A 1 114 ? -18.864 7.739   17.905  1.00 19.94 ? 113  LYS A CD  1 
ATOM   908  C  CE  . LYS A 1 114 ? -18.259 8.309   16.621  1.00 22.79 ? 113  LYS A CE  1 
ATOM   909  N  NZ  . LYS A 1 114 ? -19.105 9.374   15.984  1.00 26.26 ? 113  LYS A NZ  1 
ATOM   910  N  N   . GLY A 1 115 ? -19.806 3.380   21.392  1.00 16.10 ? 114  GLY A N   1 
ATOM   911  C  CA  . GLY A 1 115 ? -20.396 2.910   22.635  1.00 16.28 ? 114  GLY A CA  1 
ATOM   912  C  C   . GLY A 1 115 ? -19.656 1.761   23.287  1.00 17.23 ? 114  GLY A C   1 
ATOM   913  O  O   . GLY A 1 115 ? -19.658 1.647   24.519  1.00 20.81 ? 114  GLY A O   1 
ATOM   914  N  N   . TYR A 1 116 ? -19.017 0.895   22.486  1.00 16.32 ? 115  TYR A N   1 
ATOM   915  C  CA  . TYR A 1 116 ? -18.224 -0.206  23.023  1.00 14.97 ? 115  TYR A CA  1 
ATOM   916  C  C   . TYR A 1 116 ? -16.858 0.235   23.527  1.00 15.51 ? 115  TYR A C   1 
ATOM   917  O  O   . TYR A 1 116 ? -16.202 -0.531  24.238  1.00 16.20 ? 115  TYR A O   1 
ATOM   918  C  CB  . TYR A 1 116 ? -17.977 -1.288  21.962  1.00 13.84 ? 115  TYR A CB  1 
ATOM   919  C  CG  . TYR A 1 116 ? -19.203 -1.929  21.364  1.00 16.37 ? 115  TYR A CG  1 
ATOM   920  C  CD1 . TYR A 1 116 ? -20.222 -2.422  22.165  1.00 17.73 ? 115  TYR A CD1 1 
ATOM   921  C  CD2 . TYR A 1 116 ? -19.326 -2.063  19.982  1.00 14.66 ? 115  TYR A CD2 1 
ATOM   922  C  CE1 . TYR A 1 116 ? -21.336 -3.019  21.603  1.00 18.26 ? 115  TYR A CE1 1 
ATOM   923  C  CE2 . TYR A 1 116 ? -20.432 -2.656  19.413  1.00 16.51 ? 115  TYR A CE2 1 
ATOM   924  C  CZ  . TYR A 1 116 ? -21.435 -3.128  20.225  1.00 16.91 ? 115  TYR A CZ  1 
ATOM   925  O  OH  . TYR A 1 116 ? -22.542 -3.720  19.658  1.00 20.89 ? 115  TYR A OH  1 
ATOM   926  N  N   . HIS A 1 117 ? -16.397 1.420   23.127  1.00 17.95 ? 116  HIS A N   1 
ATOM   927  C  CA  . HIS A 1 117 ? -14.991 1.773   23.301  1.00 14.66 ? 116  HIS A CA  1 
ATOM   928  C  C   . HIS A 1 117 ? -14.561 1.717   24.767  1.00 15.87 ? 116  HIS A C   1 
ATOM   929  O  O   . HIS A 1 117 ? -13.498 1.173   25.091  1.00 15.92 ? 116  HIS A O   1 
ATOM   930  C  CB  . HIS A 1 117 ? -14.727 3.162   22.715  1.00 15.41 ? 116  HIS A CB  1 
ATOM   931  C  CG  . HIS A 1 117 ? -13.309 3.606   22.869  1.00 16.87 ? 116  HIS A CG  1 
ATOM   932  N  ND1 . HIS A 1 117 ? -12.335 3.305   21.941  1.00 17.39 ? 116  HIS A ND1 1 
ATOM   933  C  CD2 . HIS A 1 117 ? -12.686 4.277   23.868  1.00 17.80 ? 116  HIS A CD2 1 
ATOM   934  C  CE1 . HIS A 1 117 ? -11.177 3.795   22.350  1.00 19.32 ? 116  HIS A CE1 1 
ATOM   935  N  NE2 . HIS A 1 117 ? -11.363 4.385   23.518  1.00 17.91 ? 116  HIS A NE2 1 
ATOM   936  N  N   . ALA A 1 118 ? -15.368 2.283   25.669  1.00 17.27 ? 117  ALA A N   1 
ATOM   937  C  CA  . ALA A 1 118 ? -14.964 2.351   27.075  1.00 18.23 ? 117  ALA A CA  1 
ATOM   938  C  C   . ALA A 1 118 ? -14.741 0.961   27.661  1.00 17.23 ? 117  ALA A C   1 
ATOM   939  O  O   . ALA A 1 118 ? -13.808 0.750   28.446  1.00 15.79 ? 117  ALA A O   1 
ATOM   940  C  CB  . ALA A 1 118 ? -16.009 3.116   27.890  1.00 16.54 ? 117  ALA A CB  1 
ATOM   941  N  N   A MET A 1 119 ? -15.604 0.006   27.307  0.60 17.33 ? 118  MET A N   1 
ATOM   942  N  N   B MET A 1 119 ? -15.587 -0.005  27.306  0.40 18.25 ? 118  MET A N   1 
ATOM   943  C  CA  A MET A 1 119 ? -15.440 -1.354  27.802  0.60 16.85 ? 118  MET A CA  1 
ATOM   944  C  CA  B MET A 1 119 ? -15.398 -1.344  27.849  0.40 18.56 ? 118  MET A CA  1 
ATOM   945  C  C   A MET A 1 119 ? -14.247 -2.047  27.157  0.60 15.78 ? 118  MET A C   1 
ATOM   946  C  C   B MET A 1 119 ? -14.304 -2.124  27.123  0.40 16.80 ? 118  MET A C   1 
ATOM   947  O  O   A MET A 1 119 ? -13.575 -2.857  27.806  0.60 15.09 ? 118  MET A O   1 
ATOM   948  O  O   B MET A 1 119 ? -13.760 -3.075  27.696  0.40 16.55 ? 118  MET A O   1 
ATOM   949  C  CB  A MET A 1 119 ? -16.729 -2.144  27.576  0.60 19.19 ? 118  MET A CB  1 
ATOM   950  C  CB  B MET A 1 119 ? -16.720 -2.114  27.834  0.40 22.09 ? 118  MET A CB  1 
ATOM   951  C  CG  A MET A 1 119 ? -17.829 -1.784  28.571  0.60 20.16 ? 118  MET A CG  1 
ATOM   952  C  CG  B MET A 1 119 ? -17.732 -1.627  28.887  0.40 23.86 ? 118  MET A CG  1 
ATOM   953  S  SD  A MET A 1 119 ? -19.414 -2.560  28.194  0.60 21.26 ? 118  MET A SD  1 
ATOM   954  S  SD  B MET A 1 119 ? -17.149 -1.638  30.609  0.40 26.96 ? 118  MET A SD  1 
ATOM   955  C  CE  A MET A 1 119 ? -20.307 -2.299  29.730  0.60 22.67 ? 118  MET A CE  1 
ATOM   956  C  CE  B MET A 1 119 ? -16.664 0.074   30.827  0.40 25.77 ? 118  MET A CE  1 
ATOM   957  N  N   . MET A 1 120 ? -13.956 -1.748  25.889  1.00 14.53 ? 119  MET A N   1 
ATOM   958  C  CA  . MET A 1 120 ? -12.726 -2.273  25.308  1.00 11.25 ? 119  MET A CA  1 
ATOM   959  C  C   . MET A 1 120 ? -11.518 -1.788  26.107  1.00 13.04 ? 119  MET A C   1 
ATOM   960  O  O   . MET A 1 120 ? -10.590 -2.557  26.374  1.00 14.06 ? 119  MET A O   1 
ATOM   961  C  CB  . MET A 1 120 ? -12.590 -1.873  23.841  1.00 14.51 ? 119  MET A CB  1 
ATOM   962  C  CG  . MET A 1 120 ? -13.591 -2.525  22.921  1.00 15.83 ? 119  MET A CG  1 
ATOM   963  S  SD  . MET A 1 120 ? -13.126 -2.235  21.200  1.00 16.48 ? 119  MET A SD  1 
ATOM   964  C  CE  . MET A 1 120 ? -14.384 -3.190  20.336  1.00 15.39 ? 119  MET A CE  1 
ATOM   965  N  N   . VAL A 1 121 ? -11.529 -0.521  26.525  1.00 13.80 ? 120  VAL A N   1 
ATOM   966  C  CA  . VAL A 1 121 ? -10.407 0.018   27.292  1.00 14.33 ? 120  VAL A CA  1 
ATOM   967  C  C   . VAL A 1 121 ? -10.289 -0.686  28.644  1.00 13.13 ? 120  VAL A C   1 
ATOM   968  O  O   . VAL A 1 121 ? -9.181  -0.972  29.114  1.00 14.53 ? 120  VAL A O   1 
ATOM   969  C  CB  . VAL A 1 121 ? -10.543 1.549   27.445  1.00 15.92 ? 120  VAL A CB  1 
ATOM   970  C  CG1 . VAL A 1 121 ? -9.471  2.082   28.411  1.00 16.04 ? 120  VAL A CG1 1 
ATOM   971  C  CG2 . VAL A 1 121 ? -10.421 2.240   26.077  1.00 16.59 ? 120  VAL A CG2 1 
ATOM   972  N  N   . ASP A 1 122 ? -11.426 -0.998  29.276  1.00 14.43 ? 121  ASP A N   1 
ATOM   973  C  CA  . ASP A 1 122 ? -11.420 -1.720  30.546  1.00 14.48 ? 121  ASP A CA  1 
ATOM   974  C  C   . ASP A 1 122 ? -10.574 -2.990  30.451  1.00 14.37 ? 121  ASP A C   1 
ATOM   975  O  O   . ASP A 1 122 ? -9.689  -3.236  31.288  1.00 15.22 ? 121  ASP A O   1 
ATOM   976  C  CB  . ASP A 1 122 ? -12.870 -2.033  30.947  1.00 16.08 ? 121  ASP A CB  1 
ATOM   977  C  CG  . ASP A 1 122 ? -12.998 -2.710  32.302  1.00 14.85 ? 121  ASP A CG  1 
ATOM   978  O  OD1 . ASP A 1 122 ? -12.428 -3.802  32.497  1.00 15.03 ? 121  ASP A OD1 1 
ATOM   979  O  OD2 . ASP A 1 122 ? -13.717 -2.159  33.170  1.00 17.13 ? 121  ASP A OD2 1 
ATOM   980  N  N   . ILE A 1 123 ? -10.823 -3.803  29.421  1.00 13.13 ? 122  ILE A N   1 
ATOM   981  C  CA  . ILE A 1 123 ? -10.099 -5.064  29.280  1.00 12.50 ? 122  ILE A CA  1 
ATOM   982  C  C   . ILE A 1 123 ? -8.647  -4.807  28.877  1.00 14.72 ? 122  ILE A C   1 
ATOM   983  O  O   . ILE A 1 123 ? -7.720  -5.470  29.363  1.00 13.14 ? 122  ILE A O   1 
ATOM   984  C  CB  . ILE A 1 123 ? -10.819 -5.983  28.268  1.00 12.02 ? 122  ILE A CB  1 
ATOM   985  C  CG1 . ILE A 1 123 ? -12.293 -6.185  28.663  1.00 13.26 ? 122  ILE A CG1 1 
ATOM   986  C  CG2 . ILE A 1 123 ? -10.119 -7.342  28.187  1.00 14.32 ? 122  ILE A CG2 1 
ATOM   987  C  CD1 . ILE A 1 123 ? -12.488 -6.646  30.121  1.00 13.23 ? 122  ILE A CD1 1 
ATOM   988  N  N   . ALA A 1 124 ? -8.427  -3.848  27.976  1.00 13.40 ? 123  ALA A N   1 
ATOM   989  C  CA  . ALA A 1 124 ? -7.069  -3.545  27.530  1.00 13.82 ? 123  ALA A CA  1 
ATOM   990  C  C   . ALA A 1 124 ? -6.195  -3.110  28.698  1.00 14.98 ? 123  ALA A C   1 
ATOM   991  O  O   . ALA A 1 124 ? -5.010  -3.472  28.777  1.00 14.02 ? 123  ALA A O   1 
ATOM   992  C  CB  . ALA A 1 124 ? -7.101  -2.449  26.466  1.00 15.58 ? 123  ALA A CB  1 
ATOM   993  N  N   . VAL A 1 125 ? -6.758  -2.308  29.602  1.00 14.84 ? 124  VAL A N   1 
ATOM   994  C  CA  . VAL A 1 125 ? -6.000  -1.868  30.769  1.00 14.14 ? 124  VAL A CA  1 
ATOM   995  C  C   . VAL A 1 125 ? -5.647  -3.058  31.657  1.00 14.24 ? 124  VAL A C   1 
ATOM   996  O  O   . VAL A 1 125 ? -4.560  -3.108  32.246  1.00 14.45 ? 124  VAL A O   1 
ATOM   997  C  CB  . VAL A 1 125 ? -6.791  -0.786  31.528  1.00 16.09 ? 124  VAL A CB  1 
ATOM   998  C  CG1 . VAL A 1 125 ? -6.195  -0.537  32.900  1.00 15.51 ? 124  VAL A CG1 1 
ATOM   999  C  CG2 . VAL A 1 125 ? -6.814  0.512   30.715  1.00 17.14 ? 124  VAL A CG2 1 
ATOM   1000 N  N   . GLN A 1 126 ? -6.549  -4.039  31.768  1.00 15.03 ? 125  GLN A N   1 
ATOM   1001 C  CA  . GLN A 1 126 ? -6.214  -5.241  32.535  1.00 11.36 ? 125  GLN A CA  1 
ATOM   1002 C  C   . GLN A 1 126 ? -5.030  -5.976  31.912  1.00 13.06 ? 125  GLN A C   1 
ATOM   1003 O  O   . GLN A 1 126 ? -4.168  -6.502  32.627  1.00 13.67 ? 125  GLN A O   1 
ATOM   1004 C  CB  . GLN A 1 126 ? -7.425  -6.172  32.636  1.00 11.70 ? 125  GLN A CB  1 
ATOM   1005 C  CG  . GLN A 1 126 ? -8.591  -5.629  33.463  1.00 13.20 ? 125  GLN A CG  1 
ATOM   1006 C  CD  . GLN A 1 126 ? -9.647  -6.692  33.753  1.00 13.38 ? 125  GLN A CD  1 
ATOM   1007 O  OE1 . GLN A 1 126 ? -9.334  -7.800  34.196  1.00 15.26 ? 125  GLN A OE1 1 
ATOM   1008 N  NE2 . GLN A 1 126 ? -10.907 -6.359  33.495  1.00 14.10 ? 125  GLN A NE2 1 
ATOM   1009 N  N   . LEU A 1 127 ? -4.969  -6.026  30.577  1.00 12.17 ? 126  LEU A N   1 
ATOM   1010 C  CA  . LEU A 1 127 ? -3.821  -6.647  29.917  1.00 12.91 ? 126  LEU A CA  1 
ATOM   1011 C  C   . LEU A 1 127 ? -2.531  -5.897  30.242  1.00 15.73 ? 126  LEU A C   1 
ATOM   1012 O  O   . LEU A 1 127 ? -1.524  -6.506  30.632  1.00 14.75 ? 126  LEU A O   1 
ATOM   1013 C  CB  . LEU A 1 127 ? -4.048  -6.706  28.401  1.00 13.88 ? 126  LEU A CB  1 
ATOM   1014 C  CG  . LEU A 1 127 ? -2.841  -7.237  27.612  1.00 16.76 ? 126  LEU A CG  1 
ATOM   1015 C  CD1 . LEU A 1 127 ? -2.566  -8.704  27.934  1.00 17.47 ? 126  LEU A CD1 1 
ATOM   1016 C  CD2 . LEU A 1 127 ? -2.991  -7.052  26.096  1.00 19.72 ? 126  LEU A CD2 1 
ATOM   1017 N  N   . VAL A 1 128 ? -2.538  -4.567  30.082  1.00 14.82 ? 127  VAL A N   1 
ATOM   1018 C  CA  . VAL A 1 128 ? -1.321  -3.796  30.334  1.00 15.00 ? 127  VAL A CA  1 
ATOM   1019 C  C   . VAL A 1 128 ? -0.894  -3.935  31.793  1.00 15.97 ? 127  VAL A C   1 
ATOM   1020 O  O   . VAL A 1 128 ? 0.299   -4.071  32.097  1.00 15.84 ? 127  VAL A O   1 
ATOM   1021 C  CB  . VAL A 1 128 ? -1.520  -2.319  29.936  1.00 14.05 ? 127  VAL A CB  1 
ATOM   1022 C  CG1 . VAL A 1 128 ? -0.312  -1.484  30.347  1.00 16.02 ? 127  VAL A CG1 1 
ATOM   1023 C  CG2 . VAL A 1 128 ? -1.748  -2.194  28.420  1.00 15.19 ? 127  VAL A CG2 1 
ATOM   1024 N  N   . GLN A 1 129 ? -1.853  -3.914  32.720  1.00 14.89 ? 128  GLN A N   1 
ATOM   1025 C  CA  . GLN A 1 129 ? -1.481  -4.050  34.127  1.00 13.62 ? 128  GLN A CA  1 
ATOM   1026 C  C   . GLN A 1 129 ? -0.891  -5.428  34.417  1.00 13.50 ? 128  GLN A C   1 
ATOM   1027 O  O   . GLN A 1 129 ? 0.055   -5.547  35.209  1.00 15.44 ? 128  GLN A O   1 
ATOM   1028 C  CB  . GLN A 1 129 ? -2.693  -3.777  35.021  1.00 16.16 ? 128  GLN A CB  1 
ATOM   1029 C  CG  . GLN A 1 129 ? -3.083  -2.318  35.059  1.00 19.19 ? 128  GLN A CG  1 
ATOM   1030 C  CD  . GLN A 1 129 ? -4.325  -2.060  35.887  1.00 31.29 ? 128  GLN A CD  1 
ATOM   1031 O  OE1 . GLN A 1 129 ? -5.256  -2.867  35.897  1.00 35.36 ? 128  GLN A OE1 1 
ATOM   1032 N  NE2 . GLN A 1 129 ? -4.346  -0.929  36.590  1.00 33.72 ? 128  GLN A NE2 1 
ATOM   1033 N  N   . LYS A 1 130 ? -1.438  -6.488  33.809  1.00 14.00 ? 129  LYS A N   1 
ATOM   1034 C  CA  . LYS A 1 130 ? -0.840  -7.809  34.004  1.00 14.26 ? 129  LYS A CA  1 
ATOM   1035 C  C   . LYS A 1 130 ? 0.638   -7.789  33.622  1.00 13.51 ? 129  LYS A C   1 
ATOM   1036 O  O   . LYS A 1 130 ? 1.496   -8.289  34.362  1.00 14.17 ? 129  LYS A O   1 
ATOM   1037 C  CB  . LYS A 1 130 ? -1.580  -8.884  33.198  1.00 14.30 ? 129  LYS A CB  1 
ATOM   1038 C  CG  . LYS A 1 130 ? -0.914  -10.260 33.322  1.00 14.10 ? 129  LYS A CG  1 
ATOM   1039 C  CD  . LYS A 1 130 ? -1.664  -11.376 32.594  1.00 15.56 ? 129  LYS A CD  1 
ATOM   1040 C  CE  . LYS A 1 130 ? -0.915  -12.715 32.752  1.00 16.65 ? 129  LYS A CE  1 
ATOM   1041 N  NZ  . LYS A 1 130 ? -1.669  -13.884 32.210  1.00 18.32 ? 129  LYS A NZ  1 
ATOM   1042 N  N   . TRP A 1 131 ? 0.954   -7.197  32.469  1.00 13.18 ? 130  TRP A N   1 
ATOM   1043 C  CA  . TRP A 1 131 ? 2.334   -7.200  32.005  1.00 13.34 ? 130  TRP A CA  1 
ATOM   1044 C  C   . TRP A 1 131 ? 3.215   -6.265  32.830  1.00 15.75 ? 130  TRP A C   1 
ATOM   1045 O  O   . TRP A 1 131 ? 4.392   -6.578  33.061  1.00 18.37 ? 130  TRP A O   1 
ATOM   1046 C  CB  . TRP A 1 131 ? 2.382   -6.848  30.512  1.00 12.89 ? 130  TRP A CB  1 
ATOM   1047 C  CG  . TRP A 1 131 ? 1.767   -7.918  29.632  1.00 13.05 ? 130  TRP A CG  1 
ATOM   1048 C  CD1 . TRP A 1 131 ? 1.231   -9.125  30.032  1.00 12.78 ? 130  TRP A CD1 1 
ATOM   1049 C  CD2 . TRP A 1 131 ? 1.631   -7.875  28.204  1.00 12.81 ? 130  TRP A CD2 1 
ATOM   1050 N  NE1 . TRP A 1 131 ? 0.763   -9.821  28.933  1.00 11.98 ? 130  TRP A NE1 1 
ATOM   1051 C  CE2 . TRP A 1 131 ? 1.003   -9.078  27.803  1.00 14.18 ? 130  TRP A CE2 1 
ATOM   1052 C  CE3 . TRP A 1 131 ? 1.979   -6.933  27.226  1.00 12.07 ? 130  TRP A CE3 1 
ATOM   1053 C  CZ2 . TRP A 1 131 ? 0.716   -9.363  26.468  1.00 12.32 ? 130  TRP A CZ2 1 
ATOM   1054 C  CZ3 . TRP A 1 131 ? 1.692   -7.217  25.887  1.00 13.99 ? 130  TRP A CZ3 1 
ATOM   1055 C  CH2 . TRP A 1 131 ? 1.071   -8.425  25.523  1.00 14.90 ? 130  TRP A CH2 1 
ATOM   1056 N  N   . GLU A 1 132 ? 2.673   -5.131  33.304  1.00 15.38 ? 131  GLU A N   1 
ATOM   1057 C  CA  . GLU A 1 132 ? 3.458   -4.269  34.191  1.00 14.77 ? 131  GLU A CA  1 
ATOM   1058 C  C   . GLU A 1 132 ? 3.844   -4.993  35.475  1.00 15.18 ? 131  GLU A C   1 
ATOM   1059 O  O   . GLU A 1 132 ? 4.855   -4.651  36.105  1.00 16.81 ? 131  GLU A O   1 
ATOM   1060 C  CB  . GLU A 1 132 ? 2.691   -2.988  34.547  1.00 16.90 ? 131  GLU A CB  1 
ATOM   1061 C  CG  . GLU A 1 132 ? 2.340   -2.061  33.378  1.00 19.75 ? 131  GLU A CG  1 
ATOM   1062 C  CD  . GLU A 1 132 ? 3.487   -1.153  32.956  1.00 23.49 ? 131  GLU A CD  1 
ATOM   1063 O  OE1 . GLU A 1 132 ? 4.657   -1.476  33.252  1.00 24.84 ? 131  GLU A OE1 1 
ATOM   1064 O  OE2 . GLU A 1 132 ? 3.213   -0.109  32.321  1.00 23.30 ? 131  GLU A OE2 1 
ATOM   1065 N  N   . ARG A 1 133 ? 3.060   -5.991  35.875  1.00 13.35 ? 132  ARG A N   1 
ATOM   1066 C  CA  . ARG A 1 133 ? 3.225   -6.671  37.154  1.00 14.83 ? 132  ARG A CA  1 
ATOM   1067 C  C   . ARG A 1 133 ? 4.061   -7.946  37.073  1.00 14.95 ? 132  ARG A C   1 
ATOM   1068 O  O   . ARG A 1 133 ? 4.239   -8.615  38.099  1.00 15.72 ? 132  ARG A O   1 
ATOM   1069 C  CB  . ARG A 1 133 ? 1.842   -6.977  37.751  1.00 13.89 ? 132  ARG A CB  1 
ATOM   1070 C  CG  . ARG A 1 133 ? 1.141   -5.730  38.258  1.00 13.13 ? 132  ARG A CG  1 
ATOM   1071 C  CD  . ARG A 1 133 ? -0.346  -5.923  38.522  1.00 14.45 ? 132  ARG A CD  1 
ATOM   1072 N  NE  . ARG A 1 133 ? -0.917  -4.676  39.012  1.00 15.26 ? 132  ARG A NE  1 
ATOM   1073 C  CZ  . ARG A 1 133 ? -2.215  -4.422  39.125  1.00 15.89 ? 132  ARG A CZ  1 
ATOM   1074 N  NH1 . ARG A 1 133 ? -3.129  -5.300  38.747  1.00 14.87 ? 132  ARG A NH1 1 
ATOM   1075 N  NH2 . ARG A 1 133 ? -2.603  -3.255  39.628  1.00 18.92 ? 132  ARG A NH2 1 
ATOM   1076 N  N   . LEU A 1 134 ? 4.590   -8.297  35.901  1.00 15.22 ? 133  LEU A N   1 
ATOM   1077 C  CA  . LEU A 1 134 ? 5.480   -9.448  35.821  1.00 16.50 ? 133  LEU A CA  1 
ATOM   1078 C  C   . LEU A 1 134 ? 6.824   -9.137  36.475  1.00 17.58 ? 133  LEU A C   1 
ATOM   1079 O  O   . LEU A 1 134 ? 7.296   -7.996  36.468  1.00 19.52 ? 133  LEU A O   1 
ATOM   1080 C  CB  . LEU A 1 134 ? 5.693   -9.865  34.365  1.00 18.26 ? 133  LEU A CB  1 
ATOM   1081 C  CG  . LEU A 1 134 ? 4.429   -10.338 33.635  1.00 19.28 ? 133  LEU A CG  1 
ATOM   1082 C  CD1 . LEU A 1 134 ? 4.741   -10.743 32.186  1.00 20.62 ? 133  LEU A CD1 1 
ATOM   1083 C  CD2 . LEU A 1 134 ? 3.756   -11.478 34.389  1.00 19.01 ? 133  LEU A CD2 1 
ATOM   1084 N  N   . ASN A 1 135 ? 7.445   -10.167 37.046  1.00 17.37 ? 134  ASN A N   1 
ATOM   1085 C  CA  . ASN A 1 135 ? 8.779   -9.988  37.593  1.00 18.42 ? 134  ASN A CA  1 
ATOM   1086 C  C   . ASN A 1 135 ? 9.831   -10.055 36.489  1.00 21.48 ? 134  ASN A C   1 
ATOM   1087 O  O   . ASN A 1 135 ? 9.559   -10.437 35.345  1.00 23.00 ? 134  ASN A O   1 
ATOM   1088 C  CB  . ASN A 1 135 ? 9.082   -11.038 38.661  1.00 19.89 ? 134  ASN A CB  1 
ATOM   1089 C  CG  . ASN A 1 135 ? 8.084   -11.010 39.787  1.00 20.12 ? 134  ASN A CG  1 
ATOM   1090 O  OD1 . ASN A 1 135 ? 8.027   -10.045 40.550  1.00 20.00 ? 134  ASN A OD1 1 
ATOM   1091 N  ND2 . ASN A 1 135 ? 7.275   -12.066 39.894  1.00 19.54 ? 134  ASN A ND2 1 
ATOM   1092 N  N   . ALA A 1 136 ? 11.057  -9.682  36.858  1.00 25.18 ? 135  ALA A N   1 
ATOM   1093 C  CA  . ALA A 1 136 ? 12.169  -9.702  35.915  1.00 29.77 ? 135  ALA A CA  1 
ATOM   1094 C  C   . ALA A 1 136 ? 12.357  -11.091 35.319  1.00 34.71 ? 135  ALA A C   1 
ATOM   1095 O  O   . ALA A 1 136 ? 12.352  -12.102 36.028  1.00 35.97 ? 135  ALA A O   1 
ATOM   1096 C  CB  . ALA A 1 136 ? 13.455  -9.251  36.611  1.00 31.75 ? 135  ALA A CB  1 
ATOM   1097 N  N   . ASP A 1 137 ? 12.513  -11.139 34.001  1.00 34.57 ? 136  ASP A N   1 
ATOM   1098 C  CA  . ASP A 1 137 ? 12.833  -12.392 33.326  1.00 39.31 ? 136  ASP A CA  1 
ATOM   1099 C  C   . ASP A 1 137 ? 11.694  -13.410 33.361  1.00 36.88 ? 136  ASP A C   1 
ATOM   1100 O  O   . ASP A 1 137 ? 11.860  -14.532 32.870  1.00 39.66 ? 136  ASP A O   1 
ATOM   1101 C  CB  . ASP A 1 137 ? 14.110  -12.995 33.916  1.00 45.60 ? 136  ASP A CB  1 
ATOM   1102 C  CG  . ASP A 1 137 ? 15.350  -12.184 33.565  1.00 49.88 ? 136  ASP A CG  1 
ATOM   1103 O  OD1 . ASP A 1 137 ? 15.374  -11.587 32.464  1.00 51.74 ? 136  ASP A OD1 1 
ATOM   1104 O  OD2 . ASP A 1 137 ? 16.293  -12.137 34.384  1.00 52.60 ? 136  ASP A OD2 1 
ATOM   1105 N  N   . GLU A 1 138 ? 10.543  -13.055 33.935  1.00 30.50 ? 137  GLU A N   1 
ATOM   1106 C  CA  . GLU A 1 138 ? 9.337   -13.771 33.549  1.00 23.54 ? 137  GLU A CA  1 
ATOM   1107 C  C   . GLU A 1 138 ? 8.991   -13.390 32.115  1.00 21.24 ? 137  GLU A C   1 
ATOM   1108 O  O   . GLU A 1 138 ? 9.479   -12.395 31.582  1.00 24.32 ? 137  GLU A O   1 
ATOM   1109 C  CB  . GLU A 1 138 ? 8.170   -13.465 34.499  1.00 20.52 ? 137  GLU A CB  1 
ATOM   1110 C  CG  . GLU A 1 138 ? 8.409   -14.040 35.892  1.00 22.04 ? 137  GLU A CG  1 
ATOM   1111 C  CD  . GLU A 1 138 ? 7.306   -13.741 36.891  1.00 23.56 ? 137  GLU A CD  1 
ATOM   1112 O  OE1 . GLU A 1 138 ? 6.385   -12.967 36.573  1.00 21.06 ? 137  GLU A OE1 1 
ATOM   1113 O  OE2 . GLU A 1 138 ? 7.369   -14.292 38.012  1.00 30.36 ? 137  GLU A OE2 1 
ATOM   1114 N  N   . HIS A 1 139 ? 8.170   -14.205 31.472  1.00 18.64 ? 138  HIS A N   1 
ATOM   1115 C  CA  . HIS A 1 139 ? 7.822   -13.940 30.083  1.00 20.25 ? 138  HIS A CA  1 
ATOM   1116 C  C   . HIS A 1 139 ? 6.311   -13.934 29.909  1.00 18.88 ? 138  HIS A C   1 
ATOM   1117 O  O   . HIS A 1 139 ? 5.551   -14.254 30.823  1.00 18.59 ? 138  HIS A O   1 
ATOM   1118 C  CB  . HIS A 1 139 ? 8.467   -14.964 29.140  1.00 20.98 ? 138  HIS A CB  1 
ATOM   1119 C  CG  . HIS A 1 139 ? 8.011   -16.368 29.370  1.00 21.45 ? 138  HIS A CG  1 
ATOM   1120 N  ND1 . HIS A 1 139 ? 8.759   -17.288 30.071  1.00 26.10 ? 138  HIS A ND1 1 
ATOM   1121 C  CD2 . HIS A 1 139 ? 6.881   -17.011 28.990  1.00 23.55 ? 138  HIS A CD2 1 
ATOM   1122 C  CE1 . HIS A 1 139 ? 8.111   -18.439 30.111  1.00 28.45 ? 138  HIS A CE1 1 
ATOM   1123 N  NE2 . HIS A 1 139 ? 6.969   -18.297 29.461  1.00 25.32 ? 138  HIS A NE2 1 
ATOM   1124 N  N   . ILE A 1 140 ? 5.894   -13.557 28.702  1.00 16.44 ? 139  ILE A N   1 
ATOM   1125 C  CA  . ILE A 1 140 ? 4.494   -13.466 28.306  1.00 15.75 ? 139  ILE A CA  1 
ATOM   1126 C  C   . ILE A 1 140 ? 4.175   -14.649 27.405  1.00 15.91 ? 139  ILE A C   1 
ATOM   1127 O  O   . ILE A 1 140 ? 4.923   -14.931 26.459  1.00 15.94 ? 139  ILE A O   1 
ATOM   1128 C  CB  . ILE A 1 140 ? 4.216   -12.143 27.574  1.00 15.61 ? 139  ILE A CB  1 
ATOM   1129 C  CG1 . ILE A 1 140 ? 4.302   -10.962 28.541  1.00 16.05 ? 139  ILE A CG1 1 
ATOM   1130 C  CG2 . ILE A 1 140 ? 2.876   -12.196 26.843  1.00 15.94 ? 139  ILE A CG2 1 
ATOM   1131 C  CD1 . ILE A 1 140 ? 4.508   -9.637  27.850  1.00 18.31 ? 139  ILE A CD1 1 
ATOM   1132 N  N   . GLU A 1 141 ? 3.074   -15.341 27.700  1.00 17.05 ? 140  GLU A N   1 
ATOM   1133 C  CA  . GLU A 1 141 ? 2.512   -16.357 26.809  1.00 17.00 ? 140  GLU A CA  1 
ATOM   1134 C  C   . GLU A 1 141 ? 1.522   -15.631 25.901  1.00 15.09 ? 140  GLU A C   1 
ATOM   1135 O  O   . GLU A 1 141 ? 0.419   -15.279 26.324  1.00 14.78 ? 140  GLU A O   1 
ATOM   1136 C  CB  . GLU A 1 141 ? 1.855   -17.477 27.614  1.00 18.18 ? 140  GLU A CB  1 
ATOM   1137 C  CG  . GLU A 1 141 ? 2.827   -18.242 28.513  1.00 20.60 ? 140  GLU A CG  1 
ATOM   1138 C  CD  . GLU A 1 141 ? 2.161   -19.340 29.333  1.00 26.21 ? 140  GLU A CD  1 
ATOM   1139 O  OE1 . GLU A 1 141 ? 0.933   -19.274 29.558  1.00 26.67 ? 140  GLU A OE1 1 
ATOM   1140 O  OE2 . GLU A 1 141 ? 2.873   -20.271 29.778  1.00 29.94 ? 140  GLU A OE2 1 
ATOM   1141 N  N   . VAL A 1 142 ? 1.919   -15.380 24.653  1.00 12.70 ? 141  VAL A N   1 
ATOM   1142 C  CA  . VAL A 1 142 ? 1.222   -14.386 23.829  1.00 13.58 ? 141  VAL A CA  1 
ATOM   1143 C  C   . VAL A 1 142 ? -0.175  -14.856 23.417  1.00 13.80 ? 141  VAL A C   1 
ATOM   1144 O  O   . VAL A 1 142 ? -1.167  -14.178 23.741  1.00 13.77 ? 141  VAL A O   1 
ATOM   1145 C  CB  . VAL A 1 142 ? 2.068   -14.002 22.601  1.00 11.69 ? 141  VAL A CB  1 
ATOM   1146 C  CG1 . VAL A 1 142 ? 1.254   -13.141 21.628  1.00 14.84 ? 141  VAL A CG1 1 
ATOM   1147 C  CG2 . VAL A 1 142 ? 3.360   -13.273 23.029  1.00 12.57 ? 141  VAL A CG2 1 
ATOM   1148 N  N   . PRO A 1 143 ? -0.332  -15.961 22.681  1.00 14.42 ? 142  PRO A N   1 
ATOM   1149 C  CA  . PRO A 1 143 ? -1.703  -16.357 22.299  1.00 14.40 ? 142  PRO A CA  1 
ATOM   1150 C  C   . PRO A 1 143 ? -2.603  -16.588 23.503  1.00 13.66 ? 142  PRO A C   1 
ATOM   1151 O  O   . PRO A 1 143 ? -3.813  -16.312 23.438  1.00 12.64 ? 142  PRO A O   1 
ATOM   1152 C  CB  . PRO A 1 143 ? -1.497  -17.640 21.475  1.00 14.11 ? 142  PRO A CB  1 
ATOM   1153 C  CG  . PRO A 1 143 ? -0.072  -18.088 21.773  1.00 15.80 ? 142  PRO A CG  1 
ATOM   1154 C  CD  . PRO A 1 143 ? 0.693   -16.832 22.083  1.00 16.20 ? 142  PRO A CD  1 
ATOM   1155 N  N   . GLU A 1 144 ? -2.038  -17.053 24.617  1.00 13.17 ? 143  GLU A N   1 
ATOM   1156 C  CA  . GLU A 1 144 ? -2.839  -17.247 25.819  1.00 12.61 ? 143  GLU A CA  1 
ATOM   1157 C  C   . GLU A 1 144 ? -3.409  -15.919 26.321  1.00 12.82 ? 143  GLU A C   1 
ATOM   1158 O  O   . GLU A 1 144 ? -4.607  -15.814 26.614  1.00 12.79 ? 143  GLU A O   1 
ATOM   1159 C  CB  . GLU A 1 144 ? -1.992  -17.928 26.899  1.00 14.54 ? 143  GLU A CB  1 
ATOM   1160 C  CG  . GLU A 1 144 ? -1.691  -19.416 26.625  1.00 16.90 ? 143  GLU A CG  1 
ATOM   1161 C  CD  . GLU A 1 144 ? -0.577  -19.677 25.604  1.00 18.51 ? 143  GLU A CD  1 
ATOM   1162 O  OE1 . GLU A 1 144 ? 0.095   -18.733 25.135  1.00 15.37 ? 143  GLU A OE1 1 
ATOM   1163 O  OE2 . GLU A 1 144 ? -0.367  -20.861 25.267  1.00 21.33 ? 143  GLU A OE2 1 
ATOM   1164 N  N   . ASP A 1 145 ? -2.562  -14.888 26.427  1.00 13.54 ? 144  ASP A N   1 
ATOM   1165 C  CA  . ASP A 1 145 ? -3.035  -13.596 26.917  1.00 12.58 ? 144  ASP A CA  1 
ATOM   1166 C  C   . ASP A 1 145 ? -3.894  -12.869 25.884  1.00 12.91 ? 144  ASP A C   1 
ATOM   1167 O  O   . ASP A 1 145 ? -4.798  -12.108 26.255  1.00 12.62 ? 144  ASP A O   1 
ATOM   1168 C  CB  . ASP A 1 145 ? -1.850  -12.716 27.343  1.00 13.60 ? 144  ASP A CB  1 
ATOM   1169 C  CG  . ASP A 1 145 ? -1.405  -12.978 28.789  1.00 14.93 ? 144  ASP A CG  1 
ATOM   1170 O  OD1 . ASP A 1 145 ? -2.153  -13.657 29.544  1.00 14.66 ? 144  ASP A OD1 1 
ATOM   1171 O  OD2 . ASP A 1 145 ? -0.311  -12.499 29.167  1.00 15.87 ? 144  ASP A OD2 1 
ATOM   1172 N  N   . MET A 1 146 ? -3.628  -13.051 24.589  1.00 11.06 ? 145  MET A N   1 
ATOM   1173 C  CA  . MET A 1 146 ? -4.514  -12.422 23.613  1.00 11.20 ? 145  MET A CA  1 
ATOM   1174 C  C   . MET A 1 146 ? -5.906  -13.051 23.643  1.00 10.63 ? 145  MET A C   1 
ATOM   1175 O  O   . MET A 1 146 ? -6.904  -12.361 23.395  1.00 11.37 ? 145  MET A O   1 
ATOM   1176 C  CB  . MET A 1 146 ? -3.915  -12.510 22.203  1.00 11.99 ? 145  MET A CB  1 
ATOM   1177 C  CG  . MET A 1 146 ? -2.577  -11.788 22.026  1.00 14.06 ? 145  MET A CG  1 
ATOM   1178 S  SD  . MET A 1 146 ? -2.665  -10.031 22.440  1.00 16.15 ? 145  MET A SD  1 
ATOM   1179 C  CE  . MET A 1 146 ? -2.111  -10.043 24.149  1.00 19.43 ? 145  MET A CE  1 
ATOM   1180 N  N   . THR A 1 147 ? -5.992  -14.347 23.957  1.00 10.25 ? 146  THR A N   1 
ATOM   1181 C  CA  . THR A 1 147 ? -7.290  -15.008 24.062  1.00 11.67 ? 146  THR A CA  1 
ATOM   1182 C  C   . THR A 1 147 ? -8.019  -14.575 25.325  1.00 11.67 ? 146  THR A C   1 
ATOM   1183 O  O   . THR A 1 147 ? -9.246  -14.409 25.314  1.00 12.31 ? 146  THR A O   1 
ATOM   1184 C  CB  . THR A 1 147 ? -7.099  -16.528 24.027  1.00 14.47 ? 146  THR A CB  1 
ATOM   1185 O  OG1 . THR A 1 147 ? -6.634  -16.915 22.727  1.00 17.44 ? 146  THR A OG1 1 
ATOM   1186 C  CG2 . THR A 1 147 ? -8.408  -17.284 24.350  1.00 15.80 ? 146  THR A CG2 1 
ATOM   1187 N  N   . ARG A 1 148 ? -7.281  -14.378 26.424  1.00 12.63 ? 147  ARG A N   1 
ATOM   1188 C  CA  . ARG A 1 148 ? -7.883  -13.768 27.609  1.00 12.31 ? 147  ARG A CA  1 
ATOM   1189 C  C   . ARG A 1 148 ? -8.513  -12.428 27.260  1.00 13.61 ? 147  ARG A C   1 
ATOM   1190 O  O   . ARG A 1 148 ? -9.660  -12.148 27.633  1.00 13.33 ? 147  ARG A O   1 
ATOM   1191 C  CB  . ARG A 1 148 ? -6.834  -13.583 28.715  1.00 14.42 ? 147  ARG A CB  1 
ATOM   1192 C  CG  . ARG A 1 148 ? -6.386  -14.855 29.411  1.00 14.84 ? 147  ARG A CG  1 
ATOM   1193 C  CD  . ARG A 1 148 ? -5.402  -14.523 30.533  1.00 16.63 ? 147  ARG A CD  1 
ATOM   1194 N  NE  . ARG A 1 148 ? -5.104  -15.674 31.377  1.00 16.33 ? 147  ARG A NE  1 
ATOM   1195 C  CZ  . ARG A 1 148 ? -4.078  -16.495 31.197  1.00 17.56 ? 147  ARG A CZ  1 
ATOM   1196 N  NH1 . ARG A 1 148 ? -3.222  -16.332 30.194  1.00 16.38 ? 147  ARG A NH1 1 
ATOM   1197 N  NH2 . ARG A 1 148 ? -3.899  -17.501 32.046  1.00 21.82 ? 147  ARG A NH2 1 
ATOM   1198 N  N   . LEU A 1 149 ? -7.766  -11.584 26.540  1.00 13.60 ? 148  LEU A N   1 
ATOM   1199 C  CA  . LEU A 1 149 ? -8.250  -10.253 26.193  1.00 12.71 ? 148  LEU A CA  1 
ATOM   1200 C  C   . LEU A 1 149 ? -9.485  -10.310 25.294  1.00 12.57 ? 148  LEU A C   1 
ATOM   1201 O  O   . LEU A 1 149 ? -10.508 -9.682  25.593  1.00 12.80 ? 148  LEU A O   1 
ATOM   1202 C  CB  . LEU A 1 149 ? -7.132  -9.451  25.518  1.00 15.25 ? 148  LEU A CB  1 
ATOM   1203 C  CG  . LEU A 1 149 ? -7.634  -8.100  24.987  1.00 16.71 ? 148  LEU A CG  1 
ATOM   1204 C  CD1 . LEU A 1 149 ? -6.995  -6.931  25.708  1.00 17.22 ? 148  LEU A CD1 1 
ATOM   1205 C  CD2 . LEU A 1 149 ? -7.428  -7.987  23.492  1.00 23.75 ? 148  LEU A CD2 1 
ATOM   1206 N  N   . THR A 1 150 ? -9.411  -11.031 24.169  1.00 11.48 ? 149  THR A N   1 
ATOM   1207 C  CA  . THR A 1 150 ? -10.515 -10.929 23.213  1.00 11.10 ? 149  THR A CA  1 
ATOM   1208 C  C   . THR A 1 150 ? -11.783 -11.614 23.719  1.00 12.86 ? 149  THR A C   1 
ATOM   1209 O  O   . THR A 1 150 ? -12.894 -11.145 23.427  1.00 11.80 ? 149  THR A O   1 
ATOM   1210 C  CB  . THR A 1 150 ? -10.120 -11.498 21.846  1.00 11.57 ? 149  THR A CB  1 
ATOM   1211 O  OG1 . THR A 1 150 ? -9.809  -12.890 21.964  1.00 11.37 ? 149  THR A OG1 1 
ATOM   1212 C  CG2 . THR A 1 150 ? -8.934  -10.726 21.242  1.00 11.62 ? 149  THR A CG2 1 
ATOM   1213 N  N   . LEU A 1 151 ? -11.658 -12.718 24.463  1.00 10.92 ? 150  LEU A N   1 
ATOM   1214 C  CA  . LEU A 1 151 ? -12.852 -13.314 25.050  1.00 12.39 ? 150  LEU A CA  1 
ATOM   1215 C  C   . LEU A 1 151 ? -13.499 -12.350 26.038  1.00 11.67 ? 150  LEU A C   1 
ATOM   1216 O  O   . LEU A 1 151 ? -14.720 -12.158 26.029  1.00 12.45 ? 150  LEU A O   1 
ATOM   1217 C  CB  . LEU A 1 151 ? -12.509 -14.636 25.750  1.00 12.86 ? 150  LEU A CB  1 
ATOM   1218 C  CG  . LEU A 1 151 ? -13.728 -15.240 26.450  1.00 15.78 ? 150  LEU A CG  1 
ATOM   1219 C  CD1 . LEU A 1 151 ? -14.692 -15.781 25.404  1.00 15.99 ? 150  LEU A CD1 1 
ATOM   1220 C  CD2 . LEU A 1 151 ? -13.354 -16.311 27.476  1.00 16.63 ? 150  LEU A CD2 1 
ATOM   1221 N  N   . ASP A 1 152 ? -12.692 -11.712 26.887  1.00 12.12 ? 151  ASP A N   1 
ATOM   1222 C  CA  . ASP A 1 152 ? -13.269 -10.777 27.850  1.00 11.04 ? 151  ASP A CA  1 
ATOM   1223 C  C   . ASP A 1 152 ? -13.908 -9.592  27.144  1.00 9.89  ? 151  ASP A C   1 
ATOM   1224 O  O   . ASP A 1 152 ? -14.942 -9.079  27.588  1.00 13.66 ? 151  ASP A O   1 
ATOM   1225 C  CB  . ASP A 1 152 ? -12.205 -10.298 28.841  1.00 13.23 ? 151  ASP A CB  1 
ATOM   1226 C  CG  . ASP A 1 152 ? -12.017 -11.258 30.005  1.00 17.59 ? 151  ASP A CG  1 
ATOM   1227 O  OD1 . ASP A 1 152 ? -12.273 -12.465 29.827  1.00 18.16 ? 151  ASP A OD1 1 
ATOM   1228 O  OD2 . ASP A 1 152 ? -11.613 -10.809 31.096  1.00 19.68 ? 151  ASP A OD2 1 
ATOM   1229 N  N   . THR A 1 153 ? -13.317 -9.148  26.032  1.00 10.88 ? 152  THR A N   1 
ATOM   1230 C  CA  . THR A 1 153 ? -13.864 -7.990  25.334  1.00 13.88 ? 152  THR A CA  1 
ATOM   1231 C  C   . THR A 1 153 ? -15.233 -8.291  24.726  1.00 13.48 ? 152  THR A C   1 
ATOM   1232 O  O   . THR A 1 153 ? -16.171 -7.496  24.868  1.00 13.06 ? 152  THR A O   1 
ATOM   1233 C  CB  . THR A 1 153 ? -12.878 -7.515  24.269  1.00 12.07 ? 152  THR A CB  1 
ATOM   1234 O  OG1 . THR A 1 153 ? -11.678 -7.090  24.925  1.00 13.81 ? 152  THR A OG1 1 
ATOM   1235 C  CG2 . THR A 1 153 ? -13.459 -6.347  23.479  1.00 12.56 ? 152  THR A CG2 1 
ATOM   1236 N  N   . ILE A 1 154 ? -15.381 -9.425  24.038  1.00 11.79 ? 153  ILE A N   1 
ATOM   1237 C  CA  . ILE A 1 154 ? -16.694 -9.683  23.456  1.00 11.77 ? 153  ILE A CA  1 
ATOM   1238 C  C   . ILE A 1 154 ? -17.713 -9.963  24.563  1.00 12.93 ? 153  ILE A C   1 
ATOM   1239 O  O   . ILE A 1 154 ? -18.881 -9.577  24.449  1.00 13.76 ? 153  ILE A O   1 
ATOM   1240 C  CB  . ILE A 1 154 ? -16.631 -10.809 22.399  1.00 13.19 ? 153  ILE A CB  1 
ATOM   1241 C  CG1 . ILE A 1 154 ? -17.973 -10.943 21.656  1.00 14.34 ? 153  ILE A CG1 1 
ATOM   1242 C  CG2 . ILE A 1 154 ? -16.253 -12.154 23.003  1.00 13.44 ? 153  ILE A CG2 1 
ATOM   1243 C  CD1 . ILE A 1 154 ? -18.400 -9.692  20.894  1.00 16.14 ? 153  ILE A CD1 1 
ATOM   1244 N  N   . GLY A 1 155 ? -17.286 -10.571 25.672  1.00 12.70 ? 154  GLY A N   1 
ATOM   1245 C  CA  . GLY A 1 155 ? -18.223 -10.813 26.764  1.00 14.27 ? 154  GLY A CA  1 
ATOM   1246 C  C   . GLY A 1 155 ? -18.758 -9.524  27.366  1.00 14.68 ? 154  GLY A C   1 
ATOM   1247 O  O   . GLY A 1 155 ? -19.965 -9.370  27.587  1.00 14.25 ? 154  GLY A O   1 
ATOM   1248 N  N   . LEU A 1 156 ? -17.862 -8.578  27.647  1.00 15.02 ? 155  LEU A N   1 
ATOM   1249 C  CA  . LEU A 1 156 ? -18.254 -7.328  28.290  1.00 14.39 ? 155  LEU A CA  1 
ATOM   1250 C  C   . LEU A 1 156 ? -18.955 -6.381  27.319  1.00 14.47 ? 155  LEU A C   1 
ATOM   1251 O  O   . LEU A 1 156 ? -20.040 -5.865  27.614  1.00 16.05 ? 155  LEU A O   1 
ATOM   1252 C  CB  . LEU A 1 156 ? -17.023 -6.658  28.899  1.00 14.26 ? 155  LEU A CB  1 
ATOM   1253 C  CG  . LEU A 1 156 ? -17.264 -5.384  29.702  1.00 13.68 ? 155  LEU A CG  1 
ATOM   1254 C  CD1 . LEU A 1 156 ? -18.231 -5.663  30.840  1.00 15.23 ? 155  LEU A CD1 1 
ATOM   1255 C  CD2 . LEU A 1 156 ? -15.933 -4.878  30.239  1.00 14.93 ? 155  LEU A CD2 1 
ATOM   1256 N  N   . CYS A 1 157 ? -18.342 -6.125  26.159  1.00 14.18 ? 156  CYS A N   1 
ATOM   1257 C  CA  . CYS A 1 157 ? -18.948 -5.216  25.187  1.00 14.30 ? 156  CYS A CA  1 
ATOM   1258 C  C   . CYS A 1 157 ? -20.275 -5.748  24.665  1.00 15.60 ? 156  CYS A C   1 
ATOM   1259 O  O   . CYS A 1 157 ? -21.237 -4.987  24.491  1.00 16.92 ? 156  CYS A O   1 
ATOM   1260 C  CB  . CYS A 1 157 ? -17.989 -4.984  24.015  1.00 13.23 ? 156  CYS A CB  1 
ATOM   1261 S  SG  . CYS A 1 157 ? -16.474 -4.102  24.466  1.00 17.88 ? 156  CYS A SG  1 
ATOM   1262 N  N   . GLY A 1 158 ? -20.334 -7.044  24.362  1.00 16.06 ? 157  GLY A N   1 
ATOM   1263 C  CA  . GLY A 1 158 ? -21.517 -7.591  23.729  1.00 15.40 ? 157  GLY A CA  1 
ATOM   1264 C  C   . GLY A 1 158 ? -22.631 -7.966  24.682  1.00 16.63 ? 157  GLY A C   1 
ATOM   1265 O  O   . GLY A 1 158 ? -23.808 -7.861  24.322  1.00 19.45 ? 157  GLY A O   1 
ATOM   1266 N  N   . PHE A 1 159 ? -22.295 -8.405  25.900  1.00 17.25 ? 158  PHE A N   1 
ATOM   1267 C  CA  . PHE A 1 159 ? -23.282 -9.035  26.771  1.00 16.16 ? 158  PHE A CA  1 
ATOM   1268 C  C   . PHE A 1 159 ? -23.239 -8.562  28.218  1.00 17.47 ? 158  PHE A C   1 
ATOM   1269 O  O   . PHE A 1 159 ? -23.996 -9.089  29.044  1.00 17.74 ? 158  PHE A O   1 
ATOM   1270 C  CB  . PHE A 1 159 ? -23.106 -10.560 26.716  1.00 18.79 ? 158  PHE A CB  1 
ATOM   1271 C  CG  . PHE A 1 159 ? -23.089 -11.093 25.310  1.00 15.40 ? 158  PHE A CG  1 
ATOM   1272 C  CD1 . PHE A 1 159 ? -24.280 -11.306 24.633  1.00 14.07 ? 158  PHE A CD1 1 
ATOM   1273 C  CD2 . PHE A 1 159 ? -21.891 -11.316 24.645  1.00 17.25 ? 158  PHE A CD2 1 
ATOM   1274 C  CE1 . PHE A 1 159 ? -24.288 -11.764 23.330  1.00 15.29 ? 158  PHE A CE1 1 
ATOM   1275 C  CE2 . PHE A 1 159 ? -21.886 -11.785 23.328  1.00 17.26 ? 158  PHE A CE2 1 
ATOM   1276 C  CZ  . PHE A 1 159 ? -23.085 -12.010 22.673  1.00 17.78 ? 158  PHE A CZ  1 
ATOM   1277 N  N   . ASN A 1 160 ? -22.402 -7.583  28.544  1.00 17.36 ? 159  ASN A N   1 
ATOM   1278 C  CA  . ASN A 1 160 ? -22.245 -7.091  29.910  1.00 17.24 ? 159  ASN A CA  1 
ATOM   1279 C  C   . ASN A 1 160 ? -21.936 -8.226  30.883  1.00 17.72 ? 159  ASN A C   1 
ATOM   1280 O  O   . ASN A 1 160 ? -22.406 -8.238  32.027  1.00 18.32 ? 159  ASN A O   1 
ATOM   1281 C  CB  . ASN A 1 160 ? -23.477 -6.303  30.363  1.00 19.84 ? 159  ASN A CB  1 
ATOM   1282 C  CG  . ASN A 1 160 ? -23.144 -5.305  31.458  1.00 24.99 ? 159  ASN A CG  1 
ATOM   1283 O  OD1 . ASN A 1 160 ? -21.995 -4.880  31.587  1.00 23.76 ? 159  ASN A OD1 1 
ATOM   1284 N  ND2 . ASN A 1 160 ? -24.141 -4.933  32.260  1.00 29.12 ? 159  ASN A ND2 1 
ATOM   1285 N  N   . TYR A 1 161 ? -21.129 -9.188  30.430  1.00 15.77 ? 160  TYR A N   1 
ATOM   1286 C  CA  . TYR A 1 161 ? -20.729 -10.330 31.244  1.00 13.79 ? 160  TYR A CA  1 
ATOM   1287 C  C   . TYR A 1 161 ? -19.212 -10.345 31.356  1.00 14.16 ? 160  TYR A C   1 
ATOM   1288 O  O   . TYR A 1 161 ? -18.517 -10.170 30.350  1.00 14.93 ? 160  TYR A O   1 
ATOM   1289 C  CB  . TYR A 1 161 ? -21.235 -11.638 30.630  1.00 14.64 ? 160  TYR A CB  1 
ATOM   1290 C  CG  . TYR A 1 161 ? -20.971 -12.842 31.496  1.00 17.91 ? 160  TYR A CG  1 
ATOM   1291 C  CD1 . TYR A 1 161 ? -21.822 -13.157 32.547  1.00 18.78 ? 160  TYR A CD1 1 
ATOM   1292 C  CD2 . TYR A 1 161 ? -19.866 -13.659 31.273  1.00 18.95 ? 160  TYR A CD2 1 
ATOM   1293 C  CE1 . TYR A 1 161 ? -21.589 -14.254 33.352  1.00 20.91 ? 160  TYR A CE1 1 
ATOM   1294 C  CE2 . TYR A 1 161 ? -19.620 -14.766 32.080  1.00 21.31 ? 160  TYR A CE2 1 
ATOM   1295 C  CZ  . TYR A 1 161 ? -20.491 -15.056 33.119  1.00 23.59 ? 160  TYR A CZ  1 
ATOM   1296 O  OH  . TYR A 1 161 ? -20.276 -16.142 33.939  1.00 25.05 ? 160  TYR A OH  1 
ATOM   1297 N  N   . ARG A 1 162 ? -18.691 -10.541 32.575  1.00 12.62 ? 161  ARG A N   1 
ATOM   1298 C  CA  . ARG A 1 162 ? -17.245 -10.556 32.802  1.00 13.10 ? 161  ARG A CA  1 
ATOM   1299 C  C   . ARG A 1 162 ? -16.759 -11.999 32.933  1.00 12.87 ? 161  ARG A C   1 
ATOM   1300 O  O   . ARG A 1 162 ? -17.034 -12.671 33.934  1.00 15.49 ? 161  ARG A O   1 
ATOM   1301 C  CB  . ARG A 1 162 ? -16.872 -9.731  34.032  1.00 14.09 ? 161  ARG A CB  1 
ATOM   1302 C  CG  . ARG A 1 162 ? -16.947 -8.220  33.770  1.00 15.24 ? 161  ARG A CG  1 
ATOM   1303 C  CD  . ARG A 1 162 ? -16.523 -7.368  34.938  1.00 16.18 ? 161  ARG A CD  1 
ATOM   1304 N  NE  . ARG A 1 162 ? -16.681 -5.952  34.623  1.00 15.28 ? 161  ARG A NE  1 
ATOM   1305 C  CZ  . ARG A 1 162 ? -15.733 -5.183  34.102  1.00 13.68 ? 161  ARG A CZ  1 
ATOM   1306 N  NH1 . ARG A 1 162 ? -14.518 -5.649  33.853  1.00 12.75 ? 161  ARG A NH1 1 
ATOM   1307 N  NH2 . ARG A 1 162 ? -16.005 -3.906  33.846  1.00 15.05 ? 161  ARG A NH2 1 
ATOM   1308 N  N   . PHE A 1 163 ? -16.034 -12.476 31.916  1.00 12.33 ? 162  PHE A N   1 
ATOM   1309 C  CA  . PHE A 1 163 ? -15.380 -13.775 32.016  1.00 12.77 ? 162  PHE A CA  1 
ATOM   1310 C  C   . PHE A 1 163 ? -14.208 -13.753 32.994  1.00 13.39 ? 162  PHE A C   1 
ATOM   1311 O  O   . PHE A 1 163 ? -13.796 -14.814 33.474  1.00 15.85 ? 162  PHE A O   1 
ATOM   1312 C  CB  . PHE A 1 163 ? -14.894 -14.235 30.633  1.00 14.22 ? 162  PHE A CB  1 
ATOM   1313 C  CG  . PHE A 1 163 ? -15.995 -14.660 29.702  1.00 16.15 ? 162  PHE A CG  1 
ATOM   1314 C  CD1 . PHE A 1 163 ? -16.552 -15.926 29.802  1.00 19.34 ? 162  PHE A CD1 1 
ATOM   1315 C  CD2 . PHE A 1 163 ? -16.442 -13.809 28.697  1.00 15.11 ? 162  PHE A CD2 1 
ATOM   1316 C  CE1 . PHE A 1 163 ? -17.564 -16.329 28.937  1.00 20.55 ? 162  PHE A CE1 1 
ATOM   1317 C  CE2 . PHE A 1 163 ? -17.449 -14.205 27.827  1.00 15.69 ? 162  PHE A CE2 1 
ATOM   1318 C  CZ  . PHE A 1 163 ? -18.012 -15.471 27.948  1.00 18.49 ? 162  PHE A CZ  1 
ATOM   1319 N  N   . ASN A 1 164 ? -13.662 -12.575 33.288  1.00 13.01 ? 163  ASN A N   1 
ATOM   1320 C  CA  . ASN A 1 164 ? -12.575 -12.421 34.259  1.00 11.85 ? 163  ASN A CA  1 
ATOM   1321 C  C   . ASN A 1 164 ? -11.394 -13.341 33.939  1.00 14.16 ? 163  ASN A C   1 
ATOM   1322 O  O   . ASN A 1 164 ? -10.807 -13.993 34.811  1.00 13.84 ? 163  ASN A O   1 
ATOM   1323 C  CB  . ASN A 1 164 ? -13.114 -12.630 35.675  1.00 13.81 ? 163  ASN A CB  1 
ATOM   1324 C  CG  . ASN A 1 164 ? -13.920 -11.439 36.139  1.00 12.86 ? 163  ASN A CG  1 
ATOM   1325 O  OD1 . ASN A 1 164 ? -13.486 -10.298 35.966  1.00 15.09 ? 163  ASN A OD1 1 
ATOM   1326 N  ND2 . ASN A 1 164 ? -15.112 -11.682 36.687  1.00 12.80 ? 163  ASN A ND2 1 
ATOM   1327 N  N   . SER A 1 165 ? -11.011 -13.351 32.659  1.00 13.17 ? 164  SER A N   1 
ATOM   1328 C  CA  . SER A 1 165 ? -9.986  -14.286 32.215  1.00 12.55 ? 164  SER A CA  1 
ATOM   1329 C  C   . SER A 1 165 ? -8.624  -13.974 32.813  1.00 14.54 ? 164  SER A C   1 
ATOM   1330 O  O   . SER A 1 165 ? -7.792  -14.879 32.935  1.00 15.13 ? 164  SER A O   1 
ATOM   1331 C  CB  . SER A 1 165 ? -9.889  -14.289 30.691  1.00 13.96 ? 164  SER A CB  1 
ATOM   1332 O  OG  . SER A 1 165 ? -11.085 -14.787 30.123  1.00 14.01 ? 164  SER A OG  1 
ATOM   1333 N  N   . PHE A 1 166 ? -8.363  -12.710 33.156  1.00 14.32 ? 165  PHE A N   1 
ATOM   1334 C  CA  . PHE A 1 166 ? -7.085  -12.352 33.762  1.00 14.36 ? 165  PHE A CA  1 
ATOM   1335 C  C   . PHE A 1 166 ? -7.030  -12.690 35.241  1.00 16.86 ? 165  PHE A C   1 
ATOM   1336 O  O   . PHE A 1 166 ? -5.990  -12.465 35.877  1.00 19.28 ? 165  PHE A O   1 
ATOM   1337 C  CB  . PHE A 1 166 ? -6.788  -10.869 33.542  1.00 15.40 ? 165  PHE A CB  1 
ATOM   1338 C  CG  . PHE A 1 166 ? -6.465  -10.541 32.116  1.00 14.42 ? 165  PHE A CG  1 
ATOM   1339 C  CD1 . PHE A 1 166 ? -5.273  -10.969 31.548  1.00 14.18 ? 165  PHE A CD1 1 
ATOM   1340 C  CD2 . PHE A 1 166 ? -7.370  -9.854  31.325  1.00 12.78 ? 165  PHE A CD2 1 
ATOM   1341 C  CE1 . PHE A 1 166 ? -4.973  -10.687 30.214  1.00 15.15 ? 165  PHE A CE1 1 
ATOM   1342 C  CE2 . PHE A 1 166 ? -7.080  -9.566  30.002  1.00 15.34 ? 165  PHE A CE2 1 
ATOM   1343 C  CZ  . PHE A 1 166 ? -5.885  -9.986  29.444  1.00 14.59 ? 165  PHE A CZ  1 
ATOM   1344 N  N   . TYR A 1 167 ? -8.112  -13.230 35.798  1.00 15.70 ? 166  TYR A N   1 
ATOM   1345 C  CA  . TYR A 1 167 ? -8.108  -13.745 37.158  1.00 16.21 ? 166  TYR A CA  1 
ATOM   1346 C  C   . TYR A 1 167 ? -7.909  -15.257 37.193  1.00 17.03 ? 166  TYR A C   1 
ATOM   1347 O  O   . TYR A 1 167 ? -8.037  -15.863 38.259  1.00 20.39 ? 166  TYR A O   1 
ATOM   1348 C  CB  . TYR A 1 167 ? -9.400  -13.340 37.872  1.00 15.23 ? 166  TYR A CB  1 
ATOM   1349 C  CG  . TYR A 1 167 ? -9.474  -11.848 38.105  1.00 14.38 ? 166  TYR A CG  1 
ATOM   1350 C  CD1 . TYR A 1 167 ? -9.980  -10.989 37.124  1.00 13.05 ? 166  TYR A CD1 1 
ATOM   1351 C  CD2 . TYR A 1 167 ? -8.999  -11.287 39.288  1.00 12.30 ? 166  TYR A CD2 1 
ATOM   1352 C  CE1 . TYR A 1 167 ? -10.021 -9.613  37.324  1.00 13.14 ? 166  TYR A CE1 1 
ATOM   1353 C  CE2 . TYR A 1 167 ? -9.038  -9.917  39.498  1.00 13.90 ? 166  TYR A CE2 1 
ATOM   1354 C  CZ  . TYR A 1 167 ? -9.548  -9.085  38.519  1.00 14.00 ? 166  TYR A CZ  1 
ATOM   1355 O  OH  . TYR A 1 167 ? -9.581  -7.724  38.731  1.00 14.63 ? 166  TYR A OH  1 
ATOM   1356 N  N   . ARG A 1 168 ? -7.574  -15.869 36.051  1.00 18.05 ? 167  ARG A N   1 
ATOM   1357 C  CA  . ARG A 1 168 ? -7.411  -17.315 35.924  1.00 19.63 ? 167  ARG A CA  1 
ATOM   1358 C  C   . ARG A 1 168 ? -6.040  -17.639 35.342  1.00 24.68 ? 167  ARG A C   1 
ATOM   1359 O  O   . ARG A 1 168 ? -5.638  -17.051 34.333  1.00 25.43 ? 167  ARG A O   1 
ATOM   1360 C  CB  . ARG A 1 168 ? -8.498  -17.905 35.012  1.00 20.13 ? 167  ARG A CB  1 
ATOM   1361 C  CG  . ARG A 1 168 ? -9.901  -17.523 35.423  1.00 21.14 ? 167  ARG A CG  1 
ATOM   1362 C  CD  . ARG A 1 168 ? -10.912 -17.848 34.337  1.00 24.21 ? 167  ARG A CD  1 
ATOM   1363 N  NE  . ARG A 1 168 ? -12.214 -17.263 34.630  1.00 27.41 ? 167  ARG A NE  1 
ATOM   1364 C  CZ  . ARG A 1 168 ? -13.190 -17.889 35.272  1.00 30.16 ? 167  ARG A CZ  1 
ATOM   1365 N  NH1 . ARG A 1 168 ? -13.055 -19.142 35.685  1.00 30.74 ? 167  ARG A NH1 1 
ATOM   1366 N  NH2 . ARG A 1 168 ? -14.329 -17.242 35.510  1.00 30.56 ? 167  ARG A NH2 1 
ATOM   1367 N  N   . ASP A 1 169 ? -5.331  -18.588 35.957  1.00 29.57 ? 168  ASP A N   1 
ATOM   1368 C  CA  . ASP A 1 169 ? -4.103  -19.074 35.338  1.00 34.38 ? 168  ASP A CA  1 
ATOM   1369 C  C   . ASP A 1 169 ? -4.372  -20.162 34.308  1.00 36.89 ? 168  ASP A C   1 
ATOM   1370 O  O   . ASP A 1 169 ? -3.473  -20.487 33.525  1.00 39.96 ? 168  ASP A O   1 
ATOM   1371 C  CB  . ASP A 1 169 ? -3.103  -19.576 36.399  1.00 38.92 ? 168  ASP A CB  1 
ATOM   1372 C  CG  . ASP A 1 169 ? -3.723  -20.539 37.398  1.00 44.28 ? 168  ASP A CG  1 
ATOM   1373 O  OD1 . ASP A 1 169 ? -4.609  -20.126 38.176  1.00 45.42 ? 168  ASP A OD1 1 
ATOM   1374 O  OD2 . ASP A 1 169 ? -3.313  -21.717 37.413  1.00 49.52 ? 168  ASP A OD2 1 
ATOM   1375 N  N   . GLN A 1 170 ? -5.579  -20.711 34.283  1.00 37.26 ? 169  GLN A N   1 
ATOM   1376 C  CA  . GLN A 1 170 ? -6.029  -21.659 33.283  1.00 41.15 ? 169  GLN A CA  1 
ATOM   1377 C  C   . GLN A 1 170 ? -7.147  -21.048 32.452  1.00 40.21 ? 169  GLN A C   1 
ATOM   1378 O  O   . GLN A 1 170 ? -7.797  -20.088 32.878  1.00 40.66 ? 169  GLN A O   1 
ATOM   1379 C  CB  . GLN A 1 170 ? -6.526  -22.951 33.942  1.00 46.39 ? 169  GLN A CB  1 
ATOM   1380 C  CG  . GLN A 1 170 ? -5.459  -23.691 34.735  1.00 51.28 ? 169  GLN A CG  1 
ATOM   1381 C  CD  . GLN A 1 170 ? -6.006  -24.917 35.438  1.00 56.33 ? 169  GLN A CD  1 
ATOM   1382 O  OE1 . GLN A 1 170 ? -6.609  -24.816 36.509  1.00 58.60 ? 169  GLN A OE1 1 
ATOM   1383 N  NE2 . GLN A 1 170 ? -5.803  -26.085 34.835  1.00 57.20 ? 169  GLN A NE2 1 
ATOM   1384 N  N   . PRO A 1 171 ? -7.404  -21.578 31.258  1.00 40.70 ? 170  PRO A N   1 
ATOM   1385 C  CA  . PRO A 1 171 ? -8.458  -21.001 30.414  1.00 39.82 ? 170  PRO A CA  1 
ATOM   1386 C  C   . PRO A 1 171 ? -9.823  -21.093 31.079  1.00 38.19 ? 170  PRO A C   1 
ATOM   1387 O  O   . PRO A 1 171 ? -10.086 -21.979 31.898  1.00 37.04 ? 170  PRO A O   1 
ATOM   1388 C  CB  . PRO A 1 171 ? -8.404  -21.853 29.137  1.00 40.84 ? 170  PRO A CB  1 
ATOM   1389 C  CG  . PRO A 1 171 ? -7.053  -22.499 29.151  1.00 39.44 ? 170  PRO A CG  1 
ATOM   1390 C  CD  . PRO A 1 171 ? -6.708  -22.697 30.600  1.00 40.65 ? 170  PRO A CD  1 
ATOM   1391 N  N   . HIS A 1 172 ? -10.699 -20.160 30.714  1.00 35.39 ? 171  HIS A N   1 
ATOM   1392 C  CA  . HIS A 1 172 ? -12.080 -20.245 31.154  1.00 34.54 ? 171  HIS A CA  1 
ATOM   1393 C  C   . HIS A 1 172 ? -12.680 -21.570 30.681  1.00 34.87 ? 171  HIS A C   1 
ATOM   1394 O  O   . HIS A 1 172 ? -12.312 -22.079 29.617  1.00 32.40 ? 171  HIS A O   1 
ATOM   1395 C  CB  . HIS A 1 172 ? -12.894 -19.072 30.607  1.00 33.56 ? 171  HIS A CB  1 
ATOM   1396 C  CG  . HIS A 1 172 ? -14.224 -18.896 31.272  1.00 37.02 ? 171  HIS A CG  1 
ATOM   1397 N  ND1 . HIS A 1 172 ? -15.312 -19.692 30.984  1.00 38.43 ? 171  HIS A ND1 1 
ATOM   1398 C  CD2 . HIS A 1 172 ? -14.642 -18.011 32.208  1.00 37.59 ? 171  HIS A CD2 1 
ATOM   1399 C  CE1 . HIS A 1 172 ? -16.342 -19.308 31.718  1.00 38.18 ? 171  HIS A CE1 1 
ATOM   1400 N  NE2 . HIS A 1 172 ? -15.963 -18.290 32.470  1.00 38.70 ? 171  HIS A NE2 1 
ATOM   1401 N  N   . PRO A 1 173 ? -13.588 -22.162 31.464  1.00 35.78 ? 172  PRO A N   1 
ATOM   1402 C  CA  . PRO A 1 173 ? -14.242 -23.405 31.017  1.00 35.24 ? 172  PRO A CA  1 
ATOM   1403 C  C   . PRO A 1 173 ? -14.831 -23.305 29.621  1.00 31.42 ? 172  PRO A C   1 
ATOM   1404 O  O   . PRO A 1 173 ? -14.806 -24.282 28.857  1.00 29.27 ? 172  PRO A O   1 
ATOM   1405 C  CB  . PRO A 1 173 ? -15.327 -23.619 32.081  1.00 38.59 ? 172  PRO A CB  1 
ATOM   1406 C  CG  . PRO A 1 173 ? -14.784 -22.961 33.291  1.00 38.22 ? 172  PRO A CG  1 
ATOM   1407 C  CD  . PRO A 1 173 ? -14.029 -21.755 32.808  1.00 36.84 ? 172  PRO A CD  1 
ATOM   1408 N  N   . PHE A 1 174 ? -15.367 -22.137 29.266  1.00 28.72 ? 173  PHE A N   1 
ATOM   1409 C  CA  . PHE A 1 174 ? -15.879 -21.947 27.916  1.00 25.89 ? 173  PHE A CA  1 
ATOM   1410 C  C   . PHE A 1 174 ? -14.790 -22.213 26.885  1.00 28.83 ? 173  PHE A C   1 
ATOM   1411 O  O   . PHE A 1 174 ? -14.999 -22.954 25.917  1.00 30.61 ? 173  PHE A O   1 
ATOM   1412 C  CB  . PHE A 1 174 ? -16.435 -20.532 27.770  1.00 28.62 ? 173  PHE A CB  1 
ATOM   1413 C  CG  . PHE A 1 174 ? -17.292 -20.344 26.551  1.00 33.14 ? 173  PHE A CG  1 
ATOM   1414 C  CD1 . PHE A 1 174 ? -18.649 -20.623 26.593  1.00 32.79 ? 173  PHE A CD1 1 
ATOM   1415 C  CD2 . PHE A 1 174 ? -16.739 -19.897 25.363  1.00 36.30 ? 173  PHE A CD2 1 
ATOM   1416 C  CE1 . PHE A 1 174 ? -19.441 -20.453 25.472  1.00 33.54 ? 173  PHE A CE1 1 
ATOM   1417 C  CE2 . PHE A 1 174 ? -17.524 -19.730 24.235  1.00 34.50 ? 173  PHE A CE2 1 
ATOM   1418 C  CZ  . PHE A 1 174 ? -18.879 -20.006 24.291  1.00 35.33 ? 173  PHE A CZ  1 
ATOM   1419 N  N   . ILE A 1 175 ? -13.608 -21.624 27.088  1.00 28.38 ? 174  ILE A N   1 
ATOM   1420 C  CA  . ILE A 1 175 ? -12.517 -21.779 26.127  1.00 28.84 ? 174  ILE A CA  1 
ATOM   1421 C  C   . ILE A 1 175 ? -12.101 -23.245 26.009  1.00 29.30 ? 174  ILE A C   1 
ATOM   1422 O  O   . ILE A 1 175 ? -11.872 -23.756 24.903  1.00 27.24 ? 174  ILE A O   1 
ATOM   1423 C  CB  . ILE A 1 175 ? -11.331 -20.875 26.527  1.00 29.47 ? 174  ILE A CB  1 
ATOM   1424 C  CG1 . ILE A 1 175 ? -11.701 -19.391 26.374  1.00 27.30 ? 174  ILE A CG1 1 
ATOM   1425 C  CG2 . ILE A 1 175 ? -10.074 -21.231 25.728  1.00 28.34 ? 174  ILE A CG2 1 
ATOM   1426 C  CD1 . ILE A 1 175 ? -12.044 -18.965 24.937  1.00 25.23 ? 174  ILE A CD1 1 
ATOM   1427 N  N   . THR A 1 176 ? -11.995 -23.945 27.142  1.00 29.83 ? 175  THR A N   1 
ATOM   1428 C  CA  . THR A 1 176 ? -11.572 -25.342 27.111  1.00 29.32 ? 175  THR A CA  1 
ATOM   1429 C  C   . THR A 1 176 ? -12.541 -26.197 26.303  1.00 27.12 ? 175  THR A C   1 
ATOM   1430 O  O   . THR A 1 176 ? -12.123 -27.039 25.497  1.00 26.76 ? 175  THR A O   1 
ATOM   1431 C  CB  . THR A 1 176 ? -11.449 -25.877 28.536  1.00 31.59 ? 175  THR A CB  1 
ATOM   1432 O  OG1 . THR A 1 176 ? -10.387 -25.189 29.211  1.00 33.39 ? 175  THR A OG1 1 
ATOM   1433 C  CG2 . THR A 1 176 ? -11.165 -27.369 28.524  1.00 34.64 ? 175  THR A CG2 1 
ATOM   1434 N  N   . SER A 1 177 ? -13.842 -26.003 26.518  1.00 25.04 ? 176  SER A N   1 
ATOM   1435 C  CA  . SER A 1 177 ? -14.842 -26.735 25.753  1.00 26.06 ? 176  SER A CA  1 
ATOM   1436 C  C   . SER A 1 177 ? -14.841 -26.308 24.289  1.00 25.20 ? 176  SER A C   1 
ATOM   1437 O  O   . SER A 1 177 ? -14.899 -27.155 23.394  1.00 25.07 ? 176  SER A O   1 
ATOM   1438 C  CB  . SER A 1 177 ? -16.224 -26.529 26.376  1.00 28.88 ? 176  SER A CB  1 
ATOM   1439 O  OG  . SER A 1 177 ? -16.316 -27.217 27.598  1.00 30.22 ? 176  SER A OG  1 
ATOM   1440 N  N   . MET A 1 178 ? -14.785 -24.997 24.026  1.00 20.94 ? 177  MET A N   1 
ATOM   1441 C  CA  . MET A 1 178 ? -14.829 -24.515 22.649  1.00 20.86 ? 177  MET A CA  1 
ATOM   1442 C  C   . MET A 1 178 ? -13.672 -25.078 21.839  1.00 24.53 ? 177  MET A C   1 
ATOM   1443 O  O   . MET A 1 178 ? -13.854 -25.533 20.701  1.00 25.60 ? 177  MET A O   1 
ATOM   1444 C  CB  . MET A 1 178 ? -14.797 -22.982 22.611  1.00 23.37 ? 177  MET A CB  1 
ATOM   1445 C  CG  . MET A 1 178 ? -14.766 -22.431 21.174  1.00 22.56 ? 177  MET A CG  1 
ATOM   1446 S  SD  . MET A 1 178 ? -14.035 -20.788 20.999  1.00 24.29 ? 177  MET A SD  1 
ATOM   1447 C  CE  . MET A 1 178 ? -12.308 -21.151 21.336  1.00 26.47 ? 177  MET A CE  1 
ATOM   1448 N  N   . VAL A 1 179 ? -12.466 -25.051 22.407  1.00 24.98 ? 178  VAL A N   1 
ATOM   1449 C  CA  . VAL A 1 179 ? -11.310 -25.574 21.684  1.00 27.02 ? 178  VAL A CA  1 
ATOM   1450 C  C   . VAL A 1 179 ? -11.474 -27.068 21.438  1.00 28.68 ? 178  VAL A C   1 
ATOM   1451 O  O   . VAL A 1 179 ? -11.082 -27.588 20.386  1.00 27.91 ? 178  VAL A O   1 
ATOM   1452 C  CB  . VAL A 1 179 ? -10.010 -25.256 22.447  1.00 25.53 ? 178  VAL A CB  1 
ATOM   1453 C  CG1 . VAL A 1 179 ? -8.815  -25.932 21.775  1.00 25.83 ? 178  VAL A CG1 1 
ATOM   1454 C  CG2 . VAL A 1 179 ? -9.802  -23.749 22.542  1.00 27.93 ? 178  VAL A CG2 1 
ATOM   1455 N  N   . ARG A 1 180 ? -12.068 -27.779 22.399  1.00 29.39 ? 179  ARG A N   1 
ATOM   1456 C  CA  . ARG A 1 180 ? -12.274 -29.213 22.227  1.00 31.22 ? 179  ARG A CA  1 
ATOM   1457 C  C   . ARG A 1 180 ? -13.350 -29.502 21.187  1.00 31.56 ? 179  ARG A C   1 
ATOM   1458 O  O   . ARG A 1 180 ? -13.282 -30.527 20.497  1.00 31.84 ? 179  ARG A O   1 
ATOM   1459 C  CB  . ARG A 1 180 ? -12.631 -29.848 23.570  1.00 34.61 ? 179  ARG A CB  1 
ATOM   1460 C  CG  . ARG A 1 180 ? -12.096 -31.250 23.758  1.00 38.67 ? 179  ARG A CG  1 
ATOM   1461 C  CD  . ARG A 1 180 ? -11.793 -31.500 25.235  1.00 43.67 ? 179  ARG A CD  1 
ATOM   1462 N  NE  . ARG A 1 180 ? -12.937 -31.195 26.089  1.00 46.56 ? 179  ARG A NE  1 
ATOM   1463 C  CZ  . ARG A 1 180 ? -12.861 -30.971 27.395  1.00 49.38 ? 179  ARG A CZ  1 
ATOM   1464 N  NH1 . ARG A 1 180 ? -11.703 -31.003 28.037  1.00 51.08 ? 179  ARG A NH1 1 
ATOM   1465 N  NH2 . ARG A 1 180 ? -13.974 -30.708 28.074  1.00 49.36 ? 179  ARG A NH2 1 
ATOM   1466 N  N   . ALA A 1 181 ? -14.344 -28.615 21.059  1.00 28.82 ? 180  ALA A N   1 
ATOM   1467 C  CA  . ALA A 1 181 ? -15.340 -28.768 20.004  1.00 25.88 ? 180  ALA A CA  1 
ATOM   1468 C  C   . ALA A 1 181 ? -14.732 -28.499 18.635  1.00 24.39 ? 180  ALA A C   1 
ATOM   1469 O  O   . ALA A 1 181 ? -15.001 -29.231 17.675  1.00 25.31 ? 180  ALA A O   1 
ATOM   1470 C  CB  . ALA A 1 181 ? -16.524 -27.836 20.253  1.00 25.67 ? 180  ALA A CB  1 
ATOM   1471 N  N   . LEU A 1 182 ? -13.914 -27.449 18.526  1.00 22.44 ? 181  LEU A N   1 
ATOM   1472 C  CA  . LEU A 1 182 ? -13.271 -27.142 17.252  1.00 20.27 ? 181  LEU A CA  1 
ATOM   1473 C  C   . LEU A 1 182 ? -12.281 -28.232 16.862  1.00 23.39 ? 181  LEU A C   1 
ATOM   1474 O  O   . LEU A 1 182 ? -12.181 -28.587 15.681  1.00 24.74 ? 181  LEU A O   1 
ATOM   1475 C  CB  . LEU A 1 182 ? -12.575 -25.779 17.320  1.00 20.88 ? 181  LEU A CB  1 
ATOM   1476 C  CG  . LEU A 1 182 ? -13.472 -24.558 17.533  1.00 21.93 ? 181  LEU A CG  1 
ATOM   1477 C  CD1 . LEU A 1 182 ? -12.634 -23.282 17.696  1.00 23.57 ? 181  LEU A CD1 1 
ATOM   1478 C  CD2 . LEU A 1 182 ? -14.464 -24.414 16.373  1.00 23.49 ? 181  LEU A CD2 1 
ATOM   1479 N  N   . ASP A 1 183 ? -11.536 -28.767 17.838  1.00 25.02 ? 182  ASP A N   1 
ATOM   1480 C  CA  . ASP A 1 183 ? -10.646 -29.893 17.567  1.00 29.86 ? 182  ASP A CA  1 
ATOM   1481 C  C   . ASP A 1 183 ? -11.425 -31.077 17.016  1.00 29.79 ? 182  ASP A C   1 
ATOM   1482 O  O   . ASP A 1 183 ? -11.022 -31.698 16.025  1.00 31.83 ? 182  ASP A O   1 
ATOM   1483 C  CB  . ASP A 1 183 ? -9.900  -30.307 18.840  1.00 35.70 ? 182  ASP A CB  1 
ATOM   1484 C  CG  . ASP A 1 183 ? -8.791  -29.348 19.210  1.00 45.04 ? 182  ASP A CG  1 
ATOM   1485 O  OD1 . ASP A 1 183 ? -8.281  -28.648 18.311  1.00 49.08 ? 182  ASP A OD1 1 
ATOM   1486 O  OD2 . ASP A 1 183 ? -8.419  -29.303 20.405  1.00 48.94 ? 182  ASP A OD2 1 
ATOM   1487 N  N   . GLU A 1 184 ? -12.541 -31.413 17.666  1.00 25.95 ? 183  GLU A N   1 
ATOM   1488 C  CA  . GLU A 1 184 ? -13.362 -32.528 17.209  1.00 27.57 ? 183  GLU A CA  1 
ATOM   1489 C  C   . GLU A 1 184 ? -13.901 -32.266 15.808  1.00 27.46 ? 183  GLU A C   1 
ATOM   1490 O  O   . GLU A 1 184 ? -13.907 -33.166 14.958  1.00 29.70 ? 183  GLU A O   1 
ATOM   1491 C  CB  . GLU A 1 184 ? -14.499 -32.776 18.206  1.00 28.26 ? 183  GLU A CB  1 
ATOM   1492 C  CG  . GLU A 1 184 ? -15.608 -33.728 17.737  1.00 29.77 ? 183  GLU A CG  1 
ATOM   1493 C  CD  . GLU A 1 184 ? -15.185 -35.196 17.647  1.00 31.16 ? 183  GLU A CD  1 
ATOM   1494 O  OE1 . GLU A 1 184 ? -14.001 -35.511 17.885  1.00 31.58 ? 183  GLU A OE1 1 
ATOM   1495 O  OE2 . GLU A 1 184 ? -16.051 -36.039 17.326  1.00 31.05 ? 183  GLU A OE2 1 
ATOM   1496 N  N   . ALA A 1 185 ? -14.335 -31.031 15.539  1.00 23.94 ? 184  ALA A N   1 
ATOM   1497 C  CA  . ALA A 1 185 ? -14.839 -30.719 14.205  1.00 20.56 ? 184  ALA A CA  1 
ATOM   1498 C  C   . ALA A 1 185 ? -13.748 -30.880 13.155  1.00 23.96 ? 184  ALA A C   1 
ATOM   1499 O  O   . ALA A 1 185 ? -13.985 -31.460 12.087  1.00 23.26 ? 184  ALA A O   1 
ATOM   1500 C  CB  . ALA A 1 185 ? -15.416 -29.305 14.168  1.00 20.96 ? 184  ALA A CB  1 
ATOM   1501 N  N   . MET A 1 186 ? -12.540 -30.381 13.440  1.00 21.87 ? 185  MET A N   1 
ATOM   1502 C  CA  . MET A 1 186 ? -11.448 -30.504 12.477  1.00 24.36 ? 185  MET A CA  1 
ATOM   1503 C  C   . MET A 1 186 ? -11.043 -31.961 12.281  1.00 22.92 ? 185  MET A C   1 
ATOM   1504 O  O   . MET A 1 186 ? -10.823 -32.405 11.146  1.00 23.08 ? 185  MET A O   1 
ATOM   1505 C  CB  . MET A 1 186 ? -10.242 -29.669 12.928  1.00 24.40 ? 185  MET A CB  1 
ATOM   1506 C  CG  . MET A 1 186 ? -9.171  -29.486 11.840  1.00 21.53 ? 185  MET A CG  1 
ATOM   1507 S  SD  . MET A 1 186 ? -7.701  -28.594 12.403  1.00 23.66 ? 185  MET A SD  1 
ATOM   1508 C  CE  . MET A 1 186 ? -6.891  -29.856 13.397  1.00 27.35 ? 185  MET A CE  1 
ATOM   1509 N  N   . ASN A 1 187 ? -10.927 -32.724 13.373  1.00 24.02 ? 186  ASN A N   1 
ATOM   1510 C  CA  . ASN A 1 187 ? -10.535 -34.123 13.237  1.00 23.59 ? 186  ASN A CA  1 
ATOM   1511 C  C   . ASN A 1 187 ? -11.614 -34.938 12.541  1.00 25.28 ? 186  ASN A C   1 
ATOM   1512 O  O   . ASN A 1 187 ? -11.301 -35.888 11.817  1.00 27.88 ? 186  ASN A O   1 
ATOM   1513 C  CB  . ASN A 1 187 ? -10.220 -34.725 14.609  1.00 26.21 ? 186  ASN A CB  1 
ATOM   1514 C  CG  . ASN A 1 187 ? -9.630  -36.127 14.510  1.00 31.81 ? 186  ASN A CG  1 
ATOM   1515 O  OD1 . ASN A 1 187 ? -10.339 -37.130 14.642  1.00 34.21 ? 186  ASN A OD1 1 
ATOM   1516 N  ND2 . ASN A 1 187 ? -8.327  -36.199 14.266  1.00 32.25 ? 186  ASN A ND2 1 
ATOM   1517 N  N   . LYS A 1 188 ? -12.884 -34.577 12.738  1.00 25.05 ? 187  LYS A N   1 
ATOM   1518 C  CA  . LYS A 1 188 ? -13.982 -35.305 12.115  1.00 25.30 ? 187  LYS A CA  1 
ATOM   1519 C  C   . LYS A 1 188 ? -13.991 -35.150 10.595  1.00 25.07 ? 187  LYS A C   1 
ATOM   1520 O  O   . LYS A 1 188 ? -14.610 -35.968 9.905   1.00 26.90 ? 187  LYS A O   1 
ATOM   1521 C  CB  . LYS A 1 188 ? -15.315 -34.836 12.710  1.00 28.39 ? 187  LYS A CB  1 
ATOM   1522 C  CG  . LYS A 1 188 ? -16.420 -35.885 12.675  1.00 34.47 ? 187  LYS A CG  1 
ATOM   1523 C  CD  . LYS A 1 188 ? -17.785 -35.306 13.029  1.00 37.00 ? 187  LYS A CD  1 
ATOM   1524 C  CE  . LYS A 1 188 ? -17.841 -34.805 14.460  1.00 42.10 ? 187  LYS A CE  1 
ATOM   1525 N  NZ  . LYS A 1 188 ? -19.216 -34.341 14.834  1.00 44.64 ? 187  LYS A NZ  1 
ATOM   1526 N  N   . LEU A 1 189 ? -13.312 -34.127 10.062  1.00 24.84 ? 188  LEU A N   1 
ATOM   1527 C  CA  . LEU A 1 189 ? -13.291 -33.904 8.619   1.00 26.30 ? 188  LEU A CA  1 
ATOM   1528 C  C   . LEU A 1 189 ? -12.735 -35.101 7.857   1.00 28.60 ? 188  LEU A C   1 
ATOM   1529 O  O   . LEU A 1 189 ? -13.173 -35.374 6.733   1.00 29.42 ? 188  LEU A O   1 
ATOM   1530 C  CB  . LEU A 1 189 ? -12.468 -32.655 8.290   1.00 23.31 ? 188  LEU A CB  1 
ATOM   1531 C  CG  . LEU A 1 189 ? -13.027 -31.321 8.786   1.00 23.19 ? 188  LEU A CG  1 
ATOM   1532 C  CD1 . LEU A 1 189 ? -12.017 -30.197 8.574   1.00 26.47 ? 188  LEU A CD1 1 
ATOM   1533 C  CD2 . LEU A 1 189 ? -14.353 -30.995 8.098   1.00 23.71 ? 188  LEU A CD2 1 
ATOM   1534 N  N   . GLN A 1 190 ? -11.769 -35.815 8.428   1.00 30.44 ? 189  GLN A N   1 
ATOM   1535 C  CA  . GLN A 1 190 ? -11.134 -36.930 7.734   1.00 30.61 ? 189  GLN A CA  1 
ATOM   1536 C  C   . GLN A 1 190 ? -11.711 -38.288 8.113   1.00 32.88 ? 189  GLN A C   1 
ATOM   1537 O  O   . GLN A 1 190 ? -11.254 -39.304 7.576   1.00 35.91 ? 189  GLN A O   1 
ATOM   1538 C  CB  . GLN A 1 190 ? -9.616  -36.921 7.983   1.00 34.21 ? 189  GLN A CB  1 
ATOM   1539 C  CG  . GLN A 1 190 ? -9.203  -36.872 9.450   1.00 38.00 ? 189  GLN A CG  1 
ATOM   1540 C  CD  . GLN A 1 190 ? -9.248  -38.225 10.133  1.00 41.18 ? 189  GLN A CD  1 
ATOM   1541 O  OE1 . GLN A 1 190 ? -8.546  -39.160 9.741   1.00 43.05 ? 189  GLN A OE1 1 
ATOM   1542 N  NE2 . GLN A 1 190 ? -10.072 -38.335 11.169  1.00 43.10 ? 189  GLN A NE2 1 
ATOM   1543 N  N   . ARG A 1 191 ? -12.707 -38.335 9.000   1.00 33.32 ? 190  ARG A N   1 
ATOM   1544 C  CA  . ARG A 1 191 ? -13.283 -39.609 9.425   1.00 37.23 ? 190  ARG A CA  1 
ATOM   1545 C  C   . ARG A 1 191 ? -14.170 -40.187 8.332   1.00 41.78 ? 190  ARG A C   1 
ATOM   1546 O  O   . ARG A 1 191 ? -15.200 -39.600 7.982   1.00 42.40 ? 190  ARG A O   1 
ATOM   1547 C  CB  . ARG A 1 191 ? -14.092 -39.427 10.703  1.00 38.20 ? 190  ARG A CB  1 
ATOM   1548 C  CG  . ARG A 1 191 ? -13.293 -39.546 11.967  1.00 38.93 ? 190  ARG A CG  1 
ATOM   1549 C  CD  . ARG A 1 191 ? -14.175 -39.303 13.170  1.00 36.11 ? 190  ARG A CD  1 
ATOM   1550 N  NE  . ARG A 1 191 ? -13.445 -38.593 14.210  1.00 35.65 ? 190  ARG A NE  1 
ATOM   1551 C  CZ  . ARG A 1 191 ? -14.016 -37.985 15.238  1.00 35.08 ? 190  ARG A CZ  1 
ATOM   1552 N  NH1 . ARG A 1 191 ? -15.328 -37.994 15.403  1.00 33.50 ? 190  ARG A NH1 1 
ATOM   1553 N  NH2 . ARG A 1 191 ? -13.251 -37.350 16.118  1.00 37.30 ? 190  ARG A NH2 1 
ATOM   1554 N  N   . ALA A 1 192 ? -13.792 -41.355 7.813   1.00 45.20 ? 191  ALA A N   1 
ATOM   1555 C  CA  . ALA A 1 192 ? -14.609 -41.999 6.791   1.00 46.25 ? 191  ALA A CA  1 
ATOM   1556 C  C   . ALA A 1 192 ? -15.861 -42.651 7.375   1.00 49.28 ? 191  ALA A C   1 
ATOM   1557 O  O   . ALA A 1 192 ? -16.911 -42.655 6.720   1.00 49.05 ? 191  ALA A O   1 
ATOM   1558 C  CB  . ALA A 1 192 ? -13.774 -43.032 6.029   1.00 45.97 ? 191  ALA A CB  1 
ATOM   1559 N  N   . ASN A 1 193 ? -15.785 -43.192 8.594   1.00 49.42 ? 192  ASN A N   1 
ATOM   1560 C  CA  . ASN A 1 193 ? -16.913 -43.864 9.241   1.00 49.61 ? 192  ASN A CA  1 
ATOM   1561 C  C   . ASN A 1 193 ? -17.219 -43.180 10.568  1.00 45.81 ? 192  ASN A C   1 
ATOM   1562 O  O   . ASN A 1 193 ? -16.968 -43.745 11.642  1.00 44.58 ? 192  ASN A O   1 
ATOM   1563 C  CB  . ASN A 1 193 ? -16.632 -45.349 9.467   1.00 53.40 ? 192  ASN A CB  1 
ATOM   1564 C  CG  . ASN A 1 193 ? -15.772 -45.956 8.380   1.00 57.96 ? 192  ASN A CG  1 
ATOM   1565 O  OD1 . ASN A 1 193 ? -14.568 -46.149 8.562   1.00 61.68 ? 192  ASN A OD1 1 
ATOM   1566 N  ND2 . ASN A 1 193 ? -16.383 -46.263 7.240   1.00 56.23 ? 192  ASN A ND2 1 
ATOM   1567 N  N   . PRO A 1 194 ? -17.789 -41.973 10.533  1.00 46.01 ? 193  PRO A N   1 
ATOM   1568 C  CA  . PRO A 1 194 ? -18.010 -41.233 11.787  1.00 46.55 ? 193  PRO A CA  1 
ATOM   1569 C  C   . PRO A 1 194 ? -18.906 -41.958 12.776  1.00 47.25 ? 193  PRO A C   1 
ATOM   1570 O  O   . PRO A 1 194 ? -18.811 -41.693 13.980  1.00 46.99 ? 193  PRO A O   1 
ATOM   1571 C  CB  . PRO A 1 194 ? -18.648 -39.920 11.314  1.00 46.11 ? 193  PRO A CB  1 
ATOM   1572 C  CG  . PRO A 1 194 ? -19.285 -40.266 10.003  1.00 46.12 ? 193  PRO A CG  1 
ATOM   1573 C  CD  . PRO A 1 194 ? -18.370 -41.281 9.369   1.00 45.60 ? 193  PRO A CD  1 
ATOM   1574 N  N   . ASP A 1 195 ? -19.773 -42.857 12.317  1.00 49.47 ? 194  ASP A N   1 
ATOM   1575 C  CA  . ASP A 1 195 ? -20.657 -43.595 13.208  1.00 51.48 ? 194  ASP A CA  1 
ATOM   1576 C  C   . ASP A 1 195 ? -20.052 -44.911 13.678  1.00 51.03 ? 194  ASP A C   1 
ATOM   1577 O  O   . ASP A 1 195 ? -20.765 -45.733 14.264  1.00 51.18 ? 194  ASP A O   1 
ATOM   1578 C  CB  . ASP A 1 195 ? -22.004 -43.848 12.527  1.00 52.17 ? 194  ASP A CB  1 
ATOM   1579 C  CG  . ASP A 1 195 ? -22.816 -42.579 12.362  1.00 54.65 ? 194  ASP A CG  1 
ATOM   1580 O  OD1 . ASP A 1 195 ? -22.692 -41.676 13.217  1.00 54.91 ? 194  ASP A OD1 1 
ATOM   1581 O  OD2 . ASP A 1 195 ? -23.578 -42.482 11.378  1.00 57.49 ? 194  ASP A OD2 1 
ATOM   1582 N  N   . ASP A 1 196 ? -18.767 -45.127 13.440  1.00 50.83 ? 195  ASP A N   1 
ATOM   1583 C  CA  . ASP A 1 196 ? -18.101 -46.309 13.970  1.00 53.32 ? 195  ASP A CA  1 
ATOM   1584 C  C   . ASP A 1 196 ? -18.033 -46.222 15.491  1.00 53.76 ? 195  ASP A C   1 
ATOM   1585 O  O   . ASP A 1 196 ? -17.629 -45.184 16.030  1.00 52.12 ? 195  ASP A O   1 
ATOM   1586 C  CB  . ASP A 1 196 ? -16.698 -46.440 13.383  1.00 55.46 ? 195  ASP A CB  1 
ATOM   1587 C  CG  . ASP A 1 196 ? -15.967 -47.671 13.887  1.00 57.92 ? 195  ASP A CG  1 
ATOM   1588 O  OD1 . ASP A 1 196 ? -16.365 -48.793 13.514  1.00 59.85 ? 195  ASP A OD1 1 
ATOM   1589 O  OD2 . ASP A 1 196 ? -14.993 -47.518 14.653  1.00 58.71 ? 195  ASP A OD2 1 
ATOM   1590 N  N   . PRO A 1 197 ? -18.406 -47.281 16.216  1.00 54.32 ? 196  PRO A N   1 
ATOM   1591 C  CA  . PRO A 1 197 ? -18.412 -47.208 17.688  1.00 53.83 ? 196  PRO A CA  1 
ATOM   1592 C  C   . PRO A 1 197 ? -17.079 -46.795 18.304  1.00 51.54 ? 196  PRO A C   1 
ATOM   1593 O  O   . PRO A 1 197 ? -17.050 -46.473 19.499  1.00 51.56 ? 196  PRO A O   1 
ATOM   1594 C  CB  . PRO A 1 197 ? -18.801 -48.632 18.106  1.00 55.11 ? 196  PRO A CB  1 
ATOM   1595 C  CG  . PRO A 1 197 ? -19.575 -49.160 16.942  1.00 55.06 ? 196  PRO A CG  1 
ATOM   1596 C  CD  . PRO A 1 197 ? -18.927 -48.567 15.722  1.00 54.94 ? 196  PRO A CD  1 
ATOM   1597 N  N   . ALA A 1 198 ? -15.982 -46.796 17.543  1.00 48.55 ? 197  ALA A N   1 
ATOM   1598 C  CA  . ALA A 1 198 ? -14.728 -46.267 18.066  1.00 47.80 ? 197  ALA A CA  1 
ATOM   1599 C  C   . ALA A 1 198 ? -14.842 -44.798 18.456  1.00 46.65 ? 197  ALA A C   1 
ATOM   1600 O  O   . ALA A 1 198 ? -14.048 -44.320 19.273  1.00 47.11 ? 197  ALA A O   1 
ATOM   1601 C  CB  . ALA A 1 198 ? -13.607 -46.445 17.040  1.00 47.62 ? 197  ALA A CB  1 
ATOM   1602 N  N   . TYR A 1 199 ? -15.807 -44.072 17.895  1.00 44.55 ? 198  TYR A N   1 
ATOM   1603 C  CA  . TYR A 1 199 ? -15.980 -42.654 18.180  1.00 41.87 ? 198  TYR A CA  1 
ATOM   1604 C  C   . TYR A 1 199 ? -17.135 -42.390 19.138  1.00 40.24 ? 198  TYR A C   1 
ATOM   1605 O  O   . TYR A 1 199 ? -17.672 -41.278 19.163  1.00 39.25 ? 198  TYR A O   1 
ATOM   1606 C  CB  . TYR A 1 199 ? -16.177 -41.875 16.879  1.00 43.49 ? 198  TYR A CB  1 
ATOM   1607 C  CG  . TYR A 1 199 ? -15.062 -42.088 15.886  1.00 45.62 ? 198  TYR A CG  1 
ATOM   1608 C  CD1 . TYR A 1 199 ? -13.772 -41.650 16.158  1.00 46.31 ? 198  TYR A CD1 1 
ATOM   1609 C  CD2 . TYR A 1 199 ? -15.295 -42.735 14.678  1.00 47.51 ? 198  TYR A CD2 1 
ATOM   1610 C  CE1 . TYR A 1 199 ? -12.743 -41.852 15.253  1.00 48.01 ? 198  TYR A CE1 1 
ATOM   1611 C  CE2 . TYR A 1 199 ? -14.273 -42.940 13.768  1.00 48.21 ? 198  TYR A CE2 1 
ATOM   1612 C  CZ  . TYR A 1 199 ? -13.001 -42.496 14.060  1.00 49.42 ? 198  TYR A CZ  1 
ATOM   1613 O  OH  . TYR A 1 199 ? -11.982 -42.695 13.155  1.00 52.69 ? 198  TYR A OH  1 
ATOM   1614 N  N   . ASP A 1 200 ? -17.533 -43.393 19.923  1.00 40.67 ? 199  ASP A N   1 
ATOM   1615 C  CA  . ASP A 1 200 ? -18.595 -43.177 20.899  1.00 42.70 ? 199  ASP A CA  1 
ATOM   1616 C  C   . ASP A 1 200 ? -18.167 -42.176 21.964  1.00 42.44 ? 199  ASP A C   1 
ATOM   1617 O  O   . ASP A 1 200 ? -18.968 -41.338 22.392  1.00 42.00 ? 199  ASP A O   1 
ATOM   1618 C  CB  . ASP A 1 200 ? -19.001 -44.504 21.538  1.00 45.08 ? 199  ASP A CB  1 
ATOM   1619 C  CG  . ASP A 1 200 ? -19.899 -45.337 20.640  1.00 47.08 ? 199  ASP A CG  1 
ATOM   1620 O  OD1 . ASP A 1 200 ? -20.549 -44.759 19.743  1.00 47.15 ? 199  ASP A OD1 1 
ATOM   1621 O  OD2 . ASP A 1 200 ? -19.967 -46.569 20.842  1.00 48.16 ? 199  ASP A OD2 1 
ATOM   1622 N  N   . GLU A 1 201 ? -16.907 -42.245 22.403  1.00 43.97 ? 200  GLU A N   1 
ATOM   1623 C  CA  . GLU A 1 201 ? -16.434 -41.316 23.425  1.00 43.94 ? 200  GLU A CA  1 
ATOM   1624 C  C   . GLU A 1 201 ? -16.270 -39.912 22.859  1.00 40.15 ? 200  GLU A C   1 
ATOM   1625 O  O   . GLU A 1 201 ? -16.551 -38.924 23.549  1.00 40.58 ? 200  GLU A O   1 
ATOM   1626 C  CB  . GLU A 1 201 ? -15.119 -41.813 24.028  1.00 46.88 ? 200  GLU A CB  1 
ATOM   1627 C  CG  . GLU A 1 201 ? -14.486 -40.850 25.028  1.00 49.81 ? 200  GLU A CG  1 
ATOM   1628 C  CD  . GLU A 1 201 ? -15.393 -40.525 26.211  1.00 53.42 ? 200  GLU A CD  1 
ATOM   1629 O  OE1 . GLU A 1 201 ? -16.389 -41.250 26.429  1.00 54.37 ? 200  GLU A OE1 1 
ATOM   1630 O  OE2 . GLU A 1 201 ? -15.109 -39.536 26.922  1.00 54.09 ? 200  GLU A OE2 1 
ATOM   1631 N  N   . ASN A 1 202 ? -15.810 -39.800 21.609  1.00 38.04 ? 201  ASN A N   1 
ATOM   1632 C  CA  . ASN A 1 202 ? -15.776 -38.495 20.955  1.00 38.02 ? 201  ASN A CA  1 
ATOM   1633 C  C   . ASN A 1 202 ? -17.160 -37.861 20.947  1.00 37.62 ? 201  ASN A C   1 
ATOM   1634 O  O   . ASN A 1 202 ? -17.318 -36.677 21.266  1.00 37.87 ? 201  ASN A O   1 
ATOM   1635 C  CB  . ASN A 1 202 ? -15.248 -38.624 19.525  1.00 40.27 ? 201  ASN A CB  1 
ATOM   1636 C  CG  . ASN A 1 202 ? -13.840 -39.177 19.466  1.00 43.92 ? 201  ASN A CG  1 
ATOM   1637 O  OD1 . ASN A 1 202 ? -13.641 -40.390 19.446  1.00 45.04 ? 201  ASN A OD1 1 
ATOM   1638 N  ND2 . ASN A 1 202 ? -12.852 -38.287 19.429  1.00 44.22 ? 201  ASN A ND2 1 
ATOM   1639 N  N   . LYS A 1 203 ? -18.182 -38.643 20.584  1.00 36.11 ? 202  LYS A N   1 
ATOM   1640 C  CA  . LYS A 1 203 ? -19.540 -38.110 20.556  1.00 35.98 ? 202  LYS A CA  1 
ATOM   1641 C  C   . LYS A 1 203 ? -19.995 -37.687 21.948  1.00 36.61 ? 202  LYS A C   1 
ATOM   1642 O  O   . LYS A 1 203 ? -20.606 -36.624 22.111  1.00 36.35 ? 202  LYS A O   1 
ATOM   1643 C  CB  . LYS A 1 203 ? -20.498 -39.140 19.961  1.00 37.39 ? 202  LYS A CB  1 
ATOM   1644 C  CG  . LYS A 1 203 ? -20.256 -39.426 18.488  1.00 39.97 ? 202  LYS A CG  1 
ATOM   1645 C  CD  . LYS A 1 203 ? -21.167 -40.534 17.982  1.00 44.73 ? 202  LYS A CD  1 
ATOM   1646 C  CE  . LYS A 1 203 ? -20.782 -40.961 16.573  1.00 47.95 ? 202  LYS A CE  1 
ATOM   1647 N  NZ  . LYS A 1 203 ? -21.694 -42.016 16.052  1.00 49.44 ? 202  LYS A NZ  1 
ATOM   1648 N  N   . ARG A 1 204 ? -19.707 -38.500 22.967  1.00 37.82 ? 203  ARG A N   1 
ATOM   1649 C  CA  . ARG A 1 204 ? -20.077 -38.125 24.330  1.00 37.99 ? 203  ARG A CA  1 
ATOM   1650 C  C   . ARG A 1 204 ? -19.372 -36.840 24.757  1.00 38.77 ? 203  ARG A C   1 
ATOM   1651 O  O   . ARG A 1 204 ? -20.001 -35.921 25.293  1.00 40.22 ? 203  ARG A O   1 
ATOM   1652 C  CB  . ARG A 1 204 ? -19.753 -39.262 25.300  1.00 40.27 ? 203  ARG A CB  1 
ATOM   1653 C  CG  . ARG A 1 204 ? -20.358 -39.063 26.684  1.00 44.24 ? 203  ARG A CG  1 
ATOM   1654 C  CD  . ARG A 1 204 ? -19.523 -39.705 27.782  1.00 48.91 ? 203  ARG A CD  1 
ATOM   1655 N  NE  . ARG A 1 204 ? -18.215 -39.073 27.914  1.00 54.19 ? 203  ARG A NE  1 
ATOM   1656 C  CZ  . ARG A 1 204 ? -17.985 -37.948 28.581  1.00 57.37 ? 203  ARG A CZ  1 
ATOM   1657 N  NH1 . ARG A 1 204 ? -18.961 -37.293 29.193  1.00 58.57 ? 203  ARG A NH1 1 
ATOM   1658 N  NH2 . ARG A 1 204 ? -16.745 -37.465 28.632  1.00 57.34 ? 203  ARG A NH2 1 
ATOM   1659 N  N   . GLN A 1 205 ? -18.058 -36.762 24.531  1.00 39.04 ? 204  GLN A N   1 
ATOM   1660 C  CA  . GLN A 1 205 ? -17.310 -35.562 24.901  1.00 38.61 ? 204  GLN A CA  1 
ATOM   1661 C  C   . GLN A 1 205 ? -17.807 -34.344 24.130  1.00 37.93 ? 204  GLN A C   1 
ATOM   1662 O  O   . GLN A 1 205 ? -17.937 -33.252 24.696  1.00 38.31 ? 204  GLN A O   1 
ATOM   1663 C  CB  . GLN A 1 205 ? -15.817 -35.788 24.657  1.00 40.64 ? 204  GLN A CB  1 
ATOM   1664 C  CG  . GLN A 1 205 ? -14.939 -34.581 24.926  1.00 42.96 ? 204  GLN A CG  1 
ATOM   1665 C  CD  . GLN A 1 205 ? -14.957 -34.153 26.382  1.00 43.85 ? 204  GLN A CD  1 
ATOM   1666 O  OE1 . GLN A 1 205 ? -15.573 -33.145 26.738  1.00 46.28 ? 204  GLN A OE1 1 
ATOM   1667 N  NE2 . GLN A 1 205 ? -14.273 -34.911 27.231  1.00 42.17 ? 204  GLN A NE2 1 
ATOM   1668 N  N   . PHE A 1 206 ? -18.091 -34.515 22.837  1.00 36.85 ? 205  PHE A N   1 
ATOM   1669 C  CA  . PHE A 1 206 ? -18.648 -33.427 22.038  1.00 35.30 ? 205  PHE A CA  1 
ATOM   1670 C  C   . PHE A 1 206 ? -19.916 -32.868 22.677  1.00 35.10 ? 205  PHE A C   1 
ATOM   1671 O  O   . PHE A 1 206 ? -20.055 -31.651 22.856  1.00 32.71 ? 205  PHE A O   1 
ATOM   1672 C  CB  . PHE A 1 206 ? -18.922 -33.928 20.618  1.00 34.41 ? 205  PHE A CB  1 
ATOM   1673 C  CG  . PHE A 1 206 ? -19.190 -32.833 19.617  1.00 34.80 ? 205  PHE A CG  1 
ATOM   1674 C  CD1 . PHE A 1 206 ? -18.228 -31.875 19.337  1.00 34.38 ? 205  PHE A CD1 1 
ATOM   1675 C  CD2 . PHE A 1 206 ? -20.393 -32.790 18.927  1.00 32.90 ? 205  PHE A CD2 1 
ATOM   1676 C  CE1 . PHE A 1 206 ? -18.470 -30.876 18.396  1.00 35.22 ? 205  PHE A CE1 1 
ATOM   1677 C  CE2 . PHE A 1 206 ? -20.642 -31.798 17.982  1.00 33.19 ? 205  PHE A CE2 1 
ATOM   1678 C  CZ  . PHE A 1 206 ? -19.681 -30.839 17.719  1.00 34.18 ? 205  PHE A CZ  1 
ATOM   1679 N  N   . GLN A 1 207 ? -20.857 -33.746 23.030  1.00 36.19 ? 206  GLN A N   1 
ATOM   1680 C  CA  . GLN A 1 207 ? -22.074 -33.288 23.693  1.00 38.32 ? 206  GLN A CA  1 
ATOM   1681 C  C   . GLN A 1 207 ? -21.751 -32.599 25.013  1.00 36.99 ? 206  GLN A C   1 
ATOM   1682 O  O   . GLN A 1 207 ? -22.371 -31.588 25.365  1.00 34.51 ? 206  GLN A O   1 
ATOM   1683 C  CB  . GLN A 1 207 ? -23.023 -34.465 23.916  1.00 41.83 ? 206  GLN A CB  1 
ATOM   1684 C  CG  . GLN A 1 207 ? -23.495 -35.111 22.627  1.00 48.00 ? 206  GLN A CG  1 
ATOM   1685 C  CD  . GLN A 1 207 ? -24.198 -34.122 21.717  1.00 53.48 ? 206  GLN A CD  1 
ATOM   1686 O  OE1 . GLN A 1 207 ? -24.923 -33.243 22.185  1.00 55.56 ? 206  GLN A OE1 1 
ATOM   1687 N  NE2 . GLN A 1 207 ? -23.974 -34.248 20.412  1.00 54.67 ? 206  GLN A NE2 1 
ATOM   1688 N  N   . GLU A 1 208 ? -20.770 -33.125 25.749  1.00 37.60 ? 207  GLU A N   1 
ATOM   1689 C  CA  . GLU A 1 208 ? -20.385 -32.514 27.016  1.00 38.15 ? 207  GLU A CA  1 
ATOM   1690 C  C   . GLU A 1 208 ? -19.859 -31.099 26.810  1.00 35.61 ? 207  GLU A C   1 
ATOM   1691 O  O   . GLU A 1 208 ? -20.199 -30.184 27.570  1.00 32.86 ? 207  GLU A O   1 
ATOM   1692 C  CB  . GLU A 1 208 ? -19.340 -33.386 27.710  1.00 42.61 ? 207  GLU A CB  1 
ATOM   1693 C  CG  . GLU A 1 208 ? -18.741 -32.784 28.958  1.00 49.14 ? 207  GLU A CG  1 
ATOM   1694 C  CD  . GLU A 1 208 ? -17.903 -33.790 29.725  1.00 55.62 ? 207  GLU A CD  1 
ATOM   1695 O  OE1 . GLU A 1 208 ? -18.331 -34.962 29.837  1.00 56.69 ? 207  GLU A OE1 1 
ATOM   1696 O  OE2 . GLU A 1 208 ? -16.812 -33.411 30.204  1.00 58.51 ? 207  GLU A OE2 1 
ATOM   1697 N  N   . ASP A 1 209 ? -19.028 -30.899 25.783  1.00 32.29 ? 208  ASP A N   1 
ATOM   1698 C  CA  . ASP A 1 209 ? -18.506 -29.565 25.523  1.00 29.94 ? 208  ASP A CA  1 
ATOM   1699 C  C   . ASP A 1 209 ? -19.599 -28.625 25.034  1.00 29.47 ? 208  ASP A C   1 
ATOM   1700 O  O   . ASP A 1 209 ? -19.561 -27.424 25.335  1.00 30.79 ? 208  ASP A O   1 
ATOM   1701 C  CB  . ASP A 1 209 ? -17.356 -29.643 24.517  1.00 32.15 ? 208  ASP A CB  1 
ATOM   1702 C  CG  . ASP A 1 209 ? -16.112 -30.274 25.114  1.00 33.65 ? 208  ASP A CG  1 
ATOM   1703 O  OD1 . ASP A 1 209 ? -15.901 -30.104 26.332  1.00 34.93 ? 208  ASP A OD1 1 
ATOM   1704 O  OD2 . ASP A 1 209 ? -15.350 -30.936 24.377  1.00 35.28 ? 208  ASP A OD2 1 
ATOM   1705 N  N   . ILE A 1 210 ? -20.583 -29.151 24.300  1.00 30.91 ? 209  ILE A N   1 
ATOM   1706 C  CA  . ILE A 1 210 ? -21.709 -28.333 23.857  1.00 31.39 ? 209  ILE A CA  1 
ATOM   1707 C  C   . ILE A 1 210 ? -22.563 -27.898 25.046  1.00 31.28 ? 209  ILE A C   1 
ATOM   1708 O  O   . ILE A 1 210 ? -23.072 -26.770 25.081  1.00 31.41 ? 209  ILE A O   1 
ATOM   1709 C  CB  . ILE A 1 210 ? -22.534 -29.098 22.805  1.00 30.65 ? 209  ILE A CB  1 
ATOM   1710 C  CG1 . ILE A 1 210 ? -21.734 -29.218 21.501  1.00 29.73 ? 209  ILE A CG1 1 
ATOM   1711 C  CG2 . ILE A 1 210 ? -23.874 -28.418 22.569  1.00 29.13 ? 209  ILE A CG2 1 
ATOM   1712 C  CD1 . ILE A 1 210 ? -22.461 -29.945 20.383  1.00 27.49 ? 209  ILE A CD1 1 
ATOM   1713 N  N   . LYS A 1 211 ? -22.726 -28.768 26.042  1.00 33.54 ? 210  LYS A N   1 
ATOM   1714 C  CA  . LYS A 1 211 ? -23.518 -28.382 27.209  1.00 34.32 ? 210  LYS A CA  1 
ATOM   1715 C  C   . LYS A 1 211 ? -22.817 -27.305 28.031  1.00 33.43 ? 210  LYS A C   1 
ATOM   1716 O  O   . LYS A 1 211 ? -23.474 -26.415 28.582  1.00 33.78 ? 210  LYS A O   1 
ATOM   1717 C  CB  . LYS A 1 211 ? -23.821 -29.594 28.082  1.00 36.02 ? 210  LYS A CB  1 
ATOM   1718 C  CG  . LYS A 1 211 ? -24.528 -29.200 29.377  1.00 40.39 ? 210  LYS A CG  1 
ATOM   1719 C  CD  . LYS A 1 211 ? -24.622 -30.345 30.369  1.00 45.59 ? 210  LYS A CD  1 
ATOM   1720 C  CE  . LYS A 1 211 ? -24.999 -29.824 31.755  1.00 47.00 ? 210  LYS A CE  1 
ATOM   1721 N  NZ  . LYS A 1 211 ? -26.188 -28.922 31.713  1.00 47.62 ? 210  LYS A NZ  1 
ATOM   1722 N  N   . VAL A 1 212 ? -21.486 -27.374 28.139  1.00 31.73 ? 211  VAL A N   1 
ATOM   1723 C  CA  . VAL A 1 212 ? -20.743 -26.338 28.857  1.00 30.26 ? 211  VAL A CA  1 
ATOM   1724 C  C   . VAL A 1 212 ? -20.989 -24.975 28.220  1.00 31.01 ? 211  VAL A C   1 
ATOM   1725 O  O   . VAL A 1 212 ? -21.259 -23.982 28.906  1.00 31.40 ? 211  VAL A O   1 
ATOM   1726 C  CB  . VAL A 1 212 ? -19.241 -26.681 28.893  1.00 29.88 ? 211  VAL A CB  1 
ATOM   1727 C  CG1 . VAL A 1 212 ? -18.424 -25.485 29.391  1.00 28.83 ? 211  VAL A CG1 1 
ATOM   1728 C  CG2 . VAL A 1 212 ? -18.992 -27.897 29.768  1.00 29.10 ? 211  VAL A CG2 1 
ATOM   1729 N  N   . MET A 1 213 ? -20.898 -24.909 26.891  1.00 30.00 ? 212  MET A N   1 
ATOM   1730 C  CA  . MET A 1 213 ? -21.107 -23.640 26.204  1.00 30.51 ? 212  MET A CA  1 
ATOM   1731 C  C   . MET A 1 213 ? -22.539 -23.149 26.380  1.00 28.87 ? 212  MET A C   1 
ATOM   1732 O  O   . MET A 1 213 ? -22.766 -21.951 26.590  1.00 31.34 ? 212  MET A O   1 
ATOM   1733 C  CB  . MET A 1 213 ? -20.746 -23.785 24.725  1.00 34.62 ? 212  MET A CB  1 
ATOM   1734 C  CG  . MET A 1 213 ? -19.280 -24.107 24.513  1.00 36.47 ? 212  MET A CG  1 
ATOM   1735 S  SD  . MET A 1 213 ? -18.732 -23.939 22.804  1.00 39.81 ? 212  MET A SD  1 
ATOM   1736 C  CE  . MET A 1 213 ? -19.776 -25.151 21.995  1.00 41.33 ? 212  MET A CE  1 
ATOM   1737 N  N   . ASN A 1 214 ? -23.515 -24.059 26.314  1.00 26.05 ? 213  ASN A N   1 
ATOM   1738 C  CA  . ASN A 1 214 ? -24.912 -23.655 26.445  1.00 27.82 ? 213  ASN A CA  1 
ATOM   1739 C  C   . ASN A 1 214 ? -25.245 -23.225 27.868  1.00 32.00 ? 213  ASN A C   1 
ATOM   1740 O  O   . ASN A 1 214 ? -26.107 -22.360 28.068  1.00 31.59 ? 213  ASN A O   1 
ATOM   1741 C  CB  . ASN A 1 214 ? -25.831 -24.795 26.010  1.00 30.02 ? 213  ASN A CB  1 
ATOM   1742 C  CG  . ASN A 1 214 ? -26.289 -24.659 24.574  1.00 36.11 ? 213  ASN A CG  1 
ATOM   1743 O  OD1 . ASN A 1 214 ? -27.347 -24.089 24.302  1.00 40.94 ? 213  ASN A OD1 1 
ATOM   1744 N  ND2 . ASN A 1 214 ? -25.495 -25.177 23.645  1.00 33.32 ? 213  ASN A ND2 1 
ATOM   1745 N  N   . ASP A 1 215 ? -24.581 -23.816 28.864  1.00 34.05 ? 214  ASP A N   1 
ATOM   1746 C  CA  . ASP A 1 215 ? -24.824 -23.409 30.243  1.00 35.40 ? 214  ASP A CA  1 
ATOM   1747 C  C   . ASP A 1 215 ? -24.433 -21.954 30.461  1.00 32.82 ? 214  ASP A C   1 
ATOM   1748 O  O   . ASP A 1 215 ? -25.154 -21.204 31.128  1.00 30.99 ? 214  ASP A O   1 
ATOM   1749 C  CB  . ASP A 1 215 ? -24.061 -24.319 31.203  1.00 37.86 ? 214  ASP A CB  1 
ATOM   1750 C  CG  . ASP A 1 215 ? -24.684 -25.696 31.316  1.00 41.22 ? 214  ASP A CG  1 
ATOM   1751 O  OD1 . ASP A 1 215 ? -25.812 -25.878 30.810  1.00 43.22 ? 214  ASP A OD1 1 
ATOM   1752 O  OD2 . ASP A 1 215 ? -24.047 -26.595 31.906  1.00 42.80 ? 214  ASP A OD2 1 
ATOM   1753 N  N   . LEU A 1 216 ? -23.289 -21.539 29.909  1.00 31.53 ? 215  LEU A N   1 
ATOM   1754 C  CA  . LEU A 1 216 ? -22.889 -20.141 30.008  1.00 29.65 ? 215  LEU A CA  1 
ATOM   1755 C  C   . LEU A 1 216 ? -23.880 -19.232 29.297  1.00 29.46 ? 215  LEU A C   1 
ATOM   1756 O  O   . LEU A 1 216 ? -24.209 -18.150 29.796  1.00 28.77 ? 215  LEU A O   1 
ATOM   1757 C  CB  . LEU A 1 216 ? -21.489 -19.942 29.432  1.00 30.99 ? 215  LEU A CB  1 
ATOM   1758 C  CG  . LEU A 1 216 ? -21.060 -18.477 29.531  1.00 32.88 ? 215  LEU A CG  1 
ATOM   1759 C  CD1 . LEU A 1 216 ? -20.233 -18.247 30.790  1.00 35.07 ? 215  LEU A CD1 1 
ATOM   1760 C  CD2 . LEU A 1 216 ? -20.323 -18.033 28.285  1.00 33.62 ? 215  LEU A CD2 1 
ATOM   1761 N  N   . VAL A 1 217 ? -24.359 -19.649 28.119  1.00 29.99 ? 216  VAL A N   1 
ATOM   1762 C  CA  . VAL A 1 217 ? -25.376 -18.870 27.419  1.00 31.21 ? 216  VAL A CA  1 
ATOM   1763 C  C   . VAL A 1 217 ? -26.597 -18.665 28.310  1.00 33.32 ? 216  VAL A C   1 
ATOM   1764 O  O   . VAL A 1 217 ? -27.158 -17.562 28.372  1.00 33.08 ? 216  VAL A O   1 
ATOM   1765 C  CB  . VAL A 1 217 ? -25.744 -19.547 26.085  1.00 30.04 ? 216  VAL A CB  1 
ATOM   1766 C  CG1 . VAL A 1 217 ? -26.956 -18.871 25.464  1.00 29.67 ? 216  VAL A CG1 1 
ATOM   1767 C  CG2 . VAL A 1 217 ? -24.554 -19.504 25.135  1.00 28.85 ? 216  VAL A CG2 1 
ATOM   1768 N  N   . ASP A 1 218 ? -27.012 -19.713 29.030  1.00 35.51 ? 217  ASP A N   1 
ATOM   1769 C  CA  . ASP A 1 218 ? -28.141 -19.587 29.950  1.00 39.06 ? 217  ASP A CA  1 
ATOM   1770 C  C   . ASP A 1 218 ? -27.910 -18.462 30.951  1.00 37.50 ? 217  ASP A C   1 
ATOM   1771 O  O   . ASP A 1 218 ? -28.798 -17.632 31.190  1.00 32.93 ? 217  ASP A O   1 
ATOM   1772 C  CB  . ASP A 1 218 ? -28.371 -20.903 30.699  1.00 42.54 ? 217  ASP A CB  1 
ATOM   1773 C  CG  . ASP A 1 218 ? -28.701 -22.057 29.781  1.00 46.56 ? 217  ASP A CG  1 
ATOM   1774 O  OD1 . ASP A 1 218 ? -29.224 -21.814 28.674  1.00 48.24 ? 217  ASP A OD1 1 
ATOM   1775 O  OD2 . ASP A 1 218 ? -28.444 -23.214 30.180  1.00 46.49 ? 217  ASP A OD2 1 
ATOM   1776 N  N   . LYS A 1 219 ? -26.719 -18.431 31.559  1.00 36.07 ? 218  LYS A N   1 
ATOM   1777 C  CA  . LYS A 1 219 ? -26.428 -17.442 32.593  1.00 35.73 ? 218  LYS A CA  1 
ATOM   1778 C  C   . LYS A 1 219 ? -26.413 -16.031 32.020  1.00 31.82 ? 218  LYS A C   1 
ATOM   1779 O  O   . LYS A 1 219 ? -26.908 -15.090 32.653  1.00 33.19 ? 218  LYS A O   1 
ATOM   1780 C  CB  . LYS A 1 219 ? -25.092 -17.768 33.267  1.00 38.16 ? 218  LYS A CB  1 
ATOM   1781 C  CG  . LYS A 1 219 ? -24.576 -16.711 34.256  1.00 41.50 ? 218  LYS A CG  1 
ATOM   1782 C  CD  . LYS A 1 219 ? -25.505 -16.521 35.452  1.00 43.83 ? 218  LYS A CD  1 
ATOM   1783 C  CE  . LYS A 1 219 ? -24.736 -16.119 36.724  1.00 41.67 ? 218  LYS A CE  1 
ATOM   1784 N  NZ  . LYS A 1 219 ? -23.979 -14.822 36.633  1.00 34.88 ? 218  LYS A NZ  1 
ATOM   1785 N  N   . ILE A 1 220 ? -25.847 -15.861 30.824  1.00 27.69 ? 219  ILE A N   1 
ATOM   1786 C  CA  . ILE A 1 220 ? -25.842 -14.541 30.200  1.00 26.66 ? 219  ILE A CA  1 
ATOM   1787 C  C   . ILE A 1 220 ? -27.270 -14.050 29.992  1.00 28.89 ? 219  ILE A C   1 
ATOM   1788 O  O   . ILE A 1 220 ? -27.599 -12.897 30.303  1.00 29.90 ? 219  ILE A O   1 
ATOM   1789 C  CB  . ILE A 1 220 ? -25.054 -14.579 28.876  1.00 25.83 ? 219  ILE A CB  1 
ATOM   1790 C  CG1 . ILE A 1 220 ? -23.553 -14.755 29.150  1.00 24.52 ? 219  ILE A CG1 1 
ATOM   1791 C  CG2 . ILE A 1 220 ? -25.346 -13.333 28.044  1.00 27.41 ? 219  ILE A CG2 1 
ATOM   1792 C  CD1 . ILE A 1 220 ? -22.701 -14.927 27.893  1.00 25.22 ? 219  ILE A CD1 1 
ATOM   1793 N  N   . ILE A 1 221 ? -28.143 -14.917 29.478  1.00 28.91 ? 220  ILE A N   1 
ATOM   1794 C  CA  . ILE A 1 221 ? -29.525 -14.521 29.230  1.00 29.15 ? 220  ILE A CA  1 
ATOM   1795 C  C   . ILE A 1 221 ? -30.236 -14.224 30.542  1.00 32.66 ? 220  ILE A C   1 
ATOM   1796 O  O   . ILE A 1 221 ? -30.902 -13.191 30.682  1.00 34.21 ? 220  ILE A O   1 
ATOM   1797 C  CB  . ILE A 1 221 ? -30.259 -15.602 28.418  1.00 28.78 ? 220  ILE A CB  1 
ATOM   1798 C  CG1 . ILE A 1 221 ? -29.703 -15.655 26.991  1.00 28.29 ? 220  ILE A CG1 1 
ATOM   1799 C  CG2 . ILE A 1 221 ? -31.758 -15.331 28.406  1.00 32.01 ? 220  ILE A CG2 1 
ATOM   1800 C  CD1 . ILE A 1 221 ? -30.415 -16.651 26.091  1.00 30.45 ? 220  ILE A CD1 1 
ATOM   1801 N  N   . ALA A 1 222 ? -30.093 -15.114 31.530  1.00 37.35 ? 221  ALA A N   1 
ATOM   1802 C  CA  . ALA A 1 222 ? -30.774 -14.916 32.808  1.00 41.36 ? 221  ALA A CA  1 
ATOM   1803 C  C   . ALA A 1 222 ? -30.335 -13.621 33.481  1.00 43.26 ? 221  ALA A C   1 
ATOM   1804 O  O   . ALA A 1 222 ? -31.164 -12.888 34.035  1.00 44.68 ? 221  ALA A O   1 
ATOM   1805 C  CB  . ALA A 1 222 ? -30.521 -16.108 33.733  1.00 42.07 ? 221  ALA A CB  1 
ATOM   1806 N  N   . ASP A 1 223 ? -29.032 -13.323 33.449  1.00 41.80 ? 222  ASP A N   1 
ATOM   1807 C  CA  . ASP A 1 223 ? -28.528 -12.126 34.117  1.00 39.15 ? 222  ASP A CA  1 
ATOM   1808 C  C   . ASP A 1 223 ? -29.098 -10.857 33.495  1.00 36.07 ? 222  ASP A C   1 
ATOM   1809 O  O   . ASP A 1 223 ? -29.434 -9.903  34.208  1.00 34.53 ? 222  ASP A O   1 
ATOM   1810 C  CB  . ASP A 1 223 ? -26.999 -12.107 34.074  1.00 41.43 ? 222  ASP A CB  1 
ATOM   1811 C  CG  . ASP A 1 223 ? -26.375 -13.168 34.970  1.00 45.09 ? 222  ASP A CG  1 
ATOM   1812 O  OD1 . ASP A 1 223 ? -27.129 -13.873 35.678  1.00 46.08 ? 222  ASP A OD1 1 
ATOM   1813 O  OD2 . ASP A 1 223 ? -25.130 -13.295 34.966  1.00 43.37 ? 222  ASP A OD2 1 
ATOM   1814 N  N   . ARG A 1 224 ? -29.214 -10.822 32.165  1.00 32.81 ? 223  ARG A N   1 
ATOM   1815 C  CA  . ARG A 1 224 ? -29.730 -9.628  31.503  1.00 31.93 ? 223  ARG A CA  1 
ATOM   1816 C  C   . ARG A 1 224 ? -31.205 -9.409  31.817  1.00 35.78 ? 223  ARG A C   1 
ATOM   1817 O  O   . ARG A 1 224 ? -31.604 -8.309  32.217  1.00 36.34 ? 223  ARG A O   1 
ATOM   1818 C  CB  . ARG A 1 224 ? -29.523 -9.723  29.993  1.00 29.43 ? 223  ARG A CB  1 
ATOM   1819 C  CG  . ARG A 1 224 ? -30.199 -8.589  29.231  1.00 30.17 ? 223  ARG A CG  1 
ATOM   1820 C  CD  . ARG A 1 224 ? -29.599 -7.252  29.637  1.00 29.90 ? 223  ARG A CD  1 
ATOM   1821 N  NE  . ARG A 1 224 ? -28.153 -7.249  29.437  1.00 28.46 ? 223  ARG A NE  1 
ATOM   1822 C  CZ  . ARG A 1 224 ? -27.545 -6.776  28.356  1.00 27.63 ? 223  ARG A CZ  1 
ATOM   1823 N  NH1 . ARG A 1 224 ? -28.229 -6.237  27.355  1.00 26.96 ? 223  ARG A NH1 1 
ATOM   1824 N  NH2 . ARG A 1 224 ? -26.216 -6.842  28.277  1.00 27.99 ? 223  ARG A NH2 1 
ATOM   1825 N  N   . LYS A 1 225 ? -32.039 -10.439 31.629  1.00 38.48 ? 224  LYS A N   1 
ATOM   1826 C  CA  . LYS A 1 225 ? -33.478 -10.235 31.784  1.00 45.88 ? 224  LYS A CA  1 
ATOM   1827 C  C   . LYS A 1 225 ? -33.871 -9.965  33.231  1.00 50.23 ? 224  LYS A C   1 
ATOM   1828 O  O   . LYS A 1 225 ? -34.950 -9.411  33.475  1.00 51.62 ? 224  LYS A O   1 
ATOM   1829 C  CB  . LYS A 1 225 ? -34.258 -11.434 31.238  1.00 49.01 ? 224  LYS A CB  1 
ATOM   1830 C  CG  . LYS A 1 225 ? -33.927 -12.768 31.882  1.00 51.72 ? 224  LYS A CG  1 
ATOM   1831 C  CD  . LYS A 1 225 ? -34.590 -13.906 31.116  1.00 52.48 ? 224  LYS A CD  1 
ATOM   1832 C  CE  . LYS A 1 225 ? -33.871 -15.230 31.333  1.00 52.72 ? 224  LYS A CE  1 
ATOM   1833 N  NZ  . LYS A 1 225 ? -34.299 -16.261 30.342  1.00 50.68 ? 224  LYS A NZ  1 
ATOM   1834 N  N   . ALA A 1 226 ? -33.025 -10.333 34.189  1.00 52.03 ? 225  ALA A N   1 
ATOM   1835 C  CA  . ALA A 1 226 ? -33.248 -9.976  35.584  1.00 55.54 ? 225  ALA A CA  1 
ATOM   1836 C  C   . ALA A 1 226 ? -32.521 -8.700  35.987  1.00 60.87 ? 225  ALA A C   1 
ATOM   1837 O  O   . ALA A 1 226 ? -32.813 -8.148  37.053  1.00 61.62 ? 225  ALA A O   1 
ATOM   1838 C  CB  . ALA A 1 226 ? -32.813 -11.125 36.500  1.00 54.11 ? 225  ALA A CB  1 
ATOM   1839 N  N   . SER A 1 227 ? -31.593 -8.222  35.161  1.00 64.53 ? 226  SER A N   1 
ATOM   1840 C  CA  . SER A 1 227 ? -30.805 -7.047  35.493  1.00 68.40 ? 226  SER A CA  1 
ATOM   1841 C  C   . SER A 1 227 ? -31.698 -5.823  35.671  1.00 72.20 ? 226  SER A C   1 
ATOM   1842 O  O   . SER A 1 227 ? -32.819 -5.752  35.160  1.00 71.62 ? 226  SER A O   1 
ATOM   1843 C  CB  . SER A 1 227 ? -29.766 -6.777  34.404  1.00 67.62 ? 226  SER A CB  1 
ATOM   1844 O  OG  . SER A 1 227 ? -29.127 -5.528  34.605  1.00 67.80 ? 226  SER A OG  1 
ATOM   1845 N  N   . GLY A 1 228 ? -31.177 -4.848  36.412  1.00 76.48 ? 227  GLY A N   1 
ATOM   1846 C  CA  . GLY A 1 228 ? -31.850 -3.579  36.596  1.00 79.60 ? 227  GLY A CA  1 
ATOM   1847 C  C   . GLY A 1 228 ? -31.115 -2.451  35.903  1.00 82.90 ? 227  GLY A C   1 
ATOM   1848 O  O   . GLY A 1 228 ? -31.516 -1.286  35.992  1.00 84.02 ? 227  GLY A O   1 
ATOM   1849 N  N   . GLU A 1 229 ? -30.029 -2.791  35.211  1.00 84.05 ? 228  GLU A N   1 
ATOM   1850 C  CA  . GLU A 1 229 ? -29.240 -1.817  34.470  1.00 84.52 ? 228  GLU A CA  1 
ATOM   1851 C  C   . GLU A 1 229 ? -29.766 -1.696  33.046  1.00 83.65 ? 228  GLU A C   1 
ATOM   1852 O  O   . GLU A 1 229 ? -30.157 -2.690  32.426  1.00 84.36 ? 228  GLU A O   1 
ATOM   1853 C  CB  . GLU A 1 229 ? -27.762 -2.218  34.451  1.00 85.45 ? 228  GLU A CB  1 
ATOM   1854 C  CG  . GLU A 1 229 ? -27.187 -2.593  35.815  1.00 86.21 ? 228  GLU A CG  1 
ATOM   1855 C  CD  . GLU A 1 229 ? -27.086 -1.413  36.766  1.00 86.72 ? 228  GLU A CD  1 
ATOM   1856 O  OE1 . GLU A 1 229 ? -26.858 -0.279  36.293  1.00 86.24 ? 228  GLU A OE1 1 
ATOM   1857 O  OE2 . GLU A 1 229 ? -27.235 -1.620  37.990  1.00 87.39 ? 228  GLU A OE2 1 
ATOM   1858 N  N   . GLN A 1 230 ? -29.775 -0.468  32.533  1.00 81.39 ? 229  GLN A N   1 
ATOM   1859 C  CA  . GLN A 1 230 ? -30.242 -0.186  31.177  1.00 78.12 ? 229  GLN A CA  1 
ATOM   1860 C  C   . GLN A 1 230 ? -29.064 -0.341  30.223  1.00 74.30 ? 229  GLN A C   1 
ATOM   1861 O  O   . GLN A 1 230 ? -28.215 0.548   30.118  1.00 75.11 ? 229  GLN A O   1 
ATOM   1862 C  CB  . GLN A 1 230 ? -30.847 1.210   31.096  1.00 78.50 ? 229  GLN A CB  1 
ATOM   1863 C  CG  . GLN A 1 230 ? -32.135 1.372   31.882  1.00 80.11 ? 229  GLN A CG  1 
ATOM   1864 C  CD  . GLN A 1 230 ? -33.301 0.651   31.235  1.00 81.32 ? 229  GLN A CD  1 
ATOM   1865 O  OE1 . GLN A 1 230 ? -33.697 -0.431  31.669  1.00 81.81 ? 229  GLN A OE1 1 
ATOM   1866 N  NE2 . GLN A 1 230 ? -33.859 1.250   30.190  1.00 81.66 ? 229  GLN A NE2 1 
ATOM   1867 N  N   . SER A 1 231 ? -29.011 -1.471  29.525  1.00 68.91 ? 230  SER A N   1 
ATOM   1868 C  CA  . SER A 1 231 ? -27.940 -1.750  28.582  1.00 63.15 ? 230  SER A CA  1 
ATOM   1869 C  C   . SER A 1 231 ? -28.383 -1.430  27.160  1.00 57.72 ? 230  SER A C   1 
ATOM   1870 O  O   . SER A 1 231 ? -29.567 -1.514  26.821  1.00 57.21 ? 230  SER A O   1 
ATOM   1871 C  CB  . SER A 1 231 ? -27.497 -3.213  28.670  1.00 62.60 ? 230  SER A CB  1 
ATOM   1872 O  OG  . SER A 1 231 ? -26.910 -3.501  29.928  1.00 61.49 ? 230  SER A OG  1 
ATOM   1873 N  N   . ASP A 1 232 ? -27.410 -1.044  26.329  1.00 51.96 ? 231  ASP A N   1 
ATOM   1874 C  CA  . ASP A 1 232 ? -27.615 -0.841  24.905  1.00 48.43 ? 231  ASP A CA  1 
ATOM   1875 C  C   . ASP A 1 232 ? -26.433 -1.499  24.190  1.00 43.22 ? 231  ASP A C   1 
ATOM   1876 O  O   . ASP A 1 232 ? -25.528 -0.842  23.674  1.00 44.79 ? 231  ASP A O   1 
ATOM   1877 C  CB  . ASP A 1 232 ? -27.734 0.640   24.546  1.00 52.13 ? 231  ASP A CB  1 
ATOM   1878 C  CG  . ASP A 1 232 ? -28.048 0.858   23.075  1.00 57.58 ? 231  ASP A CG  1 
ATOM   1879 O  OD1 . ASP A 1 232 ? -28.446 -0.115  22.399  1.00 58.83 ? 231  ASP A OD1 1 
ATOM   1880 O  OD2 . ASP A 1 232 ? -27.895 2.000   22.592  1.00 60.46 ? 231  ASP A OD2 1 
ATOM   1881 N  N   . ASP A 1 233 ? -26.435 -2.831  24.171  1.00 34.61 ? 232  ASP A N   1 
ATOM   1882 C  CA  . ASP A 1 233 ? -25.333 -3.566  23.569  1.00 29.20 ? 232  ASP A CA  1 
ATOM   1883 C  C   . ASP A 1 233 ? -25.848 -4.621  22.600  1.00 28.62 ? 232  ASP A C   1 
ATOM   1884 O  O   . ASP A 1 233 ? -27.023 -4.602  22.209  1.00 28.16 ? 232  ASP A O   1 
ATOM   1885 C  CB  . ASP A 1 233 ? -24.457 -4.206  24.652  1.00 28.66 ? 232  ASP A CB  1 
ATOM   1886 C  CG  . ASP A 1 233 ? -25.227 -5.161  25.555  1.00 26.65 ? 232  ASP A CG  1 
ATOM   1887 O  OD1 . ASP A 1 233 ? -26.359 -5.561  25.210  1.00 25.53 ? 232  ASP A OD1 1 
ATOM   1888 O  OD2 . ASP A 1 233 ? -24.694 -5.502  26.630  1.00 27.17 ? 232  ASP A OD2 1 
ATOM   1889 N  N   . LEU A 1 234 ? -24.967 -5.541  22.202  1.00 25.15 ? 233  LEU A N   1 
ATOM   1890 C  CA  . LEU A 1 234 ? -25.341 -6.547  21.214  1.00 21.77 ? 233  LEU A CA  1 
ATOM   1891 C  C   . LEU A 1 234 ? -26.530 -7.377  21.693  1.00 19.24 ? 233  LEU A C   1 
ATOM   1892 O  O   . LEU A 1 234 ? -27.472 -7.629  20.930  1.00 17.58 ? 233  LEU A O   1 
ATOM   1893 C  CB  . LEU A 1 234 ? -24.127 -7.427  20.906  1.00 20.29 ? 233  LEU A CB  1 
ATOM   1894 C  CG  . LEU A 1 234 ? -24.215 -8.511  19.848  1.00 22.49 ? 233  LEU A CG  1 
ATOM   1895 C  CD1 . LEU A 1 234 ? -24.549 -7.931  18.467  1.00 24.87 ? 233  LEU A CD1 1 
ATOM   1896 C  CD2 . LEU A 1 234 ? -22.887 -9.275  19.815  1.00 22.66 ? 233  LEU A CD2 1 
ATOM   1897 N  N   . LEU A 1 235 ? -26.520 -7.783  22.964  1.00 21.68 ? 234  LEU A N   1 
ATOM   1898 C  CA  . LEU A 1 235 ? -27.615 -8.586  23.504  1.00 20.09 ? 234  LEU A CA  1 
ATOM   1899 C  C   . LEU A 1 235 ? -28.926 -7.802  23.521  1.00 23.48 ? 234  LEU A C   1 
ATOM   1900 O  O   . LEU A 1 235 ? -30.004 -8.375  23.309  1.00 24.07 ? 234  LEU A O   1 
ATOM   1901 C  CB  . LEU A 1 235 ? -27.257 -9.064  24.912  1.00 21.93 ? 234  LEU A CB  1 
ATOM   1902 C  CG  . LEU A 1 235 ? -28.267 -9.968  25.621  1.00 21.18 ? 234  LEU A CG  1 
ATOM   1903 C  CD1 . LEU A 1 235 ? -28.520 -11.206 24.782  1.00 23.99 ? 234  LEU A CD1 1 
ATOM   1904 C  CD2 . LEU A 1 235 ? -27.759 -10.354 27.010  1.00 25.47 ? 234  LEU A CD2 1 
ATOM   1905 N  N   . THR A 1 236 ? -28.855 -6.491  23.774  1.00 22.32 ? 235  THR A N   1 
ATOM   1906 C  CA  . THR A 1 236 ? -30.054 -5.655  23.716  1.00 22.41 ? 235  THR A CA  1 
ATOM   1907 C  C   . THR A 1 236 ? -30.723 -5.757  22.353  1.00 22.23 ? 235  THR A C   1 
ATOM   1908 O  O   . THR A 1 236 ? -31.950 -5.880  22.257  1.00 25.18 ? 235  THR A O   1 
ATOM   1909 C  CB  . THR A 1 236 ? -29.706 -4.195  24.024  1.00 23.87 ? 235  THR A CB  1 
ATOM   1910 O  OG1 . THR A 1 236 ? -29.069 -4.104  25.304  1.00 26.10 ? 235  THR A OG1 1 
ATOM   1911 C  CG2 . THR A 1 236 ? -30.961 -3.335  24.039  1.00 24.69 ? 235  THR A CG2 1 
ATOM   1912 N  N   . HIS A 1 237 ? -29.927 -5.673  21.281  1.00 20.77 ? 236  HIS A N   1 
ATOM   1913 C  CA  . HIS A 1 237 ? -30.477 -5.796  19.932  1.00 21.09 ? 236  HIS A CA  1 
ATOM   1914 C  C   . HIS A 1 237 ? -31.040 -7.191  19.681  1.00 21.10 ? 236  HIS A C   1 
ATOM   1915 O  O   . HIS A 1 237 ? -32.079 -7.335  19.026  1.00 22.72 ? 236  HIS A O   1 
ATOM   1916 C  CB  . HIS A 1 237 ? -29.403 -5.471  18.891  1.00 21.82 ? 236  HIS A CB  1 
ATOM   1917 C  CG  . HIS A 1 237 ? -29.126 -4.009  18.740  1.00 29.94 ? 236  HIS A CG  1 
ATOM   1918 N  ND1 . HIS A 1 237 ? -28.318 -3.309  19.612  1.00 31.45 ? 236  HIS A ND1 1 
ATOM   1919 C  CD2 . HIS A 1 237 ? -29.543 -3.114  17.812  1.00 33.00 ? 236  HIS A CD2 1 
ATOM   1920 C  CE1 . HIS A 1 237 ? -28.255 -2.045  19.230  1.00 34.87 ? 236  HIS A CE1 1 
ATOM   1921 N  NE2 . HIS A 1 237 ? -28.988 -1.901  18.139  1.00 33.14 ? 236  HIS A NE2 1 
ATOM   1922 N  N   . MET A 1 238 ? -30.352 -8.234  20.160  1.00 21.70 ? 237  MET A N   1 
ATOM   1923 C  CA  . MET A 1 238 ? -30.863 -9.590  19.984  1.00 21.64 ? 237  MET A CA  1 
ATOM   1924 C  C   . MET A 1 238 ? -32.239 -9.741  20.622  1.00 24.49 ? 237  MET A C   1 
ATOM   1925 O  O   . MET A 1 238 ? -33.138 -10.366 20.044  1.00 27.41 ? 237  MET A O   1 
ATOM   1926 C  CB  . MET A 1 238 ? -29.890 -10.613 20.580  1.00 19.03 ? 237  MET A CB  1 
ATOM   1927 C  CG  . MET A 1 238 ? -28.617 -10.882 19.765  1.00 17.34 ? 237  MET A CG  1 
ATOM   1928 S  SD  . MET A 1 238 ? -27.491 -11.980 20.674  1.00 22.19 ? 237  MET A SD  1 
ATOM   1929 C  CE  . MET A 1 238 ? -26.040 -11.988 19.617  1.00 21.67 ? 237  MET A CE  1 
ATOM   1930 N  N   . LEU A 1 239 ? -32.424 -9.172  21.816  1.00 22.85 ? 238  LEU A N   1 
ATOM   1931 C  CA  . LEU A 1 239 ? -33.667 -9.351  22.553  1.00 21.85 ? 238  LEU A CA  1 
ATOM   1932 C  C   . LEU A 1 239 ? -34.771 -8.392  22.116  1.00 26.96 ? 238  LEU A C   1 
ATOM   1933 O  O   . LEU A 1 239 ? -35.951 -8.692  22.330  1.00 30.07 ? 238  LEU A O   1 
ATOM   1934 C  CB  . LEU A 1 239 ? -33.413 -9.189  24.059  1.00 22.22 ? 238  LEU A CB  1 
ATOM   1935 C  CG  . LEU A 1 239 ? -32.410 -10.142 24.724  1.00 24.50 ? 238  LEU A CG  1 
ATOM   1936 C  CD1 . LEU A 1 239 ? -32.104 -9.733  26.167  1.00 24.82 ? 238  LEU A CD1 1 
ATOM   1937 C  CD2 . LEU A 1 239 ? -32.904 -11.584 24.664  1.00 28.35 ? 238  LEU A CD2 1 
ATOM   1938 N  N   . ASN A 1 240 ? -34.436 -7.255  21.507  1.00 29.42 ? 239  ASN A N   1 
ATOM   1939 C  CA  . ASN A 1 240 ? -35.437 -6.224  21.252  1.00 30.00 ? 239  ASN A CA  1 
ATOM   1940 C  C   . ASN A 1 240 ? -35.535 -5.752  19.808  1.00 28.70 ? 239  ASN A C   1 
ATOM   1941 O  O   . ASN A 1 240 ? -36.582 -5.207  19.438  1.00 29.47 ? 239  ASN A O   1 
ATOM   1942 C  CB  . ASN A 1 240 ? -35.178 -5.005  22.149  1.00 32.32 ? 239  ASN A CB  1 
ATOM   1943 C  CG  . ASN A 1 240 ? -35.132 -5.374  23.622  1.00 37.45 ? 239  ASN A CG  1 
ATOM   1944 O  OD1 . ASN A 1 240 ? -36.168 -5.501  24.269  1.00 41.43 ? 239  ASN A OD1 1 
ATOM   1945 N  ND2 . ASN A 1 240 ? -33.928 -5.566  24.153  1.00 39.47 ? 239  ASN A ND2 1 
ATOM   1946 N  N   . GLY A 1 241 ? -34.506 -5.929  18.986  1.00 28.05 ? 240  GLY A N   1 
ATOM   1947 C  CA  . GLY A 1 241 ? -34.560 -5.415  17.630  1.00 27.52 ? 240  GLY A CA  1 
ATOM   1948 C  C   . GLY A 1 241 ? -35.605 -6.122  16.787  1.00 27.45 ? 240  GLY A C   1 
ATOM   1949 O  O   . GLY A 1 241 ? -35.888 -7.307  16.960  1.00 28.94 ? 240  GLY A O   1 
ATOM   1950 N  N   . LYS A 1 242 ? -36.191 -5.371  15.857  1.00 27.35 ? 241  LYS A N   1 
ATOM   1951 C  CA  . LYS A 1 242 ? -37.171 -5.898  14.917  1.00 28.34 ? 241  LYS A CA  1 
ATOM   1952 C  C   . LYS A 1 242 ? -36.622 -5.787  13.504  1.00 26.91 ? 241  LYS A C   1 
ATOM   1953 O  O   . LYS A 1 242 ? -36.081 -4.742  13.127  1.00 26.94 ? 241  LYS A O   1 
ATOM   1954 C  CB  . LYS A 1 242 ? -38.502 -5.147  15.012  1.00 33.11 ? 241  LYS A CB  1 
ATOM   1955 C  CG  . LYS A 1 242 ? -39.539 -5.807  15.909  1.00 38.99 ? 241  LYS A CG  1 
ATOM   1956 C  CD  . LYS A 1 242 ? -39.088 -5.859  17.350  1.00 42.94 ? 241  LYS A CD  1 
ATOM   1957 C  CE  . LYS A 1 242 ? -40.221 -6.311  18.260  1.00 48.29 ? 241  LYS A CE  1 
ATOM   1958 N  NZ  . LYS A 1 242 ? -39.768 -6.514  19.667  1.00 51.83 ? 241  LYS A NZ  1 
ATOM   1959 N  N   . ASP A 1 243 ? -36.775 -6.854  12.729  1.00 24.20 ? 242  ASP A N   1 
ATOM   1960 C  CA  . ASP A 1 243 ? -36.332 -6.855  11.335  1.00 24.89 ? 242  ASP A CA  1 
ATOM   1961 C  C   . ASP A 1 243 ? -37.235 -5.949  10.512  1.00 26.69 ? 242  ASP A C   1 
ATOM   1962 O  O   . ASP A 1 243 ? -38.457 -6.147  10.511  1.00 31.69 ? 242  ASP A O   1 
ATOM   1963 C  CB  . ASP A 1 243 ? -36.347 -8.279  10.775  1.00 23.77 ? 242  ASP A CB  1 
ATOM   1964 C  CG  . ASP A 1 243 ? -36.121 -8.328  9.266   1.00 22.04 ? 242  ASP A CG  1 
ATOM   1965 O  OD1 . ASP A 1 243 ? -35.576 -7.357  8.699   1.00 22.78 ? 242  ASP A OD1 1 
ATOM   1966 O  OD2 . ASP A 1 243 ? -36.498 -9.345  8.643   1.00 23.48 ? 242  ASP A OD2 1 
ATOM   1967 N  N   . PRO A 1 244 ? -36.697 -4.955  9.803   1.00 31.41 ? 243  PRO A N   1 
ATOM   1968 C  CA  . PRO A 1 244 ? -37.565 -4.122  8.954   1.00 33.06 ? 243  PRO A CA  1 
ATOM   1969 C  C   . PRO A 1 244 ? -38.300 -4.909  7.876   1.00 35.24 ? 243  PRO A C   1 
ATOM   1970 O  O   . PRO A 1 244 ? -39.425 -4.542  7.517   1.00 39.02 ? 243  PRO A O   1 
ATOM   1971 C  CB  . PRO A 1 244 ? -36.586 -3.105  8.350   1.00 36.53 ? 243  PRO A CB  1 
ATOM   1972 C  CG  . PRO A 1 244 ? -35.421 -3.084  9.303   1.00 36.53 ? 243  PRO A CG  1 
ATOM   1973 C  CD  . PRO A 1 244 ? -35.301 -4.484  9.811   1.00 34.00 ? 243  PRO A CD  1 
ATOM   1974 N  N   . GLU A 1 245 ? -37.709 -5.984  7.347   1.00 39.00 ? 244  GLU A N   1 
ATOM   1975 C  CA  . GLU A 1 245 ? -38.334 -6.716  6.247   1.00 39.44 ? 244  GLU A CA  1 
ATOM   1976 C  C   . GLU A 1 245 ? -39.500 -7.576  6.732   1.00 39.64 ? 244  GLU A C   1 
ATOM   1977 O  O   . GLU A 1 245 ? -40.651 -7.356  6.339   1.00 42.92 ? 244  GLU A O   1 
ATOM   1978 C  CB  . GLU A 1 245 ? -37.290 -7.574  5.522   1.00 42.28 ? 244  GLU A CB  1 
ATOM   1979 C  CG  . GLU A 1 245 ? -37.870 -8.415  4.395   1.00 46.77 ? 244  GLU A CG  1 
ATOM   1980 C  CD  . GLU A 1 245 ? -36.816 -9.190  3.621   1.00 50.55 ? 244  GLU A CD  1 
ATOM   1981 O  OE1 . GLU A 1 245 ? -35.644 -9.215  4.056   1.00 46.74 ? 244  GLU A OE1 1 
ATOM   1982 O  OE2 . GLU A 1 245 ? -37.163 -9.773  2.570   1.00 53.97 ? 244  GLU A OE2 1 
ATOM   1983 N  N   . THR A 1 246 ? -39.221 -8.571  7.580   1.00 35.04 ? 245  THR A N   1 
ATOM   1984 C  CA  . THR A 1 246 ? -40.280 -9.440  8.089   1.00 33.75 ? 245  THR A CA  1 
ATOM   1985 C  C   . THR A 1 246 ? -41.079 -8.797  9.216   1.00 33.57 ? 245  THR A C   1 
ATOM   1986 O  O   . THR A 1 246 ? -42.198 -9.241  9.491   1.00 35.08 ? 245  THR A O   1 
ATOM   1987 C  CB  . THR A 1 246 ? -39.702 -10.777 8.586   1.00 31.84 ? 245  THR A CB  1 
ATOM   1988 O  OG1 . THR A 1 246 ? -38.777 -10.545 9.660   1.00 28.60 ? 245  THR A OG1 1 
ATOM   1989 C  CG2 . THR A 1 246 ? -38.991 -11.534 7.452   1.00 32.63 ? 245  THR A CG2 1 
ATOM   1990 N  N   . GLY A 1 247 ? -40.534 -7.776  9.876   1.00 34.90 ? 246  GLY A N   1 
ATOM   1991 C  CA  . GLY A 1 247 ? -41.195 -7.130  10.994  1.00 34.16 ? 246  GLY A CA  1 
ATOM   1992 C  C   . GLY A 1 247 ? -41.054 -7.841  12.325  1.00 35.09 ? 246  GLY A C   1 
ATOM   1993 O  O   . GLY A 1 247 ? -41.477 -7.290  13.353  1.00 35.37 ? 246  GLY A O   1 
ATOM   1994 N  N   . GLU A 1 248 ? -40.447 -9.057  12.349  1.00 32.89 ? 247  GLU A N   1 
ATOM   1995 C  CA  . GLU A 1 248 ? -40.325 -9.986  13.459  1.00 27.46 ? 247  GLU A CA  1 
ATOM   1996 C  C   . GLU A 1 248 ? -39.023 -9.761  14.230  1.00 26.12 ? 247  GLU A C   1 
ATOM   1997 O  O   . GLU A 1 248 ? -38.007 -9.365  13.650  1.00 26.30 ? 247  GLU A O   1 
ATOM   1998 C  CB  . GLU A 1 248 ? -40.359 -11.428 12.948  1.00 28.28 ? 247  GLU A CB  1 
ATOM   1999 C  CG  . GLU A 1 248 ? -41.562 -11.771 12.063  1.00 30.69 ? 247  GLU A CG  1 
ATOM   2000 C  CD  . GLU A 1 248 ? -41.472 -13.171 11.465  1.00 32.30 ? 247  GLU A CD  1 
ATOM   2001 O  OE1 . GLU A 1 248 ? -40.444 -13.849 11.682  1.00 31.39 ? 247  GLU A OE1 1 
ATOM   2002 O  OE2 . GLU A 1 248 ? -42.425 -13.593 10.772  1.00 31.17 ? 247  GLU A OE2 1 
ATOM   2003 N  N   . PRO A 1 249 ? -39.038 -10.001 15.536  1.00 23.87 ? 248  PRO A N   1 
ATOM   2004 C  CA  . PRO A 1 249 ? -37.792 -10.122 16.296  1.00 21.70 ? 248  PRO A CA  1 
ATOM   2005 C  C   . PRO A 1 249 ? -37.269 -11.550 16.185  1.00 20.79 ? 248  PRO A C   1 
ATOM   2006 O  O   . PRO A 1 249 ? -37.965 -12.458 15.725  1.00 21.67 ? 248  PRO A O   1 
ATOM   2007 C  CB  . PRO A 1 249 ? -38.234 -9.804  17.729  1.00 24.22 ? 248  PRO A CB  1 
ATOM   2008 C  CG  . PRO A 1 249 ? -39.638 -10.357 17.788  1.00 27.23 ? 248  PRO A CG  1 
ATOM   2009 C  CD  . PRO A 1 249 ? -40.230 -10.161 16.394  1.00 25.30 ? 248  PRO A CD  1 
ATOM   2010 N  N   . LEU A 1 250 ? -36.016 -11.730 16.595  1.00 17.42 ? 249  LEU A N   1 
ATOM   2011 C  CA  . LEU A 1 250 ? -35.476 -13.082 16.702  1.00 15.85 ? 249  LEU A CA  1 
ATOM   2012 C  C   . LEU A 1 250 ? -36.230 -13.850 17.775  1.00 18.22 ? 249  LEU A C   1 
ATOM   2013 O  O   . LEU A 1 250 ? -36.691 -13.272 18.760  1.00 20.39 ? 249  LEU A O   1 
ATOM   2014 C  CB  . LEU A 1 250 ? -33.987 -13.052 17.051  1.00 16.87 ? 249  LEU A CB  1 
ATOM   2015 C  CG  . LEU A 1 250 ? -33.087 -12.307 16.064  1.00 16.92 ? 249  LEU A CG  1 
ATOM   2016 C  CD1 . LEU A 1 250 ? -31.649 -12.395 16.519  1.00 17.25 ? 249  LEU A CD1 1 
ATOM   2017 C  CD2 . LEU A 1 250 ? -33.235 -12.881 14.657  1.00 18.39 ? 249  LEU A CD2 1 
ATOM   2018 N  N   . ASP A 1 251 ? -36.361 -15.164 17.588  1.00 20.65 ? 250  ASP A N   1 
ATOM   2019 C  CA  . ASP A 1 251 ? -36.971 -15.960 18.647  1.00 22.54 ? 250  ASP A CA  1 
ATOM   2020 C  C   . ASP A 1 251 ? -35.897 -16.554 19.559  1.00 22.87 ? 250  ASP A C   1 
ATOM   2021 O  O   . ASP A 1 251 ? -34.697 -16.474 19.288  1.00 21.26 ? 250  ASP A O   1 
ATOM   2022 C  CB  . ASP A 1 251 ? -37.886 -17.050 18.071  1.00 26.30 ? 250  ASP A CB  1 
ATOM   2023 C  CG  . ASP A 1 251 ? -37.139 -18.143 17.325  1.00 27.89 ? 250  ASP A CG  1 
ATOM   2024 O  OD1 . ASP A 1 251 ? -35.893 -18.225 17.381  1.00 24.53 ? 250  ASP A OD1 1 
ATOM   2025 O  OD2 . ASP A 1 251 ? -37.829 -18.943 16.668  1.00 33.98 ? 250  ASP A OD2 1 
ATOM   2026 N  N   . ASP A 1 252 ? -36.353 -17.152 20.665  1.00 23.04 ? 251  ASP A N   1 
ATOM   2027 C  CA  . ASP A 1 252 ? -35.432 -17.569 21.720  1.00 26.40 ? 251  ASP A CA  1 
ATOM   2028 C  C   . ASP A 1 252 ? -34.405 -18.576 21.216  1.00 24.92 ? 251  ASP A C   1 
ATOM   2029 O  O   . ASP A 1 252 ? -33.227 -18.493 21.577  1.00 24.53 ? 251  ASP A O   1 
ATOM   2030 C  CB  . ASP A 1 252 ? -36.208 -18.149 22.902  1.00 30.41 ? 251  ASP A CB  1 
ATOM   2031 C  CG  . ASP A 1 252 ? -36.805 -17.074 23.789  1.00 36.53 ? 251  ASP A CG  1 
ATOM   2032 O  OD1 . ASP A 1 252 ? -36.562 -15.876 23.531  1.00 39.26 ? 251  ASP A OD1 1 
ATOM   2033 O  OD2 . ASP A 1 252 ? -37.516 -17.427 24.750  1.00 38.18 ? 251  ASP A OD2 1 
ATOM   2034 N  N   . GLU A 1 253 ? -34.828 -19.546 20.398  1.00 27.31 ? 252  GLU A N   1 
ATOM   2035 C  CA  . GLU A 1 253 ? -33.877 -20.537 19.894  1.00 24.44 ? 252  GLU A CA  1 
ATOM   2036 C  C   . GLU A 1 253 ? -32.772 -19.873 19.076  1.00 21.48 ? 252  GLU A C   1 
ATOM   2037 O  O   . GLU A 1 253 ? -31.582 -20.160 19.265  1.00 21.62 ? 252  GLU A O   1 
ATOM   2038 C  CB  . GLU A 1 253 ? -34.594 -21.605 19.063  1.00 26.83 ? 252  GLU A CB  1 
ATOM   2039 C  CG  . GLU A 1 253 ? -33.657 -22.731 18.621  1.00 30.39 ? 252  GLU A CG  1 
ATOM   2040 C  CD  . GLU A 1 253 ? -34.300 -23.716 17.659  1.00 37.21 ? 252  GLU A CD  1 
ATOM   2041 O  OE1 . GLU A 1 253 ? -35.066 -24.584 18.117  1.00 40.01 ? 252  GLU A OE1 1 
ATOM   2042 O  OE2 . GLU A 1 253 ? -34.041 -23.624 16.440  1.00 38.97 ? 252  GLU A OE2 1 
ATOM   2043 N  N   . ASN A 1 254 ? -33.143 -18.982 18.150  1.00 17.52 ? 253  ASN A N   1 
ATOM   2044 C  CA  . ASN A 1 254 ? -32.120 -18.347 17.324  1.00 15.51 ? 253  ASN A CA  1 
ATOM   2045 C  C   . ASN A 1 254 ? -31.222 -17.428 18.149  1.00 15.83 ? 253  ASN A C   1 
ATOM   2046 O  O   . ASN A 1 254 ? -30.016 -17.336 17.886  1.00 16.07 ? 253  ASN A O   1 
ATOM   2047 C  CB  . ASN A 1 254 ? -32.765 -17.575 16.175  1.00 17.36 ? 253  ASN A CB  1 
ATOM   2048 C  CG  . ASN A 1 254 ? -31.738 -17.023 15.211  1.00 16.16 ? 253  ASN A CG  1 
ATOM   2049 O  OD1 . ASN A 1 254 ? -31.441 -15.835 15.224  1.00 17.59 ? 253  ASN A OD1 1 
ATOM   2050 N  ND2 . ASN A 1 254 ? -31.170 -17.897 14.384  1.00 14.51 ? 253  ASN A ND2 1 
ATOM   2051 N  N   . ILE A 1 255 ? -31.785 -16.726 19.137  1.00 15.71 ? 254  ILE A N   1 
ATOM   2052 C  CA  . ILE A 1 255 ? -30.959 -15.867 19.991  1.00 16.67 ? 254  ILE A CA  1 
ATOM   2053 C  C   . ILE A 1 255 ? -29.845 -16.678 20.646  1.00 16.32 ? 254  ILE A C   1 
ATOM   2054 O  O   . ILE A 1 255 ? -28.683 -16.251 20.685  1.00 16.84 ? 254  ILE A O   1 
ATOM   2055 C  CB  . ILE A 1 255 ? -31.824 -15.141 21.041  1.00 16.69 ? 254  ILE A CB  1 
ATOM   2056 C  CG1 . ILE A 1 255 ? -32.707 -14.076 20.381  1.00 19.65 ? 254  ILE A CG1 1 
ATOM   2057 C  CG2 . ILE A 1 255 ? -30.934 -14.493 22.110  1.00 19.23 ? 254  ILE A CG2 1 
ATOM   2058 C  CD1 . ILE A 1 255 ? -33.746 -13.488 21.302  1.00 21.40 ? 254  ILE A CD1 1 
ATOM   2059 N  N   . ARG A 1 256 ? -30.178 -17.866 21.169  1.00 17.05 ? 255  ARG A N   1 
ATOM   2060 C  CA  . ARG A 1 256 ? -29.158 -18.709 21.794  1.00 16.21 ? 255  ARG A CA  1 
ATOM   2061 C  C   . ARG A 1 256 ? -28.052 -19.058 20.807  1.00 15.16 ? 255  ARG A C   1 
ATOM   2062 O  O   . ARG A 1 256 ? -26.865 -19.067 21.167  1.00 14.98 ? 255  ARG A O   1 
ATOM   2063 C  CB  . ARG A 1 256 ? -29.789 -19.985 22.358  1.00 19.43 ? 255  ARG A CB  1 
ATOM   2064 C  CG  . ARG A 1 256 ? -30.758 -19.747 23.508  1.00 27.47 ? 255  ARG A CG  1 
ATOM   2065 C  CD  . ARG A 1 256 ? -31.317 -21.052 24.086  1.00 36.57 ? 255  ARG A CD  1 
ATOM   2066 N  NE  . ARG A 1 256 ? -30.293 -21.873 24.726  1.00 41.57 ? 255  ARG A NE  1 
ATOM   2067 C  CZ  . ARG A 1 256 ? -29.939 -21.789 26.002  1.00 46.95 ? 255  ARG A CZ  1 
ATOM   2068 N  NH1 . ARG A 1 256 ? -30.525 -20.937 26.831  1.00 47.16 ? 255  ARG A NH1 1 
ATOM   2069 N  NH2 . ARG A 1 256 ? -28.971 -22.581 26.460  1.00 48.27 ? 255  ARG A NH2 1 
ATOM   2070 N  N   . TYR A 1 257 ? -28.422 -19.351 19.555  1.00 15.21 ? 256  TYR A N   1 
ATOM   2071 C  CA  . TYR A 1 257 ? -27.423 -19.645 18.533  1.00 13.58 ? 256  TYR A CA  1 
ATOM   2072 C  C   . TYR A 1 257 ? -26.556 -18.430 18.228  1.00 11.82 ? 256  TYR A C   1 
ATOM   2073 O  O   . TYR A 1 257 ? -25.352 -18.571 17.985  1.00 12.89 ? 256  TYR A O   1 
ATOM   2074 C  CB  . TYR A 1 257 ? -28.104 -20.132 17.253  1.00 13.93 ? 256  TYR A CB  1 
ATOM   2075 C  CG  . TYR A 1 257 ? -28.616 -21.557 17.321  1.00 16.97 ? 256  TYR A CG  1 
ATOM   2076 C  CD1 . TYR A 1 257 ? -27.856 -22.565 17.907  1.00 20.03 ? 256  TYR A CD1 1 
ATOM   2077 C  CD2 . TYR A 1 257 ? -29.860 -21.895 16.791  1.00 19.46 ? 256  TYR A CD2 1 
ATOM   2078 C  CE1 . TYR A 1 257 ? -28.320 -23.875 17.961  1.00 20.79 ? 256  TYR A CE1 1 
ATOM   2079 C  CE2 . TYR A 1 257 ? -30.335 -23.198 16.852  1.00 20.15 ? 256  TYR A CE2 1 
ATOM   2080 C  CZ  . TYR A 1 257 ? -29.564 -24.183 17.435  1.00 23.39 ? 256  TYR A CZ  1 
ATOM   2081 O  OH  . TYR A 1 257 ? -30.045 -25.475 17.484  1.00 28.21 ? 256  TYR A OH  1 
ATOM   2082 N  N   . GLN A 1 258 ? -27.150 -17.229 18.204  1.00 14.16 ? 257  GLN A N   1 
ATOM   2083 C  CA  . GLN A 1 258 ? -26.353 -16.032 17.940  1.00 12.91 ? 257  GLN A CA  1 
ATOM   2084 C  C   . GLN A 1 258 ? -25.351 -15.777 19.063  1.00 13.10 ? 257  GLN A C   1 
ATOM   2085 O  O   . GLN A 1 258 ? -24.215 -15.390 18.798  1.00 13.14 ? 257  GLN A O   1 
ATOM   2086 C  CB  . GLN A 1 258 ? -27.247 -14.797 17.742  1.00 12.98 ? 257  GLN A CB  1 
ATOM   2087 C  CG  . GLN A 1 258 ? -28.312 -14.900 16.642  1.00 14.34 ? 257  GLN A CG  1 
ATOM   2088 C  CD  . GLN A 1 258 ? -27.745 -15.070 15.220  1.00 14.26 ? 257  GLN A CD  1 
ATOM   2089 O  OE1 . GLN A 1 258 ? -26.529 -15.024 14.997  1.00 13.71 ? 257  GLN A OE1 1 
ATOM   2090 N  NE2 . GLN A 1 258 ? -28.637 -15.262 14.258  1.00 12.28 ? 257  GLN A NE2 1 
ATOM   2091 N  N   . ILE A 1 259 ? -25.756 -15.968 20.325  1.00 13.10 ? 258  ILE A N   1 
ATOM   2092 C  CA  . ILE A 1 259 ? -24.826 -15.745 21.433  1.00 13.39 ? 258  ILE A CA  1 
ATOM   2093 C  C   . ILE A 1 259 ? -23.635 -16.692 21.326  1.00 13.77 ? 258  ILE A C   1 
ATOM   2094 O  O   . ILE A 1 259 ? -22.476 -16.274 21.444  1.00 14.23 ? 258  ILE A O   1 
ATOM   2095 C  CB  . ILE A 1 259 ? -25.544 -15.887 22.788  1.00 14.57 ? 258  ILE A CB  1 
ATOM   2096 C  CG1 . ILE A 1 259 ? -26.617 -14.805 22.940  1.00 16.94 ? 258  ILE A CG1 1 
ATOM   2097 C  CG2 . ILE A 1 259 ? -24.540 -15.763 23.940  1.00 14.22 ? 258  ILE A CG2 1 
ATOM   2098 C  CD1 . ILE A 1 259 ? -27.495 -14.956 24.193  1.00 17.91 ? 258  ILE A CD1 1 
ATOM   2099 N  N   . ILE A 1 260 ? -23.899 -17.983 21.089  1.00 13.92 ? 259  ILE A N   1 
ATOM   2100 C  CA  . ILE A 1 260 ? -22.811 -18.938 20.876  1.00 13.19 ? 259  ILE A CA  1 
ATOM   2101 C  C   . ILE A 1 260 ? -21.919 -18.479 19.728  1.00 12.51 ? 259  ILE A C   1 
ATOM   2102 O  O   . ILE A 1 260 ? -20.686 -18.469 19.834  1.00 12.74 ? 259  ILE A O   1 
ATOM   2103 C  CB  . ILE A 1 260 ? -23.381 -20.346 20.618  1.00 15.15 ? 259  ILE A CB  1 
ATOM   2104 C  CG1 . ILE A 1 260 ? -24.036 -20.890 21.892  1.00 21.10 ? 259  ILE A CG1 1 
ATOM   2105 C  CG2 . ILE A 1 260 ? -22.297 -21.284 20.084  1.00 19.51 ? 259  ILE A CG2 1 
ATOM   2106 C  CD1 . ILE A 1 260 ? -24.734 -22.221 21.708  1.00 25.35 ? 259  ILE A CD1 1 
ATOM   2107 N  N   . THR A 1 261 ? -22.539 -18.098 18.611  1.00 11.85 ? 260  THR A N   1 
ATOM   2108 C  CA  . THR A 1 261 ? -21.792 -17.669 17.430  1.00 12.21 ? 260  THR A CA  1 
ATOM   2109 C  C   . THR A 1 261 ? -20.872 -16.497 17.743  1.00 13.75 ? 260  THR A C   1 
ATOM   2110 O  O   . THR A 1 261 ? -19.685 -16.505 17.381  1.00 14.71 ? 260  THR A O   1 
ATOM   2111 C  CB  . THR A 1 261 ? -22.772 -17.296 16.315  1.00 13.42 ? 260  THR A CB  1 
ATOM   2112 O  OG1 . THR A 1 261 ? -23.526 -18.456 15.941  1.00 13.48 ? 260  THR A OG1 1 
ATOM   2113 C  CG2 . THR A 1 261 ? -22.037 -16.744 15.088  1.00 14.36 ? 260  THR A CG2 1 
ATOM   2114 N  N   . PHE A 1 262 ? -21.403 -15.464 18.405  1.00 12.50 ? 261  PHE A N   1 
ATOM   2115 C  CA  . PHE A 1 262 ? -20.594 -14.270 18.620  1.00 13.33 ? 261  PHE A CA  1 
ATOM   2116 C  C   . PHE A 1 262 ? -19.537 -14.480 19.699  1.00 13.26 ? 261  PHE A C   1 
ATOM   2117 O  O   . PHE A 1 262 ? -18.459 -13.880 19.621  1.00 14.57 ? 261  PHE A O   1 
ATOM   2118 C  CB  . PHE A 1 262 ? -21.497 -13.072 18.937  1.00 13.15 ? 261  PHE A CB  1 
ATOM   2119 C  CG  . PHE A 1 262 ? -22.087 -12.424 17.700  1.00 12.66 ? 261  PHE A CG  1 
ATOM   2120 C  CD1 . PHE A 1 262 ? -21.406 -11.409 17.047  1.00 15.75 ? 261  PHE A CD1 1 
ATOM   2121 C  CD2 . PHE A 1 262 ? -23.302 -12.850 17.176  1.00 18.64 ? 261  PHE A CD2 1 
ATOM   2122 C  CE1 . PHE A 1 262 ? -21.936 -10.811 15.902  1.00 15.85 ? 261  PHE A CE1 1 
ATOM   2123 C  CE2 . PHE A 1 262 ? -23.835 -12.265 16.041  1.00 17.38 ? 261  PHE A CE2 1 
ATOM   2124 C  CZ  . PHE A 1 262 ? -23.150 -11.242 15.397  1.00 17.82 ? 261  PHE A CZ  1 
ATOM   2125 N  N   . LEU A 1 263 ? -19.809 -15.322 20.706  1.00 13.98 ? 262  LEU A N   1 
ATOM   2126 C  CA  . LEU A 1 263 ? -18.765 -15.617 21.687  1.00 16.18 ? 262  LEU A CA  1 
ATOM   2127 C  C   . LEU A 1 263 ? -17.582 -16.321 21.044  1.00 16.00 ? 262  LEU A C   1 
ATOM   2128 O  O   . LEU A 1 263 ? -16.437 -16.104 21.453  1.00 18.09 ? 262  LEU A O   1 
ATOM   2129 C  CB  . LEU A 1 263 ? -19.309 -16.469 22.832  1.00 14.26 ? 262  LEU A CB  1 
ATOM   2130 C  CG  . LEU A 1 263 ? -20.251 -15.723 23.772  1.00 13.17 ? 262  LEU A CG  1 
ATOM   2131 C  CD1 . LEU A 1 263 ? -20.842 -16.668 24.800  1.00 14.80 ? 262  LEU A CD1 1 
ATOM   2132 C  CD2 . LEU A 1 263 ? -19.504 -14.575 24.449  1.00 14.48 ? 262  LEU A CD2 1 
ATOM   2133 N  N   . ILE A 1 264 ? -17.839 -17.169 20.050  1.00 15.96 ? 263  ILE A N   1 
ATOM   2134 C  CA  . ILE A 1 264 ? -16.760 -17.883 19.372  1.00 16.11 ? 263  ILE A CA  1 
ATOM   2135 C  C   . ILE A 1 264 ? -16.132 -17.011 18.291  1.00 13.71 ? 263  ILE A C   1 
ATOM   2136 O  O   . ILE A 1 264 ? -14.929 -16.718 18.321  1.00 16.99 ? 263  ILE A O   1 
ATOM   2137 C  CB  . ILE A 1 264 ? -17.283 -19.210 18.796  1.00 17.09 ? 263  ILE A CB  1 
ATOM   2138 C  CG1 . ILE A 1 264 ? -17.658 -20.151 19.945  1.00 19.95 ? 263  ILE A CG1 1 
ATOM   2139 C  CG2 . ILE A 1 264 ? -16.256 -19.836 17.868  1.00 17.34 ? 263  ILE A CG2 1 
ATOM   2140 C  CD1 . ILE A 1 264 ? -18.322 -21.437 19.494  1.00 22.77 ? 263  ILE A CD1 1 
ATOM   2141 N  N   . ALA A 1 265 ? -16.940 -16.579 17.319  1.00 14.73 ? 264  ALA A N   1 
ATOM   2142 C  CA  . ALA A 1 265 ? -16.406 -15.809 16.198  1.00 15.31 ? 264  ALA A CA  1 
ATOM   2143 C  C   . ALA A 1 265 ? -15.931 -14.435 16.633  1.00 14.69 ? 264  ALA A C   1 
ATOM   2144 O  O   . ALA A 1 265 ? -15.052 -13.849 15.984  1.00 16.86 ? 264  ALA A O   1 
ATOM   2145 C  CB  . ALA A 1 265 ? -17.459 -15.663 15.093  1.00 15.86 ? 264  ALA A CB  1 
ATOM   2146 N  N   . GLY A 1 266 ? -16.497 -13.906 17.714  1.00 15.45 ? 265  GLY A N   1 
ATOM   2147 C  CA  . GLY A 1 266 ? -16.181 -12.587 18.218  1.00 16.19 ? 265  GLY A CA  1 
ATOM   2148 C  C   . GLY A 1 266 ? -14.909 -12.471 19.024  1.00 16.29 ? 265  GLY A C   1 
ATOM   2149 O  O   . GLY A 1 266 ? -14.576 -11.364 19.452  1.00 18.32 ? 265  GLY A O   1 
ATOM   2150 N  N   . HIS A 1 267 ? -14.194 -13.574 19.264  1.00 15.61 ? 266  HIS A N   1 
ATOM   2151 C  CA  . HIS A 1 267 ? -12.915 -13.498 19.972  1.00 15.23 ? 266  HIS A CA  1 
ATOM   2152 C  C   . HIS A 1 267 ? -11.804 -14.356 19.381  1.00 17.26 ? 266  HIS A C   1 
ATOM   2153 O  O   . HIS A 1 267 ? -10.636 -13.965 19.484  1.00 15.43 ? 266  HIS A O   1 
ATOM   2154 C  CB  . HIS A 1 267 ? -13.091 -13.891 21.449  1.00 16.42 ? 266  HIS A CB  1 
ATOM   2155 C  CG  . HIS A 1 267 ? -12.802 -15.336 21.730  1.00 17.43 ? 266  HIS A CG  1 
ATOM   2156 N  ND1 . HIS A 1 267 ? -13.750 -16.326 21.592  1.00 18.87 ? 266  HIS A ND1 1 
ATOM   2157 C  CD2 . HIS A 1 267 ? -11.667 -15.958 22.131  1.00 18.81 ? 266  HIS A CD2 1 
ATOM   2158 C  CE1 . HIS A 1 267 ? -13.217 -17.493 21.906  1.00 18.61 ? 266  HIS A CE1 1 
ATOM   2159 N  NE2 . HIS A 1 267 ? -11.951 -17.299 22.230  1.00 19.40 ? 266  HIS A NE2 1 
ATOM   2160 N  N   . GLU A 1 268 ? -12.104 -15.506 18.778  1.00 16.06 ? 267  GLU A N   1 
ATOM   2161 C  CA  . GLU A 1 268 ? -11.049 -16.467 18.468  1.00 16.29 ? 267  GLU A CA  1 
ATOM   2162 C  C   . GLU A 1 268 ? -10.132 -15.952 17.362  1.00 17.17 ? 267  GLU A C   1 
ATOM   2163 O  O   . GLU A 1 268 ? -8.900  -16.019 17.478  1.00 19.39 ? 267  GLU A O   1 
ATOM   2164 C  CB  . GLU A 1 268 ? -11.683 -17.803 18.093  1.00 15.59 ? 267  GLU A CB  1 
ATOM   2165 C  CG  . GLU A 1 268 ? -10.807 -18.709 17.255  1.00 19.73 ? 267  GLU A CG  1 
ATOM   2166 C  CD  . GLU A 1 268 ? -9.577  -19.189 17.987  1.00 26.26 ? 267  GLU A CD  1 
ATOM   2167 O  OE1 . GLU A 1 268 ? -9.606  -19.243 19.232  1.00 25.38 ? 267  GLU A OE1 1 
ATOM   2168 O  OE2 . GLU A 1 268 ? -8.582  -19.524 17.306  1.00 29.82 ? 267  GLU A OE2 1 
ATOM   2169 N  N   . THR A 1 269 ? -10.708 -15.403 16.299  1.00 12.53 ? 268  THR A N   1 
ATOM   2170 C  CA  . THR A 1 269 ? -9.882  -14.928 15.193  1.00 12.57 ? 268  THR A CA  1 
ATOM   2171 C  C   . THR A 1 269 ? -9.140  -13.638 15.534  1.00 13.46 ? 268  THR A C   1 
ATOM   2172 O  O   . THR A 1 269 ? -8.038  -13.410 15.019  1.00 14.60 ? 268  THR A O   1 
ATOM   2173 C  CB  . THR A 1 269 ? -10.755 -14.737 13.957  1.00 14.69 ? 268  THR A CB  1 
ATOM   2174 O  OG1 . THR A 1 269 ? -11.966 -14.083 14.350  1.00 16.49 ? 268  THR A OG1 1 
ATOM   2175 C  CG2 . THR A 1 269 ? -11.086 -16.103 13.328  1.00 13.98 ? 268  THR A CG2 1 
ATOM   2176 N  N   . THR A 1 270 ? -9.708  -12.788 16.393  1.00 12.06 ? 269  THR A N   1 
ATOM   2177 C  CA  . THR A 1 270 ? -9.006  -11.563 16.782  1.00 10.43 ? 269  THR A CA  1 
ATOM   2178 C  C   . THR A 1 270 ? -7.798  -11.874 17.666  1.00 13.63 ? 269  THR A C   1 
ATOM   2179 O  O   . THR A 1 270 ? -6.761  -11.201 17.572  1.00 13.44 ? 269  THR A O   1 
ATOM   2180 C  CB  . THR A 1 270 ? -9.965  -10.600 17.496  1.00 11.56 ? 269  THR A CB  1 
ATOM   2181 O  OG1 . THR A 1 270 ? -11.101 -10.353 16.663  1.00 12.56 ? 269  THR A OG1 1 
ATOM   2182 C  CG2 . THR A 1 270 ? -9.289  -9.264  17.792  1.00 11.43 ? 269  THR A CG2 1 
ATOM   2183 N  N   A SER A 1 271 ? -7.903  -12.891 18.528  0.66 13.79 ? 270  SER A N   1 
ATOM   2184 N  N   B SER A 1 271 ? -7.919  -12.872 18.548  0.34 13.22 ? 270  SER A N   1 
ATOM   2185 C  CA  A SER A 1 271 ? -6.739  -13.286 19.318  0.66 13.39 ? 270  SER A CA  1 
ATOM   2186 C  CA  B SER A 1 271 ? -6.757  -13.313 19.314  0.34 12.60 ? 270  SER A CA  1 
ATOM   2187 C  C   A SER A 1 271 ? -5.627  -13.828 18.422  0.66 15.22 ? 270  SER A C   1 
ATOM   2188 C  C   B SER A 1 271 ? -5.641  -13.780 18.389  0.34 13.80 ? 270  SER A C   1 
ATOM   2189 O  O   A SER A 1 271 ? -4.439  -13.595 18.683  0.66 14.40 ? 270  SER A O   1 
ATOM   2190 O  O   B SER A 1 271 ? -4.466  -13.452 18.601  0.34 12.93 ? 270  SER A O   1 
ATOM   2191 C  CB  A SER A 1 271 ? -7.141  -14.313 20.381  0.66 14.22 ? 270  SER A CB  1 
ATOM   2192 C  CB  B SER A 1 271 ? -7.156  -14.430 20.281  0.34 12.68 ? 270  SER A CB  1 
ATOM   2193 O  OG  A SER A 1 271 ? -7.596  -15.521 19.802  0.66 13.44 ? 270  SER A OG  1 
ATOM   2194 O  OG  B SER A 1 271 ? -6.014  -15.114 20.775  0.34 12.87 ? 270  SER A OG  1 
ATOM   2195 N  N   . GLY A 1 272 ? -5.990  -14.547 17.355  1.00 13.35 ? 271  GLY A N   1 
ATOM   2196 C  CA  . GLY A 1 272 ? -4.984  -14.979 16.397  1.00 9.89  ? 271  GLY A CA  1 
ATOM   2197 C  C   . GLY A 1 272 ? -4.330  -13.807 15.692  1.00 12.32 ? 271  GLY A C   1 
ATOM   2198 O  O   . GLY A 1 272 ? -3.107  -13.773 15.520  1.00 13.23 ? 271  GLY A O   1 
ATOM   2199 N  N   . LEU A 1 273 ? -5.133  -12.827 15.278  1.00 12.64 ? 272  LEU A N   1 
ATOM   2200 C  CA  . LEU A 1 273 ? -4.581  -11.655 14.600  1.00 13.02 ? 272  LEU A CA  1 
ATOM   2201 C  C   . LEU A 1 273 ? -3.575  -10.924 15.489  1.00 11.42 ? 272  LEU A C   1 
ATOM   2202 O  O   . LEU A 1 273 ? -2.463  -10.591 15.054  1.00 11.43 ? 272  LEU A O   1 
ATOM   2203 C  CB  . LEU A 1 273 ? -5.716  -10.720 14.178  1.00 12.15 ? 272  LEU A CB  1 
ATOM   2204 C  CG  . LEU A 1 273 ? -5.282  -9.313  13.738  1.00 12.31 ? 272  LEU A CG  1 
ATOM   2205 C  CD1 . LEU A 1 273 ? -4.271  -9.349  12.559  1.00 14.09 ? 272  LEU A CD1 1 
ATOM   2206 C  CD2 . LEU A 1 273 ? -6.510  -8.450  13.405  1.00 12.92 ? 272  LEU A CD2 1 
ATOM   2207 N  N   . LEU A 1 274 ? -3.953  -10.645 16.738  1.00 11.29 ? 273  LEU A N   1 
ATOM   2208 C  CA  . LEU A 1 274 ? -3.030  -9.952  17.633  1.00 10.31 ? 273  LEU A CA  1 
ATOM   2209 C  C   . LEU A 1 274 ? -1.761  -10.765 17.852  1.00 12.65 ? 273  LEU A C   1 
ATOM   2210 O  O   . LEU A 1 274 ? -0.665  -10.201 17.937  1.00 13.48 ? 273  LEU A O   1 
ATOM   2211 C  CB  . LEU A 1 274 ? -3.717  -9.639  18.968  1.00 9.91  ? 273  LEU A CB  1 
ATOM   2212 C  CG  . LEU A 1 274 ? -4.670  -8.442  18.902  1.00 10.96 ? 273  LEU A CG  1 
ATOM   2213 C  CD1 . LEU A 1 274 ? -5.641  -8.402  20.083  1.00 10.49 ? 273  LEU A CD1 1 
ATOM   2214 C  CD2 . LEU A 1 274 ? -3.866  -7.145  18.845  1.00 14.48 ? 273  LEU A CD2 1 
ATOM   2215 N  N   . SER A 1 275 ? -1.887  -12.091 17.953  1.00 12.78 ? 274  SER A N   1 
ATOM   2216 C  CA  . SER A 1 275 ? -0.710  -12.938 18.147  1.00 12.64 ? 274  SER A CA  1 
ATOM   2217 C  C   . SER A 1 275 ? 0.216   -12.875 16.936  1.00 14.02 ? 274  SER A C   1 
ATOM   2218 O  O   . SER A 1 275 ? 1.437   -12.714 17.075  1.00 14.51 ? 274  SER A O   1 
ATOM   2219 C  CB  . SER A 1 275 ? -1.150  -14.374 18.423  1.00 13.20 ? 274  SER A CB  1 
ATOM   2220 O  OG  . SER A 1 275 ? -1.943  -14.433 19.606  1.00 14.19 ? 274  SER A OG  1 
ATOM   2221 N  N   . PHE A 1 276 ? -0.347  -13.013 15.733  1.00 13.09 ? 275  PHE A N   1 
ATOM   2222 C  CA  . PHE A 1 276 ? 0.480   -12.925 14.527  1.00 13.47 ? 275  PHE A CA  1 
ATOM   2223 C  C   . PHE A 1 276 ? 1.089   -11.536 14.374  1.00 14.51 ? 275  PHE A C   1 
ATOM   2224 O  O   . PHE A 1 276 ? 2.249   -11.402 13.964  1.00 15.50 ? 275  PHE A O   1 
ATOM   2225 C  CB  . PHE A 1 276 ? -0.339  -13.279 13.275  1.00 13.06 ? 275  PHE A CB  1 
ATOM   2226 C  CG  . PHE A 1 276 ? -0.521  -14.759 13.053  1.00 11.19 ? 275  PHE A CG  1 
ATOM   2227 C  CD1 . PHE A 1 276 ? 0.572   -15.575 12.769  1.00 12.51 ? 275  PHE A CD1 1 
ATOM   2228 C  CD2 . PHE A 1 276 ? -1.785  -15.326 13.106  1.00 11.03 ? 275  PHE A CD2 1 
ATOM   2229 C  CE1 . PHE A 1 276 ? 0.408   -16.939 12.563  1.00 13.96 ? 275  PHE A CE1 1 
ATOM   2230 C  CE2 . PHE A 1 276 ? -1.963  -16.684 12.905  1.00 12.81 ? 275  PHE A CE2 1 
ATOM   2231 C  CZ  . PHE A 1 276 ? -0.869  -17.496 12.626  1.00 13.45 ? 275  PHE A CZ  1 
ATOM   2232 N  N   . ALA A 1 277 ? 0.327   -10.485 14.696  1.00 13.47 ? 276  ALA A N   1 
ATOM   2233 C  CA  . ALA A 1 277 ? 0.856   -9.133  14.547  1.00 11.63 ? 276  ALA A CA  1 
ATOM   2234 C  C   . ALA A 1 277 ? 2.064   -8.915  15.456  1.00 12.56 ? 276  ALA A C   1 
ATOM   2235 O  O   . ALA A 1 277 ? 3.087   -8.373  15.026  1.00 15.68 ? 276  ALA A O   1 
ATOM   2236 C  CB  . ALA A 1 277 ? -0.236  -8.101  14.827  1.00 14.22 ? 276  ALA A CB  1 
ATOM   2237 N  N   . LEU A 1 278 ? 1.971   -9.334  16.720  1.00 14.81 ? 277  LEU A N   1 
ATOM   2238 C  CA  . LEU A 1 278 ? 3.115   -9.165  17.611  1.00 14.28 ? 277  LEU A CA  1 
ATOM   2239 C  C   . LEU A 1 278 ? 4.291   -10.010 17.137  1.00 15.50 ? 277  LEU A C   1 
ATOM   2240 O  O   . LEU A 1 278 ? 5.449   -9.580  17.215  1.00 16.00 ? 277  LEU A O   1 
ATOM   2241 C  CB  . LEU A 1 278 ? 2.736   -9.518  19.055  1.00 16.04 ? 277  LEU A CB  1 
ATOM   2242 C  CG  . LEU A 1 278 ? 3.834   -9.283  20.103  1.00 19.07 ? 277  LEU A CG  1 
ATOM   2243 C  CD1 . LEU A 1 278 ? 4.328   -7.842  20.069  1.00 19.59 ? 277  LEU A CD1 1 
ATOM   2244 C  CD2 . LEU A 1 278 ? 3.341   -9.621  21.494  1.00 18.29 ? 277  LEU A CD2 1 
ATOM   2245 N  N   . TYR A 1 279 ? 4.012   -11.209 16.620  1.00 15.17 ? 278  TYR A N   1 
ATOM   2246 C  CA  . TYR A 1 279 ? 5.077   -12.027 16.050  1.00 16.24 ? 278  TYR A CA  1 
ATOM   2247 C  C   . TYR A 1 279 ? 5.804   -11.274 14.941  1.00 14.75 ? 278  TYR A C   1 
ATOM   2248 O  O   . TYR A 1 279 ? 7.032   -11.136 14.962  1.00 18.13 ? 278  TYR A O   1 
ATOM   2249 C  CB  . TYR A 1 279 ? 4.506   -13.349 15.520  1.00 17.30 ? 278  TYR A CB  1 
ATOM   2250 C  CG  . TYR A 1 279 ? 5.485   -14.081 14.627  1.00 15.99 ? 278  TYR A CG  1 
ATOM   2251 C  CD1 . TYR A 1 279 ? 6.479   -14.898 15.165  1.00 16.37 ? 278  TYR A CD1 1 
ATOM   2252 C  CD2 . TYR A 1 279 ? 5.429   -13.947 13.244  1.00 16.64 ? 278  TYR A CD2 1 
ATOM   2253 C  CE1 . TYR A 1 279 ? 7.387   -15.554 14.342  1.00 17.78 ? 278  TYR A CE1 1 
ATOM   2254 C  CE2 . TYR A 1 279 ? 6.329   -14.599 12.421  1.00 18.25 ? 278  TYR A CE2 1 
ATOM   2255 C  CZ  . TYR A 1 279 ? 7.304   -15.402 12.970  1.00 18.30 ? 278  TYR A CZ  1 
ATOM   2256 O  OH  . TYR A 1 279 ? 8.209   -16.053 12.144  1.00 21.06 ? 278  TYR A OH  1 
ATOM   2257 N  N   . PHE A 1 280 ? 5.064   -10.774 13.955  1.00 15.95 ? 279  PHE A N   1 
ATOM   2258 C  CA  . PHE A 1 280 ? 5.743   -10.079 12.871  1.00 17.47 ? 279  PHE A CA  1 
ATOM   2259 C  C   . PHE A 1 280 ? 6.443   -8.819  13.363  1.00 18.44 ? 279  PHE A C   1 
ATOM   2260 O  O   . PHE A 1 280 ? 7.479   -8.438  12.815  1.00 20.82 ? 279  PHE A O   1 
ATOM   2261 C  CB  . PHE A 1 280 ? 4.754   -9.754  11.749  1.00 15.79 ? 279  PHE A CB  1 
ATOM   2262 C  CG  . PHE A 1 280 ? 4.388   -10.942 10.904  1.00 18.58 ? 279  PHE A CG  1 
ATOM   2263 C  CD1 . PHE A 1 280 ? 5.354   -11.585 10.135  1.00 18.75 ? 279  PHE A CD1 1 
ATOM   2264 C  CD2 . PHE A 1 280 ? 3.084   -11.414 10.869  1.00 20.39 ? 279  PHE A CD2 1 
ATOM   2265 C  CE1 . PHE A 1 280 ? 5.023   -12.684 9.356   1.00 19.87 ? 279  PHE A CE1 1 
ATOM   2266 C  CE2 . PHE A 1 280 ? 2.744   -12.509 10.090  1.00 19.53 ? 279  PHE A CE2 1 
ATOM   2267 C  CZ  . PHE A 1 280 ? 3.716   -13.143 9.328   1.00 19.52 ? 279  PHE A CZ  1 
ATOM   2268 N  N   . LEU A 1 281 ? 5.913   -8.163  14.398  1.00 18.32 ? 280  LEU A N   1 
ATOM   2269 C  CA  . LEU A 1 281 ? 6.564   -6.939  14.862  1.00 17.57 ? 280  LEU A CA  1 
ATOM   2270 C  C   . LEU A 1 281 ? 7.914   -7.237  15.513  1.00 18.62 ? 280  LEU A C   1 
ATOM   2271 O  O   . LEU A 1 281 ? 8.899   -6.536  15.243  1.00 20.17 ? 280  LEU A O   1 
ATOM   2272 C  CB  . LEU A 1 281 ? 5.646   -6.165  15.814  1.00 18.18 ? 280  LEU A CB  1 
ATOM   2273 C  CG  . LEU A 1 281 ? 4.500   -5.383  15.139  1.00 18.75 ? 280  LEU A CG  1 
ATOM   2274 C  CD1 . LEU A 1 281 ? 3.614   -4.683  16.166  1.00 21.73 ? 280  LEU A CD1 1 
ATOM   2275 C  CD2 . LEU A 1 281 ? 5.039   -4.372  14.132  1.00 21.61 ? 280  LEU A CD2 1 
ATOM   2276 N  N   . VAL A 1 282 ? 7.995   -8.269  16.361  1.00 20.90 ? 281  VAL A N   1 
ATOM   2277 C  CA  . VAL A 1 282 ? 9.285   -8.572  16.994  1.00 20.02 ? 281  VAL A CA  1 
ATOM   2278 C  C   . VAL A 1 282 ? 10.282  -9.147  15.997  1.00 19.91 ? 281  VAL A C   1 
ATOM   2279 O  O   . VAL A 1 282 ? 11.497  -9.021  16.203  1.00 21.27 ? 281  VAL A O   1 
ATOM   2280 C  CB  . VAL A 1 282 ? 9.144   -9.516  18.210  1.00 21.14 ? 281  VAL A CB  1 
ATOM   2281 C  CG1 . VAL A 1 282 ? 8.238   -8.886  19.250  1.00 22.92 ? 281  VAL A CG1 1 
ATOM   2282 C  CG2 . VAL A 1 282 ? 8.654   -10.922 17.797  1.00 21.03 ? 281  VAL A CG2 1 
ATOM   2283 N  N   . LYS A 1 283 ? 9.808   -9.763  14.910  1.00 21.00 ? 282  LYS A N   1 
ATOM   2284 C  CA  . LYS A 1 283 ? 10.700  -10.233 13.855  1.00 23.34 ? 282  LYS A CA  1 
ATOM   2285 C  C   . LYS A 1 283 ? 11.103  -9.133  12.878  1.00 21.92 ? 282  LYS A C   1 
ATOM   2286 O  O   . LYS A 1 283 ? 12.010  -9.353  12.062  1.00 25.44 ? 282  LYS A O   1 
ATOM   2287 C  CB  . LYS A 1 283 ? 10.042  -11.382 13.082  1.00 22.86 ? 282  LYS A CB  1 
ATOM   2288 C  CG  . LYS A 1 283 ? 9.764   -12.629 13.915  1.00 21.06 ? 282  LYS A CG  1 
ATOM   2289 C  CD  . LYS A 1 283 ? 11.048  -13.279 14.425  1.00 21.98 ? 282  LYS A CD  1 
ATOM   2290 C  CE  . LYS A 1 283 ? 10.768  -14.673 14.962  1.00 22.13 ? 282  LYS A CE  1 
ATOM   2291 N  NZ  . LYS A 1 283 ? 11.957  -15.310 15.617  1.00 21.58 ? 282  LYS A NZ  1 
ATOM   2292 N  N   . ASN A 1 284 ? 10.476  -7.959  12.945  1.00 22.21 ? 283  ASN A N   1 
ATOM   2293 C  CA  . ASN A 1 284 ? 10.754  -6.853  12.022  1.00 22.87 ? 283  ASN A CA  1 
ATOM   2294 C  C   . ASN A 1 284 ? 10.864  -5.559  12.815  1.00 26.78 ? 283  ASN A C   1 
ATOM   2295 O  O   . ASN A 1 284 ? 9.980   -4.694  12.758  1.00 25.35 ? 283  ASN A O   1 
ATOM   2296 C  CB  . ASN A 1 284 ? 9.671   -6.754  10.946  1.00 22.88 ? 283  ASN A CB  1 
ATOM   2297 C  CG  . ASN A 1 284 ? 9.664   -7.948  10.013  1.00 21.71 ? 283  ASN A CG  1 
ATOM   2298 O  OD1 . ASN A 1 284 ? 10.408  -7.985  9.024   1.00 23.42 ? 283  ASN A OD1 1 
ATOM   2299 N  ND2 . ASN A 1 284 ? 8.818   -8.928  10.312  1.00 19.37 ? 283  ASN A ND2 1 
ATOM   2300 N  N   . PRO A 1 285 ? 11.967  -5.383  13.548  1.00 28.84 ? 284  PRO A N   1 
ATOM   2301 C  CA  . PRO A 1 285 ? 12.051  -4.265  14.507  1.00 32.81 ? 284  PRO A CA  1 
ATOM   2302 C  C   . PRO A 1 285 ? 11.918  -2.891  13.882  1.00 32.11 ? 284  PRO A C   1 
ATOM   2303 O  O   . PRO A 1 285 ? 11.512  -1.950  14.576  1.00 32.15 ? 284  PRO A O   1 
ATOM   2304 C  CB  . PRO A 1 285 ? 13.436  -4.450  15.142  1.00 32.59 ? 284  PRO A CB  1 
ATOM   2305 C  CG  . PRO A 1 285 ? 13.805  -5.870  14.876  1.00 33.05 ? 284  PRO A CG  1 
ATOM   2306 C  CD  . PRO A 1 285 ? 13.158  -6.246  13.586  1.00 30.68 ? 284  PRO A CD  1 
ATOM   2307 N  N   . HIS A 1 286 ? 12.270  -2.732  12.603  1.00 30.90 ? 285  HIS A N   1 
ATOM   2308 C  CA  . HIS A 1 286 ? 12.085  -1.437  11.956  1.00 30.08 ? 285  HIS A CA  1 
ATOM   2309 C  C   . HIS A 1 286 ? 10.606  -1.092  11.844  1.00 27.12 ? 285  HIS A C   1 
ATOM   2310 O  O   . HIS A 1 286 ? 10.219  0.074   11.986  1.00 27.12 ? 285  HIS A O   1 
ATOM   2311 C  CB  . HIS A 1 286 ? 12.753  -1.437  10.581  1.00 33.55 ? 285  HIS A CB  1 
ATOM   2312 C  CG  . HIS A 1 286 ? 14.235  -1.656  10.638  1.00 42.71 ? 285  HIS A CG  1 
ATOM   2313 N  ND1 . HIS A 1 286 ? 14.910  -2.443  9.728   1.00 46.50 ? 285  HIS A ND1 1 
ATOM   2314 C  CD2 . HIS A 1 286 ? 15.171  -1.193  11.501  1.00 43.89 ? 285  HIS A CD2 1 
ATOM   2315 C  CE1 . HIS A 1 286 ? 16.197  -2.454  10.027  1.00 46.58 ? 285  HIS A CE1 1 
ATOM   2316 N  NE2 . HIS A 1 286 ? 16.382  -1.703  11.098  1.00 45.92 ? 285  HIS A NE2 1 
ATOM   2317 N  N   . VAL A 1 287 ? 9.765   -2.102  11.608  1.00 25.71 ? 286  VAL A N   1 
ATOM   2318 C  CA  . VAL A 1 287 ? 8.324   -1.879  11.566  1.00 22.55 ? 286  VAL A CA  1 
ATOM   2319 C  C   . VAL A 1 287 ? 7.790   -1.590  12.966  1.00 22.92 ? 286  VAL A C   1 
ATOM   2320 O  O   . VAL A 1 287 ? 6.976   -0.678  13.162  1.00 22.31 ? 286  VAL A O   1 
ATOM   2321 C  CB  . VAL A 1 287 ? 7.625   -3.091  10.913  1.00 21.55 ? 286  VAL A CB  1 
ATOM   2322 C  CG1 . VAL A 1 287 ? 6.115   -2.894  10.877  1.00 22.71 ? 286  VAL A CG1 1 
ATOM   2323 C  CG2 . VAL A 1 287 ? 8.176   -3.329  9.491   1.00 22.81 ? 286  VAL A CG2 1 
ATOM   2324 N  N   . LEU A 1 288 ? 8.254   -2.342  13.965  1.00 22.18 ? 287  LEU A N   1 
ATOM   2325 C  CA  . LEU A 1 288 ? 7.838   -2.077  15.338  1.00 24.02 ? 287  LEU A CA  1 
ATOM   2326 C  C   . LEU A 1 288 ? 8.134   -0.631  15.729  1.00 23.92 ? 287  LEU A C   1 
ATOM   2327 O  O   . LEU A 1 288 ? 7.268   0.069   16.267  1.00 26.05 ? 287  LEU A O   1 
ATOM   2328 C  CB  . LEU A 1 288 ? 8.529   -3.057  16.289  1.00 25.46 ? 287  LEU A CB  1 
ATOM   2329 C  CG  . LEU A 1 288 ? 7.971   -3.184  17.712  1.00 27.95 ? 287  LEU A CG  1 
ATOM   2330 C  CD1 . LEU A 1 288 ? 8.466   -4.461  18.358  1.00 28.21 ? 287  LEU A CD1 1 
ATOM   2331 C  CD2 . LEU A 1 288 ? 8.366   -1.985  18.555  1.00 28.34 ? 287  LEU A CD2 1 
ATOM   2332 N  N   . GLN A 1 289 ? 9.351   -0.159  15.440  1.00 23.91 ? 288  GLN A N   1 
ATOM   2333 C  CA  . GLN A 1 289 ? 9.714   1.211   15.789  1.00 24.60 ? 288  GLN A CA  1 
ATOM   2334 C  C   . GLN A 1 289 ? 8.766   2.218   15.149  1.00 25.65 ? 288  GLN A C   1 
ATOM   2335 O  O   . GLN A 1 289 ? 8.310   3.161   15.809  1.00 26.85 ? 288  GLN A O   1 
ATOM   2336 C  CB  . GLN A 1 289 ? 11.159  1.504   15.382  1.00 31.22 ? 288  GLN A CB  1 
ATOM   2337 C  CG  . GLN A 1 289 ? 11.593  2.923   15.713  1.00 32.91 ? 288  GLN A CG  1 
ATOM   2338 C  CD  . GLN A 1 289 ? 12.990  3.240   15.231  1.00 42.57 ? 288  GLN A CD  1 
ATOM   2339 O  OE1 . GLN A 1 289 ? 13.636  2.426   14.570  1.00 45.79 ? 288  GLN A OE1 1 
ATOM   2340 N  NE2 . GLN A 1 289 ? 13.466  4.435   15.555  1.00 47.17 ? 288  GLN A NE2 1 
ATOM   2341 N  N   . LYS A 1 290 ? 8.458   2.039   13.857  1.00 24.61 ? 289  LYS A N   1 
ATOM   2342 C  CA  . LYS A 1 290 ? 7.556   2.967   13.181  1.00 22.96 ? 289  LYS A CA  1 
ATOM   2343 C  C   . LYS A 1 290 ? 6.170   2.948   13.819  1.00 23.03 ? 289  LYS A C   1 
ATOM   2344 O  O   . LYS A 1 290 ? 5.563   4.004   14.040  1.00 23.09 ? 289  LYS A O   1 
ATOM   2345 C  CB  . LYS A 1 290 ? 7.481   2.628   11.687  1.00 23.84 ? 289  LYS A CB  1 
ATOM   2346 C  CG  . LYS A 1 290 ? 6.738   3.647   10.825  1.00 27.31 ? 289  LYS A CG  1 
ATOM   2347 C  CD  . LYS A 1 290 ? 6.987   3.409   9.325   1.00 27.37 ? 289  LYS A CD  1 
ATOM   2348 C  CE  . LYS A 1 290 ? 5.987   4.161   8.459   1.00 27.24 ? 289  LYS A CE  1 
ATOM   2349 N  NZ  . LYS A 1 290 ? 6.209   3.947   6.989   1.00 29.88 ? 289  LYS A NZ  1 
ATOM   2350 N  N   . ALA A 1 291 ? 5.659   1.756   14.137  1.00 21.98 ? 290  ALA A N   1 
ATOM   2351 C  CA  . ALA A 1 291 ? 4.364   1.663   14.806  1.00 20.88 ? 290  ALA A CA  1 
ATOM   2352 C  C   . ALA A 1 291 ? 4.422   2.255   16.210  1.00 20.31 ? 290  ALA A C   1 
ATOM   2353 O  O   . ALA A 1 291 ? 3.485   2.940   16.638  1.00 21.73 ? 290  ALA A O   1 
ATOM   2354 C  CB  . ALA A 1 291 ? 3.903   0.206   14.853  1.00 20.57 ? 290  ALA A CB  1 
ATOM   2355 N  N   . ALA A 1 292 ? 5.513   2.010   16.943  1.00 18.33 ? 291  ALA A N   1 
ATOM   2356 C  CA  . ALA A 1 292 ? 5.636   2.576   18.286  1.00 21.12 ? 291  ALA A CA  1 
ATOM   2357 C  C   . ALA A 1 292 ? 5.715   4.098   18.243  1.00 24.45 ? 291  ALA A C   1 
ATOM   2358 O  O   . ALA A 1 292 ? 5.220   4.780   19.152  1.00 25.20 ? 291  ALA A O   1 
ATOM   2359 C  CB  . ALA A 1 292 ? 6.868   2.010   18.993  1.00 21.52 ? 291  ALA A CB  1 
ATOM   2360 N  N   . GLU A 1 293 ? 6.356   4.650   17.209  1.00 23.07 ? 292  GLU A N   1 
ATOM   2361 C  CA  . GLU A 1 293 ? 6.421   6.100   17.080  1.00 24.10 ? 292  GLU A CA  1 
ATOM   2362 C  C   . GLU A 1 293 ? 5.032   6.687   16.876  1.00 24.71 ? 292  GLU A C   1 
ATOM   2363 O  O   . GLU A 1 293 ? 4.698   7.728   17.454  1.00 24.81 ? 292  GLU A O   1 
ATOM   2364 C  CB  . GLU A 1 293 ? 7.363   6.484   15.933  1.00 27.32 ? 292  GLU A CB  1 
ATOM   2365 C  CG  . GLU A 1 293 ? 8.833   6.271   16.304  1.00 29.57 ? 292  GLU A CG  1 
ATOM   2366 C  CD  . GLU A 1 293 ? 9.788   6.372   15.128  1.00 36.14 ? 292  GLU A CD  1 
ATOM   2367 O  OE1 . GLU A 1 293 ? 9.320   6.415   13.974  1.00 41.18 ? 292  GLU A OE1 1 
ATOM   2368 O  OE2 . GLU A 1 293 ? 11.016  6.395   15.368  1.00 35.09 ? 292  GLU A OE2 1 
ATOM   2369 N  N   . GLU A 1 294 ? 4.198   6.018   16.076  1.00 22.53 ? 293  GLU A N   1 
ATOM   2370 C  CA  . GLU A 1 294 ? 2.829   6.487   15.897  1.00 21.94 ? 293  GLU A CA  1 
ATOM   2371 C  C   . GLU A 1 294 ? 2.059   6.425   17.210  1.00 23.95 ? 293  GLU A C   1 
ATOM   2372 O  O   . GLU A 1 294 ? 1.362   7.376   17.582  1.00 24.60 ? 293  GLU A O   1 
ATOM   2373 C  CB  . GLU A 1 294 ? 2.128   5.661   14.822  1.00 20.56 ? 293  GLU A CB  1 
ATOM   2374 C  CG  . GLU A 1 294 ? 0.691   6.098   14.585  1.00 21.81 ? 293  GLU A CG  1 
ATOM   2375 C  CD  . GLU A 1 294 ? 0.008   5.299   13.507  1.00 20.08 ? 293  GLU A CD  1 
ATOM   2376 O  OE1 . GLU A 1 294 ? -0.399  4.151   13.783  1.00 21.13 ? 293  GLU A OE1 1 
ATOM   2377 O  OE2 . GLU A 1 294 ? -0.117  5.817   12.375  1.00 22.30 ? 293  GLU A OE2 1 
ATOM   2378 N  N   . ALA A 1 295 ? 2.176   5.304   17.928  1.00 22.90 ? 294  ALA A N   1 
ATOM   2379 C  CA  . ALA A 1 295 ? 1.467   5.149   19.193  1.00 22.77 ? 294  ALA A CA  1 
ATOM   2380 C  C   . ALA A 1 295 ? 1.842   6.247   20.181  1.00 24.23 ? 294  ALA A C   1 
ATOM   2381 O  O   . ALA A 1 295 ? 0.971   6.809   20.855  1.00 26.03 ? 294  ALA A O   1 
ATOM   2382 C  CB  . ALA A 1 295 ? 1.754   3.767   19.785  1.00 21.45 ? 294  ALA A CB  1 
ATOM   2383 N  N   . ALA A 1 296 ? 3.133   6.570   20.278  1.00 24.42 ? 295  ALA A N   1 
ATOM   2384 C  CA  . ALA A 1 296 ? 3.552   7.617   21.206  1.00 25.65 ? 295  ALA A CA  1 
ATOM   2385 C  C   . ALA A 1 296 ? 3.015   8.982   20.787  1.00 27.34 ? 295  ALA A C   1 
ATOM   2386 O  O   . ALA A 1 296 ? 2.643   9.800   21.640  1.00 26.21 ? 295  ALA A O   1 
ATOM   2387 C  CB  . ALA A 1 296 ? 5.076   7.643   21.308  1.00 26.17 ? 295  ALA A CB  1 
ATOM   2388 N  N   . ARG A 1 297 ? 2.969   9.251   19.478  1.00 28.43 ? 296  ARG A N   1 
ATOM   2389 C  CA  . ARG A 1 297 ? 2.519   10.558  19.008  1.00 28.03 ? 296  ARG A CA  1 
ATOM   2390 C  C   . ARG A 1 297 ? 1.010   10.736  19.160  1.00 27.44 ? 296  ARG A C   1 
ATOM   2391 O  O   . ARG A 1 297 ? 0.547   11.848  19.441  1.00 28.49 ? 296  ARG A O   1 
ATOM   2392 C  CB  . ARG A 1 297 ? 2.943   10.755  17.550  1.00 29.89 ? 296  ARG A CB  1 
ATOM   2393 C  CG  . ARG A 1 297 ? 2.131   11.781  16.788  1.00 32.83 ? 296  ARG A CG  1 
ATOM   2394 C  CD  . ARG A 1 297 ? 2.781   12.137  15.455  1.00 38.39 ? 296  ARG A CD  1 
ATOM   2395 N  NE  . ARG A 1 297 ? 3.340   10.976  14.770  1.00 43.65 ? 296  ARG A NE  1 
ATOM   2396 C  CZ  . ARG A 1 297 ? 2.650   10.165  13.980  1.00 49.47 ? 296  ARG A CZ  1 
ATOM   2397 N  NH1 . ARG A 1 297 ? 1.349   10.331  13.787  1.00 49.56 ? 296  ARG A NH1 1 
ATOM   2398 N  NH2 . ARG A 1 297 ? 3.280   9.162   13.369  1.00 48.95 ? 296  ARG A NH2 1 
ATOM   2399 N  N   . VAL A 1 298 ? 0.238   9.664   19.005  1.00 23.36 ? 297  VAL A N   1 
ATOM   2400 C  CA  . VAL A 1 298 ? -1.222  9.754   18.978  1.00 22.23 ? 297  VAL A CA  1 
ATOM   2401 C  C   . VAL A 1 298 ? -1.836  9.551   20.362  1.00 25.45 ? 297  VAL A C   1 
ATOM   2402 O  O   . VAL A 1 298 ? -2.760  10.274  20.748  1.00 26.47 ? 297  VAL A O   1 
ATOM   2403 C  CB  . VAL A 1 298 ? -1.774  8.739   17.951  1.00 20.98 ? 297  VAL A CB  1 
ATOM   2404 C  CG1 . VAL A 1 298 ? -3.280  8.522   18.130  1.00 19.35 ? 297  VAL A CG1 1 
ATOM   2405 C  CG2 . VAL A 1 298 ? -1.450  9.193   16.527  1.00 22.99 ? 297  VAL A CG2 1 
ATOM   2406 N  N   . LEU A 1 299 ? -1.342  8.580   21.135  1.00 24.78 ? 298  LEU A N   1 
ATOM   2407 C  CA  . LEU A 1 299 ? -1.950  8.229   22.422  1.00 23.77 ? 298  LEU A CA  1 
ATOM   2408 C  C   . LEU A 1 299 ? -1.370  9.105   23.536  1.00 26.82 ? 298  LEU A C   1 
ATOM   2409 O  O   . LEU A 1 299 ? -0.580  8.673   24.382  1.00 25.79 ? 298  LEU A O   1 
ATOM   2410 C  CB  . LEU A 1 299 ? -1.758  6.745   22.708  1.00 22.12 ? 298  LEU A CB  1 
ATOM   2411 C  CG  . LEU A 1 299 ? -2.348  5.820   21.638  1.00 19.83 ? 298  LEU A CG  1 
ATOM   2412 C  CD1 . LEU A 1 299 ? -2.080  4.355   21.966  1.00 20.63 ? 298  LEU A CD1 1 
ATOM   2413 C  CD2 . LEU A 1 299 ? -3.839  6.077   21.463  1.00 23.70 ? 298  LEU A CD2 1 
ATOM   2414 N  N   . VAL A 1 300 ? -1.812  10.369  23.538  1.00 28.28 ? 299  VAL A N   1 
ATOM   2415 C  CA  . VAL A 1 300 ? -1.256  11.377  24.442  1.00 29.31 ? 299  VAL A CA  1 
ATOM   2416 C  C   . VAL A 1 300 ? -1.963  11.429  25.789  1.00 30.01 ? 299  VAL A C   1 
ATOM   2417 O  O   . VAL A 1 300 ? -1.585  12.247  26.642  1.00 29.68 ? 299  VAL A O   1 
ATOM   2418 C  CB  . VAL A 1 300 ? -1.298  12.773  23.788  1.00 29.99 ? 299  VAL A CB  1 
ATOM   2419 C  CG1 . VAL A 1 300 ? -0.535  12.760  22.470  1.00 28.94 ? 299  VAL A CG1 1 
ATOM   2420 C  CG2 . VAL A 1 300 ? -2.740  13.218  23.581  1.00 30.82 ? 299  VAL A CG2 1 
ATOM   2421 N  N   . ASP A 1 301 ? -2.968  10.590  26.012  1.00 30.07 ? 300  ASP A N   1 
ATOM   2422 C  CA  . ASP A 1 301 ? -3.727  10.563  27.252  1.00 29.68 ? 300  ASP A CA  1 
ATOM   2423 C  C   . ASP A 1 301 ? -3.544  9.222   27.958  1.00 28.81 ? 300  ASP A C   1 
ATOM   2424 O  O   . ASP A 1 301 ? -3.210  8.215   27.325  1.00 29.70 ? 300  ASP A O   1 
ATOM   2425 C  CB  . ASP A 1 301 ? -5.221  10.810  26.985  1.00 27.79 ? 300  ASP A CB  1 
ATOM   2426 C  CG  . ASP A 1 301 ? -5.504  12.208  26.453  1.00 30.77 ? 300  ASP A CG  1 
ATOM   2427 O  OD1 . ASP A 1 301 ? -4.880  13.179  26.932  1.00 30.19 ? 300  ASP A OD1 1 
ATOM   2428 O  OD2 . ASP A 1 301 ? -6.367  12.340  25.559  1.00 34.75 ? 300  ASP A OD2 1 
ATOM   2429 N  N   . PRO A 1 302 ? -3.754  9.172   29.274  1.00 28.65 ? 301  PRO A N   1 
ATOM   2430 C  CA  . PRO A 1 302 ? -3.605  7.887   29.981  1.00 27.58 ? 301  PRO A CA  1 
ATOM   2431 C  C   . PRO A 1 302 ? -4.541  6.810   29.469  1.00 29.11 ? 301  PRO A C   1 
ATOM   2432 O  O   . PRO A 1 302 ? -4.189  5.625   29.499  1.00 30.08 ? 301  PRO A O   1 
ATOM   2433 C  CB  . PRO A 1 302 ? -3.913  8.252   31.441  1.00 27.62 ? 301  PRO A CB  1 
ATOM   2434 C  CG  . PRO A 1 302 ? -3.646  9.717   31.529  1.00 28.82 ? 301  PRO A CG  1 
ATOM   2435 C  CD  . PRO A 1 302 ? -4.026  10.289  30.193  1.00 28.34 ? 301  PRO A CD  1 
ATOM   2436 N  N   . VAL A 1 303 ? -5.722  7.198   29.000  1.00 29.64 ? 302  VAL A N   1 
ATOM   2437 C  CA  . VAL A 1 303 ? -6.715  6.290   28.446  1.00 30.43 ? 302  VAL A CA  1 
ATOM   2438 C  C   . VAL A 1 303 ? -6.918  6.682   26.988  1.00 29.82 ? 302  VAL A C   1 
ATOM   2439 O  O   . VAL A 1 303 ? -7.158  7.857   26.707  1.00 28.32 ? 302  VAL A O   1 
ATOM   2440 C  CB  . VAL A 1 303 ? -8.051  6.365   29.207  1.00 33.75 ? 302  VAL A CB  1 
ATOM   2441 C  CG1 . VAL A 1 303 ? -9.053  5.410   28.624  1.00 36.58 ? 302  VAL A CG1 1 
ATOM   2442 C  CG2 . VAL A 1 303 ? -7.840  6.105   30.703  1.00 36.14 ? 302  VAL A CG2 1 
ATOM   2443 N  N   . PRO A 1 304 ? -6.816  5.757   26.031  1.00 27.49 ? 303  PRO A N   1 
ATOM   2444 C  CA  . PRO A 1 304 ? -7.080  6.127   24.633  1.00 24.88 ? 303  PRO A CA  1 
ATOM   2445 C  C   . PRO A 1 304 ? -8.553  6.428   24.407  1.00 22.61 ? 303  PRO A C   1 
ATOM   2446 O  O   . PRO A 1 304 ? -9.434  5.796   24.998  1.00 21.12 ? 303  PRO A O   1 
ATOM   2447 C  CB  . PRO A 1 304 ? -6.635  4.889   23.843  1.00 26.86 ? 303  PRO A CB  1 
ATOM   2448 C  CG  . PRO A 1 304 ? -5.729  4.139   24.779  1.00 27.41 ? 303  PRO A CG  1 
ATOM   2449 C  CD  . PRO A 1 304 ? -6.278  4.391   26.145  1.00 27.32 ? 303  PRO A CD  1 
ATOM   2450 N  N   . SER A 1 305 ? -8.815  7.407   23.545  1.00 19.20 ? 304  SER A N   1 
ATOM   2451 C  CA  . SER A 1 305 ? -10.171 7.726   23.126  1.00 19.02 ? 304  SER A CA  1 
ATOM   2452 C  C   . SER A 1 305 ? -10.486 7.063   21.790  1.00 18.65 ? 304  SER A C   1 
ATOM   2453 O  O   . SER A 1 305 ? -9.595  6.619   21.061  1.00 18.48 ? 304  SER A O   1 
ATOM   2454 C  CB  . SER A 1 305 ? -10.359 9.236   22.996  1.00 18.50 ? 304  SER A CB  1 
ATOM   2455 O  OG  . SER A 1 305 ? -9.645  9.718   21.874  1.00 20.41 ? 304  SER A OG  1 
ATOM   2456 N  N   . TYR A 1 306 ? -11.782 7.019   21.472  1.00 17.46 ? 305  TYR A N   1 
ATOM   2457 C  CA  . TYR A 1 306 ? -12.215 6.502   20.176  1.00 18.39 ? 305  TYR A CA  1 
ATOM   2458 C  C   . TYR A 1 306 ? -11.550 7.258   19.032  1.00 19.21 ? 305  TYR A C   1 
ATOM   2459 O  O   . TYR A 1 306 ? -11.065 6.651   18.068  1.00 19.79 ? 305  TYR A O   1 
ATOM   2460 C  CB  . TYR A 1 306 ? -13.735 6.593   20.069  1.00 19.34 ? 305  TYR A CB  1 
ATOM   2461 C  CG  . TYR A 1 306 ? -14.293 6.186   18.728  1.00 21.50 ? 305  TYR A CG  1 
ATOM   2462 C  CD1 . TYR A 1 306 ? -14.601 4.859   18.462  1.00 20.75 ? 305  TYR A CD1 1 
ATOM   2463 C  CD2 . TYR A 1 306 ? -14.520 7.131   17.724  1.00 23.11 ? 305  TYR A CD2 1 
ATOM   2464 C  CE1 . TYR A 1 306 ? -15.115 4.481   17.234  1.00 23.86 ? 305  TYR A CE1 1 
ATOM   2465 C  CE2 . TYR A 1 306 ? -15.029 6.759   16.493  1.00 22.74 ? 305  TYR A CE2 1 
ATOM   2466 C  CZ  . TYR A 1 306 ? -15.323 5.432   16.255  1.00 26.07 ? 305  TYR A CZ  1 
ATOM   2467 O  OH  . TYR A 1 306 ? -15.837 5.048   15.037  1.00 31.48 ? 305  TYR A OH  1 
ATOM   2468 N  N   . LYS A 1 307 ? -11.539 8.592   19.111  1.00 20.82 ? 306  LYS A N   1 
ATOM   2469 C  CA  . LYS A 1 307 ? -10.968 9.388   18.027  1.00 20.94 ? 306  LYS A CA  1 
ATOM   2470 C  C   . LYS A 1 307 ? -9.484  9.098   17.847  1.00 20.99 ? 306  LYS A C   1 
ATOM   2471 O  O   . LYS A 1 307 ? -8.980  9.074   16.717  1.00 22.95 ? 306  LYS A O   1 
ATOM   2472 C  CB  . LYS A 1 307 ? -11.183 10.879  18.289  1.00 24.17 ? 306  LYS A CB  1 
ATOM   2473 C  CG  . LYS A 1 307 ? -12.615 11.360  18.133  1.00 31.09 ? 306  LYS A CG  1 
ATOM   2474 C  CD  . LYS A 1 307 ? -12.666 12.878  18.215  1.00 37.18 ? 306  LYS A CD  1 
ATOM   2475 C  CE  . LYS A 1 307 ? -14.014 13.373  18.706  1.00 41.61 ? 306  LYS A CE  1 
ATOM   2476 N  NZ  . LYS A 1 307 ? -13.977 14.831  19.016  1.00 44.97 ? 306  LYS A NZ  1 
ATOM   2477 N  N   . GLN A 1 308 ? -8.764  8.880   18.951  1.00 20.43 ? 307  GLN A N   1 
ATOM   2478 C  CA  . GLN A 1 308 ? -7.333  8.606   18.858  1.00 18.38 ? 307  GLN A CA  1 
ATOM   2479 C  C   . GLN A 1 308 ? -7.065  7.257   18.199  1.00 19.63 ? 307  GLN A C   1 
ATOM   2480 O  O   . GLN A 1 308 ? -6.121  7.124   17.412  1.00 22.29 ? 307  GLN A O   1 
ATOM   2481 C  CB  . GLN A 1 308 ? -6.697  8.669   20.249  1.00 18.87 ? 307  GLN A CB  1 
ATOM   2482 C  CG  . GLN A 1 308 ? -6.610  10.085  20.816  1.00 19.61 ? 307  GLN A CG  1 
ATOM   2483 C  CD  . GLN A 1 308 ? -6.312  10.121  22.311  1.00 22.09 ? 307  GLN A CD  1 
ATOM   2484 O  OE1 . GLN A 1 308 ? -6.439  9.113   23.012  1.00 24.92 ? 307  GLN A OE1 1 
ATOM   2485 N  NE2 . GLN A 1 308 ? -5.912  11.290  22.804  1.00 24.89 ? 307  GLN A NE2 1 
ATOM   2486 N  N   . VAL A 1 309 ? -7.881  6.244   18.503  1.00 18.65 ? 308  VAL A N   1 
ATOM   2487 C  CA  . VAL A 1 309 ? -7.695  4.941   17.864  1.00 18.58 ? 308  VAL A CA  1 
ATOM   2488 C  C   . VAL A 1 309 ? -7.870  5.059   16.356  1.00 18.07 ? 308  VAL A C   1 
ATOM   2489 O  O   . VAL A 1 309 ? -7.164  4.396   15.585  1.00 18.73 ? 308  VAL A O   1 
ATOM   2490 C  CB  . VAL A 1 309 ? -8.653  3.898   18.465  1.00 17.86 ? 308  VAL A CB  1 
ATOM   2491 C  CG1 . VAL A 1 309 ? -8.591  2.582   17.662  1.00 16.74 ? 308  VAL A CG1 1 
ATOM   2492 C  CG2 . VAL A 1 309 ? -8.292  3.643   19.927  1.00 18.11 ? 308  VAL A CG2 1 
ATOM   2493 N  N   . LYS A 1 310 ? -8.810  5.904   15.911  1.00 18.25 ? 309  LYS A N   1 
ATOM   2494 C  CA  . LYS A 1 310 ? -9.035  6.096   14.482  1.00 19.46 ? 309  LYS A CA  1 
ATOM   2495 C  C   . LYS A 1 310 ? -7.840  6.734   13.791  1.00 19.36 ? 309  LYS A C   1 
ATOM   2496 O  O   . LYS A 1 310 ? -7.755  6.685   12.559  1.00 20.10 ? 309  LYS A O   1 
ATOM   2497 C  CB  . LYS A 1 310 ? -10.278 6.957   14.243  1.00 21.60 ? 309  LYS A CB  1 
ATOM   2498 C  CG  . LYS A 1 310 ? -11.573 6.268   14.576  1.00 24.06 ? 309  LYS A CG  1 
ATOM   2499 C  CD  . LYS A 1 310 ? -11.714 5.004   13.757  1.00 27.93 ? 309  LYS A CD  1 
ATOM   2500 C  CE  . LYS A 1 310 ? -13.020 4.307   14.034  1.00 33.51 ? 309  LYS A CE  1 
ATOM   2501 N  NZ  . LYS A 1 310 ? -13.019 2.961   13.410  1.00 36.84 ? 309  LYS A NZ  1 
ATOM   2502 N  N   . GLN A 1 311 ? -6.925  7.336   14.546  1.00 19.73 ? 310  GLN A N   1 
ATOM   2503 C  CA  . GLN A 1 311 ? -5.745  7.961   13.969  1.00 18.89 ? 310  GLN A CA  1 
ATOM   2504 C  C   . GLN A 1 311 ? -4.518  7.061   14.000  1.00 18.66 ? 310  GLN A C   1 
ATOM   2505 O  O   . GLN A 1 311 ? -3.445  7.482   13.546  1.00 20.94 ? 310  GLN A O   1 
ATOM   2506 C  CB  . GLN A 1 311 ? -5.449  9.286   14.682  1.00 21.30 ? 310  GLN A CB  1 
ATOM   2507 C  CG  . GLN A 1 311 ? -6.515  10.346  14.415  1.00 27.57 ? 310  GLN A CG  1 
ATOM   2508 C  CD  . GLN A 1 311 ? -6.762  10.563  12.923  1.00 31.72 ? 310  GLN A CD  1 
ATOM   2509 O  OE1 . GLN A 1 311 ? -5.821  10.724  12.143  1.00 33.40 ? 310  GLN A OE1 1 
ATOM   2510 N  NE2 . GLN A 1 311 ? -8.033  10.561  12.520  1.00 32.19 ? 310  GLN A NE2 1 
ATOM   2511 N  N   . LEU A 1 312 ? -4.650  5.832   14.501  1.00 18.10 ? 311  LEU A N   1 
ATOM   2512 C  CA  . LEU A 1 312 ? -3.542  4.874   14.496  1.00 17.92 ? 311  LEU A CA  1 
ATOM   2513 C  C   . LEU A 1 312 ? -3.507  4.167   13.138  1.00 20.05 ? 311  LEU A C   1 
ATOM   2514 O  O   . LEU A 1 312 ? -3.742  2.963   13.011  1.00 20.04 ? 311  LEU A O   1 
ATOM   2515 C  CB  . LEU A 1 312 ? -3.687  3.890   15.649  1.00 17.36 ? 311  LEU A CB  1 
ATOM   2516 C  CG  . LEU A 1 312 ? -3.609  4.499   17.058  1.00 15.92 ? 311  LEU A CG  1 
ATOM   2517 C  CD1 . LEU A 1 312 ? -3.934  3.463   18.124  1.00 16.47 ? 311  LEU A CD1 1 
ATOM   2518 C  CD2 . LEU A 1 312 ? -2.229  5.103   17.309  1.00 18.48 ? 311  LEU A CD2 1 
ATOM   2519 N  N   . LYS A 1 313 ? -3.191  4.956   12.106  1.00 20.32 ? 312  LYS A N   1 
ATOM   2520 C  CA  . LYS A 1 313 ? -3.335  4.474   10.734  1.00 19.69 ? 312  LYS A CA  1 
ATOM   2521 C  C   . LYS A 1 313 ? -2.248  3.468   10.368  1.00 18.21 ? 312  LYS A C   1 
ATOM   2522 O  O   . LYS A 1 313 ? -2.527  2.470   9.690   1.00 18.42 ? 312  LYS A O   1 
ATOM   2523 C  CB  . LYS A 1 313 ? -3.348  5.663   9.773   1.00 21.61 ? 312  LYS A CB  1 
ATOM   2524 C  CG  . LYS A 1 313 ? -4.643  6.468   9.911   1.00 29.05 ? 312  LYS A CG  1 
ATOM   2525 C  CD  . LYS A 1 313 ? -4.675  7.721   9.067   1.00 35.86 ? 312  LYS A CD  1 
ATOM   2526 C  CE  . LYS A 1 313 ? -5.922  8.549   9.389   1.00 40.56 ? 312  LYS A CE  1 
ATOM   2527 N  NZ  . LYS A 1 313 ? -7.182  7.766   9.206   1.00 44.66 ? 312  LYS A NZ  1 
ATOM   2528 N  N   . TYR A 1 314 ? -1.008  3.695   10.814  1.00 20.56 ? 313  TYR A N   1 
ATOM   2529 C  CA  . TYR A 1 314 ? 0.033   2.707   10.551  1.00 17.92 ? 313  TYR A CA  1 
ATOM   2530 C  C   . TYR A 1 314 ? -0.216  1.419   11.330  1.00 18.14 ? 313  TYR A C   1 
ATOM   2531 O  O   . TYR A 1 314 ? -0.012  0.321   10.797  1.00 18.68 ? 313  TYR A O   1 
ATOM   2532 C  CB  . TYR A 1 314 ? 1.419   3.272   10.873  1.00 20.96 ? 313  TYR A CB  1 
ATOM   2533 C  CG  . TYR A 1 314 ? 2.542   2.402   10.348  1.00 20.29 ? 313  TYR A CG  1 
ATOM   2534 C  CD1 . TYR A 1 314 ? 2.833   2.366   8.987   1.00 22.72 ? 313  TYR A CD1 1 
ATOM   2535 C  CD2 . TYR A 1 314 ? 3.298   1.604   11.202  1.00 20.33 ? 313  TYR A CD2 1 
ATOM   2536 C  CE1 . TYR A 1 314 ? 3.848   1.572   8.491   1.00 23.78 ? 313  TYR A CE1 1 
ATOM   2537 C  CE2 . TYR A 1 314 ? 4.322   0.803   10.715  1.00 19.74 ? 313  TYR A CE2 1 
ATOM   2538 C  CZ  . TYR A 1 314 ? 4.589   0.793   9.355   1.00 22.61 ? 313  TYR A CZ  1 
ATOM   2539 O  OH  . TYR A 1 314 ? 5.597   0.015   8.854   1.00 22.97 ? 313  TYR A OH  1 
ATOM   2540 N  N   . VAL A 1 315 ? -0.672  1.518   12.587  1.00 17.38 ? 314  VAL A N   1 
ATOM   2541 C  CA  . VAL A 1 315 ? -1.030  0.297   13.311  1.00 15.34 ? 314  VAL A CA  1 
ATOM   2542 C  C   . VAL A 1 315 ? -2.075  -0.487  12.518  1.00 16.89 ? 314  VAL A C   1 
ATOM   2543 O  O   . VAL A 1 315 ? -2.023  -1.721  12.436  1.00 16.32 ? 314  VAL A O   1 
ATOM   2544 C  CB  . VAL A 1 315 ? -1.518  0.619   14.739  1.00 17.28 ? 314  VAL A CB  1 
ATOM   2545 C  CG1 . VAL A 1 315 ? -1.999  -0.662  15.456  1.00 16.55 ? 314  VAL A CG1 1 
ATOM   2546 C  CG2 . VAL A 1 315 ? -0.412  1.294   15.559  1.00 19.60 ? 314  VAL A CG2 1 
ATOM   2547 N  N   . GLY A 1 316 ? -3.021  0.219   11.897  1.00 15.04 ? 315  GLY A N   1 
ATOM   2548 C  CA  . GLY A 1 316 ? -4.016  -0.465  11.084  1.00 15.09 ? 315  GLY A CA  1 
ATOM   2549 C  C   . GLY A 1 316 ? -3.410  -1.179  9.886   1.00 13.94 ? 315  GLY A C   1 
ATOM   2550 O  O   . GLY A 1 316 ? -3.862  -2.266  9.502   1.00 13.93 ? 315  GLY A O   1 
ATOM   2551 N  N   . MET A 1 317 ? -2.393  -0.571  9.261   1.00 14.95 ? 316  MET A N   1 
ATOM   2552 C  CA  . MET A 1 317 ? -1.708  -1.235  8.150   1.00 16.76 ? 316  MET A CA  1 
ATOM   2553 C  C   . MET A 1 317 ? -0.939  -2.463  8.628   1.00 15.63 ? 316  MET A C   1 
ATOM   2554 O  O   . MET A 1 317 ? -0.876  -3.478  7.922   1.00 14.96 ? 316  MET A O   1 
ATOM   2555 C  CB  . MET A 1 317 ? -0.774  -0.249  7.438   1.00 19.82 ? 316  MET A CB  1 
ATOM   2556 C  CG  . MET A 1 317 ? -1.514  0.829   6.665   1.00 24.16 ? 316  MET A CG  1 
ATOM   2557 S  SD  . MET A 1 317 ? -0.447  2.140   6.019   1.00 30.71 ? 316  MET A SD  1 
ATOM   2558 C  CE  . MET A 1 317 ? 1.033   1.242   5.603   1.00 33.45 ? 316  MET A CE  1 
ATOM   2559 N  N   . VAL A 1 318 ? -0.345  -2.388  9.823   1.00 13.12 ? 317  VAL A N   1 
ATOM   2560 C  CA  . VAL A 1 318 ? 0.327   -3.548  10.406  1.00 14.86 ? 317  VAL A CA  1 
ATOM   2561 C  C   . VAL A 1 318 ? -0.651  -4.712  10.552  1.00 16.09 ? 317  VAL A C   1 
ATOM   2562 O  O   . VAL A 1 318 ? -0.342  -5.862  10.213  1.00 15.76 ? 317  VAL A O   1 
ATOM   2563 C  CB  . VAL A 1 318 ? 0.954   -3.166  11.762  1.00 14.36 ? 317  VAL A CB  1 
ATOM   2564 C  CG1 . VAL A 1 318 ? 1.287   -4.410  12.589  1.00 15.58 ? 317  VAL A CG1 1 
ATOM   2565 C  CG2 . VAL A 1 318 ? 2.189   -2.283  11.553  1.00 16.30 ? 317  VAL A CG2 1 
ATOM   2566 N  N   . LEU A 1 319 ? -1.848  -4.429  11.062  1.00 13.93 ? 318  LEU A N   1 
ATOM   2567 C  CA  . LEU A 1 319 ? -2.843  -5.484  11.237  1.00 12.34 ? 318  LEU A CA  1 
ATOM   2568 C  C   . LEU A 1 319 ? -3.278  -6.072  9.898   1.00 15.11 ? 318  LEU A C   1 
ATOM   2569 O  O   . LEU A 1 319 ? -3.447  -7.289  9.781   1.00 15.01 ? 318  LEU A O   1 
ATOM   2570 C  CB  . LEU A 1 319 ? -4.054  -4.953  12.008  1.00 14.46 ? 318  LEU A CB  1 
ATOM   2571 C  CG  . LEU A 1 319 ? -3.773  -4.575  13.461  1.00 13.45 ? 318  LEU A CG  1 
ATOM   2572 C  CD1 . LEU A 1 319 ? -4.925  -3.773  14.047  1.00 15.80 ? 318  LEU A CD1 1 
ATOM   2573 C  CD2 . LEU A 1 319 ? -3.511  -5.831  14.302  1.00 15.21 ? 318  LEU A CD2 1 
ATOM   2574 N  N   . ASN A 1 320 ? -3.467  -5.231  8.875   1.00 14.58 ? 319  ASN A N   1 
ATOM   2575 C  CA  . ASN A 1 320 ? -3.844  -5.762  7.569   1.00 13.74 ? 319  ASN A CA  1 
ATOM   2576 C  C   . ASN A 1 320 ? -2.746  -6.643  6.990   1.00 12.70 ? 319  ASN A C   1 
ATOM   2577 O  O   . ASN A 1 320 ? -3.031  -7.672  6.366   1.00 14.85 ? 319  ASN A O   1 
ATOM   2578 C  CB  . ASN A 1 320 ? -4.189  -4.619  6.611   1.00 14.46 ? 319  ASN A CB  1 
ATOM   2579 C  CG  . ASN A 1 320 ? -5.610  -4.114  6.815   1.00 17.19 ? 319  ASN A CG  1 
ATOM   2580 O  OD1 . ASN A 1 320 ? -6.490  -4.881  7.196   1.00 20.00 ? 319  ASN A OD1 1 
ATOM   2581 N  ND2 . ASN A 1 320 ? -5.838  -2.825  6.571   1.00 22.58 ? 319  ASN A ND2 1 
ATOM   2582 N  N   . GLU A 1 321 ? -1.481  -6.251  7.171   1.00 13.37 ? 320  GLU A N   1 
ATOM   2583 C  CA  . GLU A 1 321 ? -0.392  -7.059  6.644   1.00 13.87 ? 320  GLU A CA  1 
ATOM   2584 C  C   . GLU A 1 321 ? -0.262  -8.383  7.401   1.00 14.69 ? 320  GLU A C   1 
ATOM   2585 O  O   . GLU A 1 321 ? 0.098   -9.401  6.799   1.00 16.41 ? 320  GLU A O   1 
ATOM   2586 C  CB  . GLU A 1 321 ? 0.908   -6.248  6.676   1.00 16.01 ? 320  GLU A CB  1 
ATOM   2587 C  CG  . GLU A 1 321 ? 2.153   -6.968  6.172   1.00 17.31 ? 320  GLU A CG  1 
ATOM   2588 C  CD  . GLU A 1 321 ? 2.213   -7.131  4.653   1.00 16.45 ? 320  GLU A CD  1 
ATOM   2589 O  OE1 . GLU A 1 321 ? 1.156   -7.054  3.966   1.00 16.57 ? 320  GLU A OE1 1 
ATOM   2590 O  OE2 . GLU A 1 321 ? 3.335   -7.354  4.146   1.00 17.46 ? 320  GLU A OE2 1 
ATOM   2591 N  N   . ALA A 1 322 ? -0.571  -8.406  8.706   1.00 13.62 ? 321  ALA A N   1 
ATOM   2592 C  CA  . ALA A 1 322 ? -0.625  -9.683  9.418   1.00 13.58 ? 321  ALA A CA  1 
ATOM   2593 C  C   . ALA A 1 322 ? -1.785  -10.550 8.926   1.00 13.40 ? 321  ALA A C   1 
ATOM   2594 O  O   . ALA A 1 322 ? -1.652  -11.776 8.835   1.00 15.29 ? 321  ALA A O   1 
ATOM   2595 C  CB  . ALA A 1 322 ? -0.722  -9.452  10.934  1.00 14.17 ? 321  ALA A CB  1 
ATOM   2596 N  N   . LEU A 1 323 ? -2.927  -9.940  8.592   1.00 11.82 ? 322  LEU A N   1 
ATOM   2597 C  CA  . LEU A 1 323 ? -4.022  -10.712 7.995   1.00 11.66 ? 322  LEU A CA  1 
ATOM   2598 C  C   . LEU A 1 323 ? -3.694  -11.172 6.579   1.00 15.28 ? 322  LEU A C   1 
ATOM   2599 O  O   . LEU A 1 323 ? -4.258  -12.171 6.109   1.00 16.18 ? 322  LEU A O   1 
ATOM   2600 C  CB  . LEU A 1 323 ? -5.314  -9.894  7.973   1.00 11.90 ? 322  LEU A CB  1 
ATOM   2601 C  CG  . LEU A 1 323 ? -6.030  -9.687  9.312   1.00 11.61 ? 322  LEU A CG  1 
ATOM   2602 C  CD1 . LEU A 1 323 ? -7.170  -8.693  9.138   1.00 15.21 ? 322  LEU A CD1 1 
ATOM   2603 C  CD2 . LEU A 1 323 ? -6.544  -11.020 9.865   1.00 13.55 ? 322  LEU A CD2 1 
ATOM   2604 N  N   . ARG A 1 324 ? -2.811  -10.460 5.873   1.00 13.35 ? 323  ARG A N   1 
ATOM   2605 C  CA  . ARG A 1 324 ? -2.407  -10.950 4.561   1.00 12.90 ? 323  ARG A CA  1 
ATOM   2606 C  C   . ARG A 1 324 ? -1.635  -12.256 4.696   1.00 14.35 ? 323  ARG A C   1 
ATOM   2607 O  O   . ARG A 1 324 ? -1.979  -13.260 4.066   1.00 15.22 ? 323  ARG A O   1 
ATOM   2608 C  CB  . ARG A 1 324 ? -1.573  -9.899  3.817   1.00 13.82 ? 323  ARG A CB  1 
ATOM   2609 C  CG  . ARG A 1 324 ? -1.249  -10.318 2.363   1.00 14.84 ? 323  ARG A CG  1 
ATOM   2610 C  CD  . ARG A 1 324 ? -0.342  -9.332  1.621   1.00 15.45 ? 323  ARG A CD  1 
ATOM   2611 N  NE  . ARG A 1 324 ? 0.985   -9.253  2.220   1.00 15.10 ? 323  ARG A NE  1 
ATOM   2612 C  CZ  . ARG A 1 324 ? 1.977   -10.099 1.972   1.00 16.75 ? 323  ARG A CZ  1 
ATOM   2613 N  NH1 . ARG A 1 324 ? 1.821   -11.133 1.162   1.00 18.08 ? 323  ARG A NH1 1 
ATOM   2614 N  NH2 . ARG A 1 324 ? 3.160   -9.900  2.550   1.00 17.41 ? 323  ARG A NH2 1 
ATOM   2615 N  N   . LEU A 1 325 ? -0.614  -12.280 5.556   1.00 14.96 ? 324  LEU A N   1 
ATOM   2616 C  CA  . LEU A 1 325 ? 0.249   -13.456 5.612   1.00 15.16 ? 324  LEU A CA  1 
ATOM   2617 C  C   . LEU A 1 325 ? -0.425  -14.634 6.315   1.00 15.89 ? 324  LEU A C   1 
ATOM   2618 O  O   . LEU A 1 325 ? -0.259  -15.783 5.896   1.00 16.88 ? 324  LEU A O   1 
ATOM   2619 C  CB  . LEU A 1 325 ? 1.576   -13.091 6.273   1.00 17.46 ? 324  LEU A CB  1 
ATOM   2620 C  CG  . LEU A 1 325 ? 2.482   -12.341 5.291   1.00 18.08 ? 324  LEU A CG  1 
ATOM   2621 C  CD1 . LEU A 1 325 ? 3.671   -11.701 6.021   1.00 19.63 ? 324  LEU A CD1 1 
ATOM   2622 C  CD2 . LEU A 1 325 ? 2.975   -13.275 4.165   1.00 20.29 ? 324  LEU A CD2 1 
ATOM   2623 N  N   . TRP A 1 326 ? -1.178  -14.391 7.386   1.00 13.90 ? 325  TRP A N   1 
ATOM   2624 C  CA  . TRP A 1 326 ? -1.846  -15.471 8.115   1.00 13.59 ? 325  TRP A CA  1 
ATOM   2625 C  C   . TRP A 1 326 ? -3.264  -15.071 8.482   1.00 12.01 ? 325  TRP A C   1 
ATOM   2626 O  O   . TRP A 1 326 ? -3.563  -14.750 9.640   1.00 14.72 ? 325  TRP A O   1 
ATOM   2627 C  CB  . TRP A 1 326 ? -1.031  -15.886 9.349   1.00 14.83 ? 325  TRP A CB  1 
ATOM   2628 C  CG  . TRP A 1 326 ? 0.186   -16.616 8.919   1.00 13.54 ? 325  TRP A CG  1 
ATOM   2629 C  CD1 . TRP A 1 326 ? 1.484   -16.192 9.022   1.00 13.79 ? 325  TRP A CD1 1 
ATOM   2630 C  CD2 . TRP A 1 326 ? 0.230   -17.880 8.247   1.00 14.91 ? 325  TRP A CD2 1 
ATOM   2631 N  NE1 . TRP A 1 326 ? 2.332   -17.125 8.468   1.00 16.97 ? 325  TRP A NE1 1 
ATOM   2632 C  CE2 . TRP A 1 326 ? 1.589   -18.172 7.989   1.00 16.73 ? 325  TRP A CE2 1 
ATOM   2633 C  CE3 . TRP A 1 326 ? -0.748  -18.798 7.840   1.00 15.99 ? 325  TRP A CE3 1 
ATOM   2634 C  CZ2 . TRP A 1 326 ? 1.994   -19.345 7.340   1.00 18.64 ? 325  TRP A CZ2 1 
ATOM   2635 C  CZ3 . TRP A 1 326 ? -0.342  -19.965 7.200   1.00 19.17 ? 325  TRP A CZ3 1 
ATOM   2636 C  CH2 . TRP A 1 326 ? 1.019   -20.226 6.956   1.00 18.74 ? 325  TRP A CH2 1 
ATOM   2637 N  N   . PRO A 1 327 ? -4.181  -15.109 7.515   1.00 12.42 ? 326  PRO A N   1 
ATOM   2638 C  CA  . PRO A 1 327 ? -5.600  -14.847 7.826   1.00 11.83 ? 326  PRO A CA  1 
ATOM   2639 C  C   . PRO A 1 327 ? -6.144  -15.923 8.755   1.00 12.81 ? 326  PRO A C   1 
ATOM   2640 O  O   . PRO A 1 327 ? -6.075  -17.119 8.453   1.00 13.60 ? 326  PRO A O   1 
ATOM   2641 C  CB  . PRO A 1 327 ? -6.273  -14.878 6.451   1.00 13.63 ? 326  PRO A CB  1 
ATOM   2642 C  CG  . PRO A 1 327 ? -5.345  -15.734 5.588   1.00 13.72 ? 326  PRO A CG  1 
ATOM   2643 C  CD  . PRO A 1 327 ? -3.953  -15.476 6.102   1.00 13.23 ? 326  PRO A CD  1 
ATOM   2644 N  N   . THR A 1 328 ? -6.699  -15.493 9.894   1.00 12.22 ? 327  THR A N   1 
ATOM   2645 C  CA  . THR A 1 328 ? -6.929  -16.438 10.985  1.00 11.73 ? 327  THR A CA  1 
ATOM   2646 C  C   . THR A 1 328 ? -8.181  -17.285 10.795  1.00 15.53 ? 327  THR A C   1 
ATOM   2647 O  O   . THR A 1 328 ? -8.302  -18.330 11.446  1.00 14.86 ? 327  THR A O   1 
ATOM   2648 C  CB  . THR A 1 328 ? -6.968  -15.686 12.322  1.00 13.27 ? 327  THR A CB  1 
ATOM   2649 O  OG1 . THR A 1 328 ? -7.832  -14.548 12.223  1.00 15.16 ? 327  THR A OG1 1 
ATOM   2650 C  CG2 . THR A 1 328 ? -5.567  -15.197 12.652  1.00 14.96 ? 327  THR A CG2 1 
ATOM   2651 N  N   . ALA A 1 329 ? -9.117  -16.862 9.924   1.00 14.44 ? 328  ALA A N   1 
ATOM   2652 C  CA  . ALA A 1 329 ? -10.171 -17.727 9.406   1.00 12.89 ? 328  ALA A CA  1 
ATOM   2653 C  C   . ALA A 1 329 ? -9.792  -18.083 7.972   1.00 13.50 ? 328  ALA A C   1 
ATOM   2654 O  O   . ALA A 1 329 ? -10.137 -17.348 7.040   1.00 17.85 ? 328  ALA A O   1 
ATOM   2655 C  CB  . ALA A 1 329 ? -11.532 -17.039 9.461   1.00 15.42 ? 328  ALA A CB  1 
ATOM   2656 N  N   . PRO A 1 330 ? -9.090  -19.198 7.756   1.00 12.46 ? 329  PRO A N   1 
ATOM   2657 C  CA  . PRO A 1 330 ? -8.229  -19.312 6.565   1.00 12.15 ? 329  PRO A CA  1 
ATOM   2658 C  C   . PRO A 1 330 ? -8.920  -19.756 5.283   1.00 12.01 ? 329  PRO A C   1 
ATOM   2659 O  O   . PRO A 1 330 ? -8.243  -19.857 4.252   1.00 13.19 ? 329  PRO A O   1 
ATOM   2660 C  CB  . PRO A 1 330 ? -7.182  -20.347 7.008   1.00 13.83 ? 329  PRO A CB  1 
ATOM   2661 C  CG  . PRO A 1 330 ? -7.944  -21.233 7.975   1.00 13.31 ? 329  PRO A CG  1 
ATOM   2662 C  CD  . PRO A 1 330 ? -8.815  -20.255 8.751   1.00 11.90 ? 329  PRO A CD  1 
ATOM   2663 N  N   . ALA A 1 331 ? -10.225 -20.013 5.291   1.00 12.47 ? 330  ALA A N   1 
ATOM   2664 C  CA  . ALA A 1 331 ? -10.921 -20.436 4.080   1.00 11.34 ? 330  ALA A CA  1 
ATOM   2665 C  C   . ALA A 1 331 ? -12.397 -20.090 4.196   1.00 11.45 ? 330  ALA A C   1 
ATOM   2666 O  O   . ALA A 1 331 ? -12.935 -19.928 5.296   1.00 13.65 ? 330  ALA A O   1 
ATOM   2667 C  CB  . ALA A 1 331 ? -10.753 -21.941 3.827   1.00 12.20 ? 330  ALA A CB  1 
ATOM   2668 N  N   . PHE A 1 332 ? -13.038 -19.955 3.037   1.00 11.68 ? 331  PHE A N   1 
ATOM   2669 C  CA  . PHE A 1 332 ? -14.488 -19.945 2.947   1.00 13.37 ? 331  PHE A CA  1 
ATOM   2670 C  C   . PHE A 1 332 ? -14.888 -20.674 1.671   1.00 14.46 ? 331  PHE A C   1 
ATOM   2671 O  O   . PHE A 1 332 ? -14.069 -20.890 0.773   1.00 15.94 ? 331  PHE A O   1 
ATOM   2672 C  CB  . PHE A 1 332 ? -15.081 -18.518 3.015   1.00 14.61 ? 331  PHE A CB  1 
ATOM   2673 C  CG  . PHE A 1 332 ? -14.577 -17.558 1.970   1.00 13.60 ? 331  PHE A CG  1 
ATOM   2674 C  CD1 . PHE A 1 332 ? -13.449 -16.779 2.208   1.00 12.15 ? 331  PHE A CD1 1 
ATOM   2675 C  CD2 . PHE A 1 332 ? -15.289 -17.354 0.796   1.00 13.67 ? 331  PHE A CD2 1 
ATOM   2676 C  CE1 . PHE A 1 332 ? -13.011 -15.846 1.269   1.00 13.30 ? 331  PHE A CE1 1 
ATOM   2677 C  CE2 . PHE A 1 332 ? -14.856 -16.420 -0.153  1.00 14.23 ? 331  PHE A CE2 1 
ATOM   2678 C  CZ  . PHE A 1 332 ? -13.722 -15.669 0.084   1.00 14.46 ? 331  PHE A CZ  1 
ATOM   2679 N  N   . SER A 1 333 ? -16.153 -21.086 1.619   1.00 14.20 ? 332  SER A N   1 
ATOM   2680 C  CA  . SER A 1 333 ? -16.660 -21.980 0.589   1.00 12.38 ? 332  SER A CA  1 
ATOM   2681 C  C   . SER A 1 333 ? -17.789 -21.299 -0.177  1.00 13.34 ? 332  SER A C   1 
ATOM   2682 O  O   . SER A 1 333 ? -18.519 -20.471 0.378   1.00 12.30 ? 332  SER A O   1 
ATOM   2683 C  CB  . SER A 1 333 ? -17.150 -23.300 1.224   1.00 12.80 ? 332  SER A CB  1 
ATOM   2684 O  OG  . SER A 1 333 ? -17.525 -24.261 0.254   1.00 13.80 ? 332  SER A OG  1 
ATOM   2685 N  N   . LEU A 1 334 ? -17.923 -21.656 -1.462  1.00 12.39 ? 333  LEU A N   1 
ATOM   2686 C  CA  . LEU A 1 334 ? -18.932 -21.095 -2.354  1.00 13.15 ? 333  LEU A CA  1 
ATOM   2687 C  C   . LEU A 1 334 ? -19.553 -22.210 -3.193  1.00 14.57 ? 333  LEU A C   1 
ATOM   2688 O  O   . LEU A 1 334 ? -18.950 -23.271 -3.392  1.00 15.55 ? 333  LEU A O   1 
ATOM   2689 C  CB  . LEU A 1 334 ? -18.325 -20.027 -3.288  1.00 12.53 ? 333  LEU A CB  1 
ATOM   2690 C  CG  . LEU A 1 334 ? -17.596 -18.852 -2.620  1.00 12.99 ? 333  LEU A CG  1 
ATOM   2691 C  CD1 . LEU A 1 334 ? -16.649 -18.158 -3.590  1.00 16.85 ? 333  LEU A CD1 1 
ATOM   2692 C  CD2 . LEU A 1 334 ? -18.605 -17.841 -2.047  1.00 13.67 ? 333  LEU A CD2 1 
ATOM   2693 N  N   . TYR A 1 335 ? -20.771 -21.968 -3.693  1.00 12.97 ? 334  TYR A N   1 
ATOM   2694 C  CA  . TYR A 1 335 ? -21.383 -22.867 -4.672  1.00 15.10 ? 334  TYR A CA  1 
ATOM   2695 C  C   . TYR A 1 335 ? -21.920 -22.067 -5.854  1.00 16.40 ? 334  TYR A C   1 
ATOM   2696 O  O   . TYR A 1 335 ? -22.351 -20.918 -5.709  1.00 14.08 ? 334  TYR A O   1 
ATOM   2697 C  CB  . TYR A 1 335 ? -22.520 -23.734 -4.062  1.00 15.44 ? 334  TYR A CB  1 
ATOM   2698 C  CG  . TYR A 1 335 ? -23.773 -22.953 -3.719  1.00 14.66 ? 334  TYR A CG  1 
ATOM   2699 C  CD1 . TYR A 1 335 ? -23.930 -22.373 -2.462  1.00 13.64 ? 334  TYR A CD1 1 
ATOM   2700 C  CD2 . TYR A 1 335 ? -24.793 -22.779 -4.655  1.00 15.97 ? 334  TYR A CD2 1 
ATOM   2701 C  CE1 . TYR A 1 335 ? -25.066 -21.635 -2.148  1.00 12.81 ? 334  TYR A CE1 1 
ATOM   2702 C  CE2 . TYR A 1 335 ? -25.933 -22.048 -4.348  1.00 16.45 ? 334  TYR A CE2 1 
ATOM   2703 C  CZ  . TYR A 1 335 ? -26.063 -21.480 -3.090  1.00 14.92 ? 334  TYR A CZ  1 
ATOM   2704 O  OH  . TYR A 1 335 ? -27.187 -20.742 -2.775  1.00 17.42 ? 334  TYR A OH  1 
ATOM   2705 N  N   . ALA A 1 336 ? -21.888 -22.688 -7.033  1.00 15.11 ? 335  ALA A N   1 
ATOM   2706 C  CA  . ALA A 1 336 ? -22.338 -22.013 -8.245  1.00 14.79 ? 335  ALA A CA  1 
ATOM   2707 C  C   . ALA A 1 336 ? -23.859 -21.904 -8.280  1.00 17.99 ? 335  ALA A C   1 
ATOM   2708 O  O   . ALA A 1 336 ? -24.567 -22.911 -8.169  1.00 17.91 ? 335  ALA A O   1 
ATOM   2709 C  CB  . ALA A 1 336 ? -21.835 -22.755 -9.486  1.00 17.76 ? 335  ALA A CB  1 
ATOM   2710 N  N   . LYS A 1 337 ? -24.362 -20.676 -8.454  1.00 17.08 ? 336  LYS A N   1 
ATOM   2711 C  CA  . LYS A 1 337 ? -25.804 -20.454 -8.527  1.00 17.95 ? 336  LYS A CA  1 
ATOM   2712 C  C   . LYS A 1 337 ? -26.400 -20.951 -9.838  1.00 22.31 ? 336  LYS A C   1 
ATOM   2713 O  O   . LYS A 1 337 ? -27.605 -21.228 -9.891  1.00 24.14 ? 336  LYS A O   1 
ATOM   2714 C  CB  . LYS A 1 337 ? -26.118 -18.965 -8.340  1.00 18.58 ? 336  LYS A CB  1 
ATOM   2715 C  CG  . LYS A 1 337 ? -25.909 -18.470 -6.905  1.00 18.24 ? 336  LYS A CG  1 
ATOM   2716 C  CD  . LYS A 1 337 ? -25.750 -16.933 -6.818  1.00 17.11 ? 336  LYS A CD  1 
ATOM   2717 C  CE  . LYS A 1 337 ? -26.999 -16.192 -7.282  1.00 19.08 ? 336  LYS A CE  1 
ATOM   2718 N  NZ  . LYS A 1 337 ? -28.216 -16.562 -6.498  1.00 19.34 ? 336  LYS A NZ  1 
ATOM   2719 N  N   . GLU A 1 338 ? -25.583 -21.060 -10.885 1.00 18.76 ? 337  GLU A N   1 
ATOM   2720 C  CA  . GLU A 1 338 ? -25.999 -21.546 -12.194 1.00 20.91 ? 337  GLU A CA  1 
ATOM   2721 C  C   . GLU A 1 338 ? -24.783 -22.148 -12.884 1.00 21.85 ? 337  GLU A C   1 
ATOM   2722 O  O   . GLU A 1 338 ? -23.645 -21.961 -12.447 1.00 21.87 ? 337  GLU A O   1 
ATOM   2723 C  CB  . GLU A 1 338 ? -26.594 -20.423 -13.055 1.00 25.39 ? 337  GLU A CB  1 
ATOM   2724 C  CG  . GLU A 1 338 ? -27.860 -19.792 -12.499 1.00 33.91 ? 337  GLU A CG  1 
ATOM   2725 C  CD  . GLU A 1 338 ? -29.037 -20.756 -12.436 1.00 38.54 ? 337  GLU A CD  1 
ATOM   2726 O  OE1 . GLU A 1 338 ? -29.013 -21.788 -13.140 1.00 41.13 ? 337  GLU A OE1 1 
ATOM   2727 O  OE2 . GLU A 1 338 ? -29.988 -20.474 -11.669 1.00 38.04 ? 337  GLU A OE2 1 
ATOM   2728 N  N   . ASP A 1 339 ? -25.027 -22.876 -13.975 1.00 24.31 ? 338  ASP A N   1 
ATOM   2729 C  CA  . ASP A 1 339 ? -23.923 -23.257 -14.849 1.00 24.03 ? 338  ASP A CA  1 
ATOM   2730 C  C   . ASP A 1 339 ? -23.111 -22.017 -15.204 1.00 25.17 ? 338  ASP A C   1 
ATOM   2731 O  O   . ASP A 1 339 ? -23.670 -20.973 -15.548 1.00 26.52 ? 338  ASP A O   1 
ATOM   2732 C  CB  . ASP A 1 339 ? -24.435 -23.911 -16.140 1.00 26.22 ? 338  ASP A CB  1 
ATOM   2733 C  CG  . ASP A 1 339 ? -25.182 -25.217 -15.905 1.00 26.85 ? 338  ASP A CG  1 
ATOM   2734 O  OD1 . ASP A 1 339 ? -25.253 -25.704 -14.764 1.00 27.65 ? 338  ASP A OD1 1 
ATOM   2735 O  OD2 . ASP A 1 339 ? -25.711 -25.764 -16.891 1.00 28.89 ? 338  ASP A OD2 1 
ATOM   2736 N  N   . THR A 1 340 ? -21.786 -22.134 -15.140 1.00 22.93 ? 339  THR A N   1 
ATOM   2737 C  CA  . THR A 1 340 ? -20.923 -21.002 -15.458 1.00 24.00 ? 339  THR A CA  1 
ATOM   2738 C  C   . THR A 1 340 ? -19.520 -21.533 -15.724 1.00 25.90 ? 339  THR A C   1 
ATOM   2739 O  O   . THR A 1 340 ? -19.204 -22.679 -15.398 1.00 30.43 ? 339  THR A O   1 
ATOM   2740 C  CB  . THR A 1 340 ? -20.937 -19.958 -14.325 1.00 24.25 ? 339  THR A CB  1 
ATOM   2741 O  OG1 . THR A 1 340 ? -20.368 -18.722 -14.778 1.00 24.35 ? 339  THR A OG1 1 
ATOM   2742 C  CG2 . THR A 1 340 ? -20.162 -20.462 -13.102 1.00 23.15 ? 339  THR A CG2 1 
ATOM   2743 N  N   . VAL A 1 341 ? -18.687 -20.695 -16.339 1.00 22.50 ? 340  VAL A N   1 
ATOM   2744 C  CA  . VAL A 1 341 ? -17.319 -21.058 -16.690 1.00 21.51 ? 340  VAL A CA  1 
ATOM   2745 C  C   . VAL A 1 341 ? -16.358 -20.164 -15.921 1.00 24.42 ? 340  VAL A C   1 
ATOM   2746 O  O   . VAL A 1 341 ? -16.451 -18.933 -15.992 1.00 25.22 ? 340  VAL A O   1 
ATOM   2747 C  CB  . VAL A 1 341 ? -17.068 -20.947 -18.204 1.00 21.91 ? 340  VAL A CB  1 
ATOM   2748 C  CG1 . VAL A 1 341 ? -15.612 -21.271 -18.514 1.00 24.09 ? 340  VAL A CG1 1 
ATOM   2749 C  CG2 . VAL A 1 341 ? -18.000 -21.878 -18.954 1.00 22.76 ? 340  VAL A CG2 1 
ATOM   2750 N  N   . LEU A 1 342 ? -15.432 -20.786 -15.200 1.00 22.70 ? 341  LEU A N   1 
ATOM   2751 C  CA  . LEU A 1 342 ? -14.455 -20.072 -14.391 1.00 25.54 ? 341  LEU A CA  1 
ATOM   2752 C  C   . LEU A 1 342 ? -13.188 -19.839 -15.206 1.00 26.56 ? 341  LEU A C   1 
ATOM   2753 O  O   . LEU A 1 342 ? -12.596 -20.789 -15.728 1.00 28.34 ? 341  LEU A O   1 
ATOM   2754 C  CB  . LEU A 1 342 ? -14.144 -20.863 -13.120 1.00 27.33 ? 341  LEU A CB  1 
ATOM   2755 C  CG  . LEU A 1 342 ? -13.652 -20.072 -11.918 1.00 26.95 ? 341  LEU A CG  1 
ATOM   2756 C  CD1 . LEU A 1 342 ? -14.723 -19.100 -11.435 1.00 27.50 ? 341  LEU A CD1 1 
ATOM   2757 C  CD2 . LEU A 1 342 ? -13.240 -21.031 -10.807 1.00 26.30 ? 341  LEU A CD2 1 
ATOM   2758 N  N   . GLY A 1 343 ? -12.781 -18.576 -15.319 1.00 26.26 ? 342  GLY A N   1 
ATOM   2759 C  CA  . GLY A 1 343 ? -11.534 -18.238 -15.982 1.00 27.12 ? 342  GLY A CA  1 
ATOM   2760 C  C   . GLY A 1 343 ? -11.458 -18.622 -17.441 1.00 27.77 ? 342  GLY A C   1 
ATOM   2761 O  O   . GLY A 1 343 ? -10.354 -18.779 -17.976 1.00 30.43 ? 342  GLY A O   1 
ATOM   2762 N  N   . GLY A 1 344 ? -12.602 -18.765 -18.109 1.00 25.26 ? 343  GLY A N   1 
ATOM   2763 C  CA  . GLY A 1 344 ? -12.616 -19.199 -19.491 1.00 26.45 ? 343  GLY A CA  1 
ATOM   2764 C  C   . GLY A 1 344 ? -12.088 -20.595 -19.723 1.00 27.56 ? 343  GLY A C   1 
ATOM   2765 O  O   . GLY A 1 344 ? -11.872 -20.979 -20.881 1.00 28.87 ? 343  GLY A O   1 
ATOM   2766 N  N   . GLU A 1 345 ? -11.882 -21.378 -18.664 1.00 27.92 ? 344  GLU A N   1 
ATOM   2767 C  CA  . GLU A 1 345 ? -11.181 -22.648 -18.801 1.00 28.85 ? 344  GLU A CA  1 
ATOM   2768 C  C   . GLU A 1 345 ? -11.847 -23.786 -18.033 1.00 27.64 ? 344  GLU A C   1 
ATOM   2769 O  O   . GLU A 1 345 ? -11.696 -24.953 -18.407 1.00 27.77 ? 344  GLU A O   1 
ATOM   2770 C  CB  . GLU A 1 345 ? -9.724  -22.492 -18.337 1.00 32.03 ? 344  GLU A CB  1 
ATOM   2771 C  CG  . GLU A 1 345 ? -8.879  -21.648 -19.285 1.00 35.85 ? 344  GLU A CG  1 
ATOM   2772 C  CD  . GLU A 1 345 ? -7.442  -21.454 -18.818 1.00 40.03 ? 344  GLU A CD  1 
ATOM   2773 O  OE1 . GLU A 1 345 ? -7.203  -21.393 -17.595 1.00 39.29 ? 344  GLU A OE1 1 
ATOM   2774 O  OE2 . GLU A 1 345 ? -6.547  -21.351 -19.688 1.00 45.06 ? 344  GLU A OE2 1 
ATOM   2775 N  N   . TYR A 1 346 ? -12.576 -23.474 -16.962 1.00 25.52 ? 345  TYR A N   1 
ATOM   2776 C  CA  . TYR A 1 346 ? -13.093 -24.501 -16.056 1.00 24.46 ? 345  TYR A CA  1 
ATOM   2777 C  C   . TYR A 1 346 ? -14.608 -24.432 -15.954 1.00 24.48 ? 345  TYR A C   1 
ATOM   2778 O  O   . TYR A 1 346 ? -15.150 -23.652 -15.146 1.00 23.74 ? 345  TYR A O   1 
ATOM   2779 C  CB  . TYR A 1 346 ? -12.454 -24.363 -14.676 1.00 22.32 ? 345  TYR A CB  1 
ATOM   2780 C  CG  . TYR A 1 346 ? -10.950 -24.487 -14.744 1.00 22.82 ? 345  TYR A CG  1 
ATOM   2781 C  CD1 . TYR A 1 346 ? -10.353 -25.714 -15.001 1.00 24.24 ? 345  TYR A CD1 1 
ATOM   2782 C  CD2 . TYR A 1 346 ? -10.129 -23.378 -14.587 1.00 23.22 ? 345  TYR A CD2 1 
ATOM   2783 C  CE1 . TYR A 1 346 ? -8.977  -25.840 -15.083 1.00 24.13 ? 345  TYR A CE1 1 
ATOM   2784 C  CE2 . TYR A 1 346 ? -8.752  -23.491 -14.669 1.00 24.85 ? 345  TYR A CE2 1 
ATOM   2785 C  CZ  . TYR A 1 346 ? -8.180  -24.725 -14.915 1.00 25.47 ? 345  TYR A CZ  1 
ATOM   2786 O  OH  . TYR A 1 346 ? -6.806  -24.846 -14.995 1.00 26.70 ? 345  TYR A OH  1 
ATOM   2787 N  N   . PRO A 1 347 ? -15.329 -25.238 -16.730 1.00 23.79 ? 346  PRO A N   1 
ATOM   2788 C  CA  . PRO A 1 347 ? -16.793 -25.221 -16.654 1.00 25.46 ? 346  PRO A CA  1 
ATOM   2789 C  C   . PRO A 1 347 ? -17.297 -25.837 -15.357 1.00 24.73 ? 346  PRO A C   1 
ATOM   2790 O  O   . PRO A 1 347 ? -16.824 -26.887 -14.913 1.00 25.23 ? 346  PRO A O   1 
ATOM   2791 C  CB  . PRO A 1 347 ? -17.222 -26.047 -17.870 1.00 27.95 ? 346  PRO A CB  1 
ATOM   2792 C  CG  . PRO A 1 347 ? -16.045 -26.934 -18.160 1.00 28.65 ? 346  PRO A CG  1 
ATOM   2793 C  CD  . PRO A 1 347 ? -14.827 -26.139 -17.781 1.00 24.86 ? 346  PRO A CD  1 
ATOM   2794 N  N   . LEU A 1 348 ? -18.277 -25.166 -14.762 1.00 23.88 ? 347  LEU A N   1 
ATOM   2795 C  CA  . LEU A 1 348 ? -18.942 -25.607 -13.549 1.00 19.63 ? 347  LEU A CA  1 
ATOM   2796 C  C   . LEU A 1 348 ? -20.433 -25.759 -13.812 1.00 22.02 ? 347  LEU A C   1 
ATOM   2797 O  O   . LEU A 1 348 ? -21.023 -24.997 -14.586 1.00 24.11 ? 347  LEU A O   1 
ATOM   2798 C  CB  . LEU A 1 348 ? -18.724 -24.609 -12.404 1.00 20.09 ? 347  LEU A CB  1 
ATOM   2799 C  CG  . LEU A 1 348 ? -17.265 -24.286 -12.086 1.00 21.08 ? 347  LEU A CG  1 
ATOM   2800 C  CD1 . LEU A 1 348 ? -17.153 -23.132 -11.075 1.00 21.37 ? 347  LEU A CD1 1 
ATOM   2801 C  CD2 . LEU A 1 348 ? -16.562 -25.538 -11.562 1.00 22.50 ? 347  LEU A CD2 1 
ATOM   2802 N  N   . GLU A 1 349 ? -21.036 -26.748 -13.157 1.00 20.65 ? 348  GLU A N   1 
ATOM   2803 C  CA  . GLU A 1 349 ? -22.479 -26.934 -13.168 1.00 21.85 ? 348  GLU A CA  1 
ATOM   2804 C  C   . GLU A 1 349 ? -23.100 -26.330 -11.912 1.00 20.08 ? 348  GLU A C   1 
ATOM   2805 O  O   . GLU A 1 349 ? -22.456 -26.237 -10.862 1.00 19.79 ? 348  GLU A O   1 
ATOM   2806 C  CB  . GLU A 1 349 ? -22.836 -28.417 -13.266 1.00 23.58 ? 348  GLU A CB  1 
ATOM   2807 C  CG  . GLU A 1 349 ? -22.295 -29.086 -14.526 1.00 26.62 ? 348  GLU A CG  1 
ATOM   2808 C  CD  . GLU A 1 349 ? -22.759 -30.522 -14.670 1.00 37.58 ? 348  GLU A CD  1 
ATOM   2809 O  OE1 . GLU A 1 349 ? -23.600 -30.959 -13.863 1.00 43.56 ? 348  GLU A OE1 1 
ATOM   2810 O  OE2 . GLU A 1 349 ? -22.288 -31.210 -15.596 1.00 42.52 ? 348  GLU A OE2 1 
ATOM   2811 N  N   . LYS A 1 350 ? -24.359 -25.911 -12.036 1.00 21.92 ? 349  LYS A N   1 
ATOM   2812 C  CA  . LYS A 1 350 ? -25.120 -25.398 -10.900 1.00 20.87 ? 349  LYS A CA  1 
ATOM   2813 C  C   . LYS A 1 350 ? -24.948 -26.306 -9.690  1.00 20.62 ? 349  LYS A C   1 
ATOM   2814 O  O   . LYS A 1 350 ? -25.115 -27.525 -9.786  1.00 22.60 ? 349  LYS A O   1 
ATOM   2815 C  CB  . LYS A 1 350 ? -26.602 -25.294 -11.276 1.00 22.71 ? 349  LYS A CB  1 
ATOM   2816 C  CG  . LYS A 1 350 ? -27.514 -24.765 -10.172 1.00 27.06 ? 349  LYS A CG  1 
ATOM   2817 C  CD  . LYS A 1 350 ? -28.929 -24.583 -10.704 1.00 28.21 ? 349  LYS A CD  1 
ATOM   2818 C  CE  . LYS A 1 350 ? -29.885 -24.044 -9.651  1.00 31.06 ? 349  LYS A CE  1 
ATOM   2819 N  NZ  . LYS A 1 350 ? -31.169 -23.596 -10.270 1.00 37.08 ? 349  LYS A NZ  1 
ATOM   2820 N  N   . GLY A 1 351 ? -24.598 -25.705 -8.551  1.00 18.97 ? 350  GLY A N   1 
ATOM   2821 C  CA  . GLY A 1 351 ? -24.388 -26.450 -7.329  1.00 18.77 ? 350  GLY A CA  1 
ATOM   2822 C  C   . GLY A 1 351 ? -22.959 -26.874 -7.059  1.00 18.42 ? 350  GLY A C   1 
ATOM   2823 O  O   . GLY A 1 351 ? -22.654 -27.269 -5.921  1.00 17.83 ? 350  GLY A O   1 
ATOM   2824 N  N   . ASP A 1 352 ? -22.077 -26.817 -8.061  1.00 18.83 ? 351  ASP A N   1 
ATOM   2825 C  CA  . ASP A 1 352 ? -20.681 -27.182 -7.855  1.00 17.46 ? 351  ASP A CA  1 
ATOM   2826 C  C   . ASP A 1 352 ? -20.045 -26.268 -6.813  1.00 18.38 ? 351  ASP A C   1 
ATOM   2827 O  O   . ASP A 1 352 ? -20.306 -25.060 -6.789  1.00 18.95 ? 351  ASP A O   1 
ATOM   2828 C  CB  . ASP A 1 352 ? -19.900 -27.084 -9.170  1.00 18.84 ? 351  ASP A CB  1 
ATOM   2829 C  CG  . ASP A 1 352 ? -20.109 -28.287 -10.088 1.00 23.07 ? 351  ASP A CG  1 
ATOM   2830 O  OD1 . ASP A 1 352 ? -20.776 -29.272 -9.690  1.00 23.29 ? 351  ASP A OD1 1 
ATOM   2831 O  OD2 . ASP A 1 352 ? -19.587 -28.240 -11.221 1.00 22.95 ? 351  ASP A OD2 1 
ATOM   2832 N  N   . GLU A 1 353 ? -19.175 -26.844 -5.971  1.00 18.12 ? 352  GLU A N   1 
ATOM   2833 C  CA  . GLU A 1 353 ? -18.582 -26.140 -4.840  1.00 18.27 ? 352  GLU A CA  1 
ATOM   2834 C  C   . GLU A 1 353 ? -17.142 -25.706 -5.105  1.00 16.92 ? 352  GLU A C   1 
ATOM   2835 O  O   . GLU A 1 353 ? -16.412 -26.330 -5.885  1.00 17.12 ? 352  GLU A O   1 
ATOM   2836 C  CB  . GLU A 1 353 ? -18.604 -27.016 -3.583  1.00 22.31 ? 352  GLU A CB  1 
ATOM   2837 C  CG  . GLU A 1 353 ? -19.973 -27.480 -3.180  1.00 30.26 ? 352  GLU A CG  1 
ATOM   2838 C  CD  . GLU A 1 353 ? -19.947 -28.381 -1.958  1.00 33.70 ? 352  GLU A CD  1 
ATOM   2839 O  OE1 . GLU A 1 353 ? -18.928 -28.385 -1.225  1.00 29.19 ? 352  GLU A OE1 1 
ATOM   2840 O  OE2 . GLU A 1 353 ? -20.952 -29.091 -1.740  1.00 37.13 ? 352  GLU A OE2 1 
ATOM   2841 N  N   . LEU A 1 354 ? -16.739 -24.633 -4.409  1.00 13.97 ? 353  LEU A N   1 
ATOM   2842 C  CA  . LEU A 1 354 ? -15.389 -24.092 -4.427  1.00 14.73 ? 353  LEU A CA  1 
ATOM   2843 C  C   . LEU A 1 354 ? -14.926 -23.860 -2.995  1.00 15.00 ? 353  LEU A C   1 
ATOM   2844 O  O   . LEU A 1 354 ? -15.736 -23.544 -2.119  1.00 15.06 ? 353  LEU A O   1 
ATOM   2845 C  CB  . LEU A 1 354 ? -15.327 -22.747 -5.183  1.00 14.10 ? 353  LEU A CB  1 
ATOM   2846 C  CG  . LEU A 1 354 ? -15.843 -22.697 -6.618  1.00 17.64 ? 353  LEU A CG  1 
ATOM   2847 C  CD1 . LEU A 1 354 ? -15.903 -21.258 -7.095  1.00 17.03 ? 353  LEU A CD1 1 
ATOM   2848 C  CD2 . LEU A 1 354 ? -14.932 -23.538 -7.501  1.00 18.76 ? 353  LEU A CD2 1 
ATOM   2849 N  N   . MET A 1 355 ? -13.619 -23.989 -2.762  1.00 14.06 ? 354  MET A N   1 
ATOM   2850 C  CA  . MET A 1 355 ? -12.988 -23.510 -1.533  1.00 14.37 ? 354  MET A CA  1 
ATOM   2851 C  C   . MET A 1 355 ? -12.000 -22.406 -1.884  1.00 14.35 ? 354  MET A C   1 
ATOM   2852 O  O   . MET A 1 355 ? -11.183 -22.578 -2.793  1.00 16.73 ? 354  MET A O   1 
ATOM   2853 C  CB  . MET A 1 355 ? -12.249 -24.637 -0.790  1.00 13.99 ? 354  MET A CB  1 
ATOM   2854 C  CG  . MET A 1 355 ? -13.134 -25.787 -0.290  1.00 15.23 ? 354  MET A CG  1 
ATOM   2855 S  SD  . MET A 1 355 ? -14.316 -25.339 1.014   1.00 17.99 ? 354  MET A SD  1 
ATOM   2856 C  CE  . MET A 1 355 ? -13.236 -24.530 2.196   1.00 19.50 ? 354  MET A CE  1 
ATOM   2857 N  N   . VAL A 1 356 ? -12.068 -21.279 -1.173  1.00 14.62 ? 355  VAL A N   1 
ATOM   2858 C  CA  . VAL A 1 356 ? -11.105 -20.193 -1.328  1.00 13.88 ? 355  VAL A CA  1 
ATOM   2859 C  C   . VAL A 1 356 ? -10.030 -20.372 -0.258  1.00 13.52 ? 355  VAL A C   1 
ATOM   2860 O  O   . VAL A 1 356 ? -10.313 -20.293 0.945   1.00 13.55 ? 355  VAL A O   1 
ATOM   2861 C  CB  . VAL A 1 356 ? -11.774 -18.814 -1.225  1.00 13.84 ? 355  VAL A CB  1 
ATOM   2862 C  CG1 . VAL A 1 356 ? -10.736 -17.696 -1.322  1.00 13.74 ? 355  VAL A CG1 1 
ATOM   2863 C  CG2 . VAL A 1 356 ? -12.850 -18.649 -2.295  1.00 14.21 ? 355  VAL A CG2 1 
ATOM   2864 N  N   . LEU A 1 357 ? -8.791  -20.621 -0.688  1.00 12.50 ? 356  LEU A N   1 
ATOM   2865 C  CA  . LEU A 1 357 ? -7.678  -20.880 0.234   1.00 12.09 ? 356  LEU A CA  1 
ATOM   2866 C  C   . LEU A 1 357 ? -6.963  -19.556 0.479   1.00 13.20 ? 356  LEU A C   1 
ATOM   2867 O  O   . LEU A 1 357 ? -6.045  -19.177 -0.251  1.00 14.68 ? 356  LEU A O   1 
ATOM   2868 C  CB  . LEU A 1 357 ? -6.753  -21.949 -0.344  1.00 15.18 ? 356  LEU A CB  1 
ATOM   2869 C  CG  . LEU A 1 357 ? -5.644  -22.545 0.533   1.00 15.72 ? 356  LEU A CG  1 
ATOM   2870 C  CD1 . LEU A 1 357 ? -6.235  -23.222 1.780   1.00 16.16 ? 356  LEU A CD1 1 
ATOM   2871 C  CD2 . LEU A 1 357 ? -4.781  -23.535 -0.260  1.00 16.04 ? 356  LEU A CD2 1 
ATOM   2872 N  N   . ILE A 1 358 ? -7.387  -18.842 1.529   1.00 13.71 ? 357  ILE A N   1 
ATOM   2873 C  CA  . ILE A 1 358 ? -7.005  -17.431 1.672   1.00 12.15 ? 357  ILE A CA  1 
ATOM   2874 C  C   . ILE A 1 358 ? -5.503  -17.242 1.840   1.00 12.64 ? 357  ILE A C   1 
ATOM   2875 O  O   . ILE A 1 358 ? -4.945  -16.318 1.225   1.00 13.90 ? 357  ILE A O   1 
ATOM   2876 C  CB  . ILE A 1 358 ? -7.812  -16.770 2.795   1.00 11.25 ? 357  ILE A CB  1 
ATOM   2877 C  CG1 . ILE A 1 358 ? -9.311  -17.075 2.684   1.00 11.15 ? 357  ILE A CG1 1 
ATOM   2878 C  CG2 . ILE A 1 358 ? -7.613  -15.261 2.756   1.00 13.78 ? 357  ILE A CG2 1 
ATOM   2879 C  CD1 . ILE A 1 358 ? -10.144 -16.443 3.842   1.00 12.48 ? 357  ILE A CD1 1 
ATOM   2880 N  N   . PRO A 1 359 ? -4.792  -18.015 2.665   1.00 13.22 ? 358  PRO A N   1 
ATOM   2881 C  CA  . PRO A 1 359 ? -3.353  -17.748 2.802   1.00 12.93 ? 358  PRO A CA  1 
ATOM   2882 C  C   . PRO A 1 359 ? -2.610  -17.891 1.484   1.00 12.67 ? 358  PRO A C   1 
ATOM   2883 O  O   . PRO A 1 359 ? -1.609  -17.197 1.261   1.00 13.26 ? 358  PRO A O   1 
ATOM   2884 C  CB  . PRO A 1 359 ? -2.888  -18.778 3.847   1.00 12.91 ? 358  PRO A CB  1 
ATOM   2885 C  CG  . PRO A 1 359 ? -4.176  -19.222 4.563   1.00 12.20 ? 358  PRO A CG  1 
ATOM   2886 C  CD  . PRO A 1 359 ? -5.231  -19.160 3.487   1.00 13.63 ? 358  PRO A CD  1 
ATOM   2887 N  N   . GLN A 1 360 ? -3.087  -18.758 0.590   1.00 13.37 ? 359  GLN A N   1 
ATOM   2888 C  CA  . GLN A 1 360 ? -2.418  -18.918 -0.697  1.00 14.66 ? 359  GLN A CA  1 
ATOM   2889 C  C   . GLN A 1 360 ? -2.794  -17.794 -1.660  1.00 16.18 ? 359  GLN A C   1 
ATOM   2890 O  O   . GLN A 1 360 ? -1.941  -17.310 -2.418  1.00 16.82 ? 359  GLN A O   1 
ATOM   2891 C  CB  . GLN A 1 360 ? -2.754  -20.285 -1.296  1.00 17.59 ? 359  GLN A CB  1 
ATOM   2892 C  CG  . GLN A 1 360 ? -1.753  -20.750 -2.326  1.00 21.82 ? 359  GLN A CG  1 
ATOM   2893 C  CD  . GLN A 1 360 ? -0.450  -21.229 -1.707  1.00 23.60 ? 359  GLN A CD  1 
ATOM   2894 O  OE1 . GLN A 1 360 ? -0.298  -21.270 -0.479  1.00 21.95 ? 359  GLN A OE1 1 
ATOM   2895 N  NE2 . GLN A 1 360 ? 0.499   -21.612 -2.563  1.00 24.65 ? 359  GLN A NE2 1 
ATOM   2896 N  N   . LEU A 1 361 ? -4.058  -17.359 -1.645  1.00 12.85 ? 360  LEU A N   1 
ATOM   2897 C  CA  . LEU A 1 361 ? -4.435  -16.162 -2.396  1.00 14.24 ? 360  LEU A CA  1 
ATOM   2898 C  C   . LEU A 1 361 ? -3.524  -14.993 -2.049  1.00 14.01 ? 360  LEU A C   1 
ATOM   2899 O  O   . LEU A 1 361 ? -3.074  -14.247 -2.929  1.00 15.15 ? 360  LEU A O   1 
ATOM   2900 C  CB  . LEU A 1 361 ? -5.893  -15.783 -2.105  1.00 12.93 ? 360  LEU A CB  1 
ATOM   2901 C  CG  . LEU A 1 361 ? -6.320  -14.362 -2.516  1.00 11.89 ? 360  LEU A CG  1 
ATOM   2902 C  CD1 . LEU A 1 361 ? -6.349  -14.185 -4.033  1.00 13.59 ? 360  LEU A CD1 1 
ATOM   2903 C  CD2 . LEU A 1 361 ? -7.680  -13.980 -1.893  1.00 13.92 ? 360  LEU A CD2 1 
ATOM   2904 N  N   . HIS A 1 362 ? -3.262  -14.809 -0.759  1.00 12.33 ? 361  HIS A N   1 
ATOM   2905 C  CA  . HIS A 1 362 ? -2.500  -13.670 -0.278  1.00 12.54 ? 361  HIS A CA  1 
ATOM   2906 C  C   . HIS A 1 362 ? -1.015  -13.791 -0.563  1.00 14.32 ? 361  HIS A C   1 
ATOM   2907 O  O   . HIS A 1 362 ? -0.257  -12.889 -0.192  1.00 15.03 ? 361  HIS A O   1 
ATOM   2908 C  CB  . HIS A 1 362 ? -2.742  -13.500 1.229   1.00 12.83 ? 361  HIS A CB  1 
ATOM   2909 C  CG  . HIS A 1 362 ? -4.113  -13.006 1.575   1.00 12.24 ? 361  HIS A CG  1 
ATOM   2910 N  ND1 . HIS A 1 362 ? -4.571  -12.940 2.873   1.00 12.46 ? 361  HIS A ND1 1 
ATOM   2911 C  CD2 . HIS A 1 362 ? -5.114  -12.520 0.799   1.00 11.39 ? 361  HIS A CD2 1 
ATOM   2912 C  CE1 . HIS A 1 362 ? -5.799  -12.449 2.883   1.00 10.95 ? 361  HIS A CE1 1 
ATOM   2913 N  NE2 . HIS A 1 362 ? -6.152  -12.184 1.635   1.00 11.04 ? 361  HIS A NE2 1 
ATOM   2914 N  N   . ARG A 1 363 ? -0.583  -14.883 -1.196  1.00 14.01 ? 362  ARG A N   1 
ATOM   2915 C  CA  . ARG A 1 363 ? 0.797   -15.066 -1.623  1.00 13.78 ? 362  ARG A CA  1 
ATOM   2916 C  C   . ARG A 1 363 ? 0.922   -15.064 -3.143  1.00 15.43 ? 362  ARG A C   1 
ATOM   2917 O  O   . ARG A 1 363 ? 1.957   -15.470 -3.682  1.00 16.74 ? 362  ARG A O   1 
ATOM   2918 C  CB  . ARG A 1 363 ? 1.369   -16.351 -1.012  1.00 14.12 ? 362  ARG A CB  1 
ATOM   2919 C  CG  . ARG A 1 363 ? 1.595   -16.260 0.504   1.00 15.92 ? 362  ARG A CG  1 
ATOM   2920 C  CD  . ARG A 1 363 ? 1.916   -17.622 1.134   1.00 17.22 ? 362  ARG A CD  1 
ATOM   2921 N  NE  . ARG A 1 363 ? 2.396   -17.497 2.511   1.00 16.71 ? 362  ARG A NE  1 
ATOM   2922 C  CZ  . ARG A 1 363 ? 1.641   -17.112 3.535   1.00 15.52 ? 362  ARG A CZ  1 
ATOM   2923 N  NH1 . ARG A 1 363 ? 0.350   -16.846 3.386   1.00 15.75 ? 362  ARG A NH1 1 
ATOM   2924 N  NH2 . ARG A 1 363 ? 2.195   -16.985 4.738   1.00 16.73 ? 362  ARG A NH2 1 
ATOM   2925 N  N   . ASP A 1 364 ? -0.113  -14.594 -3.843  1.00 15.50 ? 363  ASP A N   1 
ATOM   2926 C  CA  . ASP A 1 364 ? -0.106  -14.552 -5.305  1.00 17.10 ? 363  ASP A CA  1 
ATOM   2927 C  C   . ASP A 1 364 ? 0.933   -13.543 -5.770  1.00 18.03 ? 363  ASP A C   1 
ATOM   2928 O  O   . ASP A 1 364 ? 0.745   -12.335 -5.602  1.00 17.48 ? 363  ASP A O   1 
ATOM   2929 C  CB  . ASP A 1 364 ? -1.499  -14.187 -5.810  1.00 16.52 ? 363  ASP A CB  1 
ATOM   2930 C  CG  . ASP A 1 364 ? -1.642  -14.298 -7.318  1.00 17.03 ? 363  ASP A CG  1 
ATOM   2931 O  OD1 . ASP A 1 364 ? -0.625  -14.223 -8.052  1.00 17.90 ? 363  ASP A OD1 1 
ATOM   2932 O  OD2 . ASP A 1 364 ? -2.800  -14.437 -7.774  1.00 17.59 ? 363  ASP A OD2 1 
ATOM   2933 N  N   . LYS A 1 365 ? 2.033   -14.031 -6.356  1.00 20.29 ? 364  LYS A N   1 
ATOM   2934 C  CA  . LYS A 1 365 ? 3.119   -13.135 -6.739  1.00 21.71 ? 364  LYS A CA  1 
ATOM   2935 C  C   . LYS A 1 365 ? 2.732   -12.173 -7.859  1.00 21.59 ? 364  LYS A C   1 
ATOM   2936 O  O   . LYS A 1 365 ? 3.352   -11.109 -7.978  1.00 22.05 ? 364  LYS A O   1 
ATOM   2937 C  CB  . LYS A 1 365 ? 4.352   -13.943 -7.145  1.00 23.47 ? 364  LYS A CB  1 
ATOM   2938 C  CG  . LYS A 1 365 ? 5.068   -14.563 -5.969  1.00 26.08 ? 364  LYS A CG  1 
ATOM   2939 C  CD  . LYS A 1 365 ? 6.305   -15.335 -6.426  1.00 30.31 ? 364  LYS A CD  1 
ATOM   2940 C  CE  . LYS A 1 365 ? 6.902   -16.152 -5.293  1.00 35.84 ? 364  LYS A CE  1 
ATOM   2941 N  NZ  . LYS A 1 365 ? 7.982   -17.048 -5.795  1.00 38.69 ? 364  LYS A NZ  1 
ATOM   2942 N  N   . THR A 1 366 ? 1.735   -12.511 -8.683  1.00 17.63 ? 365  THR A N   1 
ATOM   2943 C  CA  . THR A 1 366 ? 1.330   -11.574 -9.724  1.00 18.21 ? 365  THR A CA  1 
ATOM   2944 C  C   . THR A 1 366 ? 0.682   -10.327 -9.142  1.00 20.11 ? 365  THR A C   1 
ATOM   2945 O  O   . THR A 1 366 ? 0.661   -9.286  -9.811  1.00 19.48 ? 365  THR A O   1 
ATOM   2946 C  CB  . THR A 1 366 ? 0.383   -12.243 -10.733 1.00 20.59 ? 365  THR A CB  1 
ATOM   2947 O  OG1 . THR A 1 366 ? -0.891  -12.506 -10.128 1.00 21.85 ? 365  THR A OG1 1 
ATOM   2948 C  CG2 . THR A 1 366 ? 0.991   -13.551 -11.256 1.00 21.81 ? 365  THR A CG2 1 
ATOM   2949 N  N   . ILE A 1 367 ? 0.190   -10.404 -7.904  1.00 18.60 ? 366  ILE A N   1 
ATOM   2950 C  CA  . ILE A 1 367 ? -0.429  -9.267  -7.228  1.00 18.51 ? 366  ILE A CA  1 
ATOM   2951 C  C   . ILE A 1 367 ? 0.586   -8.505  -6.388  1.00 19.02 ? 366  ILE A C   1 
ATOM   2952 O  O   . ILE A 1 367 ? 0.739   -7.287  -6.521  1.00 20.73 ? 366  ILE A O   1 
ATOM   2953 C  CB  . ILE A 1 367 ? -1.606  -9.748  -6.352  1.00 17.88 ? 366  ILE A CB  1 
ATOM   2954 C  CG1 . ILE A 1 367 ? -2.685  -10.426 -7.198  1.00 18.80 ? 366  ILE A CG1 1 
ATOM   2955 C  CG2 . ILE A 1 367 ? -2.186  -8.576  -5.571  1.00 19.40 ? 366  ILE A CG2 1 
ATOM   2956 C  CD1 . ILE A 1 367 ? -3.384  -9.486  -8.175  1.00 19.89 ? 366  ILE A CD1 1 
ATOM   2957 N  N   . TRP A 1 368 ? 1.306   -9.210  -5.516  1.00 16.62 ? 367  TRP A N   1 
ATOM   2958 C  CA  . TRP A 1 368 ? 2.105   -8.558  -4.486  1.00 20.39 ? 367  TRP A CA  1 
ATOM   2959 C  C   . TRP A 1 368 ? 3.576   -8.405  -4.843  1.00 24.72 ? 367  TRP A C   1 
ATOM   2960 O  O   . TRP A 1 368 ? 4.282   -7.654  -4.162  1.00 28.86 ? 367  TRP A O   1 
ATOM   2961 C  CB  . TRP A 1 368 ? 1.966   -9.327  -3.168  1.00 18.55 ? 367  TRP A CB  1 
ATOM   2962 C  CG  . TRP A 1 368 ? 0.522   -9.527  -2.782  1.00 16.78 ? 367  TRP A CG  1 
ATOM   2963 C  CD1 . TRP A 1 368 ? -0.231  -10.652 -2.974  1.00 17.36 ? 367  TRP A CD1 1 
ATOM   2964 C  CD2 . TRP A 1 368 ? -0.346  -8.565  -2.166  1.00 18.51 ? 367  TRP A CD2 1 
ATOM   2965 N  NE1 . TRP A 1 368 ? -1.507  -10.455 -2.505  1.00 17.38 ? 367  TRP A NE1 1 
ATOM   2966 C  CE2 . TRP A 1 368 ? -1.604  -9.182  -2.005  1.00 16.91 ? 367  TRP A CE2 1 
ATOM   2967 C  CE3 . TRP A 1 368 ? -0.179  -7.243  -1.732  1.00 18.00 ? 367  TRP A CE3 1 
ATOM   2968 C  CZ2 . TRP A 1 368 ? -2.692  -8.526  -1.426  1.00 17.58 ? 367  TRP A CZ2 1 
ATOM   2969 C  CZ3 . TRP A 1 368 ? -1.263  -6.591  -1.155  1.00 19.08 ? 367  TRP A CZ3 1 
ATOM   2970 C  CH2 . TRP A 1 368 ? -2.504  -7.238  -1.007  1.00 18.18 ? 367  TRP A CH2 1 
ATOM   2971 N  N   . GLY A 1 369 ? 4.056   -9.076  -5.884  1.00 24.12 ? 368  GLY A N   1 
ATOM   2972 C  CA  . GLY A 1 369 ? 5.453   -8.969  -6.246  1.00 26.32 ? 368  GLY A CA  1 
ATOM   2973 C  C   . GLY A 1 369 ? 6.291   -10.078 -5.644  1.00 30.95 ? 368  GLY A C   1 
ATOM   2974 O  O   . GLY A 1 369 ? 5.814   -10.966 -4.928  1.00 32.56 ? 368  GLY A O   1 
ATOM   2975 N  N   . ASP A 1 370 ? 7.588   -10.017 -5.948  1.00 33.86 ? 369  ASP A N   1 
ATOM   2976 C  CA  . ASP A 1 370 ? 8.487   -11.076 -5.503  1.00 38.72 ? 369  ASP A CA  1 
ATOM   2977 C  C   . ASP A 1 370 ? 8.696   -11.059 -3.991  1.00 38.64 ? 369  ASP A C   1 
ATOM   2978 O  O   . ASP A 1 370 ? 9.010   -12.100 -3.406  1.00 41.71 ? 369  ASP A O   1 
ATOM   2979 C  CB  . ASP A 1 370 ? 9.823   -10.969 -6.241  1.00 42.59 ? 369  ASP A CB  1 
ATOM   2980 C  CG  . ASP A 1 370 ? 9.708   -11.368 -7.702  1.00 50.43 ? 369  ASP A CG  1 
ATOM   2981 O  OD1 . ASP A 1 370 ? 8.831   -12.204 -8.023  1.00 52.48 ? 369  ASP A OD1 1 
ATOM   2982 O  OD2 . ASP A 1 370 ? 10.492  -10.852 -8.531  1.00 53.22 ? 369  ASP A OD2 1 
ATOM   2983 N  N   . ASP A 1 371 ? 8.512   -9.910  -3.337  1.00 35.52 ? 370  ASP A N   1 
ATOM   2984 C  CA  . ASP A 1 371 ? 8.762   -9.813  -1.899  1.00 34.88 ? 370  ASP A CA  1 
ATOM   2985 C  C   . ASP A 1 371 ? 7.561   -10.267 -1.073  1.00 31.54 ? 370  ASP A C   1 
ATOM   2986 O  O   . ASP A 1 371 ? 7.345   -9.773  0.039   1.00 31.37 ? 370  ASP A O   1 
ATOM   2987 C  CB  . ASP A 1 371 ? 9.149   -8.377  -1.515  1.00 35.46 ? 370  ASP A CB  1 
ATOM   2988 C  CG  . ASP A 1 371 ? 7.985   -7.399  -1.613  1.00 39.38 ? 370  ASP A CG  1 
ATOM   2989 O  OD1 . ASP A 1 371 ? 6.911   -7.781  -2.118  1.00 39.19 ? 370  ASP A OD1 1 
ATOM   2990 O  OD2 . ASP A 1 371 ? 8.147   -6.238  -1.175  1.00 42.51 ? 370  ASP A OD2 1 
ATOM   2991 N  N   . VAL A 1 372 ? 6.811   -11.245 -1.583  1.00 30.37 ? 371  VAL A N   1 
ATOM   2992 C  CA  . VAL A 1 372 ? 5.494   -11.559 -1.028  1.00 30.15 ? 371  VAL A CA  1 
ATOM   2993 C  C   . VAL A 1 372 ? 5.581   -12.130 0.389   1.00 25.52 ? 371  VAL A C   1 
ATOM   2994 O  O   . VAL A 1 372 ? 4.626   -12.011 1.174   1.00 24.08 ? 371  VAL A O   1 
ATOM   2995 C  CB  . VAL A 1 372 ? 4.757   -12.517 -1.980  1.00 32.15 ? 371  VAL A CB  1 
ATOM   2996 C  CG1 . VAL A 1 372 ? 5.467   -13.867 -2.026  1.00 32.91 ? 371  VAL A CG1 1 
ATOM   2997 C  CG2 . VAL A 1 372 ? 3.313   -12.668 -1.563  1.00 31.57 ? 371  VAL A CG2 1 
ATOM   2998 N  N   . GLU A 1 373 ? 6.698   -12.763 0.748   1.00 24.46 ? 372  GLU A N   1 
ATOM   2999 C  CA  . GLU A 1 373 ? 6.819   -13.300 2.098   1.00 25.55 ? 372  GLU A CA  1 
ATOM   3000 C  C   . GLU A 1 373 ? 7.289   -12.263 3.112   1.00 26.54 ? 372  GLU A C   1 
ATOM   3001 O  O   . GLU A 1 373 ? 7.242   -12.539 4.315   1.00 27.84 ? 372  GLU A O   1 
ATOM   3002 C  CB  . GLU A 1 373 ? 7.764   -14.508 2.113   1.00 26.81 ? 372  GLU A CB  1 
ATOM   3003 C  CG  . GLU A 1 373 ? 7.183   -15.759 1.447   1.00 29.83 ? 372  GLU A CG  1 
ATOM   3004 C  CD  . GLU A 1 373 ? 6.124   -16.463 2.297   1.00 32.26 ? 372  GLU A CD  1 
ATOM   3005 O  OE1 . GLU A 1 373 ? 6.206   -16.415 3.549   1.00 33.87 ? 372  GLU A OE1 1 
ATOM   3006 O  OE2 . GLU A 1 373 ? 5.209   -17.076 1.709   1.00 31.45 ? 372  GLU A OE2 1 
ATOM   3007 N  N   . GLU A 1 374 ? 7.717   -11.085 2.668   1.00 24.25 ? 373  GLU A N   1 
ATOM   3008 C  CA  . GLU A 1 374 ? 8.159   -10.038 3.581   1.00 24.17 ? 373  GLU A CA  1 
ATOM   3009 C  C   . GLU A 1 374 ? 6.978   -9.356  4.266   1.00 21.66 ? 373  GLU A C   1 
ATOM   3010 O  O   . GLU A 1 374 ? 5.890   -9.222  3.699   1.00 22.61 ? 373  GLU A O   1 
ATOM   3011 C  CB  . GLU A 1 374 ? 8.980   -8.984  2.840   1.00 27.42 ? 373  GLU A CB  1 
ATOM   3012 C  CG  . GLU A 1 374 ? 10.306  -9.487  2.313   1.00 35.21 ? 373  GLU A CG  1 
ATOM   3013 C  CD  . GLU A 1 374 ? 11.149  -8.365  1.731   1.00 44.02 ? 373  GLU A CD  1 
ATOM   3014 O  OE1 . GLU A 1 374 ? 11.087  -7.236  2.264   1.00 47.28 ? 373  GLU A OE1 1 
ATOM   3015 O  OE2 . GLU A 1 374 ? 11.863  -8.607  0.735   1.00 47.56 ? 373  GLU A OE2 1 
ATOM   3016 N  N   . PHE A 1 375 ? 7.216   -8.895  5.493   1.00 20.75 ? 374  PHE A N   1 
ATOM   3017 C  CA  . PHE A 1 375 ? 6.220   -8.141  6.252   1.00 19.39 ? 374  PHE A CA  1 
ATOM   3018 C  C   . PHE A 1 375 ? 6.436   -6.657  5.972   1.00 20.94 ? 374  PHE A C   1 
ATOM   3019 O  O   . PHE A 1 375 ? 7.380   -6.047  6.486   1.00 23.19 ? 374  PHE A O   1 
ATOM   3020 C  CB  . PHE A 1 375 ? 6.330   -8.456  7.742   1.00 18.60 ? 374  PHE A CB  1 
ATOM   3021 C  CG  . PHE A 1 375 ? 5.188   -7.926  8.560   1.00 16.88 ? 374  PHE A CG  1 
ATOM   3022 C  CD1 . PHE A 1 375 ? 3.955   -8.576  8.555   1.00 15.05 ? 374  PHE A CD1 1 
ATOM   3023 C  CD2 . PHE A 1 375 ? 5.336   -6.786  9.334   1.00 18.57 ? 374  PHE A CD2 1 
ATOM   3024 C  CE1 . PHE A 1 375 ? 2.886   -8.096  9.312   1.00 15.73 ? 374  PHE A CE1 1 
ATOM   3025 C  CE2 . PHE A 1 375 ? 4.270   -6.298  10.089  1.00 19.74 ? 374  PHE A CE2 1 
ATOM   3026 C  CZ  . PHE A 1 375 ? 3.045   -6.960  10.075  1.00 19.18 ? 374  PHE A CZ  1 
ATOM   3027 N  N   . ARG A 1 376 ? 5.557   -6.068  5.156   1.00 19.82 ? 375  ARG A N   1 
ATOM   3028 C  CA  . ARG A 1 376 ? 5.694   -4.671  4.744   1.00 20.09 ? 375  ARG A CA  1 
ATOM   3029 C  C   . ARG A 1 376 ? 4.331   -3.992  4.777   1.00 18.57 ? 375  ARG A C   1 
ATOM   3030 O  O   . ARG A 1 376 ? 3.600   -3.983  3.779   1.00 19.75 ? 375  ARG A O   1 
ATOM   3031 C  CB  . ARG A 1 376 ? 6.318   -4.571  3.350   1.00 26.58 ? 375  ARG A CB  1 
ATOM   3032 C  CG  . ARG A 1 376 ? 6.613   -3.151  2.902   1.00 32.27 ? 375  ARG A CG  1 
ATOM   3033 C  CD  . ARG A 1 376 ? 7.585   -3.116  1.721   1.00 36.94 ? 375  ARG A CD  1 
ATOM   3034 N  NE  . ARG A 1 376 ? 7.061   -3.775  0.530   1.00 41.50 ? 375  ARG A NE  1 
ATOM   3035 C  CZ  . ARG A 1 376 ? 6.238   -3.205  -0.341  1.00 45.76 ? 375  ARG A CZ  1 
ATOM   3036 N  NH1 . ARG A 1 376 ? 5.783   -1.975  -0.157  1.00 46.99 ? 375  ARG A NH1 1 
ATOM   3037 N  NH2 . ARG A 1 376 ? 5.865   -3.884  -1.425  1.00 45.83 ? 375  ARG A NH2 1 
ATOM   3038 N  N   . PRO A 1 377 ? 3.958   -3.396  5.912   1.00 17.37 ? 376  PRO A N   1 
ATOM   3039 C  CA  . PRO A 1 377 ? 2.621   -2.787  6.014   1.00 17.73 ? 376  PRO A CA  1 
ATOM   3040 C  C   . PRO A 1 377 ? 2.357   -1.716  4.972   1.00 15.79 ? 376  PRO A C   1 
ATOM   3041 O  O   . PRO A 1 377 ? 1.189   -1.462  4.640   1.00 16.12 ? 376  PRO A O   1 
ATOM   3042 C  CB  . PRO A 1 377 ? 2.610   -2.201  7.435   1.00 18.45 ? 376  PRO A CB  1 
ATOM   3043 C  CG  . PRO A 1 377 ? 3.665   -2.972  8.184   1.00 17.81 ? 376  PRO A CG  1 
ATOM   3044 C  CD  . PRO A 1 377 ? 4.731   -3.267  7.159   1.00 17.80 ? 376  PRO A CD  1 
ATOM   3045 N  N   . GLU A 1 378 ? 3.407   -1.069  4.456   1.00 19.07 ? 377  GLU A N   1 
ATOM   3046 C  CA  . GLU A 1 378 ? 3.240   -0.023  3.455   1.00 20.91 ? 377  GLU A CA  1 
ATOM   3047 C  C   . GLU A 1 378 ? 2.556   -0.520  2.183   1.00 19.89 ? 377  GLU A C   1 
ATOM   3048 O  O   . GLU A 1 378 ? 2.136   0.312   1.368   1.00 20.90 ? 377  GLU A O   1 
ATOM   3049 C  CB  . GLU A 1 378 ? 4.607   0.591   3.118   1.00 23.10 ? 377  GLU A CB  1 
ATOM   3050 C  CG  . GLU A 1 378 ? 5.243   1.389   4.265   1.00 25.56 ? 377  GLU A CG  1 
ATOM   3051 C  CD  . GLU A 1 378 ? 5.936   0.517   5.325   1.00 26.61 ? 377  GLU A CD  1 
ATOM   3052 O  OE1 . GLU A 1 378 ? 6.101   -0.704  5.102   1.00 25.96 ? 377  GLU A OE1 1 
ATOM   3053 O  OE2 . GLU A 1 378 ? 6.322   1.062   6.386   1.00 27.21 ? 377  GLU A OE2 1 
ATOM   3054 N  N   . ARG A 1 379 ? 2.446   -1.842  1.992   1.00 18.82 ? 378  ARG A N   1 
ATOM   3055 C  CA  . ARG A 1 379 ? 1.667   -2.384  0.877   1.00 21.02 ? 378  ARG A CA  1 
ATOM   3056 C  C   . ARG A 1 379 ? 0.253   -1.847  0.857   1.00 18.90 ? 378  ARG A C   1 
ATOM   3057 O  O   . ARG A 1 379 ? -0.396  -1.842  -0.197  1.00 19.99 ? 378  ARG A O   1 
ATOM   3058 C  CB  . ARG A 1 379 ? 1.556   -3.909  0.959   1.00 22.62 ? 378  ARG A CB  1 
ATOM   3059 C  CG  . ARG A 1 379 ? 2.815   -4.688  0.755   1.00 26.70 ? 378  ARG A CG  1 
ATOM   3060 C  CD  . ARG A 1 379 ? 2.520   -6.147  1.022   1.00 24.92 ? 378  ARG A CD  1 
ATOM   3061 N  NE  . ARG A 1 379 ? 3.727   -6.883  1.363   1.00 25.91 ? 378  ARG A NE  1 
ATOM   3062 C  CZ  . ARG A 1 379 ? 4.592   -7.351  0.476   1.00 27.34 ? 378  ARG A CZ  1 
ATOM   3063 N  NH1 . ARG A 1 379 ? 4.437   -7.136  -0.824  1.00 25.08 ? 378  ARG A NH1 1 
ATOM   3064 N  NH2 . ARG A 1 379 ? 5.639   -8.053  0.902   1.00 29.89 ? 378  ARG A NH2 1 
ATOM   3065 N  N   . PHE A 1 380 ? -0.277  -1.476  2.020   1.00 17.29 ? 379  PHE A N   1 
ATOM   3066 C  CA  . PHE A 1 380 ? -1.672  -1.085  2.143   1.00 16.98 ? 379  PHE A CA  1 
ATOM   3067 C  C   . PHE A 1 380 ? -1.857  0.428   2.144   1.00 17.88 ? 379  PHE A C   1 
ATOM   3068 O  O   . PHE A 1 380 ? -2.941  0.918   2.480   1.00 19.87 ? 379  PHE A O   1 
ATOM   3069 C  CB  . PHE A 1 380 ? -2.274  -1.729  3.397   1.00 16.84 ? 379  PHE A CB  1 
ATOM   3070 C  CG  . PHE A 1 380 ? -2.468  -3.220  3.260   1.00 18.81 ? 379  PHE A CG  1 
ATOM   3071 C  CD1 . PHE A 1 380 ? -3.624  -3.731  2.678   1.00 17.23 ? 379  PHE A CD1 1 
ATOM   3072 C  CD2 . PHE A 1 380 ? -1.481  -4.111  3.670   1.00 19.03 ? 379  PHE A CD2 1 
ATOM   3073 C  CE1 . PHE A 1 380 ? -3.803  -5.106  2.534   1.00 18.70 ? 379  PHE A CE1 1 
ATOM   3074 C  CE2 . PHE A 1 380 ? -1.649  -5.485  3.516   1.00 17.20 ? 379  PHE A CE2 1 
ATOM   3075 C  CZ  . PHE A 1 380 ? -2.810  -5.983  2.952   1.00 18.80 ? 379  PHE A CZ  1 
ATOM   3076 N  N   . GLU A 1 381 ? -0.837  1.178   1.726   1.00 16.62 ? 380  GLU A N   1 
ATOM   3077 C  CA  . GLU A 1 381 ? -0.950  2.631   1.760   1.00 19.92 ? 380  GLU A CA  1 
ATOM   3078 C  C   . GLU A 1 381 ? -2.062  3.140   0.854   1.00 18.40 ? 380  GLU A C   1 
ATOM   3079 O  O   . GLU A 1 381 ? -2.700  4.148   1.173   1.00 20.69 ? 380  GLU A O   1 
ATOM   3080 C  CB  . GLU A 1 381 ? 0.382   3.272   1.390   1.00 23.31 ? 380  GLU A CB  1 
ATOM   3081 C  CG  . GLU A 1 381 ? 1.186   3.644   2.630   1.00 33.24 ? 380  GLU A CG  1 
ATOM   3082 C  CD  . GLU A 1 381 ? 2.638   3.930   2.333   1.00 39.84 ? 380  GLU A CD  1 
ATOM   3083 O  OE1 . GLU A 1 381 ? 2.983   4.076   1.142   1.00 44.86 ? 380  GLU A OE1 1 
ATOM   3084 O  OE2 . GLU A 1 381 ? 3.429   3.996   3.297   1.00 37.87 ? 380  GLU A OE2 1 
ATOM   3085 N  N   . ASN A 1 382 ? -2.319  2.466   -0.264  1.00 18.23 ? 381  ASN A N   1 
ATOM   3086 C  CA  . ASN A 1 382 ? -3.299  2.931   -1.242  1.00 17.51 ? 381  ASN A CA  1 
ATOM   3087 C  C   . ASN A 1 382 ? -4.191  1.784   -1.696  1.00 16.92 ? 381  ASN A C   1 
ATOM   3088 O  O   . ASN A 1 382 ? -3.819  1.030   -2.613  1.00 14.94 ? 381  ASN A O   1 
ATOM   3089 C  CB  . ASN A 1 382 ? -2.617  3.566   -2.445  1.00 17.63 ? 381  ASN A CB  1 
ATOM   3090 C  CG  . ASN A 1 382 ? -3.618  4.164   -3.417  1.00 19.33 ? 381  ASN A CG  1 
ATOM   3091 O  OD1 . ASN A 1 382 ? -4.825  4.172   -3.148  1.00 18.90 ? 381  ASN A OD1 1 
ATOM   3092 N  ND2 . ASN A 1 382 ? -3.130  4.661   -4.549  1.00 21.00 ? 381  ASN A ND2 1 
ATOM   3093 N  N   . PRO A 1 383 ? -5.376  1.628   -1.097  1.00 16.81 ? 382  PRO A N   1 
ATOM   3094 C  CA  . PRO A 1 383 ? -6.281  0.551   -1.530  1.00 16.63 ? 382  PRO A CA  1 
ATOM   3095 C  C   . PRO A 1 383 ? -6.639  0.603   -3.005  1.00 15.61 ? 382  PRO A C   1 
ATOM   3096 O  O   . PRO A 1 383 ? -6.978  -0.443  -3.574  1.00 15.02 ? 382  PRO A O   1 
ATOM   3097 C  CB  . PRO A 1 383 ? -7.517  0.753   -0.642  1.00 19.04 ? 382  PRO A CB  1 
ATOM   3098 C  CG  . PRO A 1 383 ? -6.960  1.424   0.614   1.00 18.59 ? 382  PRO A CG  1 
ATOM   3099 C  CD  . PRO A 1 383 ? -5.872  2.339   0.098   1.00 15.98 ? 382  PRO A CD  1 
ATOM   3100 N  N   . SER A 1 384 ? -6.566  1.772   -3.651  1.00 14.08 ? 383  SER A N   1 
ATOM   3101 C  CA  . SER A 1 384 ? -6.886  1.837   -5.074  1.00 14.66 ? 383  SER A CA  1 
ATOM   3102 C  C   . SER A 1 384 ? -5.816  1.188   -5.944  1.00 15.46 ? 383  SER A C   1 
ATOM   3103 O  O   . SER A 1 384 ? -6.063  0.943   -7.131  1.00 16.77 ? 383  SER A O   1 
ATOM   3104 C  CB  . SER A 1 384 ? -7.093  3.296   -5.512  1.00 14.83 ? 383  SER A CB  1 
ATOM   3105 O  OG  . SER A 1 384 ? -8.128  3.940   -4.760  1.00 17.73 ? 383  SER A OG  1 
ATOM   3106 N  N   . ALA A 1 385 ? -4.633  0.930   -5.398  1.00 14.67 ? 384  ALA A N   1 
ATOM   3107 C  CA  . ALA A 1 385 ? -3.562  0.272   -6.132  1.00 16.99 ? 384  ALA A CA  1 
ATOM   3108 C  C   . ALA A 1 385 ? -3.580  -1.245  -5.974  1.00 15.37 ? 384  ALA A C   1 
ATOM   3109 O  O   . ALA A 1 385 ? -2.722  -1.924  -6.551  1.00 19.16 ? 384  ALA A O   1 
ATOM   3110 C  CB  . ALA A 1 385 ? -2.203  0.824   -5.686  1.00 16.50 ? 384  ALA A CB  1 
ATOM   3111 N  N   . ILE A 1 386 ? -4.523  -1.790  -5.215  1.00 13.20 ? 385  ILE A N   1 
ATOM   3112 C  CA  . ILE A 1 386 ? -4.639  -3.230  -4.999  1.00 14.64 ? 385  ILE A CA  1 
ATOM   3113 C  C   . ILE A 1 386 ? -5.761  -3.745  -5.893  1.00 14.59 ? 385  ILE A C   1 
ATOM   3114 O  O   . ILE A 1 386 ? -6.895  -3.260  -5.776  1.00 15.05 ? 385  ILE A O   1 
ATOM   3115 C  CB  . ILE A 1 386 ? -4.925  -3.559  -3.527  1.00 16.82 ? 385  ILE A CB  1 
ATOM   3116 C  CG1 . ILE A 1 386 ? -3.832  -2.955  -2.632  1.00 19.99 ? 385  ILE A CG1 1 
ATOM   3117 C  CG2 . ILE A 1 386 ? -5.024  -5.076  -3.338  1.00 16.67 ? 385  ILE A CG2 1 
ATOM   3118 C  CD1 . ILE A 1 386 ? -4.080  -3.126  -1.126  1.00 22.45 ? 385  ILE A CD1 1 
ATOM   3119 N  N   . PRO A 1 387 ? -5.504  -4.720  -6.768  1.00 13.14 ? 386  PRO A N   1 
ATOM   3120 C  CA  . PRO A 1 387 ? -6.562  -5.225  -7.651  1.00 13.51 ? 386  PRO A CA  1 
ATOM   3121 C  C   . PRO A 1 387 ? -7.748  -5.781  -6.869  1.00 13.26 ? 386  PRO A C   1 
ATOM   3122 O  O   . PRO A 1 387 ? -7.643  -6.152  -5.696  1.00 14.68 ? 386  PRO A O   1 
ATOM   3123 C  CB  . PRO A 1 387 ? -5.855  -6.326  -8.454  1.00 13.89 ? 386  PRO A CB  1 
ATOM   3124 C  CG  . PRO A 1 387 ? -4.405  -5.917  -8.443  1.00 13.80 ? 386  PRO A CG  1 
ATOM   3125 C  CD  . PRO A 1 387 ? -4.194  -5.317  -7.072  1.00 15.03 ? 386  PRO A CD  1 
ATOM   3126 N  N   . GLN A 1 388 ? -8.898  -5.852  -7.544  1.00 12.26 ? 387  GLN A N   1 
ATOM   3127 C  CA  . GLN A 1 388 ? -10.107 -6.333  -6.877  1.00 10.07 ? 387  GLN A CA  1 
ATOM   3128 C  C   . GLN A 1 388 ? -9.918  -7.752  -6.354  1.00 11.25 ? 387  GLN A C   1 
ATOM   3129 O  O   . GLN A 1 388 ? -9.345  -8.610  -7.032  1.00 12.90 ? 387  GLN A O   1 
ATOM   3130 C  CB  . GLN A 1 388 ? -11.307 -6.295  -7.832  1.00 10.88 ? 387  GLN A CB  1 
ATOM   3131 C  CG  . GLN A 1 388 ? -11.789 -4.915  -8.208  1.00 13.84 ? 387  GLN A CG  1 
ATOM   3132 C  CD  . GLN A 1 388 ? -13.207 -4.950  -8.754  1.00 13.84 ? 387  GLN A CD  1 
ATOM   3133 O  OE1 . GLN A 1 388 ? -14.178 -4.976  -7.985  1.00 14.44 ? 387  GLN A OE1 1 
ATOM   3134 N  NE2 . GLN A 1 388 ? -13.339 -4.963  -10.090 1.00 13.07 ? 387  GLN A NE2 1 
ATOM   3135 N  N   . HIS A 1 389 ? -10.404 -7.991  -5.129  1.00 13.12 ? 388  HIS A N   1 
ATOM   3136 C  CA  . HIS A 1 389 ? -10.498 -9.320  -4.513  1.00 12.29 ? 388  HIS A CA  1 
ATOM   3137 C  C   . HIS A 1 389 ? -9.141  -9.982  -4.300  1.00 12.70 ? 388  HIS A C   1 
ATOM   3138 O  O   . HIS A 1 389 ? -9.052  -11.210 -4.159  1.00 14.18 ? 388  HIS A O   1 
ATOM   3139 C  CB  . HIS A 1 389 ? -11.430 -10.217 -5.326  1.00 13.57 ? 388  HIS A CB  1 
ATOM   3140 C  CG  . HIS A 1 389 ? -12.789 -9.627  -5.474  1.00 14.05 ? 388  HIS A CG  1 
ATOM   3141 N  ND1 . HIS A 1 389 ? -13.587 -9.353  -4.385  1.00 13.80 ? 388  HIS A ND1 1 
ATOM   3142 C  CD2 . HIS A 1 389 ? -13.469 -9.194  -6.561  1.00 16.57 ? 388  HIS A CD2 1 
ATOM   3143 C  CE1 . HIS A 1 389 ? -14.714 -8.803  -4.797  1.00 16.86 ? 388  HIS A CE1 1 
ATOM   3144 N  NE2 . HIS A 1 389 ? -14.670 -8.698  -6.113  1.00 16.73 ? 388  HIS A NE2 1 
ATOM   3145 N  N   . ALA A 1 390 ? -8.081  -9.182  -4.250  1.00 12.61 ? 389  ALA A N   1 
ATOM   3146 C  CA  . ALA A 1 390 ? -6.768  -9.695  -3.880  1.00 11.14 ? 389  ALA A CA  1 
ATOM   3147 C  C   . ALA A 1 390 ? -6.647  -10.003 -2.391  1.00 13.37 ? 389  ALA A C   1 
ATOM   3148 O  O   . ALA A 1 390 ? -5.786  -10.805 -2.005  1.00 14.05 ? 389  ALA A O   1 
ATOM   3149 C  CB  . ALA A 1 390 ? -5.697  -8.676  -4.262  1.00 12.64 ? 389  ALA A CB  1 
ATOM   3150 N  N   . PHE A 1 391 ? -7.478  -9.382  -1.551  1.00 11.17 ? 390  PHE A N   1 
ATOM   3151 C  CA  . PHE A 1 391 ? -7.274  -9.373  -0.096  1.00 13.03 ? 390  PHE A CA  1 
ATOM   3152 C  C   . PHE A 1 391 ? -8.630  -9.654  0.548   1.00 10.67 ? 390  PHE A C   1 
ATOM   3153 O  O   . PHE A 1 391 ? -9.500  -8.774  0.566   1.00 12.77 ? 390  PHE A O   1 
ATOM   3154 C  CB  . PHE A 1 391 ? -6.691  -8.027  0.338   1.00 11.84 ? 390  PHE A CB  1 
ATOM   3155 C  CG  . PHE A 1 391 ? -6.459  -7.878  1.835   1.00 10.01 ? 390  PHE A CG  1 
ATOM   3156 C  CD1 . PHE A 1 391 ? -5.500  -8.644  2.496   1.00 10.90 ? 390  PHE A CD1 1 
ATOM   3157 C  CD2 . PHE A 1 391 ? -7.159  -6.922  2.562   1.00 11.89 ? 390  PHE A CD2 1 
ATOM   3158 C  CE1 . PHE A 1 391 ? -5.279  -8.472  3.868   1.00 12.60 ? 390  PHE A CE1 1 
ATOM   3159 C  CE2 . PHE A 1 391 ? -6.944  -6.738  3.925   1.00 12.92 ? 390  PHE A CE2 1 
ATOM   3160 C  CZ  . PHE A 1 391 ? -6.003  -7.507  4.579   1.00 13.14 ? 390  PHE A CZ  1 
ATOM   3161 N  N   . LYS A 1 392 ? -8.815  -10.890 1.066   1.00 11.05 ? 391  LYS A N   1 
ATOM   3162 C  CA  . LYS A 1 392 ? -10.138 -11.337 1.497   1.00 11.31 ? 391  LYS A CA  1 
ATOM   3163 C  C   . LYS A 1 392 ? -10.134 -11.946 2.898   1.00 11.93 ? 391  LYS A C   1 
ATOM   3164 O  O   . LYS A 1 392 ? -10.766 -12.987 3.096   1.00 10.76 ? 391  LYS A O   1 
ATOM   3165 C  CB  . LYS A 1 392 ? -10.697 -12.382 0.512   1.00 12.29 ? 391  LYS A CB  1 
ATOM   3166 C  CG  . LYS A 1 392 ? -10.630 -11.990 -0.977  1.00 13.11 ? 391  LYS A CG  1 
ATOM   3167 C  CD  . LYS A 1 392 ? -11.537 -10.793 -1.317  1.00 15.12 ? 391  LYS A CD  1 
ATOM   3168 C  CE  . LYS A 1 392 ? -13.009 -11.067 -0.996  1.00 14.60 ? 391  LYS A CE  1 
ATOM   3169 N  NZ  . LYS A 1 392 ? -13.932 -10.014 -1.547  1.00 15.33 ? 391  LYS A NZ  1 
ATOM   3170 N  N   . PRO A 1 393 ? -9.468  -11.348 3.894   1.00 10.80 ? 392  PRO A N   1 
ATOM   3171 C  CA  . PRO A 1 393 ? -9.440  -11.982 5.226   1.00 10.74 ? 392  PRO A CA  1 
ATOM   3172 C  C   . PRO A 1 393 ? -10.777 -11.955 5.943   1.00 11.40 ? 392  PRO A C   1 
ATOM   3173 O  O   . PRO A 1 393 ? -10.934 -12.662 6.952   1.00 12.12 ? 392  PRO A O   1 
ATOM   3174 C  CB  . PRO A 1 393 ? -8.390  -11.162 5.985   1.00 10.98 ? 392  PRO A CB  1 
ATOM   3175 C  CG  . PRO A 1 393 ? -8.477  -9.792  5.350   1.00 10.30 ? 392  PRO A CG  1 
ATOM   3176 C  CD  . PRO A 1 393 ? -8.723  -10.073 3.878   1.00 11.10 ? 392  PRO A CD  1 
ATOM   3177 N  N   A HIS A 1 394 ? -11.740 -11.162 5.483   0.60 10.07 ? 393  HIS A N   1 
ATOM   3178 N  N   B HIS A 1 394 ? -11.736 -11.161 5.456   0.40 10.28 ? 393  HIS A N   1 
ATOM   3179 C  CA  A HIS A 1 394 ? -13.055 -11.124 6.111   0.60 10.89 ? 393  HIS A CA  1 
ATOM   3180 C  CA  B HIS A 1 394 ? -13.058 -11.024 6.058   0.40 10.28 ? 393  HIS A CA  1 
ATOM   3181 C  C   A HIS A 1 394 ? -14.145 -11.607 5.159   0.60 10.75 ? 393  HIS A C   1 
ATOM   3182 C  C   B HIS A 1 394 ? -14.150 -11.731 5.257   0.40 10.26 ? 393  HIS A C   1 
ATOM   3183 O  O   A HIS A 1 394 ? -15.300 -11.191 5.262   0.60 12.27 ? 393  HIS A O   1 
ATOM   3184 O  O   B HIS A 1 394 ? -15.334 -11.567 5.565   0.40 10.16 ? 393  HIS A O   1 
ATOM   3185 C  CB  A HIS A 1 394 ? -13.357 -9.725  6.646   0.60 12.93 ? 393  HIS A CB  1 
ATOM   3186 C  CB  B HIS A 1 394 ? -13.423 -9.542  6.214   0.40 10.58 ? 393  HIS A CB  1 
ATOM   3187 C  CG  A HIS A 1 394 ? -12.610 -9.398  7.905   0.60 14.74 ? 393  HIS A CG  1 
ATOM   3188 C  CG  B HIS A 1 394 ? -12.301 -8.678  6.704   0.40 13.97 ? 393  HIS A CG  1 
ATOM   3189 N  ND1 A HIS A 1 394 ? -11.491 -8.594  7.921   0.60 14.02 ? 393  HIS A ND1 1 
ATOM   3190 N  ND1 B HIS A 1 394 ? -11.858 -8.697  8.009   0.40 12.84 ? 393  HIS A ND1 1 
ATOM   3191 C  CD2 A HIS A 1 394 ? -12.799 -9.806  9.183   0.60 15.37 ? 393  HIS A CD2 1 
ATOM   3192 C  CD2 B HIS A 1 394 ? -11.544 -7.754  6.065   0.40 16.14 ? 393  HIS A CD2 1 
ATOM   3193 C  CE1 A HIS A 1 394 ? -11.039 -8.497  9.160   0.60 15.22 ? 393  HIS A CE1 1 
ATOM   3194 C  CE1 B HIS A 1 394 ? -10.874 -7.827  8.152   0.40 13.56 ? 393  HIS A CE1 1 
ATOM   3195 N  NE2 A HIS A 1 394 ? -11.814 -9.224  9.945   0.60 15.61 ? 393  HIS A NE2 1 
ATOM   3196 N  NE2 B HIS A 1 394 ? -10.662 -7.243  6.987   0.40 16.32 ? 393  HIS A NE2 1 
ATOM   3197 N  N   . GLY A 1 395 ? -13.789 -12.499 4.232   1.00 11.18 ? 394  GLY A N   1 
ATOM   3198 C  CA  . GLY A 1 395 ? -14.795 -13.105 3.372   1.00 10.78 ? 394  GLY A CA  1 
ATOM   3199 C  C   . GLY A 1 395 ? -15.261 -12.151 2.284   1.00 12.44 ? 394  GLY A C   1 
ATOM   3200 O  O   . GLY A 1 395 ? -14.555 -11.196 1.909   1.00 12.39 ? 394  GLY A O   1 
ATOM   3201 N  N   . ASN A 1 396 ? -16.484 -12.394 1.784   1.00 11.29 ? 395  ASN A N   1 
ATOM   3202 C  CA  . ASN A 1 396 ? -16.952 -11.724 0.576   1.00 11.56 ? 395  ASN A CA  1 
ATOM   3203 C  C   . ASN A 1 396 ? -18.416 -11.301 0.640   1.00 11.43 ? 395  ASN A C   1 
ATOM   3204 O  O   . ASN A 1 396 ? -19.276 -12.042 1.126   1.00 11.77 ? 395  ASN A O   1 
ATOM   3205 C  CB  . ASN A 1 396 ? -16.779 -12.621 -0.655  1.00 12.59 ? 395  ASN A CB  1 
ATOM   3206 C  CG  . ASN A 1 396 ? -17.100 -11.885 -1.945  1.00 13.52 ? 395  ASN A CG  1 
ATOM   3207 O  OD1 . ASN A 1 396 ? -16.425 -10.924 -2.292  1.00 13.91 ? 395  ASN A OD1 1 
ATOM   3208 N  ND2 . ASN A 1 396 ? -18.133 -12.329 -2.654  1.00 14.31 ? 395  ASN A ND2 1 
ATOM   3209 N  N   . GLY A 1 397 ? -18.694 -10.119 0.088   1.00 13.09 ? 396  GLY A N   1 
ATOM   3210 C  CA  . GLY A 1 397 ? -20.051 -9.729  -0.229  1.00 13.25 ? 396  GLY A CA  1 
ATOM   3211 C  C   . GLY A 1 397 ? -20.942 -9.560  0.989   1.00 13.22 ? 396  GLY A C   1 
ATOM   3212 O  O   . GLY A 1 397 ? -20.500 -9.195  2.084   1.00 12.78 ? 396  GLY A O   1 
ATOM   3213 N  N   . GLN A 1 398 ? -22.236 -9.820  0.782   1.00 11.96 ? 397  GLN A N   1 
ATOM   3214 C  CA  . GLN A 1 398 ? -23.202 -9.718  1.873   1.00 11.82 ? 397  GLN A CA  1 
ATOM   3215 C  C   . GLN A 1 398 ? -22.943 -10.753 2.961   1.00 11.98 ? 397  GLN A C   1 
ATOM   3216 O  O   . GLN A 1 398 ? -23.431 -10.580 4.084   1.00 12.50 ? 397  GLN A O   1 
ATOM   3217 C  CB  . GLN A 1 398 ? -24.637 -9.854  1.344   1.00 11.71 ? 397  GLN A CB  1 
ATOM   3218 C  CG  . GLN A 1 398 ? -25.022 -11.262 0.882   1.00 12.73 ? 397  GLN A CG  1 
ATOM   3219 C  CD  . GLN A 1 398 ? -26.429 -11.332 0.294   1.00 14.50 ? 397  GLN A CD  1 
ATOM   3220 O  OE1 . GLN A 1 398 ? -27.287 -10.502 0.604   1.00 17.06 ? 397  GLN A OE1 1 
ATOM   3221 N  NE2 . GLN A 1 398 ? -26.669 -12.321 -0.561  1.00 16.08 ? 397  GLN A NE2 1 
ATOM   3222 N  N   . ARG A 1 399 ? -22.185 -11.813 2.667   1.00 10.49 ? 398  ARG A N   1 
ATOM   3223 C  CA  . ARG A 1 399 ? -21.787 -12.790 3.679   1.00 12.06 ? 398  ARG A CA  1 
ATOM   3224 C  C   . ARG A 1 399 ? -20.390 -12.523 4.233   1.00 10.97 ? 398  ARG A C   1 
ATOM   3225 O  O   . ARG A 1 399 ? -19.781 -13.424 4.818   1.00 10.84 ? 398  ARG A O   1 
ATOM   3226 C  CB  . ARG A 1 399 ? -21.863 -14.222 3.131   1.00 11.31 ? 398  ARG A CB  1 
ATOM   3227 C  CG  . ARG A 1 399 ? -23.245 -14.659 2.643   1.00 8.90  ? 398  ARG A CG  1 
ATOM   3228 C  CD  . ARG A 1 399 ? -24.325 -14.486 3.724   1.00 9.97  ? 398  ARG A CD  1 
ATOM   3229 N  NE  . ARG A 1 399 ? -24.042 -15.211 4.965   1.00 10.38 ? 398  ARG A NE  1 
ATOM   3230 C  CZ  . ARG A 1 399 ? -24.420 -16.455 5.227   1.00 11.69 ? 398  ARG A CZ  1 
ATOM   3231 N  NH1 . ARG A 1 399 ? -25.057 -17.192 4.328   1.00 11.50 ? 398  ARG A NH1 1 
ATOM   3232 N  NH2 . ARG A 1 399 ? -24.144 -16.980 6.421   1.00 11.91 ? 398  ARG A NH2 1 
ATOM   3233 N  N   . ALA A 1 400 ? -19.871 -11.307 4.071   1.00 10.72 ? 399  ALA A N   1 
ATOM   3234 C  CA  . ALA A 1 400 ? -18.600 -10.958 4.688   1.00 10.52 ? 399  ALA A CA  1 
ATOM   3235 C  C   . ALA A 1 400 ? -18.774 -10.830 6.205   1.00 11.92 ? 399  ALA A C   1 
ATOM   3236 O  O   . ALA A 1 400 ? -19.893 -10.795 6.731   1.00 12.19 ? 399  ALA A O   1 
ATOM   3237 C  CB  . ALA A 1 400 ? -18.048 -9.660  4.096   1.00 11.74 ? 399  ALA A CB  1 
ATOM   3238 N  N   . CYS A 1 401 ? -17.644 -10.762 6.907   1.00 10.23 ? 400  CYS A N   1 
ATOM   3239 C  CA  . CYS A 1 401 ? -17.644 -10.717 8.367   1.00 10.14 ? 400  CYS A CA  1 
ATOM   3240 C  C   . CYS A 1 401 ? -18.408 -9.505  8.889   1.00 11.81 ? 400  CYS A C   1 
ATOM   3241 O  O   . CYS A 1 401 ? -18.052 -8.363  8.592   1.00 15.83 ? 400  CYS A O   1 
ATOM   3242 C  CB  . CYS A 1 401 ? -16.197 -10.687 8.866   1.00 12.06 ? 400  CYS A CB  1 
ATOM   3243 S  SG  . CYS A 1 401 ? -16.057 -10.531 10.656  1.00 13.24 ? 400  CYS A SG  1 
ATOM   3244 N  N   . ILE A 1 402 ? -19.450 -9.750  9.693   1.00 14.01 ? 401  ILE A N   1 
ATOM   3245 C  CA  . ILE A 1 402 ? -20.197 -8.638  10.278  1.00 11.42 ? 401  ILE A CA  1 
ATOM   3246 C  C   . ILE A 1 402 ? -19.400 -7.939  11.379  1.00 12.01 ? 401  ILE A C   1 
ATOM   3247 O  O   . ILE A 1 402 ? -19.666 -6.767  11.686  1.00 13.16 ? 401  ILE A O   1 
ATOM   3248 C  CB  . ILE A 1 402 ? -21.558 -9.122  10.823  1.00 11.52 ? 401  ILE A CB  1 
ATOM   3249 C  CG1 . ILE A 1 402 ? -22.511 -7.938  11.008  1.00 11.25 ? 401  ILE A CG1 1 
ATOM   3250 C  CG2 . ILE A 1 402 ? -21.376 -9.905  12.138  1.00 11.36 ? 401  ILE A CG2 1 
ATOM   3251 C  CD1 . ILE A 1 402 ? -23.926 -8.335  11.406  1.00 14.19 ? 401  ILE A CD1 1 
ATOM   3252 N  N   . GLY A 1 403 ? -18.415 -8.612  11.962  1.00 11.05 ? 402  GLY A N   1 
ATOM   3253 C  CA  . GLY A 1 403 ? -17.624 -8.075  13.057  1.00 13.12 ? 402  GLY A CA  1 
ATOM   3254 C  C   . GLY A 1 403 ? -16.325 -7.388  12.675  1.00 13.10 ? 402  GLY A C   1 
ATOM   3255 O  O   . GLY A 1 403 ? -15.542 -7.046  13.566  1.00 13.70 ? 402  GLY A O   1 
ATOM   3256 N  N   . GLN A 1 404 ? -16.083 -7.151  11.382  1.00 12.69 ? 403  GLN A N   1 
ATOM   3257 C  CA  . GLN A 1 404 ? -14.784 -6.654  10.924  1.00 12.38 ? 403  GLN A CA  1 
ATOM   3258 C  C   . GLN A 1 404 ? -14.378 -5.367  11.631  1.00 12.61 ? 403  GLN A C   1 
ATOM   3259 O  O   . GLN A 1 404 ? -13.215 -5.209  12.030  1.00 14.11 ? 403  GLN A O   1 
ATOM   3260 C  CB  . GLN A 1 404 ? -14.823 -6.440  9.405   1.00 16.72 ? 403  GLN A CB  1 
ATOM   3261 C  CG  . GLN A 1 404 ? -13.630 -5.665  8.844   1.00 22.26 ? 403  GLN A CG  1 
ATOM   3262 C  CD  . GLN A 1 404 ? -13.808 -5.280  7.383   1.00 27.36 ? 403  GLN A CD  1 
ATOM   3263 O  OE1 . GLN A 1 404 ? -14.636 -5.849  6.675   1.00 25.01 ? 403  GLN A OE1 1 
ATOM   3264 N  NE2 . GLN A 1 404 ? -13.024 -4.306  6.926   1.00 30.37 ? 403  GLN A NE2 1 
ATOM   3265 N  N   . GLN A 1 405 ? -15.312 -4.422  11.774  1.00 14.82 ? 404  GLN A N   1 
ATOM   3266 C  CA  . GLN A 1 405 ? -14.970 -3.151  12.412  1.00 17.31 ? 404  GLN A CA  1 
ATOM   3267 C  C   . GLN A 1 405 ? -14.712 -3.325  13.905  1.00 14.59 ? 404  GLN A C   1 
ATOM   3268 O  O   . GLN A 1 405 ? -13.845 -2.645  14.473  1.00 14.93 ? 404  GLN A O   1 
ATOM   3269 C  CB  . GLN A 1 405 ? -16.080 -2.126  12.175  1.00 21.41 ? 404  GLN A CB  1 
ATOM   3270 C  CG  . GLN A 1 405 ? -16.255 -1.734  10.711  1.00 29.99 ? 404  GLN A CG  1 
ATOM   3271 C  CD  . GLN A 1 405 ? -15.033 -1.032  10.150  1.00 40.46 ? 404  GLN A CD  1 
ATOM   3272 O  OE1 . GLN A 1 405 ? -14.271 -1.609  9.368   1.00 45.56 ? 404  GLN A OE1 1 
ATOM   3273 N  NE2 . GLN A 1 405 ? -14.840 0.222   10.544  1.00 43.68 ? 404  GLN A NE2 1 
ATOM   3274 N  N   . PHE A 1 406 ? -15.471 -4.212  14.558  1.00 14.05 ? 405  PHE A N   1 
ATOM   3275 C  CA  . PHE A 1 406 ? -15.245 -4.519  15.973  1.00 14.31 ? 405  PHE A CA  1 
ATOM   3276 C  C   . PHE A 1 406 ? -13.844 -5.082  16.178  1.00 13.26 ? 405  PHE A C   1 
ATOM   3277 O  O   . PHE A 1 406 ? -13.092 -4.619  17.045  1.00 14.80 ? 405  PHE A O   1 
ATOM   3278 C  CB  . PHE A 1 406 ? -16.315 -5.520  16.450  1.00 13.64 ? 405  PHE A CB  1 
ATOM   3279 C  CG  . PHE A 1 406 ? -16.336 -5.768  17.945  1.00 14.47 ? 405  PHE A CG  1 
ATOM   3280 C  CD1 . PHE A 1 406 ? -15.456 -6.678  18.538  1.00 12.24 ? 405  PHE A CD1 1 
ATOM   3281 C  CD2 . PHE A 1 406 ? -17.258 -5.117  18.751  1.00 15.63 ? 405  PHE A CD2 1 
ATOM   3282 C  CE1 . PHE A 1 406 ? -15.486 -6.917  19.913  1.00 14.48 ? 405  PHE A CE1 1 
ATOM   3283 C  CE2 . PHE A 1 406 ? -17.294 -5.339  20.131  1.00 16.60 ? 405  PHE A CE2 1 
ATOM   3284 C  CZ  . PHE A 1 406 ? -16.406 -6.245  20.713  1.00 15.92 ? 405  PHE A CZ  1 
ATOM   3285 N  N   . ALA A 1 407 ? -13.476 -6.088  15.379  1.00 12.15 ? 406  ALA A N   1 
ATOM   3286 C  CA  . ALA A 1 407 ? -12.162 -6.714  15.512  1.00 12.27 ? 406  ALA A CA  1 
ATOM   3287 C  C   . ALA A 1 407 ? -11.044 -5.707  15.271  1.00 12.62 ? 406  ALA A C   1 
ATOM   3288 O  O   . ALA A 1 407 ? -10.058 -5.661  16.018  1.00 13.69 ? 406  ALA A O   1 
ATOM   3289 C  CB  . ALA A 1 407 ? -12.042 -7.895  14.541  1.00 10.52 ? 406  ALA A CB  1 
ATOM   3290 N  N   . LEU A 1 408 ? -11.170 -4.892  14.224  1.00 11.91 ? 407  LEU A N   1 
ATOM   3291 C  CA  . LEU A 1 408 ? -10.074 -3.980  13.916  1.00 13.81 ? 407  LEU A CA  1 
ATOM   3292 C  C   . LEU A 1 408 ? -9.981  -2.844  14.930  1.00 13.98 ? 407  LEU A C   1 
ATOM   3293 O  O   . LEU A 1 408 ? -8.875  -2.371  15.232  1.00 13.39 ? 407  LEU A O   1 
ATOM   3294 C  CB  . LEU A 1 408 ? -10.224 -3.446  12.493  1.00 15.20 ? 407  LEU A CB  1 
ATOM   3295 C  CG  . LEU A 1 408 ? -9.994  -4.553  11.457  1.00 21.17 ? 407  LEU A CG  1 
ATOM   3296 C  CD1 . LEU A 1 408 ? -10.313 -4.083  10.043  1.00 23.87 ? 407  LEU A CD1 1 
ATOM   3297 C  CD2 . LEU A 1 408 ? -8.570  -5.091  11.538  1.00 25.99 ? 407  LEU A CD2 1 
ATOM   3298 N  N   . HIS A 1 409 ? -11.108 -2.392  15.482  1.00 15.99 ? 408  HIS A N   1 
ATOM   3299 C  CA  . HIS A 1 409 ? -11.014 -1.362  16.510  1.00 12.31 ? 408  HIS A CA  1 
ATOM   3300 C  C   . HIS A 1 409 ? -10.343 -1.922  17.759  1.00 12.90 ? 408  HIS A C   1 
ATOM   3301 O  O   . HIS A 1 409 ? -9.446  -1.289  18.332  1.00 14.22 ? 408  HIS A O   1 
ATOM   3302 C  CB  . HIS A 1 409 ? -12.399 -0.789  16.840  1.00 13.36 ? 408  HIS A CB  1 
ATOM   3303 C  CG  . HIS A 1 409 ? -12.352 0.459   17.675  1.00 18.06 ? 408  HIS A CG  1 
ATOM   3304 N  ND1 . HIS A 1 409 ? -12.137 1.707   17.132  1.00 17.76 ? 408  HIS A ND1 1 
ATOM   3305 C  CD2 . HIS A 1 409 ? -12.478 0.648   19.012  1.00 17.97 ? 408  HIS A CD2 1 
ATOM   3306 C  CE1 . HIS A 1 409 ? -12.142 2.613   18.096  1.00 18.00 ? 408  HIS A CE1 1 
ATOM   3307 N  NE2 . HIS A 1 409 ? -12.349 1.996   19.247  1.00 17.43 ? 408  HIS A NE2 1 
ATOM   3308 N  N   . GLU A 1 410 ? -10.755 -3.120  18.182  1.00 12.70 ? 409  GLU A N   1 
ATOM   3309 C  CA  . GLU A 1 410 ? -10.161 -3.738  19.366  1.00 13.75 ? 409  GLU A CA  1 
ATOM   3310 C  C   . GLU A 1 410 ? -8.668  -3.966  19.172  1.00 12.43 ? 409  GLU A C   1 
ATOM   3311 O  O   . GLU A 1 410 ? -7.853  -3.635  20.045  1.00 12.72 ? 409  GLU A O   1 
ATOM   3312 C  CB  . GLU A 1 410 ? -10.855 -5.064  19.678  1.00 14.37 ? 409  GLU A CB  1 
ATOM   3313 C  CG  . GLU A 1 410 ? -10.202 -5.811  20.840  1.00 12.79 ? 409  GLU A CG  1 
ATOM   3314 C  CD  . GLU A 1 410 ? -10.867 -7.147  21.159  1.00 17.64 ? 409  GLU A CD  1 
ATOM   3315 O  OE1 . GLU A 1 410 ? -11.723 -7.621  20.369  1.00 19.93 ? 409  GLU A OE1 1 
ATOM   3316 O  OE2 . GLU A 1 410 ? -10.527 -7.729  22.211  1.00 20.26 ? 409  GLU A OE2 1 
ATOM   3317 N  N   . ALA A 1 411 ? -8.295  -4.573  18.040  1.00 11.79 ? 410  ALA A N   1 
ATOM   3318 C  CA  . ALA A 1 411 ? -6.892  -4.892  17.799  1.00 12.08 ? 410  ALA A CA  1 
ATOM   3319 C  C   . ALA A 1 411 ? -6.046  -3.631  17.654  1.00 13.18 ? 410  ALA A C   1 
ATOM   3320 O  O   . ALA A 1 411 ? -4.906  -3.588  18.135  1.00 14.49 ? 410  ALA A O   1 
ATOM   3321 C  CB  . ALA A 1 411 ? -6.765  -5.791  16.566  1.00 13.99 ? 410  ALA A CB  1 
ATOM   3322 N  N   . THR A 1 412 ? -6.582  -2.586  17.012  1.00 13.00 ? 411  THR A N   1 
ATOM   3323 C  CA  . THR A 1 412 ? -5.812  -1.349  16.888  1.00 14.03 ? 411  THR A CA  1 
ATOM   3324 C  C   . THR A 1 412 ? -5.615  -0.690  18.250  1.00 13.27 ? 411  THR A C   1 
ATOM   3325 O  O   . THR A 1 412 ? -4.508  -0.236  18.579  1.00 13.98 ? 411  THR A O   1 
ATOM   3326 C  CB  . THR A 1 412 ? -6.497  -0.387  15.912  1.00 14.25 ? 411  THR A CB  1 
ATOM   3327 O  OG1 . THR A 1 412 ? -6.645  -1.025  14.639  1.00 14.05 ? 411  THR A OG1 1 
ATOM   3328 C  CG2 . THR A 1 412 ? -5.662  0.893   15.728  1.00 12.75 ? 411  THR A CG2 1 
ATOM   3329 N  N   . LEU A 1 413 ? -6.676  -0.642  19.058  1.00 13.92 ? 412  LEU A N   1 
ATOM   3330 C  CA  . LEU A 1 413 ? -6.569  -0.096  20.409  1.00 14.18 ? 412  LEU A CA  1 
ATOM   3331 C  C   . LEU A 1 413 ? -5.514  -0.835  21.226  1.00 14.55 ? 412  LEU A C   1 
ATOM   3332 O  O   . LEU A 1 413 ? -4.608  -0.219  21.809  1.00 15.96 ? 412  LEU A O   1 
ATOM   3333 C  CB  . LEU A 1 413 ? -7.930  -0.179  21.102  1.00 14.04 ? 412  LEU A CB  1 
ATOM   3334 C  CG  . LEU A 1 413 ? -7.901  0.038   22.623  1.00 17.71 ? 412  LEU A CG  1 
ATOM   3335 C  CD1 . LEU A 1 413 ? -7.486  1.467   22.943  1.00 20.23 ? 412  LEU A CD1 1 
ATOM   3336 C  CD2 . LEU A 1 413 ? -9.245  -0.308  23.270  1.00 16.97 ? 412  LEU A CD2 1 
ATOM   3337 N  N   . VAL A 1 414 ? -5.621  -2.164  21.279  1.00 15.53 ? 413  VAL A N   1 
ATOM   3338 C  CA  . VAL A 1 414 ? -4.761  -2.968  22.142  1.00 14.78 ? 413  VAL A CA  1 
ATOM   3339 C  C   . VAL A 1 414 ? -3.317  -2.929  21.657  1.00 14.35 ? 413  VAL A C   1 
ATOM   3340 O  O   . VAL A 1 414 ? -2.383  -2.751  22.453  1.00 14.96 ? 413  VAL A O   1 
ATOM   3341 C  CB  . VAL A 1 414 ? -5.307  -4.408  22.216  1.00 15.85 ? 413  VAL A CB  1 
ATOM   3342 C  CG1 . VAL A 1 414 ? -4.358  -5.303  22.970  1.00 20.13 ? 413  VAL A CG1 1 
ATOM   3343 C  CG2 . VAL A 1 414 ? -6.684  -4.414  22.875  1.00 18.67 ? 413  VAL A CG2 1 
ATOM   3344 N  N   . LEU A 1 415 ? -3.100  -3.077  20.347  1.00 15.21 ? 414  LEU A N   1 
ATOM   3345 C  CA  . LEU A 1 415 ? -1.727  -3.038  19.851  1.00 16.03 ? 414  LEU A CA  1 
ATOM   3346 C  C   . LEU A 1 415 ? -1.115  -1.657  20.062  1.00 19.52 ? 414  LEU A C   1 
ATOM   3347 O  O   . LEU A 1 415 ? 0.074   -1.539  20.393  1.00 18.64 ? 414  LEU A O   1 
ATOM   3348 C  CB  . LEU A 1 415 ? -1.688  -3.444  18.373  1.00 16.00 ? 414  LEU A CB  1 
ATOM   3349 C  CG  . LEU A 1 415 ? -0.325  -3.691  17.724  1.00 16.33 ? 414  LEU A CG  1 
ATOM   3350 C  CD1 . LEU A 1 415 ? 0.532   -4.642  18.565  1.00 18.58 ? 414  LEU A CD1 1 
ATOM   3351 C  CD2 . LEU A 1 415 ? -0.505  -4.229  16.292  1.00 16.20 ? 414  LEU A CD2 1 
ATOM   3352 N  N   . GLY A 1 416 ? -1.921  -0.602  19.905  1.00 17.18 ? 415  GLY A N   1 
ATOM   3353 C  CA  . GLY A 1 416 ? -1.430  0.738   20.194  1.00 15.45 ? 415  GLY A CA  1 
ATOM   3354 C  C   . GLY A 1 416 ? -0.993  0.893   21.639  1.00 15.20 ? 415  GLY A C   1 
ATOM   3355 O  O   . GLY A 1 416 ? 0.074   1.444   21.925  1.00 18.54 ? 415  GLY A O   1 
ATOM   3356 N  N   . MET A 1 417 ? -1.813  0.412   22.576  1.00 14.11 ? 416  MET A N   1 
ATOM   3357 C  CA  . MET A 1 417 ? -1.425  0.520   23.980  1.00 14.18 ? 416  MET A CA  1 
ATOM   3358 C  C   . MET A 1 417 ? -0.192  -0.324  24.278  1.00 15.40 ? 416  MET A C   1 
ATOM   3359 O  O   . MET A 1 417 ? 0.680   0.096   25.050  1.00 16.69 ? 416  MET A O   1 
ATOM   3360 C  CB  . MET A 1 417 ? -2.586  0.122   24.888  1.00 16.17 ? 416  MET A CB  1 
ATOM   3361 C  CG  . MET A 1 417 ? -3.749  1.095   24.846  1.00 16.36 ? 416  MET A CG  1 
ATOM   3362 S  SD  . MET A 1 417 ? -5.084  0.661   25.975  1.00 21.42 ? 416  MET A SD  1 
ATOM   3363 C  CE  . MET A 1 417 ? -4.324  1.048   27.548  1.00 22.79 ? 416  MET A CE  1 
ATOM   3364 N  N   . MET A 1 418 ? -0.098  -1.518  23.684  1.00 17.02 ? 417  MET A N   1 
ATOM   3365 C  CA  . MET A 1 418 ? 1.081   -2.353  23.899  1.00 17.47 ? 417  MET A CA  1 
ATOM   3366 C  C   . MET A 1 418 ? 2.340   -1.626  23.451  1.00 18.00 ? 417  MET A C   1 
ATOM   3367 O  O   . MET A 1 418 ? 3.362   -1.629  24.150  1.00 19.80 ? 417  MET A O   1 
ATOM   3368 C  CB  . MET A 1 418 ? 0.937   -3.682  23.147  1.00 16.36 ? 417  MET A CB  1 
ATOM   3369 C  CG  . MET A 1 418 ? -0.122  -4.617  23.709  1.00 17.30 ? 417  MET A CG  1 
ATOM   3370 S  SD  . MET A 1 418 ? -0.596  -5.943  22.575  1.00 19.89 ? 417  MET A SD  1 
ATOM   3371 C  CE  . MET A 1 418 ? 0.995   -6.636  22.121  1.00 22.36 ? 417  MET A CE  1 
ATOM   3372 N  N   . LEU A 1 419 ? 2.287   -0.994  22.276  1.00 16.64 ? 418  LEU A N   1 
ATOM   3373 C  CA  . LEU A 1 419 ? 3.458   -0.302  21.755  1.00 17.74 ? 418  LEU A CA  1 
ATOM   3374 C  C   . LEU A 1 419 ? 3.752   0.994   22.497  1.00 18.66 ? 418  LEU A C   1 
ATOM   3375 O  O   . LEU A 1 419 ? 4.904   1.437   22.509  1.00 20.70 ? 418  LEU A O   1 
ATOM   3376 C  CB  . LEU A 1 419 ? 3.272   -0.019  20.267  1.00 18.41 ? 418  LEU A CB  1 
ATOM   3377 C  CG  . LEU A 1 419 ? 3.187   -1.279  19.401  1.00 21.68 ? 418  LEU A CG  1 
ATOM   3378 C  CD1 . LEU A 1 419 ? 2.792   -0.927  17.979  1.00 20.97 ? 418  LEU A CD1 1 
ATOM   3379 C  CD2 . LEU A 1 419 ? 4.501   -2.030  19.423  1.00 25.23 ? 418  LEU A CD2 1 
ATOM   3380 N  N   . LYS A 1 420 ? 2.740   1.611   23.110  1.00 20.53 ? 419  LYS A N   1 
ATOM   3381 C  CA  . LYS A 1 420 ? 2.976   2.797   23.929  1.00 20.33 ? 419  LYS A CA  1 
ATOM   3382 C  C   . LYS A 1 420 ? 3.706   2.445   25.218  1.00 20.35 ? 419  LYS A C   1 
ATOM   3383 O  O   . LYS A 1 420 ? 4.583   3.193   25.670  1.00 22.11 ? 419  LYS A O   1 
ATOM   3384 C  CB  . LYS A 1 420 ? 1.646   3.483   24.251  1.00 23.27 ? 419  LYS A CB  1 
ATOM   3385 C  CG  . LYS A 1 420 ? 1.761   4.643   25.244  1.00 21.65 ? 419  LYS A CG  1 
ATOM   3386 C  CD  . LYS A 1 420 ? 0.410   5.303   25.492  1.00 22.86 ? 419  LYS A CD  1 
ATOM   3387 C  CE  . LYS A 1 420 ? 0.537   6.451   26.485  1.00 24.04 ? 419  LYS A CE  1 
ATOM   3388 N  NZ  . LYS A 1 420 ? -0.780  7.056   26.827  1.00 23.83 ? 419  LYS A NZ  1 
ATOM   3389 N  N   . HIS A 1 421 ? 3.365   1.310   25.824  1.00 20.01 ? 420  HIS A N   1 
ATOM   3390 C  CA  . HIS A 1 421 ? 3.762   1.056   27.201  1.00 18.36 ? 420  HIS A CA  1 
ATOM   3391 C  C   . HIS A 1 421 ? 4.959   0.128   27.361  1.00 20.25 ? 420  HIS A C   1 
ATOM   3392 O  O   . HIS A 1 421 ? 5.539   0.097   28.451  1.00 21.78 ? 420  HIS A O   1 
ATOM   3393 C  CB  . HIS A 1 421 ? 2.570   0.497   27.984  1.00 19.11 ? 420  HIS A CB  1 
ATOM   3394 C  CG  . HIS A 1 421 ? 1.563   1.544   28.348  1.00 21.48 ? 420  HIS A CG  1 
ATOM   3395 N  ND1 . HIS A 1 421 ? 1.737   2.400   29.415  1.00 23.14 ? 420  HIS A ND1 1 
ATOM   3396 C  CD2 . HIS A 1 421 ? 0.392   1.898   27.767  1.00 23.29 ? 420  HIS A CD2 1 
ATOM   3397 C  CE1 . HIS A 1 421 ? 0.707   3.225   29.486  1.00 24.23 ? 420  HIS A CE1 1 
ATOM   3398 N  NE2 . HIS A 1 421 ? -0.124  2.941   28.498  1.00 24.13 ? 420  HIS A NE2 1 
ATOM   3399 N  N   . PHE A 1 422 ? 5.361   -0.611  26.324  1.00 19.48 ? 421  PHE A N   1 
ATOM   3400 C  CA  . PHE A 1 422 ? 6.408   -1.615  26.478  1.00 19.21 ? 421  PHE A CA  1 
ATOM   3401 C  C   . PHE A 1 422 ? 7.317   -1.676  25.260  1.00 21.41 ? 421  PHE A C   1 
ATOM   3402 O  O   . PHE A 1 422 ? 6.884   -1.467  24.122  1.00 22.27 ? 421  PHE A O   1 
ATOM   3403 C  CB  . PHE A 1 422 ? 5.850   -3.036  26.678  1.00 20.99 ? 421  PHE A CB  1 
ATOM   3404 C  CG  . PHE A 1 422 ? 4.852   -3.164  27.794  1.00 19.22 ? 421  PHE A CG  1 
ATOM   3405 C  CD1 . PHE A 1 422 ? 5.270   -3.392  29.097  1.00 19.95 ? 421  PHE A CD1 1 
ATOM   3406 C  CD2 . PHE A 1 422 ? 3.496   -3.089  27.534  1.00 18.79 ? 421  PHE A CD2 1 
ATOM   3407 C  CE1 . PHE A 1 422 ? 4.349   -3.530  30.122  1.00 20.68 ? 421  PHE A CE1 1 
ATOM   3408 C  CE2 . PHE A 1 422 ? 2.570   -3.224  28.550  1.00 17.61 ? 421  PHE A CE2 1 
ATOM   3409 C  CZ  . PHE A 1 422 ? 2.994   -3.448  29.854  1.00 18.64 ? 421  PHE A CZ  1 
ATOM   3410 N  N   . ASP A 1 423 ? 8.580   -2.003  25.519  1.00 20.56 ? 422  ASP A N   1 
ATOM   3411 C  CA  . ASP A 1 423 ? 9.471   -2.578  24.520  1.00 21.23 ? 422  ASP A CA  1 
ATOM   3412 C  C   . ASP A 1 423 ? 9.367   -4.097  24.599  1.00 21.72 ? 422  ASP A C   1 
ATOM   3413 O  O   . ASP A 1 423 ? 9.076   -4.654  25.659  1.00 23.99 ? 422  ASP A O   1 
ATOM   3414 C  CB  . ASP A 1 423 ? 10.920  -2.140  24.757  1.00 23.85 ? 422  ASP A CB  1 
ATOM   3415 C  CG  . ASP A 1 423 ? 11.141  -0.672  24.464  1.00 29.09 ? 422  ASP A CG  1 
ATOM   3416 O  OD1 . ASP A 1 423 ? 10.784  -0.225  23.352  1.00 31.48 ? 422  ASP A OD1 1 
ATOM   3417 O  OD2 . ASP A 1 423 ? 11.671  0.038   25.346  1.00 33.47 ? 422  ASP A OD2 1 
ATOM   3418 N  N   . PHE A 1 424 ? 9.610   -4.772  23.473  1.00 20.55 ? 423  PHE A N   1 
ATOM   3419 C  CA  . PHE A 1 424 ? 9.429   -6.219  23.394  1.00 19.29 ? 423  PHE A CA  1 
ATOM   3420 C  C   . PHE A 1 424 ? 10.696  -6.898  22.897  1.00 21.06 ? 423  PHE A C   1 
ATOM   3421 O  O   . PHE A 1 424 ? 11.424  -6.357  22.058  1.00 25.22 ? 423  PHE A O   1 
ATOM   3422 C  CB  . PHE A 1 424 ? 8.251   -6.594  22.480  1.00 20.19 ? 423  PHE A CB  1 
ATOM   3423 C  CG  . PHE A 1 424 ? 6.927   -6.137  23.003  1.00 20.64 ? 423  PHE A CG  1 
ATOM   3424 C  CD1 . PHE A 1 424 ? 6.213   -6.924  23.896  1.00 20.90 ? 423  PHE A CD1 1 
ATOM   3425 C  CD2 . PHE A 1 424 ? 6.403   -4.909  22.621  1.00 17.65 ? 423  PHE A CD2 1 
ATOM   3426 C  CE1 . PHE A 1 424 ? 4.997   -6.508  24.396  1.00 19.77 ? 423  PHE A CE1 1 
ATOM   3427 C  CE2 . PHE A 1 424 ? 5.177   -4.482  23.119  1.00 18.27 ? 423  PHE A CE2 1 
ATOM   3428 C  CZ  . PHE A 1 424 ? 4.475   -5.288  24.011  1.00 21.45 ? 423  PHE A CZ  1 
ATOM   3429 N  N   . GLU A 1 425 ? 10.945  -8.101  23.417  1.00 22.07 ? 424  GLU A N   1 
ATOM   3430 C  CA  . GLU A 1 425 ? 12.139  -8.874  23.091  1.00 22.49 ? 424  GLU A CA  1 
ATOM   3431 C  C   . GLU A 1 425 ? 11.744  -10.302 22.742  1.00 20.27 ? 424  GLU A C   1 
ATOM   3432 O  O   . GLU A 1 425 ? 11.066  -10.974 23.526  1.00 21.12 ? 424  GLU A O   1 
ATOM   3433 C  CB  . GLU A 1 425 ? 13.141  -8.885  24.255  1.00 25.41 ? 424  GLU A CB  1 
ATOM   3434 C  CG  . GLU A 1 425 ? 14.403  -9.685  23.970  1.00 30.35 ? 424  GLU A CG  1 
ATOM   3435 C  CD  . GLU A 1 425 ? 15.248  -9.926  25.213  1.00 32.51 ? 424  GLU A CD  1 
ATOM   3436 O  OE1 . GLU A 1 425 ? 14.880  -9.437  26.303  1.00 31.41 ? 424  GLU A OE1 1 
ATOM   3437 O  OE2 . GLU A 1 425 ? 16.280  -10.616 25.100  1.00 34.32 ? 424  GLU A OE2 1 
ATOM   3438 N  N   . ASP A 1 426 ? 12.176  -10.757 21.566  1.00 21.69 ? 425  ASP A N   1 
ATOM   3439 C  CA  . ASP A 1 426 ? 12.032  -12.148 21.126  1.00 20.72 ? 425  ASP A CA  1 
ATOM   3440 C  C   . ASP A 1 426 ? 13.177  -12.970 21.727  1.00 21.01 ? 425  ASP A C   1 
ATOM   3441 O  O   . ASP A 1 426 ? 14.130  -13.374 21.057  1.00 22.67 ? 425  ASP A O   1 
ATOM   3442 C  CB  . ASP A 1 426 ? 12.022  -12.189 19.602  1.00 20.99 ? 425  ASP A CB  1 
ATOM   3443 C  CG  . ASP A 1 426 ? 11.995  -13.598 19.027  1.00 20.70 ? 425  ASP A CG  1 
ATOM   3444 O  OD1 . ASP A 1 426 ? 11.537  -14.543 19.702  1.00 21.67 ? 425  ASP A OD1 1 
ATOM   3445 O  OD2 . ASP A 1 426 ? 12.438  -13.745 17.864  1.00 22.46 ? 425  ASP A OD2 1 
ATOM   3446 N  N   . HIS A 1 427 ? 13.068  -13.220 23.036  1.00 22.33 ? 426  HIS A N   1 
ATOM   3447 C  CA  . HIS A 1 427 ? 14.215  -13.719 23.794  1.00 22.44 ? 426  HIS A CA  1 
ATOM   3448 C  C   . HIS A 1 427 ? 14.563  -15.174 23.493  1.00 25.02 ? 426  HIS A C   1 
ATOM   3449 O  O   . HIS A 1 427 ? 15.685  -15.596 23.801  1.00 26.56 ? 426  HIS A O   1 
ATOM   3450 C  CB  . HIS A 1 427 ? 13.972  -13.553 25.293  1.00 22.28 ? 426  HIS A CB  1 
ATOM   3451 C  CG  . HIS A 1 427 ? 12.825  -14.359 25.817  1.00 22.58 ? 426  HIS A CG  1 
ATOM   3452 N  ND1 . HIS A 1 427 ? 11.517  -14.121 25.449  1.00 21.49 ? 426  HIS A ND1 1 
ATOM   3453 C  CD2 . HIS A 1 427 ? 12.787  -15.394 26.690  1.00 22.96 ? 426  HIS A CD2 1 
ATOM   3454 C  CE1 . HIS A 1 427 ? 10.724  -14.976 26.069  1.00 22.40 ? 426  HIS A CE1 1 
ATOM   3455 N  NE2 . HIS A 1 427 ? 11.469  -15.758 26.832  1.00 22.43 ? 426  HIS A NE2 1 
ATOM   3456 N  N   . THR A 1 428 ? 13.645  -15.953 22.917  1.00 25.31 ? 427  THR A N   1 
ATOM   3457 C  CA  . THR A 1 428 ? 13.919  -17.344 22.559  1.00 24.14 ? 427  THR A CA  1 
ATOM   3458 C  C   . THR A 1 428 ? 14.211  -17.539 21.075  1.00 24.13 ? 427  THR A C   1 
ATOM   3459 O  O   . THR A 1 428 ? 14.438  -18.676 20.648  1.00 24.18 ? 427  THR A O   1 
ATOM   3460 C  CB  . THR A 1 428 ? 12.745  -18.253 22.960  1.00 24.97 ? 427  THR A CB  1 
ATOM   3461 O  OG1 . THR A 1 428 ? 11.654  -18.095 22.035  1.00 23.72 ? 427  THR A OG1 1 
ATOM   3462 C  CG2 . THR A 1 428 ? 12.269  -17.922 24.372  1.00 25.25 ? 427  THR A CG2 1 
ATOM   3463 N  N   . ASN A 1 429 ? 14.223  -16.470 20.283  1.00 23.29 ? 428  ASN A N   1 
ATOM   3464 C  CA  . ASN A 1 429 ? 14.303  -16.576 18.827  1.00 22.97 ? 428  ASN A CA  1 
ATOM   3465 C  C   . ASN A 1 429 ? 13.256  -17.569 18.317  1.00 22.54 ? 428  ASN A C   1 
ATOM   3466 O  O   . ASN A 1 429 ? 13.554  -18.569 17.659  1.00 25.11 ? 428  ASN A O   1 
ATOM   3467 C  CB  . ASN A 1 429 ? 15.714  -16.964 18.366  1.00 24.15 ? 428  ASN A CB  1 
ATOM   3468 C  CG  . ASN A 1 429 ? 15.914  -16.720 16.880  1.00 27.72 ? 428  ASN A CG  1 
ATOM   3469 O  OD1 . ASN A 1 429 ? 15.192  -15.922 16.274  1.00 30.78 ? 428  ASN A OD1 1 
ATOM   3470 N  ND2 . ASN A 1 429 ? 16.884  -17.407 16.283  1.00 27.85 ? 428  ASN A ND2 1 
ATOM   3471 N  N   . TYR A 1 430 ? 12.004  -17.253 18.631  1.00 19.52 ? 429  TYR A N   1 
ATOM   3472 C  CA  . TYR A 1 430 ? 10.900  -18.190 18.448  1.00 19.45 ? 429  TYR A CA  1 
ATOM   3473 C  C   . TYR A 1 430 ? 10.736  -18.604 16.989  1.00 21.56 ? 429  TYR A C   1 
ATOM   3474 O  O   . TYR A 1 430 ? 10.748  -17.766 16.083  1.00 23.64 ? 429  TYR A O   1 
ATOM   3475 C  CB  . TYR A 1 430 ? 9.617   -17.549 18.966  1.00 18.20 ? 429  TYR A CB  1 
ATOM   3476 C  CG  . TYR A 1 430 ? 8.336   -18.245 18.570  1.00 16.40 ? 429  TYR A CG  1 
ATOM   3477 C  CD1 . TYR A 1 430 ? 7.952   -19.453 19.160  1.00 16.85 ? 429  TYR A CD1 1 
ATOM   3478 C  CD2 . TYR A 1 430 ? 7.484   -17.677 17.621  1.00 17.65 ? 429  TYR A CD2 1 
ATOM   3479 C  CE1 . TYR A 1 430 ? 6.746   -20.076 18.796  1.00 15.77 ? 429  TYR A CE1 1 
ATOM   3480 C  CE2 . TYR A 1 430 ? 6.304   -18.284 17.261  1.00 17.39 ? 429  TYR A CE2 1 
ATOM   3481 C  CZ  . TYR A 1 430 ? 5.934   -19.479 17.843  1.00 17.24 ? 429  TYR A CZ  1 
ATOM   3482 O  OH  . TYR A 1 430 ? 4.743   -20.064 17.454  1.00 18.10 ? 429  TYR A OH  1 
ATOM   3483 N  N   . GLU A 1 431 ? 10.571  -19.907 16.773  1.00 22.01 ? 430  GLU A N   1 
ATOM   3484 C  CA  . GLU A 1 431 ? 10.289  -20.471 15.458  1.00 24.94 ? 430  GLU A CA  1 
ATOM   3485 C  C   . GLU A 1 431 ? 8.781   -20.635 15.305  1.00 21.21 ? 430  GLU A C   1 
ATOM   3486 O  O   . GLU A 1 431 ? 8.152   -21.352 16.092  1.00 23.15 ? 430  GLU A O   1 
ATOM   3487 C  CB  . GLU A 1 431 ? 10.998  -21.814 15.277  1.00 28.44 ? 430  GLU A CB  1 
ATOM   3488 C  CG  . GLU A 1 431 ? 10.737  -22.473 13.930  1.00 34.54 ? 430  GLU A CG  1 
ATOM   3489 C  CD  . GLU A 1 431 ? 11.500  -23.773 13.749  1.00 43.63 ? 430  GLU A CD  1 
ATOM   3490 O  OE1 . GLU A 1 431 ? 12.495  -23.993 14.469  1.00 45.93 ? 430  GLU A OE1 1 
ATOM   3491 O  OE2 . GLU A 1 431 ? 11.102  -24.578 12.881  1.00 48.53 ? 430  GLU A OE2 1 
ATOM   3492 N  N   . LEU A 1 432 ? 8.204   -19.983 14.292  1.00 18.51 ? 431  LEU A N   1 
ATOM   3493 C  CA  . LEU A 1 432 ? 6.749   -19.963 14.148  1.00 18.20 ? 431  LEU A CA  1 
ATOM   3494 C  C   . LEU A 1 432 ? 6.191   -21.376 13.996  1.00 19.09 ? 431  LEU A C   1 
ATOM   3495 O  O   . LEU A 1 432 ? 6.668   -22.171 13.174  1.00 22.27 ? 431  LEU A O   1 
ATOM   3496 C  CB  . LEU A 1 432 ? 6.342   -19.096 12.953  1.00 17.12 ? 431  LEU A CB  1 
ATOM   3497 C  CG  . LEU A 1 432 ? 4.847   -18.908 12.668  1.00 17.61 ? 431  LEU A CG  1 
ATOM   3498 C  CD1 . LEU A 1 432 ? 4.105   -18.251 13.846  1.00 18.95 ? 431  LEU A CD1 1 
ATOM   3499 C  CD2 . LEU A 1 432 ? 4.677   -18.079 11.402  1.00 19.85 ? 431  LEU A CD2 1 
ATOM   3500 N  N   . ASP A 1 433 ? 5.161   -21.670 14.790  1.00 18.10 ? 432  ASP A N   1 
ATOM   3501 C  CA  . ASP A 1 433 ? 4.502   -22.973 14.845  1.00 18.46 ? 432  ASP A CA  1 
ATOM   3502 C  C   . ASP A 1 433 ? 3.009   -22.675 14.893  1.00 19.19 ? 432  ASP A C   1 
ATOM   3503 O  O   . ASP A 1 433 ? 2.526   -22.121 15.885  1.00 20.86 ? 432  ASP A O   1 
ATOM   3504 C  CB  . ASP A 1 433 ? 4.964   -23.756 16.081  1.00 23.81 ? 432  ASP A CB  1 
ATOM   3505 C  CG  . ASP A 1 433 ? 4.319   -25.128 16.198  1.00 27.06 ? 432  ASP A CG  1 
ATOM   3506 O  OD1 . ASP A 1 433 ? 3.502   -25.491 15.333  1.00 28.56 ? 432  ASP A OD1 1 
ATOM   3507 O  OD2 . ASP A 1 433 ? 4.637   -25.848 17.171  1.00 31.01 ? 432  ASP A OD2 1 
ATOM   3508 N  N   . ILE A 1 434 ? 2.282   -22.997 13.828  1.00 16.10 ? 433  ILE A N   1 
ATOM   3509 C  CA  . ILE A 1 434 ? 0.896   -22.558 13.684  1.00 14.51 ? 433  ILE A CA  1 
ATOM   3510 C  C   . ILE A 1 434 ? -0.027  -23.717 14.043  1.00 14.90 ? 433  ILE A C   1 
ATOM   3511 O  O   . ILE A 1 434 ? -0.082  -24.725 13.333  1.00 16.88 ? 433  ILE A O   1 
ATOM   3512 C  CB  . ILE A 1 434 ? 0.613   -22.031 12.270  1.00 16.76 ? 433  ILE A CB  1 
ATOM   3513 C  CG1 . ILE A 1 434 ? 1.485   -20.799 11.994  1.00 18.04 ? 433  ILE A CG1 1 
ATOM   3514 C  CG2 . ILE A 1 434 ? -0.881  -21.691 12.101  1.00 15.54 ? 433  ILE A CG2 1 
ATOM   3515 C  CD1 . ILE A 1 434 ? 1.386   -20.272 10.590  1.00 19.01 ? 433  ILE A CD1 1 
ATOM   3516 N  N   . LYS A 1 435 ? -0.763  -23.568 15.145  1.00 13.85 ? 434  LYS A N   1 
ATOM   3517 C  CA  . LYS A 1 435 ? -1.764  -24.548 15.545  1.00 14.54 ? 434  LYS A CA  1 
ATOM   3518 C  C   . LYS A 1 435 ? -3.074  -24.312 14.801  1.00 16.10 ? 434  LYS A C   1 
ATOM   3519 O  O   . LYS A 1 435 ? -3.484  -23.167 14.581  1.00 16.52 ? 434  LYS A O   1 
ATOM   3520 C  CB  . LYS A 1 435 ? -2.000  -24.473 17.058  1.00 16.50 ? 434  LYS A CB  1 
ATOM   3521 C  CG  . LYS A 1 435 ? -3.055  -25.431 17.592  1.00 16.69 ? 434  LYS A CG  1 
ATOM   3522 C  CD  . LYS A 1 435 ? -3.116  -25.366 19.123  1.00 22.73 ? 434  LYS A CD  1 
ATOM   3523 C  CE  . LYS A 1 435 ? -4.255  -26.205 19.683  1.00 26.23 ? 434  LYS A CE  1 
ATOM   3524 N  NZ  . LYS A 1 435 ? -4.025  -27.666 19.505  1.00 31.84 ? 434  LYS A NZ  1 
ATOM   3525 N  N   . GLU A 1 436 ? -3.738  -25.401 14.421  1.00 15.40 ? 435  GLU A N   1 
ATOM   3526 C  CA  . GLU A 1 436 ? -4.986  -25.331 13.673  1.00 14.87 ? 435  GLU A CA  1 
ATOM   3527 C  C   . GLU A 1 436 ? -6.144  -25.863 14.510  1.00 14.59 ? 435  GLU A C   1 
ATOM   3528 O  O   . GLU A 1 436 ? -6.085  -26.981 15.038  1.00 15.63 ? 435  GLU A O   1 
ATOM   3529 C  CB  . GLU A 1 436 ? -4.867  -26.103 12.355  1.00 14.98 ? 435  GLU A CB  1 
ATOM   3530 C  CG  . GLU A 1 436 ? -3.761  -25.544 11.467  1.00 16.34 ? 435  GLU A CG  1 
ATOM   3531 C  CD  . GLU A 1 436 ? -3.909  -25.907 9.995   1.00 16.28 ? 435  GLU A CD  1 
ATOM   3532 O  OE1 . GLU A 1 436 ? -5.037  -26.231 9.563   1.00 15.88 ? 435  GLU A OE1 1 
ATOM   3533 O  OE2 . GLU A 1 436 ? -2.897  -25.841 9.262   1.00 15.83 ? 435  GLU A OE2 1 
ATOM   3534 N  N   . THR A 1 437 ? -7.194  -25.058 14.618  1.00 15.67 ? 436  THR A N   1 
ATOM   3535 C  CA  . THR A 1 437 ? -8.466  -25.418 15.237  1.00 16.24 ? 436  THR A CA  1 
ATOM   3536 C  C   . THR A 1 437 ? -9.607  -24.963 14.335  1.00 15.25 ? 436  THR A C   1 
ATOM   3537 O  O   . THR A 1 437 ? -10.547 -24.288 14.760  1.00 17.50 ? 436  THR A O   1 
ATOM   3538 C  CB  . THR A 1 437 ? -8.596  -24.801 16.628  1.00 18.54 ? 436  THR A CB  1 
ATOM   3539 O  OG1 . THR A 1 437 ? -8.455  -23.378 16.535  1.00 21.68 ? 436  THR A OG1 1 
ATOM   3540 C  CG2 . THR A 1 437 ? -7.513  -25.344 17.559  1.00 18.58 ? 436  THR A CG2 1 
ATOM   3541 N  N   . LEU A 1 438 ? -9.522  -25.356 13.061  1.00 14.35 ? 437  LEU A N   1 
ATOM   3542 C  CA  . LEU A 1 438 ? -10.214 -24.689 11.959  1.00 14.34 ? 437  LEU A CA  1 
ATOM   3543 C  C   . LEU A 1 438 ? -9.569  -23.313 11.759  1.00 17.78 ? 437  LEU A C   1 
ATOM   3544 O  O   . LEU A 1 438 ? -9.003  -23.041 10.693  1.00 18.00 ? 437  LEU A O   1 
ATOM   3545 C  CB  . LEU A 1 438 ? -11.733 -24.603 12.212  1.00 15.90 ? 437  LEU A CB  1 
ATOM   3546 C  CG  . LEU A 1 438 ? -12.489 -25.930 12.481  1.00 18.23 ? 437  LEU A CG  1 
ATOM   3547 C  CD1 . LEU A 1 438 ? -13.995 -25.710 12.559  1.00 20.36 ? 437  LEU A CD1 1 
ATOM   3548 C  CD2 . LEU A 1 438 ? -12.169 -27.011 11.447  1.00 18.43 ? 437  LEU A CD2 1 
ATOM   3549 N  N   . THR A 1 439 ? -9.606  -22.457 12.785  1.00 18.45 ? 438  THR A N   1 
ATOM   3550 C  CA  . THR A 1 439 ? -8.867  -21.197 12.797  1.00 15.31 ? 438  THR A CA  1 
ATOM   3551 C  C   . THR A 1 439 ? -7.354  -21.427 12.991  1.00 15.41 ? 438  THR A C   1 
ATOM   3552 O  O   . THR A 1 439 ? -6.901  -22.523 13.344  1.00 16.61 ? 438  THR A O   1 
ATOM   3553 C  CB  . THR A 1 439 ? -9.405  -20.299 13.902  1.00 15.26 ? 438  THR A CB  1 
ATOM   3554 O  OG1 . THR A 1 439 ? -9.375  -21.029 15.133  1.00 18.15 ? 438  THR A OG1 1 
ATOM   3555 C  CG2 . THR A 1 439 ? -10.855 -19.889 13.600  1.00 15.19 ? 438  THR A CG2 1 
ATOM   3556 N  N   . LEU A 1 440 ? -6.564  -20.364 12.778  1.00 12.36 ? 439  LEU A N   1 
ATOM   3557 C  CA  . LEU A 1 440 ? -5.103  -20.418 12.859  1.00 12.04 ? 439  LEU A CA  1 
ATOM   3558 C  C   . LEU A 1 440 ? -4.572  -19.520 13.974  1.00 14.15 ? 439  LEU A C   1 
ATOM   3559 O  O   . LEU A 1 440 ? -5.041  -18.390 14.148  1.00 14.08 ? 439  LEU A O   1 
ATOM   3560 C  CB  . LEU A 1 440 ? -4.459  -19.985 11.533  1.00 13.05 ? 439  LEU A CB  1 
ATOM   3561 C  CG  . LEU A 1 440 ? -4.898  -20.716 10.261  1.00 15.41 ? 439  LEU A CG  1 
ATOM   3562 C  CD1 . LEU A 1 440 ? -4.106  -20.205 9.066   1.00 15.67 ? 439  LEU A CD1 1 
ATOM   3563 C  CD2 . LEU A 1 440 ? -4.699  -22.229 10.416  1.00 16.07 ? 439  LEU A CD2 1 
ATOM   3564 N  N   . LYS A 1 441 ? -3.559  -20.011 14.713  1.00 14.02 ? 440  LYS A N   1 
ATOM   3565 C  CA  . LYS A 1 441 ? -2.973  -19.217 15.792  1.00 14.40 ? 440  LYS A CA  1 
ATOM   3566 C  C   . LYS A 1 441 ? -1.567  -19.716 16.082  1.00 15.78 ? 440  LYS A C   1 
ATOM   3567 O  O   . LYS A 1 441 ? -1.346  -20.933 16.046  1.00 18.01 ? 440  LYS A O   1 
ATOM   3568 C  CB  . LYS A 1 441 ? -3.837  -19.302 17.063  1.00 18.61 ? 440  LYS A CB  1 
ATOM   3569 C  CG  . LYS A 1 441 ? -3.542  -18.254 18.130  1.00 22.62 ? 440  LYS A CG  1 
ATOM   3570 C  CD  . LYS A 1 441 ? -4.480  -18.390 19.346  1.00 25.68 ? 440  LYS A CD  1 
ATOM   3571 C  CE  . LYS A 1 441 ? -5.946  -18.502 18.948  1.00 26.59 ? 440  LYS A CE  1 
ATOM   3572 N  NZ  . LYS A 1 441 ? -6.839  -18.453 20.155  1.00 27.80 ? 440  LYS A NZ  1 
ATOM   3573 N  N   . PRO A 1 442 ? -0.604  -18.834 16.365  1.00 16.26 ? 441  PRO A N   1 
ATOM   3574 C  CA  . PRO A 1 442 ? 0.707   -19.310 16.824  1.00 15.81 ? 441  PRO A CA  1 
ATOM   3575 C  C   . PRO A 1 442 ? 0.564   -20.129 18.099  1.00 18.31 ? 441  PRO A C   1 
ATOM   3576 O  O   . PRO A 1 442 ? -0.309  -19.874 18.932  1.00 18.50 ? 441  PRO A O   1 
ATOM   3577 C  CB  . PRO A 1 442 ? 1.491   -18.015 17.080  1.00 18.33 ? 441  PRO A CB  1 
ATOM   3578 C  CG  . PRO A 1 442 ? 0.787   -16.963 16.288  1.00 18.30 ? 441  PRO A CG  1 
ATOM   3579 C  CD  . PRO A 1 442 ? -0.662  -17.363 16.291  1.00 15.29 ? 441  PRO A CD  1 
ATOM   3580 N  N   . GLU A 1 443 ? 1.432   -21.129 18.243  1.00 17.13 ? 442  GLU A N   1 
ATOM   3581 C  CA  . GLU A 1 443 ? 1.507   -21.925 19.459  1.00 18.07 ? 442  GLU A CA  1 
ATOM   3582 C  C   . GLU A 1 443 ? 2.899   -21.781 20.051  1.00 17.04 ? 442  GLU A C   1 
ATOM   3583 O  O   . GLU A 1 443 ? 3.896   -21.797 19.322  1.00 17.37 ? 442  GLU A O   1 
ATOM   3584 C  CB  . GLU A 1 443 ? 1.200   -23.413 19.204  1.00 20.46 ? 442  GLU A CB  1 
ATOM   3585 C  CG  . GLU A 1 443 ? 1.241   -24.261 20.490  1.00 25.49 ? 442  GLU A CG  1 
ATOM   3586 C  CD  . GLU A 1 443 ? 0.794   -25.711 20.297  1.00 31.53 ? 442  GLU A CD  1 
ATOM   3587 O  OE1 . GLU A 1 443 ? 0.859   -26.232 19.166  1.00 31.93 ? 442  GLU A OE1 1 
ATOM   3588 O  OE2 . GLU A 1 443 ? 0.370   -26.334 21.292  1.00 37.70 ? 442  GLU A OE2 1 
ATOM   3589 N  N   . GLY A 1 444 ? 2.964   -21.627 21.372  1.00 17.69 ? 443  GLY A N   1 
ATOM   3590 C  CA  . GLY A 1 444 ? 4.250   -21.536 22.042  1.00 18.57 ? 443  GLY A CA  1 
ATOM   3591 C  C   . GLY A 1 444 ? 4.985   -20.227 21.870  1.00 19.91 ? 443  GLY A C   1 
ATOM   3592 O  O   . GLY A 1 444 ? 6.148   -20.133 22.272  1.00 21.15 ? 443  GLY A O   1 
ATOM   3593 N  N   . PHE A 1 445 ? 4.344   -19.214 21.288  1.00 18.87 ? 444  PHE A N   1 
ATOM   3594 C  CA  . PHE A 1 445 ? 4.966   -17.909 21.094  1.00 17.73 ? 444  PHE A CA  1 
ATOM   3595 C  C   . PHE A 1 445 ? 5.077   -17.174 22.432  1.00 15.64 ? 444  PHE A C   1 
ATOM   3596 O  O   . PHE A 1 445 ? 4.064   -16.907 23.088  1.00 16.49 ? 444  PHE A O   1 
ATOM   3597 C  CB  . PHE A 1 445 ? 4.143   -17.112 20.081  1.00 17.85 ? 444  PHE A CB  1 
ATOM   3598 C  CG  . PHE A 1 445 ? 4.649   -15.721 19.814  1.00 16.92 ? 444  PHE A CG  1 
ATOM   3599 C  CD1 . PHE A 1 445 ? 6.002   -15.430 19.839  1.00 19.94 ? 444  PHE A CD1 1 
ATOM   3600 C  CD2 . PHE A 1 445 ? 3.751   -14.698 19.509  1.00 19.23 ? 444  PHE A CD2 1 
ATOM   3601 C  CE1 . PHE A 1 445 ? 6.454   -14.139 19.584  1.00 20.60 ? 444  PHE A CE1 1 
ATOM   3602 C  CE2 . PHE A 1 445 ? 4.195   -13.402 19.254  1.00 19.36 ? 444  PHE A CE2 1 
ATOM   3603 C  CZ  . PHE A 1 445 ? 5.548   -13.122 19.291  1.00 20.04 ? 444  PHE A CZ  1 
ATOM   3604 N  N   . VAL A 1 446 ? 6.309   -16.861 22.841  1.00 16.67 ? 445  VAL A N   1 
ATOM   3605 C  CA  . VAL A 1 446 ? 6.593   -16.141 24.078  1.00 17.05 ? 445  VAL A CA  1 
ATOM   3606 C  C   . VAL A 1 446 ? 7.525   -14.974 23.774  1.00 17.50 ? 445  VAL A C   1 
ATOM   3607 O  O   . VAL A 1 446 ? 8.320   -15.023 22.830  1.00 19.73 ? 445  VAL A O   1 
ATOM   3608 C  CB  . VAL A 1 446 ? 7.229   -17.058 25.149  1.00 15.66 ? 445  VAL A CB  1 
ATOM   3609 C  CG1 . VAL A 1 446 ? 6.255   -18.139 25.593  1.00 16.46 ? 445  VAL A CG1 1 
ATOM   3610 C  CG2 . VAL A 1 446 ? 8.533   -17.669 24.627  1.00 17.87 ? 445  VAL A CG2 1 
ATOM   3611 N  N   . VAL A 1 447 ? 7.419   -13.914 24.580  1.00 18.41 ? 446  VAL A N   1 
ATOM   3612 C  CA  . VAL A 1 447 ? 8.290   -12.740 24.500  1.00 17.71 ? 446  VAL A CA  1 
ATOM   3613 C  C   . VAL A 1 447 ? 8.499   -12.196 25.912  1.00 17.81 ? 446  VAL A C   1 
ATOM   3614 O  O   . VAL A 1 447 ? 7.797   -12.567 26.855  1.00 18.82 ? 446  VAL A O   1 
ATOM   3615 C  CB  . VAL A 1 447 ? 7.706   -11.625 23.597  1.00 16.47 ? 446  VAL A CB  1 
ATOM   3616 C  CG1 . VAL A 1 447 ? 7.481   -12.134 22.188  1.00 18.93 ? 446  VAL A CG1 1 
ATOM   3617 C  CG2 . VAL A 1 447 ? 6.407   -11.074 24.190  1.00 17.23 ? 446  VAL A CG2 1 
ATOM   3618 N  N   . LYS A 1 448 ? 9.469   -11.292 26.058  1.00 17.40 ? 447  LYS A N   1 
ATOM   3619 C  CA  . LYS A 1 448 ? 9.620   -10.500 27.270  1.00 18.64 ? 447  LYS A CA  1 
ATOM   3620 C  C   . LYS A 1 448 ? 9.291   -9.045  26.965  1.00 22.34 ? 447  LYS A C   1 
ATOM   3621 O  O   . LYS A 1 448 ? 9.635   -8.532  25.895  1.00 23.63 ? 447  LYS A O   1 
ATOM   3622 C  CB  . LYS A 1 448 ? 11.037  -10.604 27.849  1.00 21.18 ? 447  LYS A CB  1 
ATOM   3623 C  CG  . LYS A 1 448 ? 11.377  -11.957 28.442  1.00 24.12 ? 447  LYS A CG  1 
ATOM   3624 C  CD  . LYS A 1 448 ? 12.802  -11.967 29.006  1.00 29.86 ? 447  LYS A CD  1 
ATOM   3625 C  CE  . LYS A 1 448 ? 13.204  -13.341 29.515  1.00 35.20 ? 447  LYS A CE  1 
ATOM   3626 N  NZ  . LYS A 1 448 ? 14.577  -13.324 30.116  1.00 38.87 ? 447  LYS A NZ  1 
ATOM   3627 N  N   . ALA A 1 449 ? 8.612   -8.390  27.900  1.00 20.02 ? 448  ALA A N   1 
ATOM   3628 C  CA  . ALA A 1 449 ? 8.283   -6.979  27.778  1.00 23.35 ? 448  ALA A CA  1 
ATOM   3629 C  C   . ALA A 1 449 ? 9.110   -6.183  28.773  1.00 27.65 ? 448  ALA A C   1 
ATOM   3630 O  O   . ALA A 1 449 ? 9.287   -6.597  29.923  1.00 33.64 ? 448  ALA A O   1 
ATOM   3631 C  CB  . ALA A 1 449 ? 6.788   -6.726  28.013  1.00 22.63 ? 448  ALA A CB  1 
ATOM   3632 N  N   . LYS A 1 450 ? 9.631   -5.055  28.318  1.00 23.89 ? 449  LYS A N   1 
ATOM   3633 C  CA  . LYS A 1 450 ? 10.351  -4.111  29.161  1.00 25.78 ? 449  LYS A CA  1 
ATOM   3634 C  C   . LYS A 1 450 ? 9.475   -2.870  29.287  1.00 24.91 ? 449  LYS A C   1 
ATOM   3635 O  O   . LYS A 1 450 ? 9.225   -2.178  28.295  1.00 24.55 ? 449  LYS A O   1 
ATOM   3636 C  CB  . LYS A 1 450 ? 11.714  -3.780  28.553  1.00 33.04 ? 449  LYS A CB  1 
ATOM   3637 C  CG  . LYS A 1 450 ? 12.745  -3.247  29.531  1.00 42.07 ? 449  LYS A CG  1 
ATOM   3638 C  CD  . LYS A 1 450 ? 13.496  -4.376  30.217  1.00 48.00 ? 449  LYS A CD  1 
ATOM   3639 C  CE  . LYS A 1 450 ? 14.953  -3.997  30.447  1.00 51.62 ? 449  LYS A CE  1 
ATOM   3640 N  NZ  . LYS A 1 450 ? 15.714  -5.062  31.162  1.00 53.93 ? 449  LYS A NZ  1 
ATOM   3641 N  N   . SER A 1 451 ? 8.992   -2.600  30.497  1.00 24.53 ? 450  SER A N   1 
ATOM   3642 C  CA  . SER A 1 451 ? 8.097   -1.470  30.698  1.00 23.35 ? 450  SER A CA  1 
ATOM   3643 C  C   . SER A 1 451 ? 8.782   -0.152  30.351  1.00 21.87 ? 450  SER A C   1 
ATOM   3644 O  O   . SER A 1 451 ? 9.947   0.072   30.688  1.00 25.54 ? 450  SER A O   1 
ATOM   3645 C  CB  . SER A 1 451 ? 7.611   -1.437  32.146  1.00 25.29 ? 450  SER A CB  1 
ATOM   3646 O  OG  . SER A 1 451 ? 6.726   -0.347  32.342  1.00 29.31 ? 450  SER A OG  1 
ATOM   3647 N  N   . LYS A 1 452 ? 8.049   0.720   29.658  1.00 24.41 ? 451  LYS A N   1 
ATOM   3648 C  CA  . LYS A 1 452 ? 8.469   2.103   29.469  1.00 25.90 ? 451  LYS A CA  1 
ATOM   3649 C  C   . LYS A 1 452 ? 8.104   2.982   30.657  1.00 27.64 ? 451  LYS A C   1 
ATOM   3650 O  O   . LYS A 1 452 ? 8.420   4.177   30.644  1.00 29.45 ? 451  LYS A O   1 
ATOM   3651 C  CB  . LYS A 1 452 ? 7.858   2.672   28.186  1.00 27.98 ? 451  LYS A CB  1 
ATOM   3652 C  CG  . LYS A 1 452 ? 8.415   2.044   26.921  1.00 26.81 ? 451  LYS A CG  1 
ATOM   3653 C  CD  . LYS A 1 452 ? 7.806   2.681   25.679  1.00 28.02 ? 451  LYS A CD  1 
ATOM   3654 C  CE  . LYS A 1 452 ? 8.407   2.100   24.420  1.00 29.61 ? 451  LYS A CE  1 
ATOM   3655 N  NZ  . LYS A 1 452 ? 9.817   2.537   24.244  1.00 33.13 ? 451  LYS A NZ  1 
ATOM   3656 N  N   . LYS A 1 453 ? 7.452   2.405   31.670  1.00 26.64 ? 452  LYS A N   1 
ATOM   3657 C  CA  . LYS A 1 453 ? 7.099   3.081   32.920  1.00 29.53 ? 452  LYS A CA  1 
ATOM   3658 C  C   . LYS A 1 453 ? 6.268   4.341   32.674  1.00 30.11 ? 452  LYS A C   1 
ATOM   3659 O  O   . LYS A 1 453 ? 6.525   5.404   33.242  1.00 32.18 ? 452  LYS A O   1 
ATOM   3660 C  CB  . LYS A 1 453 ? 8.351   3.393   33.748  1.00 31.72 ? 452  LYS A CB  1 
ATOM   3661 C  CG  . LYS A 1 453 ? 9.118   2.157   34.204  1.00 34.68 ? 452  LYS A CG  1 
ATOM   3662 C  CD  . LYS A 1 453 ? 10.196  2.531   35.213  1.00 39.89 ? 452  LYS A CD  1 
ATOM   3663 C  CE  . LYS A 1 453 ? 10.935  1.308   35.752  1.00 45.26 ? 452  LYS A CE  1 
ATOM   3664 N  NZ  . LYS A 1 453 ? 11.910  0.740   34.775  1.00 47.59 ? 452  LYS A NZ  1 
ATOM   3665 N  N   . ILE A 1 454 ? 5.239   4.205   31.848  1.00 27.14 ? 453  ILE A N   1 
ATOM   3666 C  CA  . ILE A 1 454 ? 4.314   5.292   31.537  1.00 26.25 ? 453  ILE A CA  1 
ATOM   3667 C  C   . ILE A 1 454 ? 2.995   5.015   32.252  1.00 27.39 ? 453  ILE A C   1 
ATOM   3668 O  O   . ILE A 1 454 ? 2.345   3.998   31.971  1.00 25.09 ? 453  ILE A O   1 
ATOM   3669 C  CB  . ILE A 1 454 ? 4.102   5.437   30.024  1.00 27.23 ? 453  ILE A CB  1 
ATOM   3670 C  CG1 . ILE A 1 454 ? 5.443   5.718   29.334  1.00 25.17 ? 453  ILE A CG1 1 
ATOM   3671 C  CG2 . ILE A 1 454 ? 3.089   6.531   29.739  1.00 24.72 ? 453  ILE A CG2 1 
ATOM   3672 C  CD1 . ILE A 1 454 ? 5.364   5.708   27.823  1.00 24.10 ? 453  ILE A CD1 1 
ATOM   3673 N  N   . PRO A 1 455 ? 2.548   5.895   33.148  1.00 30.93 ? 454  PRO A N   1 
ATOM   3674 C  CA  . PRO A 1 455 ? 1.379   5.583   33.980  1.00 32.28 ? 454  PRO A CA  1 
ATOM   3675 C  C   . PRO A 1 455 ? 0.084   5.514   33.189  1.00 32.26 ? 454  PRO A C   1 
ATOM   3676 O  O   . PRO A 1 455 ? -0.088  6.176   32.161  1.00 32.95 ? 454  PRO A O   1 
ATOM   3677 C  CB  . PRO A 1 455 ? 1.334   6.743   34.982  1.00 34.17 ? 454  PRO A CB  1 
ATOM   3678 C  CG  . PRO A 1 455 ? 2.693   7.376   34.920  1.00 34.73 ? 454  PRO A CG  1 
ATOM   3679 C  CD  . PRO A 1 455 ? 3.173   7.174   33.523  1.00 32.98 ? 454  PRO A CD  1 
ATOM   3680 N  N   . LEU A 1 456 ? -0.844  4.712   33.709  1.00 32.57 ? 455  LEU A N   1 
ATOM   3681 C  CA  . LEU A 1 456 ? -2.192  4.597   33.165  1.00 33.94 ? 455  LEU A CA  1 
ATOM   3682 C  C   . LEU A 1 456 ? -3.178  5.520   33.890  1.00 38.44 ? 455  LEU A C   1 
ATOM   3683 O  O   . LEU A 1 456 ? -2.829  6.214   34.856  1.00 41.02 ? 455  LEU A O   1 
ATOM   3684 C  CB  . LEU A 1 456 ? -2.675  3.148   33.257  1.00 30.46 ? 455  LEU A CB  1 
ATOM   3685 C  CG  . LEU A 1 456 ? -1.977  2.117   32.372  1.00 27.31 ? 455  LEU A CG  1 
ATOM   3686 C  CD1 . LEU A 1 456 ? -2.181  0.732   32.949  1.00 29.24 ? 455  LEU A CD1 1 
ATOM   3687 C  CD2 . LEU A 1 456 ? -2.519  2.183   30.952  1.00 25.02 ? 455  LEU A CD2 1 
ATOM   3688 O  OXT . LEU A 1 456 ? -4.358  5.586   33.531  1.00 37.70 ? 455  LEU A OXT 1 
ATOM   3689 N  N   . THR B 1 2   ? -0.242  -25.744 100.685 1.00 64.69 ? 1    THR B N   1 
ATOM   3690 C  CA  . THR B 1 2   ? -0.060  -24.668 99.718  1.00 64.80 ? 1    THR B CA  1 
ATOM   3691 C  C   . THR B 1 2   ? 0.133   -25.236 98.313  1.00 61.03 ? 1    THR B C   1 
ATOM   3692 O  O   . THR B 1 2   ? -0.485  -24.768 97.354  1.00 59.36 ? 1    THR B O   1 
ATOM   3693 C  CB  . THR B 1 2   ? 1.145   -23.770 100.090 1.00 67.46 ? 1    THR B CB  1 
ATOM   3694 O  OG1 . THR B 1 2   ? 1.243   -22.682 99.161  1.00 69.41 ? 1    THR B OG1 1 
ATOM   3695 C  CG2 . THR B 1 2   ? 2.445   -24.567 100.079 1.00 67.18 ? 1    THR B CG2 1 
ATOM   3696 N  N   . ILE B 1 3   ? 0.983   -26.256 98.205  1.00 58.23 ? 2    ILE B N   1 
ATOM   3697 C  CA  . ILE B 1 3   ? 1.248   -26.901 96.923  1.00 55.28 ? 2    ILE B CA  1 
ATOM   3698 C  C   . ILE B 1 3   ? 0.024   -27.713 96.520  1.00 55.63 ? 2    ILE B C   1 
ATOM   3699 O  O   . ILE B 1 3   ? -0.422  -28.598 97.261  1.00 55.69 ? 2    ILE B O   1 
ATOM   3700 C  CB  . ILE B 1 3   ? 2.503   -27.782 97.005  1.00 53.19 ? 2    ILE B CB  1 
ATOM   3701 C  CG1 . ILE B 1 3   ? 3.700   -26.970 97.515  1.00 53.09 ? 2    ILE B CG1 1 
ATOM   3702 C  CG2 . ILE B 1 3   ? 2.800   -28.428 95.655  1.00 51.74 ? 2    ILE B CG2 1 
ATOM   3703 C  CD1 . ILE B 1 3   ? 3.917   -25.654 96.789  1.00 53.08 ? 2    ILE B CD1 1 
ATOM   3704 N  N   . LYS B 1 4   ? -0.530  -27.409 95.347  1.00 53.08 ? 3    LYS B N   1 
ATOM   3705 C  CA  . LYS B 1 4   ? -1.703  -28.093 94.824  1.00 51.03 ? 3    LYS B CA  1 
ATOM   3706 C  C   . LYS B 1 4   ? -1.294  -29.133 93.787  1.00 47.51 ? 3    LYS B C   1 
ATOM   3707 O  O   . LYS B 1 4   ? -0.269  -28.997 93.115  1.00 47.87 ? 3    LYS B O   1 
ATOM   3708 C  CB  . LYS B 1 4   ? -2.690  -27.104 94.188  1.00 52.15 ? 3    LYS B CB  1 
ATOM   3709 C  CG  . LYS B 1 4   ? -3.069  -25.922 95.067  1.00 52.00 ? 3    LYS B CG  1 
ATOM   3710 C  CD  . LYS B 1 4   ? -4.570  -25.664 95.050  1.00 52.37 ? 3    LYS B CD  1 
ATOM   3711 C  CE  . LYS B 1 4   ? -5.084  -25.335 93.659  1.00 51.74 ? 3    LYS B CE  1 
ATOM   3712 N  NZ  . LYS B 1 4   ? -6.527  -24.956 93.694  1.00 50.46 ? 3    LYS B NZ  1 
ATOM   3713 N  N   . GLU B 1 5   ? -2.110  -30.177 93.665  1.00 44.72 ? 4    GLU B N   1 
ATOM   3714 C  CA  . GLU B 1 5   ? -1.930  -31.159 92.606  1.00 41.62 ? 4    GLU B CA  1 
ATOM   3715 C  C   . GLU B 1 5   ? -2.688  -30.701 91.366  1.00 33.49 ? 4    GLU B C   1 
ATOM   3716 O  O   . GLU B 1 5   ? -3.837  -30.260 91.450  1.00 32.18 ? 4    GLU B O   1 
ATOM   3717 C  CB  . GLU B 1 5   ? -2.408  -32.547 93.027  1.00 47.19 ? 4    GLU B CB  1 
ATOM   3718 C  CG  . GLU B 1 5   ? -1.885  -33.649 92.108  1.00 52.11 ? 4    GLU B CG  1 
ATOM   3719 C  CD  . GLU B 1 5   ? -2.846  -34.816 91.958  1.00 57.73 ? 4    GLU B CD  1 
ATOM   3720 O  OE1 . GLU B 1 5   ? -4.029  -34.675 92.335  1.00 60.57 ? 4    GLU B OE1 1 
ATOM   3721 O  OE2 . GLU B 1 5   ? -2.417  -35.878 91.455  1.00 58.74 ? 4    GLU B OE2 1 
ATOM   3722 N  N   . MET B 1 6   ? -2.049  -30.816 90.239  1.00 28.52 ? 5    MET B N   1 
ATOM   3723 C  CA  . MET B 1 6   ? -2.562  -30.317 88.975  1.00 24.93 ? 5    MET B CA  1 
ATOM   3724 C  C   . MET B 1 6   ? -3.483  -31.353 88.338  1.00 19.49 ? 5    MET B C   1 
ATOM   3725 O  O   . MET B 1 6   ? -3.145  -32.539 88.327  1.00 21.82 ? 5    MET B O   1 
ATOM   3726 C  CB  . MET B 1 6   ? -1.370  -30.035 88.072  1.00 27.59 ? 5    MET B CB  1 
ATOM   3727 C  CG  . MET B 1 6   ? -1.606  -29.248 86.861  1.00 27.95 ? 5    MET B CG  1 
ATOM   3728 S  SD  . MET B 1 6   ? 0.016   -29.114 86.107  1.00 22.13 ? 5    MET B SD  1 
ATOM   3729 C  CE  . MET B 1 6   ? 0.908   -28.282 87.418  1.00 24.24 ? 5    MET B CE  1 
ATOM   3730 N  N   . PRO B 1 7   ? -4.642  -30.962 87.802  1.00 18.01 ? 6    PRO B N   1 
ATOM   3731 C  CA  . PRO B 1 7   ? -5.476  -31.939 87.090  1.00 18.07 ? 6    PRO B CA  1 
ATOM   3732 C  C   . PRO B 1 7   ? -4.846  -32.345 85.763  1.00 15.82 ? 6    PRO B C   1 
ATOM   3733 O  O   . PRO B 1 7   ? -3.922  -31.704 85.254  1.00 16.65 ? 6    PRO B O   1 
ATOM   3734 C  CB  . PRO B 1 7   ? -6.803  -31.202 86.875  1.00 21.29 ? 6    PRO B CB  1 
ATOM   3735 C  CG  . PRO B 1 7   ? -6.467  -29.770 86.947  1.00 19.20 ? 6    PRO B CG  1 
ATOM   3736 C  CD  . PRO B 1 7   ? -5.287  -29.637 87.878  1.00 19.51 ? 6    PRO B CD  1 
ATOM   3737 N  N   . GLN B 1 8   ? -5.377  -33.433 85.197  1.00 15.93 ? 7    GLN B N   1 
ATOM   3738 C  CA  . GLN B 1 8   ? -4.832  -34.035 83.981  1.00 15.36 ? 7    GLN B CA  1 
ATOM   3739 C  C   . GLN B 1 8   ? -5.980  -34.672 83.209  1.00 16.27 ? 7    GLN B C   1 
ATOM   3740 O  O   . GLN B 1 8   ? -6.804  -35.370 83.825  1.00 16.94 ? 7    GLN B O   1 
ATOM   3741 C  CB  . GLN B 1 8   ? -3.770  -35.090 84.307  1.00 13.82 ? 7    GLN B CB  1 
ATOM   3742 C  CG  . GLN B 1 8   ? -3.117  -35.719 83.072  1.00 15.07 ? 7    GLN B CG  1 
ATOM   3743 C  CD  . GLN B 1 8   ? -2.038  -36.726 83.418  1.00 20.24 ? 7    GLN B CD  1 
ATOM   3744 O  OE1 . GLN B 1 8   ? -1.886  -37.127 84.583  1.00 25.05 ? 7    GLN B OE1 1 
ATOM   3745 N  NE2 . GLN B 1 8   ? -1.287  -37.154 82.407  1.00 20.36 ? 7    GLN B NE2 1 
ATOM   3746 N  N   . PRO B 1 9   ? -6.067  -34.473 81.884  1.00 15.15 ? 8    PRO B N   1 
ATOM   3747 C  CA  . PRO B 1 9   ? -7.164  -35.098 81.124  1.00 15.24 ? 8    PRO B CA  1 
ATOM   3748 C  C   . PRO B 1 9   ? -6.974  -36.601 80.948  1.00 16.41 ? 8    PRO B C   1 
ATOM   3749 O  O   . PRO B 1 9   ? -5.967  -37.165 81.388  1.00 16.08 ? 8    PRO B O   1 
ATOM   3750 C  CB  . PRO B 1 9   ? -7.138  -34.351 79.783  1.00 13.77 ? 8    PRO B CB  1 
ATOM   3751 C  CG  . PRO B 1 9   ? -5.713  -33.884 79.631  1.00 13.23 ? 8    PRO B CG  1 
ATOM   3752 C  CD  . PRO B 1 9   ? -5.226  -33.595 81.045  1.00 14.94 ? 8    PRO B CD  1 
ATOM   3753 N  N   . LYS B 1 10  ? -7.948  -37.252 80.311  1.00 15.81 ? 9    LYS B N   1 
ATOM   3754 C  CA  . LYS B 1 10  ? -8.005  -38.709 80.257  1.00 11.98 ? 9    LYS B CA  1 
ATOM   3755 C  C   . LYS B 1 10  ? -6.797  -39.293 79.528  1.00 12.88 ? 9    LYS B C   1 
ATOM   3756 O  O   . LYS B 1 10  ? -6.245  -38.687 78.603  1.00 14.11 ? 9    LYS B O   1 
ATOM   3757 C  CB  . LYS B 1 10  ? -9.294  -39.151 79.564  1.00 12.93 ? 9    LYS B CB  1 
ATOM   3758 C  CG  . LYS B 1 10  ? -9.421  -38.664 78.120  1.00 12.70 ? 9    LYS B CG  1 
ATOM   3759 C  CD  . LYS B 1 10  ? -10.802 -38.964 77.559  1.00 14.72 ? 9    LYS B CD  1 
ATOM   3760 C  CE  . LYS B 1 10  ? -11.003 -38.362 76.177  1.00 18.75 ? 9    LYS B CE  1 
ATOM   3761 N  NZ  . LYS B 1 10  ? -12.358 -38.695 75.634  1.00 23.89 ? 9    LYS B NZ  1 
ATOM   3762 N  N   . THR B 1 11  ? -6.411  -40.504 79.932  1.00 14.89 ? 10   THR B N   1 
ATOM   3763 C  CA  . THR B 1 11  ? -5.206  -41.162 79.451  1.00 14.00 ? 10   THR B CA  1 
ATOM   3764 C  C   . THR B 1 11  ? -5.531  -42.423 78.652  1.00 13.31 ? 10   THR B C   1 
ATOM   3765 O  O   . THR B 1 11  ? -6.639  -42.973 78.707  1.00 13.99 ? 10   THR B O   1 
ATOM   3766 C  CB  . THR B 1 11  ? -4.268  -41.531 80.612  1.00 16.72 ? 10   THR B CB  1 
ATOM   3767 O  OG1 . THR B 1 11  ? -4.973  -42.335 81.571  1.00 17.29 ? 10   THR B OG1 1 
ATOM   3768 C  CG2 . THR B 1 11  ? -3.715  -40.281 81.285  1.00 17.78 ? 10   THR B CG2 1 
ATOM   3769 N  N   . PHE B 1 12  ? -4.517  -42.882 77.922  1.00 14.99 ? 11   PHE B N   1 
ATOM   3770 C  CA  . PHE B 1 12  ? -4.617  -43.986 76.976  1.00 14.66 ? 11   PHE B CA  1 
ATOM   3771 C  C   . PHE B 1 12  ? -3.474  -44.976 77.222  1.00 18.45 ? 11   PHE B C   1 
ATOM   3772 O  O   . PHE B 1 12  ? -2.669  -45.267 76.336  1.00 18.34 ? 11   PHE B O   1 
ATOM   3773 C  CB  . PHE B 1 12  ? -4.571  -43.479 75.530  1.00 15.38 ? 11   PHE B CB  1 
ATOM   3774 C  CG  . PHE B 1 12  ? -5.717  -42.566 75.156  1.00 13.81 ? 11   PHE B CG  1 
ATOM   3775 C  CD1 . PHE B 1 12  ? -5.758  -41.252 75.603  1.00 15.10 ? 11   PHE B CD1 1 
ATOM   3776 C  CD2 . PHE B 1 12  ? -6.739  -43.022 74.329  1.00 14.27 ? 11   PHE B CD2 1 
ATOM   3777 C  CE1 . PHE B 1 12  ? -6.817  -40.410 75.254  1.00 15.11 ? 11   PHE B CE1 1 
ATOM   3778 C  CE2 . PHE B 1 12  ? -7.791  -42.189 73.976  1.00 14.97 ? 11   PHE B CE2 1 
ATOM   3779 C  CZ  . PHE B 1 12  ? -7.833  -40.879 74.440  1.00 16.01 ? 11   PHE B CZ  1 
ATOM   3780 N  N   . GLY B 1 13  ? -3.397  -45.498 78.445  1.00 17.02 ? 12   GLY B N   1 
ATOM   3781 C  CA  . GLY B 1 13  ? -2.349  -46.462 78.742  1.00 17.62 ? 12   GLY B CA  1 
ATOM   3782 C  C   . GLY B 1 13  ? -0.972  -45.851 78.571  1.00 17.87 ? 12   GLY B C   1 
ATOM   3783 O  O   . GLY B 1 13  ? -0.716  -44.702 78.958  1.00 20.57 ? 12   GLY B O   1 
ATOM   3784 N  N   . GLU B 1 14  ? -0.068  -46.623 77.961  1.00 18.52 ? 13   GLU B N   1 
ATOM   3785 C  CA  . GLU B 1 14  ? 1.298   -46.151 77.759  1.00 21.28 ? 13   GLU B CA  1 
ATOM   3786 C  C   . GLU B 1 14  ? 1.399   -44.962 76.806  1.00 20.28 ? 13   GLU B C   1 
ATOM   3787 O  O   . GLU B 1 14  ? 2.461   -44.328 76.756  1.00 21.45 ? 13   GLU B O   1 
ATOM   3788 C  CB  . GLU B 1 14  ? 2.181   -47.297 77.258  1.00 28.87 ? 13   GLU B CB  1 
ATOM   3789 C  CG  . GLU B 1 14  ? 2.374   -48.400 78.296  1.00 38.42 ? 13   GLU B CG  1 
ATOM   3790 C  CD  . GLU B 1 14  ? 2.869   -47.863 79.629  1.00 48.41 ? 13   GLU B CD  1 
ATOM   3791 O  OE1 . GLU B 1 14  ? 3.993   -47.314 79.675  1.00 51.62 ? 13   GLU B OE1 1 
ATOM   3792 O  OE2 . GLU B 1 14  ? 2.129   -47.977 80.630  1.00 52.35 ? 13   GLU B OE2 1 
ATOM   3793 N  N   . LEU B 1 15  ? 0.351   -44.645 76.044  1.00 18.81 ? 14   LEU B N   1 
ATOM   3794 C  CA  . LEU B 1 15  ? 0.395   -43.442 75.216  1.00 19.92 ? 14   LEU B CA  1 
ATOM   3795 C  C   . LEU B 1 15  ? 0.054   -42.177 75.997  1.00 19.45 ? 14   LEU B C   1 
ATOM   3796 O  O   . LEU B 1 15  ? 0.184   -41.072 75.450  1.00 18.20 ? 14   LEU B O   1 
ATOM   3797 C  CB  . LEU B 1 15  ? -0.547  -43.584 74.019  1.00 19.60 ? 14   LEU B CB  1 
ATOM   3798 C  CG  . LEU B 1 15  ? -0.209  -44.719 73.050  1.00 22.50 ? 14   LEU B CG  1 
ATOM   3799 C  CD1 . LEU B 1 15  ? -1.290  -44.854 71.976  1.00 25.24 ? 14   LEU B CD1 1 
ATOM   3800 C  CD2 . LEU B 1 15  ? 1.158   -44.499 72.420  1.00 24.54 ? 14   LEU B CD2 1 
ATOM   3801 N  N   . LYS B 1 16  ? -0.370  -42.316 77.251  1.00 17.87 ? 15   LYS B N   1 
ATOM   3802 C  CA  . LYS B 1 16  ? -0.646  -41.192 78.152  1.00 16.61 ? 15   LYS B CA  1 
ATOM   3803 C  C   . LYS B 1 16  ? -1.698  -40.295 77.496  1.00 13.18 ? 15   LYS B C   1 
ATOM   3804 O  O   . LYS B 1 16  ? -2.782  -40.792 77.147  1.00 14.80 ? 15   LYS B O   1 
ATOM   3805 C  CB  . LYS B 1 16  ? 0.681   -40.534 78.524  1.00 20.01 ? 15   LYS B CB  1 
ATOM   3806 C  CG  . LYS B 1 16  ? 1.647   -41.533 79.196  1.00 23.06 ? 15   LYS B CG  1 
ATOM   3807 C  CD  . LYS B 1 16  ? 2.893   -40.876 79.732  1.00 27.12 ? 15   LYS B CD  1 
ATOM   3808 C  CE  . LYS B 1 16  ? 3.858   -41.914 80.289  1.00 31.30 ? 15   LYS B CE  1 
ATOM   3809 N  NZ  . LYS B 1 16  ? 5.039   -41.269 80.916  1.00 35.71 ? 15   LYS B NZ  1 
ATOM   3810 N  N   . ASN B 1 17  ? -1.464  -38.992 77.351  1.00 13.70 ? 16   ASN B N   1 
ATOM   3811 C  CA  . ASN B 1 17  ? -2.465  -38.101 76.773  1.00 14.36 ? 16   ASN B CA  1 
ATOM   3812 C  C   . ASN B 1 17  ? -2.318  -37.930 75.268  1.00 14.45 ? 16   ASN B C   1 
ATOM   3813 O  O   . ASN B 1 17  ? -3.119  -37.209 74.668  1.00 15.34 ? 16   ASN B O   1 
ATOM   3814 C  CB  . ASN B 1 17  ? -2.400  -36.713 77.428  1.00 14.86 ? 16   ASN B CB  1 
ATOM   3815 C  CG  . ASN B 1 17  ? -2.718  -36.744 78.917  1.00 14.56 ? 16   ASN B CG  1 
ATOM   3816 O  OD1 . ASN B 1 17  ? -1.896  -36.340 79.743  1.00 15.05 ? 16   ASN B OD1 1 
ATOM   3817 N  ND2 . ASN B 1 17  ? -3.923  -37.201 79.264  1.00 14.23 ? 16   ASN B ND2 1 
ATOM   3818 N  N   . LEU B 1 18  ? -1.323  -38.559 74.642  1.00 15.62 ? 17   LEU B N   1 
ATOM   3819 C  CA  . LEU B 1 18  ? -1.022  -38.222 73.250  1.00 14.98 ? 17   LEU B CA  1 
ATOM   3820 C  C   . LEU B 1 18  ? -2.202  -38.412 72.300  1.00 16.89 ? 17   LEU B C   1 
ATOM   3821 O  O   . LEU B 1 18  ? -2.374  -37.569 71.401  1.00 16.43 ? 17   LEU B O   1 
ATOM   3822 C  CB  . LEU B 1 18  ? 0.196   -39.022 72.771  1.00 15.57 ? 17   LEU B CB  1 
ATOM   3823 C  CG  . LEU B 1 18  ? 0.694   -38.655 71.368  1.00 18.12 ? 17   LEU B CG  1 
ATOM   3824 C  CD1 . LEU B 1 18  ? 1.205   -37.227 71.372  1.00 19.61 ? 17   LEU B CD1 1 
ATOM   3825 C  CD2 . LEU B 1 18  ? 1.780   -39.608 70.898  1.00 18.84 ? 17   LEU B CD2 1 
ATOM   3826 N  N   . PRO B 1 19  ? -3.038  -39.449 72.421  1.00 15.31 ? 18   PRO B N   1 
ATOM   3827 C  CA  . PRO B 1 19  ? -4.163  -39.590 71.478  1.00 16.73 ? 18   PRO B CA  1 
ATOM   3828 C  C   . PRO B 1 19  ? -5.181  -38.455 71.541  1.00 17.11 ? 18   PRO B C   1 
ATOM   3829 O  O   . PRO B 1 19  ? -6.013  -38.353 70.632  1.00 17.54 ? 18   PRO B O   1 
ATOM   3830 C  CB  . PRO B 1 19  ? -4.794  -40.931 71.877  1.00 16.52 ? 18   PRO B CB  1 
ATOM   3831 C  CG  . PRO B 1 19  ? -3.648  -41.704 72.493  1.00 16.14 ? 18   PRO B CG  1 
ATOM   3832 C  CD  . PRO B 1 19  ? -2.870  -40.652 73.257  1.00 16.60 ? 18   PRO B CD  1 
ATOM   3833 N  N   . LEU B 1 20  ? -5.161  -37.607 72.574  1.00 15.59 ? 19   LEU B N   1 
ATOM   3834 C  CA  . LEU B 1 20  ? -6.050  -36.452 72.565  1.00 15.14 ? 19   LEU B CA  1 
ATOM   3835 C  C   . LEU B 1 20  ? -5.728  -35.510 71.417  1.00 17.17 ? 19   LEU B C   1 
ATOM   3836 O  O   . LEU B 1 20  ? -6.590  -34.720 71.012  1.00 20.02 ? 19   LEU B O   1 
ATOM   3837 C  CB  . LEU B 1 20  ? -5.968  -35.703 73.899  1.00 13.89 ? 19   LEU B CB  1 
ATOM   3838 C  CG  . LEU B 1 20  ? -6.462  -36.531 75.088  1.00 15.33 ? 19   LEU B CG  1 
ATOM   3839 C  CD1 . LEU B 1 20  ? -6.296  -35.778 76.398  1.00 16.47 ? 19   LEU B CD1 1 
ATOM   3840 C  CD2 . LEU B 1 20  ? -7.921  -36.942 74.899  1.00 18.23 ? 19   LEU B CD2 1 
ATOM   3841 N  N   . LEU B 1 21  ? -4.512  -35.578 70.879  1.00 15.59 ? 20   LEU B N   1 
ATOM   3842 C  CA  . LEU B 1 21  ? -4.132  -34.751 69.740  1.00 15.63 ? 20   LEU B CA  1 
ATOM   3843 C  C   . LEU B 1 21  ? -4.420  -35.419 68.403  1.00 16.38 ? 20   LEU B C   1 
ATOM   3844 O  O   . LEU B 1 21  ? -4.111  -34.835 67.359  1.00 15.69 ? 20   LEU B O   1 
ATOM   3845 C  CB  . LEU B 1 21  ? -2.645  -34.389 69.819  1.00 16.74 ? 20   LEU B CB  1 
ATOM   3846 C  CG  . LEU B 1 21  ? -2.190  -33.662 71.086  1.00 18.17 ? 20   LEU B CG  1 
ATOM   3847 C  CD1 . LEU B 1 21  ? -0.675  -33.496 71.073  1.00 19.89 ? 20   LEU B CD1 1 
ATOM   3848 C  CD2 . LEU B 1 21  ? -2.887  -32.322 71.220  1.00 22.51 ? 20   LEU B CD2 1 
ATOM   3849 N  N   . ASN B 1 22  ? -4.983  -36.628 68.402  1.00 16.82 ? 21   ASN B N   1 
ATOM   3850 C  CA  . ASN B 1 22  ? -5.316  -37.319 67.155  1.00 15.97 ? 21   ASN B CA  1 
ATOM   3851 C  C   . ASN B 1 22  ? -6.679  -36.821 66.673  1.00 16.24 ? 21   ASN B C   1 
ATOM   3852 O  O   . ASN B 1 22  ? -7.709  -37.497 66.765  1.00 17.34 ? 21   ASN B O   1 
ATOM   3853 C  CB  . ASN B 1 22  ? -5.289  -38.831 67.344  1.00 17.83 ? 21   ASN B CB  1 
ATOM   3854 C  CG  . ASN B 1 22  ? -5.514  -39.587 66.035  1.00 24.01 ? 21   ASN B CG  1 
ATOM   3855 O  OD1 . ASN B 1 22  ? -5.503  -39.001 64.947  1.00 25.13 ? 21   ASN B OD1 1 
ATOM   3856 N  ND2 . ASN B 1 22  ? -5.710  -40.893 66.137  1.00 28.44 ? 21   ASN B ND2 1 
ATOM   3857 N  N   . THR B 1 23  ? -6.665  -35.589 66.170  1.00 13.76 ? 22   THR B N   1 
ATOM   3858 C  CA  . THR B 1 23  ? -7.859  -34.892 65.707  1.00 16.17 ? 22   THR B CA  1 
ATOM   3859 C  C   . THR B 1 23  ? -7.423  -33.821 64.720  1.00 17.14 ? 22   THR B C   1 
ATOM   3860 O  O   . THR B 1 23  ? -6.297  -33.326 64.789  1.00 18.30 ? 22   THR B O   1 
ATOM   3861 C  CB  . THR B 1 23  ? -8.643  -34.247 66.861  1.00 17.99 ? 22   THR B CB  1 
ATOM   3862 O  OG1 . THR B 1 23  ? -9.653  -33.381 66.321  1.00 20.77 ? 22   THR B OG1 1 
ATOM   3863 C  CG2 . THR B 1 23  ? -7.716  -33.417 67.767  1.00 16.50 ? 22   THR B CG2 1 
ATOM   3864 N  N   . ASP B 1 24  ? -8.320  -33.461 63.797  1.00 19.00 ? 23   ASP B N   1 
ATOM   3865 C  CA  . ASP B 1 24  ? -7.968  -32.374 62.893  1.00 21.93 ? 23   ASP B CA  1 
ATOM   3866 C  C   . ASP B 1 24  ? -8.043  -31.002 63.552  1.00 16.42 ? 23   ASP B C   1 
ATOM   3867 O  O   . ASP B 1 24  ? -7.634  -30.021 62.924  1.00 16.74 ? 23   ASP B O   1 
ATOM   3868 C  CB  . ASP B 1 24  ? -8.846  -32.392 61.633  1.00 27.80 ? 23   ASP B CB  1 
ATOM   3869 C  CG  . ASP B 1 24  ? -10.330 -32.248 61.933  1.00 32.51 ? 23   ASP B CG  1 
ATOM   3870 O  OD1 . ASP B 1 24  ? -10.728 -32.385 63.104  1.00 35.86 ? 23   ASP B OD1 1 
ATOM   3871 O  OD2 . ASP B 1 24  ? -11.104 -31.998 60.985  1.00 40.06 ? 23   ASP B OD2 1 
ATOM   3872 N  N   . LYS B 1 25  ? -8.521  -30.907 64.798  1.00 16.00 ? 24   LYS B N   1 
ATOM   3873 C  CA  . LYS B 1 25  ? -8.707  -29.628 65.491  1.00 13.13 ? 24   LYS B CA  1 
ATOM   3874 C  C   . LYS B 1 25  ? -8.142  -29.725 66.904  1.00 11.54 ? 24   LYS B C   1 
ATOM   3875 O  O   . LYS B 1 25  ? -8.884  -29.654 67.896  1.00 13.27 ? 24   LYS B O   1 
ATOM   3876 C  CB  . LYS B 1 25  ? -10.185 -29.224 65.512  1.00 14.40 ? 24   LYS B CB  1 
ATOM   3877 C  CG  . LYS B 1 25  ? -10.750 -28.971 64.117  1.00 16.89 ? 24   LYS B CG  1 
ATOM   3878 C  CD  . LYS B 1 25  ? -12.244 -28.622 64.131  1.00 18.02 ? 24   LYS B CD  1 
ATOM   3879 C  CE  . LYS B 1 25  ? -12.766 -28.343 62.707  1.00 17.60 ? 24   LYS B CE  1 
ATOM   3880 N  NZ  . LYS B 1 25  ? -14.216 -27.965 62.694  1.00 20.18 ? 24   LYS B NZ  1 
ATOM   3881 N  N   . PRO B 1 26  ? -6.816  -29.847 67.031  1.00 11.63 ? 25   PRO B N   1 
ATOM   3882 C  CA  . PRO B 1 26  ? -6.233  -30.081 68.365  1.00 13.34 ? 25   PRO B CA  1 
ATOM   3883 C  C   . PRO B 1 26  ? -6.288  -28.876 69.293  1.00 11.19 ? 25   PRO B C   1 
ATOM   3884 O  O   . PRO B 1 26  ? -6.486  -29.054 70.502  1.00 12.06 ? 25   PRO B O   1 
ATOM   3885 C  CB  . PRO B 1 26  ? -4.788  -30.492 68.051  1.00 14.59 ? 25   PRO B CB  1 
ATOM   3886 C  CG  . PRO B 1 26  ? -4.519  -29.953 66.646  1.00 13.21 ? 25   PRO B CG  1 
ATOM   3887 C  CD  . PRO B 1 26  ? -5.839  -30.052 65.945  1.00 11.57 ? 25   PRO B CD  1 
ATOM   3888 N  N   . VAL B 1 27  ? -6.074  -27.656 68.789  1.00 12.54 ? 26   VAL B N   1 
ATOM   3889 C  CA  . VAL B 1 27  ? -6.177  -26.494 69.671  1.00 11.75 ? 26   VAL B CA  1 
ATOM   3890 C  C   . VAL B 1 27  ? -7.589  -26.380 70.221  1.00 12.01 ? 26   VAL B C   1 
ATOM   3891 O  O   . VAL B 1 27  ? -7.792  -26.098 71.407  1.00 13.87 ? 26   VAL B O   1 
ATOM   3892 C  CB  . VAL B 1 27  ? -5.752  -25.207 68.938  1.00 11.50 ? 26   VAL B CB  1 
ATOM   3893 C  CG1 . VAL B 1 27  ? -6.081  -23.966 69.798  1.00 13.94 ? 26   VAL B CG1 1 
ATOM   3894 C  CG2 . VAL B 1 27  ? -4.254  -25.252 68.617  1.00 14.04 ? 26   VAL B CG2 1 
ATOM   3895 N  N   . GLN B 1 28  ? -8.592  -26.595 69.373  1.00 11.38 ? 27   GLN B N   1 
ATOM   3896 C  CA  . GLN B 1 28  ? -9.959  -26.521 69.873  1.00 11.77 ? 27   GLN B CA  1 
ATOM   3897 C  C   . GLN B 1 28  ? -10.249 -27.636 70.875  1.00 13.55 ? 27   GLN B C   1 
ATOM   3898 O  O   . GLN B 1 28  ? -10.991 -27.412 71.839  1.00 12.84 ? 27   GLN B O   1 
ATOM   3899 C  CB  . GLN B 1 28  ? -10.937 -26.537 68.697  1.00 13.17 ? 27   GLN B CB  1 
ATOM   3900 C  CG  . GLN B 1 28  ? -10.845 -25.238 67.885  1.00 13.24 ? 27   GLN B CG  1 
ATOM   3901 C  CD  . GLN B 1 28  ? -11.464 -25.339 66.507  1.00 12.45 ? 27   GLN B CD  1 
ATOM   3902 O  OE1 . GLN B 1 28  ? -12.669 -25.155 66.343  1.00 14.72 ? 27   GLN B OE1 1 
ATOM   3903 N  NE2 . GLN B 1 28  ? -10.635 -25.620 65.503  1.00 12.81 ? 27   GLN B NE2 1 
ATOM   3904 N  N   . ALA B 1 29  ? -9.660  -28.827 70.685  1.00 13.67 ? 28   ALA B N   1 
ATOM   3905 C  CA  . ALA B 1 29  ? -9.794  -29.885 71.684  1.00 13.63 ? 28   ALA B CA  1 
ATOM   3906 C  C   . ALA B 1 29  ? -9.183  -29.463 73.014  1.00 14.42 ? 28   ALA B C   1 
ATOM   3907 O  O   . ALA B 1 29  ? -9.750  -29.729 74.084  1.00 13.92 ? 28   ALA B O   1 
ATOM   3908 C  CB  . ALA B 1 29  ? -9.139  -31.180 71.184  1.00 12.77 ? 28   ALA B CB  1 
ATOM   3909 N  N   . LEU B 1 30  ? -8.012  -28.822 72.969  1.00 12.72 ? 29   LEU B N   1 
ATOM   3910 C  CA  . LEU B 1 30  ? -7.364  -28.378 74.201  1.00 11.31 ? 29   LEU B CA  1 
ATOM   3911 C  C   . LEU B 1 30  ? -8.170  -27.281 74.886  1.00 13.15 ? 29   LEU B C   1 
ATOM   3912 O  O   . LEU B 1 30  ? -8.205  -27.215 76.124  1.00 13.68 ? 29   LEU B O   1 
ATOM   3913 C  CB  . LEU B 1 30  ? -5.939  -27.899 73.893  1.00 10.88 ? 29   LEU B CB  1 
ATOM   3914 C  CG  . LEU B 1 30  ? -4.935  -29.013 73.563  1.00 11.60 ? 29   LEU B CG  1 
ATOM   3915 C  CD1 . LEU B 1 30  ? -3.714  -28.485 72.784  1.00 12.02 ? 29   LEU B CD1 1 
ATOM   3916 C  CD2 . LEU B 1 30  ? -4.504  -29.766 74.847  1.00 13.94 ? 29   LEU B CD2 1 
ATOM   3917 N  N   . MET B 1 31  ? -8.827  -26.416 74.107  1.00 13.11 ? 30   MET B N   1 
ATOM   3918 C  CA  . MET B 1 31  ? -9.693  -25.406 74.713  1.00 13.31 ? 30   MET B CA  1 
ATOM   3919 C  C   . MET B 1 31  ? -10.810 -26.053 75.524  1.00 13.79 ? 30   MET B C   1 
ATOM   3920 O  O   . MET B 1 31  ? -11.118 -25.607 76.639  1.00 15.02 ? 30   MET B O   1 
ATOM   3921 C  CB  . MET B 1 31  ? -10.267 -24.484 73.631  1.00 13.57 ? 30   MET B CB  1 
ATOM   3922 C  CG  . MET B 1 31  ? -9.204  -23.609 72.977  1.00 13.91 ? 30   MET B CG  1 
ATOM   3923 S  SD  . MET B 1 31  ? -9.816  -22.672 71.553  1.00 15.02 ? 30   MET B SD  1 
ATOM   3924 C  CE  . MET B 1 31  ? -11.163 -21.737 72.283  1.00 16.68 ? 30   MET B CE  1 
ATOM   3925 N  N   . LYS B 1 32  ? -11.425 -27.114 74.985  1.00 15.40 ? 31   LYS B N   1 
ATOM   3926 C  CA  . LYS B 1 32  ? -12.504 -27.791 75.700  1.00 15.59 ? 31   LYS B CA  1 
ATOM   3927 C  C   . LYS B 1 32  ? -11.992 -28.460 76.970  1.00 15.20 ? 31   LYS B C   1 
ATOM   3928 O  O   . LYS B 1 32  ? -12.680 -28.459 77.997  1.00 14.89 ? 31   LYS B O   1 
ATOM   3929 C  CB  . LYS B 1 32  ? -13.182 -28.809 74.785  1.00 19.13 ? 31   LYS B CB  1 
ATOM   3930 C  CG  . LYS B 1 32  ? -13.987 -28.159 73.664  1.00 28.35 ? 31   LYS B CG  1 
ATOM   3931 C  CD  . LYS B 1 32  ? -14.596 -29.195 72.722  1.00 36.34 ? 31   LYS B CD  1 
ATOM   3932 C  CE  . LYS B 1 32  ? -15.205 -28.536 71.489  1.00 42.01 ? 31   LYS B CE  1 
ATOM   3933 N  NZ  . LYS B 1 32  ? -16.318 -27.602 71.837  1.00 45.54 ? 31   LYS B NZ  1 
ATOM   3934 N  N   . ILE B 1 33  ? -10.784 -29.029 76.921  1.00 15.15 ? 32   ILE B N   1 
ATOM   3935 C  CA  . ILE B 1 33  ? -10.185 -29.593 78.127  1.00 14.05 ? 32   ILE B CA  1 
ATOM   3936 C  C   . ILE B 1 33  ? -9.954  -28.498 79.163  1.00 13.66 ? 32   ILE B C   1 
ATOM   3937 O  O   . ILE B 1 33  ? -10.253 -28.673 80.352  1.00 16.57 ? 32   ILE B O   1 
ATOM   3938 C  CB  . ILE B 1 33  ? -8.881  -30.335 77.775  1.00 14.25 ? 32   ILE B CB  1 
ATOM   3939 C  CG1 . ILE B 1 33  ? -9.191  -31.556 76.902  1.00 16.56 ? 32   ILE B CG1 1 
ATOM   3940 C  CG2 . ILE B 1 33  ? -8.126  -30.722 79.047  1.00 14.09 ? 32   ILE B CG2 1 
ATOM   3941 C  CD1 . ILE B 1 33  ? -7.977  -32.136 76.217  1.00 16.91 ? 32   ILE B CD1 1 
ATOM   3942 N  N   . ALA B 1 34  ? -9.458  -27.336 78.726  1.00 14.69 ? 33   ALA B N   1 
ATOM   3943 C  CA  . ALA B 1 34  ? -9.253  -26.230 79.657  1.00 12.14 ? 33   ALA B CA  1 
ATOM   3944 C  C   . ALA B 1 34  ? -10.572 -25.784 80.279  1.00 13.90 ? 33   ALA B C   1 
ATOM   3945 O  O   . ALA B 1 34  ? -10.624 -25.445 81.470  1.00 15.96 ? 33   ALA B O   1 
ATOM   3946 C  CB  . ALA B 1 34  ? -8.560  -25.065 78.951  1.00 12.72 ? 33   ALA B CB  1 
ATOM   3947 N  N   . ASP B 1 35  ? -11.655 -25.788 79.498  1.00 15.43 ? 34   ASP B N   1 
ATOM   3948 C  CA  . ASP B 1 35  ? -12.952 -25.439 80.069  1.00 17.02 ? 34   ASP B CA  1 
ATOM   3949 C  C   . ASP B 1 35  ? -13.358 -26.418 81.165  1.00 17.72 ? 34   ASP B C   1 
ATOM   3950 O  O   . ASP B 1 35  ? -13.992 -26.024 82.150  1.00 19.76 ? 34   ASP B O   1 
ATOM   3951 C  CB  . ASP B 1 35  ? -14.017 -25.390 78.976  1.00 22.40 ? 34   ASP B CB  1 
ATOM   3952 C  CG  . ASP B 1 35  ? -13.977 -24.107 78.185  1.00 25.96 ? 34   ASP B CG  1 
ATOM   3953 O  OD1 . ASP B 1 35  ? -13.361 -23.125 78.661  1.00 27.07 ? 34   ASP B OD1 1 
ATOM   3954 O  OD2 . ASP B 1 35  ? -14.571 -24.068 77.093  1.00 28.40 ? 34   ASP B OD2 1 
ATOM   3955 N  N   . GLU B 1 36  ? -13.024 -27.700 81.003  1.00 17.25 ? 35   GLU B N   1 
ATOM   3956 C  CA  A GLU B 1 36  ? -13.383 -28.700 82.004  0.70 17.47 ? 35   GLU B CA  1 
ATOM   3957 C  CA  B GLU B 1 36  ? -13.394 -28.688 82.011  0.30 17.95 ? 35   GLU B CA  1 
ATOM   3958 C  C   . GLU B 1 36  ? -12.461 -28.647 83.217  1.00 18.38 ? 35   GLU B C   1 
ATOM   3959 O  O   . GLU B 1 36  ? -12.921 -28.777 84.359  1.00 19.99 ? 35   GLU B O   1 
ATOM   3960 C  CB  A GLU B 1 36  ? -13.346 -30.102 81.393  0.70 19.53 ? 35   GLU B CB  1 
ATOM   3961 C  CB  B GLU B 1 36  ? -13.397 -30.094 81.403  0.30 18.24 ? 35   GLU B CB  1 
ATOM   3962 C  CG  A GLU B 1 36  ? -14.409 -30.380 80.347  0.70 26.17 ? 35   GLU B CG  1 
ATOM   3963 C  CG  B GLU B 1 36  ? -13.657 -31.200 82.425  0.30 19.64 ? 35   GLU B CG  1 
ATOM   3964 C  CD  A GLU B 1 36  ? -14.464 -31.845 79.940  0.70 32.47 ? 35   GLU B CD  1 
ATOM   3965 C  CD  B GLU B 1 36  ? -13.544 -32.598 81.838  0.30 24.24 ? 35   GLU B CD  1 
ATOM   3966 O  OE1 A GLU B 1 36  ? -13.489 -32.579 80.216  0.70 35.03 ? 35   GLU B OE1 1 
ATOM   3967 O  OE1 B GLU B 1 36  ? -13.610 -32.740 80.600  0.30 25.14 ? 35   GLU B OE1 1 
ATOM   3968 O  OE2 A GLU B 1 36  ? -15.485 -32.269 79.355  0.70 33.31 ? 35   GLU B OE2 1 
ATOM   3969 O  OE2 B GLU B 1 36  ? -13.389 -33.561 82.622  0.30 27.40 ? 35   GLU B OE2 1 
ATOM   3970 N  N   . LEU B 1 37  ? -11.158 -28.464 82.993  1.00 15.58 ? 36   LEU B N   1 
ATOM   3971 C  CA  . LEU B 1 37  ? -10.186 -28.632 84.068  1.00 15.34 ? 36   LEU B CA  1 
ATOM   3972 C  C   . LEU B 1 37  ? -9.721  -27.337 84.726  1.00 15.99 ? 36   LEU B C   1 
ATOM   3973 O  O   . LEU B 1 37  ? -9.223  -27.395 85.856  1.00 17.78 ? 36   LEU B O   1 
ATOM   3974 C  CB  . LEU B 1 37  ? -8.959  -29.397 83.550  1.00 15.18 ? 36   LEU B CB  1 
ATOM   3975 C  CG  . LEU B 1 37  ? -9.247  -30.817 83.049  1.00 14.15 ? 36   LEU B CG  1 
ATOM   3976 C  CD1 . LEU B 1 37  ? -7.947  -31.519 82.668  1.00 16.04 ? 36   LEU B CD1 1 
ATOM   3977 C  CD2 . LEU B 1 37  ? -10.021 -31.628 84.094  1.00 16.66 ? 36   LEU B CD2 1 
ATOM   3978 N  N   . GLY B 1 38  ? -9.848  -26.187 84.081  1.00 15.58 ? 37   GLY B N   1 
ATOM   3979 C  CA  . GLY B 1 38  ? -9.501  -24.924 84.711  1.00 17.71 ? 37   GLY B CA  1 
ATOM   3980 C  C   . GLY B 1 38  ? -8.205  -24.310 84.206  1.00 17.45 ? 37   GLY B C   1 
ATOM   3981 O  O   . GLY B 1 38  ? -7.748  -24.561 83.087  1.00 17.85 ? 37   GLY B O   1 
ATOM   3982 N  N   . GLU B 1 39  ? -7.592  -23.496 85.076  1.00 14.96 ? 38   GLU B N   1 
ATOM   3983 C  CA  . GLU B 1 39  ? -6.520  -22.592 84.661  1.00 14.70 ? 38   GLU B CA  1 
ATOM   3984 C  C   . GLU B 1 39  ? -5.207  -23.302 84.356  1.00 14.36 ? 38   GLU B C   1 
ATOM   3985 O  O   . GLU B 1 39  ? -4.326  -22.689 83.740  1.00 14.35 ? 38   GLU B O   1 
ATOM   3986 C  CB  . GLU B 1 39  ? -6.273  -21.526 85.737  1.00 16.25 ? 38   GLU B CB  1 
ATOM   3987 C  CG  . GLU B 1 39  ? -5.796  -22.081 87.079  1.00 16.05 ? 38   GLU B CG  1 
ATOM   3988 C  CD  . GLU B 1 39  ? -5.543  -20.995 88.121  1.00 19.74 ? 38   GLU B CD  1 
ATOM   3989 O  OE1 . GLU B 1 39  ? -5.441  -19.800 87.759  1.00 21.01 ? 38   GLU B OE1 1 
ATOM   3990 O  OE2 . GLU B 1 39  ? -5.454  -21.345 89.320  1.00 23.87 ? 38   GLU B OE2 1 
ATOM   3991 N  N   . ILE B 1 40  ? -5.038  -24.554 84.783  1.00 14.16 ? 39   ILE B N   1 
ATOM   3992 C  CA  . ILE B 1 40  ? -3.782  -25.268 84.558  1.00 12.96 ? 39   ILE B CA  1 
ATOM   3993 C  C   . ILE B 1 40  ? -4.069  -26.762 84.498  1.00 15.77 ? 39   ILE B C   1 
ATOM   3994 O  O   . ILE B 1 40  ? -4.808  -27.295 85.332  1.00 16.68 ? 39   ILE B O   1 
ATOM   3995 C  CB  . ILE B 1 40  ? -2.739  -24.959 85.654  1.00 13.25 ? 39   ILE B CB  1 
ATOM   3996 C  CG1 . ILE B 1 40  ? -1.406  -25.653 85.343  1.00 14.52 ? 39   ILE B CG1 1 
ATOM   3997 C  CG2 . ILE B 1 40  ? -3.256  -25.344 87.047  1.00 15.96 ? 39   ILE B CG2 1 
ATOM   3998 C  CD1 . ILE B 1 40  ? -0.221  -25.094 86.146  1.00 17.29 ? 39   ILE B CD1 1 
ATOM   3999 N  N   . PHE B 1 41  ? -3.493  -27.445 83.512  1.00 14.51 ? 40   PHE B N   1 
ATOM   4000 C  CA  . PHE B 1 41  ? -3.527  -28.902 83.534  1.00 14.74 ? 40   PHE B CA  1 
ATOM   4001 C  C   . PHE B 1 41  ? -2.237  -29.473 82.961  1.00 16.08 ? 40   PHE B C   1 
ATOM   4002 O  O   . PHE B 1 41  ? -1.571  -28.854 82.128  1.00 14.99 ? 40   PHE B O   1 
ATOM   4003 C  CB  . PHE B 1 41  ? -4.769  -29.482 82.809  1.00 12.71 ? 40   PHE B CB  1 
ATOM   4004 C  CG  . PHE B 1 41  ? -4.859  -29.159 81.338  1.00 12.74 ? 40   PHE B CG  1 
ATOM   4005 C  CD1 . PHE B 1 41  ? -4.264  -29.978 80.391  1.00 12.88 ? 40   PHE B CD1 1 
ATOM   4006 C  CD2 . PHE B 1 41  ? -5.597  -28.062 80.900  1.00 12.61 ? 40   PHE B CD2 1 
ATOM   4007 C  CE1 . PHE B 1 41  ? -4.369  -29.686 79.030  1.00 12.34 ? 40   PHE B CE1 1 
ATOM   4008 C  CE2 . PHE B 1 41  ? -5.698  -27.764 79.540  1.00 13.48 ? 40   PHE B CE2 1 
ATOM   4009 C  CZ  . PHE B 1 41  ? -5.085  -28.581 78.605  1.00 12.44 ? 40   PHE B CZ  1 
ATOM   4010 N  N   . LYS B 1 42  ? -1.886  -30.655 83.457  1.00 15.36 ? 41   LYS B N   1 
ATOM   4011 C  CA  . LYS B 1 42  ? -0.711  -31.387 83.012  1.00 15.62 ? 41   LYS B CA  1 
ATOM   4012 C  C   . LYS B 1 42  ? -1.058  -32.208 81.779  1.00 16.46 ? 41   LYS B C   1 
ATOM   4013 O  O   . LYS B 1 42  ? -2.165  -32.743 81.672  1.00 15.82 ? 41   LYS B O   1 
ATOM   4014 C  CB  . LYS B 1 42  ? -0.222  -32.294 84.148  1.00 17.66 ? 41   LYS B CB  1 
ATOM   4015 C  CG  . LYS B 1 42  ? 0.878   -33.264 83.816  1.00 21.65 ? 41   LYS B CG  1 
ATOM   4016 C  CD  . LYS B 1 42  ? 1.241   -34.051 85.076  1.00 27.57 ? 41   LYS B CD  1 
ATOM   4017 C  CE  . LYS B 1 42  ? 2.270   -35.120 84.788  1.00 34.24 ? 41   LYS B CE  1 
ATOM   4018 N  NZ  . LYS B 1 42  ? 2.756   -35.769 86.038  1.00 37.83 ? 41   LYS B NZ  1 
ATOM   4019 N  N   . PHE B 1 43  ? -0.116  -32.293 80.837  1.00 14.73 ? 42   PHE B N   1 
ATOM   4020 C  CA  . PHE B 1 43  ? -0.305  -33.052 79.603  1.00 14.20 ? 42   PHE B CA  1 
ATOM   4021 C  C   . PHE B 1 43  ? 0.950   -33.874 79.354  1.00 14.00 ? 42   PHE B C   1 
ATOM   4022 O  O   . PHE B 1 43  ? 2.048   -33.317 79.235  1.00 14.58 ? 42   PHE B O   1 
ATOM   4023 C  CB  . PHE B 1 43  ? -0.593  -32.113 78.420  1.00 13.88 ? 42   PHE B CB  1 
ATOM   4024 C  CG  . PHE B 1 43  ? -1.027  -32.819 77.162  1.00 16.46 ? 42   PHE B CG  1 
ATOM   4025 C  CD1 . PHE B 1 43  ? -0.091  -33.407 76.313  1.00 17.52 ? 42   PHE B CD1 1 
ATOM   4026 C  CD2 . PHE B 1 43  ? -2.367  -32.876 76.814  1.00 16.26 ? 42   PHE B CD2 1 
ATOM   4027 C  CE1 . PHE B 1 43  ? -0.496  -34.057 75.139  1.00 19.83 ? 42   PHE B CE1 1 
ATOM   4028 C  CE2 . PHE B 1 43  ? -2.781  -33.514 75.645  1.00 16.93 ? 42   PHE B CE2 1 
ATOM   4029 C  CZ  . PHE B 1 43  ? -1.848  -34.106 74.809  1.00 18.85 ? 42   PHE B CZ  1 
ATOM   4030 N  N   . GLU B 1 44  ? 0.795   -35.190 79.275  1.00 15.04 ? 43   GLU B N   1 
ATOM   4031 C  CA  . GLU B 1 44  ? 1.922   -36.102 79.140  1.00 16.47 ? 43   GLU B CA  1 
ATOM   4032 C  C   . GLU B 1 44  ? 1.848   -36.860 77.825  1.00 16.75 ? 43   GLU B C   1 
ATOM   4033 O  O   . GLU B 1 44  ? 0.773   -37.289 77.405  1.00 17.56 ? 43   GLU B O   1 
ATOM   4034 C  CB  . GLU B 1 44  ? 1.955   -37.129 80.275  1.00 19.96 ? 43   GLU B CB  1 
ATOM   4035 C  CG  . GLU B 1 44  ? 2.153   -36.568 81.647  1.00 25.04 ? 43   GLU B CG  1 
ATOM   4036 C  CD  . GLU B 1 44  ? 2.332   -37.668 82.667  1.00 31.05 ? 43   GLU B CD  1 
ATOM   4037 O  OE1 . GLU B 1 44  ? 1.420   -38.507 82.814  1.00 32.43 ? 43   GLU B OE1 1 
ATOM   4038 O  OE2 . GLU B 1 44  ? 3.397   -37.707 83.304  1.00 34.07 ? 43   GLU B OE2 1 
ATOM   4039 N  N   . ALA B 1 45  ? 2.999   -37.037 77.194  1.00 16.16 ? 44   ALA B N   1 
ATOM   4040 C  CA  . ALA B 1 45  ? 3.182   -37.978 76.103  1.00 17.13 ? 44   ALA B CA  1 
ATOM   4041 C  C   . ALA B 1 45  ? 4.382   -38.839 76.453  1.00 16.84 ? 44   ALA B C   1 
ATOM   4042 O  O   . ALA B 1 45  ? 5.141   -38.507 77.372  1.00 18.01 ? 44   ALA B O   1 
ATOM   4043 C  CB  . ALA B 1 45  ? 3.403   -37.259 74.765  1.00 17.76 ? 44   ALA B CB  1 
ATOM   4044 N  N   . PRO B 1 46  ? 4.578   -39.963 75.760  1.00 18.28 ? 45   PRO B N   1 
ATOM   4045 C  CA  . PRO B 1 46  ? 5.782   -40.758 76.020  1.00 19.85 ? 45   PRO B CA  1 
ATOM   4046 C  C   . PRO B 1 46  ? 7.018   -39.885 75.911  1.00 22.99 ? 45   PRO B C   1 
ATOM   4047 O  O   . PRO B 1 46  ? 7.269   -39.285 74.861  1.00 23.51 ? 45   PRO B O   1 
ATOM   4048 C  CB  . PRO B 1 46  ? 5.739   -41.834 74.927  1.00 21.35 ? 45   PRO B CB  1 
ATOM   4049 C  CG  . PRO B 1 46  ? 4.282   -41.969 74.612  1.00 21.24 ? 45   PRO B CG  1 
ATOM   4050 C  CD  . PRO B 1 46  ? 3.736   -40.567 74.713  1.00 19.36 ? 45   PRO B CD  1 
ATOM   4051 N  N   . GLY B 1 47  ? 7.760   -39.758 77.007  1.00 24.82 ? 46   GLY B N   1 
ATOM   4052 C  CA  . GLY B 1 47  ? 8.989   -38.995 77.023  1.00 24.76 ? 46   GLY B CA  1 
ATOM   4053 C  C   . GLY B 1 47  ? 8.862   -37.494 77.210  1.00 22.54 ? 46   GLY B C   1 
ATOM   4054 O  O   . GLY B 1 47  ? 9.888   -36.802 77.146  1.00 25.68 ? 46   GLY B O   1 
ATOM   4055 N  N   . ARG B 1 48  ? 7.661   -36.955 77.434  1.00 21.06 ? 47   ARG B N   1 
ATOM   4056 C  CA  . ARG B 1 48  ? 7.523   -35.508 77.554  1.00 22.32 ? 47   ARG B CA  1 
ATOM   4057 C  C   . ARG B 1 48  ? 6.360   -35.134 78.462  1.00 20.26 ? 47   ARG B C   1 
ATOM   4058 O  O   . ARG B 1 48  ? 5.350   -35.839 78.534  1.00 21.44 ? 47   ARG B O   1 
ATOM   4059 C  CB  . ARG B 1 48  ? 7.330   -34.835 76.190  1.00 27.17 ? 47   ARG B CB  1 
ATOM   4060 C  CG  . ARG B 1 48  ? 7.112   -33.322 76.301  1.00 31.06 ? 47   ARG B CG  1 
ATOM   4061 C  CD  . ARG B 1 48  ? 6.919   -32.653 74.942  1.00 29.15 ? 47   ARG B CD  1 
ATOM   4062 N  NE  . ARG B 1 48  ? 6.472   -31.264 75.055  1.00 25.67 ? 47   ARG B NE  1 
ATOM   4063 C  CZ  . ARG B 1 48  ? 5.894   -30.592 74.066  1.00 26.76 ? 47   ARG B CZ  1 
ATOM   4064 N  NH1 . ARG B 1 48  ? 5.678   -31.155 72.887  1.00 29.37 ? 47   ARG B NH1 1 
ATOM   4065 N  NH2 . ARG B 1 48  ? 5.514   -29.330 74.267  1.00 21.58 ? 47   ARG B NH2 1 
ATOM   4066 N  N   . VAL B 1 49  ? 6.511   -33.998 79.144  1.00 19.25 ? 48   VAL B N   1 
ATOM   4067 C  CA  . VAL B 1 49  ? 5.438   -33.417 79.946  1.00 19.52 ? 48   VAL B CA  1 
ATOM   4068 C  C   . VAL B 1 49  ? 5.416   -31.910 79.720  1.00 17.42 ? 48   VAL B C   1 
ATOM   4069 O  O   . VAL B 1 49  ? 6.466   -31.266 79.601  1.00 18.42 ? 48   VAL B O   1 
ATOM   4070 C  CB  . VAL B 1 49  ? 5.591   -33.748 81.446  1.00 23.90 ? 48   VAL B CB  1 
ATOM   4071 C  CG1 . VAL B 1 49  ? 6.926   -33.260 81.973  1.00 29.48 ? 48   VAL B CG1 1 
ATOM   4072 C  CG2 . VAL B 1 49  ? 4.453   -33.128 82.244  1.00 25.16 ? 48   VAL B CG2 1 
ATOM   4073 N  N   . THR B 1 50  ? 4.215   -31.347 79.656  1.00 14.78 ? 49   THR B N   1 
ATOM   4074 C  CA  . THR B 1 50  ? 4.042   -29.903 79.627  1.00 15.46 ? 49   THR B CA  1 
ATOM   4075 C  C   . THR B 1 50  ? 2.816   -29.546 80.458  1.00 14.85 ? 49   THR B C   1 
ATOM   4076 O  O   . THR B 1 50  ? 2.084   -30.420 80.930  1.00 18.03 ? 49   THR B O   1 
ATOM   4077 C  CB  . THR B 1 50  ? 3.934   -29.380 78.183  1.00 16.97 ? 49   THR B CB  1 
ATOM   4078 O  OG1 . THR B 1 50  ? 4.111   -27.957 78.170  1.00 16.65 ? 49   THR B OG1 1 
ATOM   4079 C  CG2 . THR B 1 50  ? 2.579   -29.740 77.552  1.00 15.64 ? 49   THR B CG2 1 
ATOM   4080 N  N   . ARG B 1 51  ? 2.608   -28.245 80.660  1.00 13.85 ? 50   ARG B N   1 
ATOM   4081 C  CA  . ARG B 1 51  ? 1.486   -27.739 81.445  1.00 14.41 ? 50   ARG B CA  1 
ATOM   4082 C  C   . ARG B 1 51  ? 0.796   -26.629 80.669  1.00 13.95 ? 50   ARG B C   1 
ATOM   4083 O  O   . ARG B 1 51  ? 1.446   -25.656 80.272  1.00 16.67 ? 50   ARG B O   1 
ATOM   4084 C  CB  . ARG B 1 51  ? 1.973   -27.230 82.813  1.00 14.86 ? 50   ARG B CB  1 
ATOM   4085 C  CG  . ARG B 1 51  ? 2.740   -28.279 83.594  1.00 16.42 ? 50   ARG B CG  1 
ATOM   4086 C  CD  . ARG B 1 51  ? 4.038   -27.731 84.159  1.00 16.34 ? 50   ARG B CD  1 
ATOM   4087 N  NE  . ARG B 1 51  ? 4.855   -28.796 84.734  1.00 18.65 ? 50   ARG B NE  1 
ATOM   4088 C  CZ  . ARG B 1 51  ? 5.848   -29.410 84.104  1.00 19.08 ? 50   ARG B CZ  1 
ATOM   4089 N  NH1 . ARG B 1 51  ? 6.237   -29.037 82.886  1.00 18.80 ? 50   ARG B NH1 1 
ATOM   4090 N  NH2 . ARG B 1 51  ? 6.475   -30.417 84.711  1.00 19.29 ? 50   ARG B NH2 1 
ATOM   4091 N  N   . TYR B 1 52  ? -0.514  -26.773 80.455  1.00 12.37 ? 51   TYR B N   1 
ATOM   4092 C  CA  . TYR B 1 52  ? -1.299  -25.795 79.707  1.00 13.00 ? 51   TYR B CA  1 
ATOM   4093 C  C   . TYR B 1 52  ? -1.905  -24.764 80.647  1.00 13.13 ? 51   TYR B C   1 
ATOM   4094 O  O   . TYR B 1 52  ? -2.603  -25.124 81.604  1.00 13.57 ? 51   TYR B O   1 
ATOM   4095 C  CB  . TYR B 1 52  ? -2.407  -26.484 78.903  1.00 10.33 ? 51   TYR B CB  1 
ATOM   4096 C  CG  . TYR B 1 52  ? -1.866  -27.168 77.671  1.00 11.72 ? 51   TYR B CG  1 
ATOM   4097 C  CD1 . TYR B 1 52  ? -1.351  -28.461 77.743  1.00 13.28 ? 51   TYR B CD1 1 
ATOM   4098 C  CD2 . TYR B 1 52  ? -1.844  -26.515 76.444  1.00 11.67 ? 51   TYR B CD2 1 
ATOM   4099 C  CE1 . TYR B 1 52  ? -0.841  -29.091 76.619  1.00 13.20 ? 51   TYR B CE1 1 
ATOM   4100 C  CE2 . TYR B 1 52  ? -1.330  -27.140 75.315  1.00 12.99 ? 51   TYR B CE2 1 
ATOM   4101 C  CZ  . TYR B 1 52  ? -0.834  -28.430 75.413  1.00 13.40 ? 51   TYR B CZ  1 
ATOM   4102 O  OH  . TYR B 1 52  ? -0.307  -29.067 74.309  1.00 14.44 ? 51   TYR B OH  1 
ATOM   4103 N  N   . LEU B 1 53  ? -1.647  -23.486 80.362  1.00 11.72 ? 52   LEU B N   1 
ATOM   4104 C  CA  . LEU B 1 53  ? -2.118  -22.369 81.172  1.00 11.39 ? 52   LEU B CA  1 
ATOM   4105 C  C   . LEU B 1 53  ? -3.220  -21.600 80.455  1.00 12.11 ? 52   LEU B C   1 
ATOM   4106 O  O   . LEU B 1 53  ? -3.111  -21.311 79.258  1.00 14.53 ? 52   LEU B O   1 
ATOM   4107 C  CB  . LEU B 1 53  ? -0.973  -21.408 81.492  1.00 13.00 ? 52   LEU B CB  1 
ATOM   4108 C  CG  . LEU B 1 53  ? 0.243   -21.992 82.201  1.00 15.02 ? 52   LEU B CG  1 
ATOM   4109 C  CD1 . LEU B 1 53  ? 1.226   -20.872 82.514  1.00 17.01 ? 52   LEU B CD1 1 
ATOM   4110 C  CD2 . LEU B 1 53  ? -0.178  -22.717 83.472  1.00 17.72 ? 52   LEU B CD2 1 
ATOM   4111 N  N   . SER B 1 54  ? -4.246  -21.204 81.211  1.00 11.97 ? 53   SER B N   1 
ATOM   4112 C  CA  . SER B 1 54  ? -5.421  -20.546 80.654  1.00 11.91 ? 53   SER B CA  1 
ATOM   4113 C  C   . SER B 1 54  ? -5.856  -19.281 81.387  1.00 11.94 ? 53   SER B C   1 
ATOM   4114 O  O   . SER B 1 54  ? -6.702  -18.553 80.855  1.00 13.96 ? 53   SER B O   1 
ATOM   4115 C  CB  . SER B 1 54  ? -6.612  -21.522 80.621  1.00 14.38 ? 53   SER B CB  1 
ATOM   4116 O  OG  . SER B 1 54  ? -6.421  -22.534 79.648  1.00 16.07 ? 53   SER B OG  1 
ATOM   4117 N  N   . SER B 1 55  ? -5.337  -19.000 82.582  1.00 12.86 ? 54   SER B N   1 
ATOM   4118 C  CA  . SER B 1 55  ? -5.762  -17.825 83.337  1.00 15.14 ? 54   SER B CA  1 
ATOM   4119 C  C   . SER B 1 55  ? -4.736  -16.698 83.247  1.00 15.72 ? 54   SER B C   1 
ATOM   4120 O  O   . SER B 1 55  ? -3.529  -16.933 83.153  1.00 16.15 ? 54   SER B O   1 
ATOM   4121 C  CB  . SER B 1 55  ? -6.004  -18.170 84.812  1.00 13.77 ? 54   SER B CB  1 
ATOM   4122 O  OG  . SER B 1 55  ? -4.785  -18.504 85.457  1.00 14.71 ? 54   SER B OG  1 
ATOM   4123 N  N   . GLN B 1 56  ? -5.235  -15.460 83.287  1.00 13.21 ? 55   GLN B N   1 
ATOM   4124 C  CA  . GLN B 1 56  ? -4.345  -14.304 83.361  1.00 12.75 ? 55   GLN B CA  1 
ATOM   4125 C  C   . GLN B 1 56  ? -3.480  -14.353 84.619  1.00 13.73 ? 55   GLN B C   1 
ATOM   4126 O  O   . GLN B 1 56  ? -2.312  -13.943 84.589  1.00 13.90 ? 55   GLN B O   1 
ATOM   4127 C  CB  . GLN B 1 56  ? -5.176  -13.013 83.310  1.00 13.32 ? 55   GLN B CB  1 
ATOM   4128 C  CG  . GLN B 1 56  ? -4.374  -11.728 83.102  1.00 15.04 ? 55   GLN B CG  1 
ATOM   4129 C  CD  . GLN B 1 56  ? -3.878  -11.125 84.408  1.00 17.73 ? 55   GLN B CD  1 
ATOM   4130 O  OE1 . GLN B 1 56  ? -4.245  -11.580 85.494  1.00 18.64 ? 55   GLN B OE1 1 
ATOM   4131 N  NE2 . GLN B 1 56  ? -3.032  -10.101 84.307  1.00 19.23 ? 55   GLN B NE2 1 
ATOM   4132 N  N   . ARG B 1 57  ? -4.021  -14.870 85.724  1.00 14.22 ? 56   ARG B N   1 
ATOM   4133 C  CA  . ARG B 1 57  ? -3.256  -14.927 86.971  1.00 16.83 ? 56   ARG B CA  1 
ATOM   4134 C  C   . ARG B 1 57  ? -1.950  -15.697 86.789  1.00 15.64 ? 56   ARG B C   1 
ATOM   4135 O  O   . ARG B 1 57  ? -0.887  -15.266 87.263  1.00 16.55 ? 56   ARG B O   1 
ATOM   4136 C  CB  . ARG B 1 57  ? -4.113  -15.561 88.074  1.00 20.66 ? 56   ARG B CB  1 
ATOM   4137 C  CG  . ARG B 1 57  ? -3.371  -15.917 89.347  1.00 26.06 ? 56   ARG B CG  1 
ATOM   4138 C  CD  . ARG B 1 57  ? -4.291  -16.634 90.345  1.00 29.11 ? 56   ARG B CD  1 
ATOM   4139 N  NE  . ARG B 1 57  ? -4.199  -18.089 90.261  1.00 30.07 ? 56   ARG B NE  1 
ATOM   4140 C  CZ  . ARG B 1 57  ? -3.383  -18.830 91.003  1.00 27.33 ? 56   ARG B CZ  1 
ATOM   4141 N  NH1 . ARG B 1 57  ? -2.547  -18.281 91.867  1.00 24.84 ? 56   ARG B NH1 1 
ATOM   4142 N  NH2 . ARG B 1 57  ? -3.414  -20.156 90.881  1.00 27.46 ? 56   ARG B NH2 1 
ATOM   4143 N  N   . LEU B 1 58  ? -2.011  -16.853 86.115  1.00 14.82 ? 57   LEU B N   1 
ATOM   4144 C  CA  . LEU B 1 58  ? -0.803  -17.653 85.919  1.00 13.02 ? 57   LEU B CA  1 
ATOM   4145 C  C   . LEU B 1 58  ? -0.003  -17.196 84.701  1.00 14.10 ? 57   LEU B C   1 
ATOM   4146 O  O   . LEU B 1 58  ? 1.231   -17.235 84.716  1.00 14.42 ? 57   LEU B O   1 
ATOM   4147 C  CB  . LEU B 1 58  ? -1.161  -19.132 85.788  1.00 14.08 ? 57   LEU B CB  1 
ATOM   4148 C  CG  . LEU B 1 58  ? -1.775  -19.748 87.045  1.00 14.96 ? 57   LEU B CG  1 
ATOM   4149 C  CD1 . LEU B 1 58  ? -2.101  -21.227 86.832  1.00 16.52 ? 57   LEU B CD1 1 
ATOM   4150 C  CD2 . LEU B 1 58  ? -0.853  -19.549 88.261  1.00 16.56 ? 57   LEU B CD2 1 
ATOM   4151 N  N   . ILE B 1 59  ? -0.677  -16.774 83.631  1.00 14.43 ? 58   ILE B N   1 
ATOM   4152 C  CA  . ILE B 1 59  ? 0.065   -16.388 82.430  1.00 12.73 ? 58   ILE B CA  1 
ATOM   4153 C  C   . ILE B 1 59  ? 0.865   -15.106 82.662  1.00 14.29 ? 58   ILE B C   1 
ATOM   4154 O  O   . ILE B 1 59  ? 1.951   -14.936 82.088  1.00 15.02 ? 58   ILE B O   1 
ATOM   4155 C  CB  . ILE B 1 59  ? -0.905  -16.289 81.232  1.00 11.00 ? 58   ILE B CB  1 
ATOM   4156 C  CG1 . ILE B 1 59  ? -1.354  -17.702 80.827  1.00 12.07 ? 58   ILE B CG1 1 
ATOM   4157 C  CG2 . ILE B 1 59  ? -0.265  -15.552 80.051  1.00 11.10 ? 58   ILE B CG2 1 
ATOM   4158 C  CD1 . ILE B 1 59  ? -2.570  -17.750 79.935  1.00 12.17 ? 58   ILE B CD1 1 
ATOM   4159 N  N   . LYS B 1 60  ? 0.387   -14.199 83.522  1.00 15.59 ? 59   LYS B N   1 
ATOM   4160 C  CA  . LYS B 1 60  ? 1.208   -13.023 83.813  1.00 16.37 ? 59   LYS B CA  1 
ATOM   4161 C  C   . LYS B 1 60  ? 2.550   -13.410 84.441  1.00 15.43 ? 59   LYS B C   1 
ATOM   4162 O  O   . LYS B 1 60  ? 3.563   -12.739 84.200  1.00 15.64 ? 59   LYS B O   1 
ATOM   4163 C  CB  . LYS B 1 60  ? 0.456   -12.032 84.707  1.00 19.15 ? 59   LYS B CB  1 
ATOM   4164 C  CG  . LYS B 1 60  ? 0.247   -12.469 86.135  1.00 20.80 ? 59   LYS B CG  1 
ATOM   4165 C  CD  . LYS B 1 60  ? -0.351  -11.332 86.940  1.00 22.46 ? 59   LYS B CD  1 
ATOM   4166 C  CE  . LYS B 1 60  ? -0.569  -11.741 88.390  1.00 25.56 ? 59   LYS B CE  1 
ATOM   4167 N  NZ  . LYS B 1 60  ? -1.297  -10.670 89.131  1.00 30.69 ? 59   LYS B NZ  1 
ATOM   4168 N  N   . GLU B 1 61  ? 2.586   -14.480 85.245  1.00 15.00 ? 60   GLU B N   1 
ATOM   4169 C  CA  . GLU B 1 61  ? 3.862   -14.939 85.793  1.00 15.29 ? 60   GLU B CA  1 
ATOM   4170 C  C   . GLU B 1 61  ? 4.711   -15.609 84.717  1.00 15.82 ? 60   GLU B C   1 
ATOM   4171 O  O   . GLU B 1 61  ? 5.933   -15.409 84.662  1.00 18.22 ? 60   GLU B O   1 
ATOM   4172 C  CB  . GLU B 1 61  ? 3.631   -15.899 86.964  1.00 16.48 ? 60   GLU B CB  1 
ATOM   4173 C  CG  . GLU B 1 61  ? 3.063   -15.248 88.211  1.00 18.72 ? 60   GLU B CG  1 
ATOM   4174 C  CD  . GLU B 1 61  ? 3.050   -16.183 89.418  1.00 24.16 ? 60   GLU B CD  1 
ATOM   4175 O  OE1 . GLU B 1 61  ? 3.946   -17.054 89.524  1.00 23.98 ? 60   GLU B OE1 1 
ATOM   4176 O  OE2 . GLU B 1 61  ? 2.142   -16.044 90.265  1.00 27.74 ? 60   GLU B OE2 1 
ATOM   4177 N  N   . ALA B 1 62  ? 4.086   -16.417 83.861  1.00 15.80 ? 61   ALA B N   1 
ATOM   4178 C  CA  . ALA B 1 62  ? 4.824   -17.060 82.780  1.00 16.16 ? 61   ALA B CA  1 
ATOM   4179 C  C   . ALA B 1 62  ? 5.479   -16.034 81.859  1.00 15.82 ? 61   ALA B C   1 
ATOM   4180 O  O   . ALA B 1 62  ? 6.497   -16.337 81.220  1.00 15.12 ? 61   ALA B O   1 
ATOM   4181 C  CB  . ALA B 1 62  ? 3.889   -17.983 81.982  1.00 15.04 ? 61   ALA B CB  1 
ATOM   4182 N  N   . CYS B 1 63  ? 4.921   -14.823 81.783  1.00 16.31 ? 62   CYS B N   1 
ATOM   4183 C  CA  . CYS B 1 63  ? 5.428   -13.750 80.933  1.00 15.61 ? 62   CYS B CA  1 
ATOM   4184 C  C   . CYS B 1 63  ? 6.513   -12.907 81.598  1.00 14.99 ? 62   CYS B C   1 
ATOM   4185 O  O   . CYS B 1 63  ? 6.972   -11.922 80.997  1.00 13.84 ? 62   CYS B O   1 
ATOM   4186 C  CB  . CYS B 1 63  ? 4.275   -12.845 80.493  1.00 16.04 ? 62   CYS B CB  1 
ATOM   4187 S  SG  . CYS B 1 63  ? 3.189   -13.606 79.253  1.00 16.92 ? 62   CYS B SG  1 
ATOM   4188 N  N   . ASP B 1 64  ? 6.929   -13.262 82.814  1.00 14.39 ? 63   ASP B N   1 
ATOM   4189 C  CA  . ASP B 1 64  ? 8.054   -12.616 83.485  1.00 15.76 ? 63   ASP B CA  1 
ATOM   4190 C  C   . ASP B 1 64  ? 9.347   -13.142 82.875  1.00 15.81 ? 63   ASP B C   1 
ATOM   4191 O  O   . ASP B 1 64  ? 9.736   -14.288 83.123  1.00 15.87 ? 63   ASP B O   1 
ATOM   4192 C  CB  . ASP B 1 64  ? 7.976   -12.897 84.985  1.00 16.86 ? 63   ASP B CB  1 
ATOM   4193 C  CG  . ASP B 1 64  ? 9.137   -12.294 85.780  1.00 19.14 ? 63   ASP B CG  1 
ATOM   4194 O  OD1 . ASP B 1 64  ? 10.184  -11.931 85.202  1.00 20.41 ? 63   ASP B OD1 1 
ATOM   4195 O  OD2 . ASP B 1 64  ? 8.994   -12.194 87.018  1.00 20.22 ? 63   ASP B OD2 1 
ATOM   4196 N  N   . GLU B 1 65  ? 10.021  -12.309 82.077  1.00 14.44 ? 64   GLU B N   1 
ATOM   4197 C  CA  . GLU B 1 65  ? 11.196  -12.763 81.334  1.00 16.27 ? 64   GLU B CA  1 
ATOM   4198 C  C   . GLU B 1 65  ? 12.397  -13.066 82.222  1.00 16.73 ? 64   GLU B C   1 
ATOM   4199 O  O   . GLU B 1 65  ? 13.352  -13.690 81.745  1.00 17.41 ? 64   GLU B O   1 
ATOM   4200 C  CB  . GLU B 1 65  ? 11.591  -11.720 80.291  1.00 18.67 ? 64   GLU B CB  1 
ATOM   4201 C  CG  . GLU B 1 65  ? 10.541  -11.476 79.222  1.00 19.37 ? 64   GLU B CG  1 
ATOM   4202 C  CD  . GLU B 1 65  ? 10.962  -10.394 78.247  1.00 20.82 ? 64   GLU B CD  1 
ATOM   4203 O  OE1 . GLU B 1 65  ? 10.896  -9.195  78.604  1.00 26.83 ? 64   GLU B OE1 1 
ATOM   4204 O  OE2 . GLU B 1 65  ? 11.374  -10.744 77.126  1.00 15.43 ? 64   GLU B OE2 1 
ATOM   4205 N  N   . SER B 1 66  ? 12.397  -12.624 83.480  1.00 17.65 ? 65   SER B N   1 
ATOM   4206 C  CA  . SER B 1 66  ? 13.468  -13.029 84.380  1.00 18.17 ? 65   SER B CA  1 
ATOM   4207 C  C   . SER B 1 66  ? 13.297  -14.460 84.866  1.00 17.34 ? 65   SER B C   1 
ATOM   4208 O  O   . SER B 1 66  ? 14.260  -15.043 85.388  1.00 17.75 ? 65   SER B O   1 
ATOM   4209 C  CB  . SER B 1 66  ? 13.560  -12.080 85.586  1.00 22.71 ? 65   SER B CB  1 
ATOM   4210 O  OG  . SER B 1 66  ? 12.468  -12.248 86.481  1.00 23.16 ? 65   SER B OG  1 
ATOM   4211 N  N   . ARG B 1 67  ? 12.106  -15.038 84.698  1.00 18.42 ? 66   ARG B N   1 
ATOM   4212 C  CA  . ARG B 1 67  ? 11.806  -16.380 85.175  1.00 18.38 ? 66   ARG B CA  1 
ATOM   4213 C  C   . ARG B 1 67  ? 11.619  -17.391 84.059  1.00 16.78 ? 66   ARG B C   1 
ATOM   4214 O  O   . ARG B 1 67  ? 11.903  -18.574 84.260  1.00 17.07 ? 66   ARG B O   1 
ATOM   4215 C  CB  . ARG B 1 67  ? 10.539  -16.370 86.043  1.00 15.86 ? 66   ARG B CB  1 
ATOM   4216 C  CG  . ARG B 1 67  ? 10.664  -15.515 87.310  1.00 18.81 ? 66   ARG B CG  1 
ATOM   4217 C  CD  . ARG B 1 67  ? 9.318   -15.359 88.031  1.00 19.76 ? 66   ARG B CD  1 
ATOM   4218 N  NE  . ARG B 1 67  ? 8.864   -16.609 88.623  1.00 20.13 ? 66   ARG B NE  1 
ATOM   4219 C  CZ  . ARG B 1 67  ? 7.626   -16.843 89.038  1.00 21.35 ? 66   ARG B CZ  1 
ATOM   4220 N  NH1 . ARG B 1 67  ? 6.661   -15.945 88.888  1.00 18.73 ? 66   ARG B NH1 1 
ATOM   4221 N  NH2 . ARG B 1 67  ? 7.344   -18.014 89.606  1.00 22.90 ? 66   ARG B NH2 1 
ATOM   4222 N  N   . PHE B 1 68  ? 11.154  -16.957 82.892  1.00 14.09 ? 67   PHE B N   1 
ATOM   4223 C  CA  . PHE B 1 68  ? 10.816  -17.868 81.809  1.00 13.60 ? 67   PHE B CA  1 
ATOM   4224 C  C   . PHE B 1 68  ? 11.305  -17.292 80.489  1.00 14.70 ? 67   PHE B C   1 
ATOM   4225 O  O   . PHE B 1 68  ? 11.231  -16.081 80.274  1.00 15.69 ? 67   PHE B O   1 
ATOM   4226 C  CB  . PHE B 1 68  ? 9.299   -18.097 81.738  1.00 13.91 ? 67   PHE B CB  1 
ATOM   4227 C  CG  . PHE B 1 68  ? 8.716   -18.697 82.995  1.00 15.70 ? 67   PHE B CG  1 
ATOM   4228 C  CD1 . PHE B 1 68  ? 8.704   -20.076 83.182  1.00 16.85 ? 67   PHE B CD1 1 
ATOM   4229 C  CD2 . PHE B 1 68  ? 8.175   -17.883 83.987  1.00 16.42 ? 67   PHE B CD2 1 
ATOM   4230 C  CE1 . PHE B 1 68  ? 8.169   -20.640 84.342  1.00 18.22 ? 67   PHE B CE1 1 
ATOM   4231 C  CE2 . PHE B 1 68  ? 7.637   -18.434 85.159  1.00 16.36 ? 67   PHE B CE2 1 
ATOM   4232 C  CZ  . PHE B 1 68  ? 7.631   -19.814 85.332  1.00 19.15 ? 67   PHE B CZ  1 
ATOM   4233 N  N   . ASP B 1 69  ? 11.793  -18.168 79.609  1.00 13.47 ? 68   ASP B N   1 
ATOM   4234 C  CA  . ASP B 1 69  ? 12.237  -17.808 78.266  1.00 14.25 ? 68   ASP B CA  1 
ATOM   4235 C  C   . ASP B 1 69  ? 11.402  -18.577 77.245  1.00 13.91 ? 68   ASP B C   1 
ATOM   4236 O  O   . ASP B 1 69  ? 10.744  -19.570 77.574  1.00 12.73 ? 68   ASP B O   1 
ATOM   4237 C  CB  . ASP B 1 69  ? 13.745  -18.118 78.127  1.00 12.91 ? 68   ASP B CB  1 
ATOM   4238 C  CG  . ASP B 1 69  ? 14.341  -17.724 76.785  1.00 13.68 ? 68   ASP B CG  1 
ATOM   4239 O  OD1 . ASP B 1 69  ? 13.811  -16.838 76.079  1.00 14.70 ? 68   ASP B OD1 1 
ATOM   4240 O  OD2 . ASP B 1 69  ? 15.382  -18.330 76.444  1.00 17.23 ? 68   ASP B OD2 1 
ATOM   4241 N  N   . LYS B 1 70  ? 11.405  -18.099 75.999  1.00 11.47 ? 69   LYS B N   1 
ATOM   4242 C  CA  . LYS B 1 70  ? 10.696  -18.801 74.930  1.00 10.92 ? 69   LYS B CA  1 
ATOM   4243 C  C   . LYS B 1 70  ? 11.229  -20.221 74.757  1.00 12.00 ? 69   LYS B C   1 
ATOM   4244 O  O   . LYS B 1 70  ? 12.444  -20.442 74.690  1.00 13.61 ? 69   LYS B O   1 
ATOM   4245 C  CB  . LYS B 1 70  ? 10.824  -18.038 73.601  1.00 10.49 ? 69   LYS B CB  1 
ATOM   4246 C  CG  . LYS B 1 70  ? 10.464  -18.900 72.379  1.00 10.77 ? 69   LYS B CG  1 
ATOM   4247 C  CD  . LYS B 1 70  ? 10.031  -18.067 71.164  1.00 11.12 ? 69   LYS B CD  1 
ATOM   4248 C  CE  . LYS B 1 70  ? 9.937   -18.929 69.899  1.00 11.51 ? 69   LYS B CE  1 
ATOM   4249 N  NZ  . LYS B 1 70  ? 9.086   -18.302 68.815  1.00 11.00 ? 69   LYS B NZ  1 
ATOM   4250 N  N   . ASN B 1 71  ? 10.312  -21.183 74.675  1.00 11.68 ? 70   ASN B N   1 
ATOM   4251 C  CA  . ASN B 1 71  ? 10.616  -22.566 74.342  1.00 11.58 ? 70   ASN B CA  1 
ATOM   4252 C  C   . ASN B 1 71  ? 10.151  -22.861 72.920  1.00 10.11 ? 70   ASN B C   1 
ATOM   4253 O  O   . ASN B 1 71  ? 9.162   -22.297 72.451  1.00 11.92 ? 70   ASN B O   1 
ATOM   4254 C  CB  . ASN B 1 71  ? 9.925   -23.531 75.313  1.00 11.87 ? 70   ASN B CB  1 
ATOM   4255 C  CG  . ASN B 1 71  ? 10.260  -24.972 75.038  1.00 13.92 ? 70   ASN B CG  1 
ATOM   4256 O  OD1 . ASN B 1 71  ? 11.432  -25.338 74.932  1.00 15.49 ? 70   ASN B OD1 1 
ATOM   4257 N  ND2 . ASN B 1 71  ? 9.230   -25.810 74.916  1.00 13.66 ? 70   ASN B ND2 1 
ATOM   4258 N  N   . LEU B 1 72  ? 10.848  -23.760 72.235  1.00 11.38 ? 71   LEU B N   1 
ATOM   4259 C  CA  . LEU B 1 72  ? 10.333  -24.295 70.973  1.00 12.45 ? 71   LEU B CA  1 
ATOM   4260 C  C   . LEU B 1 72  ? 9.411   -25.468 71.290  1.00 12.92 ? 71   LEU B C   1 
ATOM   4261 O  O   . LEU B 1 72  ? 9.872   -26.526 71.730  1.00 14.59 ? 71   LEU B O   1 
ATOM   4262 C  CB  . LEU B 1 72  ? 11.460  -24.725 70.038  1.00 13.28 ? 71   LEU B CB  1 
ATOM   4263 C  CG  . LEU B 1 72  ? 12.483  -23.660 69.646  1.00 15.71 ? 71   LEU B CG  1 
ATOM   4264 C  CD1 . LEU B 1 72  ? 13.430  -24.225 68.586  1.00 17.34 ? 71   LEU B CD1 1 
ATOM   4265 C  CD2 . LEU B 1 72  ? 11.805  -22.392 69.142  1.00 13.09 ? 71   LEU B CD2 1 
ATOM   4266 N  N   . SER B 1 73  ? 8.110   -25.274 71.077  1.00 12.17 ? 72   SER B N   1 
ATOM   4267 C  CA  . SER B 1 73  ? 7.154   -26.371 71.093  1.00 12.87 ? 72   SER B CA  1 
ATOM   4268 C  C   . SER B 1 73  ? 7.544   -27.423 70.054  1.00 13.16 ? 72   SER B C   1 
ATOM   4269 O  O   . SER B 1 73  ? 8.358   -27.180 69.165  1.00 14.72 ? 72   SER B O   1 
ATOM   4270 C  CB  . SER B 1 73  ? 5.754   -25.843 70.798  1.00 13.70 ? 72   SER B CB  1 
ATOM   4271 O  OG  . SER B 1 73  ? 5.763   -25.180 69.542  1.00 12.76 ? 72   SER B OG  1 
ATOM   4272 N  N   . GLN B 1 74  ? 6.945   -28.612 70.162  1.00 14.87 ? 73   GLN B N   1 
ATOM   4273 C  CA  . GLN B 1 74  ? 7.179   -29.615 69.127  1.00 15.40 ? 73   GLN B CA  1 
ATOM   4274 C  C   . GLN B 1 74  ? 6.781   -29.069 67.764  1.00 14.81 ? 73   GLN B C   1 
ATOM   4275 O  O   . GLN B 1 74  ? 7.464   -29.309 66.758  1.00 14.92 ? 73   GLN B O   1 
ATOM   4276 C  CB  . GLN B 1 74  ? 6.408   -30.902 69.428  1.00 15.99 ? 73   GLN B CB  1 
ATOM   4277 C  CG  . GLN B 1 74  ? 6.845   -32.062 68.540  1.00 20.15 ? 73   GLN B CG  1 
ATOM   4278 C  CD  . GLN B 1 74  ? 8.318   -32.392 68.725  1.00 25.67 ? 73   GLN B CD  1 
ATOM   4279 O  OE1 . GLN B 1 74  ? 9.126   -32.252 67.803  1.00 28.91 ? 73   GLN B OE1 1 
ATOM   4280 N  NE2 . GLN B 1 74  ? 8.674   -32.828 69.926  1.00 25.12 ? 73   GLN B NE2 1 
ATOM   4281 N  N   . ALA B 1 75  ? 5.690   -28.303 67.720  1.00 14.01 ? 74   ALA B N   1 
ATOM   4282 C  CA  . ALA B 1 75  ? 5.248   -27.712 66.460  1.00 12.60 ? 74   ALA B CA  1 
ATOM   4283 C  C   . ALA B 1 75  ? 6.342   -26.840 65.853  1.00 13.55 ? 74   ALA B C   1 
ATOM   4284 O  O   . ALA B 1 75  ? 6.658   -26.962 64.664  1.00 16.36 ? 74   ALA B O   1 
ATOM   4285 C  CB  . ALA B 1 75  ? 3.969   -26.901 66.684  1.00 13.19 ? 74   ALA B CB  1 
ATOM   4286 N  N   . LEU B 1 76  ? 6.941   -25.953 66.657  1.00 13.00 ? 75   LEU B N   1 
ATOM   4287 C  CA  . LEU B 1 76  ? 7.997   -25.098 66.120  1.00 11.71 ? 75   LEU B CA  1 
ATOM   4288 C  C   . LEU B 1 76  ? 9.253   -25.890 65.764  1.00 13.26 ? 75   LEU B C   1 
ATOM   4289 O  O   . LEU B 1 76  ? 9.981   -25.506 64.835  1.00 13.02 ? 75   LEU B O   1 
ATOM   4290 C  CB  . LEU B 1 76  ? 8.338   -23.972 67.107  1.00 13.31 ? 75   LEU B CB  1 
ATOM   4291 C  CG  . LEU B 1 76  ? 7.291   -22.866 67.288  1.00 13.11 ? 75   LEU B CG  1 
ATOM   4292 C  CD1 . LEU B 1 76  ? 7.819   -21.763 68.232  1.00 12.91 ? 75   LEU B CD1 1 
ATOM   4293 C  CD2 . LEU B 1 76  ? 6.862   -22.267 65.945  1.00 14.13 ? 75   LEU B CD2 1 
ATOM   4294 N  N   . LYS B 1 77  ? 9.547   -26.977 66.491  1.00 12.56 ? 76   LYS B N   1 
ATOM   4295 C  CA  . LYS B 1 77  ? 10.690  -27.805 66.112  1.00 14.87 ? 76   LYS B CA  1 
ATOM   4296 C  C   . LYS B 1 77  ? 10.471  -28.427 64.739  1.00 14.72 ? 76   LYS B C   1 
ATOM   4297 O  O   . LYS B 1 77  ? 11.418  -28.571 63.950  1.00 14.52 ? 76   LYS B O   1 
ATOM   4298 C  CB  . LYS B 1 77  ? 10.940  -28.888 67.161  1.00 15.47 ? 76   LYS B CB  1 
ATOM   4299 C  CG  . LYS B 1 77  ? 11.485  -28.345 68.477  1.00 16.93 ? 76   LYS B CG  1 
ATOM   4300 C  CD  . LYS B 1 77  ? 11.761  -29.459 69.472  1.00 20.00 ? 76   LYS B CD  1 
ATOM   4301 C  CE  . LYS B 1 77  ? 12.393  -28.901 70.738  1.00 23.95 ? 76   LYS B CE  1 
ATOM   4302 N  NZ  . LYS B 1 77  ? 12.640  -29.963 71.744  1.00 26.27 ? 76   LYS B NZ  1 
ATOM   4303 N  N   . PHE B 1 78  ? 9.223   -28.786 64.430  1.00 13.98 ? 77   PHE B N   1 
ATOM   4304 C  CA  . PHE B 1 78  ? 8.922   -29.327 63.108  1.00 16.33 ? 77   PHE B CA  1 
ATOM   4305 C  C   . PHE B 1 78  ? 8.961   -28.237 62.042  1.00 17.06 ? 77   PHE B C   1 
ATOM   4306 O  O   . PHE B 1 78  ? 9.418   -28.480 60.916  1.00 16.97 ? 77   PHE B O   1 
ATOM   4307 C  CB  . PHE B 1 78  ? 7.561   -30.032 63.132  1.00 16.36 ? 77   PHE B CB  1 
ATOM   4308 C  CG  . PHE B 1 78  ? 7.571   -31.341 63.881  1.00 18.39 ? 77   PHE B CG  1 
ATOM   4309 C  CD1 . PHE B 1 78  ? 8.750   -32.059 64.029  1.00 20.82 ? 77   PHE B CD1 1 
ATOM   4310 C  CD2 . PHE B 1 78  ? 6.405   -31.855 64.427  1.00 18.42 ? 77   PHE B CD2 1 
ATOM   4311 C  CE1 . PHE B 1 78  ? 8.766   -33.264 64.709  1.00 25.70 ? 77   PHE B CE1 1 
ATOM   4312 C  CE2 . PHE B 1 78  ? 6.414   -33.057 65.114  1.00 22.92 ? 77   PHE B CE2 1 
ATOM   4313 C  CZ  . PHE B 1 78  ? 7.595   -33.766 65.251  1.00 26.01 ? 77   PHE B CZ  1 
ATOM   4314 N  N   . VAL B 1 79  ? 8.486   -27.030 62.369  1.00 15.64 ? 78   VAL B N   1 
ATOM   4315 C  CA  . VAL B 1 79  ? 8.593   -25.918 61.427  1.00 14.90 ? 78   VAL B CA  1 
ATOM   4316 C  C   . VAL B 1 79  ? 10.057  -25.575 61.189  1.00 14.81 ? 78   VAL B C   1 
ATOM   4317 O  O   . VAL B 1 79  ? 10.443  -25.177 60.082  1.00 14.49 ? 78   VAL B O   1 
ATOM   4318 C  CB  . VAL B 1 79  ? 7.797   -24.699 61.943  1.00 14.92 ? 78   VAL B CB  1 
ATOM   4319 C  CG1 . VAL B 1 79  ? 8.079   -23.475 61.092  1.00 15.44 ? 78   VAL B CG1 1 
ATOM   4320 C  CG2 . VAL B 1 79  ? 6.290   -25.009 61.951  1.00 12.67 ? 78   VAL B CG2 1 
ATOM   4321 N  N   . ARG B 1 80  ? 10.898  -25.736 62.217  1.00 15.05 ? 79   ARG B N   1 
ATOM   4322 C  CA  . ARG B 1 80  ? 12.324  -25.451 62.071  1.00 14.40 ? 79   ARG B CA  1 
ATOM   4323 C  C   . ARG B 1 80  ? 12.975  -26.297 60.978  1.00 16.37 ? 79   ARG B C   1 
ATOM   4324 O  O   . ARG B 1 80  ? 14.040  -25.919 60.466  1.00 16.26 ? 79   ARG B O   1 
ATOM   4325 C  CB  . ARG B 1 80  ? 13.042  -25.665 63.411  1.00 13.52 ? 79   ARG B CB  1 
ATOM   4326 C  CG  . ARG B 1 80  ? 14.547  -25.408 63.352  1.00 14.52 ? 79   ARG B CG  1 
ATOM   4327 C  CD  . ARG B 1 80  ? 15.109  -25.002 64.707  1.00 14.25 ? 79   ARG B CD  1 
ATOM   4328 N  NE  . ARG B 1 80  ? 16.569  -24.980 64.682  1.00 16.67 ? 79   ARG B NE  1 
ATOM   4329 C  CZ  . ARG B 1 80  ? 17.315  -24.130 65.378  1.00 16.07 ? 79   ARG B CZ  1 
ATOM   4330 N  NH1 . ARG B 1 80  ? 16.768  -23.189 66.132  1.00 15.39 ? 79   ARG B NH1 1 
ATOM   4331 N  NH2 . ARG B 1 80  ? 18.642  -24.215 65.303  1.00 17.97 ? 79   ARG B NH2 1 
ATOM   4332 N  N   . ASP B 1 81  ? 12.374  -27.432 60.609  1.00 16.74 ? 80   ASP B N   1 
ATOM   4333 C  CA  . ASP B 1 81  ? 12.949  -28.231 59.532  1.00 18.35 ? 80   ASP B CA  1 
ATOM   4334 C  C   . ASP B 1 81  ? 13.012  -27.462 58.214  1.00 18.95 ? 80   ASP B C   1 
ATOM   4335 O  O   . ASP B 1 81  ? 13.825  -27.812 57.346  1.00 19.91 ? 80   ASP B O   1 
ATOM   4336 C  CB  . ASP B 1 81  ? 12.169  -29.538 59.358  1.00 20.99 ? 80   ASP B CB  1 
ATOM   4337 C  CG  . ASP B 1 81  ? 12.478  -30.555 60.448  1.00 24.68 ? 80   ASP B CG  1 
ATOM   4338 O  OD1 . ASP B 1 81  ? 13.556  -30.464 61.060  1.00 26.64 ? 80   ASP B OD1 1 
ATOM   4339 O  OD2 . ASP B 1 81  ? 11.646  -31.458 60.693  1.00 28.68 ? 80   ASP B OD2 1 
ATOM   4340 N  N   . PHE B 1 82  ? 12.174  -26.433 58.027  1.00 17.18 ? 81   PHE B N   1 
ATOM   4341 C  CA  . PHE B 1 82  ? 12.349  -25.539 56.887  1.00 16.14 ? 81   PHE B CA  1 
ATOM   4342 C  C   . PHE B 1 82  ? 12.609  -24.081 57.257  1.00 16.52 ? 81   PHE B C   1 
ATOM   4343 O  O   . PHE B 1 82  ? 13.166  -23.356 56.424  1.00 15.49 ? 81   PHE B O   1 
ATOM   4344 C  CB  . PHE B 1 82  ? 11.146  -25.622 55.918  1.00 16.05 ? 81   PHE B CB  1 
ATOM   4345 C  CG  . PHE B 1 82  ? 9.793   -25.552 56.574  1.00 15.81 ? 81   PHE B CG  1 
ATOM   4346 C  CD1 . PHE B 1 82  ? 9.154   -26.709 57.010  1.00 17.75 ? 81   PHE B CD1 1 
ATOM   4347 C  CD2 . PHE B 1 82  ? 9.134   -24.339 56.700  1.00 17.85 ? 81   PHE B CD2 1 
ATOM   4348 C  CE1 . PHE B 1 82  ? 7.894   -26.646 57.601  1.00 17.74 ? 81   PHE B CE1 1 
ATOM   4349 C  CE2 . PHE B 1 82  ? 7.879   -24.269 57.289  1.00 18.89 ? 81   PHE B CE2 1 
ATOM   4350 C  CZ  . PHE B 1 82  ? 7.257   -25.424 57.738  1.00 19.67 ? 81   PHE B CZ  1 
ATOM   4351 N  N   . ALA B 1 83  ? 12.281  -23.638 58.479  1.00 13.58 ? 82   ALA B N   1 
ATOM   4352 C  CA  . ALA B 1 83  ? 12.542  -22.261 58.901  1.00 14.83 ? 82   ALA B CA  1 
ATOM   4353 C  C   . ALA B 1 83  ? 13.862  -22.090 59.659  1.00 13.83 ? 82   ALA B C   1 
ATOM   4354 O  O   . ALA B 1 83  ? 14.255  -20.947 59.935  1.00 13.88 ? 82   ALA B O   1 
ATOM   4355 C  CB  . ALA B 1 83  ? 11.382  -21.735 59.765  1.00 13.32 ? 82   ALA B CB  1 
ATOM   4356 N  N   . GLY B 1 84  ? 14.545  -23.180 60.005  1.00 13.51 ? 83   GLY B N   1 
ATOM   4357 C  CA  . GLY B 1 84  ? 15.915  -23.099 60.500  1.00 12.88 ? 83   GLY B CA  1 
ATOM   4358 C  C   . GLY B 1 84  ? 16.059  -22.211 61.723  1.00 14.93 ? 83   GLY B C   1 
ATOM   4359 O  O   . GLY B 1 84  ? 15.220  -22.225 62.638  1.00 16.62 ? 83   GLY B O   1 
ATOM   4360 N  N   . ASP B 1 85  ? 17.143  -21.432 61.761  1.00 12.57 ? 84   ASP B N   1 
ATOM   4361 C  CA  . ASP B 1 85  ? 17.320  -20.464 62.849  1.00 12.04 ? 84   ASP B CA  1 
ATOM   4362 C  C   . ASP B 1 85  ? 16.906  -19.061 62.424  1.00 14.68 ? 84   ASP B C   1 
ATOM   4363 O  O   . ASP B 1 85  ? 17.536  -18.076 62.810  1.00 14.67 ? 84   ASP B O   1 
ATOM   4364 C  CB  . ASP B 1 85  ? 18.749  -20.486 63.417  1.00 11.84 ? 84   ASP B CB  1 
ATOM   4365 C  CG  . ASP B 1 85  ? 19.835  -20.180 62.383  1.00 12.53 ? 84   ASP B CG  1 
ATOM   4366 O  OD1 . ASP B 1 85  ? 19.513  -20.042 61.185  1.00 15.75 ? 84   ASP B OD1 1 
ATOM   4367 O  OD2 . ASP B 1 85  ? 21.035  -20.085 62.788  1.00 15.48 ? 84   ASP B OD2 1 
ATOM   4368 N  N   . GLY B 1 86  ? 15.824  -18.954 61.640  1.00 13.83 ? 85   GLY B N   1 
ATOM   4369 C  CA  . GLY B 1 86  ? 15.140  -17.683 61.463  1.00 11.93 ? 85   GLY B CA  1 
ATOM   4370 C  C   . GLY B 1 86  ? 14.552  -17.198 62.781  1.00 11.77 ? 85   GLY B C   1 
ATOM   4371 O  O   . GLY B 1 86  ? 14.574  -17.892 63.796  1.00 12.96 ? 85   GLY B O   1 
ATOM   4372 N  N   . LEU B 1 87  ? 13.992  -15.981 62.753  1.00 10.91 ? 86   LEU B N   1 
ATOM   4373 C  CA  . LEU B 1 87  ? 13.613  -15.316 64.002  1.00 10.99 ? 86   LEU B CA  1 
ATOM   4374 C  C   . LEU B 1 87  ? 12.601  -16.126 64.802  1.00 12.52 ? 86   LEU B C   1 
ATOM   4375 O  O   . LEU B 1 87  ? 12.666  -16.152 66.036  1.00 13.74 ? 86   LEU B O   1 
ATOM   4376 C  CB  . LEU B 1 87  ? 13.054  -13.917 63.722  1.00 12.96 ? 86   LEU B CB  1 
ATOM   4377 C  CG  . LEU B 1 87  ? 14.074  -12.803 63.487  1.00 13.09 ? 86   LEU B CG  1 
ATOM   4378 C  CD1 . LEU B 1 87  ? 13.341  -11.527 63.122  1.00 14.08 ? 86   LEU B CD1 1 
ATOM   4379 C  CD2 . LEU B 1 87  ? 14.972  -12.582 64.708  1.00 12.20 ? 86   LEU B CD2 1 
ATOM   4380 N  N   . ALA B 1 88  ? 11.640  -16.772 64.129  1.00 11.19 ? 87   ALA B N   1 
ATOM   4381 C  CA  . ALA B 1 88  ? 10.548  -17.406 64.862  1.00 11.27 ? 87   ALA B CA  1 
ATOM   4382 C  C   . ALA B 1 88  ? 10.916  -18.761 65.446  1.00 13.24 ? 87   ALA B C   1 
ATOM   4383 O  O   . ALA B 1 88  ? 10.251  -19.203 66.393  1.00 12.98 ? 87   ALA B O   1 
ATOM   4384 C  CB  . ALA B 1 88  ? 9.311   -17.571 63.964  1.00 12.95 ? 87   ALA B CB  1 
ATOM   4385 N  N   . THR B 1 89  ? 11.935  -19.442 64.907  1.00 11.58 ? 88   THR B N   1 
ATOM   4386 C  CA  . THR B 1 89  ? 12.235  -20.811 65.322  1.00 10.82 ? 88   THR B CA  1 
ATOM   4387 C  C   . THR B 1 89  ? 13.640  -20.939 65.903  1.00 11.90 ? 88   THR B C   1 
ATOM   4388 O  O   . THR B 1 89  ? 14.156  -22.052 66.049  1.00 13.68 ? 88   THR B O   1 
ATOM   4389 C  CB  . THR B 1 89  ? 12.021  -21.798 64.161  1.00 12.03 ? 88   THR B CB  1 
ATOM   4390 O  OG1 . THR B 1 89  ? 12.670  -21.318 62.973  1.00 13.40 ? 88   THR B OG1 1 
ATOM   4391 C  CG2 . THR B 1 89  ? 10.541  -21.970 63.863  1.00 12.16 ? 88   THR B CG2 1 
ATOM   4392 N  N   . SER B 1 90  ? 14.263  -19.822 66.263  1.00 10.99 ? 89   SER B N   1 
ATOM   4393 C  CA  . SER B 1 90  ? 15.554  -19.852 66.938  1.00 11.37 ? 89   SER B CA  1 
ATOM   4394 C  C   . SER B 1 90  ? 15.375  -19.733 68.451  1.00 11.74 ? 89   SER B C   1 
ATOM   4395 O  O   . SER B 1 90  ? 14.396  -19.160 68.937  1.00 12.84 ? 89   SER B O   1 
ATOM   4396 C  CB  . SER B 1 90  ? 16.461  -18.728 66.421  1.00 14.72 ? 89   SER B CB  1 
ATOM   4397 O  OG  . SER B 1 90  ? 15.817  -17.470 66.536  1.00 20.95 ? 89   SER B OG  1 
ATOM   4398 N  N   . TRP B 1 91  ? 16.325  -20.299 69.195  1.00 11.56 ? 90   TRP B N   1 
ATOM   4399 C  CA  . TRP B 1 91  ? 16.364  -20.094 70.637  1.00 12.13 ? 90   TRP B CA  1 
ATOM   4400 C  C   . TRP B 1 91  ? 16.931  -18.714 70.940  1.00 11.25 ? 90   TRP B C   1 
ATOM   4401 O  O   . TRP B 1 91  ? 17.760  -18.181 70.190  1.00 12.69 ? 90   TRP B O   1 
ATOM   4402 C  CB  . TRP B 1 91  ? 17.216  -21.172 71.319  1.00 13.34 ? 90   TRP B CB  1 
ATOM   4403 C  CG  . TRP B 1 91  ? 16.724  -22.585 71.092  1.00 13.75 ? 90   TRP B CG  1 
ATOM   4404 C  CD1 . TRP B 1 91  ? 17.078  -23.420 70.067  1.00 12.55 ? 90   TRP B CD1 1 
ATOM   4405 C  CD2 . TRP B 1 91  ? 15.786  -23.321 71.903  1.00 14.40 ? 90   TRP B CD2 1 
ATOM   4406 N  NE1 . TRP B 1 91  ? 16.424  -24.620 70.191  1.00 13.24 ? 90   TRP B NE1 1 
ATOM   4407 C  CE2 . TRP B 1 91  ? 15.628  -24.589 71.308  1.00 13.72 ? 90   TRP B CE2 1 
ATOM   4408 C  CE3 . TRP B 1 91  ? 15.071  -23.030 73.075  1.00 14.93 ? 90   TRP B CE3 1 
ATOM   4409 C  CZ2 . TRP B 1 91  ? 14.778  -25.573 71.836  1.00 14.27 ? 90   TRP B CZ2 1 
ATOM   4410 C  CZ3 . TRP B 1 91  ? 14.224  -24.015 73.610  1.00 14.14 ? 90   TRP B CZ3 1 
ATOM   4411 C  CH2 . TRP B 1 91  ? 14.095  -25.275 72.986  1.00 13.53 ? 90   TRP B CH2 1 
ATOM   4412 N  N   . THR B 1 92  ? 16.488  -18.134 72.061  1.00 10.49 ? 91   THR B N   1 
ATOM   4413 C  CA  . THR B 1 92  ? 16.955  -16.799 72.422  1.00 12.11 ? 91   THR B CA  1 
ATOM   4414 C  C   . THR B 1 92  ? 18.473  -16.755 72.570  1.00 14.26 ? 91   THR B C   1 
ATOM   4415 O  O   . THR B 1 92  ? 19.090  -15.712 72.322  1.00 14.72 ? 91   THR B O   1 
ATOM   4416 C  CB  . THR B 1 92  ? 16.274  -16.334 73.711  1.00 12.33 ? 91   THR B CB  1 
ATOM   4417 O  OG1 . THR B 1 92  ? 14.849  -16.412 73.552  1.00 12.74 ? 91   THR B OG1 1 
ATOM   4418 C  CG2 . THR B 1 92  ? 16.668  -14.896 74.057  1.00 13.80 ? 91   THR B CG2 1 
ATOM   4419 N  N   . HIS B 1 93  ? 19.091  -17.872 72.970  1.00 11.35 ? 92   HIS B N   1 
ATOM   4420 C  CA  . HIS B 1 93  ? 20.527  -17.928 73.210  1.00 11.27 ? 92   HIS B CA  1 
ATOM   4421 C  C   . HIS B 1 93  ? 21.351  -18.241 71.959  1.00 12.55 ? 92   HIS B C   1 
ATOM   4422 O  O   . HIS B 1 93  ? 22.587  -18.190 72.019  1.00 12.81 ? 92   HIS B O   1 
ATOM   4423 C  CB  . HIS B 1 93  ? 20.831  -18.963 74.304  1.00 11.98 ? 92   HIS B CB  1 
ATOM   4424 C  CG  . HIS B 1 93  ? 20.214  -20.308 74.058  1.00 12.58 ? 92   HIS B CG  1 
ATOM   4425 N  ND1 . HIS B 1 93  ? 20.708  -21.195 73.123  1.00 14.13 ? 92   HIS B ND1 1 
ATOM   4426 C  CD2 . HIS B 1 93  ? 19.155  -20.924 74.637  1.00 13.69 ? 92   HIS B CD2 1 
ATOM   4427 C  CE1 . HIS B 1 93  ? 19.978  -22.297 73.134  1.00 16.67 ? 92   HIS B CE1 1 
ATOM   4428 N  NE2 . HIS B 1 93  ? 19.031  -22.162 74.047  1.00 15.17 ? 92   HIS B NE2 1 
ATOM   4429 N  N   . GLU B 1 94  ? 20.720  -18.556 70.829  1.00 13.14 ? 93   GLU B N   1 
ATOM   4430 C  CA  . GLU B 1 94  ? 21.488  -18.742 69.604  1.00 14.70 ? 93   GLU B CA  1 
ATOM   4431 C  C   . GLU B 1 94  ? 21.943  -17.390 69.071  1.00 12.58 ? 93   GLU B C   1 
ATOM   4432 O  O   . GLU B 1 94  ? 21.168  -16.432 69.036  1.00 12.66 ? 93   GLU B O   1 
ATOM   4433 C  CB  . GLU B 1 94  ? 20.660  -19.470 68.545  1.00 13.56 ? 93   GLU B CB  1 
ATOM   4434 C  CG  . GLU B 1 94  ? 20.470  -20.970 68.806  1.00 13.45 ? 93   GLU B CG  1 
ATOM   4435 C  CD  . GLU B 1 94  ? 19.647  -21.641 67.717  1.00 15.20 ? 93   GLU B CD  1 
ATOM   4436 O  OE1 . GLU B 1 94  ? 18.414  -21.462 67.717  1.00 15.30 ? 93   GLU B OE1 1 
ATOM   4437 O  OE2 . GLU B 1 94  ? 20.234  -22.330 66.852  1.00 17.16 ? 93   GLU B OE2 1 
ATOM   4438 N  N   . LYS B 1 95  ? 23.211  -17.321 68.642  1.00 13.88 ? 94   LYS B N   1 
ATOM   4439 C  CA  . LYS B 1 95  ? 23.778  -16.058 68.174  1.00 11.45 ? 94   LYS B CA  1 
ATOM   4440 C  C   . LYS B 1 95  ? 22.888  -15.387 67.129  1.00 14.08 ? 94   LYS B C   1 
ATOM   4441 O  O   . LYS B 1 95  ? 22.716  -14.160 67.142  1.00 13.60 ? 94   LYS B O   1 
ATOM   4442 C  CB  . LYS B 1 95  ? 25.184  -16.300 67.611  1.00 12.34 ? 94   LYS B CB  1 
ATOM   4443 C  CG  . LYS B 1 95  ? 25.859  -15.049 67.047  1.00 14.20 ? 94   LYS B CG  1 
ATOM   4444 C  CD  . LYS B 1 95  ? 27.278  -15.338 66.532  1.00 16.66 ? 94   LYS B CD  1 
ATOM   4445 C  CE  . LYS B 1 95  ? 27.910  -14.095 65.948  1.00 19.11 ? 94   LYS B CE  1 
ATOM   4446 N  NZ  . LYS B 1 95  ? 29.319  -14.355 65.478  1.00 20.63 ? 94   LYS B NZ  1 
ATOM   4447 N  N   . ASN B 1 96  ? 22.306  -16.171 66.218  1.00 13.02 ? 95   ASN B N   1 
ATOM   4448 C  CA  . ASN B 1 96  ? 21.562  -15.562 65.122  1.00 14.06 ? 95   ASN B CA  1 
ATOM   4449 C  C   . ASN B 1 96  ? 20.219  -14.977 65.541  1.00 13.30 ? 95   ASN B C   1 
ATOM   4450 O  O   . ASN B 1 96  ? 19.635  -14.235 64.744  1.00 14.00 ? 95   ASN B O   1 
ATOM   4451 C  CB  . ASN B 1 96  ? 21.335  -16.563 63.991  1.00 14.91 ? 95   ASN B CB  1 
ATOM   4452 C  CG  . ASN B 1 96  ? 22.518  -16.649 63.044  1.00 16.08 ? 95   ASN B CG  1 
ATOM   4453 O  OD1 . ASN B 1 96  ? 23.280  -15.685 62.888  1.00 18.26 ? 95   ASN B OD1 1 
ATOM   4454 N  ND2 . ASN B 1 96  ? 22.672  -17.794 62.395  1.00 15.37 ? 95   ASN B ND2 1 
ATOM   4455 N  N   . TRP B 1 97  ? 19.697  -15.277 66.737  1.00 12.37 ? 96   TRP B N   1 
ATOM   4456 C  CA  . TRP B 1 97  ? 18.446  -14.629 67.130  1.00 12.07 ? 96   TRP B CA  1 
ATOM   4457 C  C   . TRP B 1 97  ? 18.655  -13.135 67.368  1.00 11.44 ? 96   TRP B C   1 
ATOM   4458 O  O   . TRP B 1 97  ? 18.054  -12.297 66.685  1.00 12.53 ? 96   TRP B O   1 
ATOM   4459 C  CB  . TRP B 1 97  ? 17.791  -15.273 68.370  1.00 11.99 ? 96   TRP B CB  1 
ATOM   4460 C  CG  . TRP B 1 97  ? 16.547  -14.450 68.620  1.00 11.17 ? 96   TRP B CG  1 
ATOM   4461 C  CD1 . TRP B 1 97  ? 15.395  -14.450 67.861  1.00 13.09 ? 96   TRP B CD1 1 
ATOM   4462 C  CD2 . TRP B 1 97  ? 16.397  -13.389 69.571  1.00 13.20 ? 96   TRP B CD2 1 
ATOM   4463 N  NE1 . TRP B 1 97  ? 14.526  -13.486 68.323  1.00 12.53 ? 96   TRP B NE1 1 
ATOM   4464 C  CE2 . TRP B 1 97  ? 15.116  -12.825 69.373  1.00 12.29 ? 96   TRP B CE2 1 
ATOM   4465 C  CE3 . TRP B 1 97  ? 17.209  -12.886 70.602  1.00 13.50 ? 96   TRP B CE3 1 
ATOM   4466 C  CZ2 . TRP B 1 97  ? 14.633  -11.772 70.157  1.00 13.71 ? 96   TRP B CZ2 1 
ATOM   4467 C  CZ3 . TRP B 1 97  ? 16.720  -11.846 71.390  1.00 14.31 ? 96   TRP B CZ3 1 
ATOM   4468 C  CH2 . TRP B 1 97  ? 15.443  -11.299 71.157  1.00 14.45 ? 96   TRP B CH2 1 
ATOM   4469 N  N   . LYS B 1 98  ? 19.491  -12.774 68.348  1.00 11.39 ? 97   LYS B N   1 
ATOM   4470 C  CA  . LYS B 1 98  ? 19.649  -11.354 68.659  1.00 12.27 ? 97   LYS B CA  1 
ATOM   4471 C  C   . LYS B 1 98  ? 20.260  -10.601 67.484  1.00 13.39 ? 97   LYS B C   1 
ATOM   4472 O  O   . LYS B 1 98  ? 19.932  -9.434  67.242  1.00 12.60 ? 97   LYS B O   1 
ATOM   4473 C  CB  . LYS B 1 98  ? 20.508  -11.158 69.912  1.00 15.01 ? 97   LYS B CB  1 
ATOM   4474 C  CG  . LYS B 1 98  ? 20.545  -9.701  70.400  1.00 17.65 ? 97   LYS B CG  1 
ATOM   4475 C  CD  . LYS B 1 98  ? 19.133  -9.206  70.763  1.00 22.99 ? 97   LYS B CD  1 
ATOM   4476 C  CE  . LYS B 1 98  ? 19.132  -7.810  71.376  1.00 25.89 ? 97   LYS B CE  1 
ATOM   4477 N  NZ  . LYS B 1 98  ? 19.762  -7.795  72.723  1.00 30.51 ? 97   LYS B NZ  1 
ATOM   4478 N  N   . LYS B 1 99  ? 21.160  -11.250 66.751  1.00 12.46 ? 98   LYS B N   1 
ATOM   4479 C  CA  . LYS B 1 99  ? 21.782  -10.613 65.594  1.00 12.42 ? 98   LYS B CA  1 
ATOM   4480 C  C   . LYS B 1 99  ? 20.734  -10.212 64.563  1.00 12.70 ? 98   LYS B C   1 
ATOM   4481 O  O   . LYS B 1 99  ? 20.684  -9.053  64.124  1.00 14.88 ? 98   LYS B O   1 
ATOM   4482 C  CB  . LYS B 1 99  ? 22.811  -11.571 64.994  1.00 15.40 ? 98   LYS B CB  1 
ATOM   4483 C  CG  . LYS B 1 99  ? 23.521  -11.088 63.763  1.00 18.31 ? 98   LYS B CG  1 
ATOM   4484 C  CD  . LYS B 1 99  ? 24.668  -12.027 63.427  1.00 16.25 ? 98   LYS B CD  1 
ATOM   4485 C  CE  . LYS B 1 99  ? 25.208  -11.752 62.041  1.00 16.66 ? 98   LYS B CE  1 
ATOM   4486 N  NZ  . LYS B 1 99  ? 26.202  -12.788 61.658  1.00 17.19 ? 98   LYS B NZ  1 
ATOM   4487 N  N   . ALA B 1 100 ? 19.877  -11.159 64.170  1.00 12.60 ? 99   ALA B N   1 
ATOM   4488 C  CA  . ALA B 1 100 ? 18.845  -10.848 63.184  1.00 12.37 ? 99   ALA B CA  1 
ATOM   4489 C  C   . ALA B 1 100 ? 17.794  -9.902  63.759  1.00 13.52 ? 99   ALA B C   1 
ATOM   4490 O  O   . ALA B 1 100 ? 17.256  -9.049  63.040  1.00 13.92 ? 99   ALA B O   1 
ATOM   4491 C  CB  . ALA B 1 100 ? 18.200  -12.139 62.679  1.00 12.82 ? 99   ALA B CB  1 
ATOM   4492 N  N   . HIS B 1 101 ? 17.477  -10.043 65.047  1.00 12.45 ? 100  HIS B N   1 
ATOM   4493 C  CA  . HIS B 1 101 ? 16.542  -9.117  65.682  1.00 14.32 ? 100  HIS B CA  1 
ATOM   4494 C  C   . HIS B 1 101 ? 17.047  -7.683  65.577  1.00 13.36 ? 100  HIS B C   1 
ATOM   4495 O  O   . HIS B 1 101 ? 16.302  -6.775  65.184  1.00 15.64 ? 100  HIS B O   1 
ATOM   4496 C  CB  . HIS B 1 101 ? 16.318  -9.525  67.146  1.00 13.71 ? 100  HIS B CB  1 
ATOM   4497 C  CG  . HIS B 1 101 ? 15.538  -8.530  67.953  1.00 18.52 ? 100  HIS B CG  1 
ATOM   4498 N  ND1 . HIS B 1 101 ? 14.159  -8.481  67.952  1.00 18.22 ? 100  HIS B ND1 1 
ATOM   4499 C  CD2 . HIS B 1 101 ? 15.948  -7.554  68.798  1.00 22.72 ? 100  HIS B CD2 1 
ATOM   4500 C  CE1 . HIS B 1 101 ? 13.755  -7.509  68.753  1.00 20.87 ? 100  HIS B CE1 1 
ATOM   4501 N  NE2 . HIS B 1 101 ? 14.821  -6.930  69.278  1.00 25.22 ? 100  HIS B NE2 1 
ATOM   4502 N  N   . ASN B 1 102 ? 18.324  -7.459  65.904  1.00 12.27 ? 101  ASN B N   1 
ATOM   4503 C  CA  . ASN B 1 102 ? 18.868  -6.105  65.832  1.00 15.70 ? 101  ASN B CA  1 
ATOM   4504 C  C   . ASN B 1 102 ? 18.868  -5.575  64.399  1.00 15.86 ? 101  ASN B C   1 
ATOM   4505 O  O   . ASN B 1 102 ? 18.647  -4.379  64.168  1.00 16.26 ? 101  ASN B O   1 
ATOM   4506 C  CB  . ASN B 1 102 ? 20.286  -6.061  66.406  1.00 12.99 ? 101  ASN B CB  1 
ATOM   4507 C  CG  . ASN B 1 102 ? 20.310  -6.146  67.926  1.00 16.19 ? 101  ASN B CG  1 
ATOM   4508 O  OD1 . ASN B 1 102 ? 19.296  -5.923  68.602  1.00 16.86 ? 101  ASN B OD1 1 
ATOM   4509 N  ND2 . ASN B 1 102 ? 21.470  -6.479  68.472  1.00 16.69 ? 101  ASN B ND2 1 
ATOM   4510 N  N   . ILE B 1 103 ? 19.136  -6.443  63.426  1.00 14.30 ? 102  ILE B N   1 
ATOM   4511 C  CA  . ILE B 1 103 ? 19.254  -5.984  62.048  1.00 14.13 ? 102  ILE B CA  1 
ATOM   4512 C  C   . ILE B 1 103 ? 17.884  -5.661  61.461  1.00 15.06 ? 102  ILE B C   1 
ATOM   4513 O  O   . ILE B 1 103 ? 17.738  -4.700  60.691  1.00 18.33 ? 102  ILE B O   1 
ATOM   4514 C  CB  . ILE B 1 103 ? 20.010  -7.035  61.206  1.00 14.62 ? 102  ILE B CB  1 
ATOM   4515 C  CG1 . ILE B 1 103 ? 21.503  -7.019  61.556  1.00 14.10 ? 102  ILE B CG1 1 
ATOM   4516 C  CG2 . ILE B 1 103 ? 19.800  -6.772  59.713  1.00 18.54 ? 102  ILE B CG2 1 
ATOM   4517 C  CD1 . ILE B 1 103 ? 22.272  -8.231  61.082  1.00 14.60 ? 102  ILE B CD1 1 
ATOM   4518 N  N   . LEU B 1 104 ? 16.855  -6.440  61.814  1.00 14.18 ? 103  LEU B N   1 
ATOM   4519 C  CA  . LEU B 1 104 ? 15.561  -6.333  61.147  1.00 15.36 ? 103  LEU B CA  1 
ATOM   4520 C  C   . LEU B 1 104 ? 14.544  -5.468  61.886  1.00 17.30 ? 103  LEU B C   1 
ATOM   4521 O  O   . LEU B 1 104 ? 13.576  -5.018  61.262  1.00 17.80 ? 103  LEU B O   1 
ATOM   4522 C  CB  . LEU B 1 104 ? 14.967  -7.731  60.914  1.00 17.08 ? 103  LEU B CB  1 
ATOM   4523 C  CG  . LEU B 1 104 ? 15.801  -8.617  59.970  1.00 16.81 ? 103  LEU B CG  1 
ATOM   4524 C  CD1 . LEU B 1 104 ? 15.249  -10.027 59.853  1.00 19.21 ? 103  LEU B CD1 1 
ATOM   4525 C  CD2 . LEU B 1 104 ? 15.944  -7.984  58.572  1.00 19.60 ? 103  LEU B CD2 1 
ATOM   4526 N  N   . LEU B 1 105 ? 14.727  -5.205  63.178  1.00 17.13 ? 104  LEU B N   1 
ATOM   4527 C  CA  . LEU B 1 105 ? 13.737  -4.394  63.888  1.00 20.22 ? 104  LEU B CA  1 
ATOM   4528 C  C   . LEU B 1 105 ? 13.503  -3.030  63.238  1.00 19.15 ? 104  LEU B C   1 
ATOM   4529 O  O   . LEU B 1 105 ? 12.338  -2.593  63.187  1.00 19.81 ? 104  LEU B O   1 
ATOM   4530 C  CB  . LEU B 1 105 ? 14.153  -4.243  65.357  1.00 20.92 ? 104  LEU B CB  1 
ATOM   4531 C  CG  . LEU B 1 105 ? 13.125  -3.653  66.324  1.00 23.84 ? 104  LEU B CG  1 
ATOM   4532 C  CD1 . LEU B 1 105 ? 11.879  -4.533  66.443  1.00 23.52 ? 104  LEU B CD1 1 
ATOM   4533 C  CD2 . LEU B 1 105 ? 13.759  -3.405  67.695  1.00 26.99 ? 104  LEU B CD2 1 
ATOM   4534 N  N   . PRO B 1 106 ? 14.519  -2.321  62.731  1.00 22.65 ? 105  PRO B N   1 
ATOM   4535 C  CA  . PRO B 1 106 ? 14.246  -1.045  62.047  1.00 24.12 ? 105  PRO B CA  1 
ATOM   4536 C  C   . PRO B 1 106 ? 13.336  -1.176  60.840  1.00 24.40 ? 105  PRO B C   1 
ATOM   4537 O  O   . PRO B 1 106 ? 12.727  -0.174  60.443  1.00 27.69 ? 105  PRO B O   1 
ATOM   4538 C  CB  . PRO B 1 106 ? 15.642  -0.555  61.638  1.00 25.88 ? 105  PRO B CB  1 
ATOM   4539 C  CG  . PRO B 1 106 ? 16.572  -1.210  62.633  1.00 24.83 ? 105  PRO B CG  1 
ATOM   4540 C  CD  . PRO B 1 106 ? 15.965  -2.568  62.880  1.00 23.17 ? 105  PRO B CD  1 
ATOM   4541 N  N   . SER B 1 107 ? 13.237  -2.364  60.229  1.00 20.26 ? 106  SER B N   1 
ATOM   4542 C  CA  . SER B 1 107 ? 12.332  -2.578  59.104  1.00 20.65 ? 106  SER B CA  1 
ATOM   4543 C  C   . SER B 1 107 ? 10.873  -2.530  59.509  1.00 19.84 ? 106  SER B C   1 
ATOM   4544 O  O   . SER B 1 107 ? 9.994   -2.628  58.644  1.00 18.75 ? 106  SER B O   1 
ATOM   4545 C  CB  . SER B 1 107 ? 12.622  -3.918  58.432  1.00 24.44 ? 106  SER B CB  1 
ATOM   4546 O  OG  . SER B 1 107 ? 13.875  -3.873  57.781  1.00 31.06 ? 106  SER B OG  1 
ATOM   4547 N  N   . PHE B 1 108 ? 10.592  -2.379  60.797  1.00 20.97 ? 107  PHE B N   1 
ATOM   4548 C  CA  . PHE B 1 108 ? 9.219   -2.313  61.269  1.00 24.45 ? 107  PHE B CA  1 
ATOM   4549 C  C   . PHE B 1 108 ? 8.993   -1.063  62.114  1.00 30.80 ? 107  PHE B C   1 
ATOM   4550 O  O   . PHE B 1 108 ? 8.138   -1.051  62.999  1.00 36.43 ? 107  PHE B O   1 
ATOM   4551 C  CB  . PHE B 1 108 ? 8.863   -3.594  62.018  1.00 25.61 ? 107  PHE B CB  1 
ATOM   4552 C  CG  . PHE B 1 108 ? 8.923   -4.818  61.139  1.00 24.39 ? 107  PHE B CG  1 
ATOM   4553 C  CD1 . PHE B 1 108 ? 7.857   -5.143  60.305  1.00 24.51 ? 107  PHE B CD1 1 
ATOM   4554 C  CD2 . PHE B 1 108 ? 10.058  -5.607  61.100  1.00 22.80 ? 107  PHE B CD2 1 
ATOM   4555 C  CE1 . PHE B 1 108 ? 7.920   -6.251  59.471  1.00 23.09 ? 107  PHE B CE1 1 
ATOM   4556 C  CE2 . PHE B 1 108 ? 10.129  -6.715  60.265  1.00 21.75 ? 107  PHE B CE2 1 
ATOM   4557 C  CZ  . PHE B 1 108 ? 9.061   -7.039  59.454  1.00 23.81 ? 107  PHE B CZ  1 
ATOM   4558 N  N   . SER B 1 109 ? 9.739   0.002   61.827  1.00 33.04 ? 108  SER B N   1 
ATOM   4559 C  CA  . SER B 1 109 ? 9.535   1.307   62.444  1.00 35.39 ? 108  SER B CA  1 
ATOM   4560 C  C   . SER B 1 109 ? 8.430   2.075   61.718  1.00 37.49 ? 108  SER B C   1 
ATOM   4561 O  O   . SER B 1 109 ? 8.009   1.717   60.614  1.00 35.67 ? 108  SER B O   1 
ATOM   4562 C  CB  . SER B 1 109 ? 10.824  2.122   62.412  1.00 39.85 ? 108  SER B CB  1 
ATOM   4563 O  OG  . SER B 1 109 ? 11.164  2.457   61.073  1.00 37.72 ? 108  SER B OG  1 
ATOM   4564 N  N   . GLN B 1 110 ? 7.968   3.164   62.344  1.00 39.90 ? 109  GLN B N   1 
ATOM   4565 C  CA  . GLN B 1 110 ? 6.934   3.975   61.711  1.00 41.93 ? 109  GLN B CA  1 
ATOM   4566 C  C   . GLN B 1 110 ? 7.401   4.499   60.356  1.00 37.84 ? 109  GLN B C   1 
ATOM   4567 O  O   . GLN B 1 110 ? 6.644   4.477   59.378  1.00 34.41 ? 109  GLN B O   1 
ATOM   4568 C  CB  . GLN B 1 110 ? 6.522   5.133   62.624  1.00 49.14 ? 109  GLN B CB  1 
ATOM   4569 C  CG  . GLN B 1 110 ? 7.507   6.290   62.651  1.00 55.14 ? 109  GLN B CG  1 
ATOM   4570 C  CD  . GLN B 1 110 ? 6.832   7.641   62.850  1.00 58.83 ? 109  GLN B CD  1 
ATOM   4571 O  OE1 . GLN B 1 110 ? 5.777   7.740   63.481  1.00 60.06 ? 109  GLN B OE1 1 
ATOM   4572 N  NE2 . GLN B 1 110 ? 7.438   8.688   62.302  1.00 59.62 ? 109  GLN B NE2 1 
ATOM   4573 N  N   . GLN B 1 111 ? 8.645   4.976   60.275  1.00 39.91 ? 110  GLN B N   1 
ATOM   4574 C  CA  . GLN B 1 111 ? 9.151   5.443   58.989  1.00 42.37 ? 110  GLN B CA  1 
ATOM   4575 C  C   . GLN B 1 111 ? 9.103   4.329   57.952  1.00 38.17 ? 110  GLN B C   1 
ATOM   4576 O  O   . GLN B 1 111 ? 8.790   4.573   56.779  1.00 33.39 ? 110  GLN B O   1 
ATOM   4577 C  CB  . GLN B 1 111 ? 10.573  5.987   59.136  1.00 48.58 ? 110  GLN B CB  1 
ATOM   4578 C  CG  . GLN B 1 111 ? 11.273  6.215   57.798  1.00 53.78 ? 110  GLN B CG  1 
ATOM   4579 C  CD  . GLN B 1 111 ? 12.329  7.304   57.854  1.00 59.49 ? 110  GLN B CD  1 
ATOM   4580 O  OE1 . GLN B 1 111 ? 12.165  8.309   58.547  1.00 61.91 ? 110  GLN B OE1 1 
ATOM   4581 N  NE2 . GLN B 1 111 ? 13.419  7.110   57.117  1.00 60.94 ? 110  GLN B NE2 1 
ATOM   4582 N  N   . ALA B 1 112 ? 9.401   3.096   58.372  1.00 34.49 ? 111  ALA B N   1 
ATOM   4583 C  CA  . ALA B 1 112 ? 9.277   1.952   57.477  1.00 30.93 ? 111  ALA B CA  1 
ATOM   4584 C  C   . ALA B 1 112 ? 7.827   1.733   57.063  1.00 26.20 ? 111  ALA B C   1 
ATOM   4585 O  O   . ALA B 1 112 ? 7.539   1.500   55.885  1.00 28.31 ? 111  ALA B O   1 
ATOM   4586 C  CB  . ALA B 1 112 ? 9.844   0.697   58.145  1.00 30.65 ? 111  ALA B CB  1 
ATOM   4587 N  N   . MET B 1 113 ? 6.897   1.808   58.022  1.00 23.09 ? 112  MET B N   1 
ATOM   4588 C  CA  . MET B 1 113 ? 5.489   1.561   57.712  1.00 20.86 ? 112  MET B CA  1 
ATOM   4589 C  C   . MET B 1 113 ? 4.947   2.605   56.741  1.00 16.99 ? 112  MET B C   1 
ATOM   4590 O  O   . MET B 1 113 ? 4.196   2.273   55.813  1.00 18.12 ? 112  MET B O   1 
ATOM   4591 C  CB  . MET B 1 113 ? 4.655   1.538   58.994  1.00 27.22 ? 112  MET B CB  1 
ATOM   4592 C  CG  . MET B 1 113 ? 4.884   0.319   59.896  1.00 29.98 ? 112  MET B CG  1 
ATOM   4593 S  SD  . MET B 1 113 ? 4.494   -1.268  59.122  1.00 25.94 ? 112  MET B SD  1 
ATOM   4594 C  CE  . MET B 1 113 ? 2.802   -0.976  58.613  1.00 33.15 ? 112  MET B CE  1 
ATOM   4595 N  N   . LYS B 1 114 ? 5.310   3.875   56.935  1.00 19.11 ? 113  LYS B N   1 
ATOM   4596 C  CA  . LYS B 1 114 ? 4.958   4.881   55.940  1.00 19.68 ? 113  LYS B CA  1 
ATOM   4597 C  C   . LYS B 1 114 ? 5.507   4.509   54.573  1.00 20.79 ? 113  LYS B C   1 
ATOM   4598 O  O   . LYS B 1 114 ? 4.869   4.781   53.547  1.00 20.31 ? 113  LYS B O   1 
ATOM   4599 C  CB  . LYS B 1 114 ? 5.481   6.250   56.370  1.00 20.27 ? 113  LYS B CB  1 
ATOM   4600 C  CG  . LYS B 1 114 ? 4.861   6.747   57.667  1.00 20.35 ? 113  LYS B CG  1 
ATOM   4601 C  CD  . LYS B 1 114 ? 5.469   8.062   58.130  1.00 23.96 ? 113  LYS B CD  1 
ATOM   4602 C  CE  . LYS B 1 114 ? 4.828   8.513   59.430  1.00 27.55 ? 113  LYS B CE  1 
ATOM   4603 N  NZ  . LYS B 1 114 ? 5.493   9.707   60.018  1.00 31.89 ? 113  LYS B NZ  1 
ATOM   4604 N  N   . GLY B 1 115 ? 6.684   3.877   54.544  1.00 19.01 ? 114  GLY B N   1 
ATOM   4605 C  CA  . GLY B 1 115 ? 7.280   3.476   53.284  1.00 20.21 ? 114  GLY B CA  1 
ATOM   4606 C  C   . GLY B 1 115 ? 6.635   2.264   52.641  1.00 20.97 ? 114  GLY B C   1 
ATOM   4607 O  O   . GLY B 1 115 ? 6.687   2.121   51.414  1.00 23.92 ? 114  GLY B O   1 
ATOM   4608 N  N   . TYR B 1 116 ? 6.037   1.370   53.445  1.00 17.25 ? 115  TYR B N   1 
ATOM   4609 C  CA  . TYR B 1 116 ? 5.330   0.203   52.912  1.00 15.99 ? 115  TYR B CA  1 
ATOM   4610 C  C   . TYR B 1 116 ? 3.932   0.540   52.415  1.00 14.63 ? 115  TYR B C   1 
ATOM   4611 O  O   . TYR B 1 116 ? 3.364   -0.224  51.625  1.00 16.00 ? 115  TYR B O   1 
ATOM   4612 C  CB  . TYR B 1 116 ? 5.186   -0.898  53.977  1.00 15.91 ? 115  TYR B CB  1 
ATOM   4613 C  CG  . TYR B 1 116 ? 6.472   -1.490  54.505  1.00 18.29 ? 115  TYR B CG  1 
ATOM   4614 C  CD1 . TYR B 1 116 ? 7.520   -1.816  53.653  1.00 20.17 ? 115  TYR B CD1 1 
ATOM   4615 C  CD2 . TYR B 1 116 ? 6.633   -1.735  55.866  1.00 18.86 ? 115  TYR B CD2 1 
ATOM   4616 C  CE1 . TYR B 1 116 ? 8.697   -2.366  54.142  1.00 20.29 ? 115  TYR B CE1 1 
ATOM   4617 C  CE2 . TYR B 1 116 ? 7.801   -2.283  56.367  1.00 18.98 ? 115  TYR B CE2 1 
ATOM   4618 C  CZ  . TYR B 1 116 ? 8.833   -2.594  55.505  1.00 19.48 ? 115  TYR B CZ  1 
ATOM   4619 O  OH  . TYR B 1 116 ? 9.997   -3.135  56.003  1.00 21.13 ? 115  TYR B OH  1 
ATOM   4620 N  N   . HIS B 1 117 ? 3.378   1.665   52.861  1.00 14.29 ? 116  HIS B N   1 
ATOM   4621 C  CA  . HIS B 1 117 ? 1.955   1.935   52.684  1.00 12.97 ? 116  HIS B CA  1 
ATOM   4622 C  C   . HIS B 1 117 ? 1.522   1.876   51.217  1.00 12.36 ? 116  HIS B C   1 
ATOM   4623 O  O   . HIS B 1 117 ? 0.468   1.308   50.897  1.00 12.84 ? 116  HIS B O   1 
ATOM   4624 C  CB  . HIS B 1 117 ? 1.616   3.293   53.288  1.00 13.06 ? 116  HIS B CB  1 
ATOM   4625 C  CG  . HIS B 1 117 ? 0.181   3.662   53.129  1.00 13.14 ? 116  HIS B CG  1 
ATOM   4626 N  ND1 . HIS B 1 117 ? -0.777  3.336   54.065  1.00 13.47 ? 116  HIS B ND1 1 
ATOM   4627 C  CD2 . HIS B 1 117 ? -0.467  4.302   52.128  1.00 13.14 ? 116  HIS B CD2 1 
ATOM   4628 C  CE1 . HIS B 1 117 ? -1.956  3.759   53.645  1.00 14.86 ? 116  HIS B CE1 1 
ATOM   4629 N  NE2 . HIS B 1 117 ? -1.795  4.352   52.473  1.00 13.38 ? 116  HIS B NE2 1 
ATOM   4630 N  N   . ALA B 1 118 ? 2.293   2.495   50.313  1.00 13.58 ? 117  ALA B N   1 
ATOM   4631 C  CA  . ALA B 1 118 ? 1.856   2.575   48.920  1.00 16.29 ? 117  ALA B CA  1 
ATOM   4632 C  C   . ALA B 1 118 ? 1.743   1.189   48.288  1.00 14.90 ? 117  ALA B C   1 
ATOM   4633 O  O   . ALA B 1 118 ? 0.839   0.936   47.481  1.00 14.94 ? 117  ALA B O   1 
ATOM   4634 C  CB  . ALA B 1 118 ? 2.815   3.454   48.119  1.00 17.46 ? 117  ALA B CB  1 
ATOM   4635 N  N   . MET B 1 119 ? 2.663   0.281   48.618  1.00 13.97 ? 118  MET B N   1 
ATOM   4636 C  CA  A MET B 1 119 ? 2.596   -1.073  48.077  0.60 14.49 ? 118  MET B CA  1 
ATOM   4637 C  CA  B MET B 1 119 ? 2.550   -1.045  48.029  0.40 15.48 ? 118  MET B CA  1 
ATOM   4638 C  C   . MET B 1 119 ? 1.471   -1.879  48.716  1.00 14.14 ? 118  MET B C   1 
ATOM   4639 O  O   . MET B 1 119 ? 0.892   -2.761  48.075  1.00 16.04 ? 118  MET B O   1 
ATOM   4640 C  CB  A MET B 1 119 ? 3.943   -1.777  48.262  0.60 14.60 ? 118  MET B CB  1 
ATOM   4641 C  CB  B MET B 1 119 ? 3.905   -1.756  48.042  0.40 18.18 ? 118  MET B CB  1 
ATOM   4642 C  CG  A MET B 1 119 ? 5.019   -1.307  47.283  0.60 16.47 ? 118  MET B CG  1 
ATOM   4643 C  CG  B MET B 1 119 ? 4.898   -1.203  46.997  0.40 21.48 ? 118  MET B CG  1 
ATOM   4644 S  SD  A MET B 1 119 ? 6.667   -1.914  47.707  0.60 21.10 ? 118  MET B SD  1 
ATOM   4645 S  SD  B MET B 1 119 ? 4.254   -1.027  45.302  0.40 26.09 ? 118  MET B SD  1 
ATOM   4646 C  CE  A MET B 1 119 ? 7.550   -1.594  46.178  0.60 22.29 ? 118  MET B CE  1 
ATOM   4647 C  CE  B MET B 1 119 ? 4.046   0.747   45.178  0.40 26.01 ? 118  MET B CE  1 
ATOM   4648 N  N   . MET B 1 120 ? 1.156   -1.612  49.989  1.00 13.53 ? 119  MET B N   1 
ATOM   4649 C  CA  . MET B 1 120 ? -0.034  -2.236  50.560  1.00 12.01 ? 119  MET B CA  1 
ATOM   4650 C  C   . MET B 1 120 ? -1.285  -1.821  49.787  1.00 11.90 ? 119  MET B C   1 
ATOM   4651 O  O   . MET B 1 120 ? -2.148  -2.658  49.499  1.00 13.26 ? 119  MET B O   1 
ATOM   4652 C  CB  . MET B 1 120 ? -0.182  -1.874  52.040  1.00 10.11 ? 119  MET B CB  1 
ATOM   4653 C  CG  . MET B 1 120 ? 0.942   -2.371  52.931  1.00 13.05 ? 119  MET B CG  1 
ATOM   4654 S  SD  . MET B 1 120 ? 0.456   -2.198  54.666  1.00 14.68 ? 119  MET B SD  1 
ATOM   4655 C  CE  . MET B 1 120 ? 1.826   -3.023  55.476  1.00 12.16 ? 119  MET B CE  1 
ATOM   4656 N  N   . VAL B 1 121 ? -1.403  -0.529  49.455  1.00 13.01 ? 120  VAL B N   1 
ATOM   4657 C  CA  . VAL B 1 121 ? -2.557  -0.043  48.695  1.00 11.48 ? 120  VAL B CA  1 
ATOM   4658 C  C   . VAL B 1 121 ? -2.630  -0.727  47.334  1.00 11.21 ? 120  VAL B C   1 
ATOM   4659 O  O   . VAL B 1 121 ? -3.718  -1.070  46.854  1.00 12.77 ? 120  VAL B O   1 
ATOM   4660 C  CB  . VAL B 1 121 ? -2.508  1.497   48.556  1.00 13.26 ? 120  VAL B CB  1 
ATOM   4661 C  CG1 . VAL B 1 121 ? -3.606  1.991   47.602  1.00 14.79 ? 120  VAL B CG1 1 
ATOM   4662 C  CG2 . VAL B 1 121 ? -2.643  2.191   49.923  1.00 13.90 ? 120  VAL B CG2 1 
ATOM   4663 N  N   . ASP B 1 122 ? -1.475  -0.933  46.691  1.00 12.05 ? 121  ASP B N   1 
ATOM   4664 C  CA  . ASP B 1 122 ? -1.429  -1.607  45.391  1.00 12.94 ? 121  ASP B CA  1 
ATOM   4665 C  C   . ASP B 1 122 ? -2.186  -2.935  45.435  1.00 14.97 ? 121  ASP B C   1 
ATOM   4666 O  O   . ASP B 1 122 ? -3.045  -3.207  44.580  1.00 14.04 ? 121  ASP B O   1 
ATOM   4667 C  CB  . ASP B 1 122 ? 0.043   -1.806  44.981  1.00 13.41 ? 121  ASP B CB  1 
ATOM   4668 C  CG  . ASP B 1 122 ? 0.218   -2.444  43.593  1.00 16.02 ? 121  ASP B CG  1 
ATOM   4669 O  OD1 . ASP B 1 122 ? -0.232  -3.594  43.383  1.00 15.59 ? 121  ASP B OD1 1 
ATOM   4670 O  OD2 . ASP B 1 122 ? 0.840   -1.792  42.713  1.00 16.30 ? 121  ASP B OD2 1 
ATOM   4671 N  N   . ILE B 1 123 ? -1.895  -3.767  46.444  1.00 13.10 ? 122  ILE B N   1 
ATOM   4672 C  CA  . ILE B 1 123 ? -2.529  -5.083  46.534  1.00 14.00 ? 122  ILE B CA  1 
ATOM   4673 C  C   . ILE B 1 123 ? -3.986  -4.953  46.969  1.00 12.36 ? 122  ILE B C   1 
ATOM   4674 O  O   . ILE B 1 123 ? -4.866  -5.674  46.471  1.00 12.30 ? 122  ILE B O   1 
ATOM   4675 C  CB  . ILE B 1 123 ? -1.736  -6.005  47.487  1.00 11.21 ? 122  ILE B CB  1 
ATOM   4676 C  CG1 . ILE B 1 123 ? -0.249  -6.064  47.084  1.00 11.53 ? 122  ILE B CG1 1 
ATOM   4677 C  CG2 . ILE B 1 123 ? -2.382  -7.411  47.537  1.00 12.32 ? 122  ILE B CG2 1 
ATOM   4678 C  CD1 . ILE B 1 123 ? 0.007   -6.503  45.620  1.00 11.99 ? 122  ILE B CD1 1 
ATOM   4679 N  N   . ALA B 1 124 ? -4.267  -4.044  47.911  1.00 13.51 ? 123  ALA B N   1 
ATOM   4680 C  CA  . ALA B 1 124 ? -5.641  -3.834  48.353  1.00 12.23 ? 123  ALA B CA  1 
ATOM   4681 C  C   . ALA B 1 124 ? -6.536  -3.402  47.197  1.00 12.39 ? 123  ALA B C   1 
ATOM   4682 O  O   . ALA B 1 124 ? -7.696  -3.821  47.110  1.00 12.92 ? 123  ALA B O   1 
ATOM   4683 C  CB  . ALA B 1 124 ? -5.678  -2.801  49.488  1.00 12.76 ? 123  ALA B CB  1 
ATOM   4684 N  N   . VAL B 1 125 ? -6.016  -2.568  46.295  1.00 12.89 ? 124  VAL B N   1 
ATOM   4685 C  CA  . VAL B 1 125 ? -6.809  -2.145  45.145  1.00 13.09 ? 124  VAL B CA  1 
ATOM   4686 C  C   . VAL B 1 125 ? -7.093  -3.330  44.226  1.00 13.42 ? 124  VAL B C   1 
ATOM   4687 O  O   . VAL B 1 125 ? -8.194  -3.451  43.670  1.00 13.97 ? 124  VAL B O   1 
ATOM   4688 C  CB  . VAL B 1 125 ? -6.093  -0.987  44.420  1.00 12.32 ? 124  VAL B CB  1 
ATOM   4689 C  CG1 . VAL B 1 125 ? -6.717  -0.715  43.051  1.00 14.60 ? 124  VAL B CG1 1 
ATOM   4690 C  CG2 . VAL B 1 125 ? -6.129  0.253   45.299  1.00 13.81 ? 124  VAL B CG2 1 
ATOM   4691 N  N   . GLN B 1 126 ? -6.122  -4.237  44.067  1.00 13.18 ? 125  GLN B N   1 
ATOM   4692 C  CA  . GLN B 1 126 ? -6.376  -5.438  43.274  1.00 12.21 ? 125  GLN B CA  1 
ATOM   4693 C  C   . GLN B 1 126 ? -7.505  -6.271  43.875  1.00 13.37 ? 125  GLN B C   1 
ATOM   4694 O  O   . GLN B 1 126 ? -8.313  -6.854  43.140  1.00 14.90 ? 125  GLN B O   1 
ATOM   4695 C  CB  . GLN B 1 126 ? -5.106  -6.285  43.139  1.00 11.43 ? 125  GLN B CB  1 
ATOM   4696 C  CG  . GLN B 1 126 ? -4.002  -5.615  42.344  1.00 11.06 ? 125  GLN B CG  1 
ATOM   4697 C  CD  . GLN B 1 126 ? -2.846  -6.567  42.026  1.00 12.20 ? 125  GLN B CD  1 
ATOM   4698 O  OE1 . GLN B 1 126 ? -3.055  -7.683  41.549  1.00 12.87 ? 125  GLN B OE1 1 
ATOM   4699 N  NE2 . GLN B 1 126 ? -1.624  -6.123  42.294  1.00 12.72 ? 125  GLN B NE2 1 
ATOM   4700 N  N   . LEU B 1 127 ? -7.568  -6.352  45.211  1.00 12.87 ? 126  LEU B N   1 
ATOM   4701 C  CA  . LEU B 1 127 ? -8.663  -7.069  45.863  1.00 11.52 ? 126  LEU B CA  1 
ATOM   4702 C  C   . LEU B 1 127 ? -10.006 -6.407  45.574  1.00 11.53 ? 126  LEU B C   1 
ATOM   4703 O  O   . LEU B 1 127 ? -10.973 -7.079  45.187  1.00 12.93 ? 126  LEU B O   1 
ATOM   4704 C  CB  . LEU B 1 127 ? -8.423  -7.153  47.377  1.00 10.23 ? 126  LEU B CB  1 
ATOM   4705 C  CG  . LEU B 1 127 ? -9.570  -7.818  48.163  1.00 11.79 ? 126  LEU B CG  1 
ATOM   4706 C  CD1 . LEU B 1 127 ? -9.655  -9.345  47.941  1.00 14.24 ? 126  LEU B CD1 1 
ATOM   4707 C  CD2 . LEU B 1 127 ? -9.495  -7.514  49.660  1.00 14.89 ? 126  LEU B CD2 1 
ATOM   4708 N  N   . VAL B 1 128 ? -10.098 -5.088  45.781  1.00 11.07 ? 127  VAL B N   1 
ATOM   4709 C  CA  . VAL B 1 128 ? -11.362 -4.391  45.532  1.00 11.07 ? 127  VAL B CA  1 
ATOM   4710 C  C   . VAL B 1 128 ? -11.787 -4.557  44.071  1.00 15.17 ? 127  VAL B C   1 
ATOM   4711 O  O   . VAL B 1 128 ? -12.966 -4.794  43.776  1.00 15.68 ? 127  VAL B O   1 
ATOM   4712 C  CB  . VAL B 1 128 ? -11.238 -2.908  45.944  1.00 11.97 ? 127  VAL B CB  1 
ATOM   4713 C  CG1 . VAL B 1 128 ? -12.462 -2.096  45.509  1.00 12.22 ? 127  VAL B CG1 1 
ATOM   4714 C  CG2 . VAL B 1 128 ? -11.074 -2.808  47.462  1.00 12.39 ? 127  VAL B CG2 1 
ATOM   4715 N  N   . GLN B 1 129 ? -10.841 -4.456  43.131  1.00 12.86 ? 128  GLN B N   1 
ATOM   4716 C  CA  . GLN B 1 129 ? -11.226 -4.583  41.726  1.00 13.13 ? 128  GLN B CA  1 
ATOM   4717 C  C   . GLN B 1 129 ? -11.708 -5.994  41.395  1.00 14.28 ? 128  GLN B C   1 
ATOM   4718 O  O   . GLN B 1 129 ? -12.620 -6.169  40.573  1.00 14.46 ? 128  GLN B O   1 
ATOM   4719 C  CB  . GLN B 1 129 ? -10.065 -4.176  40.818  1.00 15.14 ? 128  GLN B CB  1 
ATOM   4720 C  CG  . GLN B 1 129 ? -9.783  -2.693  40.883  1.00 23.66 ? 128  GLN B CG  1 
ATOM   4721 C  CD  . GLN B 1 129 ? -8.630  -2.281  40.009  1.00 36.47 ? 128  GLN B CD  1 
ATOM   4722 O  OE1 . GLN B 1 129 ? -7.637  -2.999  39.899  1.00 41.00 ? 128  GLN B OE1 1 
ATOM   4723 N  NE2 . GLN B 1 129 ? -8.753  -1.118  39.375  1.00 40.80 ? 128  GLN B NE2 1 
ATOM   4724 N  N   . LYS B 1 130 ? -11.106 -7.020  41.999  1.00 12.07 ? 129  LYS B N   1 
ATOM   4725 C  CA  . LYS B 1 130 ? -11.601 -8.371  41.761  1.00 12.07 ? 129  LYS B CA  1 
ATOM   4726 C  C   . LYS B 1 130 ? -13.076 -8.470  42.137  1.00 13.18 ? 129  LYS B C   1 
ATOM   4727 O  O   . LYS B 1 130 ? -13.904 -8.977  41.368  1.00 13.88 ? 129  LYS B O   1 
ATOM   4728 C  CB  . LYS B 1 130 ? -10.777 -9.393  42.554  1.00 11.68 ? 129  LYS B CB  1 
ATOM   4729 C  CG  . LYS B 1 130 ? -11.322 -10.810 42.392  1.00 12.88 ? 129  LYS B CG  1 
ATOM   4730 C  CD  . LYS B 1 130 ? -10.510 -11.873 43.121  1.00 14.96 ? 129  LYS B CD  1 
ATOM   4731 C  CE  . LYS B 1 130 ? -11.074 -13.272 42.848  1.00 17.17 ? 129  LYS B CE  1 
ATOM   4732 N  NZ  . LYS B 1 130 ? -10.244 -14.362 43.427  1.00 16.94 ? 129  LYS B NZ  1 
ATOM   4733 N  N   . TRP B 1 131 ? -13.425 -7.969  43.320  1.00 13.24 ? 130  TRP B N   1 
ATOM   4734 C  CA  . TRP B 1 131 ? -14.799 -8.069  43.792  1.00 12.47 ? 130  TRP B CA  1 
ATOM   4735 C  C   . TRP B 1 131 ? -15.745 -7.165  43.005  1.00 12.78 ? 130  TRP B C   1 
ATOM   4736 O  O   . TRP B 1 131 ? -16.913 -7.526  42.812  1.00 13.42 ? 130  TRP B O   1 
ATOM   4737 C  CB  . TRP B 1 131 ? -14.845 -7.748  45.287  1.00 12.57 ? 130  TRP B CB  1 
ATOM   4738 C  CG  . TRP B 1 131 ? -14.145 -8.785  46.125  1.00 12.68 ? 130  TRP B CG  1 
ATOM   4739 C  CD1 . TRP B 1 131 ? -13.546 -9.941  45.684  1.00 15.85 ? 130  TRP B CD1 1 
ATOM   4740 C  CD2 . TRP B 1 131 ? -13.983 -8.768  47.546  1.00 12.30 ? 130  TRP B CD2 1 
ATOM   4741 N  NE1 . TRP B 1 131 ? -13.018 -10.638 46.750  1.00 13.49 ? 130  TRP B NE1 1 
ATOM   4742 C  CE2 . TRP B 1 131 ? -13.267 -9.937  47.902  1.00 14.59 ? 130  TRP B CE2 1 
ATOM   4743 C  CE3 . TRP B 1 131 ? -14.362 -7.872  48.553  1.00 10.91 ? 130  TRP B CE3 1 
ATOM   4744 C  CZ2 . TRP B 1 131 ? -12.941 -10.239 49.223  1.00 13.29 ? 130  TRP B CZ2 1 
ATOM   4745 C  CZ3 . TRP B 1 131 ? -14.024 -8.173  49.870  1.00 12.99 ? 130  TRP B CZ3 1 
ATOM   4746 C  CH2 . TRP B 1 131 ? -13.326 -9.344  50.189  1.00 13.75 ? 130  TRP B CH2 1 
ATOM   4747 N  N   . GLU B 1 132 ? -15.278 -5.987  42.559  1.00 14.06 ? 131  GLU B N   1 
ATOM   4748 C  CA  . GLU B 1 132 ? -16.119 -5.144  41.704  1.00 15.80 ? 131  GLU B CA  1 
ATOM   4749 C  C   . GLU B 1 132 ? -16.465 -5.835  40.392  1.00 14.72 ? 131  GLU B C   1 
ATOM   4750 O  O   . GLU B 1 132 ? -17.496 -5.523  39.778  1.00 16.09 ? 131  GLU B O   1 
ATOM   4751 C  CB  . GLU B 1 132 ? -15.433 -3.814  41.374  1.00 14.09 ? 131  GLU B CB  1 
ATOM   4752 C  CG  . GLU B 1 132 ? -15.149 -2.873  42.549  1.00 16.93 ? 131  GLU B CG  1 
ATOM   4753 C  CD  . GLU B 1 132 ? -16.372 -2.102  43.008  1.00 19.49 ? 131  GLU B CD  1 
ATOM   4754 O  OE1 . GLU B 1 132 ? -17.498 -2.560  42.731  1.00 17.96 ? 131  GLU B OE1 1 
ATOM   4755 O  OE2 . GLU B 1 132 ? -16.209 -1.037  43.645  1.00 21.59 ? 131  GLU B OE2 1 
ATOM   4756 N  N   . ARG B 1 133 ? -15.606 -6.737  39.924  1.00 12.99 ? 132  ARG B N   1 
ATOM   4757 C  CA  . ARG B 1 133 ? -15.777 -7.342  38.611  1.00 14.37 ? 132  ARG B CA  1 
ATOM   4758 C  C   . ARG B 1 133 ? -16.531 -8.665  38.647  1.00 14.32 ? 132  ARG B C   1 
ATOM   4759 O  O   . ARG B 1 133 ? -16.686 -9.296  37.596  1.00 16.10 ? 132  ARG B O   1 
ATOM   4760 C  CB  . ARG B 1 133 ? -14.407 -7.521  37.942  1.00 13.65 ? 132  ARG B CB  1 
ATOM   4761 C  CG  . ARG B 1 133 ? -13.771 -6.179  37.594  1.00 11.16 ? 132  ARG B CG  1 
ATOM   4762 C  CD  . ARG B 1 133 ? -12.282 -6.249  37.287  1.00 12.88 ? 132  ARG B CD  1 
ATOM   4763 N  NE  . ARG B 1 133 ? -11.798 -4.959  36.801  1.00 16.97 ? 132  ARG B NE  1 
ATOM   4764 C  CZ  . ARG B 1 133 ? -10.520 -4.613  36.701  1.00 17.38 ? 132  ARG B CZ  1 
ATOM   4765 N  NH1 . ARG B 1 133 ? -9.547  -5.438  37.057  1.00 16.08 ? 132  ARG B NH1 1 
ATOM   4766 N  NH2 . ARG B 1 133 ? -10.209 -3.404  36.241  1.00 18.99 ? 132  ARG B NH2 1 
ATOM   4767 N  N   . LEU B 1 134 ? -17.020 -9.094  39.807  1.00 14.84 ? 133  LEU B N   1 
ATOM   4768 C  CA  . LEU B 1 134 ? -17.821 -10.311 39.853  1.00 15.09 ? 133  LEU B CA  1 
ATOM   4769 C  C   . LEU B 1 134 ? -19.183 -10.086 39.192  1.00 15.10 ? 133  LEU B C   1 
ATOM   4770 O  O   . LEU B 1 134 ? -19.735 -8.980  39.212  1.00 18.46 ? 133  LEU B O   1 
ATOM   4771 C  CB  . LEU B 1 134 ? -18.004 -10.783 41.300  1.00 15.92 ? 133  LEU B CB  1 
ATOM   4772 C  CG  . LEU B 1 134 ? -16.729 -11.246 42.020  1.00 14.76 ? 133  LEU B CG  1 
ATOM   4773 C  CD1 . LEU B 1 134 ? -17.014 -11.603 43.483  1.00 17.50 ? 133  LEU B CD1 1 
ATOM   4774 C  CD2 . LEU B 1 134 ? -16.065 -12.425 41.301  1.00 15.95 ? 133  LEU B CD2 1 
ATOM   4775 N  N   . ASN B 1 135 ? -19.726 -11.154 38.602  1.00 14.68 ? 134  ASN B N   1 
ATOM   4776 C  CA  . ASN B 1 135 ? -21.045 -11.098 37.987  1.00 15.04 ? 134  ASN B CA  1 
ATOM   4777 C  C   . ASN B 1 135 ? -22.148 -11.308 39.023  1.00 20.51 ? 134  ASN B C   1 
ATOM   4778 O  O   . ASN B 1 135 ? -21.905 -11.695 40.172  1.00 20.52 ? 134  ASN B O   1 
ATOM   4779 C  CB  . ASN B 1 135 ? -21.183 -12.154 36.891  1.00 15.73 ? 134  ASN B CB  1 
ATOM   4780 C  CG  . ASN B 1 135 ? -20.141 -12.001 35.809  1.00 16.03 ? 134  ASN B CG  1 
ATOM   4781 O  OD1 . ASN B 1 135 ? -20.160 -11.032 35.046  1.00 18.44 ? 134  ASN B OD1 1 
ATOM   4782 N  ND2 . ASN B 1 135 ? -19.215 -12.949 35.743  1.00 15.86 ? 134  ASN B ND2 1 
ATOM   4783 N  N   . ALA B 1 136 ? -23.386 -11.076 38.581  1.00 21.87 ? 135  ALA B N   1 
ATOM   4784 C  CA  . ALA B 1 136 ? -24.546 -11.220 39.446  1.00 25.45 ? 135  ALA B CA  1 
ATOM   4785 C  C   . ALA B 1 136 ? -24.526 -12.560 40.163  1.00 27.56 ? 135  ALA B C   1 
ATOM   4786 O  O   . ALA B 1 136 ? -24.331 -13.610 39.547  1.00 27.18 ? 135  ALA B O   1 
ATOM   4787 C  CB  . ALA B 1 136 ? -25.831 -11.083 38.628  1.00 26.42 ? 135  ALA B CB  1 
ATOM   4788 N  N   . ASP B 1 137 ? -24.707 -12.507 41.479  1.00 29.97 ? 136  ASP B N   1 
ATOM   4789 C  CA  . ASP B 1 137 ? -24.890 -13.655 42.357  1.00 32.73 ? 136  ASP B CA  1 
ATOM   4790 C  C   . ASP B 1 137 ? -23.697 -14.602 42.404  1.00 28.05 ? 136  ASP B C   1 
ATOM   4791 O  O   . ASP B 1 137 ? -23.810 -15.687 42.986  1.00 30.97 ? 136  ASP B O   1 
ATOM   4792 C  CB  . ASP B 1 137 ? -26.163 -14.421 41.996  1.00 39.54 ? 136  ASP B CB  1 
ATOM   4793 C  CG  . ASP B 1 137 ? -27.411 -13.675 42.424  1.00 43.52 ? 136  ASP B CG  1 
ATOM   4794 O  OD1 . ASP B 1 137 ? -27.413 -13.131 43.556  1.00 45.10 ? 136  ASP B OD1 1 
ATOM   4795 O  OD2 . ASP B 1 137 ? -28.372 -13.614 41.627  1.00 45.97 ? 136  ASP B OD2 1 
ATOM   4796 N  N   . GLU B 1 138 ? -22.553 -14.225 41.842  1.00 23.50 ? 137  GLU B N   1 
ATOM   4797 C  CA  . GLU B 1 138 ? -21.320 -14.901 42.210  1.00 18.97 ? 137  GLU B CA  1 
ATOM   4798 C  C   . GLU B 1 138 ? -20.962 -14.543 43.650  1.00 20.08 ? 137  GLU B C   1 
ATOM   4799 O  O   . GLU B 1 138 ? -21.411 -13.530 44.192  1.00 22.41 ? 137  GLU B O   1 
ATOM   4800 C  CB  . GLU B 1 138 ? -20.187 -14.522 41.253  1.00 17.53 ? 137  GLU B CB  1 
ATOM   4801 C  CG  . GLU B 1 138 ? -20.514 -14.949 39.835  1.00 17.49 ? 137  GLU B CG  1 
ATOM   4802 C  CD  . GLU B 1 138 ? -19.449 -14.602 38.812  1.00 18.51 ? 137  GLU B CD  1 
ATOM   4803 O  OE1 . GLU B 1 138 ? -18.547 -13.787 39.096  1.00 18.94 ? 137  GLU B OE1 1 
ATOM   4804 O  OE2 . GLU B 1 138 ? -19.538 -15.149 37.696  1.00 20.79 ? 137  GLU B OE2 1 
ATOM   4805 N  N   . HIS B 1 139 ? -20.162 -15.390 44.283  1.00 18.40 ? 138  HIS B N   1 
ATOM   4806 C  CA  . HIS B 1 139 ? -19.803 -15.164 45.677  1.00 17.83 ? 138  HIS B CA  1 
ATOM   4807 C  C   . HIS B 1 139 ? -18.292 -15.063 45.837  1.00 15.33 ? 138  HIS B C   1 
ATOM   4808 O  O   . HIS B 1 139 ? -17.518 -15.264 44.894  1.00 14.90 ? 138  HIS B O   1 
ATOM   4809 C  CB  . HIS B 1 139 ? -20.365 -16.270 46.586  1.00 20.29 ? 138  HIS B CB  1 
ATOM   4810 C  CG  . HIS B 1 139 ? -19.796 -17.627 46.313  1.00 21.11 ? 138  HIS B CG  1 
ATOM   4811 N  ND1 . HIS B 1 139 ? -20.390 -18.522 45.450  1.00 23.27 ? 138  HIS B ND1 1 
ATOM   4812 C  CD2 . HIS B 1 139 ? -18.691 -18.247 46.793  1.00 21.90 ? 138  HIS B CD2 1 
ATOM   4813 C  CE1 . HIS B 1 139 ? -19.674 -19.632 45.408  1.00 25.59 ? 138  HIS B CE1 1 
ATOM   4814 N  NE2 . HIS B 1 139 ? -18.636 -19.491 46.213  1.00 22.95 ? 138  HIS B NE2 1 
ATOM   4815 N  N   . ILE B 1 140 ? -17.888 -14.742 47.067  1.00 13.91 ? 139  ILE B N   1 
ATOM   4816 C  CA  . ILE B 1 140 ? -16.493 -14.543 47.449  1.00 12.55 ? 139  ILE B CA  1 
ATOM   4817 C  C   . ILE B 1 140 ? -16.084 -15.679 48.373  1.00 11.71 ? 139  ILE B C   1 
ATOM   4818 O  O   . ILE B 1 140 ? -16.796 -15.982 49.341  1.00 13.62 ? 139  ILE B O   1 
ATOM   4819 C  CB  . ILE B 1 140 ? -16.301 -13.186 48.152  1.00 15.68 ? 139  ILE B CB  1 
ATOM   4820 C  CG1 . ILE B 1 140 ? -16.525 -12.026 47.177  1.00 12.88 ? 139  ILE B CG1 1 
ATOM   4821 C  CG2 . ILE B 1 140 ? -14.933 -13.109 48.857  1.00 14.84 ? 139  ILE B CG2 1 
ATOM   4822 C  CD1 . ILE B 1 140 ? -16.764 -10.700 47.888  1.00 15.65 ? 139  ILE B CD1 1 
ATOM   4823 N  N   . GLU B 1 141 ? -14.943 -16.311 48.073  1.00 13.29 ? 140  GLU B N   1 
ATOM   4824 C  CA  . GLU B 1 141 ? -14.313 -17.280 48.976  1.00 13.53 ? 140  GLU B CA  1 
ATOM   4825 C  C   . GLU B 1 141 ? -13.363 -16.491 49.868  1.00 13.17 ? 140  GLU B C   1 
ATOM   4826 O  O   . GLU B 1 141 ? -12.283 -16.084 49.432  1.00 12.98 ? 140  GLU B O   1 
ATOM   4827 C  CB  . GLU B 1 141 ? -13.585 -18.368 48.186  1.00 15.00 ? 140  GLU B CB  1 
ATOM   4828 C  CG  . GLU B 1 141 ? -14.497 -19.144 47.235  1.00 18.25 ? 140  GLU B CG  1 
ATOM   4829 C  CD  . GLU B 1 141 ? -13.767 -20.221 46.444  1.00 20.88 ? 140  GLU B CD  1 
ATOM   4830 O  OE1 . GLU B 1 141 ? -12.551 -20.067 46.207  1.00 22.69 ? 140  GLU B OE1 1 
ATOM   4831 O  OE2 . GLU B 1 141 ? -14.413 -21.218 46.040  1.00 26.19 ? 140  GLU B OE2 1 
ATOM   4832 N  N   . VAL B 1 142 ? -13.759 -16.266 51.119  1.00 11.85 ? 141  VAL B N   1 
ATOM   4833 C  CA  . VAL B 1 142 ? -13.118 -15.235 51.940  1.00 11.32 ? 141  VAL B CA  1 
ATOM   4834 C  C   . VAL B 1 142 ? -11.682 -15.602 52.317  1.00 12.07 ? 141  VAL B C   1 
ATOM   4835 O  O   . VAL B 1 142 ? -10.759 -14.833 52.001  1.00 12.74 ? 141  VAL B O   1 
ATOM   4836 C  CB  . VAL B 1 142 ? -13.972 -14.922 53.182  1.00 9.45  ? 141  VAL B CB  1 
ATOM   4837 C  CG1 . VAL B 1 142 ? -13.204 -13.993 54.157  1.00 11.41 ? 141  VAL B CG1 1 
ATOM   4838 C  CG2 . VAL B 1 142 ? -15.291 -14.263 52.741  1.00 11.38 ? 141  VAL B CG2 1 
ATOM   4839 N  N   . PRO B 1 143 ? -11.422 -16.720 53.006  1.00 11.94 ? 142  PRO B N   1 
ATOM   4840 C  CA  . PRO B 1 143 ? -10.026 -17.009 53.384  1.00 11.79 ? 142  PRO B CA  1 
ATOM   4841 C  C   . PRO B 1 143 ? -9.119  -17.164 52.186  1.00 10.00 ? 142  PRO B C   1 
ATOM   4842 O  O   . PRO B 1 143 ? -7.940  -16.785 52.253  1.00 10.60 ? 142  PRO B O   1 
ATOM   4843 C  CB  . PRO B 1 143 ? -10.128 -18.311 54.195  1.00 13.17 ? 142  PRO B CB  1 
ATOM   4844 C  CG  . PRO B 1 143 ? -11.463 -18.893 53.847  1.00 14.49 ? 142  PRO B CG  1 
ATOM   4845 C  CD  . PRO B 1 143 ? -12.362 -17.717 53.553  1.00 12.67 ? 142  PRO B CD  1 
ATOM   4846 N  N   . GLU B 1 144 ? -9.649  -17.678 51.075  1.00 12.52 ? 143  GLU B N   1 
ATOM   4847 C  CA  . GLU B 1 144 ? -8.848  -17.821 49.865  1.00 12.54 ? 143  GLU B CA  1 
ATOM   4848 C  C   . GLU B 1 144 ? -8.385  -16.460 49.348  1.00 12.13 ? 143  GLU B C   1 
ATOM   4849 O  O   . GLU B 1 144 ? -7.205  -16.274 49.017  1.00 13.24 ? 143  GLU B O   1 
ATOM   4850 C  CB  . GLU B 1 144 ? -9.659  -18.567 48.803  1.00 12.99 ? 143  GLU B CB  1 
ATOM   4851 C  CG  . GLU B 1 144 ? -9.830  -20.056 49.087  1.00 16.35 ? 143  GLU B CG  1 
ATOM   4852 C  CD  . GLU B 1 144 ? -10.899 -20.381 50.133  1.00 16.50 ? 143  GLU B CD  1 
ATOM   4853 O  OE1 . GLU B 1 144 ? -11.676 -19.484 50.522  1.00 14.37 ? 143  GLU B OE1 1 
ATOM   4854 O  OE2 . GLU B 1 144 ? -10.963 -21.555 50.562  1.00 23.76 ? 143  GLU B OE2 1 
ATOM   4855 N  N   . ASP B 1 145 ? -9.305  -15.491 49.268  1.00 11.23 ? 144  ASP B N   1 
ATOM   4856 C  CA  . ASP B 1 145 ? -8.935  -14.166 48.781  1.00 11.89 ? 144  ASP B CA  1 
ATOM   4857 C  C   . ASP B 1 145 ? -8.124  -13.381 49.811  1.00 11.66 ? 144  ASP B C   1 
ATOM   4858 O  O   . ASP B 1 145 ? -7.278  -12.557 49.433  1.00 11.56 ? 144  ASP B O   1 
ATOM   4859 C  CB  . ASP B 1 145 ? -10.183 -13.386 48.370  1.00 12.25 ? 144  ASP B CB  1 
ATOM   4860 C  CG  . ASP B 1 145 ? -10.570 -13.630 46.921  1.00 11.92 ? 144  ASP B CG  1 
ATOM   4861 O  OD1 . ASP B 1 145 ? -9.760  -14.216 46.169  1.00 12.76 ? 144  ASP B OD1 1 
ATOM   4862 O  OD2 . ASP B 1 145 ? -11.681 -13.237 46.533  1.00 13.06 ? 144  ASP B OD2 1 
ATOM   4863 N  N   . MET B 1 146 ? -8.339  -13.623 51.111  1.00 10.92 ? 145  MET B N   1 
ATOM   4864 C  CA  . MET B 1 146 ? -7.495  -12.945 52.094  1.00 9.68  ? 145  MET B CA  1 
ATOM   4865 C  C   . MET B 1 146 ? -6.056  -13.445 52.025  1.00 10.49 ? 145  MET B C   1 
ATOM   4866 O  O   . MET B 1 146 ? -5.120  -12.666 52.243  1.00 11.91 ? 145  MET B O   1 
ATOM   4867 C  CB  . MET B 1 146 ? -8.066  -13.119 53.507  1.00 11.54 ? 145  MET B CB  1 
ATOM   4868 C  CG  . MET B 1 146 ? -9.442  -12.477 53.720  1.00 12.75 ? 145  MET B CG  1 
ATOM   4869 S  SD  . MET B 1 146 ? -9.517  -10.694 53.374  1.00 13.46 ? 145  MET B SD  1 
ATOM   4870 C  CE  . MET B 1 146 ? -10.209 -10.688 51.711  1.00 14.07 ? 145  MET B CE  1 
ATOM   4871 N  N   . THR B 1 147 ? -5.860  -14.728 51.709  1.00 10.83 ? 146  THR B N   1 
ATOM   4872 C  CA  . THR B 1 147 ? -4.512  -15.266 51.553  1.00 11.74 ? 146  THR B CA  1 
ATOM   4873 C  C   . THR B 1 147 ? -3.861  -14.752 50.272  1.00 12.26 ? 146  THR B C   1 
ATOM   4874 O  O   . THR B 1 147 ? -2.652  -14.488 50.245  1.00 12.62 ? 146  THR B O   1 
ATOM   4875 C  CB  . THR B 1 147 ? -4.569  -16.800 51.579  1.00 13.43 ? 146  THR B CB  1 
ATOM   4876 O  OG1 . THR B 1 147 ? -4.864  -17.240 52.910  1.00 16.83 ? 146  THR B OG1 1 
ATOM   4877 C  CG2 . THR B 1 147 ? -3.253  -17.433 51.117  1.00 16.25 ? 146  THR B CG2 1 
ATOM   4878 N  N   . ARG B 1 148 ? -4.639  -14.604 49.194  1.00 11.68 ? 147  ARG B N   1 
ATOM   4879 C  CA  . ARG B 1 148 ? -4.099  -13.931 48.011  1.00 11.66 ? 147  ARG B CA  1 
ATOM   4880 C  C   . ARG B 1 148 ? -3.565  -12.552 48.377  1.00 12.72 ? 147  ARG B C   1 
ATOM   4881 O  O   . ARG B 1 148 ? -2.466  -12.166 47.964  1.00 14.74 ? 147  ARG B O   1 
ATOM   4882 C  CB  . ARG B 1 148 ? -5.165  -13.798 46.918  1.00 13.14 ? 147  ARG B CB  1 
ATOM   4883 C  CG  . ARG B 1 148 ? -5.568  -15.092 46.225  1.00 12.04 ? 147  ARG B CG  1 
ATOM   4884 C  CD  . ARG B 1 148 ? -6.570  -14.813 45.102  1.00 13.40 ? 147  ARG B CD  1 
ATOM   4885 N  NE  . ARG B 1 148 ? -6.790  -16.007 44.292  1.00 17.11 ? 147  ARG B NE  1 
ATOM   4886 C  CZ  . ARG B 1 148 ? -7.723  -16.923 44.530  1.00 18.75 ? 147  ARG B CZ  1 
ATOM   4887 N  NH1 . ARG B 1 148 ? -8.625  -16.766 45.492  1.00 15.77 ? 147  ARG B NH1 1 
ATOM   4888 N  NH2 . ARG B 1 148 ? -7.752  -18.026 43.786  1.00 22.83 ? 147  ARG B NH2 1 
ATOM   4889 N  N   . LEU B 1 149 ? -4.338  -11.792 49.162  1.00 12.45 ? 148  LEU B N   1 
ATOM   4890 C  CA  . LEU B 1 149 ? -3.930  -10.435 49.514  1.00 12.41 ? 148  LEU B CA  1 
ATOM   4891 C  C   . LEU B 1 149 ? -2.689  -10.433 50.400  1.00 12.16 ? 148  LEU B C   1 
ATOM   4892 O  O   . LEU B 1 149 ? -1.712  -9.728  50.114  1.00 11.97 ? 148  LEU B O   1 
ATOM   4893 C  CB  . LEU B 1 149 ? -5.077  -9.701  50.217  1.00 13.00 ? 148  LEU B CB  1 
ATOM   4894 C  CG  . LEU B 1 149 ? -4.664  -8.323  50.747  1.00 16.68 ? 148  LEU B CG  1 
ATOM   4895 C  CD1 . LEU B 1 149 ? -5.460  -7.202  50.082  1.00 14.93 ? 148  LEU B CD1 1 
ATOM   4896 C  CD2 . LEU B 1 149 ? -4.794  -8.259  52.260  1.00 21.30 ? 148  LEU B CD2 1 
ATOM   4897 N  N   . THR B 1 150 ? -2.710  -11.186 51.504  1.00 10.96 ? 149  THR B N   1 
ATOM   4898 C  CA  . THR B 1 150 ? -1.612  -11.026 52.455  1.00 10.50 ? 149  THR B CA  1 
ATOM   4899 C  C   . THR B 1 150 ? -0.301  -11.606 51.928  1.00 11.57 ? 149  THR B C   1 
ATOM   4900 O  O   . THR B 1 150 ? 0.766   -11.055 52.213  1.00 12.77 ? 149  THR B O   1 
ATOM   4901 C  CB  . THR B 1 150 ? -1.969  -11.638 53.817  1.00 11.05 ? 149  THR B CB  1 
ATOM   4902 O  OG1 . THR B 1 150 ? -2.215  -13.040 53.676  1.00 12.15 ? 149  THR B OG1 1 
ATOM   4903 C  CG2 . THR B 1 150 ? -3.212  -10.950 54.401  1.00 12.46 ? 149  THR B CG2 1 
ATOM   4904 N  N   . LEU B 1 151 ? -0.339  -12.701 51.157  1.00 10.59 ? 150  LEU B N   1 
ATOM   4905 C  CA  . LEU B 1 151 ? 0.902   -13.192 50.567  1.00 12.18 ? 150  LEU B CA  1 
ATOM   4906 C  C   . LEU B 1 151 ? 1.490   -12.160 49.612  1.00 12.58 ? 150  LEU B C   1 
ATOM   4907 O  O   . LEU B 1 151 ? 2.698   -11.891 49.627  1.00 12.56 ? 150  LEU B O   1 
ATOM   4908 C  CB  . LEU B 1 151 ? 0.668   -14.513 49.833  1.00 13.83 ? 150  LEU B CB  1 
ATOM   4909 C  CG  . LEU B 1 151 ? 1.959   -15.051 49.218  1.00 15.66 ? 150  LEU B CG  1 
ATOM   4910 C  CD1 . LEU B 1 151 ? 2.854   -15.611 50.320  1.00 17.54 ? 150  LEU B CD1 1 
ATOM   4911 C  CD2 . LEU B 1 151 ? 1.662   -16.099 48.151  1.00 20.08 ? 150  LEU B CD2 1 
ATOM   4912 N  N   . ASP B 1 152 ? 0.646   -11.574 48.758  1.00 14.42 ? 151  ASP B N   1 
ATOM   4913 C  CA  . ASP B 1 152 ? 1.146   -10.581 47.814  1.00 12.46 ? 151  ASP B CA  1 
ATOM   4914 C  C   . ASP B 1 152 ? 1.676   -9.344  48.530  1.00 11.92 ? 151  ASP B C   1 
ATOM   4915 O  O   . ASP B 1 152 ? 2.637   -8.712  48.066  1.00 12.78 ? 151  ASP B O   1 
ATOM   4916 C  CB  . ASP B 1 152 ? 0.042   -10.192 46.833  1.00 13.79 ? 151  ASP B CB  1 
ATOM   4917 C  CG  . ASP B 1 152 ? -0.123  -11.202 45.707  1.00 17.09 ? 151  ASP B CG  1 
ATOM   4918 O  OD1 . ASP B 1 152 ? 0.282   -12.378 45.868  1.00 19.10 ? 151  ASP B OD1 1 
ATOM   4919 O  OD2 . ASP B 1 152 ? -0.656  -10.807 44.655  1.00 20.03 ? 151  ASP B OD2 1 
ATOM   4920 N  N   . THR B 1 153 ? 1.075   -8.984  49.661  1.00 12.17 ? 152  THR B N   1 
ATOM   4921 C  CA  . THR B 1 153 ? 1.536   -7.798  50.376  1.00 12.22 ? 152  THR B CA  1 
ATOM   4922 C  C   . THR B 1 153 ? 2.926   -8.010  50.967  1.00 12.56 ? 152  THR B C   1 
ATOM   4923 O  O   . THR B 1 153 ? 3.806   -7.150  50.826  1.00 11.36 ? 152  THR B O   1 
ATOM   4924 C  CB  . THR B 1 153 ? 0.534   -7.420  51.462  1.00 12.22 ? 152  THR B CB  1 
ATOM   4925 O  OG1 . THR B 1 153 ? -0.729  -7.117  50.848  1.00 13.29 ? 152  THR B OG1 1 
ATOM   4926 C  CG2 . THR B 1 153 ? 1.028   -6.196  52.223  1.00 13.22 ? 152  THR B CG2 1 
ATOM   4927 N  N   . ILE B 1 154 ? 3.154   -9.139  51.643  1.00 10.30 ? 153  ILE B N   1 
ATOM   4928 C  CA  . ILE B 1 154 ? 4.494   -9.326  52.201  1.00 12.13 ? 153  ILE B CA  1 
ATOM   4929 C  C   . ILE B 1 154 ? 5.509   -9.526  51.079  1.00 14.24 ? 153  ILE B C   1 
ATOM   4930 O  O   . ILE B 1 154 ? 6.647   -9.060  51.180  1.00 13.95 ? 153  ILE B O   1 
ATOM   4931 C  CB  . ILE B 1 154 ? 4.535   -10.473 53.240  1.00 11.28 ? 153  ILE B CB  1 
ATOM   4932 C  CG1 . ILE B 1 154 ? 5.915   -10.536 53.906  1.00 13.57 ? 153  ILE B CG1 1 
ATOM   4933 C  CG2 . ILE B 1 154 ? 4.215   -11.812 52.600  1.00 13.10 ? 153  ILE B CG2 1 
ATOM   4934 C  CD1 . ILE B 1 154 ? 6.245   -9.341  54.775  1.00 14.70 ? 153  ILE B CD1 1 
ATOM   4935 N  N   . GLY B 1 155 ? 5.116   -10.178 49.977  1.00 12.69 ? 154  GLY B N   1 
ATOM   4936 C  CA  . GLY B 1 155 ? 6.039   -10.320 48.860  1.00 11.84 ? 154  GLY B CA  1 
ATOM   4937 C  C   . GLY B 1 155 ? 6.464   -8.982  48.278  1.00 12.86 ? 154  GLY B C   1 
ATOM   4938 O  O   . GLY B 1 155 ? 7.653   -8.741  48.036  1.00 12.77 ? 154  GLY B O   1 
ATOM   4939 N  N   . LEU B 1 156 ? 5.498   -8.086  48.055  1.00 12.98 ? 155  LEU B N   1 
ATOM   4940 C  CA  . LEU B 1 156 ? 5.811   -6.808  47.424  1.00 12.80 ? 155  LEU B CA  1 
ATOM   4941 C  C   . LEU B 1 156 ? 6.486   -5.854  48.402  1.00 13.66 ? 155  LEU B C   1 
ATOM   4942 O  O   . LEU B 1 156 ? 7.552   -5.303  48.102  1.00 15.02 ? 155  LEU B O   1 
ATOM   4943 C  CB  . LEU B 1 156 ? 4.538   -6.184  46.840  1.00 13.54 ? 155  LEU B CB  1 
ATOM   4944 C  CG  . LEU B 1 156 ? 4.664   -4.875  46.057  1.00 13.72 ? 155  LEU B CG  1 
ATOM   4945 C  CD1 . LEU B 1 156 ? 5.567   -5.050  44.844  1.00 14.91 ? 155  LEU B CD1 1 
ATOM   4946 C  CD2 . LEU B 1 156 ? 3.283   -4.382  45.638  1.00 15.14 ? 155  LEU B CD2 1 
ATOM   4947 N  N   . CYS B 1 157 ? 5.886   -5.655  49.583  1.00 14.65 ? 156  CYS B N   1 
ATOM   4948 C  CA  . CYS B 1 157 ? 6.471   -4.746  50.571  1.00 12.97 ? 156  CYS B CA  1 
ATOM   4949 C  C   . CYS B 1 157 ? 7.822   -5.246  51.061  1.00 14.19 ? 156  CYS B C   1 
ATOM   4950 O  O   . CYS B 1 157 ? 8.762   -4.458  51.232  1.00 14.95 ? 156  CYS B O   1 
ATOM   4951 C  CB  . CYS B 1 157 ? 5.532   -4.578  51.772  1.00 13.72 ? 156  CYS B CB  1 
ATOM   4952 S  SG  . CYS B 1 157 ? 3.963   -3.804  51.410  1.00 16.93 ? 156  CYS B SG  1 
ATOM   4953 N  N   . GLY B 1 158 ? 7.927   -6.542  51.330  1.00 13.11 ? 157  GLY B N   1 
ATOM   4954 C  CA  . GLY B 1 158 ? 9.130   -7.063  51.942  1.00 12.10 ? 157  GLY B CA  1 
ATOM   4955 C  C   . GLY B 1 158 ? 10.246  -7.298  50.944  1.00 15.15 ? 157  GLY B C   1 
ATOM   4956 O  O   . GLY B 1 158 ? 11.422  -7.079  51.254  1.00 15.88 ? 157  GLY B O   1 
ATOM   4957 N  N   . PHE B 1 159 ? 9.896   -7.722  49.726  1.00 14.42 ? 158  PHE B N   1 
ATOM   4958 C  CA  . PHE B 1 159 ? 10.900  -8.274  48.823  1.00 13.55 ? 158  PHE B CA  1 
ATOM   4959 C  C   . PHE B 1 159 ? 10.808  -7.721  47.408  1.00 14.27 ? 158  PHE B C   1 
ATOM   4960 O  O   . PHE B 1 159 ? 11.566  -8.164  46.530  1.00 15.60 ? 158  PHE B O   1 
ATOM   4961 C  CB  . PHE B 1 159 ? 10.791  -9.805  48.820  1.00 14.31 ? 158  PHE B CB  1 
ATOM   4962 C  CG  . PHE B 1 159 ? 10.887  -10.405 50.199  1.00 15.35 ? 158  PHE B CG  1 
ATOM   4963 C  CD1 . PHE B 1 159 ? 12.122  -10.655 50.770  1.00 16.59 ? 158  PHE B CD1 1 
ATOM   4964 C  CD2 . PHE B 1 159 ? 9.742   -10.672 50.938  1.00 15.71 ? 158  PHE B CD2 1 
ATOM   4965 C  CE1 . PHE B 1 159 ? 12.222  -11.177 52.056  1.00 17.33 ? 158  PHE B CE1 1 
ATOM   4966 C  CE2 . PHE B 1 159 ? 9.829   -11.202 52.224  1.00 17.91 ? 158  PHE B CE2 1 
ATOM   4967 C  CZ  . PHE B 1 159 ? 11.076  -11.450 52.786  1.00 16.79 ? 158  PHE B CZ  1 
ATOM   4968 N  N   . ASN B 1 160 ? 9.931   -6.749  47.167  1.00 14.02 ? 159  ASN B N   1 
ATOM   4969 C  CA  . ASN B 1 160 ? 9.713   -6.209  45.824  1.00 15.57 ? 159  ASN B CA  1 
ATOM   4970 C  C   . ASN B 1 160 ? 9.515   -7.332  44.804  1.00 16.41 ? 159  ASN B C   1 
ATOM   4971 O  O   . ASN B 1 160 ? 10.006  -7.272  43.669  1.00 17.66 ? 159  ASN B O   1 
ATOM   4972 C  CB  . ASN B 1 160 ? 10.861  -5.281  45.410  1.00 18.30 ? 159  ASN B CB  1 
ATOM   4973 C  CG  . ASN B 1 160 ? 10.443  -4.276  44.356  1.00 23.91 ? 159  ASN B CG  1 
ATOM   4974 O  OD1 . ASN B 1 160 ? 9.252   -4.022  44.166  1.00 24.15 ? 159  ASN B OD1 1 
ATOM   4975 N  ND2 . ASN B 1 160 ? 11.421  -3.698  43.660  1.00 27.10 ? 159  ASN B ND2 1 
ATOM   4976 N  N   . TYR B 1 161 ? 8.770   -8.361  45.206  1.00 15.26 ? 160  TYR B N   1 
ATOM   4977 C  CA  . TYR B 1 161 ? 8.469   -9.504  44.350  1.00 13.70 ? 160  TYR B CA  1 
ATOM   4978 C  C   . TYR B 1 161 ? 6.957   -9.667  44.243  1.00 13.96 ? 160  TYR B C   1 
ATOM   4979 O  O   . TYR B 1 161 ? 6.260   -9.650  45.262  1.00 15.82 ? 160  TYR B O   1 
ATOM   4980 C  CB  . TYR B 1 161 ? 9.100   -10.783 44.913  1.00 19.29 ? 160  TYR B CB  1 
ATOM   4981 C  CG  . TYR B 1 161 ? 8.998   -11.981 43.994  1.00 23.80 ? 160  TYR B CG  1 
ATOM   4982 C  CD1 . TYR B 1 161 ? 9.938   -12.192 42.994  1.00 25.38 ? 160  TYR B CD1 1 
ATOM   4983 C  CD2 . TYR B 1 161 ? 7.969   -12.908 44.134  1.00 25.07 ? 160  TYR B CD2 1 
ATOM   4984 C  CE1 . TYR B 1 161 ? 9.855   -13.284 42.156  1.00 26.95 ? 160  TYR B CE1 1 
ATOM   4985 C  CE2 . TYR B 1 161 ? 7.875   -14.001 43.296  1.00 28.77 ? 160  TYR B CE2 1 
ATOM   4986 C  CZ  . TYR B 1 161 ? 8.822   -14.188 42.308  1.00 30.04 ? 160  TYR B CZ  1 
ATOM   4987 O  OH  . TYR B 1 161 ? 8.739   -15.284 41.469  1.00 34.58 ? 160  TYR B OH  1 
ATOM   4988 N  N   . ARG B 1 162 ? 6.443   -9.837  43.020  1.00 13.81 ? 161  ARG B N   1 
ATOM   4989 C  CA  . ARG B 1 162 ? 4.999   -9.956  42.807  1.00 13.60 ? 161  ARG B CA  1 
ATOM   4990 C  C   . ARG B 1 162 ? 4.607   -11.428 42.633  1.00 12.95 ? 161  ARG B C   1 
ATOM   4991 O  O   . ARG B 1 162 ? 4.927   -12.055 41.615  1.00 14.15 ? 161  ARG B O   1 
ATOM   4992 C  CB  . ARG B 1 162 ? 4.550   -9.106  41.615  1.00 15.12 ? 161  ARG B CB  1 
ATOM   4993 C  CG  . ARG B 1 162 ? 4.529   -7.617  41.953  1.00 17.45 ? 161  ARG B CG  1 
ATOM   4994 C  CD  . ARG B 1 162 ? 3.984   -6.742  40.850  1.00 18.85 ? 161  ARG B CD  1 
ATOM   4995 N  NE  . ARG B 1 162 ? 4.096   -5.330  41.196  1.00 16.55 ? 161  ARG B NE  1 
ATOM   4996 C  CZ  . ARG B 1 162 ? 3.120   -4.604  41.725  1.00 15.36 ? 161  ARG B CZ  1 
ATOM   4997 N  NH1 . ARG B 1 162 ? 1.925   -5.120  41.966  1.00 14.03 ? 161  ARG B NH1 1 
ATOM   4998 N  NH2 . ARG B 1 162 ? 3.352   -3.328  42.024  1.00 15.75 ? 161  ARG B NH2 1 
ATOM   4999 N  N   . PHE B 1 163 ? 3.908   -11.979 43.634  1.00 13.73 ? 162  PHE B N   1 
ATOM   5000 C  CA  . PHE B 1 163 ? 3.355   -13.326 43.492  1.00 15.24 ? 162  PHE B CA  1 
ATOM   5001 C  C   . PHE B 1 163 ? 2.175   -13.363 42.527  1.00 13.62 ? 162  PHE B C   1 
ATOM   5002 O  O   . PHE B 1 163 ? 1.838   -14.440 42.015  1.00 14.36 ? 162  PHE B O   1 
ATOM   5003 C  CB  . PHE B 1 163 ? 2.915   -13.871 44.855  1.00 16.47 ? 162  PHE B CB  1 
ATOM   5004 C  CG  . PHE B 1 163 ? 4.050   -14.179 45.788  1.00 18.20 ? 162  PHE B CG  1 
ATOM   5005 C  CD1 . PHE B 1 163 ? 4.821   -15.313 45.611  1.00 25.14 ? 162  PHE B CD1 1 
ATOM   5006 C  CD2 . PHE B 1 163 ? 4.320   -13.353 46.870  1.00 17.16 ? 162  PHE B CD2 1 
ATOM   5007 C  CE1 . PHE B 1 163 ? 5.861   -15.610 46.483  1.00 26.24 ? 162  PHE B CE1 1 
ATOM   5008 C  CE2 . PHE B 1 163 ? 5.359   -13.639 47.741  1.00 20.78 ? 162  PHE B CE2 1 
ATOM   5009 C  CZ  . PHE B 1 163 ? 6.131   -14.770 47.550  1.00 23.29 ? 162  PHE B CZ  1 
ATOM   5010 N  N   . ASN B 1 164 ? 1.541   -12.216 42.280  1.00 12.33 ? 163  ASN B N   1 
ATOM   5011 C  CA  . ASN B 1 164 ? 0.421   -12.105 41.344  1.00 12.26 ? 163  ASN B CA  1 
ATOM   5012 C  C   . ASN B 1 164 ? -0.664  -13.142 41.643  1.00 13.33 ? 163  ASN B C   1 
ATOM   5013 O  O   . ASN B 1 164 ? -1.200  -13.813 40.757  1.00 13.48 ? 163  ASN B O   1 
ATOM   5014 C  CB  . ASN B 1 164 ? 0.930   -12.190 39.905  1.00 13.27 ? 163  ASN B CB  1 
ATOM   5015 C  CG  . ASN B 1 164 ? 1.669   -10.930 39.498  1.00 17.59 ? 163  ASN B CG  1 
ATOM   5016 O  OD1 . ASN B 1 164 ? 1.180   -9.817  39.732  1.00 18.84 ? 163  ASN B OD1 1 
ATOM   5017 N  ND2 . ASN B 1 164 ? 2.856   -11.087 38.907  1.00 15.99 ? 163  ASN B ND2 1 
ATOM   5018 N  N   . SER B 1 165 ? -1.034  -13.220 42.925  1.00 12.85 ? 164  SER B N   1 
ATOM   5019 C  CA  . SER B 1 165 ? -2.015  -14.208 43.358  1.00 12.57 ? 164  SER B CA  1 
ATOM   5020 C  C   . SER B 1 165 ? -3.396  -13.951 42.771  1.00 12.91 ? 164  SER B C   1 
ATOM   5021 O  O   . SER B 1 165 ? -4.193  -14.888 42.644  1.00 13.71 ? 164  SER B O   1 
ATOM   5022 C  CB  . SER B 1 165 ? -2.101  -14.223 44.880  1.00 13.65 ? 164  SER B CB  1 
ATOM   5023 O  OG  . SER B 1 165 ? -0.904  -14.736 45.438  1.00 14.27 ? 164  SER B OG  1 
ATOM   5024 N  N   . PHE B 1 166 ? -3.717  -12.700 42.451  1.00 13.76 ? 165  PHE B N   1 
ATOM   5025 C  CA  . PHE B 1 166 ? -5.030  -12.405 41.903  1.00 14.52 ? 165  PHE B CA  1 
ATOM   5026 C  C   . PHE B 1 166 ? -5.109  -12.717 40.419  1.00 16.65 ? 165  PHE B C   1 
ATOM   5027 O  O   . PHE B 1 166 ? -6.191  -12.596 39.834  1.00 18.33 ? 165  PHE B O   1 
ATOM   5028 C  CB  . PHE B 1 166 ? -5.410  -10.945 42.181  1.00 13.71 ? 165  PHE B CB  1 
ATOM   5029 C  CG  . PHE B 1 166 ? -5.749  -10.683 43.631  1.00 13.79 ? 165  PHE B CG  1 
ATOM   5030 C  CD1 . PHE B 1 166 ? -6.910  -11.203 44.190  1.00 14.93 ? 165  PHE B CD1 1 
ATOM   5031 C  CD2 . PHE B 1 166 ? -4.892  -9.951  44.447  1.00 14.16 ? 165  PHE B CD2 1 
ATOM   5032 C  CE1 . PHE B 1 166 ? -7.221  -10.985 45.528  1.00 15.76 ? 165  PHE B CE1 1 
ATOM   5033 C  CE2 . PHE B 1 166 ? -5.206  -9.714  45.790  1.00 14.66 ? 165  PHE B CE2 1 
ATOM   5034 C  CZ  . PHE B 1 166 ? -6.364  -10.239 46.328  1.00 14.19 ? 165  PHE B CZ  1 
ATOM   5035 N  N   . TYR B 1 167 ? -4.001  -13.141 39.810  1.00 13.97 ? 166  TYR B N   1 
ATOM   5036 C  CA  . TYR B 1 167 ? -4.019  -13.639 38.439  1.00 14.98 ? 166  TYR B CA  1 
ATOM   5037 C  C   . TYR B 1 167 ? -4.183  -15.154 38.373  1.00 18.16 ? 166  TYR B C   1 
ATOM   5038 O  O   . TYR B 1 167 ? -4.100  -15.727 37.281  1.00 19.98 ? 166  TYR B O   1 
ATOM   5039 C  CB  . TYR B 1 167 ? -2.750  -13.182 37.699  1.00 13.09 ? 166  TYR B CB  1 
ATOM   5040 C  CG  . TYR B 1 167 ? -2.754  -11.685 37.517  1.00 13.56 ? 166  TYR B CG  1 
ATOM   5041 C  CD1 . TYR B 1 167 ? -2.302  -10.833 38.535  1.00 13.14 ? 166  TYR B CD1 1 
ATOM   5042 C  CD2 . TYR B 1 167 ? -3.257  -11.108 36.349  1.00 14.97 ? 166  TYR B CD2 1 
ATOM   5043 C  CE1 . TYR B 1 167 ? -2.339  -9.450  38.381  1.00 13.74 ? 166  TYR B CE1 1 
ATOM   5044 C  CE2 . TYR B 1 167 ? -3.294  -9.735  36.188  1.00 12.83 ? 166  TYR B CE2 1 
ATOM   5045 C  CZ  . TYR B 1 167 ? -2.844  -8.911  37.204  1.00 13.73 ? 166  TYR B CZ  1 
ATOM   5046 O  OH  . TYR B 1 167 ? -2.891  -7.541  37.035  1.00 14.43 ? 166  TYR B OH  1 
ATOM   5047 N  N   . ARG B 1 168 ? -4.458  -15.804 39.506  1.00 18.17 ? 167  ARG B N   1 
ATOM   5048 C  CA  . ARG B 1 168 ? -4.594  -17.253 39.584  1.00 20.86 ? 167  ARG B CA  1 
ATOM   5049 C  C   . ARG B 1 168 ? -5.945  -17.619 40.183  1.00 23.43 ? 167  ARG B C   1 
ATOM   5050 O  O   . ARG B 1 168 ? -6.358  -17.040 41.193  1.00 22.22 ? 167  ARG B O   1 
ATOM   5051 C  CB  . ARG B 1 168 ? -3.468  -17.860 40.429  1.00 22.97 ? 167  ARG B CB  1 
ATOM   5052 C  CG  . ARG B 1 168 ? -2.075  -17.421 40.010  1.00 20.69 ? 167  ARG B CG  1 
ATOM   5053 C  CD  . ARG B 1 168 ? -1.048  -17.678 41.104  1.00 21.16 ? 167  ARG B CD  1 
ATOM   5054 N  NE  . ARG B 1 168 ? 0.193   -16.957 40.843  1.00 27.07 ? 167  ARG B NE  1 
ATOM   5055 C  CZ  . ARG B 1 168 ? 1.273   -17.492 40.287  1.00 30.61 ? 167  ARG B CZ  1 
ATOM   5056 N  NH1 . ARG B 1 168 ? 1.309   -18.768 39.935  1.00 32.95 ? 167  ARG B NH1 1 
ATOM   5057 N  NH2 . ARG B 1 168 ? 2.343   -16.727 40.082  1.00 30.04 ? 167  ARG B NH2 1 
ATOM   5058 N  N   . ASP B 1 169 ? -6.632  -18.582 39.565  1.00 27.84 ? 168  ASP B N   1 
ATOM   5059 C  CA  . ASP B 1 169 ? -7.866  -19.104 40.138  1.00 31.90 ? 168  ASP B CA  1 
ATOM   5060 C  C   . ASP B 1 169 ? -7.617  -20.216 41.145  1.00 32.97 ? 168  ASP B C   1 
ATOM   5061 O  O   . ASP B 1 169 ? -8.519  -20.535 41.928  1.00 30.84 ? 168  ASP B O   1 
ATOM   5062 C  CB  . ASP B 1 169 ? -8.817  -19.612 39.039  1.00 34.29 ? 168  ASP B CB  1 
ATOM   5063 C  CG  . ASP B 1 169 ? -8.186  -20.677 38.155  1.00 40.06 ? 168  ASP B CG  1 
ATOM   5064 O  OD1 . ASP B 1 169 ? -7.276  -20.345 37.367  1.00 43.76 ? 168  ASP B OD1 1 
ATOM   5065 O  OD2 . ASP B 1 169 ? -8.599  -21.852 38.242  1.00 44.00 ? 168  ASP B OD2 1 
ATOM   5066 N  N   . GLN B 1 170 ? -6.431  -20.803 41.139  1.00 33.82 ? 169  GLN B N   1 
ATOM   5067 C  CA  . GLN B 1 170 ? -5.980  -21.762 42.132  1.00 35.64 ? 169  GLN B CA  1 
ATOM   5068 C  C   . GLN B 1 170 ? -5.052  -21.079 43.118  1.00 31.59 ? 169  GLN B C   1 
ATOM   5069 O  O   . GLN B 1 170 ? -4.553  -19.977 42.867  1.00 31.91 ? 169  GLN B O   1 
ATOM   5070 C  CB  . GLN B 1 170 ? -5.256  -22.926 41.454  1.00 42.45 ? 169  GLN B CB  1 
ATOM   5071 C  CG  . GLN B 1 170 ? -6.168  -23.838 40.648  1.00 51.42 ? 169  GLN B CG  1 
ATOM   5072 C  CD  . GLN B 1 170 ? -7.185  -24.555 41.518  1.00 58.79 ? 169  GLN B CD  1 
ATOM   5073 O  OE1 . GLN B 1 170 ? -6.900  -24.917 42.662  1.00 61.20 ? 169  GLN B OE1 1 
ATOM   5074 N  NE2 . GLN B 1 170 ? -8.383  -24.759 40.981  1.00 60.55 ? 169  GLN B NE2 1 
ATOM   5075 N  N   . PRO B 1 171 ? -4.794  -21.703 44.267  1.00 29.82 ? 170  PRO B N   1 
ATOM   5076 C  CA  . PRO B 1 171 ? -3.782  -21.155 45.178  1.00 30.01 ? 170  PRO B CA  1 
ATOM   5077 C  C   . PRO B 1 171 ? -2.419  -21.097 44.504  1.00 29.21 ? 170  PRO B C   1 
ATOM   5078 O  O   . PRO B 1 171 ? -2.078  -21.929 43.656  1.00 27.88 ? 170  PRO B O   1 
ATOM   5079 C  CB  . PRO B 1 171 ? -3.784  -22.139 46.356  1.00 29.25 ? 170  PRO B CB  1 
ATOM   5080 C  CG  . PRO B 1 171 ? -5.072  -22.879 46.258  1.00 31.47 ? 170  PRO B CG  1 
ATOM   5081 C  CD  . PRO B 1 171 ? -5.429  -22.920 44.799  1.00 29.70 ? 170  PRO B CD  1 
ATOM   5082 N  N   . HIS B 1 172 ? -1.647  -20.083 44.878  1.00 28.26 ? 171  HIS B N   1 
ATOM   5083 C  CA  . HIS B 1 172 ? -0.269  -19.993 44.423  1.00 28.74 ? 171  HIS B CA  1 
ATOM   5084 C  C   . HIS B 1 172 ? 0.487   -21.251 44.849  1.00 26.87 ? 171  HIS B C   1 
ATOM   5085 O  O   . HIS B 1 172 ? 0.237   -21.780 45.939  1.00 23.58 ? 171  HIS B O   1 
ATOM   5086 C  CB  . HIS B 1 172 ? 0.405   -18.750 45.012  1.00 29.75 ? 171  HIS B CB  1 
ATOM   5087 C  CG  . HIS B 1 172 ? 1.762   -18.466 44.444  1.00 31.53 ? 171  HIS B CG  1 
ATOM   5088 N  ND1 . HIS B 1 172 ? 2.859   -19.264 44.693  1.00 33.22 ? 171  HIS B ND1 1 
ATOM   5089 C  CD2 . HIS B 1 172 ? 2.201   -17.462 43.647  1.00 32.53 ? 171  HIS B CD2 1 
ATOM   5090 C  CE1 . HIS B 1 172 ? 3.912   -18.770 44.065  1.00 31.59 ? 171  HIS B CE1 1 
ATOM   5091 N  NE2 . HIS B 1 172 ? 3.540   -17.676 43.424  1.00 32.39 ? 171  HIS B NE2 1 
ATOM   5092 N  N   . PRO B 1 173 ? 1.412   -21.756 44.023  1.00 26.98 ? 172  PRO B N   1 
ATOM   5093 C  CA  . PRO B 1 173 ? 2.115   -23.000 44.388  1.00 25.90 ? 172  PRO B CA  1 
ATOM   5094 C  C   . PRO B 1 173 ? 2.840   -22.928 45.725  1.00 24.83 ? 172  PRO B C   1 
ATOM   5095 O  O   . PRO B 1 173 ? 2.919   -23.942 46.439  1.00 22.36 ? 172  PRO B O   1 
ATOM   5096 C  CB  . PRO B 1 173 ? 3.095   -23.201 43.221  1.00 28.24 ? 172  PRO B CB  1 
ATOM   5097 C  CG  . PRO B 1 173 ? 2.479   -22.465 42.078  1.00 29.81 ? 172  PRO B CG  1 
ATOM   5098 C  CD  . PRO B 1 173 ? 1.754   -21.293 42.664  1.00 29.50 ? 172  PRO B CD  1 
ATOM   5099 N  N   . PHE B 1 174 ? 3.390   -21.766 46.088  1.00 21.26 ? 173  PHE B N   1 
ATOM   5100 C  CA  . PHE B 1 174 ? 3.978   -21.634 47.415  1.00 20.89 ? 173  PHE B CA  1 
ATOM   5101 C  C   . PHE B 1 174 ? 2.943   -21.938 48.486  1.00 19.35 ? 173  PHE B C   1 
ATOM   5102 O  O   . PHE B 1 174 ? 3.245   -22.616 49.476  1.00 21.71 ? 173  PHE B O   1 
ATOM   5103 C  CB  . PHE B 1 174 ? 4.557   -20.230 47.599  1.00 21.90 ? 173  PHE B CB  1 
ATOM   5104 C  CG  . PHE B 1 174 ? 5.266   -20.026 48.914  1.00 22.83 ? 173  PHE B CG  1 
ATOM   5105 C  CD1 . PHE B 1 174 ? 6.617   -20.322 49.043  1.00 21.99 ? 173  PHE B CD1 1 
ATOM   5106 C  CD2 . PHE B 1 174 ? 4.585   -19.532 50.018  1.00 22.10 ? 173  PHE B CD2 1 
ATOM   5107 C  CE1 . PHE B 1 174 ? 7.274   -20.129 50.241  1.00 23.53 ? 173  PHE B CE1 1 
ATOM   5108 C  CE2 . PHE B 1 174 ? 5.237   -19.344 51.231  1.00 21.82 ? 173  PHE B CE2 1 
ATOM   5109 C  CZ  . PHE B 1 174 ? 6.582   -19.642 51.343  1.00 23.52 ? 173  PHE B CZ  1 
ATOM   5110 N  N   . ILE B 1 175 ? 1.705   -21.475 48.286  1.00 19.67 ? 174  ILE B N   1 
ATOM   5111 C  CA  . ILE B 1 175 ? 0.659   -21.666 49.292  1.00 20.15 ? 174  ILE B CA  1 
ATOM   5112 C  C   . ILE B 1 175 ? 0.310   -23.144 49.432  1.00 19.65 ? 174  ILE B C   1 
ATOM   5113 O  O   . ILE B 1 175 ? 0.190   -23.669 50.547  1.00 18.67 ? 174  ILE B O   1 
ATOM   5114 C  CB  . ILE B 1 175 ? -0.578  -20.813 48.947  1.00 20.61 ? 174  ILE B CB  1 
ATOM   5115 C  CG1 . ILE B 1 175 ? -0.237  -19.319 49.028  1.00 21.38 ? 174  ILE B CG1 1 
ATOM   5116 C  CG2 . ILE B 1 175 ? -1.757  -21.160 49.850  1.00 18.63 ? 174  ILE B CG2 1 
ATOM   5117 C  CD1 . ILE B 1 175 ? 0.229   -18.842 50.413  1.00 20.24 ? 174  ILE B CD1 1 
ATOM   5118 N  N   . THR B 1 176 ? 0.146   -23.839 48.305  1.00 20.45 ? 175  THR B N   1 
ATOM   5119 C  CA  . THR B 1 176 ? -0.150  -25.269 48.348  1.00 22.76 ? 175  THR B CA  1 
ATOM   5120 C  C   . THR B 1 176 ? 0.903   -26.030 49.150  1.00 23.21 ? 175  THR B C   1 
ATOM   5121 O  O   . THR B 1 176 ? 0.571   -26.864 50.002  1.00 20.09 ? 175  THR B O   1 
ATOM   5122 C  CB  . THR B 1 176 ? -0.248  -25.817 46.924  1.00 24.31 ? 175  THR B CB  1 
ATOM   5123 O  OG1 . THR B 1 176 ? -1.342  -25.181 46.255  1.00 27.65 ? 175  THR B OG1 1 
ATOM   5124 C  CG2 . THR B 1 176 ? -0.457  -27.325 46.941  1.00 25.48 ? 175  THR B CG2 1 
ATOM   5125 N  N   . SER B 1 177 ? 2.183   -25.753 48.892  1.00 23.07 ? 176  SER B N   1 
ATOM   5126 C  CA  . SER B 1 177 ? 3.243   -26.469 49.594  1.00 21.20 ? 176  SER B CA  1 
ATOM   5127 C  C   . SER B 1 177 ? 3.329   -26.048 51.059  1.00 18.99 ? 176  SER B C   1 
ATOM   5128 O  O   . SER B 1 177 ? 3.527   -26.896 51.936  1.00 19.68 ? 176  SER B O   1 
ATOM   5129 C  CB  . SER B 1 177 ? 4.580   -26.253 48.881  1.00 23.77 ? 176  SER B CB  1 
ATOM   5130 O  OG  . SER B 1 177 ? 4.709   -27.134 47.781  1.00 25.04 ? 176  SER B OG  1 
ATOM   5131 N  N   . MET B 1 178 ? 3.177   -24.751 51.350  1.00 15.97 ? 177  MET B N   1 
ATOM   5132 C  CA  . MET B 1 178 ? 3.242   -24.299 52.739  1.00 18.20 ? 177  MET B CA  1 
ATOM   5133 C  C   . MET B 1 178 ? 2.122   -24.914 53.565  1.00 17.35 ? 177  MET B C   1 
ATOM   5134 O  O   . MET B 1 178 ? 2.345   -25.382 54.690  1.00 18.68 ? 177  MET B O   1 
ATOM   5135 C  CB  . MET B 1 178 ? 3.169   -22.770 52.815  1.00 17.72 ? 177  MET B CB  1 
ATOM   5136 C  CG  . MET B 1 178 ? 3.117   -22.236 54.263  1.00 19.15 ? 177  MET B CG  1 
ATOM   5137 S  SD  . MET B 1 178 ? 2.350   -20.608 54.458  1.00 20.22 ? 177  MET B SD  1 
ATOM   5138 C  CE  . MET B 1 178 ? 0.612   -21.030 54.220  1.00 18.63 ? 177  MET B CE  1 
ATOM   5139 N  N   . VAL B 1 179 ? 0.897   -24.903 53.036  1.00 18.75 ? 178  VAL B N   1 
ATOM   5140 C  CA  . VAL B 1 179 ? -0.222  -25.461 53.792  1.00 18.75 ? 178  VAL B CA  1 
ATOM   5141 C  C   . VAL B 1 179 ? 0.002   -26.946 54.059  1.00 21.60 ? 178  VAL B C   1 
ATOM   5142 O  O   . VAL B 1 179 ? -0.254  -27.444 55.167  1.00 18.19 ? 178  VAL B O   1 
ATOM   5143 C  CB  . VAL B 1 179 ? -1.546  -25.209 53.046  1.00 16.92 ? 178  VAL B CB  1 
ATOM   5144 C  CG1 . VAL B 1 179 ? -2.695  -25.950 53.737  1.00 19.22 ? 178  VAL B CG1 1 
ATOM   5145 C  CG2 . VAL B 1 179 ? -1.820  -23.697 52.955  1.00 19.76 ? 178  VAL B CG2 1 
ATOM   5146 N  N   . ARG B 1 180 ? 0.487   -27.675 53.053  1.00 20.58 ? 179  ARG B N   1 
ATOM   5147 C  CA  . ARG B 1 180 ? 0.735   -29.099 53.230  1.00 20.80 ? 179  ARG B CA  1 
ATOM   5148 C  C   . ARG B 1 180 ? 1.858   -29.341 54.230  1.00 21.47 ? 179  ARG B C   1 
ATOM   5149 O  O   . ARG B 1 180 ? 1.826   -30.335 54.963  1.00 23.88 ? 179  ARG B O   1 
ATOM   5150 C  CB  . ARG B 1 180 ? 1.054   -29.743 51.875  1.00 22.87 ? 179  ARG B CB  1 
ATOM   5151 C  CG  . ARG B 1 180 ? 0.823   -31.246 51.804  1.00 25.39 ? 179  ARG B CG  1 
ATOM   5152 C  CD  . ARG B 1 180 ? 0.569   -31.691 50.346  1.00 27.92 ? 179  ARG B CD  1 
ATOM   5153 N  NE  . ARG B 1 180 ? 1.549   -31.121 49.425  1.00 28.42 ? 179  ARG B NE  1 
ATOM   5154 C  CZ  . ARG B 1 180 ? 1.334   -30.887 48.136  1.00 28.75 ? 179  ARG B CZ  1 
ATOM   5155 N  NH1 . ARG B 1 180 ? 0.178   -31.184 47.558  1.00 30.22 ? 179  ARG B NH1 1 
ATOM   5156 N  NH2 . ARG B 1 180 ? 2.300   -30.331 47.409  1.00 27.51 ? 179  ARG B NH2 1 
ATOM   5157 N  N   . ALA B 1 181 ? 2.842   -28.439 54.291  1.00 20.01 ? 180  ALA B N   1 
ATOM   5158 C  CA  . ALA B 1 181 ? 3.920   -28.591 55.264  1.00 18.22 ? 180  ALA B CA  1 
ATOM   5159 C  C   . ALA B 1 181 ? 3.423   -28.313 56.678  1.00 19.04 ? 180  ALA B C   1 
ATOM   5160 O  O   . ALA B 1 181 ? 3.772   -29.039 57.619  1.00 20.02 ? 180  ALA B O   1 
ATOM   5161 C  CB  . ALA B 1 181 ? 5.089   -27.668 54.913  1.00 17.44 ? 180  ALA B CB  1 
ATOM   5162 N  N   . LEU B 1 182 ? 2.616   -27.264 56.849  1.00 17.93 ? 181  LEU B N   1 
ATOM   5163 C  CA  . LEU B 1 182 ? 2.026   -27.005 58.160  1.00 18.90 ? 181  LEU B CA  1 
ATOM   5164 C  C   . LEU B 1 182 ? 1.093   -28.135 58.573  1.00 20.37 ? 181  LEU B C   1 
ATOM   5165 O  O   . LEU B 1 182 ? 1.074   -28.533 59.745  1.00 20.67 ? 181  LEU B O   1 
ATOM   5166 C  CB  . LEU B 1 182 ? 1.279   -25.666 58.155  1.00 18.26 ? 181  LEU B CB  1 
ATOM   5167 C  CG  . LEU B 1 182 ? 2.144   -24.418 57.952  1.00 16.42 ? 181  LEU B CG  1 
ATOM   5168 C  CD1 . LEU B 1 182 ? 1.268   -23.185 57.754  1.00 20.04 ? 181  LEU B CD1 1 
ATOM   5169 C  CD2 . LEU B 1 182 ? 3.098   -24.220 59.140  1.00 16.94 ? 181  LEU B CD2 1 
ATOM   5170 N  N   . ASP B 1 183 ? 0.298   -28.651 57.625  1.00 21.60 ? 182  ASP B N   1 
ATOM   5171 C  CA  . ASP B 1 183 ? -0.526  -29.829 57.883  1.00 24.86 ? 182  ASP B CA  1 
ATOM   5172 C  C   . ASP B 1 183 ? 0.324   -30.971 58.409  1.00 22.99 ? 182  ASP B C   1 
ATOM   5173 O  O   . ASP B 1 183 ? -0.020  -31.623 59.402  1.00 23.55 ? 182  ASP B O   1 
ATOM   5174 C  CB  . ASP B 1 183 ? -1.238  -30.283 56.601  1.00 28.73 ? 182  ASP B CB  1 
ATOM   5175 C  CG  . ASP B 1 183 ? -2.471  -29.473 56.286  1.00 38.55 ? 182  ASP B CG  1 
ATOM   5176 O  OD1 . ASP B 1 183 ? -3.039  -28.857 57.209  1.00 42.92 ? 182  ASP B OD1 1 
ATOM   5177 O  OD2 . ASP B 1 183 ? -2.882  -29.471 55.103  1.00 43.56 ? 182  ASP B OD2 1 
ATOM   5178 N  N   . GLU B 1 184 ? 1.429   -31.249 57.721  1.00 19.28 ? 183  GLU B N   1 
ATOM   5179 C  CA  . GLU B 1 184 ? 2.278   -32.362 58.114  1.00 17.27 ? 183  GLU B CA  1 
ATOM   5180 C  C   . GLU B 1 184 ? 2.837   -32.144 59.514  1.00 18.78 ? 183  GLU B C   1 
ATOM   5181 O  O   . GLU B 1 184 ? 2.848   -33.069 60.338  1.00 21.77 ? 183  GLU B O   1 
ATOM   5182 C  CB  . GLU B 1 184 ? 3.398   -32.537 57.087  1.00 20.22 ? 183  GLU B CB  1 
ATOM   5183 C  CG  . GLU B 1 184 ? 4.482   -33.529 57.478  1.00 21.78 ? 183  GLU B CG  1 
ATOM   5184 C  CD  . GLU B 1 184 ? 4.023   -34.989 57.487  1.00 24.35 ? 183  GLU B CD  1 
ATOM   5185 O  OE1 . GLU B 1 184 ? 2.857   -35.278 57.142  1.00 24.51 ? 183  GLU B OE1 1 
ATOM   5186 O  OE2 . GLU B 1 184 ? 4.854   -35.853 57.841  1.00 25.76 ? 183  GLU B OE2 1 
ATOM   5187 N  N   . ALA B 1 185 ? 3.280   -30.917 59.813  1.00 19.35 ? 184  ALA B N   1 
ATOM   5188 C  CA  . ALA B 1 185 ? 3.824   -30.641 61.139  1.00 18.54 ? 184  ALA B CA  1 
ATOM   5189 C  C   . ALA B 1 185 ? 2.774   -30.869 62.219  1.00 19.59 ? 184  ALA B C   1 
ATOM   5190 O  O   . ALA B 1 185 ? 3.080   -31.427 63.281  1.00 21.44 ? 184  ALA B O   1 
ATOM   5191 C  CB  . ALA B 1 185 ? 4.366   -29.213 61.205  1.00 19.89 ? 184  ALA B CB  1 
ATOM   5192 N  N   . MET B 1 186 ? 1.525   -30.462 61.966  1.00 15.80 ? 185  MET B N   1 
ATOM   5193 C  CA  . MET B 1 186 ? 0.482   -30.672 62.967  1.00 16.58 ? 185  MET B CA  1 
ATOM   5194 C  C   . MET B 1 186 ? 0.146   -32.151 63.116  1.00 19.16 ? 185  MET B C   1 
ATOM   5195 O  O   . MET B 1 186 ? -0.041  -32.640 64.241  1.00 18.82 ? 185  MET B O   1 
ATOM   5196 C  CB  . MET B 1 186 ? -0.771  -29.872 62.606  1.00 18.41 ? 185  MET B CB  1 
ATOM   5197 C  CG  . MET B 1 186 ? -1.787  -29.741 63.740  1.00 17.37 ? 185  MET B CG  1 
ATOM   5198 S  SD  . MET B 1 186 ? -3.345  -29.008 63.189  1.00 18.84 ? 185  MET B SD  1 
ATOM   5199 C  CE  . MET B 1 186 ? -4.027  -30.331 62.174  1.00 19.82 ? 185  MET B CE  1 
ATOM   5200 N  N   . ASN B 1 187 ? 0.053   -32.881 61.994  1.00 19.84 ? 186  ASN B N   1 
ATOM   5201 C  CA  . ASN B 1 187 ? -0.257  -34.310 62.069  1.00 23.55 ? 186  ASN B CA  1 
ATOM   5202 C  C   . ASN B 1 187 ? 0.876   -35.101 62.719  1.00 22.88 ? 186  ASN B C   1 
ATOM   5203 O  O   . ASN B 1 187 ? 0.619   -36.091 63.415  1.00 22.95 ? 186  ASN B O   1 
ATOM   5204 C  CB  . ASN B 1 187 ? -0.558  -34.865 60.671  1.00 26.69 ? 186  ASN B CB  1 
ATOM   5205 C  CG  . ASN B 1 187 ? -1.112  -36.288 60.710  1.00 32.46 ? 186  ASN B CG  1 
ATOM   5206 O  OD1 . ASN B 1 187 ? -0.361  -37.272 60.639  1.00 33.34 ? 186  ASN B OD1 1 
ATOM   5207 N  ND2 . ASN B 1 187 ? -2.433  -36.403 60.828  1.00 34.53 ? 186  ASN B ND2 1 
ATOM   5208 N  N   . LYS B 1 188 ? 2.126   -34.677 62.515  1.00 22.02 ? 187  LYS B N   1 
ATOM   5209 C  CA  . LYS B 1 188 ? 3.255   -35.353 63.149  1.00 24.91 ? 187  LYS B CA  1 
ATOM   5210 C  C   . LYS B 1 188 ? 3.183   -35.292 64.671  1.00 24.40 ? 187  LYS B C   1 
ATOM   5211 O  O   . LYS B 1 188 ? 3.696   -36.190 65.349  1.00 24.75 ? 187  LYS B O   1 
ATOM   5212 C  CB  . LYS B 1 188 ? 4.570   -34.746 62.669  1.00 27.75 ? 187  LYS B CB  1 
ATOM   5213 C  CG  . LYS B 1 188 ? 5.116   -35.378 61.427  1.00 33.48 ? 187  LYS B CG  1 
ATOM   5214 C  CD  . LYS B 1 188 ? 6.631   -35.261 61.370  1.00 35.56 ? 187  LYS B CD  1 
ATOM   5215 C  CE  . LYS B 1 188 ? 7.074   -33.930 60.813  1.00 35.17 ? 187  LYS B CE  1 
ATOM   5216 N  NZ  . LYS B 1 188 ? 8.456   -34.040 60.262  1.00 34.41 ? 187  LYS B NZ  1 
ATOM   5217 N  N   . LEU B 1 189 ? 2.550   -34.250 65.223  1.00 24.14 ? 188  LEU B N   1 
ATOM   5218 C  CA  . LEU B 1 189 ? 2.526   -34.067 66.674  1.00 23.38 ? 188  LEU B CA  1 
ATOM   5219 C  C   . LEU B 1 189 ? 1.954   -35.278 67.391  1.00 21.51 ? 188  LEU B C   1 
ATOM   5220 O  O   . LEU B 1 189 ? 2.349   -35.571 68.525  1.00 24.92 ? 188  LEU B O   1 
ATOM   5221 C  CB  . LEU B 1 189 ? 1.707   -32.824 67.045  1.00 23.35 ? 188  LEU B CB  1 
ATOM   5222 C  CG  . LEU B 1 189 ? 2.266   -31.482 66.586  1.00 22.96 ? 188  LEU B CG  1 
ATOM   5223 C  CD1 . LEU B 1 189 ? 1.289   -30.339 66.866  1.00 23.63 ? 188  LEU B CD1 1 
ATOM   5224 C  CD2 . LEU B 1 189 ? 3.608   -31.238 67.273  1.00 25.65 ? 188  LEU B CD2 1 
ATOM   5225 N  N   . GLN B 1 190 ? 1.020   -35.981 66.765  1.00 22.01 ? 189  GLN B N   1 
ATOM   5226 C  CA  . GLN B 1 190 ? 0.275   -37.035 67.438  1.00 23.97 ? 189  GLN B CA  1 
ATOM   5227 C  C   . GLN B 1 190 ? 0.738   -38.439 67.073  1.00 23.79 ? 189  GLN B C   1 
ATOM   5228 O  O   . GLN B 1 190 ? 0.159   -39.407 67.574  1.00 27.06 ? 189  GLN B O   1 
ATOM   5229 C  CB  . GLN B 1 190 ? -1.225  -36.883 67.139  1.00 28.02 ? 189  GLN B CB  1 
ATOM   5230 C  CG  . GLN B 1 190 ? -1.564  -36.757 65.652  1.00 31.53 ? 189  GLN B CG  1 
ATOM   5231 C  CD  . GLN B 1 190 ? -1.828  -38.099 64.990  1.00 34.12 ? 189  GLN B CD  1 
ATOM   5232 O  OE1 . GLN B 1 190 ? -2.610  -38.907 65.492  1.00 38.41 ? 189  GLN B OE1 1 
ATOM   5233 N  NE2 . GLN B 1 190 ? -1.180  -38.342 63.854  1.00 31.78 ? 189  GLN B NE2 1 
ATOM   5234 N  N   . ARG B 1 191 ? 1.768   -38.582 66.235  1.00 22.91 ? 190  ARG B N   1 
ATOM   5235 C  CA  . ARG B 1 191 ? 2.202   -39.904 65.782  1.00 24.78 ? 190  ARG B CA  1 
ATOM   5236 C  C   . ARG B 1 191 ? 3.007   -40.585 66.883  1.00 27.70 ? 190  ARG B C   1 
ATOM   5237 O  O   . ARG B 1 191 ? 4.113   -40.146 67.214  1.00 27.86 ? 190  ARG B O   1 
ATOM   5238 C  CB  . ARG B 1 191 ? 3.025   -39.799 64.500  1.00 23.67 ? 190  ARG B CB  1 
ATOM   5239 C  CG  . ARG B 1 191 ? 2.230   -39.342 63.291  1.00 22.51 ? 190  ARG B CG  1 
ATOM   5240 C  CD  . ARG B 1 191 ? 3.113   -39.132 62.071  1.00 21.00 ? 190  ARG B CD  1 
ATOM   5241 N  NE  . ARG B 1 191 ? 2.334   -38.517 61.003  1.00 21.86 ? 190  ARG B NE  1 
ATOM   5242 C  CZ  . ARG B 1 191 ? 2.845   -37.927 59.933  1.00 22.21 ? 190  ARG B CZ  1 
ATOM   5243 N  NH1 . ARG B 1 191 ? 4.150   -37.901 59.713  1.00 24.19 ? 190  ARG B NH1 1 
ATOM   5244 N  NH2 . ARG B 1 191 ? 2.025   -37.348 59.060  1.00 23.21 ? 190  ARG B NH2 1 
ATOM   5245 N  N   . ALA B 1 192 ? 2.461   -41.670 67.440  1.00 29.90 ? 191  ALA B N   1 
ATOM   5246 C  CA  . ALA B 1 192 ? 3.182   -42.426 68.458  1.00 32.50 ? 191  ALA B CA  1 
ATOM   5247 C  C   . ALA B 1 192 ? 4.418   -43.116 67.890  1.00 34.23 ? 191  ALA B C   1 
ATOM   5248 O  O   . ALA B 1 192 ? 5.407   -43.303 68.611  1.00 33.62 ? 191  ALA B O   1 
ATOM   5249 C  CB  . ALA B 1 192 ? 2.252   -43.455 69.103  1.00 34.55 ? 191  ALA B CB  1 
ATOM   5250 N  N   A ASN B 1 193 ? 4.377   -43.532 66.626  0.40 33.58 ? 192  ASN B N   1 
ATOM   5251 N  N   B ASN B 1 193 ? 4.388   -43.479 66.607  0.60 33.23 ? 192  ASN B N   1 
ATOM   5252 C  CA  A ASN B 1 193 ? 5.533   -44.137 65.965  0.40 32.94 ? 192  ASN B CA  1 
ATOM   5253 C  CA  B ASN B 1 193 ? 5.500   -44.152 65.935  0.60 32.46 ? 192  ASN B CA  1 
ATOM   5254 C  C   A ASN B 1 193 ? 5.775   -43.394 64.662  0.40 32.10 ? 192  ASN B C   1 
ATOM   5255 C  C   B ASN B 1 193 ? 5.799   -43.412 64.640  0.60 32.03 ? 192  ASN B C   1 
ATOM   5256 O  O   A ASN B 1 193 ? 5.299   -43.808 63.595  0.40 32.66 ? 192  ASN B O   1 
ATOM   5257 O  O   B ASN B 1 193 ? 5.390   -43.851 63.556  0.60 32.99 ? 192  ASN B O   1 
ATOM   5258 C  CB  A ASN B 1 193 ? 5.334   -45.630 65.719  0.40 33.98 ? 192  ASN B CB  1 
ATOM   5259 C  CB  B ASN B 1 193 ? 5.172   -45.619 65.647  0.60 32.80 ? 192  ASN B CB  1 
ATOM   5260 C  CG  A ASN B 1 193 ? 6.533   -46.266 65.039  0.40 34.67 ? 192  ASN B CG  1 
ATOM   5261 C  CG  B ASN B 1 193 ? 4.590   -46.333 66.843  0.60 32.76 ? 192  ASN B CG  1 
ATOM   5262 O  OD1 A ASN B 1 193 ? 7.614   -45.674 64.980  0.40 32.31 ? 192  ASN B OD1 1 
ATOM   5263 O  OD1 B ASN B 1 193 ? 5.149   -46.292 67.935  0.60 33.49 ? 192  ASN B OD1 1 
ATOM   5264 N  ND2 A ASN B 1 193 ? 6.350   -47.474 64.520  0.40 37.90 ? 192  ASN B ND2 1 
ATOM   5265 N  ND2 B ASN B 1 193 ? 3.454   -46.989 66.645  0.60 33.31 ? 192  ASN B ND2 1 
ATOM   5266 N  N   . PRO B 1 194 ? 6.524   -42.292 64.709  1.00 31.32 ? 193  PRO B N   1 
ATOM   5267 C  CA  . PRO B 1 194 ? 6.745   -41.499 63.490  1.00 31.09 ? 193  PRO B CA  1 
ATOM   5268 C  C   . PRO B 1 194 ? 7.474   -42.249 62.385  1.00 31.21 ? 193  PRO B C   1 
ATOM   5269 O  O   . PRO B 1 194 ? 7.397   -41.825 61.225  1.00 29.49 ? 193  PRO B O   1 
ATOM   5270 C  CB  . PRO B 1 194 ? 7.562   -40.297 63.991  1.00 31.36 ? 193  PRO B CB  1 
ATOM   5271 C  CG  . PRO B 1 194 ? 8.145   -40.727 65.295  1.00 31.20 ? 193  PRO B CG  1 
ATOM   5272 C  CD  . PRO B 1 194 ? 7.173   -41.705 65.892  1.00 32.20 ? 193  PRO B CD  1 
ATOM   5273 N  N   . ASP B 1 195 ? 8.175   -43.340 62.691  1.00 32.65 ? 194  ASP B N   1 
ATOM   5274 C  CA  . ASP B 1 195 ? 8.900   -44.083 61.670  1.00 33.94 ? 194  ASP B CA  1 
ATOM   5275 C  C   . ASP B 1 195 ? 8.109   -45.262 61.122  1.00 33.74 ? 194  ASP B C   1 
ATOM   5276 O  O   . ASP B 1 195 ? 8.653   -46.057 60.346  1.00 34.41 ? 194  ASP B O   1 
ATOM   5277 C  CB  . ASP B 1 195 ? 10.251  -44.545 62.213  1.00 39.24 ? 194  ASP B CB  1 
ATOM   5278 C  CG  . ASP B 1 195 ? 11.248  -43.407 62.310  1.00 44.93 ? 194  ASP B CG  1 
ATOM   5279 O  OD1 . ASP B 1 195 ? 10.939  -42.303 61.808  1.00 44.31 ? 194  ASP B OD1 1 
ATOM   5280 O  OD2 . ASP B 1 195 ? 12.336  -43.611 62.886  1.00 50.10 ? 194  ASP B OD2 1 
ATOM   5281 N  N   . ASP B 1 196 ? 6.843   -45.384 61.496  1.00 32.43 ? 195  ASP B N   1 
ATOM   5282 C  CA  . ASP B 1 196 ? 5.970   -46.368 60.879  1.00 33.10 ? 195  ASP B CA  1 
ATOM   5283 C  C   . ASP B 1 196 ? 5.989   -46.185 59.359  1.00 31.12 ? 195  ASP B C   1 
ATOM   5284 O  O   . ASP B 1 196 ? 5.906   -45.047 58.876  1.00 28.60 ? 195  ASP B O   1 
ATOM   5285 C  CB  . ASP B 1 196 ? 4.550   -46.208 61.428  1.00 35.29 ? 195  ASP B CB  1 
ATOM   5286 C  CG  . ASP B 1 196 ? 3.626   -47.340 61.021  1.00 38.45 ? 195  ASP B CG  1 
ATOM   5287 O  OD1 . ASP B 1 196 ? 3.487   -47.605 59.808  1.00 37.94 ? 195  ASP B OD1 1 
ATOM   5288 O  OD2 . ASP B 1 196 ? 3.031   -47.963 61.922  1.00 41.20 ? 195  ASP B OD2 1 
ATOM   5289 N  N   . PRO B 1 197 ? 6.114   -47.262 58.580  1.00 31.15 ? 196  PRO B N   1 
ATOM   5290 C  CA  . PRO B 1 197 ? 6.146   -47.107 57.115  1.00 31.93 ? 196  PRO B CA  1 
ATOM   5291 C  C   . PRO B 1 197 ? 4.919   -46.414 56.555  1.00 30.65 ? 196  PRO B C   1 
ATOM   5292 O  O   . PRO B 1 197 ? 4.973   -45.889 55.435  1.00 30.74 ? 196  PRO B O   1 
ATOM   5293 C  CB  . PRO B 1 197 ? 6.255   -48.554 56.608  1.00 33.01 ? 196  PRO B CB  1 
ATOM   5294 C  CG  . PRO B 1 197 ? 6.788   -49.327 57.773  1.00 33.53 ? 196  PRO B CG  1 
ATOM   5295 C  CD  . PRO B 1 197 ? 6.249   -48.668 58.999  1.00 32.93 ? 196  PRO B CD  1 
ATOM   5296 N  N   . ALA B 1 198 ? 3.814   -46.387 57.302  1.00 29.33 ? 197  ALA B N   1 
ATOM   5297 C  CA  . ALA B 1 198 ? 2.629   -45.673 56.846  1.00 28.77 ? 197  ALA B CA  1 
ATOM   5298 C  C   . ALA B 1 198 ? 2.910   -44.201 56.571  1.00 28.12 ? 197  ALA B C   1 
ATOM   5299 O  O   . ALA B 1 198 ? 2.142   -43.566 55.840  1.00 29.95 ? 197  ALA B O   1 
ATOM   5300 C  CB  . ALA B 1 198 ? 1.510   -45.804 57.881  1.00 28.83 ? 197  ALA B CB  1 
ATOM   5301 N  N   . TYR B 1 199 ? 3.987   -43.644 57.133  1.00 24.24 ? 198  TYR B N   1 
ATOM   5302 C  CA  . TYR B 1 199 ? 4.318   -42.234 56.963  1.00 23.35 ? 198  TYR B CA  1 
ATOM   5303 C  C   . TYR B 1 199 ? 5.453   -42.003 55.972  1.00 22.42 ? 198  TYR B C   1 
ATOM   5304 O  O   . TYR B 1 199 ? 5.911   -40.863 55.829  1.00 23.50 ? 198  TYR B O   1 
ATOM   5305 C  CB  . TYR B 1 199 ? 4.676   -41.595 58.314  1.00 19.71 ? 198  TYR B CB  1 
ATOM   5306 C  CG  . TYR B 1 199 ? 3.655   -41.858 59.399  1.00 22.34 ? 198  TYR B CG  1 
ATOM   5307 C  CD1 . TYR B 1 199 ? 2.347   -41.411 59.271  1.00 23.89 ? 198  TYR B CD1 1 
ATOM   5308 C  CD2 . TYR B 1 199 ? 4.001   -42.552 60.554  1.00 24.79 ? 198  TYR B CD2 1 
ATOM   5309 C  CE1 . TYR B 1 199 ? 1.408   -41.653 60.256  1.00 28.56 ? 198  TYR B CE1 1 
ATOM   5310 C  CE2 . TYR B 1 199 ? 3.067   -42.800 61.549  1.00 28.28 ? 198  TYR B CE2 1 
ATOM   5311 C  CZ  . TYR B 1 199 ? 1.770   -42.342 61.394  1.00 28.88 ? 198  TYR B CZ  1 
ATOM   5312 O  OH  . TYR B 1 199 ? 0.830   -42.574 62.376  1.00 30.96 ? 198  TYR B OH  1 
ATOM   5313 N  N   . ASP B 1 200 ? 5.917   -43.052 55.285  1.00 24.49 ? 199  ASP B N   1 
ATOM   5314 C  CA  . ASP B 1 200 ? 6.989   -42.880 54.307  1.00 27.37 ? 199  ASP B CA  1 
ATOM   5315 C  C   . ASP B 1 200 ? 6.608   -41.850 53.248  1.00 29.19 ? 199  ASP B C   1 
ATOM   5316 O  O   . ASP B 1 200 ? 7.413   -40.981 52.888  1.00 28.06 ? 199  ASP B O   1 
ATOM   5317 C  CB  . ASP B 1 200 ? 7.324   -44.221 53.651  1.00 27.68 ? 199  ASP B CB  1 
ATOM   5318 C  CG  . ASP B 1 200 ? 8.082   -45.165 54.575  1.00 30.99 ? 199  ASP B CG  1 
ATOM   5319 O  OD1 . ASP B 1 200 ? 8.441   -44.760 55.701  1.00 30.16 ? 199  ASP B OD1 1 
ATOM   5320 O  OD2 . ASP B 1 200 ? 8.328   -46.323 54.167  1.00 34.71 ? 199  ASP B OD2 1 
ATOM   5321 N  N   . GLU B 1 201 ? 5.376   -41.936 52.732  1.00 30.93 ? 200  GLU B N   1 
ATOM   5322 C  CA  . GLU B 1 201 ? 4.948   -41.007 51.692  1.00 31.86 ? 200  GLU B CA  1 
ATOM   5323 C  C   . GLU B 1 201 ? 4.782   -39.592 52.239  1.00 29.04 ? 200  GLU B C   1 
ATOM   5324 O  O   . GLU B 1 201 ? 5.149   -38.621 51.568  1.00 29.02 ? 200  GLU B O   1 
ATOM   5325 C  CB  . GLU B 1 201 ? 3.651   -41.499 51.048  1.00 36.33 ? 200  GLU B CB  1 
ATOM   5326 C  CG  . GLU B 1 201 ? 3.058   -40.532 50.034  1.00 41.25 ? 200  GLU B CG  1 
ATOM   5327 C  CD  . GLU B 1 201 ? 4.005   -40.219 48.883  1.00 47.20 ? 200  GLU B CD  1 
ATOM   5328 O  OE1 . GLU B 1 201 ? 5.029   -40.920 48.732  1.00 49.97 ? 200  GLU B OE1 1 
ATOM   5329 O  OE2 . GLU B 1 201 ? 3.724   -39.262 48.130  1.00 50.22 ? 200  GLU B OE2 1 
ATOM   5330 N  N   . ASN B 1 202 ? 4.230   -39.447 53.451  1.00 25.68 ? 201  ASN B N   1 
ATOM   5331 C  CA  . ASN B 1 202 ? 4.154   -38.122 54.065  1.00 23.71 ? 201  ASN B CA  1 
ATOM   5332 C  C   . ASN B 1 202 ? 5.524   -37.465 54.109  1.00 24.63 ? 201  ASN B C   1 
ATOM   5333 O  O   . ASN B 1 202 ? 5.655   -36.256 53.880  1.00 25.34 ? 201  ASN B O   1 
ATOM   5334 C  CB  . ASN B 1 202 ? 3.590   -38.208 55.485  1.00 25.69 ? 201  ASN B CB  1 
ATOM   5335 C  CG  . ASN B 1 202 ? 2.205   -38.807 55.535  1.00 28.58 ? 201  ASN B CG  1 
ATOM   5336 O  OD1 . ASN B 1 202 ? 2.040   -39.988 55.840  1.00 31.75 ? 201  ASN B OD1 1 
ATOM   5337 N  ND2 . ASN B 1 202 ? 1.199   -37.996 55.242  1.00 30.87 ? 201  ASN B ND2 1 
ATOM   5338 N  N   . LYS B 1 203 ? 6.557   -38.248 54.423  1.00 22.62 ? 202  LYS B N   1 
ATOM   5339 C  CA  . LYS B 1 203 ? 7.904   -37.703 54.538  1.00 25.23 ? 202  LYS B CA  1 
ATOM   5340 C  C   . LYS B 1 203 ? 8.443   -37.285 53.180  1.00 26.47 ? 202  LYS B C   1 
ATOM   5341 O  O   . LYS B 1 203 ? 9.067   -36.223 53.050  1.00 25.97 ? 202  LYS B O   1 
ATOM   5342 C  CB  . LYS B 1 203 ? 8.826   -38.734 55.193  1.00 23.62 ? 202  LYS B CB  1 
ATOM   5343 C  CG  . LYS B 1 203 ? 8.475   -39.052 56.645  1.00 24.94 ? 202  LYS B CG  1 
ATOM   5344 C  CD  . LYS B 1 203 ? 9.286   -40.225 57.180  1.00 26.06 ? 202  LYS B CD  1 
ATOM   5345 C  CE  . LYS B 1 203 ? 9.033   -40.426 58.668  1.00 26.35 ? 202  LYS B CE  1 
ATOM   5346 N  NZ  . LYS B 1 203 ? 9.665   -41.664 59.175  1.00 27.36 ? 202  LYS B NZ  1 
ATOM   5347 N  N   . ARG B 1 204 ? 8.211   -38.111 52.157  1.00 26.98 ? 203  ARG B N   1 
ATOM   5348 C  CA  . ARG B 1 204 ? 8.602   -37.740 50.803  1.00 26.95 ? 203  ARG B CA  1 
ATOM   5349 C  C   . ARG B 1 204 ? 7.905   -36.458 50.362  1.00 24.69 ? 203  ARG B C   1 
ATOM   5350 O  O   . ARG B 1 204 ? 8.531   -35.573 49.763  1.00 24.64 ? 203  ARG B O   1 
ATOM   5351 C  CB  . ARG B 1 204 ? 8.286   -38.882 49.837  1.00 31.97 ? 203  ARG B CB  1 
ATOM   5352 C  CG  . ARG B 1 204 ? 8.813   -38.658 48.425  1.00 38.78 ? 203  ARG B CG  1 
ATOM   5353 C  CD  . ARG B 1 204 ? 7.936   -39.332 47.370  1.00 43.68 ? 203  ARG B CD  1 
ATOM   5354 N  NE  . ARG B 1 204 ? 6.615   -38.717 47.289  1.00 47.54 ? 203  ARG B NE  1 
ATOM   5355 C  CZ  . ARG B 1 204 ? 6.356   -37.570 46.674  1.00 50.28 ? 203  ARG B CZ  1 
ATOM   5356 N  NH1 . ARG B 1 204 ? 7.308   -36.881 46.063  1.00 50.63 ? 203  ARG B NH1 1 
ATOM   5357 N  NH2 . ARG B 1 204 ? 5.111   -37.099 46.676  1.00 50.46 ? 203  ARG B NH2 1 
ATOM   5358 N  N   . GLN B 1 205 ? 6.602   -36.341 50.644  1.00 23.73 ? 204  GLN B N   1 
ATOM   5359 C  CA  . GLN B 1 205 ? 5.867   -35.136 50.266  1.00 22.05 ? 204  GLN B CA  1 
ATOM   5360 C  C   . GLN B 1 205 ? 6.354   -33.921 51.048  1.00 21.54 ? 204  GLN B C   1 
ATOM   5361 O  O   . GLN B 1 205 ? 6.409   -32.808 50.512  1.00 23.24 ? 204  GLN B O   1 
ATOM   5362 C  CB  . GLN B 1 205 ? 4.371   -35.349 50.491  1.00 21.72 ? 204  GLN B CB  1 
ATOM   5363 C  CG  . GLN B 1 205 ? 3.512   -34.145 50.178  1.00 24.94 ? 204  GLN B CG  1 
ATOM   5364 C  CD  . GLN B 1 205 ? 3.472   -33.828 48.697  1.00 27.08 ? 204  GLN B CD  1 
ATOM   5365 O  OE1 . GLN B 1 205 ? 4.151   -32.913 48.222  1.00 27.18 ? 204  GLN B OE1 1 
ATOM   5366 N  NE2 . GLN B 1 205 ? 2.668   -34.583 47.955  1.00 29.62 ? 204  GLN B NE2 1 
ATOM   5367 N  N   . PHE B 1 206 ? 6.695   -34.112 52.324  1.00 21.10 ? 205  PHE B N   1 
ATOM   5368 C  CA  . PHE B 1 206 ? 7.223   -33.013 53.128  1.00 21.94 ? 205  PHE B CA  1 
ATOM   5369 C  C   . PHE B 1 206 ? 8.506   -32.461 52.513  1.00 21.40 ? 205  PHE B C   1 
ATOM   5370 O  O   . PHE B 1 206 ? 8.671   -31.242 52.363  1.00 20.45 ? 205  PHE B O   1 
ATOM   5371 C  CB  . PHE B 1 206 ? 7.453   -33.507 54.562  1.00 22.07 ? 205  PHE B CB  1 
ATOM   5372 C  CG  . PHE B 1 206 ? 7.764   -32.419 55.560  1.00 21.61 ? 205  PHE B CG  1 
ATOM   5373 C  CD1 . PHE B 1 206 ? 6.835   -31.428 55.850  1.00 21.77 ? 205  PHE B CD1 1 
ATOM   5374 C  CD2 . PHE B 1 206 ? 8.972   -32.423 56.249  1.00 20.99 ? 205  PHE B CD2 1 
ATOM   5375 C  CE1 . PHE B 1 206 ? 7.118   -30.438 56.791  1.00 21.43 ? 205  PHE B CE1 1 
ATOM   5376 C  CE2 . PHE B 1 206 ? 9.260   -31.449 57.183  1.00 20.03 ? 205  PHE B CE2 1 
ATOM   5377 C  CZ  . PHE B 1 206 ? 8.334   -30.453 57.458  1.00 22.30 ? 205  PHE B CZ  1 
ATOM   5378 N  N   . GLN B 1 207 ? 9.425   -33.346 52.132  1.00 20.59 ? 206  GLN B N   1 
ATOM   5379 C  CA  . GLN B 1 207 ? 10.661  -32.877 51.517  1.00 22.14 ? 206  GLN B CA  1 
ATOM   5380 C  C   . GLN B 1 207 ? 10.377  -32.166 50.203  1.00 24.23 ? 206  GLN B C   1 
ATOM   5381 O  O   . GLN B 1 207 ? 11.033  -31.171 49.872  1.00 25.05 ? 206  GLN B O   1 
ATOM   5382 C  CB  . GLN B 1 207 ? 11.623  -34.043 51.306  1.00 23.89 ? 206  GLN B CB  1 
ATOM   5383 C  CG  . GLN B 1 207 ? 12.129  -34.655 52.602  1.00 29.64 ? 206  GLN B CG  1 
ATOM   5384 C  CD  . GLN B 1 207 ? 12.808  -33.634 53.504  1.00 33.37 ? 206  GLN B CD  1 
ATOM   5385 O  OE1 . GLN B 1 207 ? 13.638  -32.840 53.051  1.00 36.82 ? 206  GLN B OE1 1 
ATOM   5386 N  NE2 . GLN B 1 207 ? 12.451  -33.643 54.789  1.00 31.88 ? 206  GLN B NE2 1 
ATOM   5387 N  N   . GLU B 1 208 ? 9.394   -32.656 49.446  1.00 21.59 ? 207  GLU B N   1 
ATOM   5388 C  CA  . GLU B 1 208 ? 9.046   -32.010 48.186  1.00 25.03 ? 207  GLU B CA  1 
ATOM   5389 C  C   . GLU B 1 208 ? 8.509   -30.606 48.425  1.00 23.84 ? 207  GLU B C   1 
ATOM   5390 O  O   . GLU B 1 208 ? 8.879   -29.661 47.717  1.00 22.38 ? 207  GLU B O   1 
ATOM   5391 C  CB  . GLU B 1 208 ? 8.026   -32.859 47.426  1.00 31.86 ? 207  GLU B CB  1 
ATOM   5392 C  CG  . GLU B 1 208 ? 7.308   -32.116 46.314  1.00 40.94 ? 207  GLU B CG  1 
ATOM   5393 C  CD  . GLU B 1 208 ? 6.225   -32.957 45.662  1.00 50.53 ? 207  GLU B CD  1 
ATOM   5394 O  OE1 . GLU B 1 208 ? 6.419   -34.187 45.538  1.00 55.01 ? 207  GLU B OE1 1 
ATOM   5395 O  OE2 . GLU B 1 208 ? 5.175   -32.391 45.285  1.00 52.75 ? 207  GLU B OE2 1 
ATOM   5396 N  N   . ASP B 1 209 ? 7.640   -30.451 49.428  1.00 21.60 ? 208  ASP B N   1 
ATOM   5397 C  CA  . ASP B 1 209 ? 7.094   -29.137 49.733  1.00 19.72 ? 208  ASP B CA  1 
ATOM   5398 C  C   . ASP B 1 209 ? 8.175   -28.187 50.242  1.00 21.50 ? 208  ASP B C   1 
ATOM   5399 O  O   . ASP B 1 209 ? 8.118   -26.982 49.970  1.00 20.08 ? 208  ASP B O   1 
ATOM   5400 C  CB  . ASP B 1 209 ? 5.956   -29.263 50.747  1.00 20.46 ? 208  ASP B CB  1 
ATOM   5401 C  CG  . ASP B 1 209 ? 4.716   -29.908 50.151  1.00 24.99 ? 208  ASP B CG  1 
ATOM   5402 O  OD1 . ASP B 1 209 ? 4.434   -29.666 48.951  1.00 25.35 ? 208  ASP B OD1 1 
ATOM   5403 O  OD2 . ASP B 1 209 ? 4.024   -30.655 50.884  1.00 23.00 ? 208  ASP B OD2 1 
ATOM   5404 N  N   . ILE B 1 210 ? 9.162   -28.699 50.980  1.00 21.93 ? 209  ILE B N   1 
ATOM   5405 C  CA  . ILE B 1 210 ? 10.261  -27.839 51.411  1.00 21.50 ? 209  ILE B CA  1 
ATOM   5406 C  C   . ILE B 1 210 ? 11.048  -27.342 50.202  1.00 22.65 ? 209  ILE B C   1 
ATOM   5407 O  O   . ILE B 1 210 ? 11.500  -26.188 50.165  1.00 23.54 ? 209  ILE B O   1 
ATOM   5408 C  CB  . ILE B 1 210 ? 11.162  -28.578 52.419  1.00 23.43 ? 209  ILE B CB  1 
ATOM   5409 C  CG1 . ILE B 1 210 ? 10.402  -28.822 53.730  1.00 23.24 ? 209  ILE B CG1 1 
ATOM   5410 C  CG2 . ILE B 1 210 ? 12.437  -27.785 52.681  1.00 23.50 ? 209  ILE B CG2 1 
ATOM   5411 C  CD1 . ILE B 1 210 ? 11.218  -29.523 54.810  1.00 24.74 ? 209  ILE B CD1 1 
ATOM   5412 N  N   . LYS B 1 211 ? 11.213  -28.195 49.188  1.00 22.68 ? 210  LYS B N   1 
ATOM   5413 C  CA  . LYS B 1 211 ? 11.935  -27.776 47.988  1.00 23.23 ? 210  LYS B CA  1 
ATOM   5414 C  C   . LYS B 1 211 ? 11.169  -26.703 47.221  1.00 23.44 ? 210  LYS B C   1 
ATOM   5415 O  O   . LYS B 1 211 ? 11.774  -25.760 46.698  1.00 25.70 ? 210  LYS B O   1 
ATOM   5416 C  CB  . LYS B 1 211 ? 12.212  -28.973 47.080  1.00 25.50 ? 210  LYS B CB  1 
ATOM   5417 C  CG  . LYS B 1 211 ? 12.954  -28.564 45.807  1.00 33.68 ? 210  LYS B CG  1 
ATOM   5418 C  CD  . LYS B 1 211 ? 13.318  -29.748 44.931  1.00 40.70 ? 210  LYS B CD  1 
ATOM   5419 C  CE  . LYS B 1 211 ? 13.879  -29.282 43.595  1.00 44.69 ? 210  LYS B CE  1 
ATOM   5420 N  NZ  . LYS B 1 211 ? 12.835  -28.654 42.740  1.00 48.82 ? 210  LYS B NZ  1 
ATOM   5421 N  N   . VAL B 1 212 ? 9.840   -26.831 47.134  1.00 21.24 ? 211  VAL B N   1 
ATOM   5422 C  CA  . VAL B 1 212 ? 9.037   -25.805 46.463  1.00 21.39 ? 211  VAL B CA  1 
ATOM   5423 C  C   . VAL B 1 212 ? 9.242   -24.453 47.135  1.00 23.08 ? 211  VAL B C   1 
ATOM   5424 O  O   . VAL B 1 212 ? 9.449   -23.428 46.470  1.00 22.95 ? 211  VAL B O   1 
ATOM   5425 C  CB  . VAL B 1 212 ? 7.548   -26.211 46.444  1.00 20.64 ? 211  VAL B CB  1 
ATOM   5426 C  CG1 . VAL B 1 212 ? 6.673   -25.068 45.925  1.00 21.24 ? 211  VAL B CG1 1 
ATOM   5427 C  CG2 . VAL B 1 212 ? 7.351   -27.434 45.578  1.00 21.99 ? 211  VAL B CG2 1 
ATOM   5428 N  N   . MET B 1 213 ? 9.199   -24.427 48.466  1.00 22.89 ? 212  MET B N   1 
ATOM   5429 C  CA  . MET B 1 213 ? 9.400   -23.163 49.165  1.00 21.78 ? 212  MET B CA  1 
ATOM   5430 C  C   . MET B 1 213 ? 10.801  -22.610 48.913  1.00 22.32 ? 212  MET B C   1 
ATOM   5431 O  O   . MET B 1 213 ? 10.967  -21.406 48.683  1.00 24.84 ? 212  MET B O   1 
ATOM   5432 C  CB  . MET B 1 213 ? 9.119   -23.346 50.658  1.00 24.06 ? 212  MET B CB  1 
ATOM   5433 C  CG  . MET B 1 213 ? 7.656   -23.716 50.913  1.00 25.99 ? 212  MET B CG  1 
ATOM   5434 S  SD  . MET B 1 213 ? 7.128   -23.632 52.631  1.00 29.34 ? 212  MET B SD  1 
ATOM   5435 C  CE  . MET B 1 213 ? 8.250   -24.840 53.317  1.00 27.73 ? 212  MET B CE  1 
ATOM   5436 N  N   . ASN B 1 214 ? 11.819  -23.475 48.916  1.00 22.12 ? 213  ASN B N   1 
ATOM   5437 C  CA  . ASN B 1 214 ? 13.180  -22.987 48.698  1.00 24.31 ? 213  ASN B CA  1 
ATOM   5438 C  C   . ASN B 1 214 ? 13.413  -22.562 47.255  1.00 25.83 ? 213  ASN B C   1 
ATOM   5439 O  O   . ASN B 1 214 ? 14.222  -21.663 47.004  1.00 25.67 ? 213  ASN B O   1 
ATOM   5440 C  CB  . ASN B 1 214 ? 14.200  -24.045 49.103  1.00 23.71 ? 213  ASN B CB  1 
ATOM   5441 C  CG  . ASN B 1 214 ? 14.549  -23.973 50.577  1.00 30.14 ? 213  ASN B CG  1 
ATOM   5442 O  OD1 . ASN B 1 214 ? 15.426  -23.208 50.984  1.00 35.75 ? 213  ASN B OD1 1 
ATOM   5443 N  ND2 . ASN B 1 214 ? 13.859  -24.764 51.386  1.00 28.12 ? 213  ASN B ND2 1 
ATOM   5444 N  N   . ASP B 1 215 ? 12.731  -23.187 46.293  1.00 25.10 ? 214  ASP B N   1 
ATOM   5445 C  CA  . ASP B 1 215 ? 12.861  -22.721 44.916  1.00 27.72 ? 214  ASP B CA  1 
ATOM   5446 C  C   . ASP B 1 215 ? 12.388  -21.277 44.780  1.00 26.06 ? 214  ASP B C   1 
ATOM   5447 O  O   . ASP B 1 215 ? 13.007  -20.475 44.071  1.00 26.33 ? 214  ASP B O   1 
ATOM   5448 C  CB  . ASP B 1 215 ? 12.091  -23.643 43.971  1.00 29.95 ? 214  ASP B CB  1 
ATOM   5449 C  CG  . ASP B 1 215 ? 12.795  -24.974 43.754  1.00 36.64 ? 214  ASP B CG  1 
ATOM   5450 O  OD1 . ASP B 1 215 ? 13.992  -25.075 44.101  1.00 37.96 ? 214  ASP B OD1 1 
ATOM   5451 O  OD2 . ASP B 1 215 ? 12.158  -25.920 43.237  1.00 40.25 ? 214  ASP B OD2 1 
ATOM   5452 N  N   . LEU B 1 216 ? 11.297  -20.923 45.461  1.00 25.20 ? 215  LEU B N   1 
ATOM   5453 C  CA  . LEU B 1 216 ? 10.802  -19.551 45.394  1.00 23.71 ? 215  LEU B CA  1 
ATOM   5454 C  C   . LEU B 1 216 ? 11.757  -18.579 46.077  1.00 23.37 ? 215  LEU B C   1 
ATOM   5455 O  O   . LEU B 1 216 ? 11.965  -17.459 45.590  1.00 24.00 ? 215  LEU B O   1 
ATOM   5456 C  CB  . LEU B 1 216 ? 9.414   -19.460 46.024  1.00 25.24 ? 215  LEU B CB  1 
ATOM   5457 C  CG  . LEU B 1 216 ? 8.881   -18.032 46.139  1.00 28.07 ? 215  LEU B CG  1 
ATOM   5458 C  CD1 . LEU B 1 216 ? 8.492   -17.487 44.764  1.00 30.74 ? 215  LEU B CD1 1 
ATOM   5459 C  CD2 . LEU B 1 216 ? 7.722   -17.985 47.091  1.00 32.21 ? 215  LEU B CD2 1 
ATOM   5460 N  N   . VAL B 1 217 ? 12.331  -18.978 47.218  1.00 19.83 ? 216  VAL B N   1 
ATOM   5461 C  CA  . VAL B 1 217 ? 13.360  -18.155 47.852  1.00 22.33 ? 216  VAL B CA  1 
ATOM   5462 C  C   . VAL B 1 217 ? 14.508  -17.903 46.883  1.00 23.20 ? 216  VAL B C   1 
ATOM   5463 O  O   . VAL B 1 217 ? 15.072  -16.802 46.840  1.00 24.82 ? 216  VAL B O   1 
ATOM   5464 C  CB  . VAL B 1 217 ? 13.859  -18.818 49.149  1.00 23.00 ? 216  VAL B CB  1 
ATOM   5465 C  CG1 . VAL B 1 217 ? 15.057  -18.059 49.704  1.00 21.67 ? 216  VAL B CG1 1 
ATOM   5466 C  CG2 . VAL B 1 217 ? 12.742  -18.892 50.169  1.00 24.59 ? 216  VAL B CG2 1 
ATOM   5467 N  N   . ASP B 1 218 ? 14.876  -18.918 46.093  1.00 28.36 ? 217  ASP B N   1 
ATOM   5468 C  CA  . ASP B 1 218 ? 15.933  -18.736 45.101  1.00 31.11 ? 217  ASP B CA  1 
ATOM   5469 C  C   . ASP B 1 218 ? 15.567  -17.643 44.104  1.00 32.04 ? 217  ASP B C   1 
ATOM   5470 O  O   . ASP B 1 218 ? 16.402  -16.795 43.763  1.00 32.84 ? 217  ASP B O   1 
ATOM   5471 C  CB  . ASP B 1 218 ? 16.207  -20.050 44.360  1.00 36.38 ? 217  ASP B CB  1 
ATOM   5472 C  CG  . ASP B 1 218 ? 16.866  -21.104 45.238  1.00 38.51 ? 217  ASP B CG  1 
ATOM   5473 O  OD1 . ASP B 1 218 ? 17.435  -20.748 46.292  1.00 37.04 ? 217  ASP B OD1 1 
ATOM   5474 O  OD2 . ASP B 1 218 ? 16.820  -22.298 44.863  1.00 39.85 ? 217  ASP B OD2 1 
ATOM   5475 N  N   . LYS B 1 219 ? 14.318  -17.647 43.625  1.00 30.99 ? 218  LYS B N   1 
ATOM   5476 C  CA  . LYS B 1 219 ? 13.899  -16.646 42.648  1.00 30.39 ? 218  LYS B CA  1 
ATOM   5477 C  C   . LYS B 1 219 ? 13.929  -15.243 43.243  1.00 27.43 ? 218  LYS B C   1 
ATOM   5478 O  O   . LYS B 1 219 ? 14.330  -14.284 42.570  1.00 25.80 ? 218  LYS B O   1 
ATOM   5479 C  CB  . LYS B 1 219 ? 12.502  -16.973 42.119  1.00 31.57 ? 218  LYS B CB  1 
ATOM   5480 C  CG  . LYS B 1 219 ? 12.449  -18.186 41.195  1.00 37.14 ? 218  LYS B CG  1 
ATOM   5481 C  CD  . LYS B 1 219 ? 11.056  -18.377 40.610  1.00 41.39 ? 218  LYS B CD  1 
ATOM   5482 C  CE  . LYS B 1 219 ? 11.006  -19.567 39.657  1.00 46.16 ? 218  LYS B CE  1 
ATOM   5483 N  NZ  . LYS B 1 219 ? 11.278  -20.864 40.343  1.00 49.00 ? 218  LYS B NZ  1 
ATOM   5484 N  N   . ILE B 1 220 ? 13.497  -15.100 44.498  1.00 22.12 ? 219  ILE B N   1 
ATOM   5485 C  CA  . ILE B 1 220 ? 13.507  -13.782 45.131  1.00 21.70 ? 219  ILE B CA  1 
ATOM   5486 C  C   . ILE B 1 220 ? 14.932  -13.258 45.256  1.00 24.69 ? 219  ILE B C   1 
ATOM   5487 O  O   . ILE B 1 220 ? 15.199  -12.075 45.004  1.00 24.38 ? 219  ILE B O   1 
ATOM   5488 C  CB  . ILE B 1 220 ? 12.805  -13.836 46.500  1.00 21.53 ? 219  ILE B CB  1 
ATOM   5489 C  CG1 . ILE B 1 220 ? 11.296  -14.049 46.331  1.00 20.78 ? 219  ILE B CG1 1 
ATOM   5490 C  CG2 . ILE B 1 220 ? 13.086  -12.559 47.286  1.00 21.82 ? 219  ILE B CG2 1 
ATOM   5491 C  CD1 . ILE B 1 220 ? 10.541  -14.195 47.656  1.00 19.61 ? 219  ILE B CD1 1 
ATOM   5492 N  N   . ILE B 1 221 ? 15.871  -14.122 45.652  1.00 23.67 ? 220  ILE B N   1 
ATOM   5493 C  CA  . ILE B 1 221 ? 17.251  -13.678 45.814  1.00 25.80 ? 220  ILE B CA  1 
ATOM   5494 C  C   . ILE B 1 221 ? 17.847  -13.298 44.467  1.00 29.14 ? 220  ILE B C   1 
ATOM   5495 O  O   . ILE B 1 221 ? 18.531  -12.274 44.342  1.00 29.31 ? 220  ILE B O   1 
ATOM   5496 C  CB  . ILE B 1 221 ? 18.085  -14.763 46.517  1.00 28.09 ? 220  ILE B CB  1 
ATOM   5497 C  CG1 . ILE B 1 221 ? 17.583  -14.982 47.946  1.00 30.22 ? 220  ILE B CG1 1 
ATOM   5498 C  CG2 . ILE B 1 221 ? 19.573  -14.389 46.507  1.00 30.17 ? 220  ILE B CG2 1 
ATOM   5499 C  CD1 . ILE B 1 221 ? 18.303  -16.104 48.681  1.00 32.05 ? 220  ILE B CD1 1 
ATOM   5500 N  N   . ALA B 1 222 ? 17.588  -14.108 43.435  1.00 33.07 ? 221  ALA B N   1 
ATOM   5501 C  CA  . ALA B 1 222 ? 18.113  -13.812 42.103  1.00 36.39 ? 221  ALA B CA  1 
ATOM   5502 C  C   . ALA B 1 222 ? 17.517  -12.526 41.539  1.00 37.25 ? 221  ALA B C   1 
ATOM   5503 O  O   . ALA B 1 222 ? 18.221  -11.736 40.896  1.00 36.75 ? 221  ALA B O   1 
ATOM   5504 C  CB  . ALA B 1 222 ? 17.843  -14.988 41.162  1.00 35.93 ? 221  ALA B CB  1 
ATOM   5505 N  N   . ASP B 1 223 ? 16.217  -12.309 41.760  1.00 37.19 ? 222  ASP B N   1 
ATOM   5506 C  CA  . ASP B 1 223 ? 15.557  -11.083 41.315  1.00 37.65 ? 222  ASP B CA  1 
ATOM   5507 C  C   . ASP B 1 223 ? 16.242  -9.849  41.894  1.00 36.60 ? 222  ASP B C   1 
ATOM   5508 O  O   . ASP B 1 223 ? 16.541  -8.890  41.171  1.00 38.21 ? 222  ASP B O   1 
ATOM   5509 C  CB  . ASP B 1 223 ? 14.073  -11.138 41.707  1.00 39.63 ? 222  ASP B CB  1 
ATOM   5510 C  CG  . ASP B 1 223 ? 13.290  -9.894  41.295  1.00 41.21 ? 222  ASP B CG  1 
ATOM   5511 O  OD1 . ASP B 1 223 ? 13.398  -8.851  41.983  1.00 40.98 ? 222  ASP B OD1 1 
ATOM   5512 O  OD2 . ASP B 1 223 ? 12.553  -9.965  40.284  1.00 39.99 ? 222  ASP B OD2 1 
ATOM   5513 N  N   . ARG B 1 224 ? 16.512  -9.861  43.202  1.00 31.40 ? 223  ARG B N   1 
ATOM   5514 C  CA  . ARG B 1 224 ? 17.152  -8.711  43.833  1.00 32.09 ? 223  ARG B CA  1 
ATOM   5515 C  C   . ARG B 1 224 ? 18.593  -8.545  43.367  1.00 35.99 ? 223  ARG B C   1 
ATOM   5516 O  O   . ARG B 1 224 ? 19.045  -7.421  43.122  1.00 37.52 ? 223  ARG B O   1 
ATOM   5517 C  CB  . ARG B 1 224 ? 17.103  -8.847  45.353  1.00 30.45 ? 223  ARG B CB  1 
ATOM   5518 C  CG  . ARG B 1 224 ? 17.773  -7.696  46.075  1.00 26.08 ? 223  ARG B CG  1 
ATOM   5519 C  CD  . ARG B 1 224 ? 17.081  -6.397  45.728  1.00 25.58 ? 223  ARG B CD  1 
ATOM   5520 N  NE  . ARG B 1 224 ? 15.655  -6.445  46.034  1.00 22.32 ? 223  ARG B NE  1 
ATOM   5521 C  CZ  . ARG B 1 224 ? 15.105  -5.940  47.130  1.00 20.98 ? 223  ARG B CZ  1 
ATOM   5522 N  NH1 . ARG B 1 224 ? 15.834  -5.341  48.053  1.00 21.88 ? 223  ARG B NH1 1 
ATOM   5523 N  NH2 . ARG B 1 224 ? 13.788  -6.049  47.306  1.00 21.30 ? 223  ARG B NH2 1 
ATOM   5524 N  N   . LYS B 1 225 ? 19.336  -9.649  43.256  1.00 40.04 ? 224  LYS B N   1 
ATOM   5525 C  CA  . LYS B 1 225 ? 20.727  -9.551  42.829  1.00 48.17 ? 224  LYS B CA  1 
ATOM   5526 C  C   . LYS B 1 225 ? 20.840  -8.988  41.417  1.00 53.00 ? 224  LYS B C   1 
ATOM   5527 O  O   . LYS B 1 225 ? 21.814  -8.294  41.099  1.00 55.77 ? 224  LYS B O   1 
ATOM   5528 C  CB  . LYS B 1 225 ? 21.399  -10.921 42.922  1.00 52.91 ? 224  LYS B CB  1 
ATOM   5529 C  CG  . LYS B 1 225 ? 22.861  -10.933 42.513  1.00 59.97 ? 224  LYS B CG  1 
ATOM   5530 C  CD  . LYS B 1 225 ? 23.615  -12.034 43.243  1.00 65.14 ? 224  LYS B CD  1 
ATOM   5531 C  CE  . LYS B 1 225 ? 24.677  -12.664 42.356  1.00 68.24 ? 224  LYS B CE  1 
ATOM   5532 N  NZ  . LYS B 1 225 ? 24.066  -13.429 41.231  1.00 70.67 ? 224  LYS B NZ  1 
ATOM   5533 N  N   . ALA B 1 226 ? 19.853  -9.261  40.565  1.00 54.96 ? 225  ALA B N   1 
ATOM   5534 C  CA  . ALA B 1 226 ? 19.845  -8.769  39.194  1.00 56.80 ? 225  ALA B CA  1 
ATOM   5535 C  C   . ALA B 1 226 ? 19.146  -7.425  39.048  1.00 61.37 ? 225  ALA B C   1 
ATOM   5536 O  O   . ALA B 1 226 ? 19.167  -6.848  37.956  1.00 61.72 ? 225  ALA B O   1 
ATOM   5537 C  CB  . ALA B 1 226 ? 19.172  -9.791  38.272  1.00 55.50 ? 225  ALA B CB  1 
ATOM   5538 N  N   . SER B 1 227 ? 18.539  -6.914  40.116  1.00 65.47 ? 226  SER B N   1 
ATOM   5539 C  CA  . SER B 1 227 ? 17.742  -5.694  40.052  1.00 68.97 ? 226  SER B CA  1 
ATOM   5540 C  C   . SER B 1 227 ? 18.661  -4.480  39.985  1.00 73.12 ? 226  SER B C   1 
ATOM   5541 O  O   . SER B 1 227 ? 19.300  -4.120  40.980  1.00 72.86 ? 226  SER B O   1 
ATOM   5542 C  CB  . SER B 1 227 ? 16.813  -5.608  41.259  1.00 68.77 ? 226  SER B CB  1 
ATOM   5543 O  OG  . SER B 1 227 ? 16.162  -4.352  41.308  1.00 70.33 ? 226  SER B OG  1 
ATOM   5544 N  N   . GLY B 1 228 ? 18.731  -3.847  38.812  1.00 76.44 ? 227  GLY B N   1 
ATOM   5545 C  CA  . GLY B 1 228 ? 19.386  -2.554  38.723  1.00 78.76 ? 227  GLY B CA  1 
ATOM   5546 C  C   . GLY B 1 228 ? 18.655  -1.487  39.511  1.00 80.27 ? 227  GLY B C   1 
ATOM   5547 O  O   . GLY B 1 228 ? 19.272  -0.537  40.004  1.00 80.58 ? 227  GLY B O   1 
ATOM   5548 N  N   . GLU B 1 229 ? 17.337  -1.626  39.638  1.00 80.64 ? 228  GLU B N   1 
ATOM   5549 C  CA  . GLU B 1 229 ? 16.561  -0.773  40.526  1.00 81.68 ? 228  GLU B CA  1 
ATOM   5550 C  C   . GLU B 1 229 ? 16.985  -0.999  41.972  1.00 81.97 ? 228  GLU B C   1 
ATOM   5551 O  O   . GLU B 1 229 ? 17.090  -2.141  42.431  1.00 83.31 ? 228  GLU B O   1 
ATOM   5552 C  CB  . GLU B 1 229 ? 15.070  -1.069  40.348  1.00 82.22 ? 228  GLU B CB  1 
ATOM   5553 C  CG  . GLU B 1 229 ? 14.193  -0.735  41.546  1.00 82.96 ? 228  GLU B CG  1 
ATOM   5554 C  CD  . GLU B 1 229 ? 12.775  -1.264  41.391  1.00 84.01 ? 228  GLU B CD  1 
ATOM   5555 O  OE1 . GLU B 1 229 ? 12.550  -2.120  40.508  1.00 84.24 ? 228  GLU B OE1 1 
ATOM   5556 O  OE2 . GLU B 1 229 ? 11.884  -0.826  42.150  1.00 84.10 ? 228  GLU B OE2 1 
ATOM   5557 N  N   . GLN B 1 230 ? 17.239  0.092   42.689  1.00 79.57 ? 229  GLN B N   1 
ATOM   5558 C  CA  . GLN B 1 230 ? 17.606  0.010   44.095  1.00 76.75 ? 229  GLN B CA  1 
ATOM   5559 C  C   . GLN B 1 230 ? 16.356  0.061   44.965  1.00 72.61 ? 229  GLN B C   1 
ATOM   5560 O  O   . GLN B 1 230 ? 15.421  0.818   44.689  1.00 73.03 ? 229  GLN B O   1 
ATOM   5561 C  CB  . GLN B 1 230 ? 18.563  1.142   44.475  1.00 77.09 ? 229  GLN B CB  1 
ATOM   5562 C  CG  . GLN B 1 230 ? 17.964  2.536   44.382  1.00 77.69 ? 229  GLN B CG  1 
ATOM   5563 C  CD  . GLN B 1 230 ? 18.936  3.615   44.825  1.00 78.30 ? 229  GLN B CD  1 
ATOM   5564 O  OE1 . GLN B 1 230 ? 20.095  3.632   44.409  1.00 78.60 ? 229  GLN B OE1 1 
ATOM   5565 N  NE2 . GLN B 1 230 ? 18.470  4.518   45.683  1.00 78.18 ? 229  GLN B NE2 1 
ATOM   5566 N  N   . SER B 1 231 ? 16.343  -0.760  46.010  1.00 67.25 ? 230  SER B N   1 
ATOM   5567 C  CA  . SER B 1 231 ? 15.234  -0.827  46.950  1.00 61.44 ? 230  SER B CA  1 
ATOM   5568 C  C   . SER B 1 231 ? 15.730  -0.494  48.354  1.00 58.03 ? 230  SER B C   1 
ATOM   5569 O  O   . SER B 1 231 ? 16.934  -0.412  48.614  1.00 55.75 ? 230  SER B O   1 
ATOM   5570 C  CB  . SER B 1 231 ? 14.573  -2.213  46.927  1.00 58.05 ? 230  SER B CB  1 
ATOM   5571 O  OG  . SER B 1 231 ? 14.078  -2.532  45.636  1.00 53.38 ? 230  SER B OG  1 
ATOM   5572 N  N   . ASP B 1 232 ? 14.770  -0.286  49.272  1.00 52.88 ? 231  ASP B N   1 
ATOM   5573 C  CA  . ASP B 1 232 ? 15.068  -0.043  50.682  1.00 50.09 ? 231  ASP B CA  1 
ATOM   5574 C  C   . ASP B 1 232 ? 13.980  -0.727  51.518  1.00 43.38 ? 231  ASP B C   1 
ATOM   5575 O  O   . ASP B 1 232 ? 13.204  -0.097  52.232  1.00 47.65 ? 231  ASP B O   1 
ATOM   5576 C  CB  . ASP B 1 232 ? 15.160  1.453   50.994  1.00 55.11 ? 231  ASP B CB  1 
ATOM   5577 C  CG  . ASP B 1 232 ? 15.749  1.726   52.368  1.00 59.98 ? 231  ASP B CG  1 
ATOM   5578 O  OD1 . ASP B 1 232 ? 16.264  0.775   52.995  1.00 61.15 ? 231  ASP B OD1 1 
ATOM   5579 O  OD2 . ASP B 1 232 ? 15.694  2.889   52.825  1.00 61.95 ? 231  ASP B OD2 1 
ATOM   5580 N  N   . ASP B 1 233 ? 13.932  -2.056  51.435  1.00 31.66 ? 232  ASP B N   1 
ATOM   5581 C  CA  . ASP B 1 233 ? 12.881  -2.827  52.086  1.00 25.28 ? 232  ASP B CA  1 
ATOM   5582 C  C   . ASP B 1 233 ? 13.467  -3.884  53.015  1.00 22.94 ? 232  ASP B C   1 
ATOM   5583 O  O   . ASP B 1 233 ? 14.661  -3.848  53.335  1.00 23.64 ? 232  ASP B O   1 
ATOM   5584 C  CB  . ASP B 1 233 ? 11.988  -3.482  51.029  1.00 23.82 ? 232  ASP B CB  1 
ATOM   5585 C  CG  . ASP B 1 233 ? 12.784  -4.290  50.018  1.00 24.84 ? 232  ASP B CG  1 
ATOM   5586 O  OD1 . ASP B 1 233 ? 13.968  -4.574  50.281  1.00 27.54 ? 232  ASP B OD1 1 
ATOM   5587 O  OD2 . ASP B 1 233 ? 12.235  -4.632  48.952  1.00 25.01 ? 232  ASP B OD2 1 
ATOM   5588 N  N   . LEU B 1 234 ? 12.627  -4.825  53.455  1.00 22.38 ? 233  LEU B N   1 
ATOM   5589 C  CA  . LEU B 1 234 ? 13.080  -5.872  54.366  1.00 19.00 ? 233  LEU B CA  1 
ATOM   5590 C  C   . LEU B 1 234 ? 14.274  -6.636  53.793  1.00 19.02 ? 233  LEU B C   1 
ATOM   5591 O  O   . LEU B 1 234 ? 15.258  -6.902  54.498  1.00 19.75 ? 233  LEU B O   1 
ATOM   5592 C  CB  . LEU B 1 234 ? 11.915  -6.817  54.673  1.00 20.39 ? 233  LEU B CB  1 
ATOM   5593 C  CG  . LEU B 1 234 ? 12.131  -7.963  55.653  1.00 24.00 ? 233  LEU B CG  1 
ATOM   5594 C  CD1 . LEU B 1 234 ? 12.449  -7.443  57.052  1.00 25.48 ? 233  LEU B CD1 1 
ATOM   5595 C  CD2 . LEU B 1 234 ? 10.886  -8.845  55.669  1.00 24.38 ? 233  LEU B CD2 1 
ATOM   5596 N  N   . LEU B 1 235 ? 14.211  -6.991  52.506  1.00 18.59 ? 234  LEU B N   1 
ATOM   5597 C  CA  . LEU B 1 235 ? 15.316  -7.725  51.893  1.00 16.84 ? 234  LEU B CA  1 
ATOM   5598 C  C   . LEU B 1 235 ? 16.590  -6.882  51.860  1.00 17.27 ? 234  LEU B C   1 
ATOM   5599 O  O   . LEU B 1 235 ? 17.698  -7.405  52.046  1.00 18.72 ? 234  LEU B O   1 
ATOM   5600 C  CB  . LEU B 1 235 ? 14.922  -8.192  50.485  1.00 18.23 ? 234  LEU B CB  1 
ATOM   5601 C  CG  . LEU B 1 235 ? 15.921  -9.097  49.750  1.00 17.40 ? 234  LEU B CG  1 
ATOM   5602 C  CD1 . LEU B 1 235 ? 16.223  -10.348 50.572  1.00 22.20 ? 234  LEU B CD1 1 
ATOM   5603 C  CD2 . LEU B 1 235 ? 15.427  -9.475  48.339  1.00 18.34 ? 234  LEU B CD2 1 
ATOM   5604 N  N   . THR B 1 236 ? 16.455  -5.568  51.659  1.00 17.90 ? 235  THR B N   1 
ATOM   5605 C  CA  . THR B 1 236 ? 17.625  -4.695  51.693  1.00 19.25 ? 235  THR B CA  1 
ATOM   5606 C  C   . THR B 1 236 ? 18.349  -4.812  53.025  1.00 19.53 ? 235  THR B C   1 
ATOM   5607 O  O   . THR B 1 236 ? 19.579  -4.925  53.069  1.00 22.63 ? 235  THR B O   1 
ATOM   5608 C  CB  . THR B 1 236 ? 17.217  -3.241  51.452  1.00 19.12 ? 235  THR B CB  1 
ATOM   5609 O  OG1 . THR B 1 236 ? 16.552  -3.132  50.191  1.00 21.00 ? 235  THR B OG1 1 
ATOM   5610 C  CG2 . THR B 1 236 ? 18.455  -2.346  51.442  1.00 20.55 ? 235  THR B CG2 1 
ATOM   5611 N  N   . HIS B 1 237 ? 17.596  -4.763  54.127  1.00 20.54 ? 236  HIS B N   1 
ATOM   5612 C  CA  . HIS B 1 237 ? 18.213  -4.889  55.442  1.00 21.30 ? 236  HIS B CA  1 
ATOM   5613 C  C   . HIS B 1 237 ? 18.810  -6.279  55.642  1.00 23.15 ? 236  HIS B C   1 
ATOM   5614 O  O   . HIS B 1 237 ? 19.887  -6.415  56.232  1.00 22.73 ? 236  HIS B O   1 
ATOM   5615 C  CB  . HIS B 1 237 ? 17.191  -4.574  56.539  1.00 24.31 ? 236  HIS B CB  1 
ATOM   5616 C  CG  . HIS B 1 237 ? 16.816  -3.125  56.625  1.00 29.58 ? 236  HIS B CG  1 
ATOM   5617 N  ND1 . HIS B 1 237 ? 15.905  -2.537  55.774  1.00 31.81 ? 236  HIS B ND1 1 
ATOM   5618 C  CD2 . HIS B 1 237 ? 17.226  -2.148  57.469  1.00 35.87 ? 236  HIS B CD2 1 
ATOM   5619 C  CE1 . HIS B 1 237 ? 15.774  -1.260  56.086  1.00 33.57 ? 236  HIS B CE1 1 
ATOM   5620 N  NE2 . HIS B 1 237 ? 16.562  -0.999  57.114  1.00 37.65 ? 236  HIS B NE2 1 
ATOM   5621 N  N   . MET B 1 238 ? 18.128  -7.328  55.170  1.00 22.03 ? 237  MET B N   1 
ATOM   5622 C  CA  . MET B 1 238 ? 18.695  -8.671  55.285  1.00 21.78 ? 237  MET B CA  1 
ATOM   5623 C  C   . MET B 1 238 ? 20.066  -8.746  54.621  1.00 24.98 ? 237  MET B C   1 
ATOM   5624 O  O   . MET B 1 238 ? 21.011  -9.313  55.187  1.00 26.65 ? 237  MET B O   1 
ATOM   5625 C  CB  . MET B 1 238 ? 17.748  -9.705  54.665  1.00 20.01 ? 237  MET B CB  1 
ATOM   5626 C  CG  . MET B 1 238 ? 16.541  -10.110 55.525  1.00 20.58 ? 237  MET B CG  1 
ATOM   5627 S  SD  . MET B 1 238 ? 15.513  -11.303 54.623  1.00 22.03 ? 237  MET B SD  1 
ATOM   5628 C  CE  . MET B 1 238 ? 14.034  -11.329 55.652  1.00 19.98 ? 237  MET B CE  1 
ATOM   5629 N  N   . LEU B 1 239 ? 20.197  -8.157  53.426  1.00 25.32 ? 238  LEU B N   1 
ATOM   5630 C  CA  . LEU B 1 239 ? 21.415  -8.304  52.637  1.00 26.47 ? 238  LEU B CA  1 
ATOM   5631 C  C   . LEU B 1 239 ? 22.519  -7.345  53.065  1.00 27.19 ? 238  LEU B C   1 
ATOM   5632 O  O   . LEU B 1 239 ? 23.699  -7.658  52.883  1.00 29.63 ? 238  LEU B O   1 
ATOM   5633 C  CB  . LEU B 1 239 ? 21.109  -8.092  51.149  1.00 26.79 ? 238  LEU B CB  1 
ATOM   5634 C  CG  . LEU B 1 239 ? 20.147  -9.089  50.501  1.00 29.95 ? 238  LEU B CG  1 
ATOM   5635 C  CD1 . LEU B 1 239 ? 19.780  -8.657  49.084  1.00 28.86 ? 238  LEU B CD1 1 
ATOM   5636 C  CD2 . LEU B 1 239 ? 20.745  -10.490 50.496  1.00 32.76 ? 238  LEU B CD2 1 
ATOM   5637 N  N   . ASN B 1 240 ? 22.177  -6.186  53.628  1.00 29.22 ? 239  ASN B N   1 
ATOM   5638 C  CA  . ASN B 1 240 ? 23.156  -5.129  53.836  1.00 28.81 ? 239  ASN B CA  1 
ATOM   5639 C  C   . ASN B 1 240 ? 23.319  -4.668  55.277  1.00 25.99 ? 239  ASN B C   1 
ATOM   5640 O  O   . ASN B 1 240 ? 24.376  -4.117  55.603  1.00 27.00 ? 239  ASN B O   1 
ATOM   5641 C  CB  . ASN B 1 240 ? 22.800  -3.906  52.979  1.00 31.28 ? 239  ASN B CB  1 
ATOM   5642 C  CG  . ASN B 1 240 ? 22.750  -4.235  51.503  1.00 35.80 ? 239  ASN B CG  1 
ATOM   5643 O  OD1 . ASN B 1 240 ? 23.782  -4.321  50.846  1.00 36.82 ? 239  ASN B OD1 1 
ATOM   5644 N  ND2 . ASN B 1 240 ? 21.546  -4.433  50.977  1.00 36.57 ? 239  ASN B ND2 1 
ATOM   5645 N  N   . GLY B 1 241 ? 22.324  -4.864  56.139  1.00 24.31 ? 240  GLY B N   1 
ATOM   5646 C  CA  . GLY B 1 241 ? 22.396  -4.307  57.482  1.00 21.27 ? 240  GLY B CA  1 
ATOM   5647 C  C   . GLY B 1 241 ? 23.401  -5.020  58.368  1.00 20.87 ? 240  GLY B C   1 
ATOM   5648 O  O   . GLY B 1 241 ? 23.611  -6.229  58.268  1.00 21.54 ? 240  GLY B O   1 
ATOM   5649 N  N   . LYS B 1 242 ? 24.024  -4.248  59.265  1.00 18.96 ? 241  LYS B N   1 
ATOM   5650 C  CA  . LYS B 1 242 ? 24.983  -4.761  60.234  1.00 19.48 ? 241  LYS B CA  1 
ATOM   5651 C  C   . LYS B 1 242 ? 24.402  -4.691  61.637  1.00 17.81 ? 241  LYS B C   1 
ATOM   5652 O  O   . LYS B 1 242 ? 23.810  -3.677  62.025  1.00 21.64 ? 241  LYS B O   1 
ATOM   5653 C  CB  . LYS B 1 242 ? 26.291  -3.966  60.206  1.00 23.44 ? 241  LYS B CB  1 
ATOM   5654 C  CG  . LYS B 1 242 ? 26.917  -3.831  58.843  1.00 30.47 ? 241  LYS B CG  1 
ATOM   5655 C  CD  . LYS B 1 242 ? 27.612  -5.103  58.431  1.00 33.80 ? 241  LYS B CD  1 
ATOM   5656 C  CE  . LYS B 1 242 ? 28.404  -4.886  57.149  1.00 35.47 ? 241  LYS B CE  1 
ATOM   5657 N  NZ  . LYS B 1 242 ? 29.330  -3.728  57.271  1.00 38.09 ? 241  LYS B NZ  1 
ATOM   5658 N  N   . ASP B 1 243 ? 24.600  -5.762  62.395  1.00 15.71 ? 242  ASP B N   1 
ATOM   5659 C  CA  . ASP B 1 243 ? 24.210  -5.808  63.799  1.00 16.54 ? 242  ASP B CA  1 
ATOM   5660 C  C   . ASP B 1 243 ? 25.151  -4.922  64.605  1.00 17.58 ? 242  ASP B C   1 
ATOM   5661 O  O   . ASP B 1 243 ? 26.365  -5.158  64.589  1.00 16.63 ? 242  ASP B O   1 
ATOM   5662 C  CB  . ASP B 1 243 ? 24.268  -7.256  64.285  1.00 14.14 ? 242  ASP B CB  1 
ATOM   5663 C  CG  . ASP B 1 243 ? 24.219  -7.378  65.793  1.00 15.20 ? 242  ASP B CG  1 
ATOM   5664 O  OD1 . ASP B 1 243 ? 23.620  -6.505  66.455  1.00 15.14 ? 242  ASP B OD1 1 
ATOM   5665 O  OD2 . ASP B 1 243 ? 24.795  -8.359  66.308  1.00 14.87 ? 242  ASP B OD2 1 
ATOM   5666 N  N   . PRO B 1 244 ? 24.655  -3.899  65.304  1.00 16.96 ? 243  PRO B N   1 
ATOM   5667 C  CA  . PRO B 1 244 ? 25.569  -3.047  66.085  1.00 17.05 ? 243  PRO B CA  1 
ATOM   5668 C  C   . PRO B 1 244 ? 26.364  -3.803  67.134  1.00 15.79 ? 243  PRO B C   1 
ATOM   5669 O  O   . PRO B 1 244 ? 27.482  -3.378  67.471  1.00 18.26 ? 243  PRO B O   1 
ATOM   5670 C  CB  . PRO B 1 244 ? 24.628  -2.018  66.734  1.00 18.56 ? 243  PRO B CB  1 
ATOM   5671 C  CG  . PRO B 1 244 ? 23.378  -2.056  65.906  1.00 21.53 ? 243  PRO B CG  1 
ATOM   5672 C  CD  . PRO B 1 244 ? 23.255  -3.455  65.400  1.00 19.19 ? 243  PRO B CD  1 
ATOM   5673 N  N   . GLU B 1 245 ? 25.825  -4.895  67.677  1.00 16.90 ? 244  GLU B N   1 
ATOM   5674 C  CA  . GLU B 1 245 ? 26.510  -5.628  68.740  1.00 15.94 ? 244  GLU B CA  1 
ATOM   5675 C  C   . GLU B 1 245 ? 27.701  -6.412  68.195  1.00 16.98 ? 244  GLU B C   1 
ATOM   5676 O  O   . GLU B 1 245 ? 28.849  -6.115  68.540  1.00 18.59 ? 244  GLU B O   1 
ATOM   5677 C  CB  . GLU B 1 245 ? 25.547  -6.573  69.472  1.00 17.92 ? 244  GLU B CB  1 
ATOM   5678 C  CG  . GLU B 1 245 ? 26.254  -7.381  70.563  1.00 24.53 ? 244  GLU B CG  1 
ATOM   5679 C  CD  . GLU B 1 245 ? 25.340  -8.265  71.390  1.00 28.71 ? 244  GLU B CD  1 
ATOM   5680 O  OE1 . GLU B 1 245 ? 24.203  -8.560  70.962  1.00 25.47 ? 244  GLU B OE1 1 
ATOM   5681 O  OE2 . GLU B 1 245 ? 25.776  -8.680  72.486  1.00 35.45 ? 244  GLU B OE2 1 
ATOM   5682 N  N   . THR B 1 246 ? 27.444  -7.419  67.351  1.00 15.87 ? 245  THR B N   1 
ATOM   5683 C  CA  . THR B 1 246 ? 28.539  -8.189  66.761  1.00 17.02 ? 245  THR B CA  1 
ATOM   5684 C  C   . THR B 1 246 ? 29.281  -7.417  65.676  1.00 16.55 ? 245  THR B C   1 
ATOM   5685 O  O   . THR B 1 246 ? 30.437  -7.749  65.381  1.00 17.65 ? 245  THR B O   1 
ATOM   5686 C  CB  . THR B 1 246 ? 28.026  -9.503  66.155  1.00 17.08 ? 245  THR B CB  1 
ATOM   5687 O  OG1 . THR B 1 246 ? 27.125  -9.218  65.072  1.00 17.57 ? 245  THR B OG1 1 
ATOM   5688 C  CG2 . THR B 1 246 ? 27.317  -10.375 67.214  1.00 17.03 ? 245  THR B CG2 1 
ATOM   5689 N  N   . GLY B 1 247 ? 28.646  -6.407  65.076  1.00 16.14 ? 246  GLY B N   1 
ATOM   5690 C  CA  . GLY B 1 247 ? 29.172  -5.725  63.907  1.00 16.63 ? 246  GLY B CA  1 
ATOM   5691 C  C   . GLY B 1 247 ? 29.012  -6.478  62.601  1.00 16.67 ? 246  GLY B C   1 
ATOM   5692 O  O   . GLY B 1 247 ? 29.486  -5.993  61.563  1.00 16.78 ? 246  GLY B O   1 
ATOM   5693 N  N   . GLU B 1 248 ? 28.344  -7.672  62.612  1.00 16.68 ? 247  GLU B N   1 
ATOM   5694 C  CA  . GLU B 1 248 ? 28.241  -8.567  61.461  1.00 15.26 ? 247  GLU B CA  1 
ATOM   5695 C  C   . GLU B 1 248 ? 26.910  -8.410  60.732  1.00 16.42 ? 247  GLU B C   1 
ATOM   5696 O  O   . GLU B 1 248 ? 25.889  -8.084  61.346  1.00 16.13 ? 247  GLU B O   1 
ATOM   5697 C  CB  . GLU B 1 248 ? 28.371  -10.027 61.899  1.00 15.38 ? 247  GLU B CB  1 
ATOM   5698 C  CG  . GLU B 1 248 ? 29.627  -10.347 62.673  1.00 16.37 ? 247  GLU B CG  1 
ATOM   5699 C  CD  . GLU B 1 248 ? 29.527  -11.686 63.383  1.00 17.16 ? 247  GLU B CD  1 
ATOM   5700 O  OE1 . GLU B 1 248 ? 28.570  -12.442 63.098  1.00 19.73 ? 247  GLU B OE1 1 
ATOM   5701 O  OE2 . GLU B 1 248 ? 30.396  -11.978 64.235  1.00 18.49 ? 247  GLU B OE2 1 
ATOM   5702 N  N   . PRO B 1 249 ? 26.908  -8.652  59.424  1.00 17.32 ? 248  PRO B N   1 
ATOM   5703 C  CA  . PRO B 1 249 ? 25.658  -8.857  58.692  1.00 17.82 ? 248  PRO B CA  1 
ATOM   5704 C  C   . PRO B 1 249 ? 25.246  -10.325 58.777  1.00 16.46 ? 248  PRO B C   1 
ATOM   5705 O  O   . PRO B 1 249 ? 26.015  -11.186 59.201  1.00 19.04 ? 248  PRO B O   1 
ATOM   5706 C  CB  . PRO B 1 249 ? 26.043  -8.474  57.255  1.00 18.56 ? 248  PRO B CB  1 
ATOM   5707 C  CG  . PRO B 1 249 ? 27.459  -8.949  57.148  1.00 20.44 ? 248  PRO B CG  1 
ATOM   5708 C  CD  . PRO B 1 249 ? 28.081  -8.713  58.532  1.00 20.77 ? 248  PRO B CD  1 
ATOM   5709 N  N   . LEU B 1 250 ? 24.003  -10.598 58.370  1.00 16.37 ? 249  LEU B N   1 
ATOM   5710 C  CA  . LEU B 1 250 ? 23.553  -11.983 58.288  1.00 16.54 ? 249  LEU B CA  1 
ATOM   5711 C  C   . LEU B 1 250 ? 24.323  -12.735 57.204  1.00 16.53 ? 249  LEU B C   1 
ATOM   5712 O  O   . LEU B 1 250 ? 24.717  -12.161 56.191  1.00 18.37 ? 249  LEU B O   1 
ATOM   5713 C  CB  . LEU B 1 250 ? 22.059  -12.045 57.988  1.00 18.41 ? 249  LEU B CB  1 
ATOM   5714 C  CG  . LEU B 1 250 ? 21.107  -11.413 59.011  1.00 17.87 ? 249  LEU B CG  1 
ATOM   5715 C  CD1 . LEU B 1 250 ? 19.670  -11.610 58.537  1.00 19.02 ? 249  LEU B CD1 1 
ATOM   5716 C  CD2 . LEU B 1 250 ? 21.306  -12.015 60.395  1.00 19.33 ? 249  LEU B CD2 1 
ATOM   5717 N  N   . ASP B 1 251 ? 24.537  -14.035 57.416  1.00 18.82 ? 250  ASP B N   1 
ATOM   5718 C  CA  . ASP B 1 251 ? 25.142  -14.846 56.364  1.00 21.76 ? 250  ASP B CA  1 
ATOM   5719 C  C   . ASP B 1 251 ? 24.067  -15.424 55.440  1.00 22.39 ? 250  ASP B C   1 
ATOM   5720 O  O   . ASP B 1 251 ? 22.865  -15.354 55.715  1.00 19.39 ? 250  ASP B O   1 
ATOM   5721 C  CB  . ASP B 1 251 ? 26.019  -15.964 56.944  1.00 24.22 ? 250  ASP B CB  1 
ATOM   5722 C  CG  . ASP B 1 251 ? 25.281  -16.849 57.925  1.00 30.44 ? 250  ASP B CG  1 
ATOM   5723 O  OD1 . ASP B 1 251 ? 24.395  -17.617 57.496  1.00 27.63 ? 250  ASP B OD1 1 
ATOM   5724 O  OD2 . ASP B 1 251 ? 25.599  -16.785 59.133  1.00 38.29 ? 250  ASP B OD2 1 
ATOM   5725 N  N   . ASP B 1 252 ? 24.524  -15.997 54.318  1.00 22.70 ? 251  ASP B N   1 
ATOM   5726 C  CA  . ASP B 1 252 ? 23.597  -16.415 53.268  1.00 23.80 ? 251  ASP B CA  1 
ATOM   5727 C  C   . ASP B 1 252 ? 22.629  -17.483 53.761  1.00 20.72 ? 251  ASP B C   1 
ATOM   5728 O  O   . ASP B 1 252 ? 21.441  -17.459 53.419  1.00 21.25 ? 251  ASP B O   1 
ATOM   5729 C  CB  . ASP B 1 252 ? 24.371  -16.918 52.047  1.00 27.64 ? 251  ASP B CB  1 
ATOM   5730 C  CG  . ASP B 1 252 ? 24.971  -15.787 51.234  1.00 34.70 ? 251  ASP B CG  1 
ATOM   5731 O  OD1 . ASP B 1 252 ? 24.491  -14.641 51.368  1.00 37.32 ? 251  ASP B OD1 1 
ATOM   5732 O  OD2 . ASP B 1 252 ? 25.913  -16.041 50.454  1.00 37.75 ? 251  ASP B OD2 1 
ATOM   5733 N  N   . GLU B 1 253 ? 23.115  -18.433 54.559  1.00 23.41 ? 252  GLU B N   1 
ATOM   5734 C  CA  . GLU B 1 253 ? 22.236  -19.493 55.038  1.00 23.46 ? 252  GLU B CA  1 
ATOM   5735 C  C   . GLU B 1 253 ? 21.117  -18.920 55.901  1.00 20.48 ? 252  GLU B C   1 
ATOM   5736 O  O   . GLU B 1 253 ? 19.940  -19.259 55.723  1.00 18.88 ? 252  GLU B O   1 
ATOM   5737 C  CB  . GLU B 1 253 ? 23.046  -20.536 55.809  1.00 28.79 ? 252  GLU B CB  1 
ATOM   5738 C  CG  . GLU B 1 253 ? 22.221  -21.685 56.353  1.00 33.61 ? 252  GLU B CG  1 
ATOM   5739 C  CD  . GLU B 1 253 ? 23.009  -22.550 57.311  1.00 40.03 ? 252  GLU B CD  1 
ATOM   5740 O  OE1 . GLU B 1 253 ? 24.166  -22.889 56.984  1.00 44.51 ? 252  GLU B OE1 1 
ATOM   5741 O  OE2 . GLU B 1 253 ? 22.481  -22.878 58.396  1.00 40.95 ? 252  GLU B OE2 1 
ATOM   5742 N  N   . ASN B 1 254 ? 21.463  -18.033 56.840  1.00 16.81 ? 253  ASN B N   1 
ATOM   5743 C  CA  . ASN B 1 254 ? 20.430  -17.469 57.703  1.00 15.19 ? 253  ASN B CA  1 
ATOM   5744 C  C   . ASN B 1 254 ? 19.473  -16.574 56.921  1.00 14.48 ? 253  ASN B C   1 
ATOM   5745 O  O   . ASN B 1 254 ? 18.275  -16.529 57.230  1.00 14.70 ? 253  ASN B O   1 
ATOM   5746 C  CB  . ASN B 1 254 ? 21.061  -16.696 58.863  1.00 13.80 ? 253  ASN B CB  1 
ATOM   5747 C  CG  . ASN B 1 254 ? 20.027  -16.234 59.876  1.00 14.78 ? 253  ASN B CG  1 
ATOM   5748 O  OD1 . ASN B 1 254 ? 19.689  -15.049 59.951  1.00 14.77 ? 253  ASN B OD1 1 
ATOM   5749 N  ND2 . ASN B 1 254 ? 19.485  -17.177 60.628  1.00 12.80 ? 253  ASN B ND2 1 
ATOM   5750 N  N   . ILE B 1 255 ? 19.967  -15.862 55.905  1.00 16.11 ? 254  ILE B N   1 
ATOM   5751 C  CA  . ILE B 1 255 ? 19.074  -15.052 55.080  1.00 17.20 ? 254  ILE B CA  1 
ATOM   5752 C  C   . ILE B 1 255 ? 17.984  -15.920 54.454  1.00 18.77 ? 254  ILE B C   1 
ATOM   5753 O  O   . ILE B 1 255 ? 16.803  -15.545 54.442  1.00 18.47 ? 254  ILE B O   1 
ATOM   5754 C  CB  . ILE B 1 255 ? 19.877  -14.290 54.007  1.00 18.20 ? 254  ILE B CB  1 
ATOM   5755 C  CG1 . ILE B 1 255 ? 20.695  -13.158 54.645  1.00 19.01 ? 254  ILE B CG1 1 
ATOM   5756 C  CG2 . ILE B 1 255 ? 18.937  -13.759 52.913  1.00 19.34 ? 254  ILE B CG2 1 
ATOM   5757 C  CD1 . ILE B 1 255 ? 21.778  -12.602 53.737  1.00 20.54 ? 254  ILE B CD1 1 
ATOM   5758 N  N   . ARG B 1 256 ? 18.354  -17.089 53.917  1.00 16.83 ? 255  ARG B N   1 
ATOM   5759 C  CA  . ARG B 1 256 ? 17.342  -17.953 53.303  1.00 15.76 ? 255  ARG B CA  1 
ATOM   5760 C  C   . ARG B 1 256 ? 16.273  -18.345 54.317  1.00 11.64 ? 255  ARG B C   1 
ATOM   5761 O  O   . ARG B 1 256 ? 15.077  -18.374 53.998  1.00 14.31 ? 255  ARG B O   1 
ATOM   5762 C  CB  . ARG B 1 256 ? 17.987  -19.203 52.707  1.00 18.26 ? 255  ARG B CB  1 
ATOM   5763 C  CG  . ARG B 1 256 ? 18.971  -18.928 51.578  1.00 24.49 ? 255  ARG B CG  1 
ATOM   5764 C  CD  . ARG B 1 256 ? 19.470  -20.229 50.953  1.00 31.35 ? 255  ARG B CD  1 
ATOM   5765 N  NE  . ARG B 1 256 ? 18.371  -21.038 50.437  1.00 36.27 ? 255  ARG B NE  1 
ATOM   5766 C  CZ  . ARG B 1 256 ? 17.926  -20.999 49.187  1.00 38.61 ? 255  ARG B CZ  1 
ATOM   5767 N  NH1 . ARG B 1 256 ? 18.490  -20.221 48.273  1.00 38.36 ? 255  ARG B NH1 1 
ATOM   5768 N  NH2 . ARG B 1 256 ? 16.891  -21.762 48.844  1.00 35.37 ? 255  ARG B NH2 1 
ATOM   5769 N  N   . TYR B 1 257 ? 16.681  -18.639 55.549  1.00 13.64 ? 256  TYR B N   1 
ATOM   5770 C  CA  . TYR B 1 257 ? 15.712  -18.996 56.580  1.00 13.92 ? 256  TYR B CA  1 
ATOM   5771 C  C   . TYR B 1 257 ? 14.825  -17.812 56.952  1.00 14.72 ? 256  TYR B C   1 
ATOM   5772 O  O   . TYR B 1 257 ? 13.641  -17.996 57.267  1.00 13.44 ? 256  TYR B O   1 
ATOM   5773 C  CB  . TYR B 1 257 ? 16.436  -19.516 57.818  1.00 15.21 ? 256  TYR B CB  1 
ATOM   5774 C  CG  . TYR B 1 257 ? 17.014  -20.911 57.707  1.00 16.20 ? 256  TYR B CG  1 
ATOM   5775 C  CD1 . TYR B 1 257 ? 16.297  -21.957 57.124  1.00 18.46 ? 256  TYR B CD1 1 
ATOM   5776 C  CD2 . TYR B 1 257 ? 18.282  -21.188 58.208  1.00 17.41 ? 256  TYR B CD2 1 
ATOM   5777 C  CE1 . TYR B 1 257 ? 16.837  -23.239 57.052  1.00 19.02 ? 256  TYR B CE1 1 
ATOM   5778 C  CE2 . TYR B 1 257 ? 18.824  -22.454 58.134  1.00 19.90 ? 256  TYR B CE2 1 
ATOM   5779 C  CZ  . TYR B 1 257 ? 18.106  -23.475 57.559  1.00 20.45 ? 256  TYR B CZ  1 
ATOM   5780 O  OH  . TYR B 1 257 ? 18.679  -24.730 57.501  1.00 23.63 ? 256  TYR B OH  1 
ATOM   5781 N  N   . GLN B 1 258 ? 15.382  -16.593 56.968  1.00 15.82 ? 257  GLN B N   1 
ATOM   5782 C  CA  . GLN B 1 258 ? 14.549  -15.435 57.283  1.00 15.15 ? 257  GLN B CA  1 
ATOM   5783 C  C   . GLN B 1 258 ? 13.512  -15.198 56.195  1.00 13.45 ? 257  GLN B C   1 
ATOM   5784 O  O   . GLN B 1 258 ? 12.369  -14.830 56.492  1.00 13.16 ? 257  GLN B O   1 
ATOM   5785 C  CB  . GLN B 1 258 ? 15.388  -14.166 57.486  1.00 14.53 ? 257  GLN B CB  1 
ATOM   5786 C  CG  . GLN B 1 258 ? 16.476  -14.231 58.567  1.00 13.08 ? 257  GLN B CG  1 
ATOM   5787 C  CD  . GLN B 1 258 ? 15.959  -14.454 59.991  1.00 13.88 ? 257  GLN B CD  1 
ATOM   5788 O  OE1 . GLN B 1 258 ? 14.747  -14.446 60.258  1.00 13.10 ? 257  GLN B OE1 1 
ATOM   5789 N  NE2 . GLN B 1 258 ? 16.895  -14.655 60.917  1.00 13.28 ? 257  GLN B NE2 1 
ATOM   5790 N  N   . ILE B 1 259 ? 13.885  -15.391 54.927  1.00 13.92 ? 258  ILE B N   1 
ATOM   5791 C  CA  . ILE B 1 259 ? 12.918  -15.174 53.852  1.00 13.69 ? 258  ILE B CA  1 
ATOM   5792 C  C   . ILE B 1 259 ? 11.756  -16.154 53.984  1.00 13.49 ? 258  ILE B C   1 
ATOM   5793 O  O   . ILE B 1 259 ? 10.580  -15.767 53.916  1.00 14.50 ? 258  ILE B O   1 
ATOM   5794 C  CB  . ILE B 1 259 ? 13.603  -15.279 52.478  1.00 14.12 ? 258  ILE B CB  1 
ATOM   5795 C  CG1 . ILE B 1 259 ? 14.641  -14.164 52.333  1.00 16.52 ? 258  ILE B CG1 1 
ATOM   5796 C  CG2 . ILE B 1 259 ? 12.551  -15.178 51.347  1.00 16.19 ? 258  ILE B CG2 1 
ATOM   5797 C  CD1 . ILE B 1 259 ? 15.466  -14.235 51.061  1.00 19.70 ? 258  ILE B CD1 1 
ATOM   5798 N  N   . ILE B 1 260 ? 12.066  -17.437 54.196  1.00 14.29 ? 259  ILE B N   1 
ATOM   5799 C  CA  . ILE B 1 260 ? 11.009  -18.422 54.425  1.00 13.33 ? 259  ILE B CA  1 
ATOM   5800 C  C   . ILE B 1 260 ? 10.150  -18.002 55.613  1.00 13.58 ? 259  ILE B C   1 
ATOM   5801 O  O   . ILE B 1 260 ? 8.911   -18.035 55.556  1.00 11.76 ? 259  ILE B O   1 
ATOM   5802 C  CB  . ILE B 1 260 ? 11.617  -19.824 54.632  1.00 15.25 ? 259  ILE B CB  1 
ATOM   5803 C  CG1 . ILE B 1 260 ? 12.327  -20.292 53.356  1.00 19.71 ? 259  ILE B CG1 1 
ATOM   5804 C  CG2 . ILE B 1 260 ? 10.550  -20.832 55.054  1.00 17.01 ? 259  ILE B CG2 1 
ATOM   5805 C  CD1 . ILE B 1 260 ? 13.170  -21.524 53.548  1.00 25.14 ? 259  ILE B CD1 1 
ATOM   5806 N  N   . THR B 1 261 ? 10.800  -17.592 56.707  1.00 11.25 ? 260  THR B N   1 
ATOM   5807 C  CA  . THR B 1 261 ? 10.076  -17.219 57.921  1.00 12.27 ? 260  THR B CA  1 
ATOM   5808 C  C   . THR B 1 261 ? 9.102   -16.078 57.654  1.00 12.18 ? 260  THR B C   1 
ATOM   5809 O  O   . THR B 1 261 ? 7.927   -16.142 58.037  1.00 11.92 ? 260  THR B O   1 
ATOM   5810 C  CB  . THR B 1 261 ? 11.073  -16.829 59.019  1.00 11.89 ? 260  THR B CB  1 
ATOM   5811 O  OG1 . THR B 1 261 ? 11.922  -17.946 59.330  1.00 13.42 ? 260  THR B OG1 1 
ATOM   5812 C  CG2 . THR B 1 261 ? 10.350  -16.368 60.289  1.00 13.04 ? 260  THR B CG2 1 
ATOM   5813 N  N   . PHE B 1 262 ? 9.575   -15.014 56.996  1.00 13.51 ? 261  PHE B N   1 
ATOM   5814 C  CA  . PHE B 1 262 ? 8.707   -13.861 56.784  1.00 13.60 ? 261  PHE B CA  1 
ATOM   5815 C  C   . PHE B 1 262 ? 7.637   -14.126 55.731  1.00 14.73 ? 261  PHE B C   1 
ATOM   5816 O  O   . PHE B 1 262 ? 6.544   -13.556 55.821  1.00 15.31 ? 261  PHE B O   1 
ATOM   5817 C  CB  . PHE B 1 262 ? 9.545   -12.629 56.434  1.00 13.36 ? 261  PHE B CB  1 
ATOM   5818 C  CG  . PHE B 1 262 ? 10.162  -11.981 57.643  1.00 15.15 ? 261  PHE B CG  1 
ATOM   5819 C  CD1 . PHE B 1 262 ? 11.398  -12.394 58.118  1.00 18.38 ? 261  PHE B CD1 1 
ATOM   5820 C  CD2 . PHE B 1 262 ? 9.473   -10.997 58.335  1.00 16.71 ? 261  PHE B CD2 1 
ATOM   5821 C  CE1 . PHE B 1 262 ? 11.946  -11.822 59.251  1.00 17.53 ? 261  PHE B CE1 1 
ATOM   5822 C  CE2 . PHE B 1 262 ? 10.012  -10.415 59.468  1.00 15.82 ? 261  PHE B CE2 1 
ATOM   5823 C  CZ  . PHE B 1 262 ? 11.258  -10.822 59.928  1.00 16.40 ? 261  PHE B CZ  1 
ATOM   5824 N  N   . LEU B 1 263 ? 7.908   -14.987 54.741  1.00 14.01 ? 262  LEU B N   1 
ATOM   5825 C  CA  . LEU B 1 263 ? 6.856   -15.303 53.778  1.00 15.48 ? 262  LEU B CA  1 
ATOM   5826 C  C   . LEU B 1 263 ? 5.705   -16.038 54.445  1.00 17.30 ? 262  LEU B C   1 
ATOM   5827 O  O   . LEU B 1 263 ? 4.543   -15.834 54.068  1.00 17.80 ? 262  LEU B O   1 
ATOM   5828 C  CB  . LEU B 1 263 ? 7.407   -16.128 52.612  1.00 13.97 ? 262  LEU B CB  1 
ATOM   5829 C  CG  . LEU B 1 263 ? 8.305   -15.355 51.642  1.00 14.10 ? 262  LEU B CG  1 
ATOM   5830 C  CD1 . LEU B 1 263 ? 8.876   -16.272 50.569  1.00 14.68 ? 262  LEU B CD1 1 
ATOM   5831 C  CD2 . LEU B 1 263 ? 7.535   -14.194 51.001  1.00 15.73 ? 262  LEU B CD2 1 
ATOM   5832 N  N   . ILE B 1 264 ? 6.002   -16.869 55.447  1.00 14.88 ? 263  ILE B N   1 
ATOM   5833 C  CA  . ILE B 1 264 ? 4.985   -17.645 56.150  1.00 14.97 ? 263  ILE B CA  1 
ATOM   5834 C  C   . ILE B 1 264 ? 4.359   -16.822 57.267  1.00 15.29 ? 263  ILE B C   1 
ATOM   5835 O  O   . ILE B 1 264 ? 3.154   -16.546 57.251  1.00 17.18 ? 263  ILE B O   1 
ATOM   5836 C  CB  . ILE B 1 264 ? 5.581   -18.957 56.692  1.00 15.99 ? 263  ILE B CB  1 
ATOM   5837 C  CG1 . ILE B 1 264 ? 6.055   -19.831 55.517  1.00 16.77 ? 263  ILE B CG1 1 
ATOM   5838 C  CG2 . ILE B 1 264 ? 4.567   -19.682 57.596  1.00 17.65 ? 263  ILE B CG2 1 
ATOM   5839 C  CD1 . ILE B 1 264 ? 6.792   -21.092 55.932  1.00 18.41 ? 263  ILE B CD1 1 
ATOM   5840 N  N   . ALA B 1 265 ? 5.168   -16.426 58.249  1.00 13.44 ? 264  ALA B N   1 
ATOM   5841 C  CA  . ALA B 1 265 ? 4.621   -15.673 59.369  1.00 16.25 ? 264  ALA B CA  1 
ATOM   5842 C  C   . ALA B 1 265 ? 4.116   -14.304 58.942  1.00 14.95 ? 264  ALA B C   1 
ATOM   5843 O  O   . ALA B 1 265 ? 3.233   -13.747 59.610  1.00 17.57 ? 264  ALA B O   1 
ATOM   5844 C  CB  . ALA B 1 265 ? 5.668   -15.533 60.480  1.00 16.50 ? 264  ALA B CB  1 
ATOM   5845 N  N   . GLY B 1 266 ? 4.627   -13.763 57.838  1.00 14.37 ? 265  GLY B N   1 
ATOM   5846 C  CA  . GLY B 1 266 ? 4.217   -12.457 57.365  1.00 16.05 ? 265  GLY B CA  1 
ATOM   5847 C  C   . GLY B 1 266 ? 2.933   -12.399 56.565  1.00 14.24 ? 265  GLY B C   1 
ATOM   5848 O  O   . GLY B 1 266 ? 2.561   -11.307 56.125  1.00 15.44 ? 265  GLY B O   1 
ATOM   5849 N  N   . HIS B 1 267 ? 2.238   -13.524 56.350  1.00 14.55 ? 266  HIS B N   1 
ATOM   5850 C  CA  . HIS B 1 267 ? 0.937   -13.480 55.675  1.00 14.69 ? 266  HIS B CA  1 
ATOM   5851 C  C   . HIS B 1 267 ? -0.120  -14.408 56.261  1.00 15.88 ? 266  HIS B C   1 
ATOM   5852 O  O   . HIS B 1 267 ? -1.308  -14.065 56.209  1.00 16.34 ? 266  HIS B O   1 
ATOM   5853 C  CB  . HIS B 1 267 ? 1.085   -13.805 54.180  1.00 15.26 ? 266  HIS B CB  1 
ATOM   5854 C  CG  . HIS B 1 267 ? 0.854   -15.250 53.849  1.00 18.11 ? 266  HIS B CG  1 
ATOM   5855 N  ND1 . HIS B 1 267 ? 1.858   -16.193 53.887  1.00 18.28 ? 266  HIS B ND1 1 
ATOM   5856 C  CD2 . HIS B 1 267 ? -0.270  -15.913 53.483  1.00 15.23 ? 266  HIS B CD2 1 
ATOM   5857 C  CE1 . HIS B 1 267 ? 1.365   -17.373 53.552  1.00 14.70 ? 266  HIS B CE1 1 
ATOM   5858 N  NE2 . HIS B 1 267 ? 0.076   -17.231 53.303  1.00 16.91 ? 266  HIS B NE2 1 
ATOM   5859 N  N   . GLU B 1 268 ? 0.252   -15.569 56.800  1.00 15.32 ? 267  GLU B N   1 
ATOM   5860 C  CA  . GLU B 1 268 ? -0.742  -16.591 57.115  1.00 15.58 ? 267  GLU B CA  1 
ATOM   5861 C  C   . GLU B 1 268 ? -1.655  -16.144 58.247  1.00 14.85 ? 267  GLU B C   1 
ATOM   5862 O  O   . GLU B 1 268 ? -2.882  -16.265 58.156  1.00 16.33 ? 267  GLU B O   1 
ATOM   5863 C  CB  . GLU B 1 268 ? -0.043  -17.904 57.465  1.00 16.74 ? 267  GLU B CB  1 
ATOM   5864 C  CG  . GLU B 1 268 ? -0.873  -18.828 58.328  1.00 17.29 ? 267  GLU B CG  1 
ATOM   5865 C  CD  . GLU B 1 268 ? -2.060  -19.431 57.589  1.00 23.34 ? 267  GLU B CD  1 
ATOM   5866 O  OE1 . GLU B 1 268 ? -2.016  -19.525 56.340  1.00 23.80 ? 267  GLU B OE1 1 
ATOM   5867 O  OE2 . GLU B 1 268 ? -3.040  -19.817 58.268  1.00 28.02 ? 267  GLU B OE2 1 
ATOM   5868 N  N   . THR B 1 269 ? -1.075  -15.626 59.326  1.00 11.16 ? 268  THR B N   1 
ATOM   5869 C  CA  . THR B 1 269 ? -1.891  -15.215 60.462  1.00 9.63  ? 268  THR B CA  1 
ATOM   5870 C  C   . THR B 1 269 ? -2.718  -13.973 60.156  1.00 11.11 ? 268  THR B C   1 
ATOM   5871 O  O   . THR B 1 269 ? -3.803  -13.802 60.728  1.00 13.70 ? 268  THR B O   1 
ATOM   5872 C  CB  . THR B 1 269 ? -0.994  -14.974 61.675  1.00 12.75 ? 268  THR B CB  1 
ATOM   5873 O  OG1 . THR B 1 269 ? 0.154   -14.220 61.269  1.00 13.93 ? 268  THR B OG1 1 
ATOM   5874 C  CG2 . THR B 1 269 ? -0.542  -16.314 62.289  1.00 14.34 ? 268  THR B CG2 1 
ATOM   5875 N  N   . THR B 1 270 ? -2.225  -13.085 59.277  1.00 10.81 ? 269  THR B N   1 
ATOM   5876 C  CA  . THR B 1 270 ? -2.998  -11.899 58.920  1.00 11.20 ? 269  THR B CA  1 
ATOM   5877 C  C   . THR B 1 270 ? -4.188  -12.272 58.042  1.00 11.38 ? 269  THR B C   1 
ATOM   5878 O  O   . THR B 1 270 ? -5.267  -11.672 58.150  1.00 11.68 ? 269  THR B O   1 
ATOM   5879 C  CB  . THR B 1 270 ? -2.110  -10.871 58.206  1.00 12.13 ? 269  THR B CB  1 
ATOM   5880 O  OG1 . THR B 1 270 ? -0.979  -10.538 59.026  1.00 13.21 ? 269  THR B OG1 1 
ATOM   5881 C  CG2 . THR B 1 270 ? -2.896  -9.591  57.905  1.00 14.41 ? 269  THR B CG2 1 
ATOM   5882 N  N   . SER B 1 271 ? -4.009  -13.251 57.152  1.00 13.01 ? 270  SER B N   1 
ATOM   5883 C  CA  . SER B 1 271 ? -5.152  -13.741 56.392  1.00 11.22 ? 270  SER B CA  1 
ATOM   5884 C  C   . SER B 1 271 ? -6.206  -14.329 57.323  1.00 9.09  ? 270  SER B C   1 
ATOM   5885 O  O   . SER B 1 271 ? -7.411  -14.115 57.129  1.00 11.12 ? 270  SER B O   1 
ATOM   5886 C  CB  . SER B 1 271 ? -4.695  -14.786 55.371  1.00 15.18 ? 270  SER B CB  1 
ATOM   5887 O  OG  . SER B 1 271 ? -5.799  -15.550 54.926  1.00 22.52 ? 270  SER B OG  1 
ATOM   5888 N  N   . GLY B 1 272 ? -5.769  -15.084 58.338  1.00 10.22 ? 271  GLY B N   1 
ATOM   5889 C  CA  . GLY B 1 272 ? -6.708  -15.572 59.333  1.00 10.31 ? 271  GLY B CA  1 
ATOM   5890 C  C   . GLY B 1 272 ? -7.444  -14.453 60.052  1.00 11.34 ? 271  GLY B C   1 
ATOM   5891 O  O   . GLY B 1 272 ? -8.661  -14.519 60.245  1.00 12.28 ? 271  GLY B O   1 
ATOM   5892 N  N   . LEU B 1 273 ? -6.718  -13.414 60.465  1.00 10.02 ? 272  LEU B N   1 
ATOM   5893 C  CA  . LEU B 1 273 ? -7.355  -12.303 61.171  1.00 10.88 ? 272  LEU B CA  1 
ATOM   5894 C  C   . LEU B 1 273 ? -8.425  -11.637 60.310  1.00 11.45 ? 272  LEU B C   1 
ATOM   5895 O  O   . LEU B 1 273 ? -9.548  -11.389 60.768  1.00 11.98 ? 272  LEU B O   1 
ATOM   5896 C  CB  . LEU B 1 273 ? -6.298  -11.290 61.605  1.00 12.48 ? 272  LEU B CB  1 
ATOM   5897 C  CG  . LEU B 1 273 ? -6.805  -9.911  62.041  1.00 10.43 ? 272  LEU B CG  1 
ATOM   5898 C  CD1 . LEU B 1 273 ? -7.817  -10.023 63.218  1.00 11.92 ? 272  LEU B CD1 1 
ATOM   5899 C  CD2 . LEU B 1 273 ? -5.627  -8.982  62.404  1.00 11.86 ? 272  LEU B CD2 1 
ATOM   5900 N  N   . LEU B 1 274 ? -8.089  -11.310 59.060  1.00 9.89  ? 273  LEU B N   1 
ATOM   5901 C  CA  . LEU B 1 274 ? -9.076  -10.659 58.202  1.00 9.46  ? 273  LEU B CA  1 
ATOM   5902 C  C   . LEU B 1 274 ? -10.302 -11.547 57.990  1.00 10.17 ? 273  LEU B C   1 
ATOM   5903 O  O   . LEU B 1 274 ? -11.440 -11.052 57.959  1.00 9.48  ? 273  LEU B O   1 
ATOM   5904 C  CB  . LEU B 1 274 ? -8.431  -10.288 56.865  1.00 8.77  ? 273  LEU B CB  1 
ATOM   5905 C  CG  . LEU B 1 274 ? -7.603  -8.991  56.898  1.00 10.03 ? 273  LEU B CG  1 
ATOM   5906 C  CD1 . LEU B 1 274 ? -6.633  -8.867  55.713  1.00 11.22 ? 273  LEU B CD1 1 
ATOM   5907 C  CD2 . LEU B 1 274 ? -8.528  -7.769  56.976  1.00 11.28 ? 273  LEU B CD2 1 
ATOM   5908 N  N   . SER B 1 275 ? -10.092 -12.862 57.853  1.00 10.51 ? 274  SER B N   1 
ATOM   5909 C  CA  . SER B 1 275 ? -11.210 -13.785 57.658  1.00 11.16 ? 274  SER B CA  1 
ATOM   5910 C  C   . SER B 1 275 ? -12.110 -13.830 58.891  1.00 12.42 ? 274  SER B C   1 
ATOM   5911 O  O   . SER B 1 275 ? -13.338 -13.742 58.780  1.00 12.65 ? 274  SER B O   1 
ATOM   5912 C  CB  . SER B 1 275 ? -10.686 -15.188 57.320  1.00 12.01 ? 274  SER B CB  1 
ATOM   5913 O  OG  . SER B 1 275 ? -9.901  -15.203 56.124  1.00 10.95 ? 274  SER B OG  1 
ATOM   5914 N  N   . PHE B 1 276 ? -11.520 -13.979 60.081  1.00 11.16 ? 275  PHE B N   1 
ATOM   5915 C  CA  . PHE B 1 276 ? -12.330 -13.955 61.302  1.00 8.92  ? 275  PHE B CA  1 
ATOM   5916 C  C   . PHE B 1 276 ? -13.044 -12.615 61.472  1.00 10.65 ? 275  PHE B C   1 
ATOM   5917 O  O   . PHE B 1 276 ? -14.198 -12.568 61.924  1.00 10.54 ? 275  PHE B O   1 
ATOM   5918 C  CB  . PHE B 1 276 ? -11.460 -14.238 62.535  1.00 9.96  ? 275  PHE B CB  1 
ATOM   5919 C  CG  . PHE B 1 276 ? -11.192 -15.696 62.782  1.00 11.82 ? 275  PHE B CG  1 
ATOM   5920 C  CD1 . PHE B 1 276 ? -12.226 -16.549 63.159  1.00 11.27 ? 275  PHE B CD1 1 
ATOM   5921 C  CD2 . PHE B 1 276 ? -9.897  -16.205 62.679  1.00 11.35 ? 275  PHE B CD2 1 
ATOM   5922 C  CE1 . PHE B 1 276 ? -11.981 -17.892 63.407  1.00 10.75 ? 275  PHE B CE1 1 
ATOM   5923 C  CE2 . PHE B 1 276 ? -9.630  -17.542 62.920  1.00 11.27 ? 275  PHE B CE2 1 
ATOM   5924 C  CZ  . PHE B 1 276 ? -10.676 -18.400 63.288  1.00 12.88 ? 275  PHE B CZ  1 
ATOM   5925 N  N   . ALA B 1 277 ? -12.368 -11.507 61.148  1.00 9.25  ? 276  ALA B N   1 
ATOM   5926 C  CA  . ALA B 1 277 ? -12.987 -10.195 61.332  1.00 9.99  ? 276  ALA B CA  1 
ATOM   5927 C  C   . ALA B 1 277 ? -14.225 -10.047 60.449  1.00 10.74 ? 276  ALA B C   1 
ATOM   5928 O  O   . ALA B 1 277 ? -15.278 -9.574  60.901  1.00 11.77 ? 276  ALA B O   1 
ATOM   5929 C  CB  . ALA B 1 277 ? -11.968 -9.087  61.047  1.00 10.27 ? 276  ALA B CB  1 
ATOM   5930 N  N   . LEU B 1 278 ? -14.123 -10.449 59.177  1.00 10.67 ? 277  LEU B N   1 
ATOM   5931 C  CA  . LEU B 1 278 ? -15.294 -10.348 58.308  1.00 9.24  ? 277  LEU B CA  1 
ATOM   5932 C  C   . LEU B 1 278 ? -16.401 -11.287 58.770  1.00 11.57 ? 277  LEU B C   1 
ATOM   5933 O  O   . LEU B 1 278 ? -17.587 -10.923 58.727  1.00 13.75 ? 277  LEU B O   1 
ATOM   5934 C  CB  . LEU B 1 278 ? -14.906 -10.625 56.851  1.00 11.26 ? 277  LEU B CB  1 
ATOM   5935 C  CG  . LEU B 1 278 ? -16.024 -10.364 55.834  1.00 16.14 ? 277  LEU B CG  1 
ATOM   5936 C  CD1 . LEU B 1 278 ? -16.457 -8.893  55.871  1.00 19.99 ? 277  LEU B CD1 1 
ATOM   5937 C  CD2 . LEU B 1 278 ? -15.595 -10.761 54.421  1.00 16.30 ? 277  LEU B CD2 1 
ATOM   5938 N  N   . TYR B 1 279 ? -16.037 -12.489 59.237  1.00 9.57  ? 278  TYR B N   1 
ATOM   5939 C  CA  . TYR B 1 279 ? -17.037 -13.392 59.810  1.00 10.18 ? 278  TYR B CA  1 
ATOM   5940 C  C   . TYR B 1 279 ? -17.800 -12.707 60.938  1.00 10.30 ? 278  TYR B C   1 
ATOM   5941 O  O   . TYR B 1 279 ? -19.037 -12.665 60.936  1.00 11.88 ? 278  TYR B O   1 
ATOM   5942 C  CB  . TYR B 1 279 ? -16.374 -14.687 60.322  1.00 10.97 ? 278  TYR B CB  1 
ATOM   5943 C  CG  . TYR B 1 279 ? -17.277 -15.491 61.236  1.00 12.15 ? 278  TYR B CG  1 
ATOM   5944 C  CD1 . TYR B 1 279 ? -18.201 -16.397 60.717  1.00 12.52 ? 278  TYR B CD1 1 
ATOM   5945 C  CD2 . TYR B 1 279 ? -17.231 -15.320 62.619  1.00 13.22 ? 278  TYR B CD2 1 
ATOM   5946 C  CE1 . TYR B 1 279 ? -19.045 -17.115 61.550  1.00 12.53 ? 278  TYR B CE1 1 
ATOM   5947 C  CE2 . TYR B 1 279 ? -18.072 -16.031 63.457  1.00 12.63 ? 278  TYR B CE2 1 
ATOM   5948 C  CZ  . TYR B 1 279 ? -18.979 -16.928 62.916  1.00 13.13 ? 278  TYR B CZ  1 
ATOM   5949 O  OH  . TYR B 1 279 ? -19.829 -17.632 63.749  1.00 16.38 ? 278  TYR B OH  1 
ATOM   5950 N  N   . PHE B 1 280 ? -17.080 -12.169 61.925  1.00 11.26 ? 279  PHE B N   1 
ATOM   5951 C  CA  . PHE B 1 280 ? -17.782 -11.555 63.050  1.00 10.51 ? 279  PHE B CA  1 
ATOM   5952 C  C   . PHE B 1 280 ? -18.598 -10.341 62.616  1.00 11.34 ? 279  PHE B C   1 
ATOM   5953 O  O   . PHE B 1 280 ? -19.673 -10.087 63.173  1.00 12.32 ? 279  PHE B O   1 
ATOM   5954 C  CB  . PHE B 1 280 ? -16.790 -11.176 64.155  1.00 12.62 ? 279  PHE B CB  1 
ATOM   5955 C  CG  . PHE B 1 280 ? -16.345 -12.346 65.005  1.00 13.03 ? 279  PHE B CG  1 
ATOM   5956 C  CD1 . PHE B 1 280 ? -17.264 -13.049 65.775  1.00 13.17 ? 279  PHE B CD1 1 
ATOM   5957 C  CD2 . PHE B 1 280 ? -15.008 -12.736 65.036  1.00 12.94 ? 279  PHE B CD2 1 
ATOM   5958 C  CE1 . PHE B 1 280 ? -16.862 -14.132 66.570  1.00 14.18 ? 279  PHE B CE1 1 
ATOM   5959 C  CE2 . PHE B 1 280 ? -14.588 -13.817 65.820  1.00 13.21 ? 279  PHE B CE2 1 
ATOM   5960 C  CZ  . PHE B 1 280 ? -15.515 -14.518 66.601  1.00 12.41 ? 279  PHE B CZ  1 
ATOM   5961 N  N   . LEU B 1 281 ? -18.125 -9.582  61.624  1.00 11.50 ? 280  LEU B N   1 
ATOM   5962 C  CA  . LEU B 1 281 ? -18.905 -8.437  61.162  1.00 11.31 ? 280  LEU B CA  1 
ATOM   5963 C  C   . LEU B 1 281 ? -20.241 -8.868  60.558  1.00 13.25 ? 280  LEU B C   1 
ATOM   5964 O  O   . LEU B 1 281 ? -21.281 -8.279  60.872  1.00 13.59 ? 280  LEU B O   1 
ATOM   5965 C  CB  . LEU B 1 281 ? -18.097 -7.605  60.166  1.00 12.40 ? 280  LEU B CB  1 
ATOM   5966 C  CG  . LEU B 1 281 ? -16.959 -6.804  60.795  1.00 12.15 ? 280  LEU B CG  1 
ATOM   5967 C  CD1 . LEU B 1 281 ? -16.108 -6.150  59.714  1.00 16.46 ? 280  LEU B CD1 1 
ATOM   5968 C  CD2 . LEU B 1 281 ? -17.493 -5.756  61.781  1.00 17.95 ? 280  LEU B CD2 1 
ATOM   5969 N  N   . VAL B 1 282 ? -20.245 -9.883  59.683  1.00 12.73 ? 281  VAL B N   1 
ATOM   5970 C  CA  . VAL B 1 282 ? -21.522 -10.270 59.076  1.00 12.52 ? 281  VAL B CA  1 
ATOM   5971 C  C   . VAL B 1 282 ? -22.449 -10.953 60.080  1.00 14.24 ? 281  VAL B C   1 
ATOM   5972 O  O   . VAL B 1 282 ? -23.669 -11.009 59.855  1.00 15.52 ? 281  VAL B O   1 
ATOM   5973 C  CB  . VAL B 1 282 ? -21.332 -11.157 57.823  1.00 14.10 ? 281  VAL B CB  1 
ATOM   5974 C  CG1 . VAL B 1 282 ? -20.493 -10.428 56.775  1.00 14.37 ? 281  VAL B CG1 1 
ATOM   5975 C  CG2 . VAL B 1 282 ? -20.748 -12.524 58.156  1.00 13.22 ? 281  VAL B CG2 1 
ATOM   5976 N  N   . LYS B 1 283 ? -21.915 -11.474 61.182  1.00 11.48 ? 282  LYS B N   1 
ATOM   5977 C  CA  . LYS B 1 283 ? -22.754 -12.045 62.231  1.00 12.41 ? 282  LYS B CA  1 
ATOM   5978 C  C   . LYS B 1 283 ? -23.232 -11.009 63.246  1.00 12.65 ? 282  LYS B C   1 
ATOM   5979 O  O   . LYS B 1 283 ? -24.098 -11.325 64.080  1.00 14.02 ? 282  LYS B O   1 
ATOM   5980 C  CB  . LYS B 1 283 ? -22.001 -13.173 62.958  1.00 13.57 ? 282  LYS B CB  1 
ATOM   5981 C  CG  . LYS B 1 283 ? -21.619 -14.366 62.079  1.00 13.86 ? 282  LYS B CG  1 
ATOM   5982 C  CD  . LYS B 1 283 ? -22.840 -15.065 61.493  1.00 14.20 ? 282  LYS B CD  1 
ATOM   5983 C  CE  . LYS B 1 283 ? -22.443 -16.405 60.845  1.00 12.79 ? 282  LYS B CE  1 
ATOM   5984 N  NZ  . LYS B 1 283 ? -23.593 -17.134 60.208  1.00 13.46 ? 282  LYS B NZ  1 
ATOM   5985 N  N   . ASN B 1 284 ? -22.715 -9.781  63.195  1.00 11.10 ? 283  ASN B N   1 
ATOM   5986 C  CA  . ASN B 1 284 ? -23.046 -8.734  64.169  1.00 12.17 ? 283  ASN B CA  1 
ATOM   5987 C  C   . ASN B 1 284 ? -23.323 -7.429  63.431  1.00 10.42 ? 283  ASN B C   1 
ATOM   5988 O  O   . ASN B 1 284 ? -22.483 -6.518  63.406  1.00 12.56 ? 283  ASN B O   1 
ATOM   5989 C  CB  . ASN B 1 284 ? -21.923 -8.576  65.196  1.00 12.89 ? 283  ASN B CB  1 
ATOM   5990 C  CG  . ASN B 1 284 ? -21.783 -9.798  66.099  1.00 14.59 ? 283  ASN B CG  1 
ATOM   5991 O  OD1 . ASN B 1 284 ? -22.470 -9.913  67.121  1.00 14.59 ? 283  ASN B OD1 1 
ATOM   5992 N  ND2 . ASN B 1 284 ? -20.886 -10.718 65.726  1.00 13.59 ? 283  ASN B ND2 1 
ATOM   5993 N  N   . PRO B 1 285 ? -24.506 -7.304  62.823  1.00 10.87 ? 284  PRO B N   1 
ATOM   5994 C  CA  . PRO B 1 285 ? -24.773 -6.137  61.967  1.00 11.88 ? 284  PRO B CA  1 
ATOM   5995 C  C   . PRO B 1 285 ? -24.690 -4.780  62.664  1.00 12.20 ? 284  PRO B C   1 
ATOM   5996 O  O   . PRO B 1 285 ? -24.361 -3.792  61.993  1.00 12.15 ? 284  PRO B O   1 
ATOM   5997 C  CB  . PRO B 1 285 ? -26.185 -6.410  61.424  1.00 14.94 ? 284  PRO B CB  1 
ATOM   5998 C  CG  . PRO B 1 285 ? -26.692 -7.627  62.103  1.00 14.28 ? 284  PRO B CG  1 
ATOM   5999 C  CD  . PRO B 1 285 ? -25.528 -8.356  62.694  1.00 11.95 ? 284  PRO B CD  1 
ATOM   6000 N  N   . HIS B 1 286 ? -24.978 -4.675  63.970  1.00 11.57 ? 285  HIS B N   1 
ATOM   6001 C  CA  . HIS B 1 286 ? -24.767 -3.389  64.643  1.00 10.83 ? 285  HIS B CA  1 
ATOM   6002 C  C   . HIS B 1 286 ? -23.298 -2.984  64.580  1.00 11.82 ? 285  HIS B C   1 
ATOM   6003 O  O   . HIS B 1 286 ? -22.971 -1.811  64.360  1.00 14.12 ? 285  HIS B O   1 
ATOM   6004 C  CB  . HIS B 1 286 ? -25.205 -3.443  66.113  1.00 11.72 ? 285  HIS B CB  1 
ATOM   6005 C  CG  . HIS B 1 286 ? -26.685 -3.499  66.322  1.00 13.86 ? 285  HIS B CG  1 
ATOM   6006 N  ND1 . HIS B 1 286 ? -27.540 -2.517  65.871  1.00 17.57 ? 285  HIS B ND1 1 
ATOM   6007 C  CD2 . HIS B 1 286 ? -27.458 -4.410  66.961  1.00 14.73 ? 285  HIS B CD2 1 
ATOM   6008 C  CE1 . HIS B 1 286 ? -28.779 -2.826  66.214  1.00 17.13 ? 285  HIS B CE1 1 
ATOM   6009 N  NE2 . HIS B 1 286 ? -28.756 -3.968  66.879  1.00 15.23 ? 285  HIS B NE2 1 
ATOM   6010 N  N   . VAL B 1 287 ? -22.398 -3.944  64.785  1.00 12.23 ? 286  VAL B N   1 
ATOM   6011 C  CA  . VAL B 1 287 ? -20.967 -3.651  64.736  1.00 12.13 ? 286  VAL B CA  1 
ATOM   6012 C  C   . VAL B 1 287 ? -20.535 -3.323  63.310  1.00 10.52 ? 286  VAL B C   1 
ATOM   6013 O  O   . VAL B 1 287 ? -19.756 -2.388  63.079  1.00 11.81 ? 286  VAL B O   1 
ATOM   6014 C  CB  . VAL B 1 287 ? -20.174 -4.834  65.316  1.00 11.55 ? 286  VAL B CB  1 
ATOM   6015 C  CG1 . VAL B 1 287 ? -18.672 -4.596  65.189  1.00 10.69 ? 286  VAL B CG1 1 
ATOM   6016 C  CG2 . VAL B 1 287 ? -20.582 -5.068  66.776  1.00 11.46 ? 286  VAL B CG2 1 
ATOM   6017 N  N   . LEU B 1 288 ? -21.034 -4.083  62.334  1.00 12.15 ? 287  LEU B N   1 
ATOM   6018 C  CA  . LEU B 1 288 ? -20.723 -3.802  60.938  1.00 10.95 ? 287  LEU B CA  1 
ATOM   6019 C  C   . LEU B 1 288 ? -21.123 -2.378  60.563  1.00 14.27 ? 287  LEU B C   1 
ATOM   6020 O  O   . LEU B 1 288 ? -20.366 -1.672  59.889  1.00 13.84 ? 287  LEU B O   1 
ATOM   6021 C  CB  . LEU B 1 288 ? -21.416 -4.838  60.045  1.00 13.16 ? 287  LEU B CB  1 
ATOM   6022 C  CG  . LEU B 1 288 ? -21.352 -4.668  58.527  1.00 18.65 ? 287  LEU B CG  1 
ATOM   6023 C  CD1 . LEU B 1 288 ? -19.948 -4.404  58.075  1.00 21.09 ? 287  LEU B CD1 1 
ATOM   6024 C  CD2 . LEU B 1 288 ? -21.894 -5.924  57.856  1.00 25.44 ? 287  LEU B CD2 1 
ATOM   6025 N  N   . GLN B 1 289 ? -22.295 -1.926  61.021  1.00 13.70 ? 288  GLN B N   1 
ATOM   6026 C  CA  . GLN B 1 289 ? -22.742 -0.571  60.707  1.00 12.28 ? 288  GLN B CA  1 
ATOM   6027 C  C   . GLN B 1 289 ? -21.785 0.479   61.269  1.00 12.50 ? 288  GLN B C   1 
ATOM   6028 O  O   . GLN B 1 289 ? -21.442 1.450   60.583  1.00 13.04 ? 288  GLN B O   1 
ATOM   6029 C  CB  . GLN B 1 289 ? -24.162 -0.352  61.238  1.00 15.11 ? 288  GLN B CB  1 
ATOM   6030 C  CG  . GLN B 1 289 ? -24.726 1.039   60.982  1.00 21.93 ? 288  GLN B CG  1 
ATOM   6031 C  CD  . GLN B 1 289 ? -26.178 1.163   61.420  1.00 36.35 ? 288  GLN B CD  1 
ATOM   6032 O  OE1 . GLN B 1 289 ? -26.468 1.611   62.528  1.00 40.41 ? 288  GLN B OE1 1 
ATOM   6033 N  NE2 . GLN B 1 289 ? -27.097 0.764   60.547  1.00 41.90 ? 288  GLN B NE2 1 
ATOM   6034 N  N   . LYS B 1 290 ? -21.348 0.308   62.523  1.00 11.42 ? 289  LYS B N   1 
ATOM   6035 C  CA  . LYS B 1 290 ? -20.438 1.286   63.120  1.00 11.73 ? 289  LYS B CA  1 
ATOM   6036 C  C   . LYS B 1 290 ? -19.099 1.317   62.393  1.00 12.68 ? 289  LYS B C   1 
ATOM   6037 O  O   . LYS B 1 290 ? -18.532 2.394   62.166  1.00 12.96 ? 289  LYS B O   1 
ATOM   6038 C  CB  . LYS B 1 290 ? -20.234 0.985   64.609  1.00 16.42 ? 289  LYS B CB  1 
ATOM   6039 C  CG  . LYS B 1 290 ? -21.337 1.535   65.497  1.00 20.58 ? 289  LYS B CG  1 
ATOM   6040 C  CD  . LYS B 1 290 ? -21.183 1.124   66.972  1.00 19.52 ? 289  LYS B CD  1 
ATOM   6041 C  CE  . LYS B 1 290 ? -20.131 1.942   67.728  1.00 17.04 ? 289  LYS B CE  1 
ATOM   6042 N  NZ  . LYS B 1 290 ? -20.279 1.764   69.236  1.00 14.77 ? 289  LYS B NZ  1 
ATOM   6043 N  N   . ALA B 1 291 ? -18.578 0.144   62.019  1.00 11.83 ? 290  ALA B N   1 
ATOM   6044 C  CA  . ALA B 1 291 ? -17.303 0.092   61.310  1.00 10.71 ? 290  ALA B CA  1 
ATOM   6045 C  C   . ALA B 1 291 ? -17.421 0.706   59.922  1.00 11.26 ? 290  ALA B C   1 
ATOM   6046 O  O   . ALA B 1 291 ? -16.520 1.433   59.475  1.00 13.48 ? 290  ALA B O   1 
ATOM   6047 C  CB  . ALA B 1 291 ? -16.818 -1.354  61.218  1.00 12.85 ? 290  ALA B CB  1 
ATOM   6048 N  N   . ALA B 1 292 ? -18.525 0.427   59.225  1.00 11.74 ? 291  ALA B N   1 
ATOM   6049 C  CA  . ALA B 1 292 ? -18.700 0.969   57.880  1.00 11.70 ? 291  ALA B CA  1 
ATOM   6050 C  C   . ALA B 1 292 ? -18.911 2.481   57.908  1.00 10.78 ? 291  ALA B C   1 
ATOM   6051 O  O   . ALA B 1 292 ? -18.455 3.190   57.006  1.00 13.04 ? 291  ALA B O   1 
ATOM   6052 C  CB  . ALA B 1 292 ? -19.871 0.277   57.174  1.00 12.21 ? 291  ALA B CB  1 
ATOM   6053 N  N   . GLU B 1 293 ? -19.622 2.997   58.914  1.00 11.78 ? 292  GLU B N   1 
ATOM   6054 C  CA  . GLU B 1 293 ? -19.739 4.447   59.039  1.00 11.99 ? 292  GLU B CA  1 
ATOM   6055 C  C   . GLU B 1 293 ? -18.362 5.087   59.127  1.00 12.35 ? 292  GLU B C   1 
ATOM   6056 O  O   . GLU B 1 293 ? -18.083 6.091   58.458  1.00 11.62 ? 292  GLU B O   1 
ATOM   6057 C  CB  . GLU B 1 293 ? -20.575 4.818   60.268  1.00 12.51 ? 292  GLU B CB  1 
ATOM   6058 C  CG  . GLU B 1 293 ? -20.933 6.316   60.362  1.00 13.22 ? 292  GLU B CG  1 
ATOM   6059 C  CD  . GLU B 1 293 ? -19.797 7.222   60.848  1.00 16.71 ? 292  GLU B CD  1 
ATOM   6060 O  OE1 . GLU B 1 293 ? -18.901 6.757   61.593  1.00 16.28 ? 292  GLU B OE1 1 
ATOM   6061 O  OE2 . GLU B 1 293 ? -19.808 8.420   60.482  1.00 18.69 ? 292  GLU B OE2 1 
ATOM   6062 N  N   . GLU B 1 294 ? -17.481 4.521   59.958  1.00 12.00 ? 293  GLU B N   1 
ATOM   6063 C  CA  . GLU B 1 294 ? -16.156 5.108   60.105  1.00 12.32 ? 293  GLU B CA  1 
ATOM   6064 C  C   . GLU B 1 294 ? -15.377 5.046   58.796  1.00 13.76 ? 293  GLU B C   1 
ATOM   6065 O  O   . GLU B 1 294 ? -14.749 6.033   58.394  1.00 13.95 ? 293  GLU B O   1 
ATOM   6066 C  CB  . GLU B 1 294 ? -15.390 4.403   61.223  1.00 11.87 ? 293  GLU B CB  1 
ATOM   6067 C  CG  . GLU B 1 294 ? -14.033 5.030   61.543  1.00 11.58 ? 293  GLU B CG  1 
ATOM   6068 C  CD  . GLU B 1 294 ? -13.299 4.260   62.620  1.00 14.58 ? 293  GLU B CD  1 
ATOM   6069 O  OE1 . GLU B 1 294 ? -12.750 3.186   62.294  1.00 13.56 ? 293  GLU B OE1 1 
ATOM   6070 O  OE2 . GLU B 1 294 ? -13.300 4.712   63.796  1.00 14.38 ? 293  GLU B OE2 1 
ATOM   6071 N  N   . ALA B 1 295 ? -15.411 3.896   58.112  1.00 11.56 ? 294  ALA B N   1 
ATOM   6072 C  CA  . ALA B 1 295 ? -14.645 3.757   56.877  1.00 12.74 ? 294  ALA B CA  1 
ATOM   6073 C  C   . ALA B 1 295 ? -15.098 4.774   55.834  1.00 13.36 ? 294  ALA B C   1 
ATOM   6074 O  O   . ALA B 1 295 ? -14.268 5.398   55.156  1.00 13.67 ? 294  ALA B O   1 
ATOM   6075 C  CB  . ALA B 1 295 ? -14.767 2.327   56.343  1.00 13.35 ? 294  ALA B CB  1 
ATOM   6076 N  N   . ALA B 1 296 ? -16.414 4.952   55.688  1.00 13.03 ? 295  ALA B N   1 
ATOM   6077 C  CA  . ALA B 1 296 ? -16.938 5.895   54.703  1.00 12.98 ? 295  ALA B CA  1 
ATOM   6078 C  C   . ALA B 1 296 ? -16.549 7.328   55.043  1.00 14.91 ? 295  ALA B C   1 
ATOM   6079 O  O   . ALA B 1 296 ? -16.259 8.131   54.144  1.00 16.28 ? 295  ALA B O   1 
ATOM   6080 C  CB  . ALA B 1 296 ? -18.461 5.755   54.609  1.00 15.18 ? 295  ALA B CB  1 
ATOM   6081 N  N   . ARG B 1 297 ? -16.538 7.669   56.335  1.00 15.29 ? 296  ARG B N   1 
ATOM   6082 C  CA  . ARG B 1 297 ? -16.288 9.045   56.758  1.00 15.12 ? 296  ARG B CA  1 
ATOM   6083 C  C   . ARG B 1 297 ? -14.810 9.407   56.672  1.00 13.58 ? 296  ARG B C   1 
ATOM   6084 O  O   . ARG B 1 297 ? -14.464 10.546  56.325  1.00 17.12 ? 296  ARG B O   1 
ATOM   6085 C  CB  . ARG B 1 297 ? -16.799 9.247   58.187  1.00 15.47 ? 296  ARG B CB  1 
ATOM   6086 C  CG  . ARG B 1 297 ? -16.341 10.541  58.842  1.00 17.12 ? 296  ARG B CG  1 
ATOM   6087 C  CD  . ARG B 1 297 ? -17.131 10.841  60.127  1.00 19.01 ? 296  ARG B CD  1 
ATOM   6088 N  NE  . ARG B 1 297 ? -17.230 9.686   61.019  1.00 17.84 ? 296  ARG B NE  1 
ATOM   6089 C  CZ  . ARG B 1 297 ? -16.351 9.397   61.971  1.00 19.62 ? 296  ARG B CZ  1 
ATOM   6090 N  NH1 . ARG B 1 297 ? -15.279 10.151  62.173  1.00 20.90 ? 296  ARG B NH1 1 
ATOM   6091 N  NH2 . ARG B 1 297 ? -16.555 8.329   62.743  1.00 19.56 ? 296  ARG B NH2 1 
ATOM   6092 N  N   . VAL B 1 298 ? -13.931 8.459   56.983  1.00 12.62 ? 297  VAL B N   1 
ATOM   6093 C  CA  . VAL B 1 298 ? -12.497 8.728   57.068  1.00 13.36 ? 297  VAL B CA  1 
ATOM   6094 C  C   . VAL B 1 298 ? -11.811 8.578   55.715  1.00 15.98 ? 297  VAL B C   1 
ATOM   6095 O  O   . VAL B 1 298 ? -10.954 9.394   55.360  1.00 17.26 ? 297  VAL B O   1 
ATOM   6096 C  CB  . VAL B 1 298 ? -11.858 7.804   58.129  1.00 15.63 ? 297  VAL B CB  1 
ATOM   6097 C  CG1 . VAL B 1 298 ? -10.332 7.789   57.990  1.00 15.85 ? 297  VAL B CG1 1 
ATOM   6098 C  CG2 . VAL B 1 298 ? -12.263 8.243   59.542  1.00 15.77 ? 297  VAL B CG2 1 
ATOM   6099 N  N   . LEU B 1 299 ? -12.163 7.543   54.947  1.00 13.95 ? 298  LEU B N   1 
ATOM   6100 C  CA  . LEU B 1 299 ? -11.469 7.231   53.688  1.00 13.95 ? 298  LEU B CA  1 
ATOM   6101 C  C   . LEU B 1 299 ? -12.093 8.021   52.536  1.00 15.67 ? 298  LEU B C   1 
ATOM   6102 O  O   . LEU B 1 299 ? -12.730 7.481   51.628  1.00 15.83 ? 298  LEU B O   1 
ATOM   6103 C  CB  . LEU B 1 299 ? -11.508 5.730   53.422  1.00 12.72 ? 298  LEU B CB  1 
ATOM   6104 C  CG  . LEU B 1 299 ? -10.823 4.839   54.462  1.00 12.01 ? 298  LEU B CG  1 
ATOM   6105 C  CD1 . LEU B 1 299 ? -10.935 3.358   54.072  1.00 13.14 ? 298  LEU B CD1 1 
ATOM   6106 C  CD2 . LEU B 1 299 ? -9.382  5.219   54.641  1.00 14.52 ? 298  LEU B CD2 1 
ATOM   6107 N  N   . VAL B 1 300 ? -11.870 9.338   52.572  1.00 17.58 ? 299  VAL B N   1 
ATOM   6108 C  CA  . VAL B 1 300 ? -12.542 10.234  51.632  1.00 18.01 ? 299  VAL B CA  1 
ATOM   6109 C  C   . VAL B 1 300 ? -11.885 10.286  50.261  1.00 17.94 ? 299  VAL B C   1 
ATOM   6110 O  O   . VAL B 1 300 ? -12.455 10.885  49.338  1.00 21.62 ? 299  VAL B O   1 
ATOM   6111 C  CB  . VAL B 1 300 ? -12.620 11.655  52.222  1.00 22.15 ? 299  VAL B CB  1 
ATOM   6112 C  CG1 . VAL B 1 300 ? -13.438 11.631  53.503  1.00 23.79 ? 299  VAL B CG1 1 
ATOM   6113 C  CG2 . VAL B 1 300 ? -11.228 12.192  52.497  1.00 19.92 ? 299  VAL B CG2 1 
ATOM   6114 N  N   . ASP B 1 301 ? -10.714 9.680   50.093  1.00 15.87 ? 300  ASP B N   1 
ATOM   6115 C  CA  . ASP B 1 301 ? -10.003 9.749   48.828  1.00 18.64 ? 300  ASP B CA  1 
ATOM   6116 C  C   . ASP B 1 301 ? -9.969  8.382   48.146  1.00 19.76 ? 300  ASP B C   1 
ATOM   6117 O  O   . ASP B 1 301 ? -9.985  7.347   48.819  1.00 19.84 ? 300  ASP B O   1 
ATOM   6118 C  CB  . ASP B 1 301 ? -8.568  10.244  49.046  1.00 19.27 ? 300  ASP B CB  1 
ATOM   6119 C  CG  . ASP B 1 301 ? -8.514  11.662  49.588  1.00 22.79 ? 300  ASP B CG  1 
ATOM   6120 O  OD1 . ASP B 1 301 ? -9.199  12.538  49.026  1.00 25.56 ? 300  ASP B OD1 1 
ATOM   6121 O  OD2 . ASP B 1 301 ? -7.778  11.905  50.564  1.00 24.27 ? 300  ASP B OD2 1 
ATOM   6122 N  N   . PRO B 1 302 ? -9.911  8.340   46.812  1.00 18.82 ? 301  PRO B N   1 
ATOM   6123 C  CA  . PRO B 1 302 ? -9.830  7.034   46.130  1.00 19.14 ? 301  PRO B CA  1 
ATOM   6124 C  C   . PRO B 1 302 ? -8.646  6.194   46.572  1.00 19.83 ? 301  PRO B C   1 
ATOM   6125 O  O   . PRO B 1 302 ? -8.746  4.960   46.601  1.00 21.40 ? 301  PRO B O   1 
ATOM   6126 C  CB  . PRO B 1 302 ? -9.717  7.413   44.646  1.00 23.43 ? 301  PRO B CB  1 
ATOM   6127 C  CG  . PRO B 1 302 ? -10.241 8.808   44.549  1.00 25.54 ? 301  PRO B CG  1 
ATOM   6128 C  CD  . PRO B 1 302 ? -9.979  9.470   45.870  1.00 23.20 ? 301  PRO B CD  1 
ATOM   6129 N  N   . VAL B 1 303 ? -7.524  6.823   46.904  1.00 19.56 ? 302  VAL B N   1 
ATOM   6130 C  CA  . VAL B 1 303 ? -6.324  6.149   47.386  1.00 23.36 ? 302  VAL B CA  1 
ATOM   6131 C  C   . VAL B 1 303 ? -6.163  6.495   48.868  1.00 22.63 ? 302  VAL B C   1 
ATOM   6132 O  O   . VAL B 1 303 ? -5.842  7.646   49.196  1.00 27.25 ? 302  VAL B O   1 
ATOM   6133 C  CB  . VAL B 1 303 ? -5.086  6.568   46.577  1.00 24.05 ? 302  VAL B CB  1 
ATOM   6134 C  CG1 . VAL B 1 303 ? -3.835  5.919   47.119  1.00 24.45 ? 302  VAL B CG1 1 
ATOM   6135 C  CG2 . VAL B 1 303 ? -5.262  6.227   45.096  1.00 26.29 ? 302  VAL B CG2 1 
ATOM   6136 N  N   . PRO B 1 304 ? -6.381  5.554   49.793  1.00 18.99 ? 303  PRO B N   1 
ATOM   6137 C  CA  . PRO B 1 304 ? -6.211  5.875   51.220  1.00 18.07 ? 303  PRO B CA  1 
ATOM   6138 C  C   . PRO B 1 304 ? -4.772  6.253   51.535  1.00 16.65 ? 303  PRO B C   1 
ATOM   6139 O  O   . PRO B 1 304 ? -3.826  5.677   50.992  1.00 17.66 ? 303  PRO B O   1 
ATOM   6140 C  CB  . PRO B 1 304 ? -6.611  4.574   51.932  1.00 19.96 ? 303  PRO B CB  1 
ATOM   6141 C  CG  . PRO B 1 304 ? -7.443  3.820   50.930  1.00 20.91 ? 303  PRO B CG  1 
ATOM   6142 C  CD  . PRO B 1 304 ? -6.854  4.173   49.591  1.00 18.90 ? 303  PRO B CD  1 
ATOM   6143 N  N   . SER B 1 305 ? -4.611  7.217   52.439  1.00 15.01 ? 304  SER B N   1 
ATOM   6144 C  CA  . SER B 1 305 ? -3.296  7.636   52.897  1.00 16.09 ? 304  SER B CA  1 
ATOM   6145 C  C   . SER B 1 305 ? -2.943  6.938   54.201  1.00 16.20 ? 304  SER B C   1 
ATOM   6146 O  O   . SER B 1 305 ? -3.800  6.378   54.893  1.00 15.04 ? 304  SER B O   1 
ATOM   6147 C  CB  . SER B 1 305 ? -3.242  9.149   53.104  1.00 17.43 ? 304  SER B CB  1 
ATOM   6148 O  OG  . SER B 1 305 ? -4.015  9.516   54.234  1.00 18.28 ? 304  SER B OG  1 
ATOM   6149 N  N   . TYR B 1 306 ? -1.652  7.002   54.537  1.00 15.38 ? 305  TYR B N   1 
ATOM   6150 C  CA  . TYR B 1 306 ? -1.177  6.469   55.811  1.00 13.05 ? 305  TYR B CA  1 
ATOM   6151 C  C   . TYR B 1 306 ? -1.894  7.126   56.985  1.00 12.90 ? 305  TYR B C   1 
ATOM   6152 O  O   . TYR B 1 306 ? -2.355  6.440   57.907  1.00 14.72 ? 305  TYR B O   1 
ATOM   6153 C  CB  . TYR B 1 306 ? 0.334   6.675   55.913  1.00 15.13 ? 305  TYR B CB  1 
ATOM   6154 C  CG  . TYR B 1 306 ? 0.931   6.256   57.233  1.00 20.26 ? 305  TYR B CG  1 
ATOM   6155 C  CD1 . TYR B 1 306 ? 1.351   4.950   57.449  1.00 20.85 ? 305  TYR B CD1 1 
ATOM   6156 C  CD2 . TYR B 1 306 ? 1.088   7.177   58.262  1.00 23.13 ? 305  TYR B CD2 1 
ATOM   6157 C  CE1 . TYR B 1 306 ? 1.902   4.571   58.664  1.00 23.78 ? 305  TYR B CE1 1 
ATOM   6158 C  CE2 . TYR B 1 306 ? 1.631   6.812   59.466  1.00 26.50 ? 305  TYR B CE2 1 
ATOM   6159 C  CZ  . TYR B 1 306 ? 2.039   5.513   59.667  1.00 26.96 ? 305  TYR B CZ  1 
ATOM   6160 O  OH  . TYR B 1 306 ? 2.579   5.172   60.886  1.00 30.85 ? 305  TYR B OH  1 
ATOM   6161 N  N   . LYS B 1 307 ? -2.016  8.459   56.957  1.00 14.51 ? 306  LYS B N   1 
ATOM   6162 C  CA  . LYS B 1 307 ? -2.680  9.174   58.048  1.00 14.73 ? 306  LYS B CA  1 
ATOM   6163 C  C   . LYS B 1 307 ? -4.139  8.760   58.188  1.00 14.01 ? 306  LYS B C   1 
ATOM   6164 O  O   . LYS B 1 307 ? -4.655  8.651   59.308  1.00 15.11 ? 306  LYS B O   1 
ATOM   6165 C  CB  . LYS B 1 307 ? -2.588  10.686  57.827  1.00 22.84 ? 306  LYS B CB  1 
ATOM   6166 C  CG  . LYS B 1 307 ? -1.285  11.314  58.286  1.00 31.64 ? 306  LYS B CG  1 
ATOM   6167 C  CD  . LYS B 1 307 ? -1.364  12.840  58.226  1.00 39.42 ? 306  LYS B CD  1 
ATOM   6168 C  CE  . LYS B 1 307 ? -0.107  13.503  58.785  1.00 45.82 ? 306  LYS B CE  1 
ATOM   6169 N  NZ  . LYS B 1 307 ? 1.081   13.329  57.898  1.00 50.66 ? 306  LYS B NZ  1 
ATOM   6170 N  N   . GLN B 1 308 ? -4.827  8.535   57.064  1.00 14.01 ? 307  GLN B N   1 
ATOM   6171 C  CA  . GLN B 1 308 ? -6.233  8.140   57.136  1.00 14.73 ? 307  GLN B CA  1 
ATOM   6172 C  C   . GLN B 1 308 ? -6.383  6.762   57.769  1.00 12.93 ? 307  GLN B C   1 
ATOM   6173 O  O   . GLN B 1 308 ? -7.279  6.546   58.592  1.00 15.03 ? 307  GLN B O   1 
ATOM   6174 C  CB  . GLN B 1 308 ? -6.870  8.170   55.739  1.00 14.96 ? 307  GLN B CB  1 
ATOM   6175 C  CG  . GLN B 1 308 ? -7.075  9.589   55.179  1.00 15.43 ? 307  GLN B CG  1 
ATOM   6176 C  CD  . GLN B 1 308 ? -7.379  9.627   53.679  1.00 17.88 ? 307  GLN B CD  1 
ATOM   6177 O  OE1 . GLN B 1 308 ? -7.122  8.672   52.947  1.00 19.21 ? 307  GLN B OE1 1 
ATOM   6178 N  NE2 . GLN B 1 308 ? -7.932  10.744  53.223  1.00 19.69 ? 307  GLN B NE2 1 
ATOM   6179 N  N   . VAL B 1 309 ? -5.512  5.817   57.410  1.00 13.37 ? 308  VAL B N   1 
ATOM   6180 C  CA  . VAL B 1 309 ? -5.585  4.497   58.031  1.00 12.44 ? 308  VAL B CA  1 
ATOM   6181 C  C   . VAL B 1 309 ? -5.414  4.609   59.542  1.00 12.01 ? 308  VAL B C   1 
ATOM   6182 O  O   . VAL B 1 309 ? -6.083  3.904   60.309  1.00 13.17 ? 308  VAL B O   1 
ATOM   6183 C  CB  . VAL B 1 309 ? -4.545  3.550   57.406  1.00 14.90 ? 308  VAL B CB  1 
ATOM   6184 C  CG1 . VAL B 1 309 ? -4.503  2.230   58.180  1.00 15.45 ? 308  VAL B CG1 1 
ATOM   6185 C  CG2 . VAL B 1 309 ? -4.891  3.299   55.953  1.00 13.84 ? 308  VAL B CG2 1 
ATOM   6186 N  N   . LYS B 1 310 ? -4.518  5.492   59.997  1.00 12.45 ? 309  LYS B N   1 
ATOM   6187 C  CA  . LYS B 1 310 ? -4.338  5.665   61.435  1.00 14.45 ? 309  LYS B CA  1 
ATOM   6188 C  C   . LYS B 1 310 ? -5.592  6.196   62.118  1.00 13.93 ? 309  LYS B C   1 
ATOM   6189 O  O   . LYS B 1 310 ? -5.724  6.051   63.342  1.00 16.64 ? 309  LYS B O   1 
ATOM   6190 C  CB  . LYS B 1 310 ? -3.158  6.598   61.722  1.00 16.66 ? 309  LYS B CB  1 
ATOM   6191 C  CG  . LYS B 1 310 ? -1.808  6.036   61.297  1.00 20.55 ? 309  LYS B CG  1 
ATOM   6192 C  CD  . LYS B 1 310 ? -1.547  4.719   61.993  1.00 26.82 ? 309  LYS B CD  1 
ATOM   6193 C  CE  . LYS B 1 310 ? -0.103  4.283   61.863  1.00 34.73 ? 309  LYS B CE  1 
ATOM   6194 N  NZ  . LYS B 1 310 ? 0.183   3.146   62.780  1.00 37.71 ? 309  LYS B NZ  1 
ATOM   6195 N  N   . GLN B 1 311 ? -6.506  6.821   61.372  1.00 11.77 ? 310  GLN B N   1 
ATOM   6196 C  CA  . GLN B 1 311 ? -7.726  7.367   61.963  1.00 11.27 ? 310  GLN B CA  1 
ATOM   6197 C  C   . GLN B 1 311 ? -8.844  6.341   62.091  1.00 13.87 ? 310  GLN B C   1 
ATOM   6198 O  O   . GLN B 1 311 ? -9.898  6.663   62.658  1.00 15.72 ? 310  GLN B O   1 
ATOM   6199 C  CB  . GLN B 1 311 ? -8.250  8.544   61.132  1.00 13.88 ? 310  GLN B CB  1 
ATOM   6200 C  CG  . GLN B 1 311 ? -7.443  9.818   61.211  1.00 18.60 ? 310  GLN B CG  1 
ATOM   6201 C  CD  . GLN B 1 311 ? -7.952  10.856  60.231  1.00 22.05 ? 310  GLN B CD  1 
ATOM   6202 O  OE1 . GLN B 1 311 ? -7.801  10.705  59.016  1.00 25.41 ? 310  GLN B OE1 1 
ATOM   6203 N  NE2 . GLN B 1 311 ? -8.570  11.908  60.749  1.00 24.54 ? 310  GLN B NE2 1 
ATOM   6204 N  N   . LEU B 1 312 ? -8.665  5.127   61.570  1.00 13.12 ? 311  LEU B N   1 
ATOM   6205 C  CA  . LEU B 1 312 ? -9.728  4.117   61.607  1.00 11.83 ? 311  LEU B CA  1 
ATOM   6206 C  C   . LEU B 1 312 ? -9.705  3.403   62.963  1.00 11.95 ? 311  LEU B C   1 
ATOM   6207 O  O   . LEU B 1 312 ? -9.374  2.222   63.081  1.00 13.85 ? 311  LEU B O   1 
ATOM   6208 C  CB  . LEU B 1 312 ? -9.565  3.140   60.452  1.00 9.55  ? 311  LEU B CB  1 
ATOM   6209 C  CG  . LEU B 1 312 ? -9.699  3.710   59.037  1.00 10.94 ? 311  LEU B CG  1 
ATOM   6210 C  CD1 . LEU B 1 312 ? -9.310  2.655   57.993  1.00 14.26 ? 311  LEU B CD1 1 
ATOM   6211 C  CD2 . LEU B 1 312 ? -11.123 4.215   58.782  1.00 12.11 ? 311  LEU B CD2 1 
ATOM   6212 N  N   . LYS B 1 313 ? -10.119 4.142   64.000  1.00 13.16 ? 312  LYS B N   1 
ATOM   6213 C  CA  A LYS B 1 313 ? -10.006 3.639   65.372  0.60 11.99 ? 312  LYS B CA  1 
ATOM   6214 C  CA  B LYS B 1 313 ? -10.002 3.635   65.367  0.40 13.04 ? 312  LYS B CA  1 
ATOM   6215 C  C   . LYS B 1 313 ? -10.921 2.440   65.605  1.00 14.24 ? 312  LYS B C   1 
ATOM   6216 O  O   . LYS B 1 313 ? -10.501 1.425   66.181  1.00 12.11 ? 312  LYS B O   1 
ATOM   6217 C  CB  A LYS B 1 313 ? -10.325 4.762   66.365  0.60 14.19 ? 312  LYS B CB  1 
ATOM   6218 C  CB  B LYS B 1 313 ? -10.307 4.755   66.363  0.40 14.45 ? 312  LYS B CB  1 
ATOM   6219 C  CG  A LYS B 1 313 ? -10.090 4.405   67.834  0.60 16.54 ? 312  LYS B CG  1 
ATOM   6220 C  CG  B LYS B 1 313 ? -9.376  5.941   66.230  0.40 15.77 ? 312  LYS B CG  1 
ATOM   6221 C  CD  A LYS B 1 313 ? -10.494 5.563   68.751  0.60 20.18 ? 312  LYS B CD  1 
ATOM   6222 C  CD  B LYS B 1 313 ? -7.927  5.511   66.375  0.40 19.59 ? 312  LYS B CD  1 
ATOM   6223 C  CE  A LYS B 1 313 ? -9.839  5.449   70.122  0.60 21.52 ? 312  LYS B CE  1 
ATOM   6224 C  CE  B LYS B 1 313 ? -6.979  6.618   65.957  0.40 23.04 ? 312  LYS B CE  1 
ATOM   6225 N  NZ  A LYS B 1 313 ? -10.324 4.276   70.879  0.60 20.35 ? 312  LYS B NZ  1 
ATOM   6226 N  NZ  B LYS B 1 313 ? -5.573  6.298   66.323  0.40 28.01 ? 312  LYS B NZ  1 
ATOM   6227 N  N   . TYR B 1 314 ? -12.189 2.544   65.187  1.00 11.24 ? 313  TYR B N   1 
ATOM   6228 C  CA  . TYR B 1 314 ? -13.134 1.459   65.443  1.00 10.91 ? 313  TYR B CA  1 
ATOM   6229 C  C   . TYR B 1 314 ? -12.812 0.228   64.595  1.00 11.03 ? 313  TYR B C   1 
ATOM   6230 O  O   . TYR B 1 314 ? -12.977 -0.908  65.057  1.00 12.62 ? 313  TYR B O   1 
ATOM   6231 C  CB  . TYR B 1 314 ? -14.573 1.936   65.204  1.00 10.76 ? 313  TYR B CB  1 
ATOM   6232 C  CG  . TYR B 1 314 ? -15.613 0.972   65.760  1.00 12.05 ? 313  TYR B CG  1 
ATOM   6233 C  CD1 . TYR B 1 314 ? -15.991 1.017   67.107  1.00 13.92 ? 313  TYR B CD1 1 
ATOM   6234 C  CD2 . TYR B 1 314 ? -16.217 0.013   64.940  1.00 12.15 ? 313  TYR B CD2 1 
ATOM   6235 C  CE1 . TYR B 1 314 ? -16.935 0.116   67.621  1.00 11.75 ? 313  TYR B CE1 1 
ATOM   6236 C  CE2 . TYR B 1 314 ? -17.159 -0.882  65.439  1.00 11.82 ? 313  TYR B CE2 1 
ATOM   6237 C  CZ  . TYR B 1 314 ? -17.517 -0.828  66.776  1.00 12.67 ? 313  TYR B CZ  1 
ATOM   6238 O  OH  . TYR B 1 314 ? -18.451 -1.720  67.254  1.00 12.83 ? 313  TYR B OH  1 
ATOM   6239 N  N   . VAL B 1 315 ? -12.346 0.427   63.355  1.00 10.73 ? 314  VAL B N   1 
ATOM   6240 C  CA  . VAL B 1 315 ? -11.869 -0.709  62.567  1.00 11.03 ? 314  VAL B CA  1 
ATOM   6241 C  C   . VAL B 1 315 ? -10.761 -1.437  63.325  1.00 12.61 ? 314  VAL B C   1 
ATOM   6242 O  O   . VAL B 1 315 ? -10.738 -2.676  63.395  1.00 10.86 ? 314  VAL B O   1 
ATOM   6243 C  CB  . VAL B 1 315 ? -11.410 -0.239  61.171  1.00 11.10 ? 314  VAL B CB  1 
ATOM   6244 C  CG1 . VAL B 1 315 ? -10.841 -1.411  60.357  1.00 11.95 ? 314  VAL B CG1 1 
ATOM   6245 C  CG2 . VAL B 1 315 ? -12.585 0.390   60.411  1.00 11.92 ? 314  VAL B CG2 1 
ATOM   6246 N  N   . GLY B 1 316 ? -9.842  -0.676  63.934  1.00 12.52 ? 315  GLY B N   1 
ATOM   6247 C  CA  . GLY B 1 316 ? -8.797  -1.294  64.738  1.00 12.53 ? 315  GLY B CA  1 
ATOM   6248 C  C   . GLY B 1 316 ? -9.342  -2.045  65.939  1.00 13.75 ? 315  GLY B C   1 
ATOM   6249 O  O   . GLY B 1 316 ? -8.821  -3.101  66.310  1.00 13.51 ? 315  GLY B O   1 
ATOM   6250 N  N   . MET B 1 317 ? -10.403 -1.519  66.556  1.00 11.58 ? 316  MET B N   1 
ATOM   6251 C  CA  . MET B 1 317 ? -11.033 -2.224  67.677  1.00 12.61 ? 316  MET B CA  1 
ATOM   6252 C  C   . MET B 1 317 ? -11.685 -3.529  67.224  1.00 12.63 ? 316  MET B C   1 
ATOM   6253 O  O   . MET B 1 317 ? -11.656 -4.533  67.951  1.00 12.42 ? 316  MET B O   1 
ATOM   6254 C  CB  . MET B 1 317 ? -12.063 -1.316  68.357  1.00 13.48 ? 316  MET B CB  1 
ATOM   6255 C  CG  . MET B 1 317 ? -11.462 -0.051  68.999  1.00 13.10 ? 316  MET B CG  1 
ATOM   6256 S  SD  . MET B 1 317 ? -12.661 1.267   69.344  1.00 19.02 ? 316  MET B SD  1 
ATOM   6257 C  CE  . MET B 1 317 ? -13.977 0.377   70.154  1.00 20.47 ? 316  MET B CE  1 
ATOM   6258 N  N   . VAL B 1 318 ? -12.307 -3.529  66.043  1.00 10.39 ? 317  VAL B N   1 
ATOM   6259 C  CA  . VAL B 1 318 ? -12.859 -4.762  65.483  1.00 9.59  ? 317  VAL B CA  1 
ATOM   6260 C  C   . VAL B 1 318 ? -11.765 -5.810  65.332  1.00 11.56 ? 317  VAL B C   1 
ATOM   6261 O  O   . VAL B 1 318 ? -11.956 -6.993  65.641  1.00 12.75 ? 317  VAL B O   1 
ATOM   6262 C  CB  . VAL B 1 318 ? -13.537 -4.469  64.127  1.00 10.21 ? 317  VAL B CB  1 
ATOM   6263 C  CG1 . VAL B 1 318 ? -13.790 -5.777  63.342  1.00 11.33 ? 317  VAL B CG1 1 
ATOM   6264 C  CG2 . VAL B 1 318 ? -14.836 -3.665  64.337  1.00 12.07 ? 317  VAL B CG2 1 
ATOM   6265 N  N   . LEU B 1 319 ? -10.615 -5.402  64.796  1.00 9.32  ? 318  LEU B N   1 
ATOM   6266 C  CA  . LEU B 1 319 ? -9.532  -6.359  64.588  1.00 10.07 ? 318  LEU B CA  1 
ATOM   6267 C  C   . LEU B 1 319 ? -9.010  -6.909  65.916  1.00 11.52 ? 318  LEU B C   1 
ATOM   6268 O  O   . LEU B 1 319 ? -8.758  -8.115  66.039  1.00 11.03 ? 318  LEU B O   1 
ATOM   6269 C  CB  . LEU B 1 319 ? -8.407  -5.700  63.786  1.00 12.06 ? 318  LEU B CB  1 
ATOM   6270 C  CG  . LEU B 1 319 ? -8.790  -5.385  62.335  1.00 11.74 ? 318  LEU B CG  1 
ATOM   6271 C  CD1 . LEU B 1 319 ? -7.802  -4.416  61.731  1.00 13.55 ? 318  LEU B CD1 1 
ATOM   6272 C  CD2 . LEU B 1 319 ? -8.864  -6.656  61.504  1.00 11.85 ? 318  LEU B CD2 1 
ATOM   6273 N  N   . ASN B 1 320 ? -8.850  -6.047  66.928  1.00 10.44 ? 319  ASN B N   1 
ATOM   6274 C  CA  . ASN B 1 320 ? -8.392  -6.547  68.224  1.00 11.30 ? 319  ASN B CA  1 
ATOM   6275 C  C   . ASN B 1 320 ? -9.405  -7.495  68.850  1.00 11.06 ? 319  ASN B C   1 
ATOM   6276 O  O   . ASN B 1 320 ? -9.024  -8.490  69.484  1.00 11.38 ? 319  ASN B O   1 
ATOM   6277 C  CB  . ASN B 1 320 ? -8.085  -5.385  69.171  1.00 12.79 ? 319  ASN B CB  1 
ATOM   6278 C  CG  . ASN B 1 320 ? -6.715  -4.797  68.913  1.00 17.41 ? 319  ASN B CG  1 
ATOM   6279 O  OD1 . ASN B 1 320 ? -5.798  -5.517  68.514  1.00 17.83 ? 319  ASN B OD1 1 
ATOM   6280 N  ND2 . ASN B 1 320 ? -6.569  -3.495  69.117  1.00 20.58 ? 319  ASN B ND2 1 
ATOM   6281 N  N   . GLU B 1 321 ? -10.700 -7.201  68.702  1.00 10.52 ? 320  GLU B N   1 
ATOM   6282 C  CA  . GLU B 1 321 ? -11.720 -8.098  69.240  1.00 9.55  ? 320  GLU B CA  1 
ATOM   6283 C  C   . GLU B 1 321 ? -11.731 -9.434  68.495  1.00 12.86 ? 320  GLU B C   1 
ATOM   6284 O  O   . GLU B 1 321 ? -11.964 -10.483 69.108  1.00 11.61 ? 320  GLU B O   1 
ATOM   6285 C  CB  . GLU B 1 321 ? -13.095 -7.406  69.199  1.00 11.48 ? 320  GLU B CB  1 
ATOM   6286 C  CG  . GLU B 1 321 ? -14.282 -8.203  69.768  1.00 11.56 ? 320  GLU B CG  1 
ATOM   6287 C  CD  . GLU B 1 321 ? -14.258 -8.408  71.285  1.00 11.08 ? 320  GLU B CD  1 
ATOM   6288 O  OE1 . GLU B 1 321 ? -13.197 -8.221  71.931  1.00 11.74 ? 320  GLU B OE1 1 
ATOM   6289 O  OE2 . GLU B 1 321 ? -15.321 -8.776  71.827  1.00 12.63 ? 320  GLU B OE2 1 
ATOM   6290 N  N   . ALA B 1 322 ? -11.433 -9.432  67.192  1.00 11.97 ? 321  ALA B N   1 
ATOM   6291 C  CA  . ALA B 1 322 ? -11.291 -10.699 66.478  1.00 10.43 ? 321  ALA B CA  1 
ATOM   6292 C  C   . ALA B 1 322 ? -10.055 -11.463 66.943  1.00 11.08 ? 321  ALA B C   1 
ATOM   6293 O  O   . ALA B 1 322 ? -10.084 -12.698 67.048  1.00 12.98 ? 321  ALA B O   1 
ATOM   6294 C  CB  . ALA B 1 322 ? -11.238 -10.454 64.967  1.00 10.33 ? 321  ALA B CB  1 
ATOM   6295 N  N   . LEU B 1 323 ? -8.954  -10.751 67.215  1.00 10.55 ? 322  LEU B N   1 
ATOM   6296 C  CA  . LEU B 1 323 ? -7.783  -11.399 67.806  1.00 9.36  ? 322  LEU B CA  1 
ATOM   6297 C  C   . LEU B 1 323 ? -8.058  -11.893 69.225  1.00 10.62 ? 322  LEU B C   1 
ATOM   6298 O  O   . LEU B 1 323 ? -7.427  -12.857 69.675  1.00 13.39 ? 322  LEU B O   1 
ATOM   6299 C  CB  . LEU B 1 323 ? -6.588  -10.449 67.827  1.00 11.11 ? 322  LEU B CB  1 
ATOM   6300 C  CG  . LEU B 1 323 ? -5.926  -10.129 66.479  1.00 10.79 ? 322  LEU B CG  1 
ATOM   6301 C  CD1 . LEU B 1 323 ? -4.777  -9.146  66.684  1.00 12.53 ? 322  LEU B CD1 1 
ATOM   6302 C  CD2 . LEU B 1 323 ? -5.443  -11.431 65.816  1.00 12.51 ? 322  LEU B CD2 1 
ATOM   6303 N  N   . ARG B 1 324 ? -8.966  -11.243 69.956  1.00 10.62 ? 323  ARG B N   1 
ATOM   6304 C  CA  . ARG B 1 324 ? -9.285  -11.740 71.291  1.00 10.61 ? 323  ARG B CA  1 
ATOM   6305 C  C   . ARG B 1 324 ? -9.948  -13.108 71.202  1.00 11.46 ? 323  ARG B C   1 
ATOM   6306 O  O   . ARG B 1 324 ? -9.519  -14.057 71.859  1.00 12.67 ? 323  ARG B O   1 
ATOM   6307 C  CB  . ARG B 1 324 ? -10.185 -10.757 72.054  1.00 11.97 ? 323  ARG B CB  1 
ATOM   6308 C  CG  . ARG B 1 324 ? -10.420 -11.187 73.521  1.00 9.73  ? 323  ARG B CG  1 
ATOM   6309 C  CD  . ARG B 1 324 ? -11.418 -10.280 74.281  1.00 9.82  ? 323  ARG B CD  1 
ATOM   6310 N  NE  . ARG B 1 324 ? -12.776 -10.350 73.737  1.00 10.50 ? 323  ARG B NE  1 
ATOM   6311 C  CZ  . ARG B 1 324 ? -13.647 -11.316 74.011  1.00 11.09 ? 323  ARG B CZ  1 
ATOM   6312 N  NH1 . ARG B 1 324 ? -13.351 -12.303 74.852  1.00 13.49 ? 323  ARG B NH1 1 
ATOM   6313 N  NH2 . ARG B 1 324 ? -14.839 -11.306 73.414  1.00 11.24 ? 323  ARG B NH2 1 
ATOM   6314 N  N   . LEU B 1 325 ? -10.983 -13.241 70.369  1.00 12.20 ? 324  LEU B N   1 
ATOM   6315 C  CA  . LEU B 1 325 ? -11.710 -14.510 70.361  1.00 11.27 ? 324  LEU B CA  1 
ATOM   6316 C  C   . LEU B 1 325 ? -10.940 -15.606 69.633  1.00 12.39 ? 324  LEU B C   1 
ATOM   6317 O  O   . LEU B 1 325 ? -10.934 -16.759 70.085  1.00 12.51 ? 324  LEU B O   1 
ATOM   6318 C  CB  . LEU B 1 325 ? -13.106 -14.321 69.763  1.00 11.42 ? 324  LEU B CB  1 
ATOM   6319 C  CG  . LEU B 1 325 ? -14.114 -13.649 70.716  1.00 12.98 ? 324  LEU B CG  1 
ATOM   6320 C  CD1 . LEU B 1 325 ? -15.334 -13.125 69.981  1.00 15.52 ? 324  LEU B CD1 1 
ATOM   6321 C  CD2 . LEU B 1 325 ? -14.556 -14.601 71.857  1.00 14.01 ? 324  LEU B CD2 1 
ATOM   6322 N  N   . TRP B 1 326 ? -10.277 -15.289 68.519  1.00 10.77 ? 325  TRP B N   1 
ATOM   6323 C  CA  . TRP B 1 326 ? -9.573  -16.301 67.722  1.00 10.81 ? 325  TRP B CA  1 
ATOM   6324 C  C   . TRP B 1 326 ? -8.181  -15.822 67.328  1.00 11.55 ? 325  TRP B C   1 
ATOM   6325 O  O   . TRP B 1 326 ? -7.894  -15.582 66.149  1.00 13.41 ? 325  TRP B O   1 
ATOM   6326 C  CB  . TRP B 1 326 ? -10.407 -16.702 66.498  1.00 11.67 ? 325  TRP B CB  1 
ATOM   6327 C  CG  . TRP B 1 326 ? -11.602 -17.476 66.957  1.00 11.50 ? 325  TRP B CG  1 
ATOM   6328 C  CD1 . TRP B 1 326 ? -12.911 -17.073 66.935  1.00 13.61 ? 325  TRP B CD1 1 
ATOM   6329 C  CD2 . TRP B 1 326 ? -11.589 -18.761 67.602  1.00 13.50 ? 325  TRP B CD2 1 
ATOM   6330 N  NE1 . TRP B 1 326 ? -13.715 -18.042 67.506  1.00 11.96 ? 325  TRP B NE1 1 
ATOM   6331 C  CE2 . TRP B 1 326 ? -12.927 -19.087 67.919  1.00 13.44 ? 325  TRP B CE2 1 
ATOM   6332 C  CE3 . TRP B 1 326 ? -10.578 -19.674 67.923  1.00 12.26 ? 325  TRP B CE3 1 
ATOM   6333 C  CZ2 . TRP B 1 326 ? -13.276 -20.280 68.548  1.00 14.14 ? 325  TRP B CZ2 1 
ATOM   6334 C  CZ3 . TRP B 1 326 ? -10.926 -20.864 68.547  1.00 14.08 ? 325  TRP B CZ3 1 
ATOM   6335 C  CH2 . TRP B 1 326 ? -12.264 -21.159 68.847  1.00 14.76 ? 325  TRP B CH2 1 
ATOM   6336 N  N   . PRO B 1 327 ? -7.265  -15.742 68.289  1.00 12.95 ? 326  PRO B N   1 
ATOM   6337 C  CA  . PRO B 1 327 ? -5.871  -15.397 67.952  1.00 10.53 ? 326  PRO B CA  1 
ATOM   6338 C  C   . PRO B 1 327 ? -5.296  -16.428 66.991  1.00 10.83 ? 326  PRO B C   1 
ATOM   6339 O  O   . PRO B 1 327 ? -5.309  -17.630 67.264  1.00 12.16 ? 326  PRO B O   1 
ATOM   6340 C  CB  . PRO B 1 327 ? -5.164  -15.415 69.311  1.00 11.40 ? 326  PRO B CB  1 
ATOM   6341 C  CG  . PRO B 1 327 ? -6.030  -16.289 70.201  1.00 9.78  ? 326  PRO B CG  1 
ATOM   6342 C  CD  . PRO B 1 327 ? -7.444  -16.090 69.713  1.00 10.10 ? 326  PRO B CD  1 
ATOM   6343 N  N   . THR B 1 328 ? -4.789  -15.955 65.846  1.00 9.68  ? 327  THR B N   1 
ATOM   6344 C  CA  . THR B 1 328 ? -4.573  -16.895 64.747  1.00 8.55  ? 327  THR B CA  1 
ATOM   6345 C  C   . THR B 1 328 ? -3.271  -17.680 64.857  1.00 9.17  ? 327  THR B C   1 
ATOM   6346 O  O   . THR B 1 328 ? -3.108  -18.670 64.134  1.00 13.42 ? 327  THR B O   1 
ATOM   6347 C  CB  . THR B 1 328 ? -4.645  -16.168 63.402  1.00 9.34  ? 327  THR B CB  1 
ATOM   6348 O  OG1 . THR B 1 328 ? -3.844  -14.979 63.441  1.00 11.93 ? 327  THR B OG1 1 
ATOM   6349 C  CG2 . THR B 1 328 ? -6.093  -15.795 63.094  1.00 9.92  ? 327  THR B CG2 1 
ATOM   6350 N  N   . ALA B 1 329 ? -2.355  -17.280 65.743  1.00 9.38  ? 328  ALA B N   1 
ATOM   6351 C  CA  . ALA B 1 329 ? -1.236  -18.115 66.181  1.00 9.85  ? 328  ALA B CA  1 
ATOM   6352 C  C   . ALA B 1 329 ? -1.527  -18.461 67.638  1.00 11.35 ? 328  ALA B C   1 
ATOM   6353 O  O   . ALA B 1 329 ? -1.118  -17.728 68.551  1.00 14.46 ? 328  ALA B O   1 
ATOM   6354 C  CB  . ALA B 1 329 ? 0.106   -17.390 66.033  1.00 12.02 ? 328  ALA B CB  1 
ATOM   6355 N  N   . PRO B 1 330 ? -2.243  -19.556 67.908  1.00 11.93 ? 329  PRO B N   1 
ATOM   6356 C  CA  . PRO B 1 330 ? -3.044  -19.644 69.142  1.00 11.76 ? 329  PRO B CA  1 
ATOM   6357 C  C   . PRO B 1 330 ? -2.308  -20.088 70.397  1.00 11.63 ? 329  PRO B C   1 
ATOM   6358 O  O   . PRO B 1 330 ? -2.952  -20.198 71.453  1.00 11.74 ? 329  PRO B O   1 
ATOM   6359 C  CB  . PRO B 1 330 ? -4.120  -20.669 68.763  1.00 12.12 ? 329  PRO B CB  1 
ATOM   6360 C  CG  . PRO B 1 330 ? -3.438  -21.550 67.760  1.00 13.43 ? 329  PRO B CG  1 
ATOM   6361 C  CD  . PRO B 1 330 ? -2.583  -20.620 66.944  1.00 11.90 ? 329  PRO B CD  1 
ATOM   6362 N  N   . ALA B 1 331 ? -1.006  -20.351 70.343  1.00 11.32 ? 330  ALA B N   1 
ATOM   6363 C  CA  . ALA B 1 331 ? -0.295  -20.743 71.552  1.00 9.03  ? 330  ALA B CA  1 
ATOM   6364 C  C   . ALA B 1 331 ? 1.164   -20.353 71.424  1.00 11.32 ? 330  ALA B C   1 
ATOM   6365 O  O   . ALA B 1 331 ? 1.690   -20.175 70.320  1.00 13.28 ? 330  ALA B O   1 
ATOM   6366 C  CB  . ALA B 1 331 ? -0.428  -22.251 71.823  1.00 9.69  ? 330  ALA B CB  1 
ATOM   6367 N  N   . PHE B 1 332 ? 1.823   -20.215 72.572  1.00 10.10 ? 331  PHE B N   1 
ATOM   6368 C  CA  . PHE B 1 332 ? 3.278   -20.145 72.586  1.00 10.97 ? 331  PHE B CA  1 
ATOM   6369 C  C   . PHE B 1 332 ? 3.777   -20.892 73.814  1.00 14.82 ? 331  PHE B C   1 
ATOM   6370 O  O   . PHE B 1 332 ? 3.003   -21.229 74.716  1.00 15.52 ? 331  PHE B O   1 
ATOM   6371 C  CB  . PHE B 1 332 ? 3.811   -18.697 72.496  1.00 12.66 ? 331  PHE B CB  1 
ATOM   6372 C  CG  . PHE B 1 332 ? 3.317   -17.748 73.568  1.00 12.11 ? 331  PHE B CG  1 
ATOM   6373 C  CD1 . PHE B 1 332 ? 2.143   -17.026 73.394  1.00 13.17 ? 331  PHE B CD1 1 
ATOM   6374 C  CD2 . PHE B 1 332 ? 4.083   -17.500 74.697  1.00 13.28 ? 331  PHE B CD2 1 
ATOM   6375 C  CE1 . PHE B 1 332 ? 1.702   -16.126 74.351  1.00 14.79 ? 331  PHE B CE1 1 
ATOM   6376 C  CE2 . PHE B 1 332 ? 3.653   -16.597 75.673  1.00 14.95 ? 331  PHE B CE2 1 
ATOM   6377 C  CZ  . PHE B 1 332 ? 2.461   -15.900 75.495  1.00 14.66 ? 331  PHE B CZ  1 
ATOM   6378 N  N   . SER B 1 333 ? 5.078   -21.194 73.813  1.00 12.92 ? 332  SER B N   1 
ATOM   6379 C  CA  . SER B 1 333 ? 5.673   -22.093 74.790  1.00 11.63 ? 332  SER B CA  1 
ATOM   6380 C  C   . SER B 1 333 ? 6.816   -21.409 75.530  1.00 10.75 ? 332  SER B C   1 
ATOM   6381 O  O   . SER B 1 333 ? 7.523   -20.574 74.970  1.00 11.39 ? 332  SER B O   1 
ATOM   6382 C  CB  . SER B 1 333 ? 6.182   -23.373 74.108  1.00 12.33 ? 332  SER B CB  1 
ATOM   6383 O  OG  . SER B 1 333 ? 6.547   -24.341 75.074  1.00 14.74 ? 332  SER B OG  1 
ATOM   6384 N  N   . LEU B 1 334 ? 7.005   -21.803 76.792  1.00 12.85 ? 333  LEU B N   1 
ATOM   6385 C  CA  . LEU B 1 334 ? 8.010   -21.228 77.677  1.00 11.33 ? 333  LEU B CA  1 
ATOM   6386 C  C   . LEU B 1 334 ? 8.689   -22.344 78.462  1.00 11.27 ? 333  LEU B C   1 
ATOM   6387 O  O   . LEU B 1 334 ? 8.130   -23.429 78.644  1.00 15.03 ? 333  LEU B O   1 
ATOM   6388 C  CB  . LEU B 1 334 ? 7.375   -20.221 78.648  1.00 14.39 ? 333  LEU B CB  1 
ATOM   6389 C  CG  . LEU B 1 334 ? 6.581   -19.105 77.953  1.00 16.32 ? 333  LEU B CG  1 
ATOM   6390 C  CD1 . LEU B 1 334 ? 5.526   -18.531 78.874  1.00 20.35 ? 333  LEU B CD1 1 
ATOM   6391 C  CD2 . LEU B 1 334 ? 7.514   -18.004 77.429  1.00 12.08 ? 333  LEU B CD2 1 
ATOM   6392 N  N   . TYR B 1 335 ? 9.916   -22.077 78.921  1.00 13.37 ? 334  TYR B N   1 
ATOM   6393 C  CA  . TYR B 1 335 ? 10.589  -22.969 79.857  1.00 13.58 ? 334  TYR B CA  1 
ATOM   6394 C  C   . TYR B 1 335 ? 11.103  -22.167 81.045  1.00 14.38 ? 334  TYR B C   1 
ATOM   6395 O  O   . TYR B 1 335 ? 11.430  -20.980 80.922  1.00 13.66 ? 334  TYR B O   1 
ATOM   6396 C  CB  . TYR B 1 335 ? 11.749  -23.757 79.192  1.00 12.92 ? 334  TYR B CB  1 
ATOM   6397 C  CG  . TYR B 1 335 ? 12.949  -22.909 78.846  1.00 14.79 ? 334  TYR B CG  1 
ATOM   6398 C  CD1 . TYR B 1 335 ? 13.034  -22.263 77.617  1.00 13.41 ? 334  TYR B CD1 1 
ATOM   6399 C  CD2 . TYR B 1 335 ? 13.998  -22.741 79.753  1.00 15.58 ? 334  TYR B CD2 1 
ATOM   6400 C  CE1 . TYR B 1 335 ? 14.129  -21.462 77.299  1.00 14.19 ? 334  TYR B CE1 1 
ATOM   6401 C  CE2 . TYR B 1 335 ? 15.091  -21.942 79.449  1.00 15.99 ? 334  TYR B CE2 1 
ATOM   6402 C  CZ  . TYR B 1 335 ? 15.153  -21.305 78.216  1.00 16.60 ? 334  TYR B CZ  1 
ATOM   6403 O  OH  . TYR B 1 335 ? 16.239  -20.513 77.905  1.00 19.02 ? 334  TYR B OH  1 
ATOM   6404 N  N   . ALA B 1 336 ? 11.146  -22.826 82.206  1.00 14.16 ? 335  ALA B N   1 
ATOM   6405 C  CA  . ALA B 1 336 ? 11.626  -22.206 83.438  1.00 16.19 ? 335  ALA B CA  1 
ATOM   6406 C  C   . ALA B 1 336 ? 13.145  -22.053 83.404  1.00 16.67 ? 335  ALA B C   1 
ATOM   6407 O  O   . ALA B 1 336 ? 13.874  -23.044 83.256  1.00 15.92 ? 335  ALA B O   1 
ATOM   6408 C  CB  . ALA B 1 336 ? 11.205  -23.045 84.647  1.00 16.24 ? 335  ALA B CB  1 
ATOM   6409 N  N   . LYS B 1 337 ? 13.629  -20.818 83.570  1.00 14.89 ? 336  LYS B N   1 
ATOM   6410 C  CA  . LYS B 1 337 ? 15.073  -20.587 83.567  1.00 16.74 ? 336  LYS B CA  1 
ATOM   6411 C  C   . LYS B 1 337 ? 15.742  -21.183 84.803  1.00 19.51 ? 336  LYS B C   1 
ATOM   6412 O  O   . LYS B 1 337 ? 16.889  -21.648 84.726  1.00 21.31 ? 336  LYS B O   1 
ATOM   6413 C  CB  . LYS B 1 337 ? 15.361  -19.086 83.467  1.00 17.40 ? 336  LYS B CB  1 
ATOM   6414 C  CG  . LYS B 1 337 ? 15.027  -18.493 82.102  1.00 19.13 ? 336  LYS B CG  1 
ATOM   6415 C  CD  . LYS B 1 337 ? 14.805  -16.979 82.168  1.00 21.48 ? 336  LYS B CD  1 
ATOM   6416 C  CE  . LYS B 1 337 ? 16.040  -16.250 82.677  1.00 22.58 ? 336  LYS B CE  1 
ATOM   6417 N  NZ  . LYS B 1 337 ? 17.199  -16.317 81.733  1.00 23.86 ? 336  LYS B NZ  1 
ATOM   6418 N  N   . GLU B 1 338 ? 15.047  -21.176 85.939  1.00 19.52 ? 337  GLU B N   1 
ATOM   6419 C  CA  . GLU B 1 338 ? 15.520  -21.778 87.179  1.00 19.62 ? 337  GLU B CA  1 
ATOM   6420 C  C   . GLU B 1 338 ? 14.326  -22.392 87.896  1.00 19.08 ? 337  GLU B C   1 
ATOM   6421 O  O   . GLU B 1 338 ? 13.170  -22.157 87.527  1.00 19.43 ? 337  GLU B O   1 
ATOM   6422 C  CB  . GLU B 1 338 ? 16.207  -20.750 88.089  1.00 22.05 ? 337  GLU B CB  1 
ATOM   6423 C  CG  . GLU B 1 338 ? 17.356  -19.986 87.440  1.00 24.33 ? 337  GLU B CG  1 
ATOM   6424 C  CD  . GLU B 1 338 ? 18.598  -20.841 87.220  1.00 28.62 ? 337  GLU B CD  1 
ATOM   6425 O  OE1 . GLU B 1 338 ? 18.692  -21.936 87.816  1.00 27.56 ? 337  GLU B OE1 1 
ATOM   6426 O  OE2 . GLU B 1 338 ? 19.483  -20.415 86.445  1.00 30.48 ? 337  GLU B OE2 1 
ATOM   6427 N  N   . ASP B 1 339 ? 14.607  -23.179 88.940  1.00 21.41 ? 338  ASP B N   1 
ATOM   6428 C  CA  . ASP B 1 339 ? 13.545  -23.610 89.842  1.00 21.08 ? 338  ASP B CA  1 
ATOM   6429 C  C   . ASP B 1 339 ? 12.726  -22.400 90.271  1.00 22.42 ? 338  ASP B C   1 
ATOM   6430 O  O   . ASP B 1 339 ? 13.278  -21.350 90.609  1.00 24.65 ? 338  ASP B O   1 
ATOM   6431 C  CB  . ASP B 1 339 ? 14.115  -24.289 91.097  1.00 21.82 ? 338  ASP B CB  1 
ATOM   6432 C  CG  . ASP B 1 339 ? 14.866  -25.579 90.809  1.00 24.23 ? 338  ASP B CG  1 
ATOM   6433 O  OD1 . ASP B 1 339 ? 14.842  -26.082 89.669  1.00 24.73 ? 338  ASP B OD1 1 
ATOM   6434 O  OD2 . ASP B 1 339 ? 15.495  -26.098 91.763  1.00 27.12 ? 338  ASP B OD2 1 
ATOM   6435 N  N   . THR B 1 340 ? 11.403  -22.553 90.279  1.00 21.17 ? 339  THR B N   1 
ATOM   6436 C  CA  . THR B 1 340 ? 10.527  -21.456 90.663  1.00 21.02 ? 339  THR B CA  1 
ATOM   6437 C  C   . THR B 1 340 ? 9.154   -22.034 90.978  1.00 22.08 ? 339  THR B C   1 
ATOM   6438 O  O   . THR B 1 340 ? 8.831   -23.154 90.574  1.00 26.15 ? 339  THR B O   1 
ATOM   6439 C  CB  . THR B 1 340 ? 10.451  -20.389 89.559  1.00 21.71 ? 339  THR B CB  1 
ATOM   6440 O  OG1 . THR B 1 340 ? 9.868   -19.191 90.083  1.00 23.30 ? 339  THR B OG1 1 
ATOM   6441 C  CG2 . THR B 1 340 ? 9.614   -20.882 88.378  1.00 21.47 ? 339  THR B CG2 1 
ATOM   6442 N  N   . VAL B 1 341 ? 8.350   -21.269 91.716  1.00 21.55 ? 340  VAL B N   1 
ATOM   6443 C  CA  . VAL B 1 341 ? 7.005   -21.692 92.095  1.00 21.92 ? 340  VAL B CA  1 
ATOM   6444 C  C   . VAL B 1 341 ? 6.011   -20.810 91.357  1.00 22.48 ? 340  VAL B C   1 
ATOM   6445 O  O   . VAL B 1 341 ? 6.031   -19.582 91.504  1.00 24.88 ? 340  VAL B O   1 
ATOM   6446 C  CB  . VAL B 1 341 ? 6.783   -21.622 93.614  1.00 23.92 ? 340  VAL B CB  1 
ATOM   6447 C  CG1 . VAL B 1 341 ? 5.360   -22.065 93.961  1.00 26.84 ? 340  VAL B CG1 1 
ATOM   6448 C  CG2 . VAL B 1 341 ? 7.802   -22.484 94.337  1.00 26.79 ? 340  VAL B CG2 1 
ATOM   6449 N  N   . LEU B 1 342 ? 5.140   -21.438 90.570  1.00 22.28 ? 341  LEU B N   1 
ATOM   6450 C  CA  . LEU B 1 342 ? 4.140   -20.732 89.783  1.00 21.75 ? 341  LEU B CA  1 
ATOM   6451 C  C   . LEU B 1 342 ? 2.882   -20.507 90.616  1.00 23.48 ? 341  LEU B C   1 
ATOM   6452 O  O   . LEU B 1 342 ? 2.300   -21.461 91.148  1.00 23.60 ? 341  LEU B O   1 
ATOM   6453 C  CB  . LEU B 1 342 ? 3.808   -21.524 88.523  1.00 22.43 ? 341  LEU B CB  1 
ATOM   6454 C  CG  . LEU B 1 342 ? 2.940   -20.849 87.465  1.00 20.32 ? 341  LEU B CG  1 
ATOM   6455 C  CD1 . LEU B 1 342 ? 3.664   -19.660 86.826  1.00 20.09 ? 341  LEU B CD1 1 
ATOM   6456 C  CD2 . LEU B 1 342 ? 2.563   -21.875 86.414  1.00 19.90 ? 341  LEU B CD2 1 
ATOM   6457 N  N   . GLY B 1 343 ? 2.469   -19.246 90.727  1.00 23.03 ? 342  GLY B N   1 
ATOM   6458 C  CA  . GLY B 1 343 ? 1.222   -18.912 91.390  1.00 24.03 ? 342  GLY B CA  1 
ATOM   6459 C  C   . GLY B 1 343 ? 1.156   -19.291 92.850  1.00 23.39 ? 342  GLY B C   1 
ATOM   6460 O  O   . GLY B 1 343 ? 0.056   -19.471 93.383  1.00 23.52 ? 342  GLY B O   1 
ATOM   6461 N  N   . GLY B 1 344 ? 2.305   -19.417 93.517  1.00 20.43 ? 343  GLY B N   1 
ATOM   6462 C  CA  . GLY B 1 344 ? 2.344   -19.812 94.913  1.00 21.09 ? 343  GLY B CA  1 
ATOM   6463 C  C   . GLY B 1 344 ? 1.908   -21.231 95.180  1.00 23.44 ? 343  GLY B C   1 
ATOM   6464 O  O   . GLY B 1 344 ? 1.790   -21.622 96.351  1.00 27.78 ? 343  GLY B O   1 
ATOM   6465 N  N   . GLU B 1 345 ? 1.692   -22.026 94.135  1.00 22.50 ? 344  GLU B N   1 
ATOM   6466 C  CA  . GLU B 1 345 ? 1.044   -23.327 94.277  1.00 23.83 ? 344  GLU B CA  1 
ATOM   6467 C  C   . GLU B 1 345 ? 1.692   -24.449 93.479  1.00 23.72 ? 344  GLU B C   1 
ATOM   6468 O  O   . GLU B 1 345 ? 1.577   -25.606 93.891  1.00 22.88 ? 344  GLU B O   1 
ATOM   6469 C  CB  . GLU B 1 345 ? -0.431  -23.223 93.863  1.00 28.58 ? 344  GLU B CB  1 
ATOM   6470 C  CG  . GLU B 1 345 ? -1.229  -22.239 94.693  1.00 32.93 ? 344  GLU B CG  1 
ATOM   6471 C  CD  . GLU B 1 345 ? -2.655  -22.086 94.211  1.00 38.00 ? 344  GLU B CD  1 
ATOM   6472 O  OE1 . GLU B 1 345 ? -2.905  -22.306 93.012  1.00 37.36 ? 344  GLU B OE1 1 
ATOM   6473 O  OE2 . GLU B 1 345 ? -3.526  -21.745 95.039  1.00 42.52 ? 344  GLU B OE2 1 
ATOM   6474 N  N   . TYR B 1 346 ? 2.359   -24.165 92.362  1.00 21.30 ? 345  TYR B N   1 
ATOM   6475 C  CA  . TYR B 1 346 ? 2.848   -25.204 91.454  1.00 19.32 ? 345  TYR B CA  1 
ATOM   6476 C  C   . TYR B 1 346 ? 4.362   -25.127 91.325  1.00 20.25 ? 345  TYR B C   1 
ATOM   6477 O  O   . TYR B 1 346 ? 4.886   -24.290 90.568  1.00 21.43 ? 345  TYR B O   1 
ATOM   6478 C  CB  . TYR B 1 346 ? 2.174   -25.070 90.088  1.00 22.04 ? 345  TYR B CB  1 
ATOM   6479 C  CG  . TYR B 1 346 ? 0.672   -25.157 90.206  1.00 21.96 ? 345  TYR B CG  1 
ATOM   6480 C  CD1 . TYR B 1 346 ? 0.053   -26.373 90.460  1.00 24.12 ? 345  TYR B CD1 1 
ATOM   6481 C  CD2 . TYR B 1 346 ? -0.126  -24.023 90.097  1.00 22.43 ? 345  TYR B CD2 1 
ATOM   6482 C  CE1 . TYR B 1 346 ? -1.317  -26.465 90.589  1.00 23.65 ? 345  TYR B CE1 1 
ATOM   6483 C  CE2 . TYR B 1 346 ? -1.496  -24.103 90.221  1.00 24.33 ? 345  TYR B CE2 1 
ATOM   6484 C  CZ  . TYR B 1 346 ? -2.089  -25.327 90.468  1.00 25.97 ? 345  TYR B CZ  1 
ATOM   6485 O  OH  . TYR B 1 346 ? -3.457  -25.414 90.600  1.00 27.87 ? 345  TYR B OH  1 
ATOM   6486 N  N   . PRO B 1 347 ? 5.105   -25.961 92.049  1.00 23.44 ? 346  PRO B N   1 
ATOM   6487 C  CA  . PRO B 1 347 ? 6.569   -25.921 91.946  1.00 23.64 ? 346  PRO B CA  1 
ATOM   6488 C  C   . PRO B 1 347 ? 7.040   -26.415 90.587  1.00 21.96 ? 346  PRO B C   1 
ATOM   6489 O  O   . PRO B 1 347 ? 6.584   -27.445 90.085  1.00 25.14 ? 346  PRO B O   1 
ATOM   6490 C  CB  . PRO B 1 347 ? 7.036   -26.856 93.074  1.00 25.15 ? 346  PRO B CB  1 
ATOM   6491 C  CG  . PRO B 1 347 ? 5.846   -27.021 93.973  1.00 26.78 ? 346  PRO B CG  1 
ATOM   6492 C  CD  . PRO B 1 347 ? 4.644   -26.903 93.084  1.00 24.59 ? 346  PRO B CD  1 
ATOM   6493 N  N   . LEU B 1 348 ? 7.966   -25.668 89.993  1.00 21.14 ? 347  LEU B N   1 
ATOM   6494 C  CA  . LEU B 1 348 ? 8.573   -26.035 88.723  1.00 19.41 ? 347  LEU B CA  1 
ATOM   6495 C  C   . LEU B 1 348 ? 10.080  -26.158 88.889  1.00 20.97 ? 347  LEU B C   1 
ATOM   6496 O  O   . LEU B 1 348 ? 10.701  -25.404 89.650  1.00 21.46 ? 347  LEU B O   1 
ATOM   6497 C  CB  . LEU B 1 348 ? 8.264   -25.002 87.628  1.00 18.83 ? 347  LEU B CB  1 
ATOM   6498 C  CG  . LEU B 1 348 ? 6.797   -24.730 87.307  1.00 18.13 ? 347  LEU B CG  1 
ATOM   6499 C  CD1 . LEU B 1 348 ? 6.701   -23.590 86.305  1.00 17.54 ? 347  LEU B CD1 1 
ATOM   6500 C  CD2 . LEU B 1 348 ? 6.096   -25.995 86.782  1.00 17.27 ? 347  LEU B CD2 1 
ATOM   6501 N  N   . GLU B 1 349 ? 10.663  -27.104 88.168  1.00 18.55 ? 348  GLU B N   1 
ATOM   6502 C  CA  . GLU B 1 349 ? 12.106  -27.274 88.127  1.00 19.28 ? 348  GLU B CA  1 
ATOM   6503 C  C   . GLU B 1 349 ? 12.665  -26.617 86.871  1.00 17.19 ? 348  GLU B C   1 
ATOM   6504 O  O   . GLU B 1 349 ? 11.986  -26.526 85.844  1.00 18.05 ? 348  GLU B O   1 
ATOM   6505 C  CB  . GLU B 1 349 ? 12.473  -28.759 88.166  1.00 24.07 ? 348  GLU B CB  1 
ATOM   6506 C  CG  . GLU B 1 349 ? 12.087  -29.421 89.482  1.00 32.46 ? 348  GLU B CG  1 
ATOM   6507 C  CD  . GLU B 1 349 ? 12.393  -30.901 89.512  1.00 41.11 ? 348  GLU B CD  1 
ATOM   6508 O  OE1 . GLU B 1 349 ? 12.723  -31.463 88.453  1.00 45.56 ? 348  GLU B OE1 1 
ATOM   6509 O  OE2 . GLU B 1 349 ? 12.302  -31.504 90.599  1.00 44.30 ? 348  GLU B OE2 1 
ATOM   6510 N  N   . LYS B 1 350 ? 13.901  -26.131 86.975  1.00 19.09 ? 349  LYS B N   1 
ATOM   6511 C  CA  . LYS B 1 350 ? 14.608  -25.573 85.830  1.00 18.02 ? 349  LYS B CA  1 
ATOM   6512 C  C   . LYS B 1 350 ? 14.418  -26.460 84.609  1.00 20.29 ? 349  LYS B C   1 
ATOM   6513 O  O   . LYS B 1 350 ? 14.620  -27.676 84.672  1.00 19.98 ? 349  LYS B O   1 
ATOM   6514 C  CB  . LYS B 1 350 ? 16.100  -25.437 86.151  1.00 20.52 ? 349  LYS B CB  1 
ATOM   6515 C  CG  . LYS B 1 350 ? 16.982  -25.032 84.972  1.00 21.39 ? 349  LYS B CG  1 
ATOM   6516 C  CD  . LYS B 1 350 ? 18.451  -24.987 85.390  1.00 23.68 ? 349  LYS B CD  1 
ATOM   6517 C  CE  . LYS B 1 350 ? 19.341  -24.464 84.273  1.00 27.16 ? 349  LYS B CE  1 
ATOM   6518 N  NZ  . LYS B 1 350 ? 20.781  -24.490 84.686  1.00 31.47 ? 349  LYS B NZ  1 
ATOM   6519 N  N   . GLY B 1 351 ? 14.004  -25.845 83.500  1.00 17.45 ? 350  GLY B N   1 
ATOM   6520 C  CA  . GLY B 1 351 ? 13.771  -26.561 82.268  1.00 16.67 ? 350  GLY B CA  1 
ATOM   6521 C  C   . GLY B 1 351 ? 12.344  -27.022 82.042  1.00 15.80 ? 350  GLY B C   1 
ATOM   6522 O  O   . GLY B 1 351 ? 12.005  -27.387 80.911  1.00 16.74 ? 350  GLY B O   1 
ATOM   6523 N  N   . ASP B 1 352 ? 11.499  -27.018 83.078  1.00 16.23 ? 351  ASP B N   1 
ATOM   6524 C  CA  . ASP B 1 352 ? 10.101  -27.401 82.910  1.00 15.36 ? 351  ASP B CA  1 
ATOM   6525 C  C   . ASP B 1 352 ? 9.398   -26.465 81.929  1.00 16.15 ? 351  ASP B C   1 
ATOM   6526 O  O   . ASP B 1 352 ? 9.599   -25.248 81.960  1.00 17.46 ? 351  ASP B O   1 
ATOM   6527 C  CB  . ASP B 1 352 ? 9.369   -27.366 84.260  1.00 16.53 ? 351  ASP B CB  1 
ATOM   6528 C  CG  . ASP B 1 352 ? 9.636   -28.595 85.128  1.00 18.82 ? 351  ASP B CG  1 
ATOM   6529 O  OD1 . ASP B 1 352 ? 10.304  -29.545 84.666  1.00 18.53 ? 351  ASP B OD1 1 
ATOM   6530 O  OD2 . ASP B 1 352 ? 9.159   -28.608 86.289  1.00 20.46 ? 351  ASP B OD2 1 
ATOM   6531 N  N   . GLU B 1 353 ? 8.525   -27.035 81.092  1.00 17.58 ? 352  GLU B N   1 
ATOM   6532 C  CA  . GLU B 1 353 ? 7.875   -26.318 80.003  1.00 15.62 ? 352  GLU B CA  1 
ATOM   6533 C  C   . GLU B 1 353 ? 6.436   -25.939 80.339  1.00 16.08 ? 352  GLU B C   1 
ATOM   6534 O  O   . GLU B 1 353 ? 5.756   -26.611 81.124  1.00 17.49 ? 352  GLU B O   1 
ATOM   6535 C  CB  . GLU B 1 353 ? 7.882   -27.165 78.726  1.00 19.05 ? 352  GLU B CB  1 
ATOM   6536 C  CG  . GLU B 1 353 ? 9.272   -27.567 78.264  1.00 26.87 ? 352  GLU B CG  1 
ATOM   6537 C  CD  . GLU B 1 353 ? 9.263   -28.522 77.076  1.00 32.92 ? 352  GLU B CD  1 
ATOM   6538 O  OE1 . GLU B 1 353 ? 8.182   -28.757 76.481  1.00 30.93 ? 352  GLU B OE1 1 
ATOM   6539 O  OE2 . GLU B 1 353 ? 10.355  -29.041 76.737  1.00 37.81 ? 352  GLU B OE2 1 
ATOM   6540 N  N   . LEU B 1 354 ? 5.980   -24.851 79.713  1.00 14.07 ? 353  LEU B N   1 
ATOM   6541 C  CA  . LEU B 1 354 ? 4.614   -24.353 79.796  1.00 13.43 ? 353  LEU B CA  1 
ATOM   6542 C  C   . LEU B 1 354 ? 4.097   -24.091 78.391  1.00 14.66 ? 353  LEU B C   1 
ATOM   6543 O  O   . LEU B 1 354 ? 4.861   -23.708 77.500  1.00 15.80 ? 353  LEU B O   1 
ATOM   6544 C  CB  . LEU B 1 354 ? 4.533   -23.043 80.601  1.00 14.48 ? 353  LEU B CB  1 
ATOM   6545 C  CG  . LEU B 1 354 ? 5.122   -23.037 82.013  1.00 15.31 ? 353  LEU B CG  1 
ATOM   6546 C  CD1 . LEU B 1 354 ? 5.205   -21.627 82.546  1.00 17.74 ? 353  LEU B CD1 1 
ATOM   6547 C  CD2 . LEU B 1 354 ? 4.272   -23.906 82.932  1.00 18.12 ? 353  LEU B CD2 1 
ATOM   6548 N  N   . MET B 1 355 ? 2.793   -24.292 78.197  1.00 12.70 ? 354  MET B N   1 
ATOM   6549 C  CA  . MET B 1 355 ? 2.096   -23.854 76.988  1.00 11.70 ? 354  MET B CA  1 
ATOM   6550 C  C   . MET B 1 355 ? 1.056   -22.810 77.374  1.00 13.24 ? 354  MET B C   1 
ATOM   6551 O  O   . MET B 1 355 ? 0.239   -23.050 78.271  1.00 14.19 ? 354  MET B O   1 
ATOM   6552 C  CB  . MET B 1 355 ? 1.405   -25.022 76.277  1.00 13.31 ? 354  MET B CB  1 
ATOM   6553 C  CG  . MET B 1 355 ? 2.329   -26.116 75.757  1.00 16.48 ? 354  MET B CG  1 
ATOM   6554 S  SD  . MET B 1 355 ? 3.378   -25.576 74.382  1.00 16.41 ? 354  MET B SD  1 
ATOM   6555 C  CE  . MET B 1 355 ? 2.170   -24.948 73.206  1.00 16.77 ? 354  MET B CE  1 
ATOM   6556 N  N   . VAL B 1 356 ? 1.059   -21.671 76.683  1.00 13.23 ? 355  VAL B N   1 
ATOM   6557 C  CA  . VAL B 1 356 ? 0.076   -20.615 76.913  1.00 12.20 ? 355  VAL B CA  1 
ATOM   6558 C  C   . VAL B 1 356 ? -1.042  -20.765 75.884  1.00 9.20  ? 355  VAL B C   1 
ATOM   6559 O  O   . VAL B 1 356 ? -0.803  -20.663 74.674  1.00 13.29 ? 355  VAL B O   1 
ATOM   6560 C  CB  . VAL B 1 356 ? 0.721   -19.221 76.838  1.00 13.65 ? 355  VAL B CB  1 
ATOM   6561 C  CG1 . VAL B 1 356 ? -0.345  -18.134 76.953  1.00 13.97 ? 355  VAL B CG1 1 
ATOM   6562 C  CG2 . VAL B 1 356 ? 1.784   -19.055 77.923  1.00 15.03 ? 355  VAL B CG2 1 
ATOM   6563 N  N   . LEU B 1 357 ? -2.262  -21.022 76.353  1.00 10.21 ? 356  LEU B N   1 
ATOM   6564 C  CA  . LEU B 1 357 ? -3.417  -21.233 75.475  1.00 12.22 ? 356  LEU B CA  1 
ATOM   6565 C  C   . LEU B 1 357 ? -4.115  -19.888 75.280  1.00 12.44 ? 356  LEU B C   1 
ATOM   6566 O  O   . LEU B 1 357 ? -4.989  -19.498 76.059  1.00 12.04 ? 356  LEU B O   1 
ATOM   6567 C  CB  . LEU B 1 357 ? -4.338  -22.286 76.083  1.00 18.37 ? 356  LEU B CB  1 
ATOM   6568 C  CG  . LEU B 1 357 ? -5.218  -23.202 75.247  1.00 23.44 ? 356  LEU B CG  1 
ATOM   6569 C  CD1 . LEU B 1 357 ? -4.454  -23.799 74.059  1.00 25.39 ? 356  LEU B CD1 1 
ATOM   6570 C  CD2 . LEU B 1 357 ? -5.758  -24.320 76.162  1.00 23.73 ? 356  LEU B CD2 1 
ATOM   6571 N  N   . ILE B 1 358 ? -3.729  -19.160 74.222  1.00 11.25 ? 357  ILE B N   1 
ATOM   6572 C  CA  . ILE B 1 358 ? -4.168  -17.763 74.084  1.00 9.87  ? 357  ILE B CA  1 
ATOM   6573 C  C   . ILE B 1 358 ? -5.685  -17.647 74.013  1.00 11.36 ? 357  ILE B C   1 
ATOM   6574 O  O   . ILE B 1 358 ? -6.241  -16.731 74.638  1.00 12.42 ? 357  ILE B O   1 
ATOM   6575 C  CB  . ILE B 1 358 ? -3.463  -17.092 72.899  1.00 9.81  ? 357  ILE B CB  1 
ATOM   6576 C  CG1 . ILE B 1 358 ? -1.945  -17.275 72.983  1.00 10.04 ? 357  ILE B CG1 1 
ATOM   6577 C  CG2 . ILE B 1 358 ? -3.744  -15.590 72.897  1.00 10.79 ? 357  ILE B CG2 1 
ATOM   6578 C  CD1 . ILE B 1 358 ? -1.223  -16.704 71.753  1.00 10.34 ? 357  ILE B CD1 1 
ATOM   6579 N  N   . PRO B 1 359 ? -6.411  -18.483 73.259  1.00 12.16 ? 358  PRO B N   1 
ATOM   6580 C  CA  . PRO B 1 359 ? -7.879  -18.335 73.232  1.00 10.89 ? 358  PRO B CA  1 
ATOM   6581 C  C   . PRO B 1 359 ? -8.509  -18.435 74.605  1.00 9.90  ? 358  PRO B C   1 
ATOM   6582 O  O   . PRO B 1 359 ? -9.536  -17.787 74.858  1.00 11.98 ? 358  PRO B O   1 
ATOM   6583 C  CB  . PRO B 1 359 ? -8.336  -19.484 72.321  1.00 10.32 ? 358  PRO B CB  1 
ATOM   6584 C  CG  . PRO B 1 359 ? -7.137  -19.762 71.438  1.00 10.29 ? 358  PRO B CG  1 
ATOM   6585 C  CD  . PRO B 1 359 ? -5.945  -19.555 72.357  1.00 11.50 ? 358  PRO B CD  1 
ATOM   6586 N  N   . GLN B 1 360 ? -7.931  -19.248 75.497  1.00 12.34 ? 359  GLN B N   1 
ATOM   6587 C  CA  . GLN B 1 360 ? -8.489  -19.378 76.839  1.00 14.23 ? 359  GLN B CA  1 
ATOM   6588 C  C   . GLN B 1 360 ? -8.145  -18.172 77.703  1.00 11.96 ? 359  GLN B C   1 
ATOM   6589 O  O   . GLN B 1 360 ? -8.998  -17.688 78.456  1.00 12.32 ? 359  GLN B O   1 
ATOM   6590 C  CB  . GLN B 1 360 ? -8.002  -20.667 77.500  1.00 13.64 ? 359  GLN B CB  1 
ATOM   6591 C  CG  . GLN B 1 360 ? -8.561  -21.945 76.877  1.00 16.98 ? 359  GLN B CG  1 
ATOM   6592 C  CD  . GLN B 1 360 ? -10.085 -21.976 76.874  1.00 17.68 ? 359  GLN B CD  1 
ATOM   6593 O  OE1 . GLN B 1 360 ? -10.718 -21.873 75.827  1.00 18.95 ? 359  GLN B OE1 1 
ATOM   6594 N  NE2 . GLN B 1 360 ? -10.672 -22.116 78.050  1.00 19.98 ? 359  GLN B NE2 1 
ATOM   6595 N  N   . LEU B 1 361 ? -6.902  -17.682 77.616  1.00 12.43 ? 360  LEU B N   1 
ATOM   6596 C  CA  . LEU B 1 361 ? -6.541  -16.429 78.272  1.00 13.57 ? 360  LEU B CA  1 
ATOM   6597 C  C   . LEU B 1 361 ? -7.558  -15.342 77.958  1.00 11.58 ? 360  LEU B C   1 
ATOM   6598 O  O   . LEU B 1 361 ? -8.035  -14.629 78.850  1.00 13.64 ? 360  LEU B O   1 
ATOM   6599 C  CB  . LEU B 1 361 ? -5.147  -15.982 77.821  1.00 12.52 ? 360  LEU B CB  1 
ATOM   6600 C  CG  . LEU B 1 361 ? -4.731  -14.578 78.272  1.00 11.73 ? 360  LEU B CG  1 
ATOM   6601 C  CD1 . LEU B 1 361 ? -4.528  -14.518 79.784  1.00 11.70 ? 360  LEU B CD1 1 
ATOM   6602 C  CD2 . LEU B 1 361 ? -3.471  -14.082 77.529  1.00 11.95 ? 360  LEU B CD2 1 
ATOM   6603 N  N   . HIS B 1 362 ? -7.915  -15.219 76.682  1.00 11.61 ? 361  HIS B N   1 
ATOM   6604 C  CA  . HIS B 1 362 ? -8.811  -14.188 76.181  1.00 12.76 ? 361  HIS B CA  1 
ATOM   6605 C  C   . HIS B 1 362 ? -10.266 -14.426 76.555  1.00 13.03 ? 361  HIS B C   1 
ATOM   6606 O  O   . HIS B 1 362 ? -11.118 -13.582 76.236  1.00 15.04 ? 361  HIS B O   1 
ATOM   6607 C  CB  . HIS B 1 362 ? -8.639  -14.096 74.664  1.00 11.52 ? 361  HIS B CB  1 
ATOM   6608 C  CG  . HIS B 1 362 ? -7.312  -13.538 74.246  1.00 10.81 ? 361  HIS B CG  1 
ATOM   6609 N  ND1 . HIS B 1 362 ? -6.898  -13.505 72.930  1.00 11.20 ? 361  HIS B ND1 1 
ATOM   6610 C  CD2 . HIS B 1 362 ? -6.308  -12.980 74.970  1.00 13.30 ? 361  HIS B CD2 1 
ATOM   6611 C  CE1 . HIS B 1 362 ? -5.700  -12.952 72.860  1.00 10.13 ? 361  HIS B CE1 1 
ATOM   6612 N  NE2 . HIS B 1 362 ? -5.315  -12.632 74.085  1.00 12.12 ? 361  HIS B NE2 1 
ATOM   6613 N  N   . ARG B 1 363 ? -10.561 -15.534 77.238  1.00 10.74 ? 362  ARG B N   1 
ATOM   6614 C  CA  . ARG B 1 363 ? -11.892 -15.836 77.747  1.00 11.44 ? 362  ARG B CA  1 
ATOM   6615 C  C   . ARG B 1 363 ? -11.929 -15.863 79.276  1.00 13.64 ? 362  ARG B C   1 
ATOM   6616 O  O   . ARG B 1 363 ? -12.907 -16.338 79.865  1.00 13.78 ? 362  ARG B O   1 
ATOM   6617 C  CB  . ARG B 1 363 ? -12.373 -17.169 77.157  1.00 11.67 ? 362  ARG B CB  1 
ATOM   6618 C  CG  . ARG B 1 363 ? -12.726 -17.097 75.653  1.00 12.93 ? 362  ARG B CG  1 
ATOM   6619 C  CD  . ARG B 1 363 ? -12.871 -18.496 75.029  1.00 13.32 ? 362  ARG B CD  1 
ATOM   6620 N  NE  . ARG B 1 363 ? -13.439 -18.466 73.682  1.00 14.06 ? 362  ARG B NE  1 
ATOM   6621 C  CZ  . ARG B 1 363 ? -12.761 -18.123 72.593  1.00 11.42 ? 362  ARG B CZ  1 
ATOM   6622 N  NH1 . ARG B 1 363 ? -11.497 -17.738 72.661  1.00 11.77 ? 362  ARG B NH1 1 
ATOM   6623 N  NH2 . ARG B 1 363 ? -13.372 -18.153 71.408  1.00 12.41 ? 362  ARG B NH2 1 
ATOM   6624 N  N   . ASP B 1 364 ? -10.887 -15.358 79.933  1.00 13.31 ? 363  ASP B N   1 
ATOM   6625 C  CA  . ASP B 1 364 ? -10.837 -15.306 81.395  1.00 12.72 ? 363  ASP B CA  1 
ATOM   6626 C  C   . ASP B 1 364 ? -11.896 -14.332 81.902  1.00 13.14 ? 363  ASP B C   1 
ATOM   6627 O  O   . ASP B 1 364 ? -11.756 -13.114 81.747  1.00 13.54 ? 363  ASP B O   1 
ATOM   6628 C  CB  . ASP B 1 364 ? -9.436  -14.892 81.837  1.00 13.17 ? 363  ASP B CB  1 
ATOM   6629 C  CG  . ASP B 1 364 ? -9.238  -14.954 83.345  1.00 15.17 ? 363  ASP B CG  1 
ATOM   6630 O  OD1 . ASP B 1 364 ? -10.232 -14.922 84.101  1.00 15.33 ? 363  ASP B OD1 1 
ATOM   6631 O  OD2 . ASP B 1 364 ? -8.070  -15.004 83.767  1.00 16.35 ? 363  ASP B OD2 1 
ATOM   6632 N  N   . LYS B 1 365 ? -12.960 -14.862 82.517  1.00 13.11 ? 364  LYS B N   1 
ATOM   6633 C  CA  . LYS B 1 365 ? -14.068 -14.016 82.944  1.00 15.24 ? 364  LYS B CA  1 
ATOM   6634 C  C   . LYS B 1 365 ? -13.690 -13.069 84.078  1.00 15.25 ? 364  LYS B C   1 
ATOM   6635 O  O   . LYS B 1 365 ? -14.361 -12.046 84.254  1.00 15.44 ? 364  LYS B O   1 
ATOM   6636 C  CB  . LYS B 1 365 ? -15.262 -14.882 83.358  1.00 16.58 ? 364  LYS B CB  1 
ATOM   6637 C  CG  . LYS B 1 365 ? -15.906 -15.613 82.190  1.00 18.56 ? 364  LYS B CG  1 
ATOM   6638 C  CD  . LYS B 1 365 ? -17.085 -16.464 82.632  1.00 23.17 ? 364  LYS B CD  1 
ATOM   6639 C  CE  . LYS B 1 365 ? -17.673 -17.228 81.450  1.00 27.81 ? 364  LYS B CE  1 
ATOM   6640 N  NZ  . LYS B 1 365 ? -18.810 -18.116 81.824  1.00 33.41 ? 364  LYS B NZ  1 
ATOM   6641 N  N   . THR B 1 366 ? -12.644 -13.376 84.854  1.00 16.36 ? 365  THR B N   1 
ATOM   6642 C  CA  . THR B 1 366 ? -12.240 -12.441 85.903  1.00 17.60 ? 365  THR B CA  1 
ATOM   6643 C  C   . THR B 1 366 ? -11.613 -11.177 85.331  1.00 16.38 ? 365  THR B C   1 
ATOM   6644 O  O   . THR B 1 366 ? -11.533 -10.165 86.038  1.00 18.54 ? 365  THR B O   1 
ATOM   6645 C  CB  . THR B 1 366 ? -11.248 -13.087 86.874  1.00 18.13 ? 365  THR B CB  1 
ATOM   6646 O  OG1 . THR B 1 366 ? -9.972  -13.208 86.240  1.00 21.09 ? 365  THR B OG1 1 
ATOM   6647 C  CG2 . THR B 1 366 ? -11.725 -14.464 87.323  1.00 20.77 ? 365  THR B CG2 1 
ATOM   6648 N  N   . ILE B 1 367 ? -11.158 -11.223 84.081  1.00 15.96 ? 366  ILE B N   1 
ATOM   6649 C  CA  . ILE B 1 367 ? -10.594 -10.061 83.399  1.00 15.06 ? 366  ILE B CA  1 
ATOM   6650 C  C   . ILE B 1 367 ? -11.646 -9.344  82.565  1.00 16.36 ? 366  ILE B C   1 
ATOM   6651 O  O   . ILE B 1 367 ? -11.802 -8.123  82.656  1.00 19.31 ? 366  ILE B O   1 
ATOM   6652 C  CB  . ILE B 1 367 ? -9.405  -10.503 82.513  1.00 14.63 ? 366  ILE B CB  1 
ATOM   6653 C  CG1 . ILE B 1 367 ? -8.268  -11.065 83.371  1.00 14.18 ? 366  ILE B CG1 1 
ATOM   6654 C  CG2 . ILE B 1 367 ? -8.946  -9.348  81.599  1.00 16.27 ? 366  ILE B CG2 1 
ATOM   6655 C  CD1 . ILE B 1 367 ? -7.530  -10.020 84.204  1.00 16.82 ? 366  ILE B CD1 1 
ATOM   6656 N  N   . TRP B 1 368 ? -12.369 -10.099 81.733  1.00 15.08 ? 367  TRP B N   1 
ATOM   6657 C  CA  . TRP B 1 368 ? -13.209 -9.542  80.680  1.00 16.21 ? 367  TRP B CA  1 
ATOM   6658 C  C   . TRP B 1 368 ? -14.683 -9.433  81.050  1.00 20.05 ? 367  TRP B C   1 
ATOM   6659 O  O   . TRP B 1 368 ? -15.433 -8.750  80.343  1.00 21.92 ? 367  TRP B O   1 
ATOM   6660 C  CB  . TRP B 1 368 ? -13.073 -10.393 79.410  1.00 15.39 ? 367  TRP B CB  1 
ATOM   6661 C  CG  . TRP B 1 368 ? -11.653 -10.455 78.902  1.00 13.55 ? 367  TRP B CG  1 
ATOM   6662 C  CD1 . TRP B 1 368 ? -10.731 -11.436 79.148  1.00 13.93 ? 367  TRP B CD1 1 
ATOM   6663 C  CD2 . TRP B 1 368 ? -10.997 -9.483  78.076  1.00 14.51 ? 367  TRP B CD2 1 
ATOM   6664 N  NE1 . TRP B 1 368 ? -9.543  -11.137 78.521  1.00 13.36 ? 367  TRP B NE1 1 
ATOM   6665 C  CE2 . TRP B 1 368 ? -9.677  -9.941  77.860  1.00 15.04 ? 367  TRP B CE2 1 
ATOM   6666 C  CE3 . TRP B 1 368 ? -11.395 -8.271  77.502  1.00 15.83 ? 367  TRP B CE3 1 
ATOM   6667 C  CZ2 . TRP B 1 368 ? -8.756  -9.233  77.086  1.00 13.71 ? 367  TRP B CZ2 1 
ATOM   6668 C  CZ3 . TRP B 1 368 ? -10.473 -7.563  76.728  1.00 15.00 ? 367  TRP B CZ3 1 
ATOM   6669 C  CH2 . TRP B 1 368 ? -9.170  -8.047  76.532  1.00 13.80 ? 367  TRP B CH2 1 
ATOM   6670 N  N   . GLY B 1 369 ? -15.127 -10.084 82.117  1.00 19.00 ? 368  GLY B N   1 
ATOM   6671 C  CA  . GLY B 1 369 ? -16.536 -10.074 82.458  1.00 18.58 ? 368  GLY B CA  1 
ATOM   6672 C  C   . GLY B 1 369 ? -17.255 -11.304 81.945  1.00 18.23 ? 368  GLY B C   1 
ATOM   6673 O  O   . GLY B 1 369 ? -16.675 -12.207 81.332  1.00 22.23 ? 368  GLY B O   1 
ATOM   6674 N  N   . ASP B 1 370 ? -18.567 -11.320 82.195  1.00 20.55 ? 369  ASP B N   1 
ATOM   6675 C  CA  . ASP B 1 370 ? -19.361 -12.514 81.948  1.00 25.27 ? 369  ASP B CA  1 
ATOM   6676 C  C   . ASP B 1 370 ? -19.636 -12.755 80.471  1.00 24.42 ? 369  ASP B C   1 
ATOM   6677 O  O   . ASP B 1 370 ? -19.906 -13.895 80.089  1.00 29.47 ? 369  ASP B O   1 
ATOM   6678 C  CB  . ASP B 1 370 ? -20.678 -12.416 82.708  1.00 31.23 ? 369  ASP B CB  1 
ATOM   6679 C  CG  . ASP B 1 370 ? -20.478 -12.425 84.197  1.00 39.99 ? 369  ASP B CG  1 
ATOM   6680 O  OD1 . ASP B 1 370 ? -19.714 -13.290 84.674  1.00 40.76 ? 369  ASP B OD1 1 
ATOM   6681 O  OD2 . ASP B 1 370 ? -21.059 -11.554 84.880  1.00 44.86 ? 369  ASP B OD2 1 
ATOM   6682 N  N   . ASP B 1 371 ? -19.565 -11.722 79.638  1.00 20.61 ? 370  ASP B N   1 
ATOM   6683 C  CA  . ASP B 1 371 ? -19.964 -11.802 78.231  1.00 21.91 ? 370  ASP B CA  1 
ATOM   6684 C  C   . ASP B 1 371 ? -18.807 -12.136 77.292  1.00 20.49 ? 370  ASP B C   1 
ATOM   6685 O  O   . ASP B 1 371 ? -18.781 -11.613 76.173  1.00 20.08 ? 370  ASP B O   1 
ATOM   6686 C  CB  . ASP B 1 371 ? -20.622 -10.480 77.829  1.00 22.08 ? 370  ASP B CB  1 
ATOM   6687 C  CG  . ASP B 1 371 ? -19.665 -9.286  77.924  1.00 27.34 ? 370  ASP B CG  1 
ATOM   6688 O  OD1 . ASP B 1 371 ? -18.502 -9.468  78.358  1.00 26.27 ? 370  ASP B OD1 1 
ATOM   6689 O  OD2 . ASP B 1 371 ? -20.075 -8.158  77.555  1.00 30.24 ? 370  ASP B OD2 1 
ATOM   6690 N  N   . VAL B 1 372 ? -17.866 -13.006 77.687  1.00 20.12 ? 371  VAL B N   1 
ATOM   6691 C  CA  . VAL B 1 372 ? -16.617 -13.162 76.936  1.00 18.25 ? 371  VAL B CA  1 
ATOM   6692 C  C   . VAL B 1 372 ? -16.818 -13.750 75.545  1.00 18.67 ? 371  VAL B C   1 
ATOM   6693 O  O   . VAL B 1 372 ? -15.964 -13.547 74.671  1.00 17.34 ? 371  VAL B O   1 
ATOM   6694 C  CB  . VAL B 1 372 ? -15.591 -14.043 77.684  1.00 21.59 ? 371  VAL B CB  1 
ATOM   6695 C  CG1 . VAL B 1 372 ? -15.147 -13.385 78.973  1.00 27.45 ? 371  VAL B CG1 1 
ATOM   6696 C  CG2 . VAL B 1 372 ? -16.153 -15.439 77.952  1.00 21.75 ? 371  VAL B CG2 1 
ATOM   6697 N  N   . GLU B 1 373 ? -17.899 -14.494 75.311  1.00 16.66 ? 372  GLU B N   1 
ATOM   6698 C  CA  . GLU B 1 373 ? -18.127 -15.056 73.984  1.00 15.27 ? 372  GLU B CA  1 
ATOM   6699 C  C   . GLU B 1 373 ? -18.754 -14.067 73.006  1.00 15.19 ? 372  GLU B C   1 
ATOM   6700 O  O   . GLU B 1 373 ? -18.812 -14.368 71.806  1.00 16.81 ? 372  GLU B O   1 
ATOM   6701 C  CB  . GLU B 1 373 ? -19.011 -16.304 74.080  1.00 17.41 ? 372  GLU B CB  1 
ATOM   6702 C  CG  . GLU B 1 373 ? -18.366 -17.464 74.816  1.00 20.13 ? 372  GLU B CG  1 
ATOM   6703 C  CD  . GLU B 1 373 ? -17.230 -18.083 74.022  1.00 24.39 ? 372  GLU B CD  1 
ATOM   6704 O  OE1 . GLU B 1 373 ? -17.333 -18.129 72.776  1.00 26.93 ? 372  GLU B OE1 1 
ATOM   6705 O  OE2 . GLU B 1 373 ? -16.236 -18.522 74.638  1.00 24.94 ? 372  GLU B OE2 1 
ATOM   6706 N  N   . GLU B 1 374 ? -19.225 -12.913 73.471  1.00 15.50 ? 373  GLU B N   1 
ATOM   6707 C  CA  . GLU B 1 374 ? -19.848 -11.946 72.572  1.00 14.30 ? 373  GLU B CA  1 
ATOM   6708 C  C   . GLU B 1 374 ? -18.785 -11.095 71.877  1.00 15.12 ? 373  GLU B C   1 
ATOM   6709 O  O   . GLU B 1 374 ? -17.706 -10.840 72.423  1.00 13.89 ? 373  GLU B O   1 
ATOM   6710 C  CB  . GLU B 1 374 ? -20.850 -11.069 73.343  1.00 18.72 ? 373  GLU B CB  1 
ATOM   6711 C  CG  . GLU B 1 374 ? -22.104 -11.862 73.737  1.00 20.24 ? 373  GLU B CG  1 
ATOM   6712 C  CD  . GLU B 1 374 ? -23.086 -11.122 74.643  1.00 25.48 ? 373  GLU B CD  1 
ATOM   6713 O  OE1 . GLU B 1 374 ? -22.834 -9.962  75.031  1.00 24.98 ? 373  GLU B OE1 1 
ATOM   6714 O  OE2 . GLU B 1 374 ? -24.126 -11.729 74.984  1.00 29.03 ? 373  GLU B OE2 1 
ATOM   6715 N  N   . PHE B 1 375 ? -19.091 -10.680 70.643  1.00 12.94 ? 374  PHE B N   1 
ATOM   6716 C  CA  . PHE B 1 375 ? -18.178 -9.875  69.829  1.00 11.50 ? 374  PHE B CA  1 
ATOM   6717 C  C   . PHE B 1 375 ? -18.511 -8.404  70.049  1.00 13.90 ? 374  PHE B C   1 
ATOM   6718 O  O   . PHE B 1 375 ? -19.477 -7.884  69.481  1.00 13.26 ? 374  PHE B O   1 
ATOM   6719 C  CB  . PHE B 1 375 ? -18.290 -10.253 68.351  1.00 11.77 ? 374  PHE B CB  1 
ATOM   6720 C  CG  . PHE B 1 375 ? -17.255 -9.593  67.481  1.00 10.52 ? 374  PHE B CG  1 
ATOM   6721 C  CD1 . PHE B 1 375 ? -15.960 -10.113 67.416  1.00 10.51 ? 374  PHE B CD1 1 
ATOM   6722 C  CD2 . PHE B 1 375 ? -17.554 -8.446  66.750  1.00 13.00 ? 374  PHE B CD2 1 
ATOM   6723 C  CE1 . PHE B 1 375 ? -14.985 -9.511  66.630  1.00 11.97 ? 374  PHE B CE1 1 
ATOM   6724 C  CE2 . PHE B 1 375 ? -16.579 -7.838  65.963  1.00 12.67 ? 374  PHE B CE2 1 
ATOM   6725 C  CZ  . PHE B 1 375 ? -15.287 -8.377  65.909  1.00 13.94 ? 374  PHE B CZ  1 
ATOM   6726 N  N   . ARG B 1 376 ? -17.705 -7.726  70.875  1.00 13.71 ? 375  ARG B N   1 
ATOM   6727 C  CA  . ARG B 1 376 ? -17.972 -6.349  71.303  1.00 12.07 ? 375  ARG B CA  1 
ATOM   6728 C  C   . ARG B 1 376 ? -16.696 -5.526  71.193  1.00 12.73 ? 375  ARG B C   1 
ATOM   6729 O  O   . ARG B 1 376 ? -15.936 -5.405  72.159  1.00 13.37 ? 375  ARG B O   1 
ATOM   6730 C  CB  . ARG B 1 376 ? -18.515 -6.309  72.734  1.00 12.95 ? 375  ARG B CB  1 
ATOM   6731 C  CG  . ARG B 1 376 ? -19.823 -7.080  72.918  1.00 17.02 ? 375  ARG B CG  1 
ATOM   6732 C  CD  . ARG B 1 376 ? -20.411 -6.923  74.324  1.00 19.28 ? 375  ARG B CD  1 
ATOM   6733 N  NE  . ARG B 1 376 ? -21.744 -7.514  74.389  1.00 23.11 ? 375  ARG B NE  1 
ATOM   6734 C  CZ  . ARG B 1 376 ? -22.841 -6.920  73.936  1.00 24.23 ? 375  ARG B CZ  1 
ATOM   6735 N  NH1 . ARG B 1 376 ? -22.811 -5.683  73.454  1.00 22.40 ? 375  ARG B NH1 1 
ATOM   6736 N  NH2 . ARG B 1 376 ? -23.996 -7.584  73.961  1.00 24.87 ? 375  ARG B NH2 1 
ATOM   6737 N  N   . PRO B 1 377 ? -16.428 -4.936  70.028  1.00 12.36 ? 376  PRO B N   1 
ATOM   6738 C  CA  . PRO B 1 377 ? -15.202 -4.131  69.884  1.00 11.09 ? 376  PRO B CA  1 
ATOM   6739 C  C   . PRO B 1 377 ? -15.097 -3.004  70.902  1.00 13.09 ? 376  PRO B C   1 
ATOM   6740 O  O   . PRO B 1 377 ? -13.983 -2.544  71.187  1.00 13.33 ? 376  PRO B O   1 
ATOM   6741 C  CB  . PRO B 1 377 ? -15.310 -3.595  68.450  1.00 10.62 ? 376  PRO B CB  1 
ATOM   6742 C  CG  . PRO B 1 377 ? -16.171 -4.629  67.743  1.00 12.80 ? 376  PRO B CG  1 
ATOM   6743 C  CD  . PRO B 1 377 ? -17.198 -5.012  68.775  1.00 13.27 ? 376  PRO B CD  1 
ATOM   6744 N  N   . GLU B 1 378 ? -16.223 -2.563  71.474  1.00 13.36 ? 377  GLU B N   1 
ATOM   6745 C  CA  . GLU B 1 378 ? -16.202 -1.505  72.477  1.00 13.40 ? 377  GLU B CA  1 
ATOM   6746 C  C   . GLU B 1 378 ? -15.331 -1.852  73.683  1.00 15.01 ? 377  GLU B C   1 
ATOM   6747 O  O   . GLU B 1 378 ? -14.926 -0.945  74.424  1.00 17.24 ? 377  GLU B O   1 
ATOM   6748 C  CB  . GLU B 1 378 ? -17.640 -1.188  72.914  1.00 12.04 ? 377  GLU B CB  1 
ATOM   6749 C  CG  . GLU B 1 378 ? -18.505 -0.515  71.816  1.00 13.16 ? 377  GLU B CG  1 
ATOM   6750 C  CD  . GLU B 1 378 ? -18.999 -1.469  70.725  1.00 14.41 ? 377  GLU B CD  1 
ATOM   6751 O  OE1 . GLU B 1 378 ? -18.966 -2.702  70.928  1.00 14.28 ? 377  GLU B OE1 1 
ATOM   6752 O  OE2 . GLU B 1 378 ? -19.438 -0.981  69.654  1.00 14.17 ? 377  GLU B OE2 1 
ATOM   6753 N  N   . ARG B 1 379 ? -15.033 -3.138  73.902  1.00 13.71 ? 378  ARG B N   1 
ATOM   6754 C  CA  . ARG B 1 379 ? -14.099 -3.515  74.969  1.00 15.86 ? 378  ARG B CA  1 
ATOM   6755 C  C   . ARG B 1 379 ? -12.765 -2.799  74.849  1.00 15.52 ? 378  ARG B C   1 
ATOM   6756 O  O   . ARG B 1 379 ? -12.053 -2.650  75.847  1.00 17.33 ? 378  ARG B O   1 
ATOM   6757 C  CB  . ARG B 1 379 ? -13.804 -5.010  74.940  1.00 18.76 ? 378  ARG B CB  1 
ATOM   6758 C  CG  . ARG B 1 379 ? -14.953 -5.907  75.201  1.00 18.94 ? 378  ARG B CG  1 
ATOM   6759 C  CD  . ARG B 1 379 ? -14.448 -7.318  75.025  1.00 17.16 ? 378  ARG B CD  1 
ATOM   6760 N  NE  . ARG B 1 379 ? -15.526 -8.197  74.616  1.00 17.51 ? 378  ARG B NE  1 
ATOM   6761 C  CZ  . ARG B 1 379 ? -16.371 -8.772  75.456  1.00 17.32 ? 378  ARG B CZ  1 
ATOM   6762 N  NH1 . ARG B 1 379 ? -16.271 -8.590  76.768  1.00 17.89 ? 378  ARG B NH1 1 
ATOM   6763 N  NH2 . ARG B 1 379 ? -17.341 -9.543  74.970  1.00 15.55 ? 378  ARG B NH2 1 
ATOM   6764 N  N   . PHE B 1 380 ? -12.370 -2.432  73.634  1.00 15.14 ? 379  PHE B N   1 
ATOM   6765 C  CA  . PHE B 1 380 ? -11.059 -1.863  73.372  1.00 16.51 ? 379  PHE B CA  1 
ATOM   6766 C  C   . PHE B 1 380 ? -11.101 -0.351  73.204  1.00 18.84 ? 379  PHE B C   1 
ATOM   6767 O  O   . PHE B 1 380 ? -10.109 0.242   72.765  1.00 17.77 ? 379  PHE B O   1 
ATOM   6768 C  CB  . PHE B 1 380 ? -10.447 -2.534  72.134  1.00 15.75 ? 379  PHE B CB  1 
ATOM   6769 C  CG  . PHE B 1 380 ? -10.036 -3.966  72.369  1.00 12.22 ? 379  PHE B CG  1 
ATOM   6770 C  CD1 . PHE B 1 380 ? -8.775  -4.262  72.885  1.00 13.34 ? 379  PHE B CD1 1 
ATOM   6771 C  CD2 . PHE B 1 380 ? -10.911 -5.013  72.103  1.00 15.08 ? 379  PHE B CD2 1 
ATOM   6772 C  CE1 . PHE B 1 380 ? -8.386  -5.583  73.115  1.00 12.37 ? 379  PHE B CE1 1 
ATOM   6773 C  CE2 . PHE B 1 380 ? -10.532 -6.335  72.331  1.00 13.42 ? 379  PHE B CE2 1 
ATOM   6774 C  CZ  . PHE B 1 380 ? -9.262  -6.619  72.841  1.00 12.13 ? 379  PHE B CZ  1 
ATOM   6775 N  N   . GLU B 1 381 ? -12.224 0.287   73.544  1.00 19.14 ? 380  GLU B N   1 
ATOM   6776 C  CA  . GLU B 1 381 ? -12.329 1.731   73.359  1.00 23.52 ? 380  GLU B CA  1 
ATOM   6777 C  C   . GLU B 1 381 ? -11.232 2.458   74.117  1.00 27.29 ? 380  GLU B C   1 
ATOM   6778 O  O   . GLU B 1 381 ? -10.659 3.434   73.616  1.00 28.83 ? 380  GLU B O   1 
ATOM   6779 C  CB  . GLU B 1 381 ? -13.703 2.224   73.806  1.00 28.13 ? 380  GLU B CB  1 
ATOM   6780 C  CG  . GLU B 1 381 ? -14.811 1.914   72.824  1.00 36.00 ? 380  GLU B CG  1 
ATOM   6781 C  CD  . GLU B 1 381 ? -16.162 2.421   73.288  1.00 41.43 ? 380  GLU B CD  1 
ATOM   6782 O  OE1 . GLU B 1 381 ? -16.308 2.704   74.494  1.00 42.76 ? 380  GLU B OE1 1 
ATOM   6783 O  OE2 . GLU B 1 381 ? -17.072 2.533   72.440  1.00 45.61 ? 380  GLU B OE2 1 
ATOM   6784 N  N   . ASN B 1 382 ? -10.916 1.983   75.321  1.00 28.08 ? 381  ASN B N   1 
ATOM   6785 C  CA  . ASN B 1 382 ? -9.949  2.613   76.215  1.00 30.81 ? 381  ASN B CA  1 
ATOM   6786 C  C   . ASN B 1 382 ? -8.818  1.624   76.472  1.00 31.08 ? 381  ASN B C   1 
ATOM   6787 O  O   . ASN B 1 382 ? -8.910  0.780   77.376  1.00 27.77 ? 381  ASN B O   1 
ATOM   6788 C  CB  . ASN B 1 382 ? -10.628 3.047   77.513  1.00 34.49 ? 381  ASN B CB  1 
ATOM   6789 C  CG  . ASN B 1 382 ? -9.655  3.635   78.511  1.00 40.54 ? 381  ASN B CG  1 
ATOM   6790 O  OD1 . ASN B 1 382 ? -8.493  3.889   78.186  1.00 41.97 ? 381  ASN B OD1 1 
ATOM   6791 N  ND2 . ASN B 1 382 ? -10.126 3.860   79.735  1.00 41.46 ? 381  ASN B ND2 1 
ATOM   6792 N  N   . PRO B 1 383 ? -7.726  1.696   75.710  1.00 33.08 ? 382  PRO B N   1 
ATOM   6793 C  CA  . PRO B 1 383 ? -6.672  0.678   75.855  1.00 34.25 ? 382  PRO B CA  1 
ATOM   6794 C  C   . PRO B 1 383 ? -6.090  0.607   77.255  1.00 32.24 ? 382  PRO B C   1 
ATOM   6795 O  O   . PRO B 1 383 ? -5.596  -0.455  77.658  1.00 30.11 ? 382  PRO B O   1 
ATOM   6796 C  CB  . PRO B 1 383 ? -5.621  1.113   74.823  1.00 36.97 ? 382  PRO B CB  1 
ATOM   6797 C  CG  . PRO B 1 383 ? -5.860  2.579   74.635  1.00 36.65 ? 382  PRO B CG  1 
ATOM   6798 C  CD  . PRO B 1 383 ? -7.352  2.754   74.756  1.00 34.76 ? 382  PRO B CD  1 
ATOM   6799 N  N   . SER B 1 384 ? -6.147  1.707   78.011  1.00 32.82 ? 383  SER B N   1 
ATOM   6800 C  CA  . SER B 1 384 ? -5.587  1.735   79.359  1.00 33.87 ? 383  SER B CA  1 
ATOM   6801 C  C   . SER B 1 384 ? -6.305  0.798   80.315  1.00 33.41 ? 383  SER B C   1 
ATOM   6802 O  O   . SER B 1 384 ? -5.732  0.429   81.346  1.00 36.58 ? 383  SER B O   1 
ATOM   6803 C  CB  . SER B 1 384 ? -5.641  3.154   79.926  1.00 35.77 ? 383  SER B CB  1 
ATOM   6804 O  OG  . SER B 1 384 ? -4.729  3.992   79.255  1.00 41.90 ? 383  SER B OG  1 
ATOM   6805 N  N   . ALA B 1 385 ? -7.544  0.423   80.012  1.00 31.09 ? 384  ALA B N   1 
ATOM   6806 C  CA  . ALA B 1 385 ? -8.322  -0.423  80.905  1.00 30.82 ? 384  ALA B CA  1 
ATOM   6807 C  C   . ALA B 1 385 ? -7.989  -1.906  80.778  1.00 30.84 ? 384  ALA B C   1 
ATOM   6808 O  O   . ALA B 1 385 ? -8.527  -2.711  81.543  1.00 30.93 ? 384  ALA B O   1 
ATOM   6809 C  CB  . ALA B 1 385 ? -9.816  -0.209  80.651  1.00 33.76 ? 384  ALA B CB  1 
ATOM   6810 N  N   . ILE B 1 386 ? -7.125  -2.290  79.846  1.00 29.56 ? 385  ILE B N   1 
ATOM   6811 C  CA  . ILE B 1 386 ? -6.754  -3.689  79.648  1.00 27.34 ? 385  ILE B CA  1 
ATOM   6812 C  C   . ILE B 1 386 ? -5.567  -3.994  80.556  1.00 27.57 ? 385  ILE B C   1 
ATOM   6813 O  O   . ILE B 1 386 ? -4.508  -3.366  80.399  1.00 26.72 ? 385  ILE B O   1 
ATOM   6814 C  CB  . ILE B 1 386 ? -6.402  -3.977  78.183  1.00 26.54 ? 385  ILE B CB  1 
ATOM   6815 C  CG1 . ILE B 1 386 ? -7.460  -3.402  77.235  1.00 29.56 ? 385  ILE B CG1 1 
ATOM   6816 C  CG2 . ILE B 1 386 ? -6.235  -5.472  77.967  1.00 27.40 ? 385  ILE B CG2 1 
ATOM   6817 C  CD1 . ILE B 1 386 ? -8.740  -4.204  77.165  1.00 28.86 ? 385  ILE B CD1 1 
ATOM   6818 N  N   . PRO B 1 387 ? -5.690  -4.934  81.498  1.00 27.17 ? 386  PRO B N   1 
ATOM   6819 C  CA  . PRO B 1 387 ? -4.560  -5.250  82.384  1.00 25.85 ? 386  PRO B CA  1 
ATOM   6820 C  C   . PRO B 1 387 ? -3.366  -5.806  81.619  1.00 24.48 ? 386  PRO B C   1 
ATOM   6821 O  O   . PRO B 1 387 ? -3.509  -6.397  80.546  1.00 21.44 ? 386  PRO B O   1 
ATOM   6822 C  CB  . PRO B 1 387 ? -5.143  -6.301  83.337  1.00 26.93 ? 386  PRO B CB  1 
ATOM   6823 C  CG  . PRO B 1 387 ? -6.623  -6.056  83.313  1.00 26.21 ? 386  PRO B CG  1 
ATOM   6824 C  CD  . PRO B 1 387 ? -6.940  -5.584  81.926  1.00 27.61 ? 386  PRO B CD  1 
ATOM   6825 N  N   . GLN B 1 388 ? -2.173  -5.611  82.187  1.00 21.43 ? 387  GLN B N   1 
ATOM   6826 C  CA  . GLN B 1 388 ? -0.971  -6.173  81.586  1.00 24.63 ? 387  GLN B CA  1 
ATOM   6827 C  C   . GLN B 1 388 ? -1.096  -7.687  81.481  1.00 23.73 ? 387  GLN B C   1 
ATOM   6828 O  O   . GLN B 1 388 ? -1.527  -8.361  82.424  1.00 22.23 ? 387  GLN B O   1 
ATOM   6829 C  CB  . GLN B 1 388 ? 0.276   -5.809  82.400  1.00 26.88 ? 387  GLN B CB  1 
ATOM   6830 C  CG  . GLN B 1 388 ? 1.595   -6.218  81.724  1.00 32.56 ? 387  GLN B CG  1 
ATOM   6831 C  CD  . GLN B 1 388 ? 2.829   -5.950  82.584  1.00 39.19 ? 387  GLN B CD  1 
ATOM   6832 O  OE1 . GLN B 1 388 ? 2.804   -6.117  83.805  1.00 42.10 ? 387  GLN B OE1 1 
ATOM   6833 N  NE2 . GLN B 1 388 ? 3.916   -5.532  81.942  1.00 39.57 ? 387  GLN B NE2 1 
ATOM   6834 N  N   . HIS B 1 389 ? -0.713  -8.218  80.318  1.00 21.47 ? 388  HIS B N   1 
ATOM   6835 C  CA  . HIS B 1 389 ? -0.683  -9.648  80.034  1.00 18.82 ? 388  HIS B CA  1 
ATOM   6836 C  C   . HIS B 1 389 ? -2.070  -10.276 79.969  1.00 18.03 ? 388  HIS B C   1 
ATOM   6837 O  O   . HIS B 1 389 ? -2.192  -11.497 80.026  1.00 20.12 ? 388  HIS B O   1 
ATOM   6838 C  CB  . HIS B 1 389 ? 0.189   -10.394 81.053  1.00 19.85 ? 388  HIS B CB  1 
ATOM   6839 C  CG  . HIS B 1 389 ? 1.602   -9.901  81.097  1.00 23.19 ? 388  HIS B CG  1 
ATOM   6840 N  ND1 . HIS B 1 389 ? 2.293   -9.536  79.961  1.00 25.18 ? 388  HIS B ND1 1 
ATOM   6841 C  CD2 . HIS B 1 389 ? 2.445   -9.691  82.135  1.00 25.78 ? 388  HIS B CD2 1 
ATOM   6842 C  CE1 . HIS B 1 389 ? 3.507   -9.136  80.297  1.00 25.94 ? 388  HIS B CE1 1 
ATOM   6843 N  NE2 . HIS B 1 389 ? 3.623   -9.214  81.611  1.00 24.58 ? 388  HIS B NE2 1 
ATOM   6844 N  N   . ALA B 1 390 ? -3.128  -9.477  79.830  1.00 16.18 ? 389  ALA B N   1 
ATOM   6845 C  CA  . ALA B 1 390 ? -4.460  -10.034 79.615  1.00 15.45 ? 389  ALA B CA  1 
ATOM   6846 C  C   . ALA B 1 390 ? -4.762  -10.306 78.149  1.00 16.12 ? 389  ALA B C   1 
ATOM   6847 O  O   . ALA B 1 390 ? -5.632  -11.134 77.854  1.00 16.21 ? 389  ALA B O   1 
ATOM   6848 C  CB  . ALA B 1 390 ? -5.535  -9.096  80.158  1.00 18.53 ? 389  ALA B CB  1 
ATOM   6849 N  N   . PHE B 1 391 ? -4.065  -9.632  77.236  1.00 14.37 ? 390  PHE B N   1 
ATOM   6850 C  CA  . PHE B 1 391 ? -4.347  -9.681  75.804  1.00 13.69 ? 390  PHE B CA  1 
ATOM   6851 C  C   . PHE B 1 391 ? -3.011  -9.892  75.102  1.00 12.59 ? 390  PHE B C   1 
ATOM   6852 O  O   . PHE B 1 391 ? -2.176  -8.979  75.065  1.00 13.57 ? 390  PHE B O   1 
ATOM   6853 C  CB  . PHE B 1 391 ? -5.041  -8.383  75.364  1.00 14.10 ? 390  PHE B CB  1 
ATOM   6854 C  CG  . PHE B 1 391 ? -5.392  -8.318  73.889  1.00 11.30 ? 390  PHE B CG  1 
ATOM   6855 C  CD1 . PHE B 1 391 ? -6.343  -9.166  73.350  1.00 11.23 ? 390  PHE B CD1 1 
ATOM   6856 C  CD2 . PHE B 1 391 ? -4.806  -7.367  73.061  1.00 13.37 ? 390  PHE B CD2 1 
ATOM   6857 C  CE1 . PHE B 1 391 ? -6.676  -9.089  72.004  1.00 13.40 ? 390  PHE B CE1 1 
ATOM   6858 C  CE2 . PHE B 1 391 ? -5.142  -7.279  71.713  1.00 12.16 ? 390  PHE B CE2 1 
ATOM   6859 C  CZ  . PHE B 1 391 ? -6.070  -8.135  71.184  1.00 14.56 ? 390  PHE B CZ  1 
ATOM   6860 N  N   . LYS B 1 392 ? -2.779  -11.107 74.582  1.00 12.37 ? 391  LYS B N   1 
ATOM   6861 C  CA  . LYS B 1 392 ? -1.447  -11.498 74.103  1.00 11.44 ? 391  LYS B CA  1 
ATOM   6862 C  C   . LYS B 1 392 ? -1.490  -12.210 72.749  1.00 13.43 ? 391  LYS B C   1 
ATOM   6863 O  O   . LYS B 1 392 ? -0.823  -13.227 72.550  1.00 11.55 ? 391  LYS B O   1 
ATOM   6864 C  CB  . LYS B 1 392 ? -0.756  -12.380 75.141  1.00 12.45 ? 391  LYS B CB  1 
ATOM   6865 C  CG  . LYS B 1 392 ? -0.722  -11.776 76.542  1.00 15.85 ? 391  LYS B CG  1 
ATOM   6866 C  CD  . LYS B 1 392 ? 0.242   -10.604 76.619  1.00 18.69 ? 391  LYS B CD  1 
ATOM   6867 C  CE  . LYS B 1 392 ? 1.694   -11.082 76.650  1.00 19.47 ? 391  LYS B CE  1 
ATOM   6868 N  NZ  . LYS B 1 392 ? 2.603   -9.961  77.031  1.00 21.25 ? 391  LYS B NZ  1 
ATOM   6869 N  N   . PRO B 1 393 ? -2.231  -11.676 71.771  1.00 11.62 ? 392  PRO B N   1 
ATOM   6870 C  CA  . PRO B 1 393 ? -2.252  -12.324 70.452  1.00 11.82 ? 392  PRO B CA  1 
ATOM   6871 C  C   . PRO B 1 393 ? -0.921  -12.248 69.721  1.00 11.05 ? 392  PRO B C   1 
ATOM   6872 O  O   . PRO B 1 393 ? -0.753  -12.945 68.709  1.00 10.34 ? 392  PRO B O   1 
ATOM   6873 C  CB  . PRO B 1 393 ? -3.337  -11.545 69.701  1.00 10.29 ? 392  PRO B CB  1 
ATOM   6874 C  CG  . PRO B 1 393 ? -3.238  -10.154 70.290  1.00 12.68 ? 392  PRO B CG  1 
ATOM   6875 C  CD  . PRO B 1 393 ? -2.967  -10.396 71.761  1.00 11.42 ? 392  PRO B CD  1 
ATOM   6876 N  N   A HIS B 1 394 ? 0.027   -11.430 70.177  0.80 11.58 ? 393  HIS B N   1 
ATOM   6877 N  N   B HIS B 1 394 ? 0.020   -11.434 70.207  0.20 10.87 ? 393  HIS B N   1 
ATOM   6878 C  CA  A HIS B 1 394 ? 1.318   -11.314 69.506  0.80 13.47 ? 393  HIS B CA  1 
ATOM   6879 C  CA  B HIS B 1 394 ? 1.308   -11.213 69.562  0.20 10.75 ? 393  HIS B CA  1 
ATOM   6880 C  C   A HIS B 1 394 ? 2.470   -11.736 70.412  0.80 11.99 ? 393  HIS B C   1 
ATOM   6881 C  C   B HIS B 1 394 ? 2.468   -11.863 70.308  0.20 11.21 ? 393  HIS B C   1 
ATOM   6882 O  O   A HIS B 1 394 ? 3.601   -11.272 70.253  0.80 12.44 ? 393  HIS B O   1 
ATOM   6883 O  O   B HIS B 1 394 ? 3.625   -11.660 69.925  0.20 12.36 ? 393  HIS B O   1 
ATOM   6884 C  CB  A HIS B 1 394 ? 1.525   -9.896  68.974  0.80 14.07 ? 393  HIS B CB  1 
ATOM   6885 C  CB  B HIS B 1 394 ? 1.580   -9.711  69.420  0.20 9.19  ? 393  HIS B CB  1 
ATOM   6886 C  CG  A HIS B 1 394 ? 0.694   -9.586  67.764  0.80 14.91 ? 393  HIS B CG  1 
ATOM   6887 C  CG  B HIS B 1 394 ? 0.374   -8.901  69.056  0.20 9.90  ? 393  HIS B CG  1 
ATOM   6888 N  ND1 A HIS B 1 394 ? -0.433  -8.797  67.815  0.80 17.47 ? 393  HIS B ND1 1 
ATOM   6889 N  ND1 B HIS B 1 394 ? -0.112  -8.823  67.769  0.20 9.98  ? 393  HIS B ND1 1 
ATOM   6890 C  CD2 A HIS B 1 394 ? 0.817   -9.983  66.474  0.80 18.10 ? 393  HIS B CD2 1 
ATOM   6891 C  CD2 B HIS B 1 394 ? -0.433  -8.116  69.810  0.20 10.05 ? 393  HIS B CD2 1 
ATOM   6892 C  CE1 A HIS B 1 394 ? -0.968  -8.714  66.609  0.80 18.55 ? 393  HIS B CE1 1 
ATOM   6893 C  CE1 B HIS B 1 394 ? -1.171  -8.034  67.746  0.20 11.00 ? 393  HIS B CE1 1 
ATOM   6894 N  NE2 A HIS B 1 394 ? -0.229  -9.426  65.776  0.80 19.47 ? 393  HIS B NE2 1 
ATOM   6895 N  NE2 B HIS B 1 394 ? -1.387  -7.592  68.972  0.20 11.24 ? 393  HIS B NE2 1 
ATOM   6896 N  N   . GLY B 1 395 ? 2.200   -12.626 71.362  1.00 11.07 ? 394  GLY B N   1 
ATOM   6897 C  CA  . GLY B 1 395 ? 3.275   -13.179 72.165  1.00 12.48 ? 394  GLY B CA  1 
ATOM   6898 C  C   . GLY B 1 395 ? 3.713   -12.225 73.264  1.00 14.01 ? 394  GLY B C   1 
ATOM   6899 O  O   . GLY B 1 395 ? 2.962   -11.327 73.686  1.00 13.32 ? 394  GLY B O   1 
ATOM   6900 N  N   . ASN B 1 396 ? 4.960   -12.415 73.723  1.00 12.13 ? 395  ASN B N   1 
ATOM   6901 C  CA  . ASN B 1 396 ? 5.443   -11.754 74.930  1.00 13.20 ? 395  ASN B CA  1 
ATOM   6902 C  C   . ASN B 1 396 ? 6.883   -11.266 74.815  1.00 14.31 ? 395  ASN B C   1 
ATOM   6903 O  O   . ASN B 1 396 ? 7.762   -11.985 74.327  1.00 13.53 ? 395  ASN B O   1 
ATOM   6904 C  CB  . ASN B 1 396 ? 5.369   -12.692 76.138  1.00 13.37 ? 395  ASN B CB  1 
ATOM   6905 C  CG  . ASN B 1 396 ? 5.760   -11.994 77.419  1.00 15.41 ? 395  ASN B CG  1 
ATOM   6906 O  OD1 . ASN B 1 396 ? 5.090   -11.045 77.836  1.00 15.40 ? 395  ASN B OD1 1 
ATOM   6907 N  ND2 . ASN B 1 396 ? 6.857   -12.440 78.046  1.00 14.66 ? 395  ASN B ND2 1 
ATOM   6908 N  N   . GLY B 1 397 ? 7.118   -10.051 75.318  1.00 12.54 ? 396  GLY B N   1 
ATOM   6909 C  CA  . GLY B 1 397 ? 8.468   -9.607  75.632  1.00 12.04 ? 396  GLY B CA  1 
ATOM   6910 C  C   . GLY B 1 397 ? 9.345   -9.454  74.404  1.00 9.99  ? 396  GLY B C   1 
ATOM   6911 O  O   . GLY B 1 397 ? 8.881   -9.107  73.309  1.00 13.96 ? 396  GLY B O   1 
ATOM   6912 N  N   . GLN B 1 398 ? 10.646  -9.718  74.594  1.00 10.87 ? 397  GLN B N   1 
ATOM   6913 C  CA  . GLN B 1 398 ? 11.588  -9.595  73.483  1.00 12.11 ? 397  GLN B CA  1 
ATOM   6914 C  C   . GLN B 1 398 ? 11.337  -10.631 72.393  1.00 12.48 ? 397  GLN B C   1 
ATOM   6915 O  O   . GLN B 1 398 ? 11.806  -10.445 71.259  1.00 13.37 ? 397  GLN B O   1 
ATOM   6916 C  CB  . GLN B 1 398 ? 13.033  -9.698  73.988  1.00 13.58 ? 397  GLN B CB  1 
ATOM   6917 C  CG  . GLN B 1 398 ? 13.489  -11.098 74.403  1.00 14.52 ? 397  GLN B CG  1 
ATOM   6918 C  CD  . GLN B 1 398 ? 14.923  -11.095 74.942  1.00 16.97 ? 397  GLN B CD  1 
ATOM   6919 O  OE1 . GLN B 1 398 ? 15.719  -10.207 74.621  1.00 18.04 ? 397  GLN B OE1 1 
ATOM   6920 N  NE2 . GLN B 1 398 ? 15.248  -12.079 75.770  1.00 16.99 ? 397  GLN B NE2 1 
ATOM   6921 N  N   . ARG B 1 399 ? 10.615  -11.713 72.699  1.00 11.26 ? 398  ARG B N   1 
ATOM   6922 C  CA  . ARG B 1 399 ? 10.231  -12.693 71.690  1.00 11.34 ? 398  ARG B CA  1 
ATOM   6923 C  C   . ARG B 1 399 ? 8.814   -12.460 71.172  1.00 11.50 ? 398  ARG B C   1 
ATOM   6924 O  O   . ARG B 1 399 ? 8.203   -13.374 70.606  1.00 11.90 ? 398  ARG B O   1 
ATOM   6925 C  CB  . ARG B 1 399 ? 10.378  -14.116 72.241  1.00 12.14 ? 398  ARG B CB  1 
ATOM   6926 C  CG  . ARG B 1 399 ? 11.805  -14.506 72.677  1.00 12.38 ? 398  ARG B CG  1 
ATOM   6927 C  CD  . ARG B 1 399 ? 12.846  -14.275 71.557  1.00 11.28 ? 398  ARG B CD  1 
ATOM   6928 N  NE  . ARG B 1 399 ? 12.549  -14.998 70.318  1.00 10.38 ? 398  ARG B NE  1 
ATOM   6929 C  CZ  . ARG B 1 399 ? 12.979  -16.216 70.020  1.00 10.51 ? 398  ARG B CZ  1 
ATOM   6930 N  NH1 . ARG B 1 399 ? 13.693  -16.932 70.880  1.00 10.46 ? 398  ARG B NH1 1 
ATOM   6931 N  NH2 . ARG B 1 399 ? 12.679  -16.736 68.825  1.00 10.69 ? 398  ARG B NH2 1 
ATOM   6932 N  N   . ALA B 1 400 ? 8.277   -11.254 71.351  1.00 11.59 ? 399  ALA B N   1 
ATOM   6933 C  CA  . ALA B 1 400 ? 6.974   -10.927 70.789  1.00 11.57 ? 399  ALA B CA  1 
ATOM   6934 C  C   . ALA B 1 400 ? 7.063   -10.798 69.266  1.00 12.36 ? 399  ALA B C   1 
ATOM   6935 O  O   . ALA B 1 400 ? 8.140   -10.680 68.680  1.00 13.98 ? 399  ALA B O   1 
ATOM   6936 C  CB  . ALA B 1 400 ? 6.446   -9.627  71.391  1.00 11.80 ? 399  ALA B CB  1 
ATOM   6937 N  N   . CYS B 1 401 ? 5.899   -10.785 68.630  1.00 10.15 ? 400  CYS B N   1 
ATOM   6938 C  CA  . CYS B 1 401 ? 5.820   -10.710 67.173  1.00 9.91  ? 400  CYS B CA  1 
ATOM   6939 C  C   . CYS B 1 401 ? 6.485   -9.441  66.643  1.00 10.22 ? 400  CYS B C   1 
ATOM   6940 O  O   . CYS B 1 401 ? 6.106   -8.327  67.018  1.00 12.17 ? 400  CYS B O   1 
ATOM   6941 C  CB  . CYS B 1 401 ? 4.354   -10.750 66.750  1.00 10.74 ? 400  CYS B CB  1 
ATOM   6942 S  SG  . CYS B 1 401 ? 4.132   -10.536 64.968  1.00 12.92 ? 400  CYS B SG  1 
ATOM   6943 N  N   . ILE B 1 402 ? 7.470   -9.605  65.754  1.00 11.05 ? 401  ILE B N   1 
ATOM   6944 C  CA  . ILE B 1 402 ? 8.150   -8.438  65.193  1.00 11.59 ? 401  ILE B CA  1 
ATOM   6945 C  C   . ILE B 1 402 ? 7.284   -7.730  64.157  1.00 11.60 ? 401  ILE B C   1 
ATOM   6946 O  O   . ILE B 1 402 ? 7.498   -6.536  63.884  1.00 13.76 ? 401  ILE B O   1 
ATOM   6947 C  CB  . ILE B 1 402 ? 9.507   -8.833  64.572  1.00 12.01 ? 401  ILE B CB  1 
ATOM   6948 C  CG1 . ILE B 1 402 ? 10.427  -7.617  64.446  1.00 10.59 ? 401  ILE B CG1 1 
ATOM   6949 C  CG2 . ILE B 1 402 ? 9.316   -9.466  63.190  1.00 12.17 ? 401  ILE B CG2 1 
ATOM   6950 C  CD1 . ILE B 1 402 ? 11.850  -7.967  63.932  1.00 12.91 ? 401  ILE B CD1 1 
ATOM   6951 N  N   . GLY B 1 403 ? 6.305   -8.424  63.584  1.00 12.34 ? 402  GLY B N   1 
ATOM   6952 C  CA  . GLY B 1 403 ? 5.474   -7.845  62.542  1.00 11.29 ? 402  GLY B CA  1 
ATOM   6953 C  C   . GLY B 1 403 ? 4.128   -7.301  62.990  1.00 12.12 ? 402  GLY B C   1 
ATOM   6954 O  O   . GLY B 1 403 ? 3.255   -7.065  62.150  1.00 13.35 ? 402  GLY B O   1 
ATOM   6955 N  N   . GLN B 1 404 ? 3.947   -7.086  64.301  1.00 12.59 ? 403  GLN B N   1 
ATOM   6956 C  CA  . GLN B 1 404 ? 2.632   -6.718  64.825  1.00 12.69 ? 403  GLN B CA  1 
ATOM   6957 C  C   . GLN B 1 404 ? 2.090   -5.460  64.151  1.00 14.10 ? 403  GLN B C   1 
ATOM   6958 O  O   . GLN B 1 404 ? 0.919   -5.414  63.741  1.00 14.93 ? 403  GLN B O   1 
ATOM   6959 C  CB  . GLN B 1 404 ? 2.709   -6.514  66.341  1.00 16.72 ? 403  GLN B CB  1 
ATOM   6960 C  CG  . GLN B 1 404 ? 1.443   -5.925  66.954  1.00 20.45 ? 403  GLN B CG  1 
ATOM   6961 C  CD  . GLN B 1 404 ? 1.622   -5.568  68.425  1.00 23.81 ? 403  GLN B CD  1 
ATOM   6962 O  OE1 . GLN B 1 404 ? 2.483   -6.122  69.106  1.00 24.26 ? 403  GLN B OE1 1 
ATOM   6963 N  NE2 . GLN B 1 404 ? 0.813   -4.621  68.915  1.00 26.08 ? 403  GLN B NE2 1 
ATOM   6964 N  N   A GLN B 1 405 ? 2.926   -4.426  64.032  0.41 14.03 ? 404  GLN B N   1 
ATOM   6965 N  N   B GLN B 1 405 ? 2.926   -4.426  64.028  0.59 14.27 ? 404  GLN B N   1 
ATOM   6966 C  CA  A GLN B 1 405 ? 2.478   -3.176  63.422  0.41 14.15 ? 404  GLN B CA  1 
ATOM   6967 C  CA  B GLN B 1 405 ? 2.474   -3.173  63.429  0.59 14.15 ? 404  GLN B CA  1 
ATOM   6968 C  C   A GLN B 1 405 ? 2.210   -3.350  61.933  0.41 13.84 ? 404  GLN B C   1 
ATOM   6969 C  C   B GLN B 1 405 ? 2.241   -3.313  61.929  0.59 13.36 ? 404  GLN B C   1 
ATOM   6970 O  O   A GLN B 1 405 ? 1.272   -2.751  61.392  0.41 14.63 ? 404  GLN B O   1 
ATOM   6971 O  O   B GLN B 1 405 ? 1.355   -2.648  61.378  0.59 13.41 ? 404  GLN B O   1 
ATOM   6972 C  CB  A GLN B 1 405 ? 3.515   -2.078  63.652  0.41 18.35 ? 404  GLN B CB  1 
ATOM   6973 C  CB  B GLN B 1 405 ? 3.489   -2.059  63.696  0.59 20.19 ? 404  GLN B CB  1 
ATOM   6974 C  CG  A GLN B 1 405 ? 3.671   -1.694  65.106  0.41 22.22 ? 404  GLN B CG  1 
ATOM   6975 C  CG  B GLN B 1 405 ? 3.700   -1.734  65.171  0.59 26.20 ? 404  GLN B CG  1 
ATOM   6976 C  CD  A GLN B 1 405 ? 2.352   -1.291  65.731  0.41 25.01 ? 404  GLN B CD  1 
ATOM   6977 C  CD  B GLN B 1 405 ? 4.561   -2.759  65.893  0.59 31.91 ? 404  GLN B CD  1 
ATOM   6978 O  OE1 A GLN B 1 405 ? 1.782   -0.257  65.388  0.41 28.22 ? 404  GLN B OE1 1 
ATOM   6979 O  OE1 B GLN B 1 405 ? 5.368   -3.454  65.277  0.59 32.19 ? 404  GLN B OE1 1 
ATOM   6980 N  NE2 A GLN B 1 405 ? 1.853   -2.113  66.646  0.41 28.05 ? 404  GLN B NE2 1 
ATOM   6981 N  NE2 B GLN B 1 405 ? 4.387   -2.857  67.207  0.59 35.04 ? 404  GLN B NE2 1 
ATOM   6982 N  N   . PHE B 1 406 ? 3.031   -4.152  61.253  1.00 13.79 ? 405  PHE B N   1 
ATOM   6983 C  CA  . PHE B 1 406 ? 2.805   -4.427  59.834  1.00 11.85 ? 405  PHE B CA  1 
ATOM   6984 C  C   . PHE B 1 406 ? 1.453   -5.100  59.628  1.00 9.63  ? 405  PHE B C   1 
ATOM   6985 O  O   . PHE B 1 406 ? 0.641   -4.664  58.799  1.00 12.16 ? 405  PHE B O   1 
ATOM   6986 C  CB  . PHE B 1 406 ? 3.956   -5.301  59.309  1.00 12.21 ? 405  PHE B CB  1 
ATOM   6987 C  CG  . PHE B 1 406 ? 3.950   -5.531  57.813  1.00 13.42 ? 405  PHE B CG  1 
ATOM   6988 C  CD1 . PHE B 1 406 ? 3.119   -6.488  57.247  1.00 13.39 ? 405  PHE B CD1 1 
ATOM   6989 C  CD2 . PHE B 1 406 ? 4.810   -4.816  56.983  1.00 14.43 ? 405  PHE B CD2 1 
ATOM   6990 C  CE1 . PHE B 1 406 ? 3.131   -6.732  55.871  1.00 13.64 ? 405  PHE B CE1 1 
ATOM   6991 C  CE2 . PHE B 1 406 ? 4.822   -5.039  55.600  1.00 14.17 ? 405  PHE B CE2 1 
ATOM   6992 C  CZ  . PHE B 1 406 ? 3.971   -5.997  55.043  1.00 14.98 ? 405  PHE B CZ  1 
ATOM   6993 N  N   . ALA B 1 407 ? 1.188   -6.164  60.387  1.00 9.67  ? 406  ALA B N   1 
ATOM   6994 C  CA  . ALA B 1 407 ? -0.086  -6.875  60.269  1.00 11.12 ? 406  ALA B CA  1 
ATOM   6995 C  C   . ALA B 1 407 ? -1.278  -5.948  60.509  1.00 12.86 ? 406  ALA B C   1 
ATOM   6996 O  O   . ALA B 1 407 ? -2.266  -5.983  59.761  1.00 12.18 ? 406  ALA B O   1 
ATOM   6997 C  CB  . ALA B 1 407 ? -0.122  -8.049  61.252  1.00 10.56 ? 406  ALA B CB  1 
ATOM   6998 N  N   . LEU B 1 408 ? -1.222  -5.127  61.568  1.00 12.09 ? 407  LEU B N   1 
ATOM   6999 C  CA  . LEU B 1 408 ? -2.394  -4.319  61.906  1.00 12.65 ? 407  LEU B CA  1 
ATOM   7000 C  C   . LEU B 1 408 ? -2.586  -3.166  60.932  1.00 12.13 ? 407  LEU B C   1 
ATOM   7001 O  O   . LEU B 1 408 ? -3.729  -2.768  60.667  1.00 13.19 ? 407  LEU B O   1 
ATOM   7002 C  CB  . LEU B 1 408 ? -2.305  -3.800  63.347  1.00 15.44 ? 407  LEU B CB  1 
ATOM   7003 C  CG  . LEU B 1 408 ? -2.454  -4.902  64.401  1.00 19.81 ? 407  LEU B CG  1 
ATOM   7004 C  CD1 . LEU B 1 408 ? -2.291  -4.355  65.816  1.00 23.46 ? 407  LEU B CD1 1 
ATOM   7005 C  CD2 . LEU B 1 408 ? -3.787  -5.629  64.247  1.00 23.67 ? 407  LEU B CD2 1 
ATOM   7006 N  N   . HIS B 1 409 ? -1.502  -2.636  60.358  1.00 11.52 ? 408  HIS B N   1 
ATOM   7007 C  CA  . HIS B 1 409 ? -1.675  -1.577  59.371  1.00 12.88 ? 408  HIS B CA  1 
ATOM   7008 C  C   . HIS B 1 409 ? -2.304  -2.135  58.103  1.00 12.14 ? 408  HIS B C   1 
ATOM   7009 O  O   . HIS B 1 409 ? -3.251  -1.554  57.556  1.00 11.05 ? 408  HIS B O   1 
ATOM   7010 C  CB  . HIS B 1 409 ? -0.341  -0.902  59.055  1.00 11.83 ? 408  HIS B CB  1 
ATOM   7011 C  CG  . HIS B 1 409 ? -0.494  0.366   58.270  1.00 11.26 ? 408  HIS B CG  1 
ATOM   7012 N  ND1 . HIS B 1 409 ? -0.851  1.563   58.856  1.00 13.76 ? 408  HIS B ND1 1 
ATOM   7013 C  CD2 . HIS B 1 409 ? -0.409  0.608   56.937  1.00 11.78 ? 408  HIS B CD2 1 
ATOM   7014 C  CE1 . HIS B 1 409 ? -0.943  2.495   57.921  1.00 15.31 ? 408  HIS B CE1 1 
ATOM   7015 N  NE2 . HIS B 1 409 ? -0.677  1.942   56.749  1.00 14.17 ? 408  HIS B NE2 1 
ATOM   7016 N  N   . GLU B 1 410 ? -1.786  -3.265  57.627  1.00 12.23 ? 409  GLU B N   1 
ATOM   7017 C  CA  . GLU B 1 410 ? -2.356  -3.917  56.452  1.00 11.39 ? 409  GLU B CA  1 
ATOM   7018 C  C   . GLU B 1 410 ? -3.824  -4.274  56.675  1.00 12.22 ? 409  GLU B C   1 
ATOM   7019 O  O   . GLU B 1 410 ? -4.680  -3.995  55.827  1.00 12.15 ? 409  GLU B O   1 
ATOM   7020 C  CB  . GLU B 1 410 ? -1.544  -5.169  56.101  1.00 14.08 ? 409  GLU B CB  1 
ATOM   7021 C  CG  . GLU B 1 410 ? -2.141  -5.951  54.928  1.00 13.38 ? 409  GLU B CG  1 
ATOM   7022 C  CD  . GLU B 1 410 ? -1.404  -7.238  54.614  1.00 18.00 ? 409  GLU B CD  1 
ATOM   7023 O  OE1 . GLU B 1 410 ? -0.531  -7.655  55.415  1.00 20.22 ? 409  GLU B OE1 1 
ATOM   7024 O  OE2 . GLU B 1 410 ? -1.701  -7.840  53.561  1.00 18.45 ? 409  GLU B OE2 1 
ATOM   7025 N  N   . ALA B 1 411 ? -4.136  -4.901  57.813  1.00 10.99 ? 410  ALA B N   1 
ATOM   7026 C  CA  . ALA B 1 411 ? -5.507  -5.360  58.022  1.00 10.56 ? 410  ALA B CA  1 
ATOM   7027 C  C   . ALA B 1 411 ? -6.471  -4.193  58.216  1.00 11.74 ? 410  ALA B C   1 
ATOM   7028 O  O   . ALA B 1 411 ? -7.630  -4.281  57.790  1.00 11.20 ? 410  ALA B O   1 
ATOM   7029 C  CB  . ALA B 1 411 ? -5.580  -6.329  59.217  1.00 12.16 ? 410  ALA B CB  1 
ATOM   7030 N  N   . THR B 1 412 ? -6.025  -3.103  58.860  1.00 11.51 ? 411  THR B N   1 
ATOM   7031 C  CA  . THR B 1 412 ? -6.890  -1.936  59.010  1.00 11.25 ? 411  THR B CA  1 
ATOM   7032 C  C   . THR B 1 412 ? -7.158  -1.272  57.667  1.00 12.47 ? 411  THR B C   1 
ATOM   7033 O  O   . THR B 1 412 ? -8.304  -0.914  57.362  1.00 12.53 ? 411  THR B O   1 
ATOM   7034 C  CB  . THR B 1 412 ? -6.273  -0.933  59.993  1.00 10.37 ? 411  THR B CB  1 
ATOM   7035 O  OG1 . THR B 1 412 ? -6.045  -1.576  61.253  1.00 11.27 ? 411  THR B OG1 1 
ATOM   7036 C  CG2 . THR B 1 412 ? -7.198  0.259   60.215  1.00 12.14 ? 411  THR B CG2 1 
ATOM   7037 N  N   . LEU B 1 413 ? -6.107  -1.095  56.859  1.00 12.65 ? 412  LEU B N   1 
ATOM   7038 C  CA  . LEU B 1 413 ? -6.264  -0.555  55.512  1.00 11.24 ? 412  LEU B CA  1 
ATOM   7039 C  C   . LEU B 1 413 ? -7.247  -1.382  54.697  1.00 11.85 ? 412  LEU B C   1 
ATOM   7040 O  O   . LEU B 1 413 ? -8.179  -0.840  54.087  1.00 13.57 ? 412  LEU B O   1 
ATOM   7041 C  CB  . LEU B 1 413 ? -4.905  -0.517  54.811  1.00 10.75 ? 412  LEU B CB  1 
ATOM   7042 C  CG  . LEU B 1 413 ? -4.963  -0.299  53.297  1.00 15.18 ? 412  LEU B CG  1 
ATOM   7043 C  CD1 . LEU B 1 413 ? -5.495  1.101   52.992  1.00 16.55 ? 412  LEU B CD1 1 
ATOM   7044 C  CD2 . LEU B 1 413 ? -3.599  -0.508  52.686  1.00 18.72 ? 412  LEU B CD2 1 
ATOM   7045 N  N   . VAL B 1 414 ? -7.043  -2.701  54.657  1.00 11.58 ? 413  VAL B N   1 
ATOM   7046 C  CA  . VAL B 1 414 ? -7.830  -3.558  53.768  1.00 12.27 ? 413  VAL B CA  1 
ATOM   7047 C  C   . VAL B 1 414 ? -9.272  -3.650  54.250  1.00 12.70 ? 413  VAL B C   1 
ATOM   7048 O  O   . VAL B 1 414 ? -10.219 -3.517  53.458  1.00 13.17 ? 413  VAL B O   1 
ATOM   7049 C  CB  . VAL B 1 414 ? -7.175  -4.951  53.656  1.00 13.27 ? 413  VAL B CB  1 
ATOM   7050 C  CG1 . VAL B 1 414 ? -8.098  -5.948  52.941  1.00 18.75 ? 413  VAL B CG1 1 
ATOM   7051 C  CG2 . VAL B 1 414 ? -5.838  -4.834  52.924  1.00 16.35 ? 413  VAL B CG2 1 
ATOM   7052 N  N   . LEU B 1 415 ? -9.466  -3.894  55.551  1.00 13.21 ? 414  LEU B N   1 
ATOM   7053 C  CA  . LEU B 1 415 ? -10.826 -3.970  56.075  1.00 11.47 ? 414  LEU B CA  1 
ATOM   7054 C  C   . LEU B 1 415 ? -11.555 -2.639  55.901  1.00 12.51 ? 414  LEU B C   1 
ATOM   7055 O  O   . LEU B 1 415 ? -12.756 -2.615  55.589  1.00 12.17 ? 414  LEU B O   1 
ATOM   7056 C  CB  . LEU B 1 415 ? -10.805 -4.398  57.546  1.00 12.88 ? 414  LEU B CB  1 
ATOM   7057 C  CG  . LEU B 1 415 ? -12.145 -4.716  58.217  1.00 12.38 ? 414  LEU B CG  1 
ATOM   7058 C  CD1 . LEU B 1 415 ? -12.993 -5.656  57.363  1.00 13.14 ? 414  LEU B CD1 1 
ATOM   7059 C  CD2 . LEU B 1 415 ? -11.912 -5.324  59.597  1.00 14.20 ? 414  LEU B CD2 1 
ATOM   7060 N  N   . GLY B 1 416 ? -10.848 -1.520  56.098  1.00 11.14 ? 415  GLY B N   1 
ATOM   7061 C  CA  . GLY B 1 416 ? -11.445 -0.218  55.833  1.00 10.06 ? 415  GLY B CA  1 
ATOM   7062 C  C   . GLY B 1 416 ? -11.893 -0.071  54.388  1.00 12.26 ? 415  GLY B C   1 
ATOM   7063 O  O   . GLY B 1 416 ? -13.004 0.389   54.119  1.00 12.78 ? 415  GLY B O   1 
ATOM   7064 N  N   . MET B 1 417 ? -11.043 -0.476  53.436  1.00 10.60 ? 416  MET B N   1 
ATOM   7065 C  CA  . MET B 1 417 ? -11.432 -0.379  52.026  1.00 12.38 ? 416  MET B CA  1 
ATOM   7066 C  C   . MET B 1 417 ? -12.591 -1.319  51.691  1.00 13.65 ? 416  MET B C   1 
ATOM   7067 O  O   . MET B 1 417 ? -13.481 -0.956  50.906  1.00 12.99 ? 416  MET B O   1 
ATOM   7068 C  CB  . MET B 1 417 ? -10.230 -0.657  51.113  1.00 10.83 ? 416  MET B CB  1 
ATOM   7069 C  CG  . MET B 1 417 ? -9.215  0.468   51.117  1.00 14.57 ? 416  MET B CG  1 
ATOM   7070 S  SD  . MET B 1 417 ? -7.853  0.255   49.963  1.00 17.84 ? 416  MET B SD  1 
ATOM   7071 C  CE  . MET B 1 417 ? -8.703  0.553   48.413  1.00 19.66 ? 416  MET B CE  1 
ATOM   7072 N  N   . MET B 1 418 ? -12.587 -2.539  52.244  1.00 12.11 ? 417  MET B N   1 
ATOM   7073 C  CA  . MET B 1 418 ? -13.710 -3.451  52.026  1.00 12.25 ? 417  MET B CA  1 
ATOM   7074 C  C   . MET B 1 418 ? -15.023 -2.829  52.491  1.00 13.99 ? 417  MET B C   1 
ATOM   7075 O  O   . MET B 1 418 ? -16.040 -2.887  51.783  1.00 14.45 ? 417  MET B O   1 
ATOM   7076 C  CB  . MET B 1 418 ? -13.463 -4.780  52.747  1.00 11.74 ? 417  MET B CB  1 
ATOM   7077 C  CG  . MET B 1 418 ? -12.320 -5.603  52.170  1.00 13.15 ? 417  MET B CG  1 
ATOM   7078 S  SD  . MET B 1 418 ? -11.766 -6.973  53.230  1.00 17.47 ? 417  MET B SD  1 
ATOM   7079 C  CE  . MET B 1 418 ? -13.317 -7.781  53.617  1.00 16.75 ? 417  MET B CE  1 
ATOM   7080 N  N   . LEU B 1 419 ? -15.024 -2.235  53.692  1.00 13.89 ? 418  LEU B N   1 
ATOM   7081 C  CA  . LEU B 1 419 ? -16.257 -1.675  54.241  1.00 13.22 ? 418  LEU B CA  1 
ATOM   7082 C  C   . LEU B 1 419 ? -16.661 -0.392  53.529  1.00 15.29 ? 418  LEU B C   1 
ATOM   7083 O  O   . LEU B 1 419 ? -17.851 -0.049  53.499  1.00 16.47 ? 418  LEU B O   1 
ATOM   7084 C  CB  . LEU B 1 419 ? -16.096 -1.426  55.742  1.00 13.54 ? 418  LEU B CB  1 
ATOM   7085 C  CG  . LEU B 1 419 ? -15.901 -2.698  56.567  1.00 15.23 ? 418  LEU B CG  1 
ATOM   7086 C  CD1 . LEU B 1 419 ? -15.677 -2.343  58.030  1.00 17.45 ? 418  LEU B CD1 1 
ATOM   7087 C  CD2 . LEU B 1 419 ? -17.092 -3.663  56.413  1.00 18.06 ? 418  LEU B CD2 1 
ATOM   7088 N  N   . LYS B 1 420 ? -15.697 0.328   52.952  1.00 13.01 ? 419  LYS B N   1 
ATOM   7089 C  CA  . LYS B 1 420 ? -16.039 1.514   52.175  1.00 11.89 ? 419  LYS B CA  1 
ATOM   7090 C  C   . LYS B 1 420 ? -16.727 1.143   50.866  1.00 13.89 ? 419  LYS B C   1 
ATOM   7091 O  O   . LYS B 1 420 ? -17.674 1.819   50.445  1.00 14.49 ? 419  LYS B O   1 
ATOM   7092 C  CB  . LYS B 1 420 ? -14.786 2.347   51.890  1.00 12.10 ? 419  LYS B CB  1 
ATOM   7093 C  CG  . LYS B 1 420 ? -14.984 3.459   50.839  1.00 12.37 ? 419  LYS B CG  1 
ATOM   7094 C  CD  . LYS B 1 420 ? -13.660 4.174   50.545  1.00 13.88 ? 419  LYS B CD  1 
ATOM   7095 C  CE  . LYS B 1 420 ? -13.799 5.236   49.459  1.00 13.28 ? 419  LYS B CE  1 
ATOM   7096 N  NZ  . LYS B 1 420 ? -12.526 5.998   49.274  1.00 13.94 ? 419  LYS B NZ  1 
ATOM   7097 N  N   . HIS B 1 421 ? -16.272 0.073   50.209  1.00 11.91 ? 420  HIS B N   1 
ATOM   7098 C  CA  . HIS B 1 421 ? -16.679 -0.158  48.832  1.00 11.43 ? 420  HIS B CA  1 
ATOM   7099 C  C   . HIS B 1 421 ? -17.830 -1.144  48.647  1.00 12.78 ? 420  HIS B C   1 
ATOM   7100 O  O   . HIS B 1 421 ? -18.424 -1.157  47.559  1.00 13.36 ? 420  HIS B O   1 
ATOM   7101 C  CB  . HIS B 1 421 ? -15.464 -0.611  48.008  1.00 13.01 ? 420  HIS B CB  1 
ATOM   7102 C  CG  . HIS B 1 421 ? -14.528 0.509   47.675  1.00 14.91 ? 420  HIS B CG  1 
ATOM   7103 N  ND1 . HIS B 1 421 ? -14.760 1.384   46.633  1.00 16.11 ? 420  HIS B ND1 1 
ATOM   7104 C  CD2 . HIS B 1 421 ? -13.380 0.920   48.264  1.00 14.71 ? 420  HIS B CD2 1 
ATOM   7105 C  CE1 . HIS B 1 421 ? -13.783 2.273   46.582  1.00 16.52 ? 420  HIS B CE1 1 
ATOM   7106 N  NE2 . HIS B 1 421 ? -12.930 2.011   47.558  1.00 16.06 ? 420  HIS B NE2 1 
ATOM   7107 N  N   . PHE B 1 422 ? -18.180 -1.952  49.655  1.00 14.02 ? 421  PHE B N   1 
ATOM   7108 C  CA  . PHE B 1 422 ? -19.200 -2.987  49.497  1.00 13.45 ? 421  PHE B CA  1 
ATOM   7109 C  C   . PHE B 1 422 ? -20.075 -3.103  50.738  1.00 12.94 ? 421  PHE B C   1 
ATOM   7110 O  O   . PHE B 1 422 ? -19.627 -2.860  51.861  1.00 14.85 ? 421  PHE B O   1 
ATOM   7111 C  CB  . PHE B 1 422 ? -18.589 -4.384  49.248  1.00 12.49 ? 421  PHE B CB  1 
ATOM   7112 C  CG  . PHE B 1 422 ? -17.608 -4.425  48.113  1.00 12.53 ? 421  PHE B CG  1 
ATOM   7113 C  CD1 . PHE B 1 422 ? -18.039 -4.647  46.810  1.00 13.99 ? 421  PHE B CD1 1 
ATOM   7114 C  CD2 . PHE B 1 422 ? -16.258 -4.225  48.345  1.00 13.04 ? 421  PHE B CD2 1 
ATOM   7115 C  CE1 . PHE B 1 422 ? -17.137 -4.677  45.760  1.00 12.95 ? 421  PHE B CE1 1 
ATOM   7116 C  CE2 . PHE B 1 422 ? -15.343 -4.246  47.289  1.00 13.69 ? 421  PHE B CE2 1 
ATOM   7117 C  CZ  . PHE B 1 422 ? -15.790 -4.474  45.998  1.00 13.28 ? 421  PHE B CZ  1 
ATOM   7118 N  N   . ASP B 1 423 ? -21.330 -3.499  50.515  1.00 12.94 ? 422  ASP B N   1 
ATOM   7119 C  CA  . ASP B 1 423 ? -22.152 -4.142  51.536  1.00 15.41 ? 422  ASP B CA  1 
ATOM   7120 C  C   . ASP B 1 423 ? -21.973 -5.658  51.443  1.00 16.50 ? 422  ASP B C   1 
ATOM   7121 O  O   . ASP B 1 423 ? -21.789 -6.209  50.356  1.00 20.32 ? 422  ASP B O   1 
ATOM   7122 C  CB  . ASP B 1 423 ? -23.632 -3.786  51.361  1.00 18.27 ? 422  ASP B CB  1 
ATOM   7123 C  CG  . ASP B 1 423 ? -23.940 -2.347  51.731  1.00 22.78 ? 422  ASP B CG  1 
ATOM   7124 O  OD1 . ASP B 1 423 ? -23.717 -1.969  52.897  1.00 25.64 ? 422  ASP B OD1 1 
ATOM   7125 O  OD2 . ASP B 1 423 ? -24.408 -1.591  50.854  1.00 28.38 ? 422  ASP B OD2 1 
ATOM   7126 N  N   . PHE B 1 424 ? -22.036 -6.336  52.586  1.00 15.69 ? 423  PHE B N   1 
ATOM   7127 C  CA  . PHE B 1 424 ? -21.779 -7.771  52.632  1.00 14.99 ? 423  PHE B CA  1 
ATOM   7128 C  C   . PHE B 1 424 ? -23.001 -8.541  53.118  1.00 17.51 ? 423  PHE B C   1 
ATOM   7129 O  O   . PHE B 1 424 ? -23.751 -8.065  53.984  1.00 19.39 ? 423  PHE B O   1 
ATOM   7130 C  CB  . PHE B 1 424 ? -20.565 -8.077  53.519  1.00 14.73 ? 423  PHE B CB  1 
ATOM   7131 C  CG  . PHE B 1 424 ? -19.269 -7.559  52.953  1.00 14.10 ? 423  PHE B CG  1 
ATOM   7132 C  CD1 . PHE B 1 424 ? -18.563 -8.299  52.016  1.00 16.11 ? 423  PHE B CD1 1 
ATOM   7133 C  CD2 . PHE B 1 424 ? -18.776 -6.320  53.329  1.00 16.38 ? 423  PHE B CD2 1 
ATOM   7134 C  CE1 . PHE B 1 424 ? -17.377 -7.820  51.477  1.00 16.42 ? 423  PHE B CE1 1 
ATOM   7135 C  CE2 . PHE B 1 424 ? -17.585 -5.838  52.808  1.00 17.38 ? 423  PHE B CE2 1 
ATOM   7136 C  CZ  . PHE B 1 424 ? -16.885 -6.587  51.871  1.00 16.80 ? 423  PHE B CZ  1 
ATOM   7137 N  N   . GLU B 1 425 ? -23.189 -9.740  52.555  1.00 16.33 ? 424  GLU B N   1 
ATOM   7138 C  CA  . GLU B 1 425 ? -24.307 -10.619 52.886  1.00 16.83 ? 424  GLU B CA  1 
ATOM   7139 C  C   . GLU B 1 425 ? -23.785 -12.014 53.217  1.00 16.51 ? 424  GLU B C   1 
ATOM   7140 O  O   . GLU B 1 425 ? -23.040 -12.609 52.433  1.00 17.63 ? 424  GLU B O   1 
ATOM   7141 C  CB  . GLU B 1 425 ? -25.327 -10.715 51.740  1.00 19.65 ? 424  GLU B CB  1 
ATOM   7142 C  CG  . GLU B 1 425 ? -26.496 -11.657 52.058  1.00 23.31 ? 424  GLU B CG  1 
ATOM   7143 C  CD  . GLU B 1 425 ? -27.404 -11.929 50.863  1.00 30.15 ? 424  GLU B CD  1 
ATOM   7144 O  OE1 . GLU B 1 425 ? -27.110 -11.437 49.749  1.00 30.31 ? 424  GLU B OE1 1 
ATOM   7145 O  OE2 . GLU B 1 425 ? -28.417 -12.644 51.045  1.00 31.81 ? 424  GLU B OE2 1 
ATOM   7146 N  N   . ASP B 1 426 ? -24.183 -12.526 54.380  1.00 15.36 ? 425  ASP B N   1 
ATOM   7147 C  CA  . ASP B 1 426 ? -23.929 -13.911 54.791  1.00 15.63 ? 425  ASP B CA  1 
ATOM   7148 C  C   . ASP B 1 426 ? -25.032 -14.793 54.192  1.00 15.35 ? 425  ASP B C   1 
ATOM   7149 O  O   . ASP B 1 426 ? -25.958 -15.253 54.862  1.00 16.40 ? 425  ASP B O   1 
ATOM   7150 C  CB  . ASP B 1 426 ? -23.863 -13.972 56.315  1.00 16.02 ? 425  ASP B CB  1 
ATOM   7151 C  CG  . ASP B 1 426 ? -23.799 -15.386 56.877  1.00 15.99 ? 425  ASP B CG  1 
ATOM   7152 O  OD1 . ASP B 1 426 ? -23.263 -16.304 56.222  1.00 16.38 ? 425  ASP B OD1 1 
ATOM   7153 O  OD2 . ASP B 1 426 ? -24.279 -15.560 58.024  1.00 16.61 ? 425  ASP B OD2 1 
ATOM   7154 N  N   . HIS B 1 427 ? -24.926 -15.010 52.877  1.00 17.31 ? 426  HIS B N   1 
ATOM   7155 C  CA  . HIS B 1 427 ? -26.045 -15.573 52.127  1.00 17.63 ? 426  HIS B CA  1 
ATOM   7156 C  C   . HIS B 1 427 ? -26.275 -17.059 52.399  1.00 17.69 ? 426  HIS B C   1 
ATOM   7157 O  O   . HIS B 1 427 ? -27.371 -17.557 52.108  1.00 20.10 ? 426  HIS B O   1 
ATOM   7158 C  CB  . HIS B 1 427 ? -25.841 -15.344 50.627  1.00 16.58 ? 426  HIS B CB  1 
ATOM   7159 C  CG  . HIS B 1 427 ? -24.658 -16.065 50.067  1.00 16.29 ? 426  HIS B CG  1 
ATOM   7160 N  ND1 . HIS B 1 427 ? -23.365 -15.800 50.468  1.00 18.31 ? 426  HIS B ND1 1 
ATOM   7161 C  CD2 . HIS B 1 427 ? -24.571 -17.050 49.142  1.00 17.51 ? 426  HIS B CD2 1 
ATOM   7162 C  CE1 . HIS B 1 427 ? -22.532 -16.584 49.806  1.00 20.83 ? 426  HIS B CE1 1 
ATOM   7163 N  NE2 . HIS B 1 427 ? -23.238 -17.355 48.997  1.00 19.31 ? 426  HIS B NE2 1 
ATOM   7164 N  N   . THR B 1 428 ? -25.285 -17.783 52.934  1.00 15.28 ? 427  THR B N   1 
ATOM   7165 C  CA  . THR B 1 428 ? -25.456 -19.195 53.270  1.00 15.20 ? 427  THR B CA  1 
ATOM   7166 C  C   . THR B 1 428 ? -25.738 -19.429 54.750  1.00 15.90 ? 427  THR B C   1 
ATOM   7167 O  O   . THR B 1 428 ? -25.856 -20.587 55.166  1.00 17.22 ? 427  THR B O   1 
ATOM   7168 C  CB  . THR B 1 428 ? -24.218 -20.021 52.875  1.00 15.32 ? 427  THR B CB  1 
ATOM   7169 O  OG1 . THR B 1 428 ? -23.117 -19.721 53.760  1.00 16.33 ? 427  THR B OG1 1 
ATOM   7170 C  CG2 . THR B 1 428 ? -23.809 -19.764 51.430  1.00 14.08 ? 427  THR B CG2 1 
ATOM   7171 N  N   . ASN B 1 429 ? -25.860 -18.371 55.547  1.00 15.19 ? 428  ASN B N   1 
ATOM   7172 C  CA  . ASN B 1 429 ? -25.897 -18.470 57.011  1.00 14.80 ? 428  ASN B CA  1 
ATOM   7173 C  C   . ASN B 1 429 ? -24.795 -19.407 57.505  1.00 14.80 ? 428  ASN B C   1 
ATOM   7174 O  O   . ASN B 1 429 ? -25.035 -20.449 58.124  1.00 17.38 ? 428  ASN B O   1 
ATOM   7175 C  CB  . ASN B 1 429 ? -27.279 -18.913 57.509  1.00 16.93 ? 428  ASN B CB  1 
ATOM   7176 C  CG  . ASN B 1 429 ? -27.414 -18.789 59.014  1.00 23.95 ? 428  ASN B CG  1 
ATOM   7177 O  OD1 . ASN B 1 429 ? -26.643 -18.074 59.659  1.00 25.06 ? 428  ASN B OD1 1 
ATOM   7178 N  ND2 . ASN B 1 429 ? -28.395 -19.480 59.583  1.00 28.67 ? 428  ASN B ND2 1 
ATOM   7179 N  N   . TYR B 1 430 ? -23.561 -18.992 57.225  1.00 12.57 ? 429  TYR B N   1 
ATOM   7180 C  CA  . TYR B 1 430 ? -22.389 -19.849 57.381  1.00 12.72 ? 429  TYR B CA  1 
ATOM   7181 C  C   . TYR B 1 430 ? -22.177 -20.272 58.830  1.00 14.79 ? 429  TYR B C   1 
ATOM   7182 O  O   . TYR B 1 430 ? -22.213 -19.440 59.743  1.00 15.58 ? 429  TYR B O   1 
ATOM   7183 C  CB  . TYR B 1 430 ? -21.159 -19.104 56.857  1.00 14.14 ? 429  TYR B CB  1 
ATOM   7184 C  CG  . TYR B 1 430 ? -19.815 -19.691 57.260  1.00 12.87 ? 429  TYR B CG  1 
ATOM   7185 C  CD1 . TYR B 1 430 ? -19.313 -20.829 56.634  1.00 12.18 ? 429  TYR B CD1 1 
ATOM   7186 C  CD2 . TYR B 1 430 ? -19.040 -19.093 58.257  1.00 12.78 ? 429  TYR B CD2 1 
ATOM   7187 C  CE1 . TYR B 1 430 ? -18.075 -21.359 56.984  1.00 12.37 ? 429  TYR B CE1 1 
ATOM   7188 C  CE2 . TYR B 1 430 ? -17.804 -19.614 58.619  1.00 12.65 ? 429  TYR B CE2 1 
ATOM   7189 C  CZ  . TYR B 1 430 ? -17.328 -20.755 57.980  1.00 13.50 ? 429  TYR B CZ  1 
ATOM   7190 O  OH  . TYR B 1 430 ? -16.101 -21.284 58.331  1.00 14.19 ? 429  TYR B OH  1 
ATOM   7191 N  N   . GLU B 1 431 ? -21.949 -21.573 59.034  1.00 14.29 ? 430  GLU B N   1 
ATOM   7192 C  CA  . GLU B 1 431 ? -21.606 -22.122 60.345  1.00 14.33 ? 430  GLU B CA  1 
ATOM   7193 C  C   . GLU B 1 431 ? -20.086 -22.146 60.498  1.00 13.95 ? 430  GLU B C   1 
ATOM   7194 O  O   . GLU B 1 431 ? -19.389 -22.809 59.720  1.00 15.46 ? 430  GLU B O   1 
ATOM   7195 C  CB  . GLU B 1 431 ? -22.181 -23.529 60.520  1.00 20.70 ? 430  GLU B CB  1 
ATOM   7196 C  CG  . GLU B 1 431 ? -21.893 -24.141 61.895  1.00 28.86 ? 430  GLU B CG  1 
ATOM   7197 C  CD  . GLU B 1 431 ? -22.469 -25.537 62.064  1.00 40.15 ? 430  GLU B CD  1 
ATOM   7198 O  OE1 . GLU B 1 431 ? -23.234 -25.979 61.180  1.00 43.66 ? 430  GLU B OE1 1 
ATOM   7199 O  OE2 . GLU B 1 431 ? -22.155 -26.194 63.084  1.00 45.00 ? 430  GLU B OE2 1 
ATOM   7200 N  N   . LEU B 1 432 ? -19.578 -21.455 61.517  1.00 13.22 ? 431  LEU B N   1 
ATOM   7201 C  CA  . LEU B 1 432 ? -18.137 -21.356 61.713  1.00 13.83 ? 431  LEU B CA  1 
ATOM   7202 C  C   . LEU B 1 432 ? -17.493 -22.739 61.793  1.00 13.06 ? 431  LEU B C   1 
ATOM   7203 O  O   . LEU B 1 432 ? -17.913 -23.599 62.574  1.00 15.02 ? 431  LEU B O   1 
ATOM   7204 C  CB  . LEU B 1 432 ? -17.833 -20.546 62.976  1.00 14.39 ? 431  LEU B CB  1 
ATOM   7205 C  CG  . LEU B 1 432 ? -16.355 -20.248 63.263  1.00 15.16 ? 431  LEU B CG  1 
ATOM   7206 C  CD1 . LEU B 1 432 ? -15.659 -19.580 62.065  1.00 15.03 ? 431  LEU B CD1 1 
ATOM   7207 C  CD2 . LEU B 1 432 ? -16.194 -19.416 64.544  1.00 18.55 ? 431  LEU B CD2 1 
ATOM   7208 N  N   . ASP B 1 433 ? -16.459 -22.933 60.975  1.00 10.94 ? 432  ASP B N   1 
ATOM   7209 C  CA  . ASP B 1 433 ? -15.690 -24.172 60.889  1.00 13.23 ? 432  ASP B CA  1 
ATOM   7210 C  C   . ASP B 1 433 ? -14.227 -23.742 60.846  1.00 14.30 ? 432  ASP B C   1 
ATOM   7211 O  O   . ASP B 1 433 ? -13.786 -23.153 59.851  1.00 15.71 ? 432  ASP B O   1 
ATOM   7212 C  CB  . ASP B 1 433 ? -16.100 -24.959 59.639  1.00 14.73 ? 432  ASP B CB  1 
ATOM   7213 C  CG  . ASP B 1 433 ? -15.365 -26.277 59.489  1.00 17.65 ? 432  ASP B CG  1 
ATOM   7214 O  OD1 . ASP B 1 433 ? -14.587 -26.656 60.382  1.00 17.87 ? 432  ASP B OD1 1 
ATOM   7215 O  OD2 . ASP B 1 433 ? -15.572 -26.941 58.451  1.00 20.00 ? 432  ASP B OD2 1 
ATOM   7216 N  N   . ILE B 1 434 ? -13.485 -23.965 61.932  1.00 11.13 ? 433  ILE B N   1 
ATOM   7217 C  CA  . ILE B 1 434 ? -12.138 -23.414 62.073  1.00 10.51 ? 433  ILE B CA  1 
ATOM   7218 C  C   . ILE B 1 434 ? -11.129 -24.498 61.704  1.00 13.37 ? 433  ILE B C   1 
ATOM   7219 O  O   . ILE B 1 434 ? -10.985 -25.499 62.415  1.00 15.92 ? 433  ILE B O   1 
ATOM   7220 C  CB  . ILE B 1 434 ? -11.885 -22.878 63.487  1.00 11.33 ? 433  ILE B CB  1 
ATOM   7221 C  CG1 . ILE B 1 434 ? -12.826 -21.714 63.796  1.00 12.16 ? 433  ILE B CG1 1 
ATOM   7222 C  CG2 . ILE B 1 434 ? -10.430 -22.401 63.613  1.00 11.81 ? 433  ILE B CG2 1 
ATOM   7223 C  CD1 . ILE B 1 434 ? -12.857 -21.343 65.270  1.00 11.94 ? 433  ILE B CD1 1 
ATOM   7224 N  N   . LYS B 1 435 ? -10.435 -24.305 60.581  1.00 12.87 ? 434  LYS B N   1 
ATOM   7225 C  CA  . LYS B 1 435 ? -9.400  -25.238 60.144  1.00 12.99 ? 434  LYS B CA  1 
ATOM   7226 C  C   . LYS B 1 435 ? -8.097  -24.963 60.889  1.00 11.47 ? 434  LYS B C   1 
ATOM   7227 O  O   . LYS B 1 435 ? -7.721  -23.806 61.104  1.00 13.91 ? 434  LYS B O   1 
ATOM   7228 C  CB  . LYS B 1 435 ? -9.175  -25.122 58.634  1.00 15.03 ? 434  LYS B CB  1 
ATOM   7229 C  CG  . LYS B 1 435 ? -8.130  -26.084 58.058  1.00 17.45 ? 434  LYS B CG  1 
ATOM   7230 C  CD  . LYS B 1 435 ? -8.014  -25.903 56.546  1.00 20.60 ? 434  LYS B CD  1 
ATOM   7231 C  CE  . LYS B 1 435 ? -6.878  -26.729 55.949  1.00 25.96 ? 434  LYS B CE  1 
ATOM   7232 N  NZ  . LYS B 1 435 ? -7.094  -28.199 56.084  1.00 27.11 ? 434  LYS B NZ  1 
ATOM   7233 N  N   . GLU B 1 436 ? -7.415  -26.028 61.295  1.00 12.09 ? 435  GLU B N   1 
ATOM   7234 C  CA  . GLU B 1 436 ? -6.164  -25.911 62.037  1.00 11.07 ? 435  GLU B CA  1 
ATOM   7235 C  C   . GLU B 1 436 ? -5.000  -26.375 61.171  1.00 11.17 ? 435  GLU B C   1 
ATOM   7236 O  O   . GLU B 1 436 ? -5.042  -27.469 60.595  1.00 14.11 ? 435  GLU B O   1 
ATOM   7237 C  CB  . GLU B 1 436 ? -6.216  -26.710 63.342  1.00 11.95 ? 435  GLU B CB  1 
ATOM   7238 C  CG  . GLU B 1 436 ? -7.387  -26.303 64.237  1.00 12.67 ? 435  GLU B CG  1 
ATOM   7239 C  CD  . GLU B 1 436 ? -7.139  -26.570 65.719  1.00 11.12 ? 435  GLU B CD  1 
ATOM   7240 O  OE1 . GLU B 1 436 ? -5.974  -26.823 66.113  1.00 12.04 ? 435  GLU B OE1 1 
ATOM   7241 O  OE2 . GLU B 1 436 ? -8.111  -26.508 66.495  1.00 12.84 ? 435  GLU B OE2 1 
ATOM   7242 N  N   . THR B 1 437 ? -3.988  -25.517 61.058  1.00 12.02 ? 436  THR B N   1 
ATOM   7243 C  CA  . THR B 1 437 ? -2.713  -25.812 60.405  1.00 12.82 ? 436  THR B CA  1 
ATOM   7244 C  C   . THR B 1 437 ? -1.596  -25.274 61.294  1.00 13.70 ? 436  THR B C   1 
ATOM   7245 O  O   . THR B 1 437 ? -0.700  -24.560 60.848  1.00 16.90 ? 436  THR B O   1 
ATOM   7246 C  CB  . THR B 1 437 ? -2.630  -25.209 58.994  1.00 13.84 ? 436  THR B CB  1 
ATOM   7247 O  OG1 . THR B 1 437 ? -2.818  -23.786 59.058  1.00 15.17 ? 436  THR B OG1 1 
ATOM   7248 C  CG2 . THR B 1 437 ? -3.683  -25.809 58.079  1.00 13.25 ? 436  THR B CG2 1 
ATOM   7249 N  N   . LEU B 1 438 ? -1.660  -25.622 62.583  1.00 11.89 ? 437  LEU B N   1 
ATOM   7250 C  CA  . LEU B 1 438 ? -0.960  -24.907 63.650  1.00 12.59 ? 437  LEU B CA  1 
ATOM   7251 C  C   . LEU B 1 438 ? -1.652  -23.563 63.873  1.00 14.65 ? 437  LEU B C   1 
ATOM   7252 O  O   . LEU B 1 438 ? -2.181  -23.300 64.963  1.00 13.90 ? 437  LEU B O   1 
ATOM   7253 C  CB  . LEU B 1 438 ? 0.534   -24.736 63.326  1.00 13.97 ? 437  LEU B CB  1 
ATOM   7254 C  CG  . LEU B 1 438 ? 1.358   -26.014 63.037  1.00 13.85 ? 437  LEU B CG  1 
ATOM   7255 C  CD1 . LEU B 1 438 ? 2.850   -25.673 62.897  1.00 15.36 ? 437  LEU B CD1 1 
ATOM   7256 C  CD2 . LEU B 1 438 ? 1.159   -27.132 64.092  1.00 15.39 ? 437  LEU B CD2 1 
ATOM   7257 N  N   . THR B 1 439 ? -1.676  -22.722 62.838  1.00 15.16 ? 438  THR B N   1 
ATOM   7258 C  CA  . THR B 1 439 ? -2.493  -21.512 62.819  1.00 11.68 ? 438  THR B CA  1 
ATOM   7259 C  C   . THR B 1 439 ? -3.976  -21.860 62.618  1.00 11.03 ? 438  THR B C   1 
ATOM   7260 O  O   . THR B 1 439 ? -4.331  -22.975 62.239  1.00 12.37 ? 438  THR B O   1 
ATOM   7261 C  CB  . THR B 1 439 ? -2.030  -20.587 61.699  1.00 14.17 ? 438  THR B CB  1 
ATOM   7262 O  OG1 . THR B 1 439 ? -2.023  -21.329 60.467  1.00 15.80 ? 438  THR B OG1 1 
ATOM   7263 C  CG2 . THR B 1 439 ? -0.627  -20.052 61.982  1.00 15.33 ? 438  THR B CG2 1 
ATOM   7264 N  N   . LEU B 1 440 ? -4.845  -20.874 62.852  1.00 12.18 ? 439  LEU B N   1 
ATOM   7265 C  CA  . LEU B 1 440 ? -6.295  -21.039 62.790  1.00 11.74 ? 439  LEU B CA  1 
ATOM   7266 C  C   . LEU B 1 440 ? -6.890  -20.155 61.702  1.00 11.15 ? 439  LEU B C   1 
ATOM   7267 O  O   . LEU B 1 440 ? -6.491  -18.997 61.553  1.00 14.04 ? 439  LEU B O   1 
ATOM   7268 C  CB  . LEU B 1 440 ? -6.964  -20.664 64.122  1.00 12.79 ? 439  LEU B CB  1 
ATOM   7269 C  CG  . LEU B 1 440 ? -6.443  -21.325 65.398  1.00 11.66 ? 439  LEU B CG  1 
ATOM   7270 C  CD1 . LEU B 1 440 ? -7.212  -20.801 66.618  1.00 12.40 ? 439  LEU B CD1 1 
ATOM   7271 C  CD2 . LEU B 1 440 ? -6.554  -22.839 65.308  1.00 12.50 ? 439  LEU B CD2 1 
ATOM   7272 N  N   . LYS B 1 441 ? -7.895  -20.677 60.983  1.00 11.33 ? 440  LYS B N   1 
ATOM   7273 C  CA  . LYS B 1 441 ? -8.544  -19.872 59.952  1.00 12.51 ? 440  LYS B CA  1 
ATOM   7274 C  C   . LYS B 1 441 ? -9.907  -20.466 59.637  1.00 14.32 ? 440  LYS B C   1 
ATOM   7275 O  O   . LYS B 1 441 ? -10.023 -21.696 59.593  1.00 14.35 ? 440  LYS B O   1 
ATOM   7276 C  CB  . LYS B 1 441 ? -7.684  -19.814 58.677  1.00 16.45 ? 440  LYS B CB  1 
ATOM   7277 C  CG  . LYS B 1 441 ? -8.174  -18.770 57.669  1.00 20.62 ? 440  LYS B CG  1 
ATOM   7278 C  CD  . LYS B 1 441 ? -7.298  -18.683 56.409  1.00 24.94 ? 440  LYS B CD  1 
ATOM   7279 C  CE  . LYS B 1 441 ? -5.817  -18.588 56.736  1.00 30.81 ? 440  LYS B CE  1 
ATOM   7280 N  NZ  . LYS B 1 441 ? -5.128  -19.852 56.344  1.00 32.60 ? 440  LYS B NZ  1 
ATOM   7281 N  N   . PRO B 1 442 ? -10.946 -19.655 59.404  1.00 13.09 ? 441  PRO B N   1 
ATOM   7282 C  CA  . PRO B 1 442 ? -12.216 -20.224 58.929  1.00 12.93 ? 441  PRO B CA  1 
ATOM   7283 C  C   . PRO B 1 442 ? -12.022 -20.980 57.621  1.00 14.82 ? 441  PRO B C   1 
ATOM   7284 O  O   . PRO B 1 442 ? -11.236 -20.576 56.758  1.00 16.82 ? 441  PRO B O   1 
ATOM   7285 C  CB  . PRO B 1 442 ? -13.114 -18.997 58.737  1.00 13.74 ? 441  PRO B CB  1 
ATOM   7286 C  CG  . PRO B 1 442 ? -12.497 -17.917 59.586  1.00 13.80 ? 441  PRO B CG  1 
ATOM   7287 C  CD  . PRO B 1 442 ? -11.015 -18.188 59.533  1.00 11.79 ? 441  PRO B CD  1 
ATOM   7288 N  N   . GLU B 1 443 ? -12.744 -22.087 57.487  1.00 13.09 ? 442  GLU B N   1 
ATOM   7289 C  CA  . GLU B 1 443 ? -12.805 -22.857 56.251  1.00 14.60 ? 442  GLU B CA  1 
ATOM   7290 C  C   . GLU B 1 443 ? -14.216 -22.805 55.670  1.00 12.59 ? 442  GLU B C   1 
ATOM   7291 O  O   . GLU B 1 443 ? -15.204 -22.891 56.408  1.00 13.02 ? 442  GLU B O   1 
ATOM   7292 C  CB  . GLU B 1 443 ? -12.385 -24.318 56.495  1.00 15.95 ? 442  GLU B CB  1 
ATOM   7293 C  CG  . GLU B 1 443 ? -12.540 -25.187 55.269  1.00 21.07 ? 442  GLU B CG  1 
ATOM   7294 C  CD  . GLU B 1 443 ? -11.993 -26.589 55.442  1.00 27.49 ? 442  GLU B CD  1 
ATOM   7295 O  OE1 . GLU B 1 443 ? -11.757 -27.035 56.587  1.00 26.80 ? 442  GLU B OE1 1 
ATOM   7296 O  OE2 . GLU B 1 443 ? -11.797 -27.256 54.412  1.00 34.49 ? 442  GLU B OE2 1 
ATOM   7297 N  N   . GLY B 1 444 ? -14.311 -22.662 54.342  1.00 14.63 ? 443  GLY B N   1 
ATOM   7298 C  CA  . GLY B 1 444 ? -15.601 -22.667 53.662  1.00 14.99 ? 443  GLY B CA  1 
ATOM   7299 C  C   . GLY B 1 444 ? -16.435 -21.421 53.856  1.00 15.94 ? 443  GLY B C   1 
ATOM   7300 O  O   . GLY B 1 444 ? -17.618 -21.421 53.511  1.00 16.63 ? 443  GLY B O   1 
ATOM   7301 N  N   . PHE B 1 445 ? -15.851 -20.358 54.394  1.00 14.13 ? 444  PHE B N   1 
ATOM   7302 C  CA  . PHE B 1 445 ? -16.554 -19.105 54.636  1.00 13.46 ? 444  PHE B CA  1 
ATOM   7303 C  C   . PHE B 1 445 ? -16.714 -18.355 53.314  1.00 13.48 ? 444  PHE B C   1 
ATOM   7304 O  O   . PHE B 1 445 ? -15.720 -18.017 52.667  1.00 13.09 ? 444  PHE B O   1 
ATOM   7305 C  CB  . PHE B 1 445 ? -15.770 -18.286 55.662  1.00 14.42 ? 444  PHE B CB  1 
ATOM   7306 C  CG  . PHE B 1 445 ? -16.364 -16.935 55.972  1.00 13.31 ? 444  PHE B CG  1 
ATOM   7307 C  CD1 . PHE B 1 445 ? -17.741 -16.742 55.977  1.00 14.07 ? 444  PHE B CD1 1 
ATOM   7308 C  CD2 . PHE B 1 445 ? -15.532 -15.854 56.265  1.00 13.63 ? 444  PHE B CD2 1 
ATOM   7309 C  CE1 . PHE B 1 445 ? -18.286 -15.498 56.265  1.00 13.36 ? 444  PHE B CE1 1 
ATOM   7310 C  CE2 . PHE B 1 445 ? -16.059 -14.606 56.555  1.00 11.87 ? 444  PHE B CE2 1 
ATOM   7311 C  CZ  . PHE B 1 445 ? -17.455 -14.426 56.549  1.00 12.88 ? 444  PHE B CZ  1 
ATOM   7312 N  N   . VAL B 1 446 ? -17.965 -18.116 52.907  1.00 13.60 ? 445  VAL B N   1 
ATOM   7313 C  CA  . VAL B 1 446 ? -18.291 -17.403 51.679  1.00 14.68 ? 445  VAL B CA  1 
ATOM   7314 C  C   . VAL B 1 446 ? -19.299 -16.309 52.008  1.00 15.40 ? 445  VAL B C   1 
ATOM   7315 O  O   . VAL B 1 446 ? -20.081 -16.423 52.958  1.00 16.59 ? 445  VAL B O   1 
ATOM   7316 C  CB  . VAL B 1 446 ? -18.855 -18.349 50.590  1.00 14.93 ? 445  VAL B CB  1 
ATOM   7317 C  CG1 . VAL B 1 446 ? -17.795 -19.353 50.127  1.00 16.83 ? 445  VAL B CG1 1 
ATOM   7318 C  CG2 . VAL B 1 446 ? -20.088 -19.077 51.114  1.00 15.44 ? 445  VAL B CG2 1 
ATOM   7319 N  N   . VAL B 1 447 ? -19.271 -15.233 51.218  1.00 12.57 ? 446  VAL B N   1 
ATOM   7320 C  CA  . VAL B 1 447 ? -20.209 -14.119 51.337  1.00 14.17 ? 446  VAL B CA  1 
ATOM   7321 C  C   . VAL B 1 447 ? -20.509 -13.606 49.936  1.00 13.34 ? 446  VAL B C   1 
ATOM   7322 O  O   . VAL B 1 447 ? -19.848 -13.972 48.960  1.00 15.21 ? 446  VAL B O   1 
ATOM   7323 C  CB  . VAL B 1 447 ? -19.673 -12.963 52.218  1.00 13.01 ? 446  VAL B CB  1 
ATOM   7324 C  CG1 . VAL B 1 447 ? -19.379 -13.444 53.637  1.00 15.64 ? 446  VAL B CG1 1 
ATOM   7325 C  CG2 . VAL B 1 447 ? -18.443 -12.311 51.579  1.00 12.68 ? 446  VAL B CG2 1 
ATOM   7326 N  N   . LYS B 1 448 ? -21.529 -12.758 49.843  1.00 13.98 ? 447  LYS B N   1 
ATOM   7327 C  CA  . LYS B 1 448 ? -21.792 -11.974 48.647  1.00 15.03 ? 447  LYS B CA  1 
ATOM   7328 C  C   . LYS B 1 448 ? -21.549 -10.502 48.953  1.00 16.30 ? 447  LYS B C   1 
ATOM   7329 O  O   . LYS B 1 448 ? -21.887 -10.011 50.038  1.00 16.10 ? 447  LYS B O   1 
ATOM   7330 C  CB  . LYS B 1 448 ? -23.225 -12.187 48.135  1.00 16.98 ? 447  LYS B CB  1 
ATOM   7331 C  CG  . LYS B 1 448 ? -23.445 -13.527 47.440  1.00 18.99 ? 447  LYS B CG  1 
ATOM   7332 C  CD  . LYS B 1 448 ? -24.887 -13.702 46.964  1.00 20.47 ? 447  LYS B CD  1 
ATOM   7333 C  CE  . LYS B 1 448 ? -25.052 -15.038 46.261  1.00 24.48 ? 447  LYS B CE  1 
ATOM   7334 N  NZ  . LYS B 1 448 ? -26.436 -15.243 45.744  1.00 29.18 ? 447  LYS B NZ  1 
ATOM   7335 N  N   . ALA B 1 449 ? -20.947 -9.800  48.003  1.00 16.23 ? 448  ALA B N   1 
ATOM   7336 C  CA  . ALA B 1 449 ? -20.667 -8.380  48.148  1.00 16.72 ? 448  ALA B CA  1 
ATOM   7337 C  C   . ALA B 1 449 ? -21.505 -7.603  47.145  1.00 22.26 ? 448  ALA B C   1 
ATOM   7338 O  O   . ALA B 1 449 ? -21.561 -7.963  45.965  1.00 29.27 ? 448  ALA B O   1 
ATOM   7339 C  CB  . ALA B 1 449 ? -19.179 -8.088  47.946  1.00 19.28 ? 448  ALA B CB  1 
ATOM   7340 N  N   . LYS B 1 450 ? -22.163 -6.552  47.612  1.00 18.99 ? 449  LYS B N   1 
ATOM   7341 C  CA  . LYS B 1 450 ? -22.905 -5.654  46.739  1.00 21.30 ? 449  LYS B CA  1 
ATOM   7342 C  C   . LYS B 1 450 ? -22.162 -4.327  46.697  1.00 18.68 ? 449  LYS B C   1 
ATOM   7343 O  O   . LYS B 1 450 ? -22.018 -3.657  47.728  1.00 19.13 ? 449  LYS B O   1 
ATOM   7344 C  CB  . LYS B 1 450 ? -24.340 -5.466  47.226  1.00 26.81 ? 449  LYS B CB  1 
ATOM   7345 C  CG  . LYS B 1 450 ? -25.185 -4.584  46.319  1.00 34.57 ? 449  LYS B CG  1 
ATOM   7346 C  CD  . LYS B 1 450 ? -26.576 -4.370  46.901  1.00 38.99 ? 449  LYS B CD  1 
ATOM   7347 C  CE  . LYS B 1 450 ? -27.325 -3.279  46.153  1.00 42.53 ? 449  LYS B CE  1 
ATOM   7348 N  NZ  . LYS B 1 450 ? -27.456 -2.032  46.971  1.00 46.82 ? 449  LYS B NZ  1 
ATOM   7349 N  N   . SER B 1 451 ? -21.681 -3.961  45.513  1.00 16.00 ? 450  SER B N   1 
ATOM   7350 C  CA  . SER B 1 451 ? -20.860 -2.765  45.375  1.00 16.49 ? 450  SER B CA  1 
ATOM   7351 C  C   . SER B 1 451 ? -21.638 -1.508  45.743  1.00 16.50 ? 450  SER B C   1 
ATOM   7352 O  O   . SER B 1 451 ? -22.791 -1.333  45.345  1.00 19.01 ? 450  SER B O   1 
ATOM   7353 C  CB  . SER B 1 451 ? -20.348 -2.638  43.939  1.00 17.82 ? 450  SER B CB  1 
ATOM   7354 O  OG  . SER B 1 451 ? -19.602 -1.445  43.776  1.00 19.25 ? 450  SER B OG  1 
ATOM   7355 N  N   . LYS B 1 452 ? -20.988 -0.615  46.490  1.00 14.58 ? 451  LYS B N   1 
ATOM   7356 C  CA  . LYS B 1 452 ? -21.524 0.726   46.691  1.00 18.76 ? 451  LYS B CA  1 
ATOM   7357 C  C   . LYS B 1 452 ? -21.214 1.658   45.524  1.00 20.49 ? 451  LYS B C   1 
ATOM   7358 O  O   . LYS B 1 452 ? -21.619 2.824   45.559  1.00 21.41 ? 451  LYS B O   1 
ATOM   7359 C  CB  . LYS B 1 452 ? -20.988 1.318   48.002  1.00 19.13 ? 451  LYS B CB  1 
ATOM   7360 C  CG  . LYS B 1 452 ? -21.384 0.525   49.239  1.00 22.44 ? 451  LYS B CG  1 
ATOM   7361 C  CD  . LYS B 1 452 ? -20.819 1.154   50.502  1.00 24.40 ? 451  LYS B CD  1 
ATOM   7362 C  CE  . LYS B 1 452 ? -21.263 0.398   51.733  1.00 26.20 ? 451  LYS B CE  1 
ATOM   7363 N  NZ  . LYS B 1 452 ? -22.726 0.550   51.941  1.00 34.13 ? 451  LYS B NZ  1 
ATOM   7364 N  N   . LYS B 1 453 ? -20.505 1.168   44.506  1.00 19.60 ? 452  LYS B N   1 
ATOM   7365 C  CA  . LYS B 1 453 ? -20.200 1.920   43.281  1.00 21.56 ? 452  LYS B CA  1 
ATOM   7366 C  C   . LYS B 1 453 ? -19.434 3.213   43.573  1.00 21.92 ? 452  LYS B C   1 
ATOM   7367 O  O   . LYS B 1 453 ? -19.750 4.286   43.043  1.00 22.80 ? 452  LYS B O   1 
ATOM   7368 C  CB  . LYS B 1 453 ? -21.477 2.206   42.480  1.00 25.06 ? 452  LYS B CB  1 
ATOM   7369 C  CG  . LYS B 1 453 ? -22.251 0.956   42.064  1.00 29.85 ? 452  LYS B CG  1 
ATOM   7370 C  CD  . LYS B 1 453 ? -21.455 0.076   41.102  1.00 34.44 ? 452  LYS B CD  1 
ATOM   7371 C  CE  . LYS B 1 453 ? -22.264 -1.142  40.655  1.00 37.18 ? 452  LYS B CE  1 
ATOM   7372 N  NZ  . LYS B 1 453 ? -21.445 -2.142  39.905  1.00 39.94 ? 452  LYS B NZ  1 
ATOM   7373 N  N   . ILE B 1 454 ? -18.391 3.099   44.387  1.00 19.21 ? 453  ILE B N   1 
ATOM   7374 C  CA  . ILE B 1 454 ? -17.509 4.220   44.705  1.00 20.05 ? 453  ILE B CA  1 
ATOM   7375 C  C   . ILE B 1 454 ? -16.224 4.051   43.901  1.00 21.38 ? 453  ILE B C   1 
ATOM   7376 O  O   . ILE B 1 454 ? -15.547 3.020   44.050  1.00 20.84 ? 453  ILE B O   1 
ATOM   7377 C  CB  . ILE B 1 454 ? -17.214 4.298   46.210  1.00 20.65 ? 453  ILE B CB  1 
ATOM   7378 C  CG1 . ILE B 1 454 ? -18.517 4.434   46.997  1.00 22.58 ? 453  ILE B CG1 1 
ATOM   7379 C  CG2 . ILE B 1 454 ? -16.275 5.468   46.525  1.00 20.21 ? 453  ILE B CG2 1 
ATOM   7380 C  CD1 . ILE B 1 454 ? -18.328 4.279   48.479  1.00 24.97 ? 453  ILE B CD1 1 
ATOM   7381 N  N   . PRO B 1 455 ? -15.849 5.013   43.061  1.00 23.96 ? 454  PRO B N   1 
ATOM   7382 C  CA  . PRO B 1 455 ? -14.704 4.804   42.170  1.00 24.94 ? 454  PRO B CA  1 
ATOM   7383 C  C   . PRO B 1 455 ? -13.393 4.715   42.929  1.00 24.65 ? 454  PRO B C   1 
ATOM   7384 O  O   . PRO B 1 455 ? -13.236 5.262   44.026  1.00 24.54 ? 454  PRO B O   1 
ATOM   7385 C  CB  . PRO B 1 455 ? -14.724 6.040   41.261  1.00 27.57 ? 454  PRO B CB  1 
ATOM   7386 C  CG  . PRO B 1 455 ? -16.112 6.575   41.368  1.00 28.27 ? 454  PRO B CG  1 
ATOM   7387 C  CD  . PRO B 1 455 ? -16.554 6.272   42.763  1.00 26.30 ? 454  PRO B CD  1 
ATOM   7388 N  N   . LEU B 1 456 ? -12.449 4.003   42.324  1.00 23.05 ? 455  LEU B N   1 
ATOM   7389 C  CA  . LEU B 1 456 ? -11.078 3.926   42.808  1.00 24.31 ? 455  LEU B CA  1 
ATOM   7390 C  C   . LEU B 1 456 ? -10.207 4.939   42.071  1.00 28.27 ? 455  LEU B C   1 
ATOM   7391 O  O   . LEU B 1 456 ? -10.666 5.614   41.144  1.00 29.24 ? 455  LEU B O   1 
ATOM   7392 C  CB  . LEU B 1 456 ? -10.516 2.514   42.618  1.00 24.97 ? 455  LEU B CB  1 
ATOM   7393 C  CG  . LEU B 1 456 ? -10.993 1.447   43.600  1.00 22.18 ? 455  LEU B CG  1 
ATOM   7394 C  CD1 . LEU B 1 456 ? -10.713 0.045   43.053  1.00 22.07 ? 455  LEU B CD1 1 
ATOM   7395 C  CD2 . LEU B 1 456 ? -10.303 1.656   44.948  1.00 21.19 ? 455  LEU B CD2 1 
ATOM   7396 O  OXT . LEU B 1 456 ? -9.021  5.093   42.366  1.00 31.88 ? 455  LEU B OXT 1 
HETATM 7397 C  CHA . HEM C 2 .   ? -17.897 -14.229 9.110   1.00 9.99  ? 501  HEM A CHA 1 
HETATM 7398 C  CHB . HEM C 2 .   ? -13.066 -13.533 9.407   1.00 12.23 ? 501  HEM A CHB 1 
HETATM 7399 C  CHC . HEM C 2 .   ? -13.681 -11.269 13.746  1.00 12.87 ? 501  HEM A CHC 1 
HETATM 7400 C  CHD . HEM C 2 .   ? -18.473 -12.241 13.528  1.00 11.63 ? 501  HEM A CHD 1 
HETATM 7401 C  C1A . HEM C 2 .   ? -16.531 -14.198 8.833   1.00 10.16 ? 501  HEM A C1A 1 
HETATM 7402 C  C2A . HEM C 2 .   ? -15.959 -14.730 7.639   1.00 10.25 ? 501  HEM A C2A 1 
HETATM 7403 C  C3A . HEM C 2 .   ? -14.606 -14.532 7.703   1.00 9.48  ? 501  HEM A C3A 1 
HETATM 7404 C  C4A . HEM C 2 .   ? -14.320 -13.900 8.932   1.00 10.33 ? 501  HEM A C4A 1 
HETATM 7405 C  CMA . HEM C 2 .   ? -13.574 -14.932 6.672   1.00 10.02 ? 501  HEM A CMA 1 
HETATM 7406 C  CAA . HEM C 2 .   ? -16.686 -15.360 6.456   1.00 10.13 ? 501  HEM A CAA 1 
HETATM 7407 C  CBA . HEM C 2 .   ? -16.860 -16.874 6.640   1.00 11.10 ? 501  HEM A CBA 1 
HETATM 7408 C  CGA . HEM C 2 .   ? -17.493 -17.586 5.465   1.00 8.92  ? 501  HEM A CGA 1 
HETATM 7409 O  O1A . HEM C 2 .   ? -17.827 -18.794 5.608   1.00 12.32 ? 501  HEM A O1A 1 
HETATM 7410 O  O2A . HEM C 2 .   ? -17.687 -17.013 4.351   1.00 10.55 ? 501  HEM A O2A 1 
HETATM 7411 C  C1B . HEM C 2 .   ? -12.875 -12.841 10.629  1.00 11.10 ? 501  HEM A C1B 1 
HETATM 7412 C  C2B . HEM C 2 .   ? -11.580 -12.448 11.065  1.00 9.80  ? 501  HEM A C2B 1 
HETATM 7413 C  C3B . HEM C 2 .   ? -11.722 -11.802 12.269  1.00 12.10 ? 501  HEM A C3B 1 
HETATM 7414 C  C4B . HEM C 2 .   ? -13.158 -11.830 12.575  1.00 12.08 ? 501  HEM A C4B 1 
HETATM 7415 C  CMB . HEM C 2 .   ? -10.291 -12.709 10.312  1.00 12.48 ? 501  HEM A CMB 1 
HETATM 7416 C  CAB . HEM C 2 .   ? -10.706 -11.197 13.161  1.00 11.78 ? 501  HEM A CAB 1 
HETATM 7417 C  CBB . HEM C 2 .   ? -9.595  -10.601 12.713  1.00 12.49 ? 501  HEM A CBB 1 
HETATM 7418 C  C1C . HEM C 2 .   ? -15.036 -11.332 14.069  1.00 12.53 ? 501  HEM A C1C 1 
HETATM 7419 C  C2C . HEM C 2 .   ? -15.648 -10.780 15.201  1.00 14.16 ? 501  HEM A C2C 1 
HETATM 7420 C  C3C . HEM C 2 .   ? -16.993 -11.095 15.134  1.00 13.38 ? 501  HEM A C3C 1 
HETATM 7421 C  C4C . HEM C 2 .   ? -17.219 -11.790 13.911  1.00 11.67 ? 501  HEM A C4C 1 
HETATM 7422 C  CMC . HEM C 2 .   ? -14.964 -9.949  16.263  1.00 16.11 ? 501  HEM A CMC 1 
HETATM 7423 C  CAC . HEM C 2 .   ? -18.051 -10.710 16.095  1.00 12.59 ? 501  HEM A CAC 1 
HETATM 7424 C  CBC . HEM C 2 .   ? -18.032 -9.541  16.733  1.00 13.17 ? 501  HEM A CBC 1 
HETATM 7425 C  C1D . HEM C 2 .   ? -18.718 -12.868 12.298  1.00 10.63 ? 501  HEM A C1D 1 
HETATM 7426 C  C2D . HEM C 2 .   ? -20.040 -13.318 11.865  1.00 11.27 ? 501  HEM A C2D 1 
HETATM 7427 C  C3D . HEM C 2 .   ? -19.875 -13.862 10.631  1.00 10.38 ? 501  HEM A C3D 1 
HETATM 7428 C  C4D . HEM C 2 .   ? -18.447 -13.761 10.311  1.00 9.93  ? 501  HEM A C4D 1 
HETATM 7429 C  CMD . HEM C 2 .   ? -21.279 -13.428 12.739  1.00 10.72 ? 501  HEM A CMD 1 
HETATM 7430 C  CAD . HEM C 2 .   ? -20.963 -14.414 9.745   1.00 11.39 ? 501  HEM A CAD 1 
HETATM 7431 C  CBD . HEM C 2 .   ? -21.516 -13.194 8.980   1.00 12.18 ? 501  HEM A CBD 1 
HETATM 7432 C  CGD . HEM C 2 .   ? -22.694 -13.493 8.081   1.00 13.12 ? 501  HEM A CGD 1 
HETATM 7433 O  O1D . HEM C 2 .   ? -22.605 -14.386 7.209   1.00 12.26 ? 501  HEM A O1D 1 
HETATM 7434 O  O2D . HEM C 2 .   ? -23.762 -12.836 8.191   1.00 13.21 ? 501  HEM A O2D 1 
HETATM 7435 N  NA  . HEM C 2 .   ? -15.488 -13.710 9.612   1.00 11.36 ? 501  HEM A NA  1 
HETATM 7436 N  NB  . HEM C 2 .   ? -13.777 -12.471 11.563  1.00 11.98 ? 501  HEM A NB  1 
HETATM 7437 N  NC  . HEM C 2 .   ? -15.989 -11.935 13.300  1.00 11.83 ? 501  HEM A NC  1 
HETATM 7438 N  ND  . HEM C 2 .   ? -17.828 -13.183 11.357  1.00 11.39 ? 501  HEM A ND  1 
HETATM 7439 FE FE  A HEM C 2 .   ? -15.798 -12.807 11.452  0.50 11.85 ? 501  HEM A FE  1 
HETATM 7440 FE FE  B HEM C 2 .   ? -15.828 -12.760 11.421  0.50 13.40 ? 501  HEM A FE  1 
HETATM 7441 C  CAF A SYN D 3 .   ? -15.243 -18.216 13.341  0.70 21.33 ? 502  SYN A CAF 1 
HETATM 7442 C  CAD A SYN D 3 .   ? -14.427 -18.785 14.303  0.70 22.12 ? 502  SYN A CAD 1 
HETATM 7443 C  CAC A SYN D 3 .   ? -14.604 -20.099 14.672  0.70 22.66 ? 502  SYN A CAC 1 
HETATM 7444 C  CAE A SYN D 3 .   ? -15.602 -20.847 14.089  0.70 24.64 ? 502  SYN A CAE 1 
HETATM 7445 C  CAG A SYN D 3 .   ? -16.425 -20.281 13.130  0.70 23.64 ? 502  SYN A CAG 1 
HETATM 7446 C  CAH A SYN D 3 .   ? -16.257 -18.955 12.732  0.70 21.20 ? 502  SYN A CAH 1 
HETATM 7447 C  CAB A SYN D 3 .   ? -17.130 -18.350 11.711  0.70 15.50 ? 502  SYN A CAB 1 
HETATM 7448 C  CAA A SYN D 3 .   ? -16.905 -17.253 11.040  0.70 20.01 ? 502  SYN A CAA 1 
HETATM 7449 O  O1  A OXY E 4 .   ? -15.510 -14.690 12.198  0.50 11.08 ? 503  OXY A O1  1 
HETATM 7450 O  O2  A OXY E 4 .   ? -14.634 -14.704 13.210  0.50 14.47 ? 503  OXY A O2  1 
HETATM 7451 C  C1  . D0L F 5 .   ? -12.896 -30.763 1.791   1.00 21.71 ? 504  D0L A C1  1 
HETATM 7452 C  C2  . D0L F 5 .   ? -12.954 -30.919 3.172   1.00 18.41 ? 504  D0L A C2  1 
HETATM 7453 C  C15 . D0L F 5 .   ? -11.540 -24.726 6.567   1.00 25.06 ? 504  D0L A C15 1 
HETATM 7454 C  C14 . D0L F 5 .   ? -10.304 -26.221 8.009   1.00 23.15 ? 504  D0L A C14 1 
HETATM 7455 C  C7  . D0L F 5 .   ? -12.286 -29.914 4.088   1.00 16.13 ? 504  D0L A C7  1 
HETATM 7456 C  C12 . D0L F 5 .   ? -9.208  -27.560 6.308   1.00 19.64 ? 504  D0L A C12 1 
HETATM 7457 C  C10 . D0L F 5 .   ? -10.913 -27.074 4.546   1.00 16.34 ? 504  D0L A C10 1 
HETATM 7458 C  C3  . D0L F 5 .   ? -13.611 -32.026 3.708   1.00 21.87 ? 504  D0L A C3  1 
HETATM 7459 C  C13 . D0L F 5 .   ? -9.498  -27.498 7.803   1.00 21.88 ? 504  D0L A C13 1 
HETATM 7460 C  C11 . D0L F 5 .   ? -10.136 -26.510 5.696   1.00 17.66 ? 504  D0L A C11 1 
HETATM 7461 C  C6  . D0L F 5 .   ? -13.499 -31.693 0.945   1.00 22.53 ? 504  D0L A C6  1 
HETATM 7462 C  C8  . D0L F 5 .   ? -12.871 -28.501 4.007   1.00 14.82 ? 504  D0L A C8  1 
HETATM 7463 C  C5  . D0L F 5 .   ? -14.160 -32.793 1.483   1.00 23.35 ? 504  D0L A C5  1 
HETATM 7464 C  C9  . D0L F 5 .   ? -14.298 -28.527 4.497   1.00 16.10 ? 504  D0L A C9  1 
HETATM 7465 C  C4  . D0L F 5 .   ? -14.214 -32.958 2.862   1.00 24.03 ? 504  D0L A C4  1 
HETATM 7466 O  O2  . D0L F 5 .   ? -14.523 -28.275 5.708   1.00 15.96 ? 504  D0L A O2  1 
HETATM 7467 O  O3  . D0L F 5 .   ? -10.447 -27.026 3.415   1.00 17.59 ? 504  D0L A O3  1 
HETATM 7468 O  O1  . D0L F 5 .   ? -15.212 -28.813 3.696   1.00 16.98 ? 504  D0L A O1  1 
HETATM 7469 N  N2  . D0L F 5 .   ? -11.064 -26.106 6.769   1.00 21.94 ? 504  D0L A N2  1 
HETATM 7470 C  C16 . D0L F 5 .   ? -12.691 -24.427 7.526   1.00 30.17 ? 504  D0L A C16 1 
HETATM 7471 C  C17 . D0L F 5 .   ? -13.100 -22.959 7.462   1.00 32.77 ? 504  D0L A C17 1 
HETATM 7472 C  C18 . D0L F 5 .   ? -13.592 -22.451 8.816   1.00 35.90 ? 504  D0L A C18 1 
HETATM 7473 C  C19 . D0L F 5 .   ? -12.980 -21.091 9.132   1.00 37.05 ? 504  D0L A C19 1 
HETATM 7474 C  C20 . D0L F 5 .   ? -13.288 -20.665 10.561  1.00 39.39 ? 504  D0L A C20 1 
HETATM 7475 C  C21 . D0L F 5 .   ? -14.467 -21.452 11.084  1.00 42.39 ? 504  D0L A C21 1 
HETATM 7476 N  N1  . D0L F 5 .   ? -12.088 -27.620 4.861   1.00 14.13 ? 504  D0L A N1  1 
HETATM 7477 C  C1  . GOL G 6 .   ? -28.390 -15.589 -2.847  1.00 34.20 ? 505  GOL A C1  1 
HETATM 7478 O  O1  . GOL G 6 .   ? -27.451 -15.912 -3.840  1.00 31.50 ? 505  GOL A O1  1 
HETATM 7479 C  C2  . GOL G 6 .   ? -29.666 -16.410 -3.133  1.00 39.96 ? 505  GOL A C2  1 
HETATM 7480 O  O2  . GOL G 6 .   ? -29.832 -16.658 -4.484  1.00 42.97 ? 505  GOL A O2  1 
HETATM 7481 C  C3  . GOL G 6 .   ? -29.523 -17.702 -2.282  1.00 40.81 ? 505  GOL A C3  1 
HETATM 7482 O  O3  . GOL G 6 .   ? -30.620 -18.525 -2.594  1.00 44.09 ? 505  GOL A O3  1 
HETATM 7483 C  CHA . HEM H 2 .   ? 6.238   -14.147 66.379  1.00 11.28 ? 501  HEM B CHA 1 
HETATM 7484 C  CHB . HEM H 2 .   ? 1.359   -13.743 66.218  1.00 10.85 ? 501  HEM B CHB 1 
HETATM 7485 C  CHC . HEM H 2 .   ? 1.738   -11.325 61.934  1.00 12.87 ? 501  HEM B CHC 1 
HETATM 7486 C  CHD . HEM H 2 .   ? 6.584   -12.055 61.978  1.00 11.14 ? 501  HEM B CHD 1 
HETATM 7487 C  C1A . HEM H 2 .   ? 4.880   -14.211 66.690  1.00 10.14 ? 501  HEM B C1A 1 
HETATM 7488 C  C2A . HEM H 2 .   ? 4.367   -14.797 67.883  1.00 9.54  ? 501  HEM B C2A 1 
HETATM 7489 C  C3A . HEM H 2 .   ? 2.998   -14.677 67.851  1.00 10.09 ? 501  HEM B C3A 1 
HETATM 7490 C  C4A . HEM H 2 .   ? 2.642   -14.039 66.648  1.00 12.62 ? 501  HEM B C4A 1 
HETATM 7491 C  CMA . HEM H 2 .   ? 2.013   -15.153 68.897  1.00 12.43 ? 501  HEM B CMA 1 
HETATM 7492 C  CAA . HEM H 2 .   ? 5.160   -15.404 69.044  1.00 10.17 ? 501  HEM B CAA 1 
HETATM 7493 C  CBA . HEM H 2 .   ? 5.414   -16.896 68.816  1.00 13.59 ? 501  HEM B CBA 1 
HETATM 7494 C  CGA . HEM H 2 .   ? 6.091   -17.608 69.960  1.00 11.66 ? 501  HEM B CGA 1 
HETATM 7495 O  O1A . HEM H 2 .   ? 6.462   -18.793 69.783  1.00 11.11 ? 501  HEM B O1A 1 
HETATM 7496 O  O2A . HEM H 2 .   ? 6.291   -17.058 71.077  1.00 11.89 ? 501  HEM B O2A 1 
HETATM 7497 C  C1B . HEM H 2 .   ? 1.094   -13.028 65.022  1.00 12.20 ? 501  HEM B C1B 1 
HETATM 7498 C  C2B . HEM H 2 .   ? -0.238  -12.700 64.617  1.00 11.06 ? 501  HEM B C2B 1 
HETATM 7499 C  C3B . HEM H 2 .   ? -0.148  -12.012 63.429  1.00 10.42 ? 501  HEM B C3B 1 
HETATM 7500 C  C4B . HEM H 2 .   ? 1.279   -11.952 63.101  1.00 10.65 ? 501  HEM B C4B 1 
HETATM 7501 C  CMB . HEM H 2 .   ? -1.507  -13.094 65.353  1.00 11.05 ? 501  HEM B CMB 1 
HETATM 7502 C  CAB . HEM H 2 .   ? -1.185  -11.423 62.546  1.00 10.61 ? 501  HEM B CAB 1 
HETATM 7503 C  CBB . HEM H 2 .   ? -2.320  -10.902 63.017  1.00 13.18 ? 501  HEM B CBB 1 
HETATM 7504 C  C1C . HEM H 2 .   ? 3.082   -11.309 61.569  1.00 10.94 ? 501  HEM B C1C 1 
HETATM 7505 C  C2C . HEM H 2 .   ? 3.625   -10.709 60.426  1.00 11.82 ? 501  HEM B C2C 1 
HETATM 7506 C  C3C . HEM H 2 .   ? 4.993   -10.956 60.441  1.00 12.63 ? 501  HEM B C3C 1 
HETATM 7507 C  C4C . HEM H 2 .   ? 5.294   -11.658 61.644  1.00 11.30 ? 501  HEM B C4C 1 
HETATM 7508 C  CMC . HEM H 2 .   ? 2.845   -9.857  59.441  1.00 12.52 ? 501  HEM B CMC 1 
HETATM 7509 C  CAC . HEM H 2 .   ? 6.003   -10.513 59.459  1.00 14.63 ? 501  HEM B CAC 1 
HETATM 7510 C  CBC . HEM H 2 .   ? 5.934   -9.359  58.793  1.00 15.38 ? 501  HEM B CBC 1 
HETATM 7511 C  C1D . HEM H 2 .   ? 6.903   -12.695 63.193  1.00 12.11 ? 501  HEM B C1D 1 
HETATM 7512 C  C2D . HEM H 2 .   ? 8.262   -13.080 63.586  1.00 11.41 ? 501  HEM B C2D 1 
HETATM 7513 C  C3D . HEM H 2 .   ? 8.153   -13.659 64.812  1.00 12.77 ? 501  HEM B C3D 1 
HETATM 7514 C  C4D . HEM H 2 .   ? 6.730   -13.644 65.167  1.00 11.34 ? 501  HEM B C4D 1 
HETATM 7515 C  CMD . HEM H 2 .   ? 9.490   -13.085 62.694  1.00 9.87  ? 501  HEM B CMD 1 
HETATM 7516 C  CAD . HEM H 2 .   ? 9.287   -14.162 65.671  1.00 12.91 ? 501  HEM B CAD 1 
HETATM 7517 C  CBD . HEM H 2 .   ? 9.781   -12.961 66.492  1.00 11.73 ? 501  HEM B CBD 1 
HETATM 7518 C  CGD . HEM H 2 .   ? 11.025  -13.265 67.308  1.00 12.60 ? 501  HEM B CGD 1 
HETATM 7519 O  O1D . HEM H 2 .   ? 10.982  -14.169 68.174  1.00 13.25 ? 501  HEM B O1D 1 
HETATM 7520 O  O2D . HEM H 2 .   ? 12.099  -12.609 67.132  1.00 12.07 ? 501  HEM B O2D 1 
HETATM 7521 N  NA  . HEM H 2 .   ? 3.787   -13.764 65.945  1.00 12.05 ? 501  HEM B NA  1 
HETATM 7522 N  NB  . HEM H 2 .   ? 1.956   -12.582 64.080  1.00 11.07 ? 501  HEM B NB  1 
HETATM 7523 N  NC  . HEM H 2 .   ? 4.086   -11.876 62.295  1.00 11.09 ? 501  HEM B NC  1 
HETATM 7524 N  ND  . HEM H 2 .   ? 6.053   -13.071 64.147  1.00 11.04 ? 501  HEM B ND  1 
HETATM 7525 FE FE  A HEM H 2 .   ? 3.995   -12.806 64.118  0.50 11.85 ? 501  HEM B FE  1 
HETATM 7526 FE FE  B HEM H 2 .   ? 4.023   -12.755 64.152  0.50 13.17 ? 501  HEM B FE  1 
HETATM 7527 C  CAF A SYN I 3 .   ? 5.047   -20.191 62.407  0.70 19.96 ? 502  SYN B CAF 1 
HETATM 7528 C  CAD A SYN I 3 .   ? 4.278   -20.847 61.460  0.70 21.25 ? 502  SYN B CAD 1 
HETATM 7529 C  CAC A SYN I 3 .   ? 3.203   -20.211 60.881  0.70 18.90 ? 502  SYN B CAC 1 
HETATM 7530 C  CAE A SYN I 3 .   ? 2.892   -18.920 61.244  0.70 20.67 ? 502  SYN B CAE 1 
HETATM 7531 C  CAG A SYN I 3 .   ? 3.651   -18.263 62.197  0.70 19.32 ? 502  SYN B CAG 1 
HETATM 7532 C  CAH A SYN I 3 .   ? 4.746   -18.886 62.796  0.70 19.70 ? 502  SYN B CAH 1 
HETATM 7533 C  CAB A SYN I 3 .   ? 5.553   -18.187 63.809  0.70 16.42 ? 502  SYN B CAB 1 
HETATM 7534 C  CAA A SYN I 3 .   ? 5.220   -17.112 64.462  0.70 18.81 ? 502  SYN B CAA 1 
HETATM 7535 O  O1  A OXY J 4 .   ? 3.824   -14.708 63.302  0.50 10.66 ? 503  OXY B O1  1 
HETATM 7536 O  O2  A OXY J 4 .   ? 2.831   -14.875 62.343  0.50 13.68 ? 503  OXY B O2  1 
HETATM 7537 C  C1  . D0L K 5 .   ? 2.144   -31.148 73.601  1.00 19.08 ? 504  D0L B C1  1 
HETATM 7538 C  C2  . D0L K 5 .   ? 2.183   -31.316 72.213  1.00 19.72 ? 504  D0L B C2  1 
HETATM 7539 C  C15 . D0L K 5 .   ? 0.436   -25.078 69.076  1.00 26.70 ? 504  D0L B C15 1 
HETATM 7540 C  C14 . D0L K 5 .   ? -0.751  -26.579 67.568  1.00 22.89 ? 504  D0L B C14 1 
HETATM 7541 C  C7  . D0L K 5 .   ? 1.570   -30.302 71.266  1.00 18.61 ? 504  D0L B C7  1 
HETATM 7542 C  C12 . D0L K 5 .   ? -1.754  -27.966 69.274  1.00 16.71 ? 504  D0L B C12 1 
HETATM 7543 C  C10 . D0L K 5 .   ? 0.059   -27.540 70.956  1.00 13.80 ? 504  D0L B C10 1 
HETATM 7544 C  C3  . D0L K 5 .   ? 2.756   -32.474 71.688  1.00 20.45 ? 504  D0L B C3  1 
HETATM 7545 C  C13 . D0L K 5 .   ? -1.504  -27.891 67.767  1.00 22.57 ? 504  D0L B C13 1 
HETATM 7546 C  C11 . D0L K 5 .   ? -0.785  -26.944 69.867  1.00 14.41 ? 504  D0L B C11 1 
HETATM 7547 C  C6  . D0L K 5 .   ? 2.701   -32.120 74.436  1.00 19.42 ? 504  D0L B C6  1 
HETATM 7548 C  C8  . D0L K 5 .   ? 2.090   -28.861 71.397  1.00 16.01 ? 504  D0L B C8  1 
HETATM 7549 C  C5  . D0L K 5 .   ? 3.289   -33.270 73.903  1.00 18.25 ? 504  D0L B C5  1 
HETATM 7550 C  C9  . D0L K 5 .   ? 3.503   -28.787 70.890  1.00 16.32 ? 504  D0L B C9  1 
HETATM 7551 C  C4  . D0L K 5 .   ? 3.312   -33.447 72.522  1.00 20.63 ? 504  D0L B C4  1 
HETATM 7552 O  O2  . D0L K 5 .   ? 4.459   -29.040 71.659  1.00 15.65 ? 504  D0L B O2  1 
HETATM 7553 O  O3  . D0L K 5 .   ? -0.359  -27.580 72.107  1.00 16.50 ? 504  D0L B O3  1 
HETATM 7554 O  O1  . D0L K 5 .   ? 3.670   -28.486 69.689  1.00 15.82 ? 504  D0L B O1  1 
HETATM 7555 N  N2  . D0L K 5 .   ? 0.070   -26.474 68.766  1.00 20.73 ? 504  D0L B N2  1 
HETATM 7556 C  C16 . D0L K 5 .   ? 1.512   -24.547 68.144  1.00 28.69 ? 504  D0L B C16 1 
HETATM 7557 C  C17 . D0L K 5 .   ? 1.366   -23.041 67.994  1.00 31.93 ? 504  D0L B C17 1 
HETATM 7558 C  C18 . D0L K 5 .   ? 2.085   -22.543 66.746  1.00 33.09 ? 504  D0L B C18 1 
HETATM 7559 C  C19 . D0L K 5 .   ? 1.504   -21.204 66.320  1.00 32.47 ? 504  D0L B C19 1 
HETATM 7560 C  C20 . D0L K 5 .   ? 1.976   -20.815 64.927  1.00 32.38 ? 504  D0L B C20 1 
HETATM 7561 C  C21 . D0L K 5 .   ? 3.234   -21.572 64.571  1.00 37.45 ? 504  D0L B C21 1 
HETATM 7562 N  N1  . D0L K 5 .   ? 1.249   -28.006 70.579  1.00 14.09 ? 504  D0L B N1  1 
HETATM 7563 C  C1  . GOL L 6 .   ? 19.043  -17.362 77.291  1.00 50.09 ? 505  GOL B C1  1 
HETATM 7564 O  O1  . GOL L 6 .   ? 18.161  -18.110 76.524  1.00 51.15 ? 505  GOL B O1  1 
HETATM 7565 C  C2  . GOL L 6 .   ? 18.242  -16.865 78.509  1.00 47.38 ? 505  GOL B C2  1 
HETATM 7566 O  O2  . GOL L 6 .   ? 19.042  -16.206 79.420  1.00 46.92 ? 505  GOL B O2  1 
HETATM 7567 C  C3  . GOL L 6 .   ? 17.150  -15.936 77.932  1.00 45.89 ? 505  GOL B C3  1 
HETATM 7568 O  O3  . GOL L 6 .   ? 16.355  -15.558 79.009  1.00 41.50 ? 505  GOL B O3  1 
HETATM 7569 C  C1  . GOL M 6 .   ? 4.805   -7.749  74.477  1.00 33.52 ? 506  GOL B C1  1 
HETATM 7570 O  O1  . GOL M 6 .   ? 4.804   -8.315  75.755  1.00 29.69 ? 506  GOL B O1  1 
HETATM 7571 C  C2  . GOL M 6 .   ? 3.425   -8.038  73.834  1.00 36.97 ? 506  GOL B C2  1 
HETATM 7572 O  O2  . GOL M 6 .   ? 2.374   -7.754  74.709  1.00 37.64 ? 506  GOL B O2  1 
HETATM 7573 C  C3  . GOL M 6 .   ? 3.407   -7.161  72.536  1.00 38.02 ? 506  GOL B C3  1 
HETATM 7574 O  O3  . GOL M 6 .   ? 2.120   -7.225  71.993  1.00 38.80 ? 506  GOL B O3  1 
HETATM 7575 C  C1  . GOL N 6 .   ? -4.488  1.875   62.726  0.50 29.44 ? 507  GOL B C1  1 
HETATM 7576 O  O1  . GOL N 6 .   ? -3.254  2.253   63.272  0.50 32.52 ? 507  GOL B O1  1 
HETATM 7577 C  C2  . GOL N 6 .   ? -5.337  1.283   63.879  0.50 28.33 ? 507  GOL B C2  1 
HETATM 7578 O  O2  . GOL N 6 .   ? -6.576  1.901   63.985  0.50 27.10 ? 507  GOL B O2  1 
HETATM 7579 C  C3  . GOL N 6 .   ? -5.459  -0.224  63.549  0.50 26.54 ? 507  GOL B C3  1 
HETATM 7580 O  O3  . GOL N 6 .   ? -5.162  -0.932  64.708  0.50 31.96 ? 507  GOL B O3  1 
HETATM 7581 H  H2  . GOL N 6 .   ? -4.897  1.419   64.733  0.50 34.00 ? 507  GOL B H2  1 
HETATM 7582 O  O   . HOH O 7 .   ? -20.187 -32.223 14.573  1.00 44.26 ? 601  HOH A O   1 
HETATM 7583 O  O   . HOH O 7 .   ? -27.923 -23.317 -14.554 1.00 33.57 ? 602  HOH A O   1 
HETATM 7584 O  O   . HOH O 7 .   ? -42.715 -7.675  15.314  1.00 47.17 ? 603  HOH A O   1 
HETATM 7585 O  O   . HOH O 7 .   ? 11.571  -0.131  27.700  1.00 54.59 ? 604  HOH A O   1 
HETATM 7586 O  O   . HOH O 7 .   ? -16.668 -7.074  6.517   1.00 27.79 ? 605  HOH A O   1 
HETATM 7587 O  O   . HOH O 7 .   ? -22.712 5.695   21.396  1.00 49.45 ? 606  HOH A O   1 
HETATM 7588 O  O   . HOH O 7 .   ? 1.219   7.608   11.500  1.00 49.07 ? 607  HOH A O   1 
HETATM 7589 O  O   B HOH O 7 .   ? -14.154 -14.870 13.756  0.20 13.29 ? 608  HOH A O   1 
HETATM 7590 O  O   . HOH O 7 .   ? -16.843 -27.148 -0.982  1.00 25.84 ? 609  HOH A O   1 
HETATM 7591 O  O   . HOH O 7 .   ? 5.318   -17.628 -0.668  1.00 46.58 ? 610  HOH A O   1 
HETATM 7592 O  O   . HOH O 7 .   ? -17.873 -40.719 -3.865  1.00 50.60 ? 611  HOH A O   1 
HETATM 7593 O  O   . HOH O 7 .   ? -11.238 1.595   14.387  1.00 37.18 ? 612  HOH A O   1 
HETATM 7594 O  O   . HOH O 7 .   ? 9.540   -0.021  21.249  1.00 37.80 ? 613  HOH A O   1 
HETATM 7595 O  O   . HOH O 7 .   ? -6.571  -4.832  36.607  1.00 16.98 ? 614  HOH A O   1 
HETATM 7596 O  O   . HOH O 7 .   ? 0.793   -32.394 7.957   1.00 54.60 ? 615  HOH A O   1 
HETATM 7597 O  O   . HOH O 7 .   ? -12.801 -8.948  18.562  1.00 33.12 ? 616  HOH A O   1 
HETATM 7598 O  O   . HOH O 7 .   ? -34.173 -7.193  3.870   1.00 37.34 ? 617  HOH A O   1 
HETATM 7599 O  O   . HOH O 7 .   ? 11.893  6.184   17.719  1.00 53.01 ? 618  HOH A O   1 
HETATM 7600 O  O   . HOH O 7 .   ? -22.412 -36.213 20.079  1.00 62.60 ? 619  HOH A O   1 
HETATM 7601 O  O   . HOH O 7 .   ? -20.494 -15.612 6.515   1.00 11.96 ? 620  HOH A O   1 
HETATM 7602 O  O   . HOH O 7 .   ? -15.598 -35.337 5.983   1.00 37.58 ? 621  HOH A O   1 
HETATM 7603 O  O   . HOH O 7 .   ? -14.419 0.282   33.196  1.00 47.40 ? 622  HOH A O   1 
HETATM 7604 O  O   . HOH O 7 .   ? 10.891  -15.476 21.980  1.00 19.75 ? 623  HOH A O   1 
HETATM 7605 O  O   . HOH O 7 .   ? -8.617  9.863   26.133  1.00 34.23 ? 624  HOH A O   1 
HETATM 7606 O  O   . HOH O 7 .   ? -1.302  -22.940 26.413  1.00 48.19 ? 625  HOH A O   1 
HETATM 7607 O  O   . HOH O 7 .   ? -4.926  -23.143 -14.668 1.00 35.18 ? 626  HOH A O   1 
HETATM 7608 O  O   . HOH O 7 .   ? -7.680  -2.093  35.622  1.00 24.81 ? 627  HOH A O   1 
HETATM 7609 O  O   . HOH O 7 .   ? 1.542   1.634   33.195  1.00 35.14 ? 628  HOH A O   1 
HETATM 7610 O  O   . HOH O 7 .   ? 9.784   -17.993 12.743  1.00 23.92 ? 629  HOH A O   1 
HETATM 7611 O  O   . HOH O 7 .   ? -22.346 -17.484 -15.873 1.00 36.76 ? 630  HOH A O   1 
HETATM 7612 O  O   . HOH O 7 .   ? 8.296   -21.452 22.879  1.00 35.61 ? 631  HOH A O   1 
HETATM 7613 O  O   . HOH O 7 .   ? -23.921 -10.146 8.421   1.00 22.79 ? 632  HOH A O   1 
HETATM 7614 O  O   . HOH O 7 .   ? -8.685  12.989  24.570  1.00 47.82 ? 633  HOH A O   1 
HETATM 7615 O  O   . HOH O 7 .   ? 12.280  2.715   25.070  1.00 51.98 ? 634  HOH A O   1 
HETATM 7616 O  O   . HOH O 7 .   ? 6.519   -7.177  31.677  1.00 39.94 ? 635  HOH A O   1 
HETATM 7617 O  O   . HOH O 7 .   ? -32.204 -14.941 4.447   1.00 16.93 ? 636  HOH A O   1 
HETATM 7618 O  O   . HOH O 7 .   ? -3.040  -11.650 -11.345 1.00 39.52 ? 637  HOH A O   1 
HETATM 7619 O  O   . HOH O 7 .   ? -6.167  -10.911 -12.468 1.00 30.80 ? 638  HOH A O   1 
HETATM 7620 O  O   . HOH O 7 .   ? 1.116   -26.293 16.565  1.00 31.20 ? 639  HOH A O   1 
HETATM 7621 O  O   . HOH O 7 .   ? -33.222 -21.712 9.732   1.00 23.74 ? 640  HOH A O   1 
HETATM 7622 O  O   . HOH O 7 .   ? -13.305 -9.705  21.027  1.00 20.75 ? 641  HOH A O   1 
HETATM 7623 O  O   . HOH O 7 .   ? -10.302 -14.306 -14.501 1.00 26.31 ? 642  HOH A O   1 
HETATM 7624 O  O   . HOH O 7 .   ? -21.417 -9.082  -9.678  1.00 38.64 ? 643  HOH A O   1 
HETATM 7625 O  O   . HOH O 7 .   ? -4.038  -40.301 -7.237  1.00 20.79 ? 644  HOH A O   1 
HETATM 7626 O  O   . HOH O 7 .   ? -25.897 -20.100 -16.638 1.00 55.59 ? 645  HOH A O   1 
HETATM 7627 O  O   . HOH O 7 .   ? -13.321 -2.653  35.722  1.00 17.70 ? 646  HOH A O   1 
HETATM 7628 O  O   . HOH O 7 .   ? -19.049 -30.221 -12.868 1.00 46.01 ? 647  HOH A O   1 
HETATM 7629 O  O   . HOH O 7 .   ? 0.690   -22.002 23.138  1.00 21.78 ? 648  HOH A O   1 
HETATM 7630 O  O   . HOH O 7 .   ? -11.030 -7.242  2.071   1.00 33.10 ? 649  HOH A O   1 
HETATM 7631 O  O   . HOH O 7 .   ? -22.074 -9.308  6.670   1.00 32.77 ? 650  HOH A O   1 
HETATM 7632 O  O   . HOH O 7 .   ? 7.851   -22.026 10.817  1.00 48.15 ? 651  HOH A O   1 
HETATM 7633 O  O   . HOH O 7 .   ? -13.047 2.230   30.499  1.00 35.97 ? 652  HOH A O   1 
HETATM 7634 O  O   . HOH O 7 .   ? -35.463 -10.545 6.528   1.00 23.10 ? 653  HOH A O   1 
HETATM 7635 O  O   . HOH O 7 .   ? 13.506  -7.810  27.870  1.00 50.88 ? 654  HOH A O   1 
HETATM 7636 O  O   . HOH O 7 .   ? -4.652  -0.467  6.393   1.00 30.40 ? 655  HOH A O   1 
HETATM 7637 O  O   . HOH O 7 .   ? -24.955 -31.279 24.872  1.00 43.38 ? 656  HOH A O   1 
HETATM 7638 O  O   . HOH O 7 .   ? -18.447 0.675   26.669  1.00 28.84 ? 657  HOH A O   1 
HETATM 7639 O  O   . HOH O 7 .   ? -7.693  -7.024  40.464  1.00 15.08 ? 658  HOH A O   1 
HETATM 7640 O  O   . HOH O 7 .   ? -14.303 -27.448 -14.289 1.00 29.77 ? 659  HOH A O   1 
HETATM 7641 O  O   . HOH O 7 .   ? -2.713  -28.087 14.942  1.00 20.41 ? 660  HOH A O   1 
HETATM 7642 O  O   . HOH O 7 .   ? 8.474   -23.147 18.030  1.00 23.42 ? 661  HOH A O   1 
HETATM 7643 O  O   . HOH O 7 .   ? -0.917  0.378   -1.574  1.00 36.89 ? 662  HOH A O   1 
HETATM 7644 O  O   . HOH O 7 .   ? 7.495   7.847   12.663  1.00 51.62 ? 663  HOH A O   1 
HETATM 7645 O  O   . HOH O 7 .   ? -25.362 -14.261 -3.948  1.00 16.82 ? 664  HOH A O   1 
HETATM 7646 O  O   . HOH O 7 .   ? -9.621  12.382  22.114  1.00 26.38 ? 665  HOH A O   1 
HETATM 7647 O  O   . HOH O 7 .   ? -21.090 -3.184  33.449  1.00 52.42 ? 666  HOH A O   1 
HETATM 7648 O  O   . HOH O 7 .   ? -39.884 -14.234 16.300  1.00 36.36 ? 667  HOH A O   1 
HETATM 7649 O  O   . HOH O 7 .   ? -20.534 -30.791 3.080   1.00 48.19 ? 668  HOH A O   1 
HETATM 7650 O  O   . HOH O 7 .   ? -24.019 -27.519 -3.629  1.00 47.65 ? 669  HOH A O   1 
HETATM 7651 O  O   . HOH O 7 .   ? -13.935 -9.868  32.047  1.00 13.10 ? 670  HOH A O   1 
HETATM 7652 O  O   . HOH O 7 .   ? 12.822  -7.647  18.085  1.00 31.63 ? 671  HOH A O   1 
HETATM 7653 O  O   . HOH O 7 .   ? -16.190 -22.534 5.101   1.00 15.17 ? 672  HOH A O   1 
HETATM 7654 O  O   . HOH O 7 .   ? 4.281   1.686   30.640  1.00 21.62 ? 673  HOH A O   1 
HETATM 7655 O  O   . HOH O 7 .   ? -3.705  -14.244 -10.292 1.00 18.68 ? 674  HOH A O   1 
HETATM 7656 O  O   . HOH O 7 .   ? 11.305  -16.587 31.236  1.00 39.13 ? 675  HOH A O   1 
HETATM 7657 O  O   . HOH O 7 .   ? -10.274 -10.387 33.385  1.00 12.34 ? 676  HOH A O   1 
HETATM 7658 O  O   . HOH O 7 .   ? -5.096  -24.059 -5.432  1.00 16.77 ? 677  HOH A O   1 
HETATM 7659 O  O   . HOH O 7 .   ? -12.525 -12.631 16.680  1.00 19.48 ? 678  HOH A O   1 
HETATM 7660 O  O   . HOH O 7 .   ? 0.384   8.735   31.493  1.00 55.88 ? 679  HOH A O   1 
HETATM 7661 O  O   . HOH O 7 .   ? 14.230  -10.714 12.723  1.00 49.96 ? 680  HOH A O   1 
HETATM 7662 O  O   . HOH O 7 .   ? -2.462  4.609   27.707  1.00 24.82 ? 681  HOH A O   1 
HETATM 7663 O  O   . HOH O 7 .   ? -4.598  -21.983 -17.267 1.00 56.74 ? 682  HOH A O   1 
HETATM 7664 O  O   . HOH O 7 .   ? -9.830  10.483  14.585  1.00 33.01 ? 683  HOH A O   1 
HETATM 7665 O  O   . HOH O 7 .   ? -37.569 -16.616 11.794  1.00 25.61 ? 684  HOH A O   1 
HETATM 7666 O  O   . HOH O 7 .   ? -4.884  2.115   8.434   1.00 24.59 ? 685  HOH A O   1 
HETATM 7667 O  O   . HOH O 7 .   ? 4.100   -17.092 -3.475  1.00 44.37 ? 686  HOH A O   1 
HETATM 7668 O  O   . HOH O 7 .   ? -27.807 -14.307 -10.420 1.00 47.60 ? 687  HOH A O   1 
HETATM 7669 O  O   . HOH O 7 .   ? -24.993 -29.382 10.246  1.00 37.31 ? 688  HOH A O   1 
HETATM 7670 O  O   . HOH O 7 .   ? -18.969 -29.769 -6.052  1.00 19.51 ? 689  HOH A O   1 
HETATM 7671 O  O   . HOH O 7 .   ? 11.313  -5.789  19.418  1.00 41.01 ? 690  HOH A O   1 
HETATM 7672 O  O   . HOH O 7 .   ? 9.849   -9.181  6.664   1.00 25.87 ? 691  HOH A O   1 
HETATM 7673 O  O   . HOH O 7 .   ? 2.074   9.171   24.208  1.00 31.30 ? 692  HOH A O   1 
HETATM 7674 O  O   . HOH O 7 .   ? -0.221  -28.317 -12.029 1.00 38.04 ? 693  HOH A O   1 
HETATM 7675 O  O   . HOH O 7 .   ? -33.222 -21.141 15.372  1.00 25.30 ? 694  HOH A O   1 
HETATM 7676 O  O   . HOH O 7 .   ? -36.268 -11.061 20.270  1.00 30.61 ? 695  HOH A O   1 
HETATM 7677 O  O   . HOH O 7 .   ? -23.474 -19.178 13.327  1.00 13.52 ? 696  HOH A O   1 
HETATM 7678 O  O   . HOH O 7 .   ? -13.492 -43.452 10.020  1.00 55.92 ? 697  HOH A O   1 
HETATM 7679 O  O   . HOH O 7 .   ? -17.443 -39.330 14.353  1.00 37.74 ? 698  HOH A O   1 
HETATM 7680 O  O   . HOH O 7 .   ? -21.403 8.069   15.369  1.00 45.59 ? 699  HOH A O   1 
HETATM 7681 O  O   . HOH O 7 .   ? -34.741 -22.268 12.731  1.00 41.12 ? 700  HOH A O   1 
HETATM 7682 O  O   . HOH O 7 .   ? -17.651 -12.310 -12.732 1.00 43.33 ? 701  HOH A O   1 
HETATM 7683 O  O   . HOH O 7 .   ? 9.314   -4.191  6.032   1.00 33.24 ? 702  HOH A O   1 
HETATM 7684 O  O   . HOH O 7 .   ? -26.517 -30.731 17.709  1.00 44.62 ? 703  HOH A O   1 
HETATM 7685 O  O   . HOH O 7 .   ? 11.204  -18.090 28.214  1.00 35.46 ? 704  HOH A O   1 
HETATM 7686 O  O   . HOH O 7 .   ? 6.280   -15.001 5.878   1.00 36.89 ? 705  HOH A O   1 
HETATM 7687 O  O   . HOH O 7 .   ? 8.525   -1.393  6.141   1.00 34.89 ? 706  HOH A O   1 
HETATM 7688 O  O   . HOH O 7 .   ? -19.134 -31.469 -8.887  1.00 41.24 ? 707  HOH A O   1 
HETATM 7689 O  O   . HOH O 7 .   ? 4.019   -13.616 37.766  1.00 27.94 ? 708  HOH A O   1 
HETATM 7690 O  O   . HOH O 7 .   ? -27.712 -8.054  1.734   1.00 30.15 ? 709  HOH A O   1 
HETATM 7691 O  O   . HOH O 7 .   ? 9.014   -7.500  40.566  1.00 43.45 ? 710  HOH A O   1 
HETATM 7692 O  O   . HOH O 7 .   ? -4.240  8.490   24.507  1.00 24.45 ? 711  HOH A O   1 
HETATM 7693 O  O   . HOH O 7 .   ? -17.911 -14.569 3.150   1.00 12.63 ? 712  HOH A O   1 
HETATM 7694 O  O   . HOH O 7 .   ? -13.470 -15.031 -17.526 1.00 37.33 ? 713  HOH A O   1 
HETATM 7695 O  O   . HOH O 7 .   ? -26.081 -25.145 20.734  1.00 25.03 ? 714  HOH A O   1 
HETATM 7696 O  O   . HOH O 7 .   ? 3.614   -23.392 7.808   1.00 33.31 ? 715  HOH A O   1 
HETATM 7697 O  O   . HOH O 7 .   ? 6.302   -2.473  35.197  1.00 39.28 ? 716  HOH A O   1 
HETATM 7698 O  O   . HOH O 7 .   ? -30.710 -4.992  27.305  1.00 40.18 ? 717  HOH A O   1 
HETATM 7699 O  O   . HOH O 7 .   ? 7.104   -0.315  21.645  1.00 22.95 ? 718  HOH A O   1 
HETATM 7700 O  O   . HOH O 7 .   ? -3.779  12.524  19.560  1.00 25.92 ? 719  HOH A O   1 
HETATM 7701 O  O   . HOH O 7 .   ? 7.680   -16.314 9.467   1.00 42.28 ? 720  HOH A O   1 
HETATM 7702 O  O   . HOH O 7 .   ? 6.507   9.545   18.424  1.00 37.94 ? 721  HOH A O   1 
HETATM 7703 O  O   . HOH O 7 .   ? -2.170  8.876   34.831  1.00 45.84 ? 722  HOH A O   1 
HETATM 7704 O  O   . HOH O 7 .   ? 10.556  -20.576 21.621  1.00 26.88 ? 723  HOH A O   1 
HETATM 7705 O  O   . HOH O 7 .   ? -29.497 -18.924 -7.057  1.00 38.80 ? 724  HOH A O   1 
HETATM 7706 O  O   . HOH O 7 .   ? -14.975 -17.404 -17.877 1.00 27.09 ? 725  HOH A O   1 
HETATM 7707 O  O   . HOH O 7 .   ? -7.381  -17.616 15.358  1.00 33.99 ? 726  HOH A O   1 
HETATM 7708 O  O   . HOH O 7 .   ? -15.774 -10.271 29.919  1.00 12.89 ? 727  HOH A O   1 
HETATM 7709 O  O   . HOH O 7 .   ? -1.495  -34.415 4.304   1.00 30.18 ? 728  HOH A O   1 
HETATM 7710 O  O   . HOH O 7 .   ? 1.309   -14.595 29.908  1.00 15.96 ? 729  HOH A O   1 
HETATM 7711 O  O   . HOH O 7 .   ? -0.249  -16.963 30.472  1.00 24.69 ? 730  HOH A O   1 
HETATM 7712 O  O   . HOH O 7 .   ? 3.017   -14.259 31.900  1.00 27.73 ? 731  HOH A O   1 
HETATM 7713 O  O   . HOH O 7 .   ? 0.628   -31.325 1.654   1.00 20.57 ? 732  HOH A O   1 
HETATM 7714 O  O   . HOH O 7 .   ? -9.274  5.721   10.474  1.00 53.51 ? 733  HOH A O   1 
HETATM 7715 O  O   . HOH O 7 .   ? -9.141  -4.773  6.456   1.00 21.86 ? 734  HOH A O   1 
HETATM 7716 O  O   . HOH O 7 .   ? -3.695  -25.588 -11.034 1.00 19.96 ? 735  HOH A O   1 
HETATM 7717 O  O   . HOH O 7 .   ? -3.779  -11.702 -3.718  1.00 18.59 ? 736  HOH A O   1 
HETATM 7718 O  O   . HOH O 7 .   ? -18.150 -29.286 -15.207 1.00 36.35 ? 737  HOH A O   1 
HETATM 7719 O  O   . HOH O 7 .   ? -9.536  -1.736  33.601  1.00 22.06 ? 738  HOH A O   1 
HETATM 7720 O  O   . HOH O 7 .   ? -7.227  0.313   12.293  1.00 25.81 ? 739  HOH A O   1 
HETATM 7721 O  O   . HOH O 7 .   ? -24.657 -12.674 -13.688 1.00 26.65 ? 740  HOH A O   1 
HETATM 7722 O  O   . HOH O 7 .   ? -26.543 -28.099 -14.265 1.00 37.62 ? 741  HOH A O   1 
HETATM 7723 O  O   . HOH O 7 .   ? 1.552   -8.920  -12.405 1.00 44.24 ? 742  HOH A O   1 
HETATM 7724 O  O   . HOH O 7 .   ? -7.673  -25.774 10.271  1.00 18.95 ? 743  HOH A O   1 
HETATM 7725 O  O   . HOH O 7 .   ? -23.440 -29.729 -9.094  1.00 36.00 ? 744  HOH A O   1 
HETATM 7726 O  O   . HOH O 7 .   ? -18.655 -18.107 1.814   1.00 11.29 ? 745  HOH A O   1 
HETATM 7727 O  O   . HOH O 7 .   ? -6.553  -2.875  9.786   1.00 38.95 ? 746  HOH A O   1 
HETATM 7728 O  O   . HOH O 7 .   ? -2.205  -21.518 20.114  1.00 20.78 ? 747  HOH A O   1 
HETATM 7729 O  O   . HOH O 7 .   ? -3.146  -12.643 11.396  1.00 16.63 ? 748  HOH A O   1 
HETATM 7730 O  O   . HOH O 7 .   ? -34.592 -9.630  17.752  1.00 21.74 ? 749  HOH A O   1 
HETATM 7731 O  O   . HOH O 7 .   ? -9.276  -14.803 7.738   1.00 15.95 ? 750  HOH A O   1 
HETATM 7732 O  O   . HOH O 7 .   ? -22.542 -4.011  27.553  1.00 26.67 ? 751  HOH A O   1 
HETATM 7733 O  O   . HOH O 7 .   ? -26.127 -19.909 1.163   1.00 13.08 ? 752  HOH A O   1 
HETATM 7734 O  O   . HOH O 7 .   ? -6.643  -44.270 -5.746  1.00 18.74 ? 753  HOH A O   1 
HETATM 7735 O  O   . HOH O 7 .   ? -0.228  -28.564 15.847  1.00 26.72 ? 754  HOH A O   1 
HETATM 7736 O  O   . HOH O 7 .   ? 3.303   -24.649 11.625  1.00 22.89 ? 755  HOH A O   1 
HETATM 7737 O  O   . HOH O 7 .   ? -31.411 -2.867  29.691  1.00 47.61 ? 756  HOH A O   1 
HETATM 7738 O  O   . HOH O 7 .   ? 2.643   -19.269 24.154  1.00 19.13 ? 757  HOH A O   1 
HETATM 7739 O  O   . HOH O 7 .   ? -26.344 -28.961 -11.829 1.00 31.83 ? 758  HOH A O   1 
HETATM 7740 O  O   . HOH O 7 .   ? -18.057 -20.829 3.722   1.00 12.25 ? 759  HOH A O   1 
HETATM 7741 O  O   . HOH O 7 .   ? -5.255  0.523   3.977   1.00 49.60 ? 760  HOH A O   1 
HETATM 7742 O  O   . HOH O 7 .   ? -5.285  -27.150 -15.374 1.00 50.01 ? 761  HOH A O   1 
HETATM 7743 O  O   . HOH O 7 .   ? -9.454  -27.837 25.354  1.00 50.61 ? 762  HOH A O   1 
HETATM 7744 O  O   . HOH O 7 .   ? -14.054 -4.501  -5.239  1.00 21.42 ? 763  HOH A O   1 
HETATM 7745 O  O   . HOH O 7 .   ? 2.308   -21.626 0.452   1.00 27.68 ? 764  HOH A O   1 
HETATM 7746 O  O   A HOH O 7 .   ? -10.748 -6.817  5.901   0.60 32.24 ? 765  HOH A O   1 
HETATM 7747 O  O   . HOH O 7 .   ? -15.381 -32.008 21.796  1.00 39.95 ? 766  HOH A O   1 
HETATM 7748 O  O   . HOH O 7 .   ? 1.547   -40.730 0.747   1.00 25.15 ? 767  HOH A O   1 
HETATM 7749 O  O   . HOH O 7 .   ? -21.917 3.647   10.897  1.00 30.36 ? 768  HOH A O   1 
HETATM 7750 O  O   . HOH O 7 .   ? -8.375  -2.538  -2.338  1.00 25.00 ? 769  HOH A O   1 
HETATM 7751 O  O   . HOH O 7 .   ? -29.763 -20.964 -3.864  1.00 30.94 ? 770  HOH A O   1 
HETATM 7752 O  O   . HOH O 7 .   ? -16.248 -37.954 -4.871  1.00 36.47 ? 771  HOH A O   1 
HETATM 7753 O  O   . HOH O 7 .   ? -24.514 -14.228 -1.423  1.00 18.22 ? 772  HOH A O   1 
HETATM 7754 O  O   . HOH O 7 .   ? -23.190 -19.280 -11.729 1.00 27.21 ? 773  HOH A O   1 
HETATM 7755 O  O   . HOH O 7 .   ? -35.653 -13.090 6.267   1.00 20.09 ? 774  HOH A O   1 
HETATM 7756 O  O   . HOH O 7 .   ? -30.166 -3.087  9.299   1.00 50.78 ? 775  HOH A O   1 
HETATM 7757 O  O   . HOH O 7 .   ? -9.015  -4.886  -3.588  1.00 24.35 ? 776  HOH A O   1 
HETATM 7758 O  O   . HOH O 7 .   ? -22.611 -6.899  -1.431  1.00 35.68 ? 777  HOH A O   1 
HETATM 7759 O  O   . HOH O 7 .   ? 5.518   -20.627 28.812  1.00 40.13 ? 778  HOH A O   1 
HETATM 7760 O  O   . HOH O 7 .   ? -22.126 -13.136 -0.486  1.00 16.60 ? 779  HOH A O   1 
HETATM 7761 O  O   . HOH O 7 .   ? -22.036 2.114   25.964  1.00 42.83 ? 780  HOH A O   1 
HETATM 7762 O  O   . HOH O 7 .   ? -12.575 -28.613 -16.155 1.00 31.96 ? 781  HOH A O   1 
HETATM 7763 O  O   . HOH O 7 .   ? -17.991 -4.715  12.664  1.00 29.32 ? 782  HOH A O   1 
HETATM 7764 O  O   . HOH O 7 .   ? 14.416  -12.061 16.757  1.00 39.06 ? 783  HOH A O   1 
HETATM 7765 O  O   . HOH O 7 .   ? -17.944 -9.048  -3.763  1.00 26.56 ? 784  HOH A O   1 
HETATM 7766 O  O   . HOH O 7 .   ? -17.600 4.197   25.212  1.00 22.60 ? 785  HOH A O   1 
HETATM 7767 O  O   . HOH O 7 .   ? -18.545 -2.668  34.016  1.00 49.97 ? 786  HOH A O   1 
HETATM 7768 O  O   . HOH O 7 .   ? 2.548   -16.734 -7.022  1.00 27.14 ? 787  HOH A O   1 
HETATM 7769 O  O   . HOH O 7 .   ? 5.830   4.073   22.049  1.00 22.69 ? 788  HOH A O   1 
HETATM 7770 O  O   . HOH O 7 .   ? 5.493   5.526   24.345  1.00 29.23 ? 789  HOH A O   1 
HETATM 7771 O  O   . HOH O 7 .   ? -25.671 -10.667 30.697  1.00 33.84 ? 790  HOH A O   1 
HETATM 7772 O  O   . HOH O 7 .   ? -13.201 -8.172  34.112  1.00 16.10 ? 791  HOH A O   1 
HETATM 7773 O  O   . HOH O 7 .   ? -32.114 -3.931  15.739  1.00 33.06 ? 792  HOH A O   1 
HETATM 7774 O  O   . HOH O 7 .   ? 6.824   -5.731  38.115  1.00 31.62 ? 793  HOH A O   1 
HETATM 7775 O  O   . HOH O 7 .   ? 4.311   -28.588 16.487  1.00 54.39 ? 794  HOH A O   1 
HETATM 7776 O  O   . HOH O 7 .   ? -11.978 -6.000  -3.840  1.00 18.56 ? 795  HOH A O   1 
HETATM 7777 O  O   . HOH O 7 .   ? -12.412 -9.733  3.081   1.00 12.26 ? 796  HOH A O   1 
HETATM 7778 O  O   . HOH O 7 .   ? -17.540 -33.494 3.180   1.00 36.90 ? 797  HOH A O   1 
HETATM 7779 O  O   . HOH O 7 .   ? -28.794 -16.008 11.439  1.00 13.63 ? 798  HOH A O   1 
HETATM 7780 O  O   . HOH O 7 .   ? 18.494  -19.155 17.875  1.00 37.06 ? 799  HOH A O   1 
HETATM 7781 O  O   . HOH O 7 .   ? -19.667 -14.821 -4.373  1.00 14.18 ? 800  HOH A O   1 
HETATM 7782 O  O   . HOH O 7 .   ? -14.647 -26.939 29.914  1.00 35.44 ? 801  HOH A O   1 
HETATM 7783 O  O   . HOH O 7 .   ? -0.322  -16.165 33.302  1.00 27.39 ? 802  HOH A O   1 
HETATM 7784 O  O   . HOH O 7 .   ? -29.936 -14.565 -7.627  1.00 50.21 ? 803  HOH A O   1 
HETATM 7785 O  O   . HOH O 7 .   ? -7.042  -8.075  35.897  1.00 15.86 ? 804  HOH A O   1 
HETATM 7786 O  O   . HOH O 7 .   ? 0.762   -10.181 36.392  1.00 18.61 ? 805  HOH A O   1 
HETATM 7787 O  O   . HOH O 7 .   ? -15.507 -20.358 6.506   1.00 13.91 ? 806  HOH A O   1 
HETATM 7788 O  O   . HOH O 7 .   ? 3.479   4.830   6.049   1.00 45.00 ? 807  HOH A O   1 
HETATM 7789 O  O   . HOH O 7 .   ? -25.701 -24.288 -19.360 1.00 46.68 ? 808  HOH A O   1 
HETATM 7790 O  O   . HOH O 7 .   ? 3.205   -23.823 1.789   1.00 53.55 ? 809  HOH A O   1 
HETATM 7791 O  O   . HOH O 7 .   ? -11.328 -35.029 18.846  1.00 41.47 ? 810  HOH A O   1 
HETATM 7792 O  O   . HOH O 7 .   ? -19.145 -6.669  1.747   1.00 41.48 ? 811  HOH A O   1 
HETATM 7793 O  O   . HOH O 7 .   ? 3.306   0.720   -1.239  1.00 50.10 ? 812  HOH A O   1 
HETATM 7794 O  O   . HOH O 7 .   ? -14.595 -29.036 -12.166 1.00 25.66 ? 813  HOH A O   1 
HETATM 7795 O  O   . HOH O 7 .   ? -8.688  -22.328 19.217  1.00 31.01 ? 814  HOH A O   1 
HETATM 7796 O  O   . HOH O 7 .   ? -22.655 0.391   21.689  1.00 28.26 ? 815  HOH A O   1 
HETATM 7797 O  O   . HOH O 7 .   ? -1.368  -7.331  -10.455 1.00 41.60 ? 816  HOH A O   1 
HETATM 7798 O  O   . HOH O 7 .   ? -16.486 6.840   22.507  1.00 29.22 ? 817  HOH A O   1 
HETATM 7799 O  O   . HOH O 7 .   ? -12.606 -0.393  13.131  1.00 31.01 ? 818  HOH A O   1 
HETATM 7800 O  O   . HOH O 7 .   ? -4.989  -0.217  -9.564  1.00 29.39 ? 819  HOH A O   1 
HETATM 7801 O  O   . HOH O 7 .   ? 12.112  -1.681  17.404  1.00 37.49 ? 820  HOH A O   1 
HETATM 7802 O  O   . HOH O 7 .   ? -36.146 -2.482  16.165  1.00 51.67 ? 821  HOH A O   1 
HETATM 7803 O  O   . HOH O 7 .   ? 7.791   -9.886  30.254  1.00 27.66 ? 822  HOH A O   1 
HETATM 7804 O  O   . HOH O 7 .   ? -20.445 11.772  15.029  1.00 44.39 ? 823  HOH A O   1 
HETATM 7805 O  O   . HOH O 7 .   ? 14.936  -21.062 18.237  1.00 42.52 ? 824  HOH A O   1 
HETATM 7806 O  O   . HOH O 7 .   ? 14.008  -8.987  20.162  1.00 29.09 ? 825  HOH A O   1 
HETATM 7807 O  O   . HOH O 7 .   ? -37.582 -20.406 20.023  1.00 41.74 ? 826  HOH A O   1 
HETATM 7808 O  O   . HOH O 7 .   ? -13.910 7.894   23.255  1.00 24.76 ? 827  HOH A O   1 
HETATM 7809 O  O   . HOH O 7 .   ? -1.435  -22.335 -11.643 1.00 33.30 ? 828  HOH A O   1 
HETATM 7810 O  O   . HOH O 7 .   ? -4.699  -37.927 -8.310  1.00 34.98 ? 829  HOH A O   1 
HETATM 7811 O  O   . HOH O 7 .   ? -22.735 -0.189  24.178  1.00 33.35 ? 830  HOH A O   1 
HETATM 7812 O  O   . HOH O 7 .   ? -9.064  -42.006 10.095  1.00 55.66 ? 831  HOH A O   1 
HETATM 7813 O  O   . HOH O 7 .   ? 10.529  -2.958  21.384  1.00 29.10 ? 832  HOH A O   1 
HETATM 7814 O  O   . HOH O 7 .   ? -27.955 -27.633 15.244  1.00 42.54 ? 833  HOH A O   1 
HETATM 7815 O  O   . HOH O 7 .   ? -11.125 -37.539 -10.311 1.00 46.86 ? 834  HOH A O   1 
HETATM 7816 O  O   . HOH O 7 .   ? 6.169   -25.870 -0.569  1.00 47.98 ? 835  HOH A O   1 
HETATM 7817 O  O   . HOH O 7 .   ? -7.934  -17.523 31.481  1.00 26.71 ? 836  HOH A O   1 
HETATM 7818 O  O   . HOH O 7 .   ? -8.704  -15.074 -16.585 1.00 37.32 ? 837  HOH A O   1 
HETATM 7819 O  O   . HOH O 7 .   ? 4.759   -18.469 5.045   1.00 31.44 ? 838  HOH A O   1 
HETATM 7820 O  O   . HOH O 7 .   ? -19.484 -18.371 -17.925 1.00 34.43 ? 839  HOH A O   1 
HETATM 7821 O  O   . HOH O 7 .   ? 2.912   -5.506  -2.716  1.00 23.33 ? 840  HOH A O   1 
HETATM 7822 O  O   . HOH O 7 .   ? -22.967 -33.254 11.813  1.00 51.25 ? 841  HOH A O   1 
HETATM 7823 O  O   . HOH O 7 .   ? -9.805  -42.227 -5.659  1.00 41.80 ? 842  HOH A O   1 
HETATM 7824 O  O   . HOH O 7 .   ? -39.202 -17.237 21.342  1.00 42.89 ? 843  HOH A O   1 
HETATM 7825 O  O   . HOH O 7 .   ? -0.129  -16.765 -9.423  1.00 50.03 ? 844  HOH A O   1 
HETATM 7826 O  O   . HOH O 7 .   ? 11.686  2.596   11.694  1.00 46.70 ? 845  HOH A O   1 
HETATM 7827 O  O   . HOH O 7 .   ? -20.707 -24.481 -17.456 1.00 38.76 ? 846  HOH A O   1 
HETATM 7828 O  O   . HOH O 7 .   ? -16.239 -10.476 -10.564 1.00 33.99 ? 847  HOH A O   1 
HETATM 7829 O  O   . HOH O 7 .   ? -16.435 -6.816  -7.622  1.00 26.64 ? 848  HOH A O   1 
HETATM 7830 O  O   . HOH O 7 .   ? 9.131   -13.438 -0.795  1.00 37.15 ? 849  HOH A O   1 
HETATM 7831 O  O   . HOH O 7 .   ? -16.531 -15.185 35.366  1.00 26.28 ? 850  HOH A O   1 
HETATM 7832 O  O   . HOH O 7 .   ? -6.060  -34.089 -13.967 1.00 55.56 ? 851  HOH A O   1 
HETATM 7833 O  O   B HOH O 7 .   ? -13.013 -9.678  10.528  0.40 18.74 ? 852  HOH A O   1 
HETATM 7834 O  O   . HOH O 7 .   ? -10.058 -48.543 -1.256  1.00 51.66 ? 853  HOH A O   1 
HETATM 7835 O  O   . HOH O 7 .   ? 13.646  -18.972 14.746  1.00 43.88 ? 854  HOH A O   1 
HETATM 7836 O  O   . HOH O 7 .   ? -30.188 -10.989 0.699   1.00 43.04 ? 855  HOH A O   1 
HETATM 7837 O  O   . HOH O 7 .   ? -10.040 -4.706  24.377  1.00 18.29 ? 856  HOH A O   1 
HETATM 7838 O  O   . HOH O 7 .   ? -6.151  -18.182 27.447  1.00 28.08 ? 857  HOH A O   1 
HETATM 7839 O  O   . HOH O 7 .   ? -8.604  -5.424  -10.446 1.00 13.70 ? 858  HOH A O   1 
HETATM 7840 O  O   . HOH O 7 .   ? 8.998   -11.626 9.136   1.00 27.20 ? 859  HOH A O   1 
HETATM 7841 O  O   . HOH O 7 .   ? -5.642  -22.495 16.479  1.00 17.32 ? 860  HOH A O   1 
HETATM 7842 O  O   . HOH O 7 .   ? -26.503 -8.259  31.670  1.00 40.74 ? 861  HOH A O   1 
HETATM 7843 O  O   . HOH O 7 .   ? -35.683 -16.618 27.755  1.00 53.25 ? 862  HOH A O   1 
HETATM 7844 O  O   . HOH O 7 .   ? -19.951 -14.386 -1.550  1.00 13.87 ? 863  HOH A O   1 
HETATM 7845 O  O   . HOH O 7 .   ? -35.362 -20.133 15.182  1.00 29.83 ? 864  HOH A O   1 
HETATM 7846 O  O   . HOH O 7 .   ? -20.648 -9.229  -6.774  1.00 22.30 ? 865  HOH A O   1 
HETATM 7847 O  O   . HOH O 7 .   ? 5.065   6.518   12.548  1.00 34.10 ? 866  HOH A O   1 
HETATM 7848 O  O   . HOH O 7 .   ? 2.570   -24.997 4.118   1.00 26.55 ? 867  HOH A O   1 
HETATM 7849 O  O   . HOH O 7 .   ? -11.179 -32.603 20.763  1.00 49.95 ? 868  HOH A O   1 
HETATM 7850 O  O   . HOH O 7 .   ? -35.975 -15.970 14.652  1.00 28.59 ? 869  HOH A O   1 
HETATM 7851 O  O   . HOH O 7 .   ? 14.048  -15.231 13.508  1.00 50.30 ? 870  HOH A O   1 
HETATM 7852 O  O   . HOH O 7 .   ? -3.092  -34.105 -11.275 1.00 31.80 ? 871  HOH A O   1 
HETATM 7853 O  O   . HOH O 7 .   ? -22.804 -33.073 7.331   1.00 51.45 ? 872  HOH A O   1 
HETATM 7854 O  O   . HOH O 7 .   ? -9.493  -7.248  -2.043  1.00 17.32 ? 873  HOH A O   1 
HETATM 7855 O  O   . HOH O 7 .   ? -7.802  -7.933  -11.548 1.00 15.26 ? 874  HOH A O   1 
HETATM 7856 O  O   . HOH O 7 .   ? -0.295  3.448   36.352  1.00 39.90 ? 875  HOH A O   1 
HETATM 7857 O  O   . HOH O 7 .   ? -7.155  0.049   36.792  1.00 39.06 ? 876  HOH A O   1 
HETATM 7858 O  O   . HOH O 7 .   ? 16.088  -12.278 19.092  1.00 37.91 ? 877  HOH A O   1 
HETATM 7859 O  O   . HOH O 7 .   ? -27.911 -27.632 6.095   1.00 30.62 ? 878  HOH A O   1 
HETATM 7860 O  O   . HOH O 7 .   ? 5.192   -16.449 7.938   1.00 32.26 ? 879  HOH A O   1 
HETATM 7861 O  O   . HOH O 7 .   ? -15.058 -34.722 21.180  1.00 45.54 ? 880  HOH A O   1 
HETATM 7862 O  O   . HOH O 7 .   ? 17.549  -11.226 22.462  1.00 47.73 ? 881  HOH A O   1 
HETATM 7863 O  O   . HOH O 7 .   ? -15.271 -44.727 21.977  1.00 45.72 ? 882  HOH A O   1 
HETATM 7864 O  O   . HOH O 7 .   ? -22.738 -28.341 0.723   1.00 51.07 ? 883  HOH A O   1 
HETATM 7865 O  O   . HOH O 7 .   ? -7.650  -46.737 1.292   1.00 44.02 ? 884  HOH A O   1 
HETATM 7866 O  O   . HOH O 7 .   ? -16.733 -38.234 3.018   1.00 34.48 ? 885  HOH A O   1 
HETATM 7867 O  O   . HOH O 7 .   ? -5.786  13.770  21.117  1.00 24.89 ? 886  HOH A O   1 
HETATM 7868 O  O   . HOH O 7 .   ? -7.485  -20.437 22.316  1.00 42.57 ? 887  HOH A O   1 
HETATM 7869 O  O   . HOH O 7 .   ? 10.756  -21.776 19.124  1.00 27.91 ? 888  HOH A O   1 
HETATM 7870 O  O   . HOH O 7 .   ? 1.536   -35.958 2.069   1.00 34.51 ? 889  HOH A O   1 
HETATM 7871 O  O   . HOH O 7 .   ? -11.328 -30.392 -14.369 1.00 44.71 ? 890  HOH A O   1 
HETATM 7872 O  O   . HOH O 7 .   ? -0.852  -5.548  -8.398  1.00 44.32 ? 891  HOH A O   1 
HETATM 7873 O  O   . HOH O 7 .   ? -7.001  9.809   29.821  1.00 49.63 ? 892  HOH A O   1 
HETATM 7874 O  O   . HOH O 7 .   ? -1.146  -17.884 -5.278  1.00 36.47 ? 893  HOH A O   1 
HETATM 7875 O  O   . HOH O 7 .   ? 0.837   -29.651 7.361   1.00 39.30 ? 894  HOH A O   1 
HETATM 7876 O  O   . HOH O 7 .   ? -0.710  -21.897 -5.688  1.00 40.83 ? 895  HOH A O   1 
HETATM 7877 O  O   . HOH O 7 .   ? 8.951   -11.972 6.747   1.00 58.00 ? 896  HOH A O   1 
HETATM 7878 O  O   . HOH O 7 .   ? -0.371  -35.114 -3.805  1.00 26.30 ? 897  HOH A O   1 
HETATM 7879 O  O   . HOH O 7 .   ? -13.329 10.023  21.089  1.00 23.70 ? 898  HOH A O   1 
HETATM 7880 O  O   . HOH O 7 .   ? -28.464 -23.200 21.620  1.00 51.48 ? 899  HOH A O   1 
HETATM 7881 O  O   . HOH O 7 .   ? -19.591 -28.874 1.753   1.00 30.66 ? 900  HOH A O   1 
HETATM 7882 O  O   . HOH O 7 .   ? 4.913   -29.480 12.815  1.00 60.56 ? 901  HOH A O   1 
HETATM 7883 O  O   . HOH O 7 .   ? -34.745 -19.837 8.994   1.00 21.82 ? 902  HOH A O   1 
HETATM 7884 O  O   . HOH O 7 .   ? -4.057  -14.222 34.096  1.00 23.23 ? 903  HOH A O   1 
HETATM 7885 O  O   . HOH O 7 .   ? -20.082 -32.313 -3.603  1.00 39.55 ? 904  HOH A O   1 
HETATM 7886 O  O   . HOH O 7 .   ? -24.104 -10.459 35.585  1.00 43.71 ? 905  HOH A O   1 
HETATM 7887 O  O   . HOH O 7 .   ? -29.523 -12.557 -1.697  1.00 43.54 ? 906  HOH A O   1 
HETATM 7888 O  O   . HOH O 7 .   ? -16.325 -8.150  -0.062  1.00 29.58 ? 907  HOH A O   1 
HETATM 7889 O  O   . HOH O 7 .   ? -34.844 -11.762 2.114   1.00 41.48 ? 908  HOH A O   1 
HETATM 7890 O  O   . HOH O 7 .   ? -30.900 -22.946 20.418  1.00 38.54 ? 909  HOH A O   1 
HETATM 7891 O  O   . HOH O 7 .   ? -26.992 -27.463 19.973  1.00 45.28 ? 910  HOH A O   1 
HETATM 7892 O  O   . HOH O 7 .   ? -16.220 -31.429 -12.219 1.00 44.21 ? 911  HOH A O   1 
HETATM 7893 O  O   . HOH O 7 .   ? -45.317 -13.238 11.832  1.00 38.81 ? 912  HOH A O   1 
HETATM 7894 O  O   . HOH O 7 .   ? 11.120  -8.736  31.241  1.00 46.49 ? 913  HOH A O   1 
HETATM 7895 O  O   . HOH O 7 .   ? 2.905   -35.718 -1.709  1.00 46.01 ? 914  HOH A O   1 
HETATM 7896 O  O   . HOH O 7 .   ? 6.978   -16.562 33.118  1.00 28.02 ? 915  HOH A O   1 
HETATM 7897 O  O   . HOH O 7 .   ? 16.851  -13.471 15.263  1.00 49.25 ? 916  HOH A O   1 
HETATM 7898 O  O   . HOH O 7 .   ? -27.005 1.807   16.055  1.00 54.90 ? 917  HOH A O   1 
HETATM 7899 O  O   . HOH O 7 .   ? -6.181  -9.980  37.807  1.00 15.22 ? 918  HOH A O   1 
HETATM 7900 O  O   . HOH O 7 .   ? -9.056  -12.136 -16.027 1.00 43.25 ? 919  HOH A O   1 
HETATM 7901 O  O   . HOH O 7 .   ? -6.600  15.480  25.008  1.00 55.84 ? 920  HOH A O   1 
HETATM 7902 O  O   . HOH O 7 .   ? -39.265 -16.579 14.677  1.00 33.87 ? 921  HOH A O   1 
HETATM 7903 O  O   . HOH O 7 .   ? -10.584 -21.152 35.079  1.00 44.65 ? 922  HOH A O   1 
HETATM 7904 O  O   . HOH O 7 .   ? -27.573 -23.319 -7.016  1.00 36.11 ? 923  HOH A O   1 
HETATM 7905 O  O   . HOH O 7 .   ? -3.871  -31.660 -15.047 1.00 54.20 ? 924  HOH A O   1 
HETATM 7906 O  O   . HOH O 7 .   ? -0.568  -1.278  -8.958  1.00 54.43 ? 925  HOH A O   1 
HETATM 7907 O  O   . HOH O 7 .   ? -38.869 -9.830  21.209  1.00 52.02 ? 926  HOH A O   1 
HETATM 7908 O  O   . HOH O 7 .   ? -10.728 -15.546 -18.728 1.00 40.02 ? 927  HOH A O   1 
HETATM 7909 O  O   . HOH O 7 .   ? 12.444  -17.444 13.089  1.00 37.73 ? 928  HOH A O   1 
HETATM 7910 O  O   . HOH O 7 .   ? 0.000   -33.156 -5.153  1.00 45.78 ? 929  HOH A O   1 
HETATM 7911 O  O   . HOH O 7 .   ? 14.723  -5.618  10.909  1.00 53.69 ? 930  HOH A O   1 
HETATM 7912 O  O   . HOH O 7 .   ? -15.919 -6.808  3.656   1.00 42.45 ? 931  HOH A O   1 
HETATM 7913 O  O   . HOH O 7 .   ? -29.215 -21.661 -6.892  1.00 41.69 ? 932  HOH A O   1 
HETATM 7914 O  O   . HOH O 7 .   ? -8.729  -17.963 28.947  1.00 42.51 ? 933  HOH A O   1 
HETATM 7915 O  O   . HOH O 7 .   ? -5.364  6.484   -6.459  1.00 33.01 ? 934  HOH A O   1 
HETATM 7916 O  O   . HOH O 7 .   ? -19.685 4.068   27.001  1.00 44.21 ? 935  HOH A O   1 
HETATM 7917 O  O   . HOH O 7 .   ? -11.166 -46.146 -6.018  1.00 39.10 ? 936  HOH A O   1 
HETATM 7918 O  O   . HOH O 7 .   ? -2.070  -19.768 -7.175  1.00 50.00 ? 937  HOH A O   1 
HETATM 7919 O  O   . HOH O 7 .   ? -11.194 -0.464  10.611  1.00 46.17 ? 938  HOH A O   1 
HETATM 7920 O  O   . HOH O 7 .   ? -7.802  12.257  17.682  1.00 33.39 ? 939  HOH A O   1 
HETATM 7921 O  O   . HOH O 7 .   ? -12.923 -35.750 21.914  1.00 53.81 ? 940  HOH A O   1 
HETATM 7922 O  O   . HOH O 7 .   ? 4.387   1.877   35.023  1.00 39.32 ? 941  HOH A O   1 
HETATM 7923 O  O   . HOH O 7 .   ? 3.321   -1.381  -2.685  1.00 49.43 ? 942  HOH A O   1 
HETATM 7924 O  O   . HOH O 7 .   ? -19.007 -15.603 0.663   1.00 13.80 ? 943  HOH A O   1 
HETATM 7925 O  O   . HOH O 7 .   ? 5.266   -32.350 -9.452  1.00 48.06 ? 944  HOH A O   1 
HETATM 7926 O  O   . HOH O 7 .   ? 4.606   -17.399 32.430  1.00 52.01 ? 945  HOH A O   1 
HETATM 7927 O  O   . HOH O 7 .   ? -3.443  -25.110 -13.545 1.00 36.01 ? 946  HOH A O   1 
HETATM 7928 O  O   . HOH O 7 .   ? 11.599  -3.508  8.424   1.00 49.68 ? 947  HOH A O   1 
HETATM 7929 O  O   . HOH O 7 .   ? -28.955 -26.148 -14.431 1.00 38.93 ? 948  HOH A O   1 
HETATM 7930 O  O   . HOH O 7 .   ? -27.153 -11.959 -4.554  1.00 44.16 ? 949  HOH A O   1 
HETATM 7931 O  O   . HOH O 7 .   ? -24.327 3.026   22.013  1.00 53.23 ? 950  HOH A O   1 
HETATM 7932 O  O   . HOH O 7 .   ? -9.072  -44.510 -6.929  1.00 28.70 ? 951  HOH A O   1 
HETATM 7933 O  O   . HOH O 7 .   ? -2.049  14.562  18.992  1.00 45.72 ? 952  HOH A O   1 
HETATM 7934 O  O   . HOH O 7 .   ? -21.770 -22.622 -18.891 1.00 46.39 ? 953  HOH A O   1 
HETATM 7935 O  O   . HOH O 7 .   ? -12.305 12.432  22.090  1.00 38.84 ? 954  HOH A O   1 
HETATM 7936 O  O   . HOH O 7 .   ? 8.846   -25.065 16.622  1.00 48.74 ? 955  HOH A O   1 
HETATM 7937 O  O   . HOH O 7 .   ? 2.586   -29.216 5.447   1.00 45.78 ? 956  HOH A O   1 
HETATM 7938 O  O   . HOH O 7 .   ? 3.358   6.586   10.541  1.00 47.43 ? 957  HOH A O   1 
HETATM 7939 O  O   . HOH O 7 .   ? -24.507 -17.848 -13.429 1.00 42.85 ? 958  HOH A O   1 
HETATM 7940 O  O   . HOH O 7 .   ? -28.862 -24.217 -3.181  1.00 47.51 ? 959  HOH A O   1 
HETATM 7941 O  O   . HOH O 7 .   ? -13.148 -13.636 39.406  1.00 26.77 ? 960  HOH A O   1 
HETATM 7942 O  O   . HOH O 7 .   ? 6.028   11.614  19.970  1.00 46.03 ? 961  HOH A O   1 
HETATM 7943 O  O   . HOH O 7 .   ? -0.469  -37.882 3.239   1.00 43.74 ? 962  HOH A O   1 
HETATM 7944 O  O   . HOH O 7 .   ? 4.219   -20.818 3.666   1.00 45.85 ? 963  HOH A O   1 
HETATM 7945 O  O   . HOH O 7 .   ? -4.198  12.710  15.162  1.00 37.54 ? 964  HOH A O   1 
HETATM 7946 O  O   . HOH O 7 .   ? 10.833  0.666   19.038  1.00 49.45 ? 965  HOH A O   1 
HETATM 7947 O  O   . HOH O 7 .   ? 2.301   -24.114 24.409  1.00 46.30 ? 966  HOH A O   1 
HETATM 7948 O  O   . HOH O 7 .   ? -0.366  6.472   -2.312  1.00 42.82 ? 967  HOH A O   1 
HETATM 7949 O  O   . HOH O 7 .   ? -10.678 1.765   32.070  1.00 42.30 ? 968  HOH A O   1 
HETATM 7950 O  O   . HOH O 7 .   ? 0.287   1.404   35.656  1.00 48.76 ? 969  HOH A O   1 
HETATM 7951 O  O   . HOH O 7 .   ? -23.422 -1.978  28.040  1.00 44.17 ? 970  HOH A O   1 
HETATM 7952 O  O   . HOH O 7 .   ? -2.310  -15.739 -12.030 1.00 38.81 ? 971  HOH A O   1 
HETATM 7953 O  O   . HOH O 7 .   ? 2.154   -32.082 -0.772  1.00 38.50 ? 972  HOH A O   1 
HETATM 7954 O  O   . HOH O 7 .   ? 3.941   -26.838 5.271   1.00 60.15 ? 973  HOH A O   1 
HETATM 7955 O  O   . HOH O 7 .   ? -8.910  13.065  15.557  1.00 41.37 ? 974  HOH A O   1 
HETATM 7956 O  O   . HOH O 7 .   ? -6.032  -41.573 -10.103 1.00 50.78 ? 975  HOH A O   1 
HETATM 7957 O  O   . HOH O 7 .   ? -5.607  -8.544  -15.426 1.00 41.39 ? 976  HOH A O   1 
HETATM 7958 O  O   . HOH O 7 .   ? -10.013 -4.687  3.851   1.00 47.45 ? 977  HOH A O   1 
HETATM 7959 O  O   . HOH O 7 .   ? -15.830 6.361   25.855  1.00 39.52 ? 978  HOH A O   1 
HETATM 7960 O  O   . HOH O 7 .   ? 3.702   -21.155 25.787  1.00 34.60 ? 979  HOH A O   1 
HETATM 7961 O  O   . HOH O 7 .   ? 0.070   -34.390 -1.174  1.00 30.28 ? 980  HOH A O   1 
HETATM 7962 O  O   . HOH O 7 .   ? 0.554   -33.286 5.651   1.00 29.28 ? 981  HOH A O   1 
HETATM 7963 O  O   . HOH O 7 .   ? -27.358 -25.338 -5.392  1.00 47.20 ? 982  HOH A O   1 
HETATM 7964 O  O   . HOH O 7 .   ? 4.477   8.118   25.074  1.00 33.03 ? 983  HOH A O   1 
HETATM 7965 O  O   . HOH O 7 .   ? 1.870   -14.947 34.316  1.00 31.01 ? 984  HOH A O   1 
HETATM 7966 O  O   . HOH O 7 .   ? -5.434  -7.616  -12.905 1.00 34.36 ? 985  HOH A O   1 
HETATM 7967 O  O   . HOH O 7 .   ? 11.955  -3.254  19.171  1.00 44.32 ? 986  HOH A O   1 
HETATM 7968 O  O   . HOH O 7 .   ? -40.786 -14.477 19.057  1.00 33.04 ? 987  HOH A O   1 
HETATM 7969 O  O   . HOH O 7 .   ? -19.647 1.548   28.829  1.00 41.60 ? 988  HOH A O   1 
HETATM 7970 O  O   . HOH O 7 .   ? -8.295  13.629  20.077  1.00 25.95 ? 989  HOH A O   1 
HETATM 7971 O  O   . HOH O 7 .   ? 3.281   -28.085 8.211   1.00 57.49 ? 990  HOH A O   1 
HETATM 7972 O  O   . HOH O 7 .   ? -3.191  -8.570  -11.718 1.00 43.83 ? 991  HOH A O   1 
HETATM 7973 O  O   . HOH O 7 .   ? -34.726 -13.980 3.583   1.00 25.36 ? 992  HOH A O   1 
HETATM 7974 O  O   . HOH O 7 .   ? -16.496 -30.743 -16.923 1.00 50.02 ? 993  HOH A O   1 
HETATM 7975 O  O   . HOH O 7 .   ? -42.674 -9.781  19.852  1.00 53.75 ? 994  HOH A O   1 
HETATM 7976 O  O   . HOH O 7 .   ? -16.582 -35.834 3.402   1.00 56.67 ? 995  HOH A O   1 
HETATM 7977 O  O   . HOH O 7 .   ? -37.279 -20.237 9.900   1.00 44.02 ? 996  HOH A O   1 
HETATM 7978 O  O   . HOH O 7 .   ? -4.823  -22.198 19.083  1.00 22.48 ? 997  HOH A O   1 
HETATM 7979 O  O   . HOH O 7 .   ? 13.244  -23.101 18.718  1.00 42.55 ? 998  HOH A O   1 
HETATM 7980 O  O   . HOH O 7 .   ? -6.662  -22.837 20.744  1.00 45.93 ? 999  HOH A O   1 
HETATM 7981 O  O   . HOH O 7 .   ? 11.744  -14.038 10.337  1.00 50.66 ? 1000 HOH A O   1 
HETATM 7982 O  O   . HOH O 7 .   ? 1.199   5.804   7.552   1.00 54.17 ? 1001 HOH A O   1 
HETATM 7983 O  O   . HOH O 7 .   ? -4.851  4.064   6.184   1.00 46.09 ? 1002 HOH A O   1 
HETATM 7984 O  O   . HOH O 7 .   ? -5.346  11.713  17.354  1.00 27.45 ? 1003 HOH A O   1 
HETATM 7985 O  O   . HOH O 7 .   ? 2.808   -22.904 5.297   1.00 53.74 ? 1004 HOH A O   1 
HETATM 7986 O  O   . HOH O 7 .   ? 7.868   6.651   24.672  1.00 45.58 ? 1005 HOH A O   1 
HETATM 7987 O  O   . HOH O 7 .   ? 8.641   -21.453 25.904  1.00 52.48 ? 1006 HOH A O   1 
HETATM 7988 O  O   . HOH O 7 .   ? -15.735 10.394  19.676  1.00 44.63 ? 1007 HOH A O   1 
HETATM 7989 O  O   . HOH O 7 .   ? 2.098   -31.563 4.061   1.00 30.28 ? 1008 HOH A O   1 
HETATM 7990 O  O   . HOH O 7 .   ? 5.447   -21.450 8.716   1.00 45.65 ? 1009 HOH A O   1 
HETATM 7991 O  O   . HOH O 7 .   ? -17.413 9.007   21.347  1.00 41.03 ? 1010 HOH A O   1 
HETATM 7992 O  O   . HOH O 7 .   ? -0.406  -33.873 1.615   1.00 29.05 ? 1011 HOH A O   1 
HETATM 7993 O  O   . HOH P 7 .   ? 9.314   -31.730 60.776  1.00 39.54 ? 601  HOH B O   1 
HETATM 7994 O  O   B HOH P 7 .   ? 2.415   -14.782 61.838  0.25 14.62 ? 602  HOH B O   1 
HETATM 7995 O  O   . HOH P 7 .   ? 16.138  -24.147 46.243  1.00 49.77 ? 603  HOH B O   1 
HETATM 7996 O  O   . HOH P 7 .   ? -2.197  -36.937 86.970  1.00 46.20 ? 604  HOH B O   1 
HETATM 7997 O  O   . HOH P 7 .   ? -5.371  12.005  51.022  1.00 56.21 ? 605  HOH B O   1 
HETATM 7998 O  O   . HOH P 7 .   ? 4.719   -7.144  69.164  1.00 20.49 ? 606  HOH B O   1 
HETATM 7999 O  O   . HOH P 7 .   ? -0.051  -14.939 89.975  1.00 30.49 ? 607  HOH B O   1 
HETATM 8000 O  O   . HOH P 7 .   ? 0.572   -9.043  57.149  1.00 32.18 ? 608  HOH B O   1 
HETATM 8001 O  O   . HOH P 7 .   ? -12.998 -32.579 64.097  1.00 33.75 ? 609  HOH B O   1 
HETATM 8002 O  O   . HOH P 7 .   ? 6.021   -27.511 76.322  1.00 27.91 ? 610  HOH B O   1 
HETATM 8003 O  O   . HOH P 7 .   ? 8.120   -2.388  42.650  1.00 42.05 ? 611  HOH B O   1 
HETATM 8004 O  O   . HOH P 7 .   ? -6.015  12.165  58.050  1.00 52.96 ? 612  HOH B O   1 
HETATM 8005 O  O   . HOH P 7 .   ? -6.113  -4.901  39.303  1.00 17.78 ? 613  HOH B O   1 
HETATM 8006 O  O   . HOH P 7 .   ? 3.158   6.893   62.622  1.00 50.73 ? 614  HOH B O   1 
HETATM 8007 O  O   . HOH P 7 .   ? 0.564   -34.732 56.246  1.00 38.90 ? 615  HOH B O   1 
HETATM 8008 O  O   . HOH P 7 .   ? -4.829  9.885   49.791  1.00 36.60 ? 616  HOH B O   1 
HETATM 8009 O  O   . HOH P 7 .   ? -2.397  -18.584 54.001  1.00 25.95 ? 617  HOH B O   1 
HETATM 8010 O  O   . HOH P 7 .   ? 8.874   -30.658 87.780  1.00 33.97 ? 618  HOH B O   1 
HETATM 8011 O  O   . HOH P 7 .   ? 2.042   1.542   63.598  1.00 44.58 ? 619  HOH B O   1 
HETATM 8012 O  O   . HOH P 7 .   ? -16.919 -21.550 46.394  1.00 36.84 ? 620  HOH B O   1 
HETATM 8013 O  O   . HOH P 7 .   ? 1.607   0.641   42.804  1.00 43.27 ? 621  HOH B O   1 
HETATM 8014 O  O   . HOH P 7 .   ? 13.760  -8.181  44.422  1.00 44.54 ? 622  HOH B O   1 
HETATM 8015 O  O   . HOH P 7 .   ? 0.967   -9.597  54.698  1.00 20.88 ? 623  HOH B O   1 
HETATM 8016 O  O   . HOH P 7 .   ? 14.182  -14.217 79.180  1.00 19.88 ? 624  HOH B O   1 
HETATM 8017 O  O   . HOH P 7 .   ? 9.028   6.517   55.130  1.00 52.82 ? 625  HOH B O   1 
HETATM 8018 O  O   . HOH P 7 .   ? -17.612 -16.678 70.676  1.00 25.12 ? 626  HOH B O   1 
HETATM 8019 O  O   . HOH P 7 .   ? -16.334 -19.162 77.146  1.00 35.17 ? 627  HOH B O   1 
HETATM 8020 O  O   . HOH P 7 .   ? -22.318 -1.477  55.023  1.00 38.61 ? 628  HOH B O   1 
HETATM 8021 O  O   . HOH P 7 .   ? -21.565 -16.132 36.413  1.00 32.38 ? 629  HOH B O   1 
HETATM 8022 O  O   . HOH P 7 .   ? 2.723   -49.833 58.723  1.00 42.20 ? 630  HOH B O   1 
HETATM 8023 O  O   . HOH P 7 .   ? 9.759   -15.077 39.090  1.00 47.16 ? 631  HOH B O   1 
HETATM 8024 O  O   . HOH P 7 .   ? 9.633   -48.472 54.829  1.00 46.58 ? 632  HOH B O   1 
HETATM 8025 O  O   . HOH P 7 .   ? 7.425   -35.466 57.854  1.00 49.07 ? 633  HOH B O   1 
HETATM 8026 O  O   . HOH P 7 .   ? -1.433  1.528   61.535  1.00 36.35 ? 634  HOH B O   1 
HETATM 8027 O  O   . HOH P 7 .   ? -21.361 9.361   58.612  1.00 40.05 ? 635  HOH B O   1 
HETATM 8028 O  O   . HOH P 7 .   ? 2.122   -41.727 53.896  1.00 45.25 ? 636  HOH B O   1 
HETATM 8029 O  O   . HOH P 7 .   ? 5.355   1.348   49.300  1.00 30.43 ? 637  HOH B O   1 
HETATM 8030 O  O   . HOH P 7 .   ? 18.901  -17.547 43.581  1.00 47.48 ? 638  HOH B O   1 
HETATM 8031 O  O   . HOH P 7 .   ? 22.428  -23.671 67.338  1.00 19.84 ? 639  HOH B O   1 
HETATM 8032 O  O   . HOH P 7 .   ? -5.445  -23.716 90.482  1.00 37.06 ? 640  HOH B O   1 
HETATM 8033 O  O   . HOH P 7 .   ? 20.776  -14.362 70.589  1.00 15.80 ? 641  HOH B O   1 
HETATM 8034 O  O   . HOH P 7 .   ? -9.416  -23.507 49.756  1.00 39.18 ? 642  HOH B O   1 
HETATM 8035 O  O   . HOH P 7 .   ? -14.556 -35.911 82.589  1.00 42.33 ? 643  HOH B O   1 
HETATM 8036 O  O   . HOH P 7 .   ? 11.779  -17.722 91.123  1.00 49.34 ? 644  HOH B O   1 
HETATM 8037 O  O   . HOH P 7 .   ? -0.298  -47.361 81.425  1.00 37.76 ? 645  HOH B O   1 
HETATM 8038 O  O   . HOH P 7 .   ? -5.181  -2.113  40.195  1.00 22.89 ? 646  HOH B O   1 
HETATM 8039 O  O   . HOH P 7 .   ? 21.932  -21.025 65.072  1.00 18.50 ? 647  HOH B O   1 
HETATM 8040 O  O   . HOH P 7 .   ? -22.517 -17.163 53.803  1.00 15.36 ? 648  HOH B O   1 
HETATM 8041 O  O   . HOH P 7 .   ? 8.859   -15.550 68.884  1.00 12.37 ? 649  HOH B O   1 
HETATM 8042 O  O   . HOH P 7 .   ? -27.045 -0.264  64.605  1.00 41.40 ? 650  HOH B O   1 
HETATM 8043 O  O   . HOH P 7 .   ? -4.718  -6.846  35.263  1.00 15.44 ? 651  HOH B O   1 
HETATM 8044 O  O   . HOH P 7 .   ? 5.668   -4.546  62.892  1.00 25.60 ? 652  HOH B O   1 
HETATM 8045 O  O   . HOH P 7 .   ? -18.593 4.764   63.340  1.00 14.08 ? 653  HOH B O   1 
HETATM 8046 O  O   . HOH P 7 .   ? -21.364 -8.676  35.043  1.00 51.33 ? 654  HOH B O   1 
HETATM 8047 O  O   . HOH P 7 .   ? -13.655 7.310   64.199  1.00 30.90 ? 655  HOH B O   1 
HETATM 8048 O  O   . HOH P 7 .   ? -5.237  -29.086 53.942  1.00 39.94 ? 656  HOH B O   1 
HETATM 8049 O  O   . HOH P 7 .   ? 10.447  -9.425  69.061  1.00 20.89 ? 657  HOH B O   1 
HETATM 8050 O  O   . HOH P 7 .   ? 29.779  -4.596  70.508  1.00 26.47 ? 658  HOH B O   1 
HETATM 8051 O  O   . HOH P 7 .   ? -24.368 -1.641  48.200  1.00 34.33 ? 659  HOH B O   1 
HETATM 8052 O  O   . HOH P 7 .   ? -21.296 -19.780 63.218  1.00 18.90 ? 660  HOH B O   1 
HETATM 8053 O  O   . HOH P 7 .   ? -7.601  7.171   41.521  1.00 37.82 ? 661  HOH B O   1 
HETATM 8054 O  O   . HOH P 7 .   ? -5.015  -27.919 91.024  1.00 47.37 ? 662  HOH B O   1 
HETATM 8055 O  O   . HOH P 7 .   ? 7.737   -6.732  72.992  1.00 35.61 ? 663  HOH B O   1 
HETATM 8056 O  O   . HOH P 7 .   ? 22.340  -8.455  57.325  1.00 26.77 ? 664  HOH B O   1 
HETATM 8057 O  O   . HOH P 7 .   ? -6.303  -0.081  39.252  1.00 47.45 ? 665  HOH B O   1 
HETATM 8058 O  O   . HOH P 7 .   ? -12.027 -27.425 59.211  1.00 24.99 ? 666  HOH B O   1 
HETATM 8059 O  O   . HOH P 7 .   ? 13.642  -30.849 50.322  1.00 37.98 ? 667  HOH B O   1 
HETATM 8060 O  O   . HOH P 7 .   ? -15.827 -19.663 71.195  1.00 20.16 ? 668  HOH B O   1 
HETATM 8061 O  O   . HOH P 7 .   ? -6.168  -12.433 87.141  1.00 27.43 ? 669  HOH B O   1 
HETATM 8062 O  O   . HOH P 7 .   ? -17.339 0.582   45.449  1.00 17.05 ? 670  HOH B O   1 
HETATM 8063 O  O   . HOH P 7 .   ? -1.297  -24.622 43.640  1.00 47.04 ? 671  HOH B O   1 
HETATM 8064 O  O   . HOH P 7 .   ? -19.893 -1.983  54.374  1.00 22.07 ? 672  HOH B O   1 
HETATM 8065 O  O   . HOH P 7 .   ? -19.702 -22.981 52.894  1.00 30.28 ? 673  HOH B O   1 
HETATM 8066 O  O   . HOH P 7 .   ? -14.399 -24.431 68.252  1.00 31.92 ? 674  HOH B O   1 
HETATM 8067 O  O   . HOH P 7 .   ? 15.600  -20.775 91.809  1.00 36.16 ? 675  HOH B O   1 
HETATM 8068 O  O   . HOH P 7 .   ? -10.787 -29.587 59.864  1.00 24.69 ? 676  HOH B O   1 
HETATM 8069 O  O   . HOH P 7 .   ? 7.864   -43.410 58.064  1.00 28.05 ? 677  HOH B O   1 
HETATM 8070 O  O   . HOH P 7 .   ? -8.330  -28.778 60.653  1.00 18.98 ? 678  HOH B O   1 
HETATM 8071 O  O   . HOH P 7 .   ? 5.845   -37.498 66.277  1.00 48.64 ? 679  HOH B O   1 
HETATM 8072 O  O   . HOH P 7 .   ? 23.760  -9.703  68.577  1.00 15.34 ? 680  HOH B O   1 
HETATM 8073 O  O   . HOH P 7 .   ? 21.035  -21.533 84.561  1.00 62.20 ? 681  HOH B O   1 
HETATM 8074 O  O   . HOH P 7 .   ? 25.950  -15.438 63.040  1.00 30.87 ? 682  HOH B O   1 
HETATM 8075 O  O   . HOH P 7 .   ? 0.436   -2.251  40.097  1.00 19.94 ? 683  HOH B O   1 
HETATM 8076 O  O   . HOH P 7 .   ? -14.454 0.879   42.850  1.00 23.16 ? 684  HOH B O   1 
HETATM 8077 O  O   . HOH P 7 .   ? 4.828   -35.331 69.535  1.00 30.68 ? 685  HOH B O   1 
HETATM 8078 O  O   . HOH P 7 .   ? -9.248  -34.967 71.334  1.00 27.61 ? 686  HOH B O   1 
HETATM 8079 O  O   . HOH P 7 .   ? -12.076 -22.827 52.655  1.00 19.27 ? 687  HOH B O   1 
HETATM 8080 O  O   . HOH P 7 .   ? -6.784  -26.214 86.804  1.00 16.69 ? 688  HOH B O   1 
HETATM 8081 O  O   . HOH P 7 .   ? 4.104   -31.622 53.396  1.00 23.25 ? 689  HOH B O   1 
HETATM 8082 O  O   . HOH P 7 .   ? -8.576  -11.367 87.631  1.00 42.95 ? 690  HOH B O   1 
HETATM 8083 O  O   . HOH P 7 .   ? -19.634 -24.554 57.678  1.00 20.60 ? 691  HOH B O   1 
HETATM 8084 O  O   . HOH P 7 .   ? 9.920   -3.458  48.216  1.00 24.00 ? 692  HOH B O   1 
HETATM 8085 O  O   . HOH P 7 .   ? -19.989 -9.315  83.821  1.00 48.82 ? 693  HOH B O   1 
HETATM 8086 O  O   . HOH P 7 .   ? -6.958  -14.929 86.225  1.00 15.65 ? 694  HOH B O   1 
HETATM 8087 O  O   . HOH P 7 .   ? -11.534 -0.115  76.904  1.00 30.40 ? 695  HOH B O   1 
HETATM 8088 O  O   . HOH P 7 .   ? 14.006  -29.000 64.593  1.00 33.31 ? 696  HOH B O   1 
HETATM 8089 O  O   . HOH P 7 .   ? 10.854  -13.076 75.865  1.00 15.87 ? 697  HOH B O   1 
HETATM 8090 O  O   . HOH P 7 .   ? -4.385  12.187  54.060  1.00 28.10 ? 698  HOH B O   1 
HETATM 8091 O  O   . HOH P 7 .   ? -22.888 -17.953 44.136  1.00 29.49 ? 699  HOH B O   1 
HETATM 8092 O  O   . HOH P 7 .   ? -12.193 -40.949 74.146  1.00 42.08 ? 700  HOH B O   1 
HETATM 8093 O  O   . HOH P 7 .   ? -10.043 11.533  56.751  1.00 24.75 ? 701  HOH B O   1 
HETATM 8094 O  O   . HOH P 7 .   ? 12.895  -29.977 84.002  1.00 29.11 ? 702  HOH B O   1 
HETATM 8095 O  O   . HOH P 7 .   ? 0.853   -7.880  41.598  1.00 15.13 ? 703  HOH B O   1 
HETATM 8096 O  O   . HOH P 7 .   ? 8.363   -30.068 81.123  1.00 21.71 ? 704  HOH B O   1 
HETATM 8097 O  O   . HOH P 7 .   ? -0.124  2.682   45.644  1.00 32.80 ? 705  HOH B O   1 
HETATM 8098 O  O   . HOH P 7 .   ? -26.169 -12.986 63.523  1.00 33.57 ? 706  HOH B O   1 
HETATM 8099 O  O   . HOH P 7 .   ? -14.722 -18.354 79.803  1.00 35.98 ? 707  HOH B O   1 
HETATM 8100 O  O   . HOH P 7 .   ? 17.431  -23.641 89.511  1.00 25.95 ? 708  HOH B O   1 
HETATM 8101 O  O   . HOH P 7 .   ? -19.962 -14.278 69.344  1.00 39.94 ? 709  HOH B O   1 
HETATM 8102 O  O   . HOH P 7 .   ? -2.004  -40.430 68.868  1.00 50.93 ? 710  HOH B O   1 
HETATM 8103 O  O   A HOH P 7 .   ? -1.272  -7.071  69.743  0.80 36.32 ? 711  HOH B O   1 
HETATM 8104 O  O   . HOH P 7 .   ? -5.629  -24.629 81.192  1.00 14.08 ? 712  HOH B O   1 
HETATM 8105 O  O   . HOH P 7 .   ? -12.252 -9.799  88.636  1.00 33.98 ? 713  HOH B O   1 
HETATM 8106 O  O   . HOH P 7 .   ? -16.180 -14.156 37.804  1.00 21.84 ? 714  HOH B O   1 
HETATM 8107 O  O   . HOH P 7 .   ? 21.602  -20.498 59.384  1.00 22.55 ? 715  HOH B O   1 
HETATM 8108 O  O   . HOH P 7 .   ? 14.536  -24.387 54.308  1.00 23.16 ? 716  HOH B O   1 
HETATM 8109 O  O   . HOH P 7 .   ? 13.593  -32.394 56.928  1.00 39.17 ? 717  HOH B O   1 
HETATM 8110 O  O   . HOH P 7 .   ? -15.672 7.499   51.555  1.00 25.16 ? 718  HOH B O   1 
HETATM 8111 O  O   . HOH P 7 .   ? 12.094  -9.866  66.820  1.00 16.24 ? 719  HOH B O   1 
HETATM 8112 O  O   . HOH P 7 .   ? 3.528   -9.822  45.733  1.00 13.39 ? 720  HOH B O   1 
HETATM 8113 O  O   . HOH P 7 .   ? 20.378  -12.677 39.505  1.00 46.16 ? 721  HOH B O   1 
HETATM 8114 O  O   . HOH P 7 .   ? -18.121 -7.596  80.317  1.00 41.51 ? 722  HOH B O   1 
HETATM 8115 O  O   . HOH P 7 .   ? -18.856 3.957   51.678  1.00 21.38 ? 723  HOH B O   1 
HETATM 8116 O  O   . HOH P 7 .   ? -21.883 -6.664  69.941  1.00 18.06 ? 724  HOH B O   1 
HETATM 8117 O  O   . HOH P 7 .   ? 13.178  -27.567 78.445  1.00 33.06 ? 725  HOH B O   1 
HETATM 8118 O  O   . HOH P 7 .   ? -13.183 8.023   47.554  1.00 26.73 ? 726  HOH B O   1 
HETATM 8119 O  O   . HOH P 7 .   ? 6.801   -42.916 49.343  1.00 43.09 ? 727  HOH B O   1 
HETATM 8120 O  O   . HOH P 7 .   ? 0.606   -12.769 58.911  1.00 16.77 ? 728  HOH B O   1 
HETATM 8121 O  O   . HOH P 7 .   ? 4.006   -28.112 89.442  1.00 30.91 ? 729  HOH B O   1 
HETATM 8122 O  O   . HOH P 7 .   ? 11.962  -18.799 61.934  1.00 14.03 ? 730  HOH B O   1 
HETATM 8123 O  O   . HOH P 7 .   ? 5.082   -22.631 70.286  1.00 14.27 ? 731  HOH B O   1 
HETATM 8124 O  O   . HOH P 7 .   ? 8.920   -31.830 84.045  1.00 36.12 ? 732  HOH B O   1 
HETATM 8125 O  O   . HOH P 7 .   ? -25.118 -9.688  57.937  1.00 42.76 ? 733  HOH B O   1 
HETATM 8126 O  O   . HOH P 7 .   ? -8.178  -1.294  69.418  1.00 23.10 ? 734  HOH B O   1 
HETATM 8127 O  O   . HOH P 7 .   ? 24.199  -14.759 60.341  1.00 23.91 ? 735  HOH B O   1 
HETATM 8128 O  O   . HOH P 7 .   ? -10.112 -29.162 87.757  1.00 32.57 ? 736  HOH B O   1 
HETATM 8129 O  O   . HOH P 7 .   ? -19.321 -17.865 66.435  1.00 42.99 ? 737  HOH B O   1 
HETATM 8130 O  O   . HOH P 7 .   ? 6.349   -39.297 61.027  1.00 27.64 ? 738  HOH B O   1 
HETATM 8131 O  O   . HOH P 7 .   ? -9.245  7.596   51.579  1.00 16.18 ? 739  HOH B O   1 
HETATM 8132 O  O   . HOH P 7 .   ? -19.211 -3.494  40.755  1.00 32.82 ? 740  HOH B O   1 
HETATM 8133 O  O   . HOH P 7 .   ? 6.808   -20.812 71.614  1.00 11.91 ? 741  HOH B O   1 
HETATM 8134 O  O   . HOH P 7 .   ? 16.514  -26.941 59.843  1.00 35.01 ? 742  HOH B O   1 
HETATM 8135 O  O   . HOH P 7 .   ? -2.026  -10.224 42.343  1.00 13.65 ? 743  HOH B O   1 
HETATM 8136 O  O   . HOH P 7 .   ? -11.039 8.836   63.899  1.00 35.82 ? 744  HOH B O   1 
HETATM 8137 O  O   . HOH P 7 .   ? -19.109 2.308   54.153  1.00 22.10 ? 745  HOH B O   1 
HETATM 8138 O  O   . HOH P 7 .   ? 4.749   -18.155 93.507  1.00 35.84 ? 746  HOH B O   1 
HETATM 8139 O  O   . HOH P 7 .   ? -3.808  -17.606 44.048  1.00 19.67 ? 747  HOH B O   1 
HETATM 8140 O  O   . HOH P 7 .   ? 4.320   4.608   50.856  1.00 21.71 ? 748  HOH B O   1 
HETATM 8141 O  O   . HOH P 7 .   ? -13.879 7.825   44.801  1.00 31.35 ? 749  HOH B O   1 
HETATM 8142 O  O   . HOH P 7 .   ? -3.330  -1.639  42.331  1.00 20.38 ? 750  HOH B O   1 
HETATM 8143 O  O   . HOH P 7 .   ? -7.176  -12.221 79.881  1.00 15.89 ? 751  HOH B O   1 
HETATM 8144 O  O   . HOH P 7 .   ? -3.681  10.113  61.433  1.00 21.68 ? 752  HOH B O   1 
HETATM 8145 O  O   . HOH P 7 .   ? 18.868  -20.698 78.718  1.00 36.59 ? 753  HOH B O   1 
HETATM 8146 O  O   . HOH P 7 .   ? -14.988 -14.780 43.906  1.00 28.81 ? 754  HOH B O   1 
HETATM 8147 O  O   . HOH P 7 .   ? -21.808 -11.108 69.519  1.00 18.65 ? 755  HOH B O   1 
HETATM 8148 O  O   . HOH P 7 .   ? 7.969   -29.828 90.271  1.00 34.27 ? 756  HOH B O   1 
HETATM 8149 O  O   . HOH P 7 .   ? 15.085  -30.256 57.075  1.00 45.30 ? 757  HOH B O   1 
HETATM 8150 O  O   . HOH P 7 .   ? -2.254  -41.645 65.377  1.00 37.21 ? 758  HOH B O   1 
HETATM 8151 O  O   . HOH P 7 .   ? 14.980  -19.616 73.965  1.00 13.40 ? 759  HOH B O   1 
HETATM 8152 O  O   . HOH P 7 .   ? -2.138  -15.233 67.936  1.00 12.61 ? 760  HOH B O   1 
HETATM 8153 O  O   . HOH P 7 .   ? 3.643   -34.358 53.836  1.00 26.48 ? 761  HOH B O   1 
HETATM 8154 O  O   . HOH P 7 .   ? -26.574 -14.328 58.958  1.00 37.76 ? 762  HOH B O   1 
HETATM 8155 O  O   . HOH P 7 .   ? 6.751   -13.147 88.331  1.00 22.22 ? 763  HOH B O   1 
HETATM 8156 O  O   . HOH P 7 .   ? 6.411   -14.552 72.361  1.00 14.49 ? 764  HOH B O   1 
HETATM 8157 O  O   . HOH P 7 .   ? 10.783  -35.901 48.180  1.00 35.53 ? 765  HOH B O   1 
HETATM 8158 O  O   . HOH P 7 .   ? 21.357  -2.487  61.518  1.00 42.79 ? 766  HOH B O   1 
HETATM 8159 O  O   . HOH P 7 .   ? 5.804   -2.035  41.895  1.00 48.91 ? 767  HOH B O   1 
HETATM 8160 O  O   . HOH P 7 .   ? -14.494 -25.534 64.287  1.00 17.03 ? 768  HOH B O   1 
HETATM 8161 O  O   . HOH P 7 .   ? 3.247   -16.179 92.812  1.00 42.27 ? 769  HOH B O   1 
HETATM 8162 O  O   . HOH P 7 .   ? -13.419 -22.370 75.216  1.00 19.05 ? 770  HOH B O   1 
HETATM 8163 O  O   . HOH P 7 .   ? -14.680 -6.785  78.524  1.00 18.07 ? 771  HOH B O   1 
HETATM 8164 O  O   . HOH P 7 .   ? -3.141  -5.103  69.246  1.00 21.35 ? 772  HOH B O   1 
HETATM 8165 O  O   . HOH P 7 .   ? -16.115 12.691  55.661  1.00 41.50 ? 773  HOH B O   1 
HETATM 8166 O  O   . HOH P 7 .   ? 16.252  -7.620  73.726  1.00 36.81 ? 774  HOH B O   1 
HETATM 8167 O  O   . HOH P 7 .   ? -1.673  -3.834  84.279  1.00 46.79 ? 775  HOH B O   1 
HETATM 8168 O  O   . HOH P 7 .   ? 0.358   -38.140 85.896  1.00 48.04 ? 776  HOH B O   1 
HETATM 8169 O  O   . HOH P 7 .   ? 1.591   -9.548  43.581  1.00 14.50 ? 777  HOH B O   1 
HETATM 8170 O  O   . HOH P 7 .   ? -11.466 -31.932 74.112  1.00 17.87 ? 778  HOH B O   1 
HETATM 8171 O  O   . HOH P 7 .   ? 18.875  -18.282 84.747  1.00 47.74 ? 779  HOH B O   1 
HETATM 8172 O  O   . HOH P 7 .   ? 13.948  -29.184 74.088  1.00 47.27 ? 780  HOH B O   1 
HETATM 8173 O  O   . HOH P 7 .   ? -5.238  -8.075  39.841  1.00 16.77 ? 781  HOH B O   1 
HETATM 8174 O  O   . HOH P 7 .   ? -21.906 -22.217 54.140  1.00 20.92 ? 782  HOH B O   1 
HETATM 8175 O  O   . HOH P 7 .   ? 24.336  -10.000 54.448  1.00 30.63 ? 783  HOH B O   1 
HETATM 8176 O  O   . HOH P 7 .   ? -10.829 12.986  46.789  1.00 57.54 ? 784  HOH B O   1 
HETATM 8177 O  O   . HOH P 7 .   ? 8.195   -4.601  65.792  1.00 25.02 ? 785  HOH B O   1 
HETATM 8178 O  O   . HOH P 7 .   ? -13.296 -15.422 45.821  1.00 15.14 ? 786  HOH B O   1 
HETATM 8179 O  O   . HOH P 7 .   ? -8.080  1.068   67.561  1.00 22.48 ? 787  HOH B O   1 
HETATM 8180 O  O   . HOH P 7 .   ? -14.184 -20.248 51.533  1.00 15.44 ? 788  HOH B O   1 
HETATM 8181 O  O   . HOH P 7 .   ? -24.584 -2.548  43.553  1.00 44.07 ? 789  HOH B O   1 
HETATM 8182 O  O   . HOH P 7 .   ? -10.843 -19.112 42.626  1.00 47.67 ? 790  HOH B O   1 
HETATM 8183 O  O   . HOH P 7 .   ? -4.255  -17.882 60.249  1.00 21.24 ? 791  HOH B O   1 
HETATM 8184 O  O   . HOH P 7 .   ? -26.628 -6.582  74.084  1.00 33.71 ? 792  HOH B O   1 
HETATM 8185 O  O   . HOH P 7 .   ? -11.520 8.298   40.999  1.00 43.10 ? 793  HOH B O   1 
HETATM 8186 O  O   . HOH P 7 .   ? 8.581   -14.359 76.904  1.00 15.00 ? 794  HOH B O   1 
HETATM 8187 O  O   . HOH P 7 .   ? -1.524  -41.034 62.602  1.00 58.96 ? 795  HOH B O   1 
HETATM 8188 O  O   . HOH P 7 .   ? -3.417  -26.029 65.219  1.00 17.35 ? 796  HOH B O   1 
HETATM 8189 O  O   . HOH P 7 .   ? 5.456   -16.410 41.782  1.00 39.38 ? 797  HOH B O   1 
HETATM 8190 O  O   . HOH P 7 .   ? -9.104  -22.015 55.594  1.00 20.65 ? 798  HOH B O   1 
HETATM 8191 O  O   . HOH P 7 .   ? 13.162  -14.149 76.646  1.00 17.60 ? 799  HOH B O   1 
HETATM 8192 O  O   . HOH P 7 .   ? 5.233   -10.499 84.622  1.00 37.08 ? 800  HOH B O   1 
HETATM 8193 O  O   . HOH P 7 .   ? 17.162  -15.427 63.720  1.00 12.56 ? 801  HOH B O   1 
HETATM 8194 O  O   . HOH P 7 .   ? -25.009 -3.694  59.244  1.00 20.98 ? 802  HOH B O   1 
HETATM 8195 O  O   . HOH P 7 .   ? -2.095  -27.762 50.327  1.00 30.78 ? 803  HOH B O   1 
HETATM 8196 O  O   . HOH P 7 .   ? 10.730  -30.585 74.392  1.00 53.62 ? 804  HOH B O   1 
HETATM 8197 O  O   . HOH P 7 .   ? -3.070  -47.125 74.235  1.00 48.82 ? 805  HOH B O   1 
HETATM 8198 O  O   . HOH P 7 .   ? -11.537 -17.619 45.200  1.00 29.55 ? 806  HOH B O   1 
HETATM 8199 O  O   . HOH P 7 .   ? -13.159 -10.825 39.351  1.00 16.00 ? 807  HOH B O   1 
HETATM 8200 O  O   . HOH P 7 .   ? -8.742  -13.470 64.458  1.00 14.07 ? 808  HOH B O   1 
HETATM 8201 O  O   . HOH P 7 .   ? 9.743   0.982   54.178  1.00 42.92 ? 809  HOH B O   1 
HETATM 8202 O  O   . HOH P 7 .   ? -7.405  3.715   44.246  1.00 26.49 ? 810  HOH B O   1 
HETATM 8203 O  O   . HOH P 7 .   ? 14.553  -5.914  71.914  1.00 50.06 ? 811  HOH B O   1 
HETATM 8204 O  O   . HOH P 7 .   ? -4.565  -45.102 81.088  1.00 14.76 ? 812  HOH B O   1 
HETATM 8205 O  O   . HOH P 7 .   ? -1.440  -15.694 92.241  1.00 32.23 ? 813  HOH B O   1 
HETATM 8206 O  O   . HOH P 7 .   ? 11.437  -7.733  38.929  1.00 42.85 ? 814  HOH B O   1 
HETATM 8207 O  O   . HOH P 7 .   ? 19.734  -3.041  59.535  1.00 36.39 ? 815  HOH B O   1 
HETATM 8208 O  O   . HOH P 7 .   ? 24.118  -12.323 68.796  1.00 17.33 ? 816  HOH B O   1 
HETATM 8209 O  O   . HOH P 7 .   ? 0.772   -9.939  72.504  1.00 15.63 ? 817  HOH B O   1 
HETATM 8210 O  O   . HOH P 7 .   ? -17.348 10.495  53.001  1.00 46.02 ? 818  HOH B O   1 
HETATM 8211 O  O   . HOH P 7 .   ? 10.242  -41.223 52.709  1.00 51.55 ? 819  HOH B O   1 
HETATM 8212 O  O   . HOH P 7 .   ? 12.605  -19.345 86.907  1.00 25.16 ? 820  HOH B O   1 
HETATM 8213 O  O   . HOH P 7 .   ? -0.833  -20.643 39.852  1.00 51.19 ? 821  HOH B O   1 
HETATM 8214 O  O   . HOH P 7 .   ? -18.680 -26.251 61.871  1.00 51.16 ? 822  HOH B O   1 
HETATM 8215 O  O   . HOH P 7 .   ? -2.740  -29.746 52.271  1.00 61.88 ? 823  HOH B O   1 
HETATM 8216 O  O   . HOH P 7 .   ? 8.641   -15.063 79.660  1.00 13.58 ? 824  HOH B O   1 
HETATM 8217 O  O   . HOH P 7 .   ? 7.421   -18.059 73.496  1.00 12.24 ? 825  HOH B O   1 
HETATM 8218 O  O   . HOH P 7 .   ? 21.026  -23.555 87.563  1.00 45.19 ? 826  HOH B O   1 
HETATM 8219 O  O   . HOH P 7 .   ? -8.052  -14.391 41.600  1.00 18.67 ? 827  HOH B O   1 
HETATM 8220 O  O   . HOH P 7 .   ? 10.117  -37.337 45.850  1.00 51.54 ? 828  HOH B O   1 
HETATM 8221 O  O   . HOH P 7 .   ? 23.828  -19.227 59.784  1.00 33.24 ? 829  HOH B O   1 
HETATM 8222 O  O   . HOH P 7 .   ? -18.632 -5.695  77.569  1.00 53.91 ? 830  HOH B O   1 
HETATM 8223 O  O   . HOH P 7 .   ? -13.120 -17.636 83.175  1.00 20.24 ? 831  HOH B O   1 
HETATM 8224 O  O   . HOH P 7 .   ? 16.013  -29.365 86.508  1.00 26.15 ? 832  HOH B O   1 
HETATM 8225 O  O   . HOH P 7 .   ? 31.872  -10.245 65.963  1.00 36.81 ? 833  HOH B O   1 
HETATM 8226 O  O   . HOH P 7 .   ? 3.147   -26.570 45.337  1.00 29.39 ? 834  HOH B O   1 
HETATM 8227 O  O   . HOH P 7 .   ? 4.629   -14.511 40.177  1.00 26.59 ? 835  HOH B O   1 
HETATM 8228 O  O   . HOH P 7 .   ? -20.052 -11.104 45.615  1.00 23.41 ? 836  HOH B O   1 
HETATM 8229 O  O   . HOH P 7 .   ? -13.193 -25.608 71.496  1.00 31.07 ? 837  HOH B O   1 
HETATM 8230 O  O   . HOH P 7 .   ? 25.323  -1.350  62.744  1.00 40.85 ? 838  HOH B O   1 
HETATM 8231 O  O   . HOH P 7 .   ? 6.591   -33.766 71.660  1.00 33.92 ? 839  HOH B O   1 
HETATM 8232 O  O   . HOH P 7 .   ? 18.089  -2.488  66.251  1.00 49.66 ? 840  HOH B O   1 
HETATM 8233 O  O   . HOH P 7 .   ? -11.476 -30.788 68.370  1.00 25.15 ? 841  HOH B O   1 
HETATM 8234 O  O   . HOH P 7 .   ? -0.806  -49.273 77.135  1.00 35.22 ? 842  HOH B O   1 
HETATM 8235 O  O   . HOH P 7 .   ? -3.685  -33.938 63.760  1.00 40.36 ? 843  HOH B O   1 
HETATM 8236 O  O   . HOH P 7 .   ? 16.260  -28.522 89.122  1.00 39.90 ? 844  HOH B O   1 
HETATM 8237 O  O   . HOH P 7 .   ? 18.220  -21.847 82.180  1.00 53.96 ? 845  HOH B O   1 
HETATM 8238 O  O   . HOH P 7 .   ? -16.358 -26.185 76.304  1.00 45.16 ? 846  HOH B O   1 
HETATM 8239 O  O   . HOH P 7 .   ? -26.290 -22.934 57.384  1.00 36.94 ? 847  HOH B O   1 
HETATM 8240 O  O   . HOH P 7 .   ? -0.006  -42.765 66.432  1.00 37.22 ? 848  HOH B O   1 
HETATM 8241 O  O   . HOH P 7 .   ? 18.590  -10.462 74.570  1.00 39.21 ? 849  HOH B O   1 
HETATM 8242 O  O   . HOH P 7 .   ? -10.948 -17.565 85.005  1.00 45.77 ? 850  HOH B O   1 
HETATM 8243 O  O   . HOH P 7 .   ? 19.241  -14.483 82.620  1.00 47.74 ? 851  HOH B O   1 
HETATM 8244 O  O   . HOH P 7 .   ? -1.696  -16.622 35.958  1.00 45.39 ? 852  HOH B O   1 
HETATM 8245 O  O   . HOH P 7 .   ? 25.952  -18.922 54.768  1.00 36.81 ? 853  HOH B O   1 
HETATM 8246 O  O   . HOH P 7 .   ? -1.598  -16.229 47.812  1.00 24.19 ? 854  HOH B O   1 
HETATM 8247 O  O   . HOH P 7 .   ? 5.723   -38.888 72.452  1.00 32.64 ? 855  HOH B O   1 
HETATM 8248 O  O   . HOH P 7 .   ? -10.833 3.826   48.373  1.00 18.73 ? 856  HOH B O   1 
HETATM 8249 O  O   . HOH P 7 .   ? 4.212   -20.428 68.930  1.00 13.39 ? 857  HOH B O   1 
HETATM 8250 O  O   . HOH P 7 .   ? -25.100 -20.986 60.964  1.00 34.65 ? 858  HOH B O   1 
HETATM 8251 O  O   . HOH P 7 .   ? -22.580 -19.720 47.465  1.00 38.26 ? 859  HOH B O   1 
HETATM 8252 O  O   . HOH P 7 .   ? -15.574 -28.466 77.998  1.00 46.88 ? 860  HOH B O   1 
HETATM 8253 O  O   . HOH P 7 .   ? 22.213  -6.488  71.313  1.00 26.29 ? 861  HOH B O   1 
HETATM 8254 O  O   . HOH P 7 .   ? -0.639  -7.349  73.232  1.00 50.41 ? 862  HOH B O   1 
HETATM 8255 O  O   . HOH P 7 .   ? -2.769  -22.555 56.436  1.00 30.49 ? 863  HOH B O   1 
HETATM 8256 O  O   . HOH P 7 .   ? -5.683  -23.010 59.200  1.00 18.06 ? 864  HOH B O   1 
HETATM 8257 O  O   . HOH P 7 .   ? 10.583  -25.348 92.548  1.00 32.26 ? 865  HOH B O   1 
HETATM 8258 O  O   . HOH P 7 .   ? 4.343   -29.664 87.456  1.00 25.18 ? 866  HOH B O   1 
HETATM 8259 O  O   . HOH P 7 .   ? -25.802 -9.239  48.372  1.00 38.22 ? 867  HOH B O   1 
HETATM 8260 O  O   . HOH P 7 .   ? -5.620  -18.536 48.117  1.00 21.63 ? 868  HOH B O   1 
HETATM 8261 O  O   . HOH P 7 .   ? 8.555   3.902   65.092  1.00 43.12 ? 869  HOH B O   1 
HETATM 8262 O  O   . HOH P 7 .   ? 27.372  -15.918 53.732  1.00 42.17 ? 870  HOH B O   1 
HETATM 8263 O  O   . HOH P 7 .   ? 6.732   -8.936  79.007  1.00 35.16 ? 871  HOH B O   1 
HETATM 8264 O  O   . HOH P 7 .   ? -9.986  -29.357 56.580  1.00 39.01 ? 872  HOH B O   1 
HETATM 8265 O  O   . HOH P 7 .   ? -10.245 -35.632 79.513  1.00 20.59 ? 873  HOH B O   1 
HETATM 8266 O  O   . HOH P 7 .   ? -6.025  -29.350 58.584  1.00 45.59 ? 874  HOH B O   1 
HETATM 8267 O  O   . HOH P 7 .   ? -23.029 2.365   58.304  1.00 33.59 ? 875  HOH B O   1 
HETATM 8268 O  O   . HOH P 7 .   ? -13.505 -35.470 79.557  1.00 46.43 ? 876  HOH B O   1 
HETATM 8269 O  O   . HOH P 7 .   ? -1.214  -43.090 81.353  1.00 25.41 ? 877  HOH B O   1 
HETATM 8270 O  O   . HOH P 7 .   ? 9.324   -9.471  81.847  1.00 30.58 ? 878  HOH B O   1 
HETATM 8271 O  O   . HOH P 7 .   ? 0.419   8.057   52.750  1.00 23.48 ? 879  HOH B O   1 
HETATM 8272 O  O   . HOH P 7 .   ? -10.822 -33.556 81.002  1.00 35.50 ? 880  HOH B O   1 
HETATM 8273 O  O   . HOH P 7 .   ? -11.464 -16.656 42.067  1.00 28.26 ? 881  HOH B O   1 
HETATM 8274 O  O   . HOH P 7 .   ? 3.053   7.084   53.560  1.00 32.12 ? 882  HOH B O   1 
HETATM 8275 O  O   . HOH P 7 .   ? 1.942   -43.612 64.993  1.00 34.09 ? 883  HOH B O   1 
HETATM 8276 O  O   . HOH P 7 .   ? -15.064 -30.761 62.965  1.00 39.01 ? 884  HOH B O   1 
HETATM 8277 O  O   . HOH P 7 .   ? -19.260 -6.482  37.634  1.00 28.95 ? 885  HOH B O   1 
HETATM 8278 O  O   . HOH P 7 .   ? 5.690   -38.463 80.333  1.00 30.02 ? 886  HOH B O   1 
HETATM 8279 O  O   . HOH P 7 .   ? 0.563   -6.895  78.024  1.00 35.13 ? 887  HOH B O   1 
HETATM 8280 O  O   . HOH P 7 .   ? -0.081  -0.546  62.849  1.00 24.23 ? 888  HOH B O   1 
HETATM 8281 O  O   . HOH P 7 .   ? -26.050 -10.947 56.015  1.00 33.26 ? 889  HOH B O   1 
HETATM 8282 O  O   . HOH P 7 .   ? -20.236 7.678   57.231  1.00 28.06 ? 890  HOH B O   1 
HETATM 8283 O  O   . HOH P 7 .   ? 24.460  -1.207  56.042  1.00 56.92 ? 891  HOH B O   1 
HETATM 8284 O  O   . HOH P 7 .   ? -25.209 -6.906  65.879  1.00 28.07 ? 892  HOH B O   1 
HETATM 8285 O  O   . HOH P 7 .   ? 18.356  -3.650  47.921  1.00 42.90 ? 893  HOH B O   1 
HETATM 8286 O  O   . HOH P 7 .   ? -2.514  -4.843  51.443  1.00 22.91 ? 894  HOH B O   1 
HETATM 8287 O  O   . HOH P 7 .   ? -20.719 -3.601  73.413  1.00 19.12 ? 895  HOH B O   1 
HETATM 8288 O  O   . HOH P 7 .   ? -13.490 12.816  57.947  1.00 42.47 ? 896  HOH B O   1 
HETATM 8289 O  O   . HOH P 7 .   ? 3.896   -44.474 53.062  1.00 41.50 ? 897  HOH B O   1 
HETATM 8290 O  O   . HOH P 7 .   ? -2.548  -7.158  77.812  1.00 25.64 ? 898  HOH B O   1 
HETATM 8291 O  O   . HOH P 7 .   ? -18.863 -17.432 42.580  1.00 27.71 ? 899  HOH B O   1 
HETATM 8292 O  O   . HOH P 7 .   ? -20.717 -13.417 66.930  1.00 18.43 ? 900  HOH B O   1 
HETATM 8293 O  O   . HOH P 7 .   ? -13.899 12.254  60.609  1.00 25.11 ? 901  HOH B O   1 
HETATM 8294 O  O   . HOH P 7 .   ? -9.621  -18.436 81.348  1.00 29.53 ? 902  HOH B O   1 
HETATM 8295 O  O   . HOH P 7 .   ? 31.463  -2.918  59.162  1.00 37.88 ? 903  HOH B O   1 
HETATM 8296 O  O   . HOH P 7 .   ? 21.902  -14.025 50.064  1.00 47.56 ? 904  HOH B O   1 
HETATM 8297 O  O   . HOH P 7 .   ? 5.232   -44.532 77.788  1.00 56.09 ? 905  HOH B O   1 
HETATM 8298 O  O   . HOH P 7 .   ? -22.023 -23.465 56.751  1.00 20.01 ? 906  HOH B O   1 
HETATM 8299 O  O   . HOH P 7 .   ? -6.248  -38.722 83.897  1.00 25.67 ? 907  HOH B O   1 
HETATM 8300 O  O   . HOH P 7 .   ? 9.246   -19.003 93.413  1.00 31.33 ? 908  HOH B O   1 
HETATM 8301 O  O   . HOH P 7 .   ? -6.497  -19.689 52.469  1.00 26.53 ? 909  HOH B O   1 
HETATM 8302 O  O   . HOH P 7 .   ? 23.344  -18.927 65.776  1.00 19.20 ? 910  HOH B O   1 
HETATM 8303 O  O   . HOH P 7 .   ? 6.322   -8.938  82.842  1.00 36.96 ? 911  HOH B O   1 
HETATM 8304 O  O   . HOH P 7 .   ? -9.068  -23.105 87.635  1.00 23.19 ? 912  HOH B O   1 
HETATM 8305 O  O   . HOH P 7 .   ? -8.191  12.995  55.159  1.00 27.83 ? 913  HOH B O   1 
HETATM 8306 O  O   . HOH P 7 .   ? -17.838 -17.590 37.457  1.00 51.89 ? 914  HOH B O   1 
HETATM 8307 O  O   . HOH P 7 .   ? -13.071 2.813   39.654  1.00 39.96 ? 915  HOH B O   1 
HETATM 8308 O  O   . HOH P 7 .   ? -20.156 -15.194 77.157  1.00 28.71 ? 916  HOH B O   1 
HETATM 8309 O  O   . HOH P 7 .   ? 9.309   -32.913 79.189  1.00 38.72 ? 917  HOH B O   1 
HETATM 8310 O  O   . HOH P 7 .   ? 11.985  -33.058 68.245  1.00 43.80 ? 918  HOH B O   1 
HETATM 8311 O  O   . HOH P 7 .   ? -21.101 -15.858 65.813  1.00 48.08 ? 919  HOH B O   1 
HETATM 8312 O  O   . HOH P 7 .   ? -19.195 1.861   74.562  1.00 39.55 ? 920  HOH B O   1 
HETATM 8313 O  O   . HOH P 7 .   ? -4.308  -20.653 53.561  1.00 32.73 ? 921  HOH B O   1 
HETATM 8314 O  O   . HOH P 7 .   ? -16.664 -17.810 68.071  1.00 24.46 ? 922  HOH B O   1 
HETATM 8315 O  O   . HOH P 7 .   ? 9.542   -30.378 44.868  1.00 44.03 ? 923  HOH B O   1 
HETATM 8316 O  O   . HOH P 7 .   ? -9.299  -37.743 69.315  1.00 54.92 ? 924  HOH B O   1 
HETATM 8317 O  O   . HOH P 7 .   ? -10.325 6.399   74.050  1.00 49.33 ? 925  HOH B O   1 
HETATM 8318 O  O   . HOH P 7 .   ? -6.718  9.623   46.101  1.00 23.26 ? 926  HOH B O   1 
HETATM 8319 O  O   . HOH P 7 .   ? -7.028  -35.087 87.123  1.00 29.39 ? 927  HOH B O   1 
HETATM 8320 O  O   . HOH P 7 .   ? 8.893   -28.916 73.317  1.00 40.03 ? 928  HOH B O   1 
HETATM 8321 O  O   . HOH P 7 .   ? -0.603  -40.250 57.306  1.00 52.84 ? 929  HOH B O   1 
HETATM 8322 O  O   . HOH P 7 .   ? -15.409 -21.397 74.091  1.00 44.39 ? 930  HOH B O   1 
HETATM 8323 O  O   . HOH P 7 .   ? 18.562  -19.040 81.796  1.00 46.02 ? 931  HOH B O   1 
HETATM 8324 O  O   . HOH P 7 .   ? -12.435 -21.706 81.197  1.00 56.31 ? 932  HOH B O   1 
HETATM 8325 O  O   . HOH P 7 .   ? 18.122  -12.357 76.755  1.00 42.39 ? 933  HOH B O   1 
HETATM 8326 O  O   . HOH P 7 .   ? 15.627  -26.735 55.131  1.00 35.00 ? 934  HOH B O   1 
HETATM 8327 O  O   . HOH P 7 .   ? 23.703  -1.213  59.163  1.00 42.33 ? 935  HOH B O   1 
HETATM 8328 O  O   . HOH P 7 .   ? -3.104  -17.958 46.530  1.00 34.38 ? 936  HOH B O   1 
HETATM 8329 O  O   B HOH P 7 .   ? 1.084   -9.824  65.102  0.20 14.92 ? 937  HOH B O   1 
HETATM 8330 O  O   . HOH P 7 .   ? -13.056 5.664   70.712  1.00 41.55 ? 938  HOH B O   1 
HETATM 8331 O  O   . HOH P 7 .   ? -5.913  -42.341 63.438  1.00 45.38 ? 939  HOH B O   1 
HETATM 8332 O  O   . HOH P 7 .   ? 16.713  -27.203 68.550  1.00 33.17 ? 940  HOH B O   1 
HETATM 8333 O  O   . HOH P 7 .   ? 9.587   -30.874 72.133  1.00 41.27 ? 941  HOH B O   1 
HETATM 8334 O  O   . HOH P 7 .   ? -11.158 -35.394 64.528  1.00 43.24 ? 942  HOH B O   1 
HETATM 8335 O  O   . HOH P 7 .   ? -17.209 -11.711 85.549  1.00 49.29 ? 943  HOH B O   1 
HETATM 8336 O  O   . HOH P 7 .   ? 26.525  -8.540  53.762  1.00 40.57 ? 944  HOH B O   1 
HETATM 8337 O  O   . HOH P 7 .   ? -17.259 -28.284 62.264  1.00 52.59 ? 945  HOH B O   1 
HETATM 8338 O  O   . HOH P 7 .   ? 30.765  -6.665  58.829  1.00 37.05 ? 946  HOH B O   1 
HETATM 8339 O  O   . HOH P 7 .   ? -0.238  10.156  55.072  1.00 21.24 ? 947  HOH B O   1 
HETATM 8340 O  O   . HOH P 7 .   ? -23.506 -4.628  54.719  1.00 48.96 ? 948  HOH B O   1 
HETATM 8341 O  O   . HOH P 7 .   ? -12.369 -36.390 73.546  1.00 30.33 ? 949  HOH B O   1 
HETATM 8342 O  O   . HOH P 7 .   ? -5.215  -36.549 63.050  1.00 47.50 ? 950  HOH B O   1 
HETATM 8343 O  O   . HOH P 7 .   ? 19.229  -22.029 54.482  1.00 34.90 ? 951  HOH B O   1 
HETATM 8344 O  O   . HOH P 7 .   ? 2.464   -29.302 91.640  1.00 39.81 ? 952  HOH B O   1 
HETATM 8345 O  O   . HOH P 7 .   ? 1.977   10.683  56.505  1.00 43.12 ? 953  HOH B O   1 
HETATM 8346 O  O   . HOH P 7 .   ? -4.493  -1.590  67.767  1.00 50.66 ? 954  HOH B O   1 
HETATM 8347 O  O   . HOH P 7 .   ? -24.526 -7.650  49.868  1.00 36.99 ? 955  HOH B O   1 
HETATM 8348 O  O   . HOH P 7 .   ? 23.643  -21.369 61.621  1.00 57.07 ? 956  HOH B O   1 
HETATM 8349 O  O   . HOH P 7 .   ? -28.252 -11.906 46.861  1.00 60.53 ? 957  HOH B O   1 
HETATM 8350 O  O   . HOH P 7 .   ? -6.633  -22.597 56.760  1.00 18.52 ? 958  HOH B O   1 
HETATM 8351 O  O   . HOH P 7 .   ? -9.875  -22.370 81.501  1.00 31.34 ? 959  HOH B O   1 
HETATM 8352 O  O   . HOH P 7 .   ? -0.649  -30.574 44.562  1.00 44.04 ? 960  HOH B O   1 
HETATM 8353 O  O   . HOH P 7 .   ? 10.079  0.217   51.821  1.00 38.58 ? 961  HOH B O   1 
HETATM 8354 O  O   . HOH P 7 .   ? 5.810   -31.746 87.529  1.00 44.63 ? 962  HOH B O   1 
HETATM 8355 O  O   . HOH P 7 .   ? -0.217  -32.805 54.893  1.00 42.03 ? 963  HOH B O   1 
HETATM 8356 O  O   . HOH P 7 .   ? 21.430  -15.008 40.274  1.00 49.70 ? 964  HOH B O   1 
HETATM 8357 O  O   . HOH P 7 .   ? 1.106   -35.512 53.187  1.00 39.32 ? 965  HOH B O   1 
HETATM 8358 O  O   . HOH P 7 .   ? -23.851 -19.275 62.628  1.00 32.13 ? 966  HOH B O   1 
HETATM 8359 O  O   . HOH P 7 .   ? 24.794  -15.824 71.778  1.00 36.27 ? 967  HOH B O   1 
HETATM 8360 O  O   . HOH P 7 .   ? -22.939 -8.933  71.174  1.00 25.30 ? 968  HOH B O   1 
HETATM 8361 O  O   . HOH P 7 .   ? -25.383 0.472   46.569  1.00 54.05 ? 969  HOH B O   1 
HETATM 8362 O  O   . HOH P 7 .   ? -1.968  -2.858  68.789  1.00 36.31 ? 970  HOH B O   1 
HETATM 8363 O  O   . HOH P 7 .   ? -13.474 -35.989 77.162  1.00 30.19 ? 971  HOH B O   1 
HETATM 8364 O  O   . HOH P 7 .   ? -25.400 -9.578  71.716  1.00 50.21 ? 972  HOH B O   1 
HETATM 8365 O  O   . HOH P 7 .   ? 24.858  -11.323 51.776  1.00 50.30 ? 973  HOH B O   1 
HETATM 8366 O  O   . HOH P 7 .   ? -13.403 -39.405 72.513  1.00 41.03 ? 974  HOH B O   1 
HETATM 8367 O  O   . HOH P 7 .   ? 30.952  -2.957  61.429  1.00 51.17 ? 975  HOH B O   1 
HETATM 8368 O  O   . HOH P 7 .   ? 6.497   4.724   49.202  1.00 38.85 ? 976  HOH B O   1 
HETATM 8369 O  O   . HOH P 7 .   ? -0.958  6.063   49.103  1.00 50.83 ? 977  HOH B O   1 
HETATM 8370 O  O   . HOH P 7 .   ? 27.059  -6.081  54.567  1.00 48.54 ? 978  HOH B O   1 
HETATM 8371 O  O   . HOH P 7 .   ? -8.390  -21.352 52.901  1.00 35.80 ? 979  HOH B O   1 
HETATM 8372 O  O   . HOH P 7 .   ? -21.715 3.176   55.719  1.00 35.39 ? 980  HOH B O   1 
HETATM 8373 O  O   . HOH P 7 .   ? 18.333  -25.497 61.640  1.00 46.04 ? 981  HOH B O   1 
HETATM 8374 O  O   . HOH P 7 .   ? -24.670 2.617   65.443  1.00 39.62 ? 982  HOH B O   1 
HETATM 8375 O  O   . HOH P 7 .   ? -8.763  -20.576 82.954  1.00 35.92 ? 983  HOH B O   1 
HETATM 8376 O  O   . HOH P 7 .   ? 0.607   -15.657 37.146  1.00 54.05 ? 984  HOH B O   1 
HETATM 8377 O  O   . HOH P 7 .   ? 1.396   -37.699 51.679  1.00 56.96 ? 985  HOH B O   1 
HETATM 8378 O  O   . HOH P 7 .   ? -23.800 -13.278 67.067  1.00 51.79 ? 986  HOH B O   1 
HETATM 8379 O  O   . HOH P 7 .   ? 14.782  -27.926 49.931  1.00 50.66 ? 987  HOH B O   1 
HETATM 8380 O  O   . HOH P 7 .   ? 0.902   -16.075 94.248  1.00 49.59 ? 988  HOH B O   1 
HETATM 8381 O  O   . HOH P 7 .   ? 7.621   -15.598 74.720  1.00 15.29 ? 989  HOH B O   1 
HETATM 8382 O  O   . HOH P 7 .   ? 7.270   -12.997 90.958  1.00 41.50 ? 990  HOH B O   1 
HETATM 8383 O  O   . HOH P 7 .   ? -7.174  -20.401 46.740  1.00 44.13 ? 991  HOH B O   1 
HETATM 8384 O  O   . HOH P 7 .   ? -17.436 1.302   41.075  1.00 37.76 ? 992  HOH B O   1 
HETATM 8385 O  O   . HOH P 7 .   ? -6.956  -25.838 89.423  1.00 44.45 ? 993  HOH B O   1 
HETATM 8386 O  O   . HOH P 7 .   ? 4.587   -11.703 87.647  1.00 39.76 ? 994  HOH B O   1 
HETATM 8387 O  O   . HOH P 7 .   ? 15.890  -11.795 79.725  1.00 44.31 ? 995  HOH B O   1 
HETATM 8388 O  O   . HOH P 7 .   ? 12.089  -33.676 47.020  1.00 58.99 ? 996  HOH B O   1 
HETATM 8389 O  O   . HOH P 7 .   ? 18.592  -26.102 89.314  1.00 47.15 ? 997  HOH B O   1 
HETATM 8390 O  O   . HOH P 7 .   ? 1.064   -13.086 36.246  1.00 29.53 ? 998  HOH B O   1 
HETATM 8391 O  O   . HOH P 7 .   ? 5.672   -48.461 52.535  1.00 52.34 ? 999  HOH B O   1 
HETATM 8392 O  O   . HOH P 7 .   ? 8.070   -5.375  68.355  1.00 48.13 ? 1000 HOH B O   1 
HETATM 8393 O  O   . HOH P 7 .   ? -5.015  -23.410 55.028  1.00 34.39 ? 1001 HOH B O   1 
HETATM 8394 O  O   . HOH P 7 .   ? -16.849 -27.946 80.548  1.00 37.83 ? 1002 HOH B O   1 
HETATM 8395 O  O   . HOH P 7 .   ? -19.717 9.577   55.410  1.00 50.38 ? 1003 HOH B O   1 
HETATM 8396 O  O   . HOH P 7 .   ? -12.763 -32.702 76.456  1.00 33.23 ? 1004 HOH B O   1 
HETATM 8397 O  O   . HOH P 7 .   ? -1.518  12.428  54.181  1.00 37.60 ? 1005 HOH B O   1 
HETATM 8398 O  O   . HOH P 7 .   ? -4.419  10.513  47.041  1.00 53.26 ? 1006 HOH B O   1 
HETATM 8399 O  O   . HOH P 7 .   ? -13.504 -24.985 51.361  1.00 41.96 ? 1007 HOH B O   1 
HETATM 8400 O  O   . HOH P 7 .   ? -23.864 -1.683  57.487  1.00 36.60 ? 1008 HOH B O   1 
HETATM 8401 O  O   . HOH P 7 .   ? -19.986 -26.742 59.098  1.00 38.51 ? 1009 HOH B O   1 
HETATM 8402 O  O   . HOH P 7 .   ? -16.948 -20.079 68.482  1.00 41.11 ? 1010 HOH B O   1 
HETATM 8403 O  O   . HOH P 7 .   ? 20.439  -0.885  63.740  1.00 52.18 ? 1011 HOH B O   1 
HETATM 8404 O  O   . HOH P 7 .   ? 14.344  -32.475 48.152  1.00 57.15 ? 1012 HOH B O   1 
HETATM 8405 O  O   . HOH P 7 .   ? 5.586   -45.294 50.651  1.00 45.69 ? 1013 HOH B O   1 
HETATM 8406 O  O   . HOH P 7 .   ? -17.761 6.616   50.797  1.00 37.30 ? 1014 HOH B O   1 
HETATM 8407 O  O   . HOH P 7 .   ? -11.366 -33.757 69.893  1.00 30.65 ? 1015 HOH B O   1 
HETATM 8408 O  O   . HOH P 7 .   ? 2.058   6.472   50.168  1.00 50.63 ? 1016 HOH B O   1 
HETATM 8409 O  O   . HOH P 7 .   ? -13.310 -31.781 66.388  1.00 45.65 ? 1017 HOH B O   1 
HETATM 8410 O  O   . HOH P 7 .   ? -15.196 -22.172 49.837  1.00 27.40 ? 1018 HOH B O   1 
HETATM 8411 O  O   . HOH P 7 .   ? 1.023   -33.790 89.056  1.00 53.87 ? 1019 HOH B O   1 
HETATM 8412 O  O   . HOH P 7 .   ? -3.707  -25.221 49.499  1.00 48.49 ? 1020 HOH B O   1 
HETATM 8413 O  O   . HOH P 7 .   ? -24.428 4.925   61.541  1.00 34.30 ? 1021 HOH B O   1 
HETATM 8414 O  O   . HOH P 7 .   ? -2.243  -45.490 82.621  1.00 24.70 ? 1022 HOH B O   1 
HETATM 8415 O  O   . HOH P 7 .   ? 13.375  -17.611 88.827  1.00 33.77 ? 1023 HOH B O   1 
HETATM 8416 O  O   . HOH P 7 .   ? -14.579 -2.101  37.531  1.00 51.18 ? 1024 HOH B O   1 
HETATM 8417 O  O   . HOH P 7 .   ? 11.957  -6.091  72.039  1.00 50.54 ? 1025 HOH B O   1 
HETATM 8418 O  O   . HOH P 7 .   ? -22.960 3.877   63.711  1.00 27.53 ? 1026 HOH B O   1 
HETATM 8419 O  O   . HOH P 7 .   ? -8.139  -16.423 88.046  1.00 30.38 ? 1027 HOH B O   1 
HETATM 8420 O  O   . HOH P 7 .   ? -10.962 -35.006 76.835  1.00 36.58 ? 1028 HOH B O   1 
HETATM 8421 O  O   . HOH P 7 .   ? 3.338   -31.878 87.404  1.00 51.98 ? 1029 HOH B O   1 
HETATM 8422 O  O   . HOH P 7 .   ? 10.032  -6.971  69.785  1.00 42.60 ? 1030 HOH B O   1 
HETATM 8423 O  O   . HOH P 7 .   ? 20.388  -12.145 74.085  1.00 48.35 ? 1031 HOH B O   1 
HETATM 8424 O  O   . HOH P 7 .   ? -5.588  13.865  47.334  1.00 56.87 ? 1032 HOH B O   1 
HETATM 8425 O  O   . HOH P 7 .   ? -12.982 9.319   42.939  1.00 33.05 ? 1033 HOH B O   1 
HETATM 8426 O  O   . HOH P 7 .   ? -24.068 -24.938 57.185  1.00 43.31 ? 1034 HOH B O   1 
HETATM 8427 O  O   . HOH P 7 .   ? 6.418   2.359   47.199  1.00 34.82 ? 1035 HOH B O   1 
HETATM 8428 O  O   . HOH P 7 .   ? -2.702  -49.642 79.322  1.00 44.76 ? 1036 HOH B O   1 
HETATM 8429 O  O   . HOH P 7 .   ? 23.231  -13.323 71.260  1.00 22.42 ? 1037 HOH B O   1 
HETATM 8430 O  O   . HOH P 7 .   ? -5.609  -20.371 50.144  1.00 25.76 ? 1038 HOH B O   1 
HETATM 8431 O  O   . HOH P 7 .   ? -21.098 -21.367 65.492  1.00 39.68 ? 1039 HOH B O   1 
HETATM 8432 O  O   . HOH P 7 .   ? -5.100  -42.597 85.825  1.00 49.00 ? 1040 HOH B O   1 
HETATM 8433 O  O   . HOH P 7 .   ? -18.868 -3.550  75.736  1.00 45.01 ? 1041 HOH B O   1 
HETATM 8434 O  O   . HOH P 7 .   ? -13.633 0.339   40.460  1.00 34.63 ? 1042 HOH B O   1 
HETATM 8435 O  O   . HOH P 7 .   ? 25.983  -19.161 64.738  1.00 43.64 ? 1043 HOH B O   1 
HETATM 8436 O  O   . HOH P 7 .   ? -5.189  3.141   42.985  1.00 37.71 ? 1044 HOH B O   1 
HETATM 8437 O  O   . HOH P 7 .   ? -13.948 -15.399 41.402  1.00 31.39 ? 1045 HOH B O   1 
HETATM 8438 O  O   . HOH P 7 .   ? -21.141 4.664   51.779  1.00 50.44 ? 1046 HOH B O   1 
HETATM 8439 O  O   . HOH P 7 .   ? -27.853 -9.665  59.140  1.00 43.34 ? 1047 HOH B O   1 
HETATM 8440 O  O   . HOH P 7 .   ? -7.337  -23.065 48.451  1.00 46.66 ? 1048 HOH B O   1 
HETATM 8441 O  O   . HOH P 7 .   ? -17.278 -29.056 82.900  1.00 54.25 ? 1049 HOH B O   1 
HETATM 8442 O  O   . HOH P 7 .   ? -19.750 -20.430 67.323  1.00 55.58 ? 1050 HOH B O   1 
HETATM 8443 O  O   . HOH P 7 .   ? -21.999 5.932   56.071  1.00 38.88 ? 1051 HOH B O   1 
HETATM 8444 O  O   . HOH P 7 .   ? -14.490 -29.155 67.717  1.00 54.96 ? 1052 HOH B O   1 
HETATM 8445 O  O   . HOH P 7 .   ? -0.148  5.303   46.386  1.00 41.60 ? 1053 HOH B O   1 
HETATM 8446 O  O   . HOH P 7 .   ? -13.040 -32.180 71.903  1.00 28.16 ? 1054 HOH B O   1 
HETATM 8447 O  O   . HOH P 7 .   ? -18.930 11.894  56.105  1.00 44.43 ? 1055 HOH B O   1 
HETATM 8448 O  O   . HOH P 7 .   ? 4.770   -26.455 42.945  1.00 40.04 ? 1056 HOH B O   1 
HETATM 8449 O  O   . HOH P 7 .   ? 22.811  -20.149 83.151  1.00 51.87 ? 1057 HOH B O   1 
HETATM 8450 O  O   . HOH P 7 .   ? -9.301  15.197  53.772  1.00 44.27 ? 1058 HOH B O   1 
HETATM 8451 O  O   . HOH P 7 .   ? 26.690  -12.446 69.829  1.00 28.48 ? 1059 HOH B O   1 
HETATM 8452 O  O   . HOH P 7 .   ? -23.214 -13.342 70.255  1.00 43.58 ? 1060 HOH B O   1 
HETATM 8453 O  O   . HOH P 7 .   ? -25.406 -6.137  57.944  1.00 39.88 ? 1061 HOH B O   1 
HETATM 8454 O  O   . HOH P 7 .   ? -16.582 -22.637 67.243  1.00 46.51 ? 1062 HOH B O   1 
HETATM 8455 O  O   . HOH P 7 .   ? -24.224 4.789   58.628  1.00 48.82 ? 1063 HOH B O   1 
HETATM 8456 O  O   . HOH P 7 .   ? 3.754   9.221   54.894  1.00 45.64 ? 1064 HOH B O   1 
HETATM 8457 O  O   . HOH P 7 .   ? -10.430 -34.482 73.879  1.00 25.16 ? 1065 HOH B O   1 
HETATM 8458 O  O   . HOH P 7 .   ? -11.799 11.973  44.165  1.00 57.17 ? 1066 HOH B O   1 
HETATM 8459 O  O   . HOH P 7 .   ? -1.056  -48.485 73.008  1.00 47.96 ? 1067 HOH B O   1 
HETATM 8460 O  O   . HOH P 7 .   ? 4.263   -31.428 92.539  1.00 58.07 ? 1068 HOH B O   1 
HETATM 8461 O  O   . HOH P 7 .   ? -5.178  -23.382 50.152  1.00 33.44 ? 1069 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . THR A 2   ? 1.0164 0.7652 0.5736 0.0387  0.0104  0.1742  1    THR A N   
2    C  CA  . THR A 2   ? 1.0284 0.7678 0.5814 0.0395  0.0332  0.1550  1    THR A CA  
3    C  C   . THR A 2   ? 0.9445 0.7317 0.5532 0.0636  0.0180  0.1439  1    THR A C   
4    O  O   . THR A 2   ? 0.9156 0.7132 0.5731 0.0746  -0.0088 0.1389  1    THR A O   
5    C  CB  . THR A 2   ? 1.0950 0.8078 0.6066 0.0277  0.0761  0.1474  1    THR A CB  
6    O  OG1 . THR A 2   ? 1.1428 0.8256 0.6155 0.0370  0.1021  0.1400  1    THR A OG1 
7    C  CG2 . THR A 2   ? 1.1244 0.8252 0.6175 0.0133  0.0756  0.1420  1    THR A CG2 
8    N  N   . ILE A 3   ? 0.8924 0.7225 0.5174 0.0574  0.0209  0.1221  2    ILE A N   
9    C  CA  . ILE A 3   ? 0.8037 0.7175 0.4876 0.0596  0.0331  0.0838  2    ILE A CA  
10   C  C   . ILE A 3   ? 0.7930 0.7007 0.4302 0.0760  0.0411  0.0691  2    ILE A C   
11   O  O   . ILE A 3   ? 0.7963 0.7080 0.4030 0.0884  0.0488  0.0618  2    ILE A O   
12   C  CB  . ILE A 3   ? 0.6889 0.7242 0.5186 0.0538  0.0230  0.0502  2    ILE A CB  
13   C  CG1 . ILE A 3   ? 0.6735 0.7321 0.5402 0.0469  0.0426  0.0211  2    ILE A CG1 
14   C  CG2 . ILE A 3   ? 0.6561 0.7141 0.5253 0.0515  0.0080  0.0488  2    ILE A CG2 
15   C  CD1 . ILE A 3   ? 0.6871 0.7309 0.5556 0.0307  0.0454  0.0098  2    ILE A CD1 
16   N  N   . LYS A 4   ? 0.7194 0.6640 0.3855 0.0746  0.0675  0.0592  3    LYS A N   
17   C  CA  . LYS A 4   ? 0.6820 0.6366 0.3691 0.0787  0.0764  0.0542  3    LYS A CA  
18   C  C   . LYS A 4   ? 0.7211 0.6210 0.3440 0.0538  0.0718  0.0496  3    LYS A C   
19   O  O   . LYS A 4   ? 0.6933 0.6293 0.3331 0.0002  0.1041  0.0507  3    LYS A O   
20   C  CB  . LYS A 4   ? 0.5507 0.6395 0.3930 0.0921  0.0778  0.0387  3    LYS A CB  
21   C  CG  . LYS A 4   ? 0.5288 0.6593 0.4366 0.1149  0.0837  0.0179  3    LYS A CG  
22   C  CD  . LYS A 4   ? 0.5571 0.6758 0.4669 0.1322  0.0802  0.0280  3    LYS A CD  
23   C  CE  . LYS A 4   ? 0.6269 0.6913 0.5054 0.1532  0.0387  0.0383  3    LYS A CE  
24   N  NZ  . LYS A 4   ? 0.6842 0.7036 0.5128 0.1390  0.0180  0.0501  3    LYS A NZ  
25   N  N   . GLU A 5   ? 0.7398 0.5793 0.3333 0.0730  0.0855  0.0383  4    GLU A N   
26   C  CA  . GLU A 5   ? 0.6854 0.5558 0.3350 0.0418  0.0714  0.0399  4    GLU A CA  
27   C  C   . GLU A 5   ? 0.5831 0.5057 0.2713 0.0681  0.1032  0.0215  4    GLU A C   
28   O  O   . GLU A 5   ? 0.6238 0.5207 0.2604 0.0705  0.1251  -0.0049 4    GLU A O   
29   C  CB  . GLU A 5   ? 0.7643 0.5981 0.4041 -0.0114 0.0240  0.0652  4    GLU A CB  
30   C  CG  . GLU A 5   ? 0.8551 0.6530 0.4487 -0.0539 0.0003  0.0836  4    GLU A CG  
31   C  CD  . GLU A 5   ? 0.9921 0.6942 0.4986 -0.0782 -0.0038 0.0930  4    GLU A CD  
32   O  OE1 . GLU A 5   ? 1.0249 0.7130 0.5130 -0.0618 -0.0201 0.0899  4    GLU A OE1 
33   O  OE2 . GLU A 5   ? 1.0112 0.6965 0.5147 -0.1232 0.0083  0.0964  4    GLU A OE2 
34   N  N   . MET A 6   ? 0.4893 0.4318 0.2344 0.0621  0.0689  0.0625  5    MET A N   
35   C  CA  . MET A 6   ? 0.4595 0.3562 0.2036 0.1050  0.0657  0.0406  5    MET A CA  
36   C  C   . MET A 6   ? 0.3581 0.3145 0.1883 0.0765  0.0698  -0.0051 5    MET A C   
37   O  O   . MET A 6   ? 0.3444 0.3426 0.1870 -0.0098 0.0307  -0.0388 5    MET A O   
38   C  CB  . MET A 6   ? 0.4273 0.3223 0.2278 0.1336  0.0398  0.0622  5    MET A CB  
39   C  CG  . MET A 6   ? 0.3529 0.3218 0.2352 0.1396  0.0763  0.0262  5    MET A CG  
40   S  SD  . MET A 6   ? 0.3404 0.3067 0.2250 0.0784  0.0263  -0.0014 5    MET A SD  
41   C  CE  . MET A 6   ? 0.2935 0.3226 0.2123 0.1290  -0.0247 0.0386  5    MET A CE  
42   N  N   . PRO A 7   ? 0.3325 0.2643 0.1869 0.0939  0.0889  -0.0151 6    PRO A N   
43   C  CA  . PRO A 7   ? 0.2818 0.2660 0.1904 0.0902  0.1150  0.0176  6    PRO A CA  
44   C  C   . PRO A 7   ? 0.3430 0.2629 0.1768 0.0944  0.1108  0.0162  6    PRO A C   
45   O  O   . PRO A 7   ? 0.3131 0.2325 0.1811 0.0775  0.0616  0.0022  6    PRO A O   
46   C  CB  . PRO A 7   ? 0.4159 0.2673 0.2036 0.0848  0.0867  -0.0113 6    PRO A CB  
47   C  CG  . PRO A 7   ? 0.3624 0.2420 0.2213 0.1038  0.0408  -0.0148 6    PRO A CG  
48   C  CD  . PRO A 7   ? 0.3915 0.2491 0.2141 0.0646  0.0432  -0.0053 6    PRO A CD  
49   N  N   . GLN A 8   ? 0.3137 0.2518 0.1739 0.0880  0.0918  0.0252  7    GLN A N   
50   C  CA  . GLN A 8   ? 0.3035 0.2431 0.1897 0.0793  0.1075  0.0465  7    GLN A CA  
51   C  C   . GLN A 8   ? 0.3086 0.2033 0.1901 0.0901  0.0938  0.0244  7    GLN A C   
52   O  O   . GLN A 8   ? 0.3380 0.1933 0.2074 0.0735  0.0965  0.0489  7    GLN A O   
53   C  CB  . GLN A 8   ? 0.2552 0.2428 0.1825 0.0665  0.0989  0.0153  7    GLN A CB  
54   C  CG  . GLN A 8   ? 0.3288 0.2575 0.1900 0.0989  0.1084  0.0094  7    GLN A CG  
55   C  CD  . GLN A 8   ? 0.3733 0.3113 0.2064 0.0895  0.0752  -0.0011 7    GLN A CD  
56   O  OE1 . GLN A 8   ? 0.3585 0.3726 0.2198 0.0420  0.0527  -0.0094 7    GLN A OE1 
57   N  NE2 . GLN A 8   ? 0.3941 0.2855 0.2365 0.1134  0.0303  0.0063  7    GLN A NE2 
58   N  N   . PRO A 9   ? 0.2612 0.1830 0.1915 0.0657  0.0922  0.0208  8    PRO A N   
59   C  CA  . PRO A 9   ? 0.2243 0.1754 0.1973 0.0855  0.0338  -0.0206 8    PRO A CA  
60   C  C   . PRO A 9   ? 0.1839 0.1940 0.2244 0.0533  0.0219  -0.0141 8    PRO A C   
61   O  O   . PRO A 9   ? 0.2238 0.2252 0.2155 0.0312  0.0167  -0.0459 8    PRO A O   
62   C  CB  . PRO A 9   ? 0.1582 0.1884 0.1868 0.0691  0.0632  -0.0197 8    PRO A CB  
63   C  CG  . PRO A 9   ? 0.1618 0.1990 0.1817 0.0272  0.0579  -0.0045 8    PRO A CG  
64   C  CD  . PRO A 9   ? 0.2860 0.1972 0.1553 0.0134  0.0984  -0.0052 8    PRO A CD  
65   N  N   . LYS A 10  ? 0.2237 0.1894 0.2265 0.1079  0.0404  0.0182  9    LYS A N   
66   C  CA  . LYS A 10  ? 0.2222 0.2035 0.2284 0.0923  0.0480  0.0282  9    LYS A CA  
67   C  C   . LYS A 10  ? 0.2509 0.2059 0.2243 0.0864  0.0724  0.0083  9    LYS A C   
68   O  O   . LYS A 10  ? 0.2436 0.2061 0.2359 0.0790  0.0693  0.0057  9    LYS A O   
69   C  CB  . LYS A 10  ? 0.2337 0.2263 0.2100 0.1320  -0.0310 0.0102  9    LYS A CB  
70   C  CG  . LYS A 10  ? 0.2425 0.2271 0.1814 0.0928  -0.0534 -0.0061 9    LYS A CG  
71   C  CD  . LYS A 10  ? 0.2254 0.2343 0.2087 0.0607  0.0244  -0.0080 9    LYS A CD  
72   C  CE  . LYS A 10  ? 0.2760 0.2811 0.2564 0.1524  0.0284  -0.0045 9    LYS A CE  
73   N  NZ  . LYS A 10  ? 0.3128 0.2998 0.2812 0.1738  0.0692  0.0214  9    LYS A NZ  
74   N  N   . THR A 11  ? 0.2485 0.1939 0.2221 0.0615  0.0037  0.0127  10   THR A N   
75   C  CA  . THR A 11  ? 0.2518 0.1996 0.2031 0.1121  0.0130  0.0130  10   THR A CA  
76   C  C   . THR A 11  ? 0.2706 0.1683 0.1906 0.1022  0.0326  -0.0132 10   THR A C   
77   O  O   . THR A 11  ? 0.2404 0.1413 0.1937 0.0474  0.0398  -0.0068 10   THR A O   
78   C  CB  . THR A 11  ? 0.2849 0.2179 0.1941 0.1434  0.0066  -0.0143 10   THR A CB  
79   O  OG1 . THR A 11  ? 0.2620 0.2731 0.2085 0.1196  0.0246  0.0007  10   THR A OG1 
80   C  CG2 . THR A 11  ? 0.1804 0.2185 0.2147 0.1176  -0.0010 0.0120  10   THR A CG2 
81   N  N   . PHE A 12  ? 0.2706 0.1669 0.1978 0.0972  0.0764  -0.0038 11   PHE A N   
82   C  CA  . PHE A 12  ? 0.3272 0.1806 0.1959 0.0662  0.0259  -0.0151 11   PHE A CA  
83   C  C   . PHE A 12  ? 0.3621 0.2079 0.2502 0.0729  0.0331  0.0021  11   PHE A C   
84   O  O   . PHE A 12  ? 0.4070 0.2366 0.2588 0.0970  0.0569  0.0105  11   PHE A O   
85   C  CB  . PHE A 12  ? 0.2931 0.1423 0.1777 0.0815  0.0384  -0.0344 11   PHE A CB  
86   C  CG  . PHE A 12  ? 0.2719 0.1697 0.1976 0.0759  0.0257  -0.0118 11   PHE A CG  
87   C  CD1 . PHE A 12  ? 0.2744 0.1685 0.1980 0.0722  0.0313  -0.0032 11   PHE A CD1 
88   C  CD2 . PHE A 12  ? 0.2407 0.1966 0.2049 0.0493  0.0260  -0.0169 11   PHE A CD2 
89   C  CE1 . PHE A 12  ? 0.2700 0.1810 0.1824 0.0395  0.0229  -0.0147 11   PHE A CE1 
90   C  CE2 . PHE A 12  ? 0.2749 0.1758 0.1728 0.0630  0.0304  -0.0253 11   PHE A CE2 
91   C  CZ  . PHE A 12  ? 0.2711 0.1645 0.1791 0.0919  0.0323  -0.0336 11   PHE A CZ  
92   N  N   . GLY A 13  ? 0.2999 0.2040 0.2873 0.0651  0.0158  -0.0008 12   GLY A N   
93   C  CA  . GLY A 13  ? 0.2723 0.2016 0.3200 0.1010  0.0295  -0.0355 12   GLY A CA  
94   C  C   . GLY A 13  ? 0.2385 0.2313 0.3611 0.0682  0.0566  -0.0450 12   GLY A C   
95   O  O   . GLY A 13  ? 0.2352 0.2708 0.3471 0.0952  0.0566  -0.0353 12   GLY A O   
96   N  N   . GLU A 14  ? 0.2333 0.2170 0.4010 0.0105  0.1122  -0.0505 13   GLU A N   
97   C  CA  . GLU A 14  ? 0.2929 0.2610 0.4706 -0.0106 0.1318  -0.0495 13   GLU A CA  
98   C  C   . GLU A 14  ? 0.2330 0.2598 0.4361 0.0452  0.1015  -0.0608 13   GLU A C   
99   O  O   . GLU A 14  ? 0.2302 0.2983 0.4336 0.0508  0.0876  -0.0930 13   GLU A O   
100  C  CB  . GLU A 14  ? 0.4210 0.3289 0.5677 -0.0307 0.1851  -0.0658 13   GLU A CB  
101  C  CG  . GLU A 14  ? 0.5784 0.4058 0.6891 -0.0192 0.2160  -0.0529 13   GLU A CG  
102  C  CD  . GLU A 14  ? 0.7141 0.4817 0.8130 0.0213  0.1998  -0.0689 13   GLU A CD  
103  O  OE1 . GLU A 14  ? 0.7901 0.5345 0.8657 -0.0248 0.1683  -0.0693 13   GLU A OE1 
104  O  OE2 . GLU A 14  ? 0.7897 0.5065 0.8459 0.0617  0.2152  -0.0795 13   GLU A OE2 
105  N  N   . LEU A 15  ? 0.2464 0.2268 0.4044 0.0479  0.0882  -0.0099 14   LEU A N   
106  C  CA  . LEU A 15  ? 0.2525 0.1902 0.3601 0.0794  0.1015  -0.0044 14   LEU A CA  
107  C  C   . LEU A 15  ? 0.2439 0.2030 0.3348 0.1167  0.0659  0.0075  14   LEU A C   
108  O  O   . LEU A 15  ? 0.2793 0.2156 0.3250 0.1077  0.0762  -0.0054 14   LEU A O   
109  C  CB  . LEU A 15  ? 0.2980 0.1685 0.3671 0.0439  0.1031  0.0436  14   LEU A CB  
110  C  CG  . LEU A 15  ? 0.3799 0.1979 0.3832 0.0323  0.1025  0.0665  14   LEU A CG  
111  C  CD1 . LEU A 15  ? 0.4514 0.2129 0.3787 0.0514  0.0470  0.0605  14   LEU A CD1 
112  C  CD2 . LEU A 15  ? 0.4439 0.2268 0.3955 0.0463  0.1473  0.0540  14   LEU A CD2 
113  N  N   . LYS A 16  ? 0.1780 0.2100 0.3003 0.0833  0.0664  0.0014  15   LYS A N   
114  C  CA  . LYS A 16  ? 0.2479 0.2236 0.2992 0.0679  0.0105  0.0165  15   LYS A CA  
115  C  C   . LYS A 16  ? 0.3267 0.2138 0.2668 0.0640  0.0727  0.0100  15   LYS A C   
116  O  O   . LYS A 16  ? 0.3119 0.1983 0.2498 0.0510  0.1065  -0.0071 15   LYS A O   
117  C  CB  . LYS A 16  ? 0.2479 0.2734 0.3482 0.0737  -0.0420 0.0082  15   LYS A CB  
118  C  CG  . LYS A 16  ? 0.3647 0.3457 0.4092 0.0119  -0.0866 0.0096  15   LYS A CG  
119  C  CD  . LYS A 16  ? 0.5116 0.3881 0.4401 -0.0692 -0.0970 -0.0065 15   LYS A CD  
120  C  CE  . LYS A 16  ? 0.5990 0.4310 0.4729 -0.0784 -0.0954 -0.0248 15   LYS A CE  
121  N  NZ  . LYS A 16  ? 0.6344 0.4526 0.4962 -0.1019 -0.1194 -0.0379 15   LYS A NZ  
122  N  N   . ASN A 17  ? 0.2904 0.1807 0.2565 0.0870  0.0869  0.0034  16   ASN A N   
123  C  CA  . ASN A 17  ? 0.2700 0.1638 0.2506 0.0592  0.1320  0.0176  16   ASN A CA  
124  C  C   . ASN A 17  ? 0.2760 0.1533 0.2450 0.0578  0.0923  0.0122  16   ASN A C   
125  O  O   . ASN A 17  ? 0.2936 0.1538 0.2514 0.0756  0.0504  0.0054  16   ASN A O   
126  C  CB  . ASN A 17  ? 0.2845 0.1768 0.2479 0.0980  0.1208  0.0361  16   ASN A CB  
127  C  CG  . ASN A 17  ? 0.2829 0.1772 0.2426 0.0845  0.1186  0.0067  16   ASN A CG  
128  O  OD1 . ASN A 17  ? 0.2882 0.2006 0.2101 0.1024  0.0776  0.0069  16   ASN A OD1 
129  N  ND2 . ASN A 17  ? 0.2574 0.1603 0.2715 0.0793  0.0889  0.0192  16   ASN A ND2 
130  N  N   . LEU A 18  ? 0.2554 0.1597 0.2433 0.0950  0.0770  -0.0011 17   LEU A N   
131  C  CA  . LEU A 18  ? 0.3065 0.1863 0.2493 0.0448  0.1195  0.0243  17   LEU A CA  
132  C  C   . LEU A 18  ? 0.3662 0.1736 0.2281 0.0636  0.0820  0.0242  17   LEU A C   
133  O  O   . LEU A 18  ? 0.3494 0.1566 0.2502 0.0811  0.1068  0.0240  17   LEU A O   
134  C  CB  . LEU A 18  ? 0.4073 0.2042 0.2862 -0.0395 0.1629  0.0077  17   LEU A CB  
135  C  CG  . LEU A 18  ? 0.4999 0.1999 0.3297 -0.0103 0.1206  0.0010  17   LEU A CG  
136  C  CD1 . LEU A 18  ? 0.4793 0.1797 0.3566 0.0159  0.0972  -0.0315 17   LEU A CD1 
137  C  CD2 . LEU A 18  ? 0.5242 0.2208 0.3153 0.0109  0.1187  -0.0020 17   LEU A CD2 
138  N  N   . PRO A 19  ? 0.3409 0.1654 0.2148 0.0720  0.0797  0.0436  18   PRO A N   
139  C  CA  . PRO A 19  ? 0.2822 0.1487 0.2025 0.0788  0.0211  0.0316  18   PRO A CA  
140  C  C   . PRO A 19  ? 0.2709 0.1736 0.2049 0.0813  0.0415  0.0234  18   PRO A C   
141  O  O   . PRO A 19  ? 0.2855 0.1542 0.2334 0.0858  0.0270  0.0283  18   PRO A O   
142  C  CB  . PRO A 19  ? 0.3479 0.1773 0.2055 0.0846  -0.0113 0.0221  18   PRO A CB  
143  C  CG  . PRO A 19  ? 0.3754 0.1610 0.2169 0.0792  0.0257  0.0328  18   PRO A CG  
144  C  CD  . PRO A 19  ? 0.3209 0.1396 0.2097 0.0770  0.0675  0.0392  18   PRO A CD  
145  N  N   . LEU A 20  ? 0.2527 0.1882 0.1560 0.0946  0.0614  -0.0102 19   LEU A N   
146  C  CA  . LEU A 20  ? 0.3111 0.1781 0.1433 0.0713  0.0652  -0.0095 19   LEU A CA  
147  C  C   . LEU A 20  ? 0.2835 0.1866 0.1731 0.0706  0.0367  0.0032  19   LEU A C   
148  O  O   . LEU A 20  ? 0.3446 0.1882 0.1804 0.0455  0.0344  0.0272  19   LEU A O   
149  C  CB  . LEU A 20  ? 0.2575 0.1795 0.1576 0.0475  0.0675  -0.0354 19   LEU A CB  
150  C  CG  . LEU A 20  ? 0.2382 0.1891 0.1772 0.0992  0.0503  -0.0305 19   LEU A CG  
151  C  CD1 . LEU A 20  ? 0.3574 0.1730 0.1882 0.0947  0.0158  -0.0176 19   LEU A CD1 
152  C  CD2 . LEU A 20  ? 0.2405 0.2193 0.2195 0.0517  0.0442  -0.0049 19   LEU A CD2 
153  N  N   . LEU A 21  ? 0.3069 0.2083 0.1684 0.0788  0.0267  0.0112  20   LEU A N   
154  C  CA  . LEU A 21  ? 0.3208 0.1922 0.1900 0.1037  -0.0114 -0.0106 20   LEU A CA  
155  C  C   . LEU A 21  ? 0.3132 0.2163 0.2106 0.0623  -0.0108 -0.0018 20   LEU A C   
156  O  O   . LEU A 21  ? 0.2991 0.2560 0.2186 0.0630  -0.0103 -0.0178 20   LEU A O   
157  C  CB  . LEU A 21  ? 0.3118 0.2005 0.1942 0.1222  0.0091  0.0066  20   LEU A CB  
158  C  CG  . LEU A 21  ? 0.4121 0.1986 0.2315 0.1113  0.0175  0.0031  20   LEU A CG  
159  C  CD1 . LEU A 21  ? 0.3752 0.2429 0.2351 0.1101  0.0719  -0.0153 20   LEU A CD1 
160  C  CD2 . LEU A 21  ? 0.4240 0.1648 0.2272 0.0586  0.0087  0.0021  20   LEU A CD2 
161  N  N   . ASN A 22  ? 0.3374 0.2016 0.2239 0.0466  -0.0006 0.0278  21   ASN A N   
162  C  CA  . ASN A 22  ? 0.4133 0.2130 0.2203 0.0623  0.0080  0.0644  21   ASN A CA  
163  C  C   . ASN A 22  ? 0.3436 0.2174 0.2183 0.1043  0.0354  0.0657  21   ASN A C   
164  O  O   . ASN A 22  ? 0.4749 0.2398 0.2452 0.1018  0.0243  0.0367  21   ASN A O   
165  C  CB  . ASN A 22  ? 0.5241 0.2253 0.2200 0.0573  0.0017  0.0847  21   ASN A CB  
166  C  CG  . ASN A 22  ? 0.6937 0.2703 0.2378 0.0710  -0.0091 0.0534  21   ASN A CG  
167  O  OD1 . ASN A 22  ? 0.7785 0.2957 0.2399 0.0446  -0.0077 0.0509  21   ASN A OD1 
168  N  ND2 . ASN A 22  ? 0.7554 0.2797 0.2476 0.0876  -0.0196 0.0507  21   ASN A ND2 
169  N  N   . THR A 23  ? 0.3625 0.2127 0.2286 0.0925  0.0444  0.0495  22   THR A N   
170  C  CA  . THR A 23  ? 0.3132 0.2320 0.2334 0.0929  0.0356  0.0346  22   THR A CA  
171  C  C   . THR A 23  ? 0.3196 0.2469 0.2053 0.0317  -0.0282 0.0153  22   THR A C   
172  O  O   . THR A 23  ? 0.3493 0.2402 0.1989 0.0533  -0.0011 0.0046  22   THR A O   
173  C  CB  . THR A 23  ? 0.3387 0.2554 0.2665 0.0975  0.0409  0.0503  22   THR A CB  
174  O  OG1 . THR A 23  ? 0.4289 0.2954 0.2852 0.0821  0.0633  0.0414  22   THR A OG1 
175  C  CG2 . THR A 23  ? 0.2929 0.2484 0.2705 0.1519  0.0492  0.0664  22   THR A CG2 
176  N  N   . ASP A 24  ? 0.3578 0.2492 0.2333 0.0209  -0.0454 0.0340  23   ASP A N   
177  C  CA  . ASP A 24  ? 0.3618 0.2699 0.2272 0.0045  -0.0986 0.0235  23   ASP A CA  
178  C  C   . ASP A 24  ? 0.3218 0.2299 0.1822 0.0083  -0.0418 0.0417  23   ASP A C   
179  O  O   . ASP A 24  ? 0.2982 0.2387 0.1773 -0.0427 -0.0168 0.0215  23   ASP A O   
180  C  CB  . ASP A 24  ? 0.5649 0.3296 0.2899 0.0309  -0.0992 0.0300  23   ASP A CB  
181  C  CG  . ASP A 24  ? 0.8047 0.4150 0.3600 0.0432  -0.1196 0.0165  23   ASP A CG  
182  O  OD1 . ASP A 24  ? 0.8554 0.4461 0.4055 0.0975  -0.1203 0.0178  23   ASP A OD1 
183  O  OD2 . ASP A 24  ? 0.9355 0.4723 0.4096 0.0320  -0.0711 0.0100  23   ASP A OD2 
184  N  N   . LYS A 25  ? 0.2883 0.2267 0.1645 0.0326  -0.0462 0.0166  24   LYS A N   
185  C  CA  . LYS A 25  ? 0.2429 0.2019 0.1524 0.0138  -0.0473 0.0230  24   LYS A CA  
186  C  C   . LYS A 25  ? 0.2707 0.2109 0.1671 0.0298  0.0031  0.0343  24   LYS A C   
187  O  O   . LYS A 25  ? 0.2758 0.2001 0.1672 0.0312  0.0209  0.0476  24   LYS A O   
188  C  CB  . LYS A 25  ? 0.2317 0.1963 0.1691 0.0281  -0.0419 0.0270  24   LYS A CB  
189  C  CG  . LYS A 25  ? 0.2993 0.1890 0.1928 -0.0028 -0.0740 0.0094  24   LYS A CG  
190  C  CD  . LYS A 25  ? 0.3116 0.2149 0.2181 0.0134  -0.1055 -0.0371 24   LYS A CD  
191  C  CE  . LYS A 25  ? 0.2734 0.2406 0.2413 0.0117  -0.0899 -0.0368 24   LYS A CE  
192  N  NZ  . LYS A 25  ? 0.3519 0.2567 0.2669 -0.0021 -0.1389 -0.0510 24   LYS A NZ  
193  N  N   . PRO A 26  ? 0.2214 0.1866 0.1672 0.0660  0.0097  0.0203  25   PRO A N   
194  C  CA  . PRO A 26  ? 0.2290 0.1741 0.1571 0.0531  -0.0363 0.0224  25   PRO A CA  
195  C  C   . PRO A 26  ? 0.2627 0.1510 0.1799 0.1050  0.0024  0.0295  25   PRO A C   
196  O  O   . PRO A 26  ? 0.2739 0.1847 0.1710 0.0904  0.0068  0.0449  25   PRO A O   
197  C  CB  . PRO A 26  ? 0.1992 0.2034 0.1534 0.0123  0.0121  0.0025  25   PRO A CB  
198  C  CG  . PRO A 26  ? 0.2256 0.1889 0.1480 0.0678  -0.0002 0.0039  25   PRO A CG  
199  C  CD  . PRO A 26  ? 0.1944 0.1892 0.1776 0.0796  0.0424  0.0092  25   PRO A CD  
200  N  N   . VAL A 27  ? 0.2617 0.1375 0.1948 0.0685  0.0004  0.0233  26   VAL A N   
201  C  CA  . VAL A 27  ? 0.1792 0.1373 0.1992 0.0832  0.0478  0.0052  26   VAL A CA  
202  C  C   . VAL A 27  ? 0.2590 0.1642 0.1845 0.1149  0.0241  0.0294  26   VAL A C   
203  O  O   . VAL A 27  ? 0.2478 0.1474 0.1855 0.0478  0.0278  0.0525  26   VAL A O   
204  C  CB  . VAL A 27  ? 0.2407 0.1195 0.2288 0.0828  0.0260  0.0063  26   VAL A CB  
205  C  CG1 . VAL A 27  ? 0.2093 0.1182 0.2407 0.0689  0.0104  0.0078  26   VAL A CG1 
206  C  CG2 . VAL A 27  ? 0.2099 0.1620 0.2385 0.0639  0.0144  -0.0038 26   VAL A CG2 
207  N  N   . GLN A 28  ? 0.2421 0.1903 0.1616 0.1165  0.0234  -0.0111 27   GLN A N   
208  C  CA  . GLN A 28  ? 0.1721 0.2009 0.1703 0.1099  0.0044  -0.0111 27   GLN A CA  
209  C  C   . GLN A 28  ? 0.2477 0.2027 0.2054 0.0923  0.0199  -0.0125 27   GLN A C   
210  O  O   . GLN A 28  ? 0.2222 0.2207 0.1977 0.0674  0.0396  0.0026  27   GLN A O   
211  C  CB  . GLN A 28  ? 0.1985 0.2390 0.1449 0.1109  -0.0264 -0.0388 27   GLN A CB  
212  C  CG  . GLN A 28  ? 0.2227 0.2742 0.1218 0.0741  -0.0030 -0.0356 27   GLN A CG  
213  C  CD  . GLN A 28  ? 0.1825 0.2782 0.1452 0.1158  0.0301  -0.0088 27   GLN A CD  
214  O  OE1 . GLN A 28  ? 0.2401 0.2907 0.1757 0.1210  0.0186  -0.0152 27   GLN A OE1 
215  N  NE2 . GLN A 28  ? 0.2519 0.2874 0.1384 0.1104  0.0646  0.0072  27   GLN A NE2 
216  N  N   . ALA A 29  ? 0.2603 0.1526 0.1881 0.1086  0.0201  -0.0084 28   ALA A N   
217  C  CA  . ALA A 29  ? 0.2542 0.1557 0.1677 0.0489  0.0177  -0.0448 28   ALA A CA  
218  C  C   . ALA A 29  ? 0.3144 0.1904 0.1668 0.0562  0.0036  -0.0140 28   ALA A C   
219  O  O   . ALA A 29  ? 0.3255 0.2207 0.1862 0.0699  0.0183  -0.0007 28   ALA A O   
220  C  CB  . ALA A 29  ? 0.2229 0.1813 0.1956 0.0241  0.0090  -0.0406 28   ALA A CB  
221  N  N   . LEU A 30  ? 0.2343 0.1649 0.1330 0.1059  -0.0215 0.0110  29   LEU A N   
222  C  CA  . LEU A 30  ? 0.1946 0.2142 0.1693 0.1101  0.0025  0.0257  29   LEU A CA  
223  C  C   . LEU A 30  ? 0.2529 0.2052 0.1894 0.0952  0.0115  0.0100  29   LEU A C   
224  O  O   . LEU A 30  ? 0.2546 0.2005 0.1813 0.1274  0.0107  0.0157  29   LEU A O   
225  C  CB  . LEU A 30  ? 0.1989 0.2365 0.1648 0.0703  0.0104  0.0005  29   LEU A CB  
226  C  CG  . LEU A 30  ? 0.2110 0.2006 0.1277 0.0463  0.0285  -0.0147 29   LEU A CG  
227  C  CD1 . LEU A 30  ? 0.2193 0.1909 0.1423 0.0828  0.0508  0.0032  29   LEU A CD1 
228  C  CD2 . LEU A 30  ? 0.2702 0.1932 0.0975 0.0626  -0.0211 -0.0299 29   LEU A CD2 
229  N  N   . MET A 31  ? 0.2542 0.2242 0.2059 0.0936  0.0505  -0.0206 30   MET A N   
230  C  CA  . MET A 31  ? 0.2138 0.2051 0.1990 0.0649  0.0417  -0.0129 30   MET A CA  
231  C  C   . MET A 31  ? 0.2276 0.2286 0.2170 0.1036  0.0419  0.0178  30   MET A C   
232  O  O   . MET A 31  ? 0.2236 0.2483 0.2608 0.0848  0.0547  0.0528  30   MET A O   
233  C  CB  . MET A 31  ? 0.1366 0.1777 0.1894 0.0660  0.0125  -0.0165 30   MET A CB  
234  C  CG  . MET A 31  ? 0.1610 0.1999 0.1948 0.0637  0.0019  -0.0100 30   MET A CG  
235  S  SD  . MET A 31  ? 0.2416 0.2241 0.2038 0.0510  0.0164  0.0026  30   MET A SD  
236  C  CE  . MET A 31  ? 0.2214 0.2276 0.2067 0.0605  0.0622  0.0103  30   MET A CE  
237  N  N   . LYS A 32  ? 0.2165 0.2120 0.2049 0.1202  0.0587  0.0299  31   LYS A N   
238  C  CA  . LYS A 32  ? 0.2436 0.2552 0.2098 0.1296  0.0826  0.0327  31   LYS A CA  
239  C  C   . LYS A 32  ? 0.2658 0.2404 0.1967 0.1189  0.0894  0.0130  31   LYS A C   
240  O  O   . LYS A 32  ? 0.2456 0.2829 0.1790 0.1154  0.0770  0.0055  31   LYS A O   
241  C  CB  . LYS A 32  ? 0.2981 0.3190 0.2789 0.1800  0.0484  0.0563  31   LYS A CB  
242  C  CG  . LYS A 32  ? 0.4107 0.3956 0.3465 0.2032  0.0264  0.1052  31   LYS A CG  
243  C  CD  . LYS A 32  ? 0.5871 0.4373 0.4188 0.1982  0.0055  0.1293  31   LYS A CD  
244  C  CE  . LYS A 32  ? 0.7101 0.4692 0.4632 0.1619  -0.0154 0.1543  31   LYS A CE  
245  N  NZ  . LYS A 32  ? 0.7700 0.4885 0.4893 0.1335  -0.0235 0.1891  31   LYS A NZ  
246  N  N   . ILE A 33  ? 0.2736 0.1808 0.1760 0.1080  0.0482  0.0131  32   ILE A N   
247  C  CA  . ILE A 33  ? 0.2572 0.1800 0.1875 0.0411  0.0111  0.0186  32   ILE A CA  
248  C  C   . ILE A 33  ? 0.3213 0.1835 0.1936 0.0710  0.0243  0.0222  32   ILE A C   
249  O  O   . ILE A 33  ? 0.2516 0.1936 0.1903 0.1013  0.0612  0.0185  32   ILE A O   
250  C  CB  . ILE A 33  ? 0.2802 0.2012 0.1691 0.0408  0.0169  0.0134  32   ILE A CB  
251  C  CG1 . ILE A 33  ? 0.2543 0.1939 0.1694 -0.0042 0.0432  0.0429  32   ILE A CG1 
252  C  CG2 . ILE A 33  ? 0.2597 0.2402 0.1594 0.0395  0.0679  0.0095  32   ILE A CG2 
253  C  CD1 . ILE A 33  ? 0.2130 0.1816 0.1550 0.0530  0.0475  0.0480  32   ILE A CD1 
254  N  N   . ALA A 34  ? 0.3280 0.1654 0.2206 0.0858  0.0198  0.0379  33   ALA A N   
255  C  CA  . ALA A 34  ? 0.2853 0.1596 0.2166 0.1009  0.0570  0.0067  33   ALA A CA  
256  C  C   . ALA A 34  ? 0.3077 0.2385 0.2011 0.0994  0.0813  0.0280  33   ALA A C   
257  O  O   . ALA A 34  ? 0.2934 0.2515 0.2075 0.1041  0.0801  0.0586  33   ALA A O   
258  C  CB  . ALA A 34  ? 0.2702 0.1317 0.2387 0.0808  0.0713  -0.0030 33   ALA A CB  
259  N  N   . ASP A 35  ? 0.2134 0.2816 0.2064 0.1106  0.0663  0.0340  34   ASP A N   
260  C  CA  . ASP A 35  ? 0.2116 0.3365 0.2264 0.0902  0.0496  0.0445  34   ASP A CA  
261  C  C   . ASP A 35  ? 0.2184 0.3426 0.2273 0.0617  0.0412  0.0361  34   ASP A C   
262  O  O   . ASP A 35  ? 0.3310 0.3622 0.2658 0.0234  0.0854  0.0416  34   ASP A O   
263  C  CB  . ASP A 35  ? 0.3177 0.3604 0.2509 0.1038  0.0445  0.0707  34   ASP A CB  
264  C  CG  . ASP A 35  ? 0.3991 0.4155 0.3077 0.0735  0.0850  0.0807  34   ASP A CG  
265  O  OD1 . ASP A 35  ? 0.4612 0.4281 0.3403 0.0857  0.0925  0.0855  34   ASP A OD1 
266  O  OD2 . ASP A 35  ? 0.4615 0.4709 0.3429 0.0288  0.1332  0.0497  34   ASP A OD2 
267  N  N   . GLU A 36  ? 0.2771 0.3129 0.2339 0.0563  0.0279  0.0226  35   GLU A N   
268  C  CA  . GLU A 36  ? 0.2622 0.3119 0.2902 0.0533  0.0683  0.0028  35   GLU A CA  
269  C  C   . GLU A 36  ? 0.2379 0.3314 0.2748 0.0819  0.1198  0.0179  35   GLU A C   
270  O  O   . GLU A 36  ? 0.2793 0.3871 0.3011 0.1074  0.1328  0.0062  35   GLU A O   
271  C  CB  . GLU A 36  ? 0.3845 0.3086 0.3412 0.1253  0.0624  -0.0163 35   GLU A CB  
272  C  CG  . GLU A 36  ? 0.6003 0.2981 0.3904 0.1551  0.0480  -0.0218 35   GLU A CG  
273  C  CD  . GLU A 36  ? 0.8487 0.3326 0.4448 0.1277  0.0417  -0.0164 35   GLU A CD  
274  O  OE1 . GLU A 36  ? 0.8946 0.3296 0.4434 0.0846  0.1302  -0.0099 35   GLU A OE1 
275  O  OE2 . GLU A 36  ? 0.9358 0.3545 0.4831 0.1616  -0.0090 0.0011  35   GLU A OE2 
276  N  N   . LEU A 37  ? 0.1645 0.3041 0.2581 0.0624  0.0529  0.0331  36   LEU A N   
277  C  CA  . LEU A 37  ? 0.2694 0.2656 0.2307 0.0846  0.0265  0.0201  36   LEU A CA  
278  C  C   . LEU A 37  ? 0.2956 0.2490 0.2174 0.0752  0.0698  0.0239  36   LEU A C   
279  O  O   . LEU A 37  ? 0.3303 0.2294 0.2273 0.0888  0.0584  0.0206  36   LEU A O   
280  C  CB  . LEU A 37  ? 0.2557 0.2456 0.2278 0.0863  0.0553  0.0000  36   LEU A CB  
281  C  CG  . LEU A 37  ? 0.3175 0.2536 0.2229 0.0859  0.0912  -0.0101 36   LEU A CG  
282  C  CD1 . LEU A 37  ? 0.3665 0.2369 0.2042 0.0310  0.0667  0.0228  36   LEU A CD1 
283  C  CD2 . LEU A 37  ? 0.3430 0.2560 0.2328 0.0998  0.0640  0.0002  36   LEU A CD2 
284  N  N   . GLY A 38  ? 0.2564 0.2484 0.1838 0.0853  0.0799  0.0110  37   GLY A N   
285  C  CA  . GLY A 38  ? 0.2937 0.2265 0.1858 0.0919  0.0613  0.0461  37   GLY A CA  
286  C  C   . GLY A 38  ? 0.2884 0.2183 0.1978 0.1297  0.0188  0.0449  37   GLY A C   
287  O  O   . GLY A 38  ? 0.2704 0.2308 0.2247 0.1003  0.0556  0.0424  37   GLY A O   
288  N  N   . GLU A 39  ? 0.2469 0.1877 0.2034 0.1219  0.0511  0.0378  38   GLU A N   
289  C  CA  . GLU A 39  ? 0.2440 0.2202 0.1847 0.1321  0.0542  0.0588  38   GLU A CA  
290  C  C   . GLU A 39  ? 0.2595 0.2059 0.1692 0.1074  0.0663  0.0339  38   GLU A C   
291  O  O   . GLU A 39  ? 0.2278 0.1816 0.1695 0.0714  0.0750  0.0160  38   GLU A O   
292  C  CB  . GLU A 39  ? 0.2800 0.2501 0.1802 0.1214  0.0626  0.0764  38   GLU A CB  
293  C  CG  . GLU A 39  ? 0.3272 0.2779 0.1704 0.0898  0.1054  0.0704  38   GLU A CG  
294  C  CD  . GLU A 39  ? 0.4356 0.3062 0.1680 0.0936  0.0751  0.0469  38   GLU A CD  
295  O  OE1 . GLU A 39  ? 0.3620 0.2877 0.1741 0.0660  0.0947  0.0317  38   GLU A OE1 
296  O  OE2 . GLU A 39  ? 0.5194 0.3277 0.1585 0.1103  0.0597  0.0407  38   GLU A OE2 
297  N  N   . ILE A 40  ? 0.2500 0.2214 0.1391 0.0510  0.0727  0.0380  39   ILE A N   
298  C  CA  . ILE A 40  ? 0.1728 0.2266 0.1354 0.0843  0.0198  0.0339  39   ILE A CA  
299  C  C   . ILE A 40  ? 0.2802 0.2265 0.1502 0.0386  0.0679  0.0268  39   ILE A C   
300  O  O   . ILE A 40  ? 0.2961 0.2378 0.1931 0.0315  0.0776  0.0041  39   ILE A O   
301  C  CB  . ILE A 40  ? 0.1859 0.2573 0.1398 0.0488  0.0288  -0.0097 39   ILE A CB  
302  C  CG1 . ILE A 40  ? 0.2872 0.2115 0.1317 -0.0150 -0.0379 0.0198  39   ILE A CG1 
303  C  CG2 . ILE A 40  ? 0.3058 0.2692 0.1627 0.0538  0.0270  0.0031  39   ILE A CG2 
304  C  CD1 . ILE A 40  ? 0.3493 0.1961 0.1245 0.0262  -0.0032 0.0278  39   ILE A CD1 
305  N  N   . PHE A 41  ? 0.2636 0.2008 0.1063 0.0753  0.0514  0.0124  40   PHE A N   
306  C  CA  . PHE A 41  ? 0.2781 0.1740 0.1351 0.0537  0.0273  0.0115  40   PHE A CA  
307  C  C   . PHE A 41  ? 0.2520 0.1728 0.1725 0.0759  0.0497  0.0039  40   PHE A C   
308  O  O   . PHE A 41  ? 0.2020 0.1775 0.1918 0.0748  0.0395  -0.0115 40   PHE A O   
309  C  CB  . PHE A 41  ? 0.2449 0.2208 0.1385 0.0662  0.0047  -0.0052 40   PHE A CB  
310  C  CG  . PHE A 41  ? 0.2430 0.2009 0.1305 0.0571  0.0589  -0.0083 40   PHE A CG  
311  C  CD1 . PHE A 41  ? 0.2876 0.2110 0.1421 0.1074  0.0285  0.0224  40   PHE A CD1 
312  C  CD2 . PHE A 41  ? 0.2675 0.1857 0.1453 0.0383  0.0971  -0.0155 40   PHE A CD2 
313  C  CE1 . PHE A 41  ? 0.2354 0.2172 0.1434 0.0402  0.0412  0.0217  40   PHE A CE1 
314  C  CE2 . PHE A 41  ? 0.2312 0.1512 0.1500 0.0520  0.0767  -0.0264 40   PHE A CE2 
315  C  CZ  . PHE A 41  ? 0.2286 0.2087 0.1575 0.0143  -0.0017 0.0016  40   PHE A CZ  
316  N  N   . LYS A 42  ? 0.3027 0.1638 0.2027 0.0391  0.0401  0.0244  41   LYS A N   
317  C  CA  . LYS A 42  ? 0.3215 0.1816 0.1977 0.0367  0.0033  0.0224  41   LYS A CA  
318  C  C   . LYS A 42  ? 0.2938 0.1685 0.1611 0.0544  0.0571  0.0294  41   LYS A C   
319  O  O   . LYS A 42  ? 0.3815 0.1679 0.1621 0.0694  0.0912  -0.0093 41   LYS A O   
320  C  CB  . LYS A 42  ? 0.3885 0.2000 0.2208 0.0178  0.0073  0.0248  41   LYS A CB  
321  C  CG  . LYS A 42  ? 0.4137 0.2308 0.2666 -0.0260 -0.0041 -0.0078 41   LYS A CG  
322  C  CD  . LYS A 42  ? 0.5591 0.2630 0.2963 -0.1105 0.0218  -0.0320 41   LYS A CD  
323  C  CE  . LYS A 42  ? 0.6964 0.3143 0.3269 -0.0861 0.0021  -0.0422 41   LYS A CE  
324  N  NZ  . LYS A 42  ? 0.7509 0.3591 0.3536 -0.0940 -0.0373 -0.0450 41   LYS A NZ  
325  N  N   . PHE A 43  ? 0.2726 0.1745 0.1675 0.0327  0.0677  0.0188  42   PHE A N   
326  C  CA  . PHE A 43  ? 0.2581 0.1728 0.1850 0.0257  0.1125  0.0182  42   PHE A CA  
327  C  C   . PHE A 43  ? 0.2010 0.1619 0.2261 0.0902  0.0777  0.0311  42   PHE A C   
328  O  O   . PHE A 43  ? 0.2516 0.1694 0.2512 0.0987  0.1033  0.0713  42   PHE A O   
329  C  CB  . PHE A 43  ? 0.3265 0.1974 0.1555 0.0543  0.0801  0.0061  42   PHE A CB  
330  C  CG  . PHE A 43  ? 0.3992 0.1961 0.1749 0.0926  0.0635  0.0117  42   PHE A CG  
331  C  CD1 . PHE A 43  ? 0.4116 0.2032 0.1780 0.0956  0.0855  0.0629  42   PHE A CD1 
332  C  CD2 . PHE A 43  ? 0.4411 0.1724 0.1958 0.0818  0.0230  0.0108  42   PHE A CD2 
333  C  CE1 . PHE A 43  ? 0.4499 0.2125 0.2030 0.1138  0.0693  0.0493  42   PHE A CE1 
334  C  CE2 . PHE A 43  ? 0.4340 0.1679 0.2180 0.1162  0.0212  0.0290  42   PHE A CE2 
335  C  CZ  . PHE A 43  ? 0.4585 0.1947 0.2007 0.1387  0.0256  0.0303  42   PHE A CZ  
336  N  N   . GLU A 44  ? 0.3064 0.1809 0.2349 0.0791  0.0915  0.0314  43   GLU A N   
337  C  CA  . GLU A 44  ? 0.2674 0.2214 0.2592 0.0747  0.0761  0.0297  43   GLU A CA  
338  C  C   . GLU A 44  ? 0.2484 0.2135 0.2710 0.0557  0.0585  0.0298  43   GLU A C   
339  O  O   . GLU A 44  ? 0.3120 0.1936 0.2619 0.0036  0.0384  0.0333  43   GLU A O   
340  C  CB  . GLU A 44  ? 0.3295 0.2926 0.2825 0.0755  0.0109  0.0302  43   GLU A CB  
341  C  CG  . GLU A 44  ? 0.3474 0.3518 0.3260 0.1213  -0.0217 -0.0167 43   GLU A CG  
342  C  CD  . GLU A 44  ? 0.4312 0.3986 0.3802 0.1152  -0.0506 -0.0445 43   GLU A CD  
343  O  OE1 . GLU A 44  ? 0.4218 0.4060 0.3768 0.0665  0.0409  -0.0275 43   GLU A OE1 
344  O  OE2 . GLU A 44  ? 0.5015 0.4252 0.4324 0.1322  -0.0709 -0.0857 43   GLU A OE2 
345  N  N   . ALA A 45  ? 0.1937 0.2034 0.2945 0.0547  0.0770  0.0442  44   ALA A N   
346  C  CA  . ALA A 45  ? 0.2890 0.2436 0.3038 0.0218  0.1043  0.0354  44   ALA A CA  
347  C  C   . ALA A 45  ? 0.3398 0.2304 0.3495 0.0646  0.1192  0.0655  44   ALA A C   
348  O  O   . ALA A 45  ? 0.3782 0.2257 0.3687 0.0876  0.1122  0.0763  44   ALA A O   
349  C  CB  . ALA A 45  ? 0.4103 0.2620 0.2981 -0.0033 0.0711  0.0202  44   ALA A CB  
350  N  N   . PRO A 46  ? 0.3291 0.2411 0.4049 0.1183  0.1033  0.0644  45   PRO A N   
351  C  CA  . PRO A 46  ? 0.3372 0.2600 0.4350 0.0973  0.1138  0.0851  45   PRO A CA  
352  C  C   . PRO A 46  ? 0.3579 0.3168 0.4735 0.0440  0.1085  0.0678  45   PRO A C   
353  O  O   . PRO A 46  ? 0.3108 0.3284 0.4851 0.0614  0.1273  0.0397  45   PRO A O   
354  C  CB  . PRO A 46  ? 0.3036 0.2727 0.3990 0.1470  0.0753  0.1055  45   PRO A CB  
355  C  CG  . PRO A 46  ? 0.2909 0.2493 0.3887 0.1341  0.1077  0.0899  45   PRO A CG  
356  C  CD  . PRO A 46  ? 0.3138 0.2282 0.3977 0.0773  0.1276  0.1111  45   PRO A CD  
357  N  N   . GLY A 47  ? 0.4324 0.3299 0.5068 0.0391  0.0688  0.0919  46   GLY A N   
358  C  CA  . GLY A 47  ? 0.3981 0.3289 0.5187 0.0145  0.0419  0.0939  46   GLY A CA  
359  C  C   . GLY A 47  ? 0.3786 0.3125 0.4990 0.0276  0.0416  0.1082  46   GLY A C   
360  O  O   . GLY A 47  ? 0.4636 0.3418 0.5318 0.0327  0.0531  0.1430  46   GLY A O   
361  N  N   . ARG A 48  ? 0.3150 0.2933 0.4428 0.0069  0.0474  0.0809  47   ARG A N   
362  C  CA  . ARG A 48  ? 0.2805 0.2844 0.4008 0.0113  0.0608  0.0259  47   ARG A CA  
363  C  C   . ARG A 48  ? 0.3694 0.2552 0.3691 0.0325  0.0551  0.0120  47   ARG A C   
364  O  O   . ARG A 48  ? 0.3593 0.2402 0.3690 0.0650  0.0804  -0.0102 47   ARG A O   
365  C  CB  . ARG A 48  ? 0.3891 0.3002 0.3801 -0.0190 0.0758  -0.0325 47   ARG A CB  
366  C  CG  . ARG A 48  ? 0.5072 0.3416 0.3648 -0.0323 0.0874  -0.0561 47   ARG A CG  
367  C  CD  . ARG A 48  ? 0.4651 0.3267 0.2948 -0.0354 0.0323  -0.0889 47   ARG A CD  
368  N  NE  . ARG A 48  ? 0.3972 0.3125 0.2505 -0.0211 -0.0264 -0.0820 47   ARG A NE  
369  C  CZ  . ARG A 48  ? 0.5123 0.3007 0.2024 -0.0214 0.0108  -0.0285 47   ARG A CZ  
370  N  NH1 . ARG A 48  ? 0.5455 0.3297 0.2164 -0.0125 0.0738  -0.0176 47   ARG A NH1 
371  N  NH2 . ARG A 48  ? 0.5013 0.2595 0.1571 -0.0261 0.0053  0.0172  47   ARG A NH2 
372  N  N   . VAL A 49  ? 0.2970 0.2108 0.3318 0.0291  -0.0063 0.0151  48   VAL A N   
373  C  CA  . VAL A 49  ? 0.3813 0.1828 0.2919 -0.0325 0.0487  -0.0044 48   VAL A CA  
374  C  C   . VAL A 49  ? 0.3826 0.1753 0.2748 -0.0457 0.0384  -0.0220 48   VAL A C   
375  O  O   . VAL A 49  ? 0.4029 0.1810 0.2916 0.0081  0.0730  -0.0280 48   VAL A O   
376  C  CB  . VAL A 49  ? 0.3980 0.1984 0.2830 -0.0814 0.0876  -0.0425 48   VAL A CB  
377  C  CG1 . VAL A 49  ? 0.3420 0.1953 0.2753 -0.1121 0.0835  -0.0624 48   VAL A CG1 
378  C  CG2 . VAL A 49  ? 0.5012 0.2459 0.3102 -0.0577 0.0710  -0.0011 48   VAL A CG2 
379  N  N   . THR A 50  ? 0.2914 0.1318 0.2112 -0.0689 -0.0175 -0.0263 49   THR A N   
380  C  CA  . THR A 50  ? 0.2103 0.1565 0.1803 -0.0233 0.0220  -0.0033 49   THR A CA  
381  C  C   . THR A 50  ? 0.2676 0.1585 0.1940 0.0633  0.0331  0.0181  49   THR A C   
382  O  O   . THR A 50  ? 0.3399 0.1871 0.2243 0.0759  0.0564  0.0444  49   THR A O   
383  C  CB  . THR A 50  ? 0.2793 0.1785 0.1589 0.0555  -0.0126 -0.0170 49   THR A CB  
384  O  OG1 . THR A 50  ? 0.3518 0.1886 0.1333 0.1057  -0.0168 -0.0295 49   THR A OG1 
385  C  CG2 . THR A 50  ? 0.2386 0.2233 0.1586 -0.0037 -0.0285 -0.0163 49   THR A CG2 
386  N  N   . ARG A 51  ? 0.2340 0.1232 0.1769 0.0877  0.0140  0.0270  50   ARG A N   
387  C  CA  . ARG A 51  ? 0.2243 0.1872 0.1478 0.0484  0.0188  0.0067  50   ARG A CA  
388  C  C   . ARG A 51  ? 0.2420 0.2024 0.1613 0.0245  0.0247  -0.0058 50   ARG A C   
389  O  O   . ARG A 51  ? 0.2017 0.2277 0.1957 0.0164  0.0018  -0.0314 50   ARG A O   
390  C  CB  . ARG A 51  ? 0.3552 0.1802 0.1657 0.0347  0.0118  -0.0130 50   ARG A CB  
391  C  CG  . ARG A 51  ? 0.3737 0.1971 0.1723 0.0410  -0.0013 -0.0525 50   ARG A CG  
392  C  CD  . ARG A 51  ? 0.3666 0.2016 0.1994 0.0135  -0.0374 -0.0597 50   ARG A CD  
393  N  NE  . ARG A 51  ? 0.3514 0.2150 0.2353 0.0875  -0.0196 -0.0638 50   ARG A NE  
394  C  CZ  . ARG A 51  ? 0.3715 0.1919 0.2268 0.0614  -0.0497 -0.0445 50   ARG A CZ  
395  N  NH1 . ARG A 51  ? 0.3701 0.1943 0.2176 0.0720  -0.0841 -0.0563 50   ARG A NH1 
396  N  NH2 . ARG A 51  ? 0.3597 0.1562 0.2348 0.0358  -0.0491 -0.0215 50   ARG A NH2 
397  N  N   . TYR A 52  ? 0.2194 0.1849 0.1428 0.0369  0.0210  0.0030  51   TYR A N   
398  C  CA  . TYR A 52  ? 0.2161 0.1363 0.1312 0.0543  -0.0071 0.0343  51   TYR A CA  
399  C  C   . TYR A 52  ? 0.2603 0.1441 0.1425 0.0454  0.0359  0.0227  51   TYR A C   
400  O  O   . TYR A 52  ? 0.3025 0.1690 0.1463 0.0186  0.0453  0.0330  51   TYR A O   
401  C  CB  . TYR A 52  ? 0.1666 0.1012 0.1381 0.0622  0.0016  0.0363  51   TYR A CB  
402  C  CG  . TYR A 52  ? 0.2088 0.1419 0.1300 0.0711  0.0473  0.0233  51   TYR A CG  
403  C  CD1 . TYR A 52  ? 0.2243 0.1592 0.1351 0.0230  0.0389  0.0207  51   TYR A CD1 
404  C  CD2 . TYR A 52  ? 0.2582 0.1623 0.1161 0.0496  0.0296  0.0166  51   TYR A CD2 
405  C  CE1 . TYR A 52  ? 0.3020 0.1677 0.1141 0.0909  0.0441  0.0192  51   TYR A CE1 
406  C  CE2 . TYR A 52  ? 0.2371 0.1626 0.1239 0.0529  0.0703  0.0252  51   TYR A CE2 
407  C  CZ  . TYR A 52  ? 0.2942 0.1808 0.1315 0.0869  0.0559  0.0332  51   TYR A CZ  
408  O  OH  . TYR A 52  ? 0.2060 0.1967 0.1583 0.0763  0.0426  0.0349  51   TYR A OH  
409  N  N   . LEU A 53  ? 0.2913 0.1106 0.1463 0.0772  0.0365  0.0099  52   LEU A N   
410  C  CA  . LEU A 53  ? 0.2695 0.1447 0.1365 0.0660  0.0355  0.0185  52   LEU A CA  
411  C  C   . LEU A 53  ? 0.1643 0.1706 0.1253 0.0706  0.0285  0.0272  52   LEU A C   
412  O  O   . LEU A 53  ? 0.2316 0.1768 0.1294 0.0486  0.0229  0.0262  52   LEU A O   
413  C  CB  . LEU A 53  ? 0.1969 0.2022 0.1674 0.0546  -0.0047 0.0061  52   LEU A CB  
414  C  CG  . LEU A 53  ? 0.2182 0.2233 0.1824 0.0691  -0.0051 0.0058  52   LEU A CG  
415  C  CD1 . LEU A 53  ? 0.2113 0.2208 0.1846 0.1243  -0.0137 0.0199  52   LEU A CD1 
416  C  CD2 . LEU A 53  ? 0.2782 0.2260 0.1726 0.0393  0.0188  -0.0103 52   LEU A CD2 
417  N  N   . SER A 54  ? 0.1719 0.1885 0.1409 0.0089  0.0116  0.0302  53   SER A N   
418  C  CA  . SER A 54  ? 0.1515 0.2074 0.1835 0.0497  -0.0049 0.0713  53   SER A CA  
419  C  C   . SER A 54  ? 0.1972 0.1826 0.1645 0.0435  0.0376  0.0598  53   SER A C   
420  O  O   . SER A 54  ? 0.2619 0.1897 0.1653 0.0090  -0.0178 0.0301  53   SER A O   
421  C  CB  . SER A 54  ? 0.2167 0.2295 0.1983 0.0648  -0.0382 0.0954  53   SER A CB  
422  O  OG  . SER A 54  ? 0.3048 0.2970 0.2494 0.1215  -0.0114 0.0316  53   SER A OG  
423  N  N   . SER A 55  ? 0.2478 0.1675 0.1580 0.0868  0.0684  0.0511  54   SER A N   
424  C  CA  . SER A 55  ? 0.2543 0.2025 0.1517 0.0693  0.0800  0.0427  54   SER A CA  
425  C  C   . SER A 55  ? 0.2205 0.1854 0.1577 0.0706  0.0714  0.0254  54   SER A C   
426  O  O   . SER A 55  ? 0.1959 0.2199 0.1430 0.0781  0.0721  0.0329  54   SER A O   
427  C  CB  . SER A 55  ? 0.2803 0.2382 0.1485 0.0847  0.0403  0.0311  54   SER A CB  
428  O  OG  . SER A 55  ? 0.2534 0.2232 0.1516 0.1132  0.0207  0.0285  54   SER A OG  
429  N  N   . GLN A 56  ? 0.2109 0.1692 0.1385 0.0855  0.0517  0.0128  55   GLN A N   
430  C  CA  . GLN A 56  ? 0.2264 0.1558 0.1517 0.0350  0.0205  0.0244  55   GLN A CA  
431  C  C   . GLN A 56  ? 0.1664 0.1852 0.1578 0.0003  0.0123  0.0268  55   GLN A C   
432  O  O   . GLN A 56  ? 0.1477 0.2039 0.1623 0.0151  0.0053  0.0347  55   GLN A O   
433  C  CB  . GLN A 56  ? 0.2268 0.1570 0.1673 0.0548  0.0217  0.0015  55   GLN A CB  
434  C  CG  . GLN A 56  ? 0.2100 0.1422 0.1643 0.0676  0.0180  0.0488  55   GLN A CG  
435  C  CD  . GLN A 56  ? 0.2100 0.1336 0.1642 0.0595  0.0136  0.0164  55   GLN A CD  
436  O  OE1 . GLN A 56  ? 0.3119 0.1320 0.1647 0.0338  0.0475  0.0097  55   GLN A OE1 
437  N  NE2 . GLN A 56  ? 0.2007 0.1472 0.1777 0.0282  -0.0391 0.0210  55   GLN A NE2 
438  N  N   . ARG A 57  ? 0.2247 0.1939 0.1663 0.0105  0.0051  0.0335  56   ARG A N   
439  C  CA  . ARG A 57  ? 0.1870 0.2347 0.1642 0.0046  0.0179  0.0077  56   ARG A CA  
440  C  C   . ARG A 57  ? 0.1789 0.2079 0.1784 0.0492  0.0276  0.0184  56   ARG A C   
441  O  O   . ARG A 57  ? 0.2282 0.2077 0.1996 0.0497  -0.0081 0.0187  56   ARG A O   
442  C  CB  . ARG A 57  ? 0.2411 0.3235 0.1261 -0.0134 0.0441  -0.0300 56   ARG A CB  
443  C  CG  . ARG A 57  ? 0.3817 0.3557 0.1996 0.0102  0.1076  -0.0741 56   ARG A CG  
444  C  CD  . ARG A 57  ? 0.5035 0.3557 0.2270 0.1094  0.1103  -0.0597 56   ARG A CD  
445  N  NE  . ARG A 57  ? 0.5246 0.3645 0.2503 0.1311  0.0985  -0.0757 56   ARG A NE  
446  C  CZ  . ARG A 57  ? 0.5027 0.4193 0.2567 0.1395  0.0454  -0.0365 56   ARG A CZ  
447  N  NH1 . ARG A 57  ? 0.4296 0.4431 0.2875 0.1493  0.0068  -0.0226 56   ARG A NH1 
448  N  NH2 . ARG A 57  ? 0.4727 0.4511 0.2463 0.1589  0.0161  -0.0407 56   ARG A NH2 
449  N  N   . LEU A 58  ? 0.2043 0.1890 0.1688 0.0571  0.0749  0.0192  57   LEU A N   
450  C  CA  . LEU A 58  ? 0.2310 0.1774 0.1747 0.0600  0.0867  -0.0026 57   LEU A CA  
451  C  C   . LEU A 58  ? 0.2333 0.1865 0.1625 0.0564  0.0279  0.0137  57   LEU A C   
452  O  O   . LEU A 58  ? 0.2055 0.1743 0.1663 0.0700  -0.0030 0.0257  57   LEU A O   
453  C  CB  . LEU A 58  ? 0.2132 0.1653 0.1883 0.0802  0.0646  -0.0273 57   LEU A CB  
454  C  CG  . LEU A 58  ? 0.2727 0.1258 0.1702 0.0270  0.0401  -0.0574 57   LEU A CG  
455  C  CD1 . LEU A 58  ? 0.3489 0.1364 0.2038 0.0437  0.0658  -0.0453 57   LEU A CD1 
456  C  CD2 . LEU A 58  ? 0.3313 0.1440 0.1883 0.0026  -0.0175 -0.0792 57   LEU A CD2 
457  N  N   . ILE A 59  ? 0.1827 0.1878 0.1461 0.0199  0.0486  0.0202  58   ILE A N   
458  C  CA  . ILE A 59  ? 0.1950 0.1837 0.1316 0.0742  0.0326  0.0602  58   ILE A CA  
459  C  C   . ILE A 59  ? 0.1745 0.1949 0.1419 0.0403  0.0559  0.0329  58   ILE A C   
460  O  O   . ILE A 59  ? 0.2031 0.2005 0.1612 0.0664  0.0064  0.0278  58   ILE A O   
461  C  CB  . ILE A 59  ? 0.1419 0.1655 0.1334 0.0879  0.0157  0.0336  58   ILE A CB  
462  C  CG1 . ILE A 59  ? 0.2259 0.1637 0.1525 0.0842  -0.0107 0.0543  58   ILE A CG1 
463  C  CG2 . ILE A 59  ? 0.1878 0.1776 0.1304 0.0604  0.0481  -0.0245 58   ILE A CG2 
464  C  CD1 . ILE A 59  ? 0.2635 0.1615 0.1594 0.0727  -0.0177 0.0620  58   ILE A CD1 
465  N  N   . LYS A 60  ? 0.1721 0.2001 0.1447 0.0283  0.0258  0.0256  59   LYS A N   
466  C  CA  . LYS A 60  ? 0.1948 0.2043 0.1545 0.0203  0.0175  0.0026  59   LYS A CA  
467  C  C   . LYS A 60  ? 0.1697 0.2324 0.1563 0.0807  0.0059  -0.0214 59   LYS A C   
468  O  O   . LYS A 60  ? 0.2267 0.2775 0.1805 0.0598  -0.0436 -0.0285 59   LYS A O   
469  C  CB  . LYS A 60  ? 0.1700 0.1909 0.1442 -0.0015 0.0581  -0.0088 59   LYS A CB  
470  C  CG  . LYS A 60  ? 0.1800 0.2076 0.1559 0.0198  0.0675  0.0143  59   LYS A CG  
471  C  CD  . LYS A 60  ? 0.2436 0.2210 0.1749 -0.0166 0.0137  0.0525  59   LYS A CD  
472  C  CE  . LYS A 60  ? 0.2782 0.2357 0.2695 0.0193  0.0778  0.0736  59   LYS A CE  
473  N  NZ  . LYS A 60  ? 0.3541 0.2690 0.3139 -0.0020 0.0812  0.0574  59   LYS A NZ  
474  N  N   . GLU A 61  ? 0.2463 0.2047 0.1290 0.0641  0.0253  -0.0277 60   GLU A N   
475  C  CA  . GLU A 61  ? 0.2150 0.1995 0.1328 0.0680  0.0658  -0.0241 60   GLU A CA  
476  C  C   . GLU A 61  ? 0.1988 0.1835 0.1514 0.0889  0.0487  -0.0034 60   GLU A C   
477  O  O   . GLU A 61  ? 0.1996 0.1959 0.1829 0.1044  0.0320  0.0238  60   GLU A O   
478  C  CB  . GLU A 61  ? 0.1841 0.2501 0.1174 0.0813  0.0341  0.0014  60   GLU A CB  
479  C  CG  . GLU A 61  ? 0.2410 0.3107 0.1005 0.0408  0.0518  0.0074  60   GLU A CG  
480  C  CD  . GLU A 61  ? 0.3063 0.3929 0.1626 0.0106  0.0307  -0.0186 60   GLU A CD  
481  O  OE1 . GLU A 61  ? 0.3370 0.3769 0.1617 -0.0098 0.0121  -0.0444 60   GLU A OE1 
482  O  OE2 . GLU A 61  ? 0.3348 0.4577 0.1918 0.0140  0.0157  -0.0448 60   GLU A OE2 
483  N  N   . ALA A 62  ? 0.2285 0.1579 0.1502 0.0376  0.0476  -0.0003 61   ALA A N   
484  C  CA  . ALA A 62  ? 0.2270 0.1553 0.1490 0.0409  0.0646  0.0267  61   ALA A CA  
485  C  C   . ALA A 62  ? 0.2228 0.1519 0.1561 0.0367  0.0170  0.0178  61   ALA A C   
486  O  O   . ALA A 62  ? 0.3265 0.1692 0.1392 0.0686  0.0314  0.0223  61   ALA A O   
487  C  CB  . ALA A 62  ? 0.2536 0.1680 0.1664 0.0545  0.0891  0.0506  61   ALA A CB  
488  N  N   . CYS A 63  ? 0.2249 0.1320 0.1398 0.0388  -0.0375 -0.0046 62   CYS A N   
489  C  CA  . CYS A 63  ? 0.2068 0.1042 0.1592 0.0151  -0.0243 -0.0186 62   CYS A CA  
490  C  C   . CYS A 63  ? 0.1944 0.0934 0.1336 0.0106  0.0180  -0.0132 62   CYS A C   
491  O  O   . CYS A 63  ? 0.2168 0.1020 0.1481 0.0352  0.0115  0.0257  62   CYS A O   
492  C  CB  . CYS A 63  ? 0.2433 0.1024 0.1577 0.0298  -0.0121 0.0119  62   CYS A CB  
493  S  SG  . CYS A 63  ? 0.2064 0.1719 0.1729 -0.0074 -0.0016 0.0070  62   CYS A SG  
494  N  N   . ASP A 64  ? 0.2220 0.1342 0.1612 0.0074  -0.0426 -0.0074 63   ASP A N   
495  C  CA  . ASP A 64  ? 0.2358 0.2103 0.1359 0.0169  -0.0303 0.0075  63   ASP A CA  
496  C  C   . ASP A 64  ? 0.1838 0.2058 0.1380 0.0472  -0.0092 0.0128  63   ASP A C   
497  O  O   . ASP A 64  ? 0.2926 0.1783 0.1535 0.0348  0.0011  0.0084  63   ASP A O   
498  C  CB  . ASP A 64  ? 0.2621 0.2515 0.1329 0.0628  -0.0857 -0.0012 63   ASP A CB  
499  C  CG  . ASP A 64  ? 0.3024 0.3052 0.1539 0.0342  -0.0428 0.0443  63   ASP A CG  
500  O  OD1 . ASP A 64  ? 0.3189 0.2940 0.1732 0.0143  -0.0421 0.0772  63   ASP A OD1 
501  O  OD2 . ASP A 64  ? 0.3345 0.3693 0.1920 0.0171  -0.0117 0.0648  63   ASP A OD2 
502  N  N   . GLU A 65  ? 0.1507 0.2171 0.1044 0.0081  0.0144  0.0314  64   GLU A N   
503  C  CA  . GLU A 65  ? 0.1462 0.2277 0.1316 0.0249  0.0178  -0.0038 64   GLU A CA  
504  C  C   . GLU A 65  ? 0.2110 0.2437 0.1456 0.0363  0.0061  0.0201  64   GLU A C   
505  O  O   . GLU A 65  ? 0.2313 0.2591 0.1610 0.0133  -0.0157 0.0122  64   GLU A O   
506  C  CB  . GLU A 65  ? 0.2467 0.2346 0.1414 0.0337  0.0318  -0.0026 64   GLU A CB  
507  C  CG  . GLU A 65  ? 0.1966 0.2189 0.1716 0.0439  0.0163  -0.0222 64   GLU A CG  
508  C  CD  . GLU A 65  ? 0.2855 0.2332 0.1674 0.0343  0.0106  0.0128  64   GLU A CD  
509  O  OE1 . GLU A 65  ? 0.3837 0.2632 0.2010 0.0373  0.0642  0.0561  64   GLU A OE1 
510  O  OE2 . GLU A 65  ? 0.1987 0.2339 0.1576 0.0259  -0.0181 0.0155  64   GLU A OE2 
511  N  N   . SER A 66  ? 0.2303 0.2458 0.1239 0.0388  -0.0314 0.0554  65   SER A N   
512  C  CA  . SER A 66  ? 0.2671 0.2323 0.1470 0.0084  -0.0061 0.0556  65   SER A CA  
513  C  C   . SER A 66  ? 0.3169 0.1972 0.1741 -0.0232 -0.0136 0.0349  65   SER A C   
514  O  O   . SER A 66  ? 0.3663 0.2029 0.2372 -0.0323 -0.0256 0.0288  65   SER A O   
515  C  CB  . SER A 66  ? 0.2855 0.2575 0.1456 0.0023  0.0017  0.0573  65   SER A CB  
516  O  OG  . SER A 66  ? 0.3515 0.2527 0.1656 -0.0186 -0.0080 0.0396  65   SER A OG  
517  N  N   . ARG A 67  ? 0.2987 0.1834 0.1526 -0.0066 -0.0150 0.0319  66   ARG A N   
518  C  CA  . ARG A 67  ? 0.3251 0.1894 0.1411 0.0121  -0.0202 0.0146  66   ARG A CA  
519  C  C   . ARG A 67  ? 0.2779 0.1940 0.1501 0.0035  0.0107  -0.0002 66   ARG A C   
520  O  O   . ARG A 67  ? 0.3187 0.1949 0.1492 -0.0385 -0.0800 0.0105  66   ARG A O   
521  C  CB  . ARG A 67  ? 0.3374 0.2223 0.1355 0.0101  0.0362  0.0134  66   ARG A CB  
522  C  CG  . ARG A 67  ? 0.3103 0.2439 0.1929 -0.0070 0.0942  0.0427  66   ARG A CG  
523  C  CD  . ARG A 67  ? 0.3989 0.2559 0.1994 0.0391  0.1104  0.0195  66   ARG A CD  
524  N  NE  . ARG A 67  ? 0.4913 0.2415 0.2157 0.0137  0.0448  0.0369  66   ARG A NE  
525  C  CZ  . ARG A 67  ? 0.5565 0.2570 0.2000 -0.0459 -0.0250 0.0282  66   ARG A CZ  
526  N  NH1 . ARG A 67  ? 0.5211 0.2504 0.1611 -0.1250 -0.0559 0.0046  66   ARG A NH1 
527  N  NH2 . ARG A 67  ? 0.5727 0.3113 0.1848 0.0148  -0.0703 0.0138  66   ARG A NH2 
528  N  N   . PHE A 68  ? 0.2396 0.1960 0.1388 0.0551  -0.0027 0.0105  67   PHE A N   
529  C  CA  . PHE A 68  ? 0.1986 0.1969 0.1215 0.0453  0.0374  0.0314  67   PHE A CA  
530  C  C   . PHE A 68  ? 0.1903 0.1895 0.1229 0.0415  0.0132  0.0368  67   PHE A C   
531  O  O   . PHE A 68  ? 0.2181 0.1846 0.1551 0.0152  0.0371  0.0032  67   PHE A O   
532  C  CB  . PHE A 68  ? 0.1907 0.1980 0.1252 0.0809  0.0526  -0.0133 67   PHE A CB  
533  C  CG  . PHE A 68  ? 0.1996 0.2298 0.1504 0.0454  0.0510  0.0119  67   PHE A CG  
534  C  CD1 . PHE A 68  ? 0.2787 0.2133 0.1699 0.0665  0.0207  0.0096  67   PHE A CD1 
535  C  CD2 . PHE A 68  ? 0.2182 0.2710 0.1397 0.0560  0.0576  0.0117  67   PHE A CD2 
536  C  CE1 . PHE A 68  ? 0.3075 0.2190 0.1494 0.0623  0.0206  0.0237  67   PHE A CE1 
537  C  CE2 . PHE A 68  ? 0.2048 0.2564 0.1590 0.0771  0.0445  -0.0088 67   PHE A CE2 
538  C  CZ  . PHE A 68  ? 0.2773 0.2497 0.1727 0.0614  0.0167  0.0090  67   PHE A CZ  
539  N  N   . ASP A 69  ? 0.2007 0.1660 0.1082 0.0049  0.0251  0.0500  68   ASP A N   
540  C  CA  . ASP A 69  ? 0.2210 0.1765 0.1117 -0.0051 0.0202  0.0482  68   ASP A CA  
541  C  C   . ASP A 69  ? 0.2198 0.1638 0.1289 0.0018  0.0079  0.0269  68   ASP A C   
542  O  O   . ASP A 69  ? 0.1500 0.1836 0.1606 0.0179  0.0058  0.0106  68   ASP A O   
543  C  CB  . ASP A 69  ? 0.1840 0.2133 0.1455 0.0340  0.0598  -0.0036 68   ASP A CB  
544  C  CG  . ASP A 69  ? 0.1571 0.1946 0.1539 -0.0513 0.0172  -0.0104 68   ASP A CG  
545  O  OD1 . ASP A 69  ? 0.2224 0.1201 0.1742 0.0022  -0.0282 -0.0085 68   ASP A OD1 
546  O  OD2 . ASP A 69  ? 0.1708 0.2276 0.1477 0.0102  0.0258  -0.0352 68   ASP A OD2 
547  N  N   . LYS A 70  ? 0.2084 0.1406 0.0753 -0.0365 -0.0189 -0.0027 69   LYS A N   
548  C  CA  . LYS A 70  ? 0.1857 0.1278 0.0645 -0.0312 -0.0183 -0.0165 69   LYS A CA  
549  C  C   . LYS A 70  ? 0.1939 0.1268 0.1274 -0.0250 0.0191  -0.0240 69   LYS A C   
550  O  O   . LYS A 70  ? 0.2204 0.1507 0.1655 -0.0213 -0.0494 0.0002  69   LYS A O   
551  C  CB  . LYS A 70  ? 0.1248 0.1342 0.0987 -0.0156 0.0184  -0.0328 69   LYS A CB  
552  C  CG  . LYS A 70  ? 0.1566 0.1427 0.0847 -0.0064 -0.0199 -0.0142 69   LYS A CG  
553  C  CD  . LYS A 70  ? 0.2270 0.1645 0.0655 -0.0158 -0.0267 0.0176  69   LYS A CD  
554  C  CE  . LYS A 70  ? 0.1497 0.1664 0.0724 -0.0332 -0.0457 0.0142  69   LYS A CE  
555  N  NZ  . LYS A 70  ? 0.1232 0.1239 0.0943 -0.0247 -0.0359 0.0187  69   LYS A NZ  
556  N  N   . ASN A 71  ? 0.1935 0.0644 0.1278 0.0010  -0.0149 -0.0161 70   ASN A N   
557  C  CA  . ASN A 71  ? 0.2188 0.1043 0.1375 0.0228  -0.0059 -0.0177 70   ASN A CA  
558  C  C   . ASN A 71  ? 0.2523 0.1164 0.1350 0.0365  0.0114  -0.0096 70   ASN A C   
559  O  O   . ASN A 71  ? 0.2285 0.1302 0.1892 0.0242  0.0067  0.0255  70   ASN A O   
560  C  CB  . ASN A 71  ? 0.2237 0.0886 0.1440 0.0285  -0.0017 -0.0296 70   ASN A CB  
561  C  CG  . ASN A 71  ? 0.2552 0.1297 0.1789 0.0281  -0.0036 -0.0410 70   ASN A CG  
562  O  OD1 . ASN A 71  ? 0.2417 0.1731 0.2212 0.0006  -0.0266 -0.0517 70   ASN A OD1 
563  N  ND2 . ASN A 71  ? 0.3392 0.1098 0.1544 0.0646  0.0045  -0.0152 70   ASN A ND2 
564  N  N   . LEU A 72  ? 0.2670 0.1327 0.1067 0.0001  0.0250  0.0026  71   LEU A N   
565  C  CA  . LEU A 72  ? 0.2105 0.1251 0.1227 -0.0083 0.0500  0.0149  71   LEU A CA  
566  C  C   . LEU A 72  ? 0.1954 0.1282 0.1392 0.0020  -0.0036 0.0111  71   LEU A C   
567  O  O   . LEU A 72  ? 0.2888 0.1565 0.1555 -0.0424 -0.0274 0.0129  71   LEU A O   
568  C  CB  . LEU A 72  ? 0.2194 0.1283 0.1180 -0.0069 0.0390  -0.0153 71   LEU A CB  
569  C  CG  . LEU A 72  ? 0.2106 0.1380 0.1415 -0.0190 0.0493  -0.0204 71   LEU A CG  
570  C  CD1 . LEU A 72  ? 0.2406 0.1299 0.1640 -0.0687 0.0034  -0.0011 71   LEU A CD1 
571  C  CD2 . LEU A 72  ? 0.2497 0.1362 0.1652 -0.0440 0.0548  0.0005  71   LEU A CD2 
572  N  N   . SER A 73  ? 0.1918 0.1350 0.1569 0.0444  0.0158  -0.0080 72   SER A N   
573  C  CA  . SER A 73  ? 0.1873 0.1329 0.1670 0.0341  -0.0011 -0.0024 72   SER A CA  
574  C  C   . SER A 73  ? 0.2193 0.1204 0.1702 0.0363  -0.0048 0.0166  72   SER A C   
575  O  O   . SER A 73  ? 0.2756 0.1144 0.1768 0.0138  -0.0114 0.0150  72   SER A O   
576  C  CB  . SER A 73  ? 0.2389 0.1722 0.1727 0.0577  0.0293  -0.0231 72   SER A CB  
577  O  OG  . SER A 73  ? 0.1793 0.1863 0.1462 0.0235  0.0171  0.0030  72   SER A OG  
578  N  N   . GLN A 74  ? 0.2189 0.1044 0.1568 0.0079  0.0489  0.0287  73   GLN A N   
579  C  CA  . GLN A 74  ? 0.2794 0.1306 0.1919 -0.0171 0.0291  0.0196  73   GLN A CA  
580  C  C   . GLN A 74  ? 0.2281 0.1359 0.1874 -0.0003 0.0357  0.0015  73   GLN A C   
581  O  O   . GLN A 74  ? 0.2384 0.1638 0.1921 -0.0186 0.0092  0.0094  73   GLN A O   
582  C  CB  . GLN A 74  ? 0.3499 0.1361 0.2243 -0.0204 0.0458  0.0118  73   GLN A CB  
583  C  CG  . GLN A 74  ? 0.4154 0.2173 0.2571 -0.0152 0.0301  -0.0219 73   GLN A CG  
584  C  CD  . GLN A 74  ? 0.4615 0.2647 0.2743 -0.0371 0.0060  -0.0204 73   GLN A CD  
585  O  OE1 . GLN A 74  ? 0.5056 0.2994 0.2735 -0.0595 -0.0313 -0.0517 73   GLN A OE1 
586  N  NE2 . GLN A 74  ? 0.4590 0.2696 0.3097 0.0016  0.0168  0.0095  73   GLN A NE2 
587  N  N   . ALA A 75  ? 0.1949 0.1478 0.1940 -0.0331 -0.0331 -0.0194 74   ALA A N   
588  C  CA  . ALA A 75  ? 0.1980 0.1466 0.1811 0.0047  -0.0280 -0.0292 74   ALA A CA  
589  C  C   . ALA A 75  ? 0.2086 0.1342 0.1713 0.0660  -0.0175 -0.0116 74   ALA A C   
590  O  O   . ALA A 75  ? 0.2606 0.1438 0.1639 0.0069  -0.0282 -0.0160 74   ALA A O   
591  C  CB  . ALA A 75  ? 0.2126 0.1702 0.2037 -0.0464 -0.0018 -0.0129 74   ALA A CB  
592  N  N   . LEU A 76  ? 0.1783 0.1103 0.1678 0.0448  0.0053  -0.0300 75   LEU A N   
593  C  CA  . LEU A 76  ? 0.2436 0.0780 0.1859 0.0366  0.0124  -0.0258 75   LEU A CA  
594  C  C   . LEU A 76  ? 0.2089 0.0966 0.1867 0.0236  -0.0091 -0.0232 75   LEU A C   
595  O  O   . LEU A 76  ? 0.2214 0.1469 0.1951 0.0190  -0.0137 -0.0188 75   LEU A O   
596  C  CB  . LEU A 76  ? 0.2860 0.0756 0.1639 -0.0096 -0.0026 0.0182  75   LEU A CB  
597  C  CG  . LEU A 76  ? 0.2420 0.1014 0.1492 -0.0222 0.0215  0.0443  75   LEU A CG  
598  C  CD1 . LEU A 76  ? 0.1844 0.1293 0.1974 -0.0071 -0.0001 0.0623  75   LEU A CD1 
599  C  CD2 . LEU A 76  ? 0.2938 0.1204 0.1506 -0.0073 0.0122  0.0212  75   LEU A CD2 
600  N  N   . LYS A 77  ? 0.2338 0.0970 0.1841 -0.0121 -0.0162 -0.0184 76   LYS A N   
601  C  CA  . LYS A 77  ? 0.2522 0.1278 0.1618 -0.0191 -0.0310 -0.0218 76   LYS A CA  
602  C  C   . LYS A 77  ? 0.2490 0.1254 0.1784 0.0158  -0.0247 0.0022  76   LYS A C   
603  O  O   . LYS A 77  ? 0.2404 0.1591 0.2093 -0.0180 0.0129  0.0087  76   LYS A O   
604  C  CB  . LYS A 77  ? 0.2841 0.1743 0.1575 -0.0289 -0.0195 -0.0231 76   LYS A CB  
605  C  CG  . LYS A 77  ? 0.2698 0.1959 0.1392 0.0039  -0.0144 -0.0249 76   LYS A CG  
606  C  CD  . LYS A 77  ? 0.3570 0.2654 0.1680 0.0426  -0.0783 -0.0482 76   LYS A CD  
607  C  CE  . LYS A 77  ? 0.4136 0.3028 0.1985 -0.0031 -0.1305 -0.0606 76   LYS A CE  
608  N  NZ  . LYS A 77  ? 0.5987 0.3469 0.2304 0.0210  -0.1077 -0.0468 76   LYS A NZ  
609  N  N   . PHE A 78  ? 0.2710 0.1183 0.1605 0.0312  -0.0617 0.0014  77   PHE A N   
610  C  CA  . PHE A 78  ? 0.3018 0.1778 0.1677 0.0651  -0.0226 0.0139  77   PHE A CA  
611  C  C   . PHE A 78  ? 0.3139 0.1714 0.1722 0.0387  0.0329  0.0140  77   PHE A C   
612  O  O   . PHE A 78  ? 0.2762 0.2129 0.1822 0.0254  0.0287  -0.0059 77   PHE A O   
613  C  CB  . PHE A 78  ? 0.4136 0.1821 0.1982 0.0942  -0.0017 -0.0153 77   PHE A CB  
614  C  CG  . PHE A 78  ? 0.4883 0.1890 0.2388 0.0860  -0.0310 -0.0194 77   PHE A CG  
615  C  CD1 . PHE A 78  ? 0.5046 0.1857 0.2672 0.1104  -0.0367 -0.0411 77   PHE A CD1 
616  C  CD2 . PHE A 78  ? 0.4727 0.1652 0.2260 0.0863  -0.0090 -0.0234 77   PHE A CD2 
617  C  CE1 . PHE A 78  ? 0.5738 0.2198 0.2920 0.0770  -0.0398 -0.0447 77   PHE A CE1 
618  C  CE2 . PHE A 78  ? 0.5440 0.1967 0.2743 0.0680  -0.0024 -0.0290 77   PHE A CE2 
619  C  CZ  . PHE A 78  ? 0.5696 0.1970 0.2974 0.0934  -0.0258 -0.0454 77   PHE A CZ  
620  N  N   . VAL A 79  ? 0.2497 0.1512 0.1708 0.0255  0.0375  0.0037  78   VAL A N   
621  C  CA  . VAL A 79  ? 0.2111 0.1759 0.1610 0.0272  0.0214  -0.0123 78   VAL A CA  
622  C  C   . VAL A 79  ? 0.2060 0.1709 0.1617 -0.0013 -0.0015 -0.0091 78   VAL A C   
623  O  O   . VAL A 79  ? 0.2621 0.1976 0.1643 -0.0137 0.0133  0.0261  78   VAL A O   
624  C  CB  . VAL A 79  ? 0.1416 0.1877 0.1907 0.0259  0.0352  -0.0682 78   VAL A CB  
625  C  CG1 . VAL A 79  ? 0.2615 0.2356 0.1997 -0.0081 0.0499  -0.0471 78   VAL A CG1 
626  C  CG2 . VAL A 79  ? 0.1341 0.2422 0.1958 -0.0073 0.0321  -0.0831 78   VAL A CG2 
627  N  N   . ARG A 80  ? 0.2098 0.1824 0.1828 -0.0409 -0.0384 0.0022  79   ARG A N   
628  C  CA  . ARG A 80  ? 0.2002 0.1768 0.1970 -0.0066 -0.0809 0.0432  79   ARG A CA  
629  C  C   . ARG A 80  ? 0.2057 0.2040 0.2181 -0.0395 -0.0427 0.0325  79   ARG A C   
630  O  O   . ARG A 80  ? 0.2020 0.2007 0.2187 -0.0576 0.0174  0.0408  79   ARG A O   
631  C  CB  . ARG A 80  ? 0.2244 0.1959 0.2195 0.0359  -0.0898 0.0365  79   ARG A CB  
632  C  CG  . ARG A 80  ? 0.1598 0.1933 0.2517 0.0084  -0.0986 0.0447  79   ARG A CG  
633  C  CD  . ARG A 80  ? 0.1295 0.2069 0.2685 -0.0005 -0.0800 0.0458  79   ARG A CD  
634  N  NE  . ARG A 80  ? 0.1835 0.2308 0.2827 -0.0046 -0.0527 0.0469  79   ARG A NE  
635  C  CZ  . ARG A 80  ? 0.2007 0.2206 0.2432 -0.0292 -0.0387 0.0416  79   ARG A CZ  
636  N  NH1 . ARG A 80  ? 0.1923 0.1817 0.1935 -0.0539 0.0443  0.0024  79   ARG A NH1 
637  N  NH2 . ARG A 80  ? 0.2245 0.2181 0.2317 -0.0281 -0.0651 0.0450  79   ARG A NH2 
638  N  N   . ASP A 81  ? 0.2295 0.1874 0.2165 -0.0060 -0.0177 0.0419  80   ASP A N   
639  C  CA  . ASP A 81  ? 0.3304 0.2030 0.2470 0.0149  0.0453  0.0478  80   ASP A CA  
640  C  C   . ASP A 81  ? 0.3176 0.2313 0.2253 -0.0045 0.0452  0.0670  80   ASP A C   
641  O  O   . ASP A 81  ? 0.4302 0.2680 0.2405 -0.0525 0.0573  0.0525  80   ASP A O   
642  C  CB  . ASP A 81  ? 0.3451 0.1896 0.2777 0.0162  0.0599  0.0161  80   ASP A CB  
643  C  CG  . ASP A 81  ? 0.4624 0.1902 0.3492 0.0493  0.0228  -0.0014 80   ASP A CG  
644  O  OD1 . ASP A 81  ? 0.5243 0.1901 0.3438 0.0008  -0.0376 0.0045  80   ASP A OD1 
645  O  OD2 . ASP A 81  ? 0.6248 0.1955 0.3919 0.0506  0.0379  -0.0278 80   ASP A OD2 
646  N  N   . PHE A 82  ? 0.3047 0.2115 0.2016 0.0347  0.0240  0.0589  81   PHE A N   
647  C  CA  . PHE A 82  ? 0.2220 0.2463 0.1871 0.0414  -0.0071 0.0348  81   PHE A CA  
648  C  C   . PHE A 82  ? 0.2638 0.2424 0.1711 -0.0291 -0.0232 0.0176  81   PHE A C   
649  O  O   . PHE A 82  ? 0.2920 0.2465 0.1673 -0.0290 0.0363  -0.0140 81   PHE A O   
650  C  CB  . PHE A 82  ? 0.2700 0.2628 0.1895 0.1094  0.0051  0.0306  81   PHE A CB  
651  C  CG  . PHE A 82  ? 0.2918 0.2517 0.2085 0.0782  -0.0277 0.0010  81   PHE A CG  
652  C  CD1 . PHE A 82  ? 0.3346 0.2669 0.2127 0.0300  -0.0585 -0.0212 81   PHE A CD1 
653  C  CD2 . PHE A 82  ? 0.2961 0.2561 0.2365 0.1166  -0.0167 0.0106  81   PHE A CD2 
654  C  CE1 . PHE A 82  ? 0.4119 0.2595 0.1898 -0.0072 -0.0689 -0.0274 81   PHE A CE1 
655  C  CE2 . PHE A 82  ? 0.4095 0.2478 0.2096 0.0697  -0.0760 -0.0073 81   PHE A CE2 
656  C  CZ  . PHE A 82  ? 0.4228 0.2552 0.1816 -0.0034 -0.0764 0.0135  81   PHE A CZ  
657  N  N   . ALA A 83  ? 0.2479 0.2347 0.1676 -0.0323 -0.0168 0.0216  82   ALA A N   
658  C  CA  . ALA A 83  ? 0.1940 0.2307 0.1584 -0.0687 -0.0101 -0.0075 82   ALA A CA  
659  C  C   . ALA A 83  ? 0.2110 0.2179 0.1650 -0.0272 -0.0096 -0.0053 82   ALA A C   
660  O  O   . ALA A 83  ? 0.1567 0.2462 0.1758 -0.0046 0.0195  -0.0179 82   ALA A O   
661  C  CB  . ALA A 83  ? 0.2104 0.2393 0.1749 -0.1221 0.0281  0.0229  82   ALA A CB  
662  N  N   . GLY A 84  ? 0.2290 0.1874 0.1778 -0.0388 0.0064  -0.0296 83   GLY A N   
663  C  CA  . GLY A 84  ? 0.2125 0.1874 0.1898 -0.0188 0.0305  -0.0335 83   GLY A CA  
664  C  C   . GLY A 84  ? 0.1567 0.1953 0.1919 -0.0614 0.0266  -0.0230 83   GLY A C   
665  O  O   . GLY A 84  ? 0.1770 0.2393 0.1938 -0.0612 0.0542  -0.0391 83   GLY A O   
666  N  N   . ASP A 85  ? 0.2001 0.1766 0.2126 -0.0277 -0.0214 -0.0023 84   ASP A N   
667  C  CA  . ASP A 85  ? 0.1155 0.1869 0.2284 -0.0260 -0.0681 -0.0142 84   ASP A CA  
668  C  C   . ASP A 85  ? 0.1605 0.2060 0.2125 -0.0343 -0.0189 -0.0250 84   ASP A C   
669  O  O   . ASP A 85  ? 0.1541 0.1799 0.1939 -0.0166 -0.0019 -0.0122 84   ASP A O   
670  C  CB  . ASP A 85  ? 0.0925 0.2142 0.2394 -0.0093 -0.0070 -0.0134 84   ASP A CB  
671  C  CG  . ASP A 85  ? 0.1296 0.2558 0.2368 -0.0336 -0.0479 -0.0392 84   ASP A CG  
672  O  OD1 . ASP A 85  ? 0.1912 0.2481 0.1920 -0.0919 -0.0114 -0.0767 84   ASP A OD1 
673  O  OD2 . ASP A 85  ? 0.2039 0.2767 0.2388 -0.0593 -0.0125 -0.0224 84   ASP A OD2 
674  N  N   . GLY A 86  ? 0.1689 0.1928 0.1770 -0.0863 0.0117  -0.0286 85   GLY A N   
675  C  CA  . GLY A 86  ? 0.1499 0.1942 0.1508 -0.0844 0.0383  -0.0156 85   GLY A CA  
676  C  C   . GLY A 86  ? 0.1305 0.1773 0.1426 -0.0557 0.0503  -0.0095 85   GLY A C   
677  O  O   . GLY A 86  ? 0.1687 0.1770 0.1470 0.0325  -0.0136 -0.0215 85   GLY A O   
678  N  N   . LEU A 87  ? 0.0962 0.1497 0.1341 -0.0223 0.0162  -0.0089 86   LEU A N   
679  C  CA  . LEU A 87  ? 0.1447 0.1442 0.1527 0.0048  0.0509  -0.0317 86   LEU A CA  
680  C  C   . LEU A 87  ? 0.1635 0.1871 0.1415 -0.0128 0.0148  -0.0442 86   LEU A C   
681  O  O   . LEU A 87  ? 0.1943 0.2307 0.1321 -0.0046 0.0389  -0.0482 86   LEU A O   
682  C  CB  . LEU A 87  ? 0.1365 0.1051 0.1566 -0.0117 0.0123  -0.0177 86   LEU A CB  
683  C  CG  . LEU A 87  ? 0.1565 0.1506 0.1649 -0.0290 -0.0460 -0.0134 86   LEU A CG  
684  C  CD1 . LEU A 87  ? 0.1877 0.1607 0.1875 -0.0464 -0.0315 -0.0266 86   LEU A CD1 
685  C  CD2 . LEU A 87  ? 0.1365 0.1808 0.1344 -0.0145 0.0170  0.0264  86   LEU A CD2 
686  N  N   . ALA A 88  ? 0.1215 0.1998 0.1498 0.0074  0.0360  -0.0146 87   ALA A N   
687  C  CA  . ALA A 88  ? 0.1238 0.1613 0.1334 0.0256  0.0170  0.0026  87   ALA A CA  
688  C  C   . ALA A 88  ? 0.1860 0.1458 0.1184 -0.0072 -0.0072 -0.0027 87   ALA A C   
689  O  O   . ALA A 88  ? 0.2197 0.1364 0.1465 0.0290  -0.0190 0.0041  87   ALA A O   
690  C  CB  . ALA A 88  ? 0.1266 0.1483 0.1347 0.0489  -0.0011 -0.0065 87   ALA A CB  
691  N  N   . THR A 89  ? 0.1631 0.1468 0.1270 -0.0854 -0.0003 0.0150  88   THR A N   
692  C  CA  . THR A 89  ? 0.1412 0.1438 0.1444 -0.0632 -0.0259 0.0103  88   THR A CA  
693  C  C   . THR A 89  ? 0.1435 0.1589 0.1562 0.0006  -0.0223 0.0344  88   THR A C   
694  O  O   . THR A 89  ? 0.1813 0.1714 0.1933 -0.0019 -0.0004 0.0025  88   THR A O   
695  C  CB  . THR A 89  ? 0.2297 0.1552 0.1549 -0.0025 -0.0095 0.0356  88   THR A CB  
696  O  OG1 . THR A 89  ? 0.2107 0.1542 0.1747 -0.0185 -0.0157 0.0123  88   THR A OG1 
697  C  CG2 . THR A 89  ? 0.1687 0.1742 0.1242 0.0528  -0.0071 0.0409  88   THR A CG2 
698  N  N   . SER A 90  ? 0.1048 0.1845 0.1567 -0.0019 -0.0223 0.0113  89   SER A N   
699  C  CA  . SER A 90  ? 0.1394 0.1923 0.1906 -0.0374 0.0016  -0.0158 89   SER A CA  
700  C  C   . SER A 90  ? 0.1434 0.1589 0.1375 -0.0809 0.0367  0.0009  89   SER A C   
701  O  O   . SER A 90  ? 0.2117 0.1366 0.1287 -0.0581 0.0131  0.0223  89   SER A O   
702  C  CB  . SER A 90  ? 0.1645 0.1869 0.2926 -0.0782 -0.0516 -0.0373 89   SER A CB  
703  O  OG  . SER A 90  ? 0.2802 0.2572 0.3258 0.0195  -0.0348 -0.0658 89   SER A OG  
704  N  N   . TRP A 91  ? 0.2378 0.1624 0.1147 -0.0603 0.0254  -0.0037 90   TRP A N   
705  C  CA  . TRP A 91  ? 0.2117 0.1547 0.1247 -0.0658 -0.0153 -0.0375 90   TRP A CA  
706  C  C   . TRP A 91  ? 0.2309 0.1218 0.1272 -0.0491 0.0233  -0.0138 90   TRP A C   
707  O  O   . TRP A 91  ? 0.2156 0.1462 0.1326 -0.0515 0.0091  -0.0253 90   TRP A O   
708  C  CB  . TRP A 91  ? 0.1787 0.1404 0.1530 -0.0034 0.0068  -0.0431 90   TRP A CB  
709  C  CG  . TRP A 91  ? 0.2339 0.1550 0.1855 -0.0250 -0.0132 -0.0270 90   TRP A CG  
710  C  CD1 . TRP A 91  ? 0.2211 0.1344 0.2151 -0.0141 -0.0662 0.0006  90   TRP A CD1 
711  C  CD2 . TRP A 91  ? 0.1815 0.1563 0.1840 -0.0137 -0.0018 -0.0283 90   TRP A CD2 
712  N  NE1 . TRP A 91  ? 0.1759 0.1386 0.2230 -0.0137 0.0064  -0.0168 90   TRP A NE1 
713  C  CE2 . TRP A 91  ? 0.1975 0.1539 0.1915 -0.0372 0.0162  -0.0150 90   TRP A CE2 
714  C  CE3 . TRP A 91  ? 0.1763 0.1282 0.1725 -0.0456 0.0395  -0.0332 90   TRP A CE3 
715  C  CZ2 . TRP A 91  ? 0.1928 0.1431 0.2101 -0.0582 -0.0102 0.0088  90   TRP A CZ2 
716  C  CZ3 . TRP A 91  ? 0.2299 0.1407 0.1879 -0.0485 0.0507  -0.0230 90   TRP A CZ3 
717  C  CH2 . TRP A 91  ? 0.1997 0.1446 0.1775 -0.0711 0.0468  -0.0014 90   TRP A CH2 
718  N  N   . THR A 92  ? 0.1884 0.0912 0.1407 -0.0216 -0.0048 -0.0001 91   THR A N   
719  C  CA  . THR A 92  ? 0.1826 0.1418 0.1551 -0.0610 -0.0151 -0.0067 91   THR A CA  
720  C  C   . THR A 92  ? 0.2190 0.1515 0.1776 -0.0371 0.0075  -0.0060 91   THR A C   
721  O  O   . THR A 92  ? 0.1899 0.1428 0.1712 -0.0408 -0.0160 -0.0097 91   THR A O   
722  C  CB  . THR A 92  ? 0.1597 0.1203 0.1580 -0.0211 -0.0070 -0.0038 91   THR A CB  
723  O  OG1 . THR A 92  ? 0.1425 0.1076 0.1735 -0.0030 -0.0329 -0.0296 91   THR A OG1 
724  C  CG2 . THR A 92  ? 0.2782 0.1231 0.1819 -0.0104 0.0223  -0.0299 91   THR A CG2 
725  N  N   . HIS A 93  ? 0.1826 0.1445 0.1646 -0.0575 0.0165  -0.0329 92   HIS A N   
726  C  CA  . HIS A 93  ? 0.1553 0.1523 0.1666 -0.0773 -0.0231 -0.0107 92   HIS A CA  
727  C  C   . HIS A 93  ? 0.1559 0.1860 0.1804 -0.0610 -0.0531 0.0117  92   HIS A C   
728  O  O   . HIS A 93  ? 0.1394 0.1810 0.1776 -0.0660 -0.0288 0.0065  92   HIS A O   
729  C  CB  . HIS A 93  ? 0.2411 0.1537 0.1841 -0.0871 -0.0389 -0.0108 92   HIS A CB  
730  C  CG  . HIS A 93  ? 0.2726 0.1574 0.2079 -0.0311 -0.0850 -0.0148 92   HIS A CG  
731  N  ND1 . HIS A 93  ? 0.2614 0.1185 0.2141 0.0135  -0.0975 0.0168  92   HIS A ND1 
732  C  CD2 . HIS A 93  ? 0.2554 0.1467 0.2318 0.0090  -0.0725 -0.0309 92   HIS A CD2 
733  C  CE1 . HIS A 93  ? 0.3102 0.1511 0.2452 -0.0528 -0.0874 -0.0115 92   HIS A CE1 
734  N  NE2 . HIS A 93  ? 0.2765 0.1538 0.2322 -0.0058 -0.0620 -0.0186 92   HIS A NE2 
735  N  N   . GLU A 94  ? 0.1455 0.1994 0.1723 -0.0392 -0.0204 -0.0069 93   GLU A N   
736  C  CA  . GLU A 94  ? 0.1854 0.2013 0.1833 -0.0301 0.0324  0.0168  93   GLU A CA  
737  C  C   . GLU A 94  ? 0.1529 0.2245 0.1771 -0.0340 0.0244  -0.0089 93   GLU A C   
738  O  O   . GLU A 94  ? 0.1743 0.2238 0.1794 -0.0290 -0.0090 -0.0175 93   GLU A O   
739  C  CB  . GLU A 94  ? 0.1928 0.1621 0.1992 0.0529  -0.0007 0.0140  93   GLU A CB  
740  C  CG  . GLU A 94  ? 0.1876 0.1460 0.2136 0.0073  0.0101  0.0195  93   GLU A CG  
741  C  CD  . GLU A 94  ? 0.1773 0.1775 0.2027 -0.0787 -0.0036 0.0290  93   GLU A CD  
742  O  OE1 . GLU A 94  ? 0.1806 0.1860 0.1770 -0.0883 -0.0060 -0.0192 93   GLU A OE1 
743  O  OE2 . GLU A 94  ? 0.2158 0.2122 0.2247 -0.1223 -0.0109 0.0388  93   GLU A OE2 
744  N  N   . LYS A 95  ? 0.1473 0.2499 0.1883 -0.0525 -0.0207 -0.0448 94   LYS A N   
745  C  CA  . LYS A 95  ? 0.1235 0.2662 0.2064 -0.0110 0.0519  -0.0438 94   LYS A CA  
746  C  C   . LYS A 95  ? 0.1325 0.2523 0.2101 -0.0330 0.0080  -0.0354 94   LYS A C   
747  O  O   . LYS A 95  ? 0.1806 0.2388 0.2048 0.0115  -0.0165 -0.0745 94   LYS A O   
748  C  CB  . LYS A 95  ? 0.1259 0.3123 0.2540 -0.0296 0.0125  -0.0439 94   LYS A CB  
749  C  CG  . LYS A 95  ? 0.1705 0.3645 0.2538 -0.0589 0.0449  -0.0482 94   LYS A CG  
750  C  CD  . LYS A 95  ? 0.1358 0.4101 0.2782 -0.0431 0.0226  -0.0597 94   LYS A CD  
751  C  CE  . LYS A 95  ? 0.2427 0.4634 0.3272 -0.1030 0.0726  -0.0590 94   LYS A CE  
752  N  NZ  . LYS A 95  ? 0.3588 0.4817 0.3637 -0.1540 0.0959  -0.0470 94   LYS A NZ  
753  N  N   . ASN A 96  ? 0.1325 0.2363 0.2114 -0.0330 0.0053  -0.0235 95   ASN A N   
754  C  CA  . ASN A 96  ? 0.1804 0.2359 0.2116 -0.0478 -0.0113 -0.0116 95   ASN A CA  
755  C  C   . ASN A 96  ? 0.1459 0.2002 0.1798 -0.0592 0.0227  -0.0092 95   ASN A C   
756  O  O   . ASN A 96  ? 0.1532 0.1914 0.1808 -0.0338 -0.0143 -0.0123 95   ASN A O   
757  C  CB  . ASN A 96  ? 0.1363 0.2703 0.2216 -0.0508 0.0143  0.0041  95   ASN A CB  
758  C  CG  . ASN A 96  ? 0.1971 0.2605 0.2853 -0.0312 0.0033  0.0224  95   ASN A CG  
759  O  OD1 . ASN A 96  ? 0.2692 0.2383 0.3152 0.0141  0.0646  0.0422  95   ASN A OD1 
760  N  ND2 . ASN A 96  ? 0.2108 0.2376 0.2647 -0.1006 0.0264  0.0017  95   ASN A ND2 
761  N  N   . TRP A 97  ? 0.1218 0.1886 0.1728 -0.0077 0.0387  0.0089  96   TRP A N   
762  C  CA  . TRP A 97  ? 0.1259 0.2068 0.1811 0.0250  -0.0043 0.0008  96   TRP A CA  
763  C  C   . TRP A 97  ? 0.0827 0.2013 0.2038 0.0309  -0.0120 -0.0052 96   TRP A C   
764  O  O   . TRP A 97  ? 0.1482 0.1838 0.2311 -0.0088 -0.0074 0.0037  96   TRP A O   
765  C  CB  . TRP A 97  ? 0.1310 0.2080 0.1656 -0.0125 -0.0130 -0.0194 96   TRP A CB  
766  C  CG  . TRP A 97  ? 0.1744 0.2146 0.1756 0.0079  0.0012  0.0025  96   TRP A CG  
767  C  CD1 . TRP A 97  ? 0.1325 0.2476 0.1834 0.0186  0.0625  -0.0114 96   TRP A CD1 
768  C  CD2 . TRP A 97  ? 0.1672 0.2194 0.1584 -0.0137 0.0177  -0.0105 96   TRP A CD2 
769  N  NE1 . TRP A 97  ? 0.1042 0.2347 0.1699 -0.0031 0.0248  -0.0503 96   TRP A NE1 
770  C  CE2 . TRP A 97  ? 0.1731 0.2433 0.1584 0.0103  0.0346  -0.0245 96   TRP A CE2 
771  C  CE3 . TRP A 97  ? 0.2284 0.1911 0.1483 -0.0205 0.0102  0.0100  96   TRP A CE3 
772  C  CZ2 . TRP A 97  ? 0.1773 0.2482 0.1694 -0.0430 0.0066  -0.0297 96   TRP A CZ2 
773  C  CZ3 . TRP A 97  ? 0.1325 0.2117 0.1652 -0.0297 0.0242  -0.0071 96   TRP A CZ3 
774  C  CH2 . TRP A 97  ? 0.1682 0.2361 0.1870 0.0018  0.0150  -0.0238 96   TRP A CH2 
775  N  N   . LYS A 98  ? 0.1444 0.2001 0.1909 0.0685  -0.0158 -0.0027 97   LYS A N   
776  C  CA  . LYS A 98  ? 0.1644 0.1986 0.1764 0.0875  -0.0329 -0.0033 97   LYS A CA  
777  C  C   . LYS A 98  ? 0.1647 0.2057 0.1921 0.0464  0.0057  -0.0157 97   LYS A C   
778  O  O   . LYS A 98  ? 0.1611 0.1791 0.2091 0.0135  -0.0200 -0.0066 97   LYS A O   
779  C  CB  . LYS A 98  ? 0.2568 0.1749 0.1813 0.0625  -0.0569 0.0368  97   LYS A CB  
780  C  CG  . LYS A 98  ? 0.3289 0.2399 0.2211 0.0214  -0.0237 0.0364  97   LYS A CG  
781  C  CD  . LYS A 98  ? 0.3894 0.2801 0.2586 -0.0124 0.0072  0.0306  97   LYS A CD  
782  C  CE  . LYS A 98  ? 0.4931 0.3319 0.2793 -0.0070 0.0282  0.0298  97   LYS A CE  
783  N  NZ  . LYS A 98  ? 0.5731 0.3642 0.3329 -0.0267 0.1044  0.0247  97   LYS A NZ  
784  N  N   . LYS A 99  ? 0.1138 0.2164 0.1867 -0.0020 0.0476  0.0004  98   LYS A N   
785  C  CA  . LYS A 99  ? 0.0837 0.2457 0.2006 -0.0232 0.0495  -0.0079 98   LYS A CA  
786  C  C   . LYS A 99  ? 0.1225 0.2443 0.2224 -0.0171 0.0139  -0.0129 98   LYS A C   
787  O  O   . LYS A 99  ? 0.1798 0.2184 0.1812 -0.0050 -0.0107 -0.0206 98   LYS A O   
788  C  CB  . LYS A 99  ? 0.1092 0.3078 0.2579 -0.0467 0.0469  0.0159  98   LYS A CB  
789  C  CG  . LYS A 99  ? 0.1320 0.3350 0.2829 -0.0332 0.0776  0.0222  98   LYS A CG  
790  C  CD  . LYS A 99  ? 0.1795 0.3878 0.3007 -0.0771 0.0581  0.0197  98   LYS A CD  
791  C  CE  . LYS A 99  ? 0.1610 0.4019 0.2842 -0.1090 0.0409  -0.0090 98   LYS A CE  
792  N  NZ  . LYS A 99  ? 0.1697 0.4004 0.2796 -0.1121 0.0488  -0.0005 98   LYS A NZ  
793  N  N   . ALA A 100 ? 0.1511 0.1902 0.2107 0.0392  -0.0312 -0.0073 99   ALA A N   
794  C  CA  . ALA A 100 ? 0.1628 0.1608 0.1952 -0.0008 -0.0049 0.0306  99   ALA A CA  
795  C  C   . ALA A 100 ? 0.1486 0.1740 0.1804 -0.0095 -0.0122 0.0056  99   ALA A C   
796  O  O   . ALA A 100 ? 0.1851 0.1690 0.1806 0.0249  -0.0455 -0.0137 99   ALA A O   
797  C  CB  . ALA A 100 ? 0.1752 0.1347 0.2081 -0.0147 -0.0139 0.0429  99   ALA A CB  
798  N  N   . HIS A 101 ? 0.1572 0.1866 0.1826 0.0205  -0.0007 0.0286  100  HIS A N   
799  C  CA  . HIS A 101 ? 0.1864 0.2077 0.1926 0.0120  0.0509  -0.0057 100  HIS A CA  
800  C  C   . HIS A 101 ? 0.1877 0.2108 0.2087 -0.0027 -0.0209 -0.0087 100  HIS A C   
801  O  O   . HIS A 101 ? 0.1653 0.2127 0.1957 0.0139  -0.0018 -0.0226 100  HIS A O   
802  C  CB  . HIS A 101 ? 0.2317 0.2239 0.1655 -0.0538 0.0982  -0.0447 100  HIS A CB  
803  C  CG  . HIS A 101 ? 0.3086 0.2935 0.2404 -0.1200 0.0245  -0.0509 100  HIS A CG  
804  N  ND1 . HIS A 101 ? 0.3470 0.3482 0.2575 -0.1153 0.0232  -0.0349 100  HIS A ND1 
805  C  CD2 . HIS A 101 ? 0.3888 0.3333 0.2985 -0.2130 0.0403  -0.0310 100  HIS A CD2 
806  C  CE1 . HIS A 101 ? 0.3477 0.3768 0.3166 -0.1181 0.0197  -0.0104 100  HIS A CE1 
807  N  NE2 . HIS A 101 ? 0.4325 0.3852 0.3509 -0.1735 0.0531  -0.0028 100  HIS A NE2 
808  N  N   . ASN A 102 ? 0.1601 0.2258 0.2064 -0.0015 -0.0534 0.0287  101  ASN A N   
809  C  CA  . ASN A 102 ? 0.1230 0.2272 0.2122 0.0163  -0.0479 -0.0070 101  ASN A CA  
810  C  C   . ASN A 102 ? 0.1795 0.2401 0.2221 0.0202  -0.0521 -0.0295 101  ASN A C   
811  O  O   . ASN A 102 ? 0.2129 0.2490 0.2655 0.0877  -0.0418 -0.0419 101  ASN A O   
812  C  CB  . ASN A 102 ? 0.1087 0.2218 0.2234 0.0328  -0.0573 0.0065  101  ASN A CB  
813  C  CG  . ASN A 102 ? 0.1357 0.2547 0.2323 0.0337  -0.0433 0.0095  101  ASN A CG  
814  O  OD1 . ASN A 102 ? 0.1337 0.3001 0.2586 0.0362  -0.0110 0.0093  101  ASN A OD1 
815  N  ND2 . ASN A 102 ? 0.2205 0.2716 0.2198 0.0425  -0.0473 0.0162  101  ASN A ND2 
816  N  N   . ILE A 103 ? 0.1323 0.2535 0.1903 0.0461  -0.0387 -0.0091 102  ILE A N   
817  C  CA  . ILE A 103 ? 0.1645 0.2491 0.1842 0.0024  -0.0343 -0.0257 102  ILE A CA  
818  C  C   . ILE A 103 ? 0.1242 0.2244 0.1919 0.0292  -0.0466 -0.0637 102  ILE A C   
819  O  O   . ILE A 103 ? 0.1888 0.2654 0.2239 0.0177  -0.0527 -0.0880 102  ILE A O   
820  C  CB  . ILE A 103 ? 0.1485 0.2512 0.1871 -0.0202 -0.0417 -0.0133 102  ILE A CB  
821  C  CG1 . ILE A 103 ? 0.1297 0.2306 0.2205 -0.0176 -0.0380 0.0113  102  ILE A CG1 
822  C  CG2 . ILE A 103 ? 0.1611 0.2313 0.2228 -0.0160 -0.0048 -0.0650 102  ILE A CG2 
823  C  CD1 . ILE A 103 ? 0.1330 0.2439 0.2305 -0.0039 -0.0091 0.0279  102  ILE A CD1 
824  N  N   . LEU A 104 ? 0.0738 0.2262 0.1925 0.0217  -0.0137 -0.0266 103  LEU A N   
825  C  CA  . LEU A 104 ? 0.1552 0.1875 0.1959 0.0382  -0.0262 -0.0199 103  LEU A CA  
826  C  C   . LEU A 104 ? 0.1667 0.1858 0.1967 0.0408  -0.0015 -0.0083 103  LEU A C   
827  O  O   . LEU A 104 ? 0.2114 0.1723 0.2229 0.0288  -0.0103 -0.0222 103  LEU A O   
828  C  CB  . LEU A 104 ? 0.1726 0.1860 0.1621 0.0168  -0.0545 -0.0129 103  LEU A CB  
829  C  CG  . LEU A 104 ? 0.2023 0.1697 0.1470 0.0468  0.0170  0.0064  103  LEU A CG  
830  C  CD1 . LEU A 104 ? 0.2335 0.1647 0.1542 0.0448  0.0240  0.0107  103  LEU A CD1 
831  C  CD2 . LEU A 104 ? 0.3176 0.2176 0.1884 -0.0158 0.0107  0.0138  103  LEU A CD2 
832  N  N   . LEU A 105 ? 0.2122 0.1741 0.1910 -0.0217 -0.0125 0.0073  104  LEU A N   
833  C  CA  . LEU A 105 ? 0.1851 0.1888 0.1984 -0.0368 -0.0109 0.0197  104  LEU A CA  
834  C  C   . LEU A 105 ? 0.2405 0.1936 0.2238 -0.0332 -0.0703 0.0075  104  LEU A C   
835  O  O   . LEU A 105 ? 0.2478 0.1863 0.2306 -0.0814 -0.0427 0.0123  104  LEU A O   
836  C  CB  . LEU A 105 ? 0.2534 0.2456 0.1949 -0.0566 -0.0082 0.0563  104  LEU A CB  
837  C  CG  . LEU A 105 ? 0.3121 0.3030 0.2254 0.0059  -0.0289 0.0930  104  LEU A CG  
838  C  CD1 . LEU A 105 ? 0.2904 0.3144 0.2385 0.0052  0.0478  0.0682  104  LEU A CD1 
839  C  CD2 . LEU A 105 ? 0.3563 0.3242 0.2301 0.0315  -0.0214 0.1265  104  LEU A CD2 
840  N  N   . PRO A 106 ? 0.2022 0.2023 0.2514 -0.0235 -0.0675 -0.0399 105  PRO A N   
841  C  CA  . PRO A 106 ? 0.2236 0.2228 0.2662 0.0304  -0.0407 -0.0609 105  PRO A CA  
842  C  C   . PRO A 106 ? 0.2793 0.2064 0.2420 0.0537  -0.0268 -0.0527 105  PRO A C   
843  O  O   . PRO A 106 ? 0.3336 0.2180 0.2577 0.0789  -0.0748 -0.0443 105  PRO A O   
844  C  CB  . PRO A 106 ? 0.2490 0.2567 0.2963 -0.0031 -0.0250 -0.0691 105  PRO A CB  
845  C  CG  . PRO A 106 ? 0.1724 0.2453 0.3060 -0.0382 -0.0669 -0.0409 105  PRO A CG  
846  C  CD  . PRO A 106 ? 0.1661 0.2403 0.2873 -0.0055 -0.0550 -0.0435 105  PRO A CD  
847  N  N   . SER A 107 ? 0.1439 0.1724 0.2173 0.0528  0.0308  -0.0146 106  SER A N   
848  C  CA  . SER A 107 ? 0.2409 0.1929 0.2174 -0.0080 -0.0010 0.0015  106  SER A CA  
849  C  C   . SER A 107 ? 0.1865 0.1906 0.2135 -0.0162 -0.0233 -0.0107 106  SER A C   
850  O  O   . SER A 107 ? 0.2311 0.1809 0.1915 -0.0040 -0.0072 0.0027  106  SER A O   
851  C  CB  . SER A 107 ? 0.2625 0.2728 0.2435 -0.0181 -0.0177 0.0475  106  SER A CB  
852  O  OG  . SER A 107 ? 0.3778 0.3283 0.2795 -0.0570 0.0263  0.0426  106  SER A OG  
853  N  N   . PHE A 108 ? 0.1921 0.2411 0.2139 0.0130  0.0310  -0.0107 107  PHE A N   
854  C  CA  . PHE A 108 ? 0.2146 0.3115 0.2349 0.0597  -0.0084 -0.0017 107  PHE A CA  
855  C  C   . PHE A 108 ? 0.2295 0.3813 0.2336 -0.0125 -0.0111 0.0120  107  PHE A C   
856  O  O   . PHE A 108 ? 0.3142 0.4737 0.2432 -0.0672 0.0531  0.0024  107  PHE A O   
857  C  CB  . PHE A 108 ? 0.2617 0.3328 0.2479 0.1552  -0.0603 0.0121  107  PHE A CB  
858  C  CG  . PHE A 108 ? 0.2483 0.3075 0.2303 0.1582  -0.0230 0.0040  107  PHE A CG  
859  C  CD1 . PHE A 108 ? 0.1893 0.3263 0.2574 0.1371  -0.0171 0.0032  107  PHE A CD1 
860  C  CD2 . PHE A 108 ? 0.2833 0.2729 0.2285 0.1590  -0.0708 -0.0676 107  PHE A CD2 
861  C  CE1 . PHE A 108 ? 0.3289 0.3129 0.2617 0.1185  -0.0443 -0.0288 107  PHE A CE1 
862  C  CE2 . PHE A 108 ? 0.2525 0.2706 0.2260 0.1440  -0.0868 -0.0778 107  PHE A CE2 
863  C  CZ  . PHE A 108 ? 0.2913 0.2851 0.2619 0.1383  -0.0493 -0.0837 107  PHE A CZ  
864  N  N   . SER A 109 ? 0.2993 0.3479 0.2789 -0.1080 -0.0933 0.0766  108  SER A N   
865  C  CA  . SER A 109 ? 0.3829 0.2870 0.3191 -0.1404 -0.0911 0.1274  108  SER A CA  
866  C  C   . SER A 109 ? 0.4541 0.3050 0.3407 -0.1553 -0.1140 0.1490  108  SER A C   
867  O  O   . SER A 109 ? 0.4131 0.3498 0.3318 -0.1933 -0.1423 0.1528  108  SER A O   
868  C  CB  . SER A 109 ? 0.4940 0.2681 0.3281 -0.1330 -0.0549 0.0964  108  SER A CB  
869  O  OG  . SER A 109 ? 0.5303 0.2610 0.3467 -0.0585 -0.0515 0.0626  108  SER A OG  
870  N  N   . GLN A 110 ? 0.5205 0.2803 0.3672 -0.1122 -0.0798 0.1324  109  GLN A N   
871  C  CA  . GLN A 110 ? 0.5377 0.3141 0.3945 -0.1225 -0.1195 0.1175  109  GLN A CA  
872  C  C   . GLN A 110 ? 0.5252 0.2882 0.4407 -0.0854 -0.1827 0.1076  109  GLN A C   
873  O  O   . GLN A 110 ? 0.5752 0.2831 0.4585 -0.0409 -0.2486 0.1148  109  GLN A O   
874  C  CB  . GLN A 110 ? 0.6669 0.3975 0.4052 -0.1301 -0.0640 0.0988  109  GLN A CB  
875  C  CG  . GLN A 110 ? 0.7904 0.4578 0.4248 -0.0971 0.0099  0.1016  109  GLN A CG  
876  C  CD  . GLN A 110 ? 0.8690 0.4908 0.4227 -0.0209 0.0664  0.1017  109  GLN A CD  
877  O  OE1 . GLN A 110 ? 0.9433 0.5180 0.4262 0.0097  0.0285  0.1230  109  GLN A OE1 
878  N  NE2 . GLN A 110 ? 0.8025 0.4871 0.4091 -0.0061 0.1654  0.0827  109  GLN A NE2 
879  N  N   . GLN A 111 ? 0.5135 0.2626 0.4658 -0.1135 -0.1677 0.0675  110  GLN A N   
880  C  CA  . GLN A 111 ? 0.4778 0.2779 0.5068 -0.0169 -0.1611 0.0417  110  GLN A CA  
881  C  C   . GLN A 111 ? 0.4279 0.2390 0.4858 0.0155  -0.1742 0.0306  110  GLN A C   
882  O  O   . GLN A 111 ? 0.2897 0.2395 0.5198 0.0479  -0.1528 0.0445  110  GLN A O   
883  C  CB  . GLN A 111 ? 0.5454 0.3320 0.5627 -0.0101 -0.1671 0.0238  110  GLN A CB  
884  C  CG  . GLN A 111 ? 0.6284 0.3952 0.6060 0.0474  -0.1289 0.0289  110  GLN A CG  
885  C  CD  . GLN A 111 ? 0.7522 0.4734 0.6481 0.0418  -0.0638 0.0398  110  GLN A CD  
886  O  OE1 . GLN A 111 ? 0.7724 0.4820 0.6749 0.0210  -0.0454 0.0590  110  GLN A OE1 
887  N  NE2 . GLN A 111 ? 0.8203 0.5201 0.6601 0.0347  -0.0318 0.0219  110  GLN A NE2 
888  N  N   . ALA A 112 ? 0.4156 0.2044 0.4337 -0.0384 -0.1978 0.0283  111  ALA A N   
889  C  CA  . ALA A 112 ? 0.3210 0.1696 0.3861 -0.0404 -0.1524 0.0024  111  ALA A CA  
890  C  C   . ALA A 112 ? 0.3541 0.1848 0.3065 -0.0318 -0.1120 -0.0239 111  ALA A C   
891  O  O   . ALA A 112 ? 0.3487 0.2088 0.2724 -0.0010 -0.0441 -0.0403 111  ALA A O   
892  C  CB  . ALA A 112 ? 0.2516 0.1508 0.3690 -0.0565 -0.1207 -0.0007 111  ALA A CB  
893  N  N   . MET A 113 ? 0.3599 0.1840 0.2437 -0.0696 -0.0513 -0.0141 112  MET A N   
894  C  CA  . MET A 113 ? 0.3063 0.1949 0.2373 -0.0291 0.0257  -0.0322 112  MET A CA  
895  C  C   . MET A 113 ? 0.2886 0.1942 0.2072 0.0197  0.0201  -0.0191 112  MET A C   
896  O  O   . MET A 113 ? 0.3230 0.1843 0.2093 0.0455  0.0015  -0.0099 112  MET A O   
897  C  CB  . MET A 113 ? 0.4761 0.1980 0.2431 -0.0288 0.0355  -0.0401 112  MET A CB  
898  C  CG  . MET A 113 ? 0.5410 0.2120 0.2826 -0.0252 0.0928  -0.0214 112  MET A CG  
899  S  SD  . MET A 113 ? 0.4806 0.2064 0.2943 0.0579  0.0999  -0.0013 112  MET A SD  
900  C  CE  . MET A 113 ? 0.6738 0.2482 0.3275 0.0368  0.0914  -0.0243 112  MET A CE  
901  N  N   . LYS A 114 ? 0.2895 0.1600 0.1871 0.0277  -0.0136 -0.0420 113  LYS A N   
902  C  CA  . LYS A 114 ? 0.2789 0.1493 0.1799 0.0714  0.0175  -0.0302 113  LYS A CA  
903  C  C   . LYS A 114 ? 0.3402 0.1719 0.1978 0.0703  -0.0116 -0.0154 113  LYS A C   
904  O  O   . LYS A 114 ? 0.3663 0.2166 0.2013 0.0573  -0.0493 -0.0124 113  LYS A O   
905  C  CB  . LYS A 114 ? 0.2818 0.1522 0.1871 0.0715  -0.0423 0.0148  113  LYS A CB  
906  C  CG  . LYS A 114 ? 0.3552 0.1844 0.1982 0.0380  -0.0698 0.0236  113  LYS A CG  
907  C  CD  . LYS A 114 ? 0.3243 0.2149 0.2184 0.1123  -0.0585 0.0491  113  LYS A CD  
908  C  CE  . LYS A 114 ? 0.3745 0.2293 0.2623 0.0823  -0.0281 0.0647  113  LYS A CE  
909  N  NZ  . LYS A 114 ? 0.4902 0.2286 0.2791 0.0158  -0.0212 0.0582  113  LYS A NZ  
910  N  N   . GLY A 115 ? 0.2740 0.1405 0.1971 0.0712  -0.0079 -0.0243 114  GLY A N   
911  C  CA  . GLY A 115 ? 0.2605 0.1734 0.1847 0.1050  -0.0085 -0.0180 114  GLY A CA  
912  C  C   . GLY A 115 ? 0.3118 0.1601 0.1826 0.1150  -0.0382 -0.0214 114  GLY A C   
913  O  O   . GLY A 115 ? 0.3658 0.2101 0.2150 0.0914  -0.0371 -0.0243 114  GLY A O   
914  N  N   . TYR A 116 ? 0.2700 0.1565 0.1935 0.0574  -0.0574 -0.0145 115  TYR A N   
915  C  CA  . TYR A 116 ? 0.2344 0.1495 0.1849 -0.0013 -0.0530 -0.0091 115  TYR A CA  
916  C  C   . TYR A 116 ? 0.2437 0.1824 0.1634 -0.0003 -0.0336 -0.0124 115  TYR A C   
917  O  O   . TYR A 116 ? 0.2915 0.2021 0.1218 0.0293  -0.0164 -0.0005 115  TYR A O   
918  C  CB  . TYR A 116 ? 0.2189 0.1374 0.1695 0.0091  -0.0342 -0.0069 115  TYR A CB  
919  C  CG  . TYR A 116 ? 0.2747 0.1688 0.1786 0.0087  -0.0386 -0.0017 115  TYR A CG  
920  C  CD1 . TYR A 116 ? 0.2893 0.2053 0.1792 -0.0206 -0.0580 0.0148  115  TYR A CD1 
921  C  CD2 . TYR A 116 ? 0.2461 0.1531 0.1577 -0.0024 -0.0827 -0.0059 115  TYR A CD2 
922  C  CE1 . TYR A 116 ? 0.2691 0.2451 0.1796 -0.0526 -0.0451 -0.0022 115  TYR A CE1 
923  C  CE2 . TYR A 116 ? 0.2722 0.1766 0.1784 -0.0417 -0.0528 -0.0130 115  TYR A CE2 
924  C  CZ  . TYR A 116 ? 0.2160 0.2425 0.1842 -0.0827 -0.0418 -0.0287 115  TYR A CZ  
925  O  OH  . TYR A 116 ? 0.2936 0.3032 0.1970 -0.0526 -0.0508 -0.0369 115  TYR A OH  
926  N  N   . HIS A 117 ? 0.3089 0.1778 0.1952 -0.0271 -0.0239 0.0035  116  HIS A N   
927  C  CA  . HIS A 117 ? 0.2108 0.1796 0.1668 -0.0817 -0.0186 0.0346  116  HIS A CA  
928  C  C   . HIS A 117 ? 0.2567 0.1876 0.1587 0.0000  -0.0372 0.0040  116  HIS A C   
929  O  O   . HIS A 117 ? 0.2591 0.1783 0.1676 -0.0188 -0.0216 -0.0077 116  HIS A O   
930  C  CB  . HIS A 117 ? 0.2468 0.1776 0.1610 -0.0952 -0.0203 0.0352  116  HIS A CB  
931  C  CG  . HIS A 117 ? 0.2965 0.1723 0.1720 -0.0878 -0.0070 0.0412  116  HIS A CG  
932  N  ND1 . HIS A 117 ? 0.3048 0.1770 0.1787 -0.0656 0.0123  0.0313  116  HIS A ND1 
933  C  CD2 . HIS A 117 ? 0.3433 0.1495 0.1835 -0.0939 -0.0022 0.0408  116  HIS A CD2 
934  C  CE1 . HIS A 117 ? 0.3639 0.1668 0.2032 -0.0434 -0.0190 -0.0004 116  HIS A CE1 
935  N  NE2 . HIS A 117 ? 0.3165 0.1845 0.1793 -0.0516 -0.0302 0.0103  116  HIS A NE2 
936  N  N   . ALA A 118 ? 0.3007 0.2076 0.1481 0.0450  -0.0307 0.0125  117  ALA A N   
937  C  CA  . ALA A 118 ? 0.3223 0.2065 0.1638 0.0815  -0.0145 -0.0257 117  ALA A CA  
938  C  C   . ALA A 118 ? 0.2710 0.2094 0.1743 0.0288  -0.0368 -0.0263 117  ALA A C   
939  O  O   . ALA A 118 ? 0.2041 0.2059 0.1900 0.0220  -0.0090 -0.0419 117  ALA A O   
940  C  CB  . ALA A 118 ? 0.2831 0.2083 0.1372 0.0747  0.0299  -0.0542 117  ALA A CB  
941  N  N   A MET A 119 ? 0.2712 0.2068 0.1806 0.0155  -0.0430 -0.0305 118  MET A N   
942  N  N   B MET A 119 ? 0.2912 0.2214 0.1810 0.0342  -0.0207 -0.0200 118  MET A N   
943  C  CA  A MET A 119 ? 0.2341 0.2186 0.1876 -0.0236 0.0041  -0.0137 118  MET A CA  
944  C  CA  B MET A 119 ? 0.2780 0.2412 0.1859 0.0200  0.0254  -0.0025 118  MET A CA  
945  C  C   A MET A 119 ? 0.2330 0.2057 0.1611 -0.0088 -0.0149 -0.0172 118  MET A C   
946  C  C   B MET A 119 ? 0.2520 0.2177 0.1686 0.0267  0.0159  0.0001  118  MET A C   
947  O  O   A MET A 119 ? 0.2188 0.2036 0.1511 0.0101  -0.0394 -0.0431 118  MET A O   
948  O  O   B MET A 119 ? 0.2460 0.2104 0.1725 0.0747  0.0277  -0.0088 118  MET A O   
949  C  CB  A MET A 119 ? 0.2545 0.2437 0.2311 0.0080  -0.0073 -0.0171 118  MET A CB  
950  C  CB  B MET A 119 ? 0.3420 0.2827 0.2148 0.0551  0.0371  -0.0048 118  MET A CB  
951  C  CG  A MET A 119 ? 0.2309 0.2615 0.2737 0.0223  -0.0049 -0.0055 118  MET A CG  
952  C  CG  B MET A 119 ? 0.3640 0.3135 0.2291 0.0933  0.0531  0.0029  118  MET A CG  
953  S  SD  A MET A 119 ? 0.2468 0.2557 0.3051 0.0160  0.0063  -0.0069 118  MET A SD  
954  S  SD  B MET A 119 ? 0.4378 0.3322 0.2542 0.1392  0.0876  0.0052  118  MET A SD  
955  C  CE  A MET A 119 ? 0.2785 0.2653 0.3175 0.0000  -0.0268 -0.0209 118  MET A CE  
956  C  CE  B MET A 119 ? 0.3997 0.3374 0.2420 0.1293  0.0465  -0.0015 118  MET A CE  
957  N  N   . MET A 120 ? 0.2091 0.1995 0.1434 0.0079  0.0168  0.0082  119  MET A N   
958  C  CA  . MET A 120 ? 0.1517 0.1731 0.1027 0.0156  -0.0168 -0.0056 119  MET A CA  
959  C  C   . MET A 120 ? 0.1922 0.1692 0.1341 -0.0033 -0.0466 -0.0116 119  MET A C   
960  O  O   . MET A 120 ? 0.2131 0.1971 0.1241 0.0134  -0.0370 -0.0012 119  MET A O   
961  C  CB  . MET A 120 ? 0.2443 0.1897 0.1171 0.0206  -0.0184 -0.0016 119  MET A CB  
962  C  CG  . MET A 120 ? 0.3102 0.1973 0.0940 -0.0038 -0.0241 -0.0394 119  MET A CG  
963  S  SD  . MET A 120 ? 0.2541 0.2281 0.1440 -0.0166 -0.0452 -0.0286 119  MET A SD  
964  C  CE  . MET A 120 ? 0.2651 0.1849 0.1346 -0.0382 -0.0442 -0.0670 119  MET A CE  
965  N  N   . VAL A 121 ? 0.2438 0.1377 0.1428 0.0333  -0.0564 -0.0202 120  VAL A N   
966  C  CA  . VAL A 121 ? 0.2528 0.1300 0.1618 -0.0101 -0.0536 -0.0055 120  VAL A CA  
967  C  C   . VAL A 121 ? 0.1485 0.1897 0.1605 0.0047  -0.0053 -0.0005 120  VAL A C   
968  O  O   . VAL A 121 ? 0.1563 0.2119 0.1838 0.0119  -0.0098 0.0220  120  VAL A O   
969  C  CB  . VAL A 121 ? 0.3280 0.1367 0.1400 -0.0255 -0.0397 0.0037  120  VAL A CB  
970  C  CG1 . VAL A 121 ? 0.2971 0.1628 0.1497 -0.0778 -0.0311 -0.0072 120  VAL A CG1 
971  C  CG2 . VAL A 121 ? 0.3199 0.1498 0.1606 -0.0187 -0.0306 0.0122  120  VAL A CG2 
972  N  N   . ASP A 122 ? 0.2355 0.1773 0.1355 0.0104  0.0011  0.0129  121  ASP A N   
973  C  CA  . ASP A 122 ? 0.2403 0.1880 0.1218 0.0299  -0.0012 0.0090  121  ASP A CA  
974  C  C   . ASP A 122 ? 0.2419 0.1800 0.1242 0.0532  0.0058  0.0208  121  ASP A C   
975  O  O   . ASP A 122 ? 0.2769 0.1561 0.1454 0.0244  -0.0172 0.0407  121  ASP A O   
976  C  CB  . ASP A 122 ? 0.2685 0.2229 0.1195 0.0301  0.0157  -0.0011 121  ASP A CB  
977  C  CG  . ASP A 122 ? 0.1802 0.2322 0.1520 0.0198  0.0177  -0.0195 121  ASP A CG  
978  O  OD1 . ASP A 122 ? 0.2058 0.2038 0.1613 0.0232  -0.0102 0.0034  121  ASP A OD1 
979  O  OD2 . ASP A 122 ? 0.2559 0.2473 0.1478 0.0162  0.0277  -0.0282 121  ASP A OD2 
980  N  N   . ILE A 123 ? 0.2011 0.1759 0.1218 0.0226  0.0168  0.0005  122  ILE A N   
981  C  CA  . ILE A 123 ? 0.1546 0.1849 0.1356 0.0018  -0.0103 -0.0023 122  ILE A CA  
982  C  C   . ILE A 123 ? 0.2149 0.2019 0.1423 -0.0385 -0.0134 0.0161  122  ILE A C   
983  O  O   . ILE A 123 ? 0.1802 0.1967 0.1223 -0.0349 -0.0303 0.0105  122  ILE A O   
984  C  CB  . ILE A 123 ? 0.1374 0.1828 0.1366 -0.0342 -0.0228 -0.0018 122  ILE A CB  
985  C  CG1 . ILE A 123 ? 0.1484 0.2209 0.1346 -0.0565 -0.0544 0.0121  122  ILE A CG1 
986  C  CG2 . ILE A 123 ? 0.2351 0.1683 0.1406 -0.0323 -0.0197 0.0000  122  ILE A CG2 
987  C  CD1 . ILE A 123 ? 0.1487 0.2005 0.1536 -0.0785 -0.0087 0.0159  122  ILE A CD1 
988  N  N   . ALA A 124 ? 0.1779 0.1899 0.1412 -0.0700 0.0193  0.0327  123  ALA A N   
989  C  CA  . ALA A 124 ? 0.1894 0.1965 0.1391 -0.0598 -0.0226 0.0272  123  ALA A CA  
990  C  C   . ALA A 124 ? 0.2287 0.2167 0.1239 -0.0054 -0.0384 -0.0114 123  ALA A C   
991  O  O   . ALA A 124 ? 0.1637 0.2014 0.1676 -0.0015 -0.0385 -0.0267 123  ALA A O   
992  C  CB  . ALA A 124 ? 0.2769 0.1856 0.1295 -0.0280 -0.0722 0.0477  123  ALA A CB  
993  N  N   . VAL A 125 ? 0.2672 0.1800 0.1169 -0.0128 -0.0294 -0.0187 124  VAL A N   
994  C  CA  . VAL A 125 ? 0.2369 0.2030 0.0974 0.0264  -0.0503 0.0033  124  VAL A CA  
995  C  C   . VAL A 125 ? 0.1983 0.2105 0.1322 0.0035  -0.0414 0.0073  124  VAL A C   
996  O  O   . VAL A 125 ? 0.1752 0.2202 0.1535 -0.0006 -0.0544 0.0008  124  VAL A O   
997  C  CB  . VAL A 125 ? 0.2993 0.2171 0.0951 0.0447  -0.0123 0.0104  124  VAL A CB  
998  C  CG1 . VAL A 125 ? 0.2335 0.2394 0.1163 -0.0102 -0.0657 -0.0070 124  VAL A CG1 
999  C  CG2 . VAL A 125 ? 0.3225 0.2242 0.1044 0.0242  -0.0492 0.0326  124  VAL A CG2 
1000 N  N   . GLN A 126 ? 0.2271 0.2037 0.1403 0.0135  -0.0018 0.0098  125  GLN A N   
1001 C  CA  . GLN A 126 ? 0.1197 0.1857 0.1261 -0.0075 0.0119  0.0166  125  GLN A CA  
1002 C  C   . GLN A 126 ? 0.1499 0.2271 0.1191 -0.0262 -0.0324 0.0183  125  GLN A C   
1003 O  O   . GLN A 126 ? 0.1810 0.2199 0.1184 -0.0305 -0.0334 0.0248  125  GLN A O   
1004 C  CB  . GLN A 126 ? 0.0749 0.2310 0.1386 -0.0012 0.0372  0.0000  125  GLN A CB  
1005 C  CG  . GLN A 126 ? 0.1392 0.2351 0.1271 0.0066  0.0078  -0.0117 125  GLN A CG  
1006 C  CD  . GLN A 126 ? 0.1815 0.2017 0.1250 0.0438  -0.0081 -0.0007 125  GLN A CD  
1007 O  OE1 . GLN A 126 ? 0.2013 0.2434 0.1352 0.0560  -0.0167 0.0061  125  GLN A OE1 
1008 N  NE2 . GLN A 126 ? 0.2154 0.1923 0.1282 0.0730  0.0209  -0.0246 125  GLN A NE2 
1009 N  N   . LEU A 127 ? 0.1508 0.2029 0.1086 -0.0092 -0.0049 -0.0175 126  LEU A N   
1010 C  CA  . LEU A 127 ? 0.1524 0.2256 0.1128 -0.0146 0.0113  -0.0131 126  LEU A CA  
1011 C  C   . LEU A 127 ? 0.2179 0.2361 0.1436 -0.0241 -0.0121 0.0225  126  LEU A C   
1012 O  O   . LEU A 127 ? 0.1988 0.2435 0.1182 -0.0503 -0.0002 0.0325  126  LEU A O   
1013 C  CB  . LEU A 127 ? 0.1684 0.2373 0.1215 0.0428  -0.0069 0.0071  126  LEU A CB  
1014 C  CG  . LEU A 127 ? 0.2375 0.2686 0.1308 0.0771  -0.0170 0.0129  126  LEU A CG  
1015 C  CD1 . LEU A 127 ? 0.1919 0.2991 0.1730 0.0402  -0.0207 -0.0023 126  LEU A CD1 
1016 C  CD2 . LEU A 127 ? 0.3233 0.2760 0.1499 0.1032  0.0191  0.0329  126  LEU A CD2 
1017 N  N   . VAL A 128 ? 0.1860 0.2294 0.1476 0.0112  -0.0349 0.0093  127  VAL A N   
1018 C  CA  . VAL A 128 ? 0.1913 0.2355 0.1433 -0.0805 -0.0295 0.0231  127  VAL A CA  
1019 C  C   . VAL A 128 ? 0.2175 0.2605 0.1287 -0.0647 -0.0262 0.0044  127  VAL A C   
1020 O  O   . VAL A 128 ? 0.1766 0.2819 0.1434 -0.0253 -0.0391 0.0144  127  VAL A O   
1021 C  CB  . VAL A 128 ? 0.1812 0.2278 0.1249 -0.0630 -0.0312 0.0483  127  VAL A CB  
1022 C  CG1 . VAL A 128 ? 0.2258 0.2437 0.1391 -0.0758 -0.0632 0.0270  127  VAL A CG1 
1023 C  CG2 . VAL A 128 ? 0.2709 0.2117 0.0947 -0.0341 -0.0168 0.0539  127  VAL A CG2 
1024 N  N   . GLN A 129 ? 0.2205 0.2392 0.1059 -0.0476 -0.0303 0.0111  128  GLN A N   
1025 C  CA  . GLN A 129 ? 0.1567 0.2479 0.1131 -0.0190 -0.0074 0.0180  128  GLN A CA  
1026 C  C   . GLN A 129 ? 0.1383 0.2453 0.1294 -0.0325 -0.0289 0.0173  128  GLN A C   
1027 O  O   . GLN A 129 ? 0.1724 0.2496 0.1646 -0.0108 -0.0259 0.0284  128  GLN A O   
1028 C  CB  . GLN A 129 ? 0.2034 0.2813 0.1292 0.0204  0.0208  0.0141  128  GLN A CB  
1029 C  CG  . GLN A 129 ? 0.2286 0.3285 0.1719 0.0693  0.0102  0.0133  128  GLN A CG  
1030 C  CD  . GLN A 129 ? 0.5404 0.3802 0.2682 0.0299  -0.0116 0.0021  128  GLN A CD  
1031 O  OE1 . GLN A 129 ? 0.6490 0.3848 0.3098 0.0251  0.0400  0.0233  128  GLN A OE1 
1032 N  NE2 . GLN A 129 ? 0.6138 0.3986 0.2689 0.0164  -0.0384 -0.0331 128  GLN A NE2 
1033 N  N   . LYS A 130 ? 0.1762 0.2308 0.1251 -0.0629 0.0078  0.0019  129  LYS A N   
1034 C  CA  . LYS A 130 ? 0.1678 0.2238 0.1503 -0.0710 0.0012  -0.0243 129  LYS A CA  
1035 C  C   . LYS A 130 ? 0.1295 0.2523 0.1313 -0.0648 -0.0003 0.0158  129  LYS A C   
1036 O  O   . LYS A 130 ? 0.1560 0.2774 0.1050 -0.0544 -0.0315 0.0214  129  LYS A O   
1037 C  CB  . LYS A 130 ? 0.1908 0.2052 0.1473 -0.0095 0.0284  -0.0446 129  LYS A CB  
1038 C  CG  . LYS A 130 ? 0.2038 0.1881 0.1439 -0.0819 0.0092  -0.0610 129  LYS A CG  
1039 C  CD  . LYS A 130 ? 0.2352 0.1745 0.1814 -0.0532 -0.0508 -0.0279 129  LYS A CD  
1040 C  CE  . LYS A 130 ? 0.2666 0.1820 0.1841 -0.0390 -0.0321 0.0118  129  LYS A CE  
1041 N  NZ  . LYS A 130 ? 0.3037 0.1868 0.2055 -0.0090 -0.0229 0.0420  129  LYS A NZ  
1042 N  N   . TRP A 131 ? 0.1367 0.2381 0.1260 -0.0518 0.0161  0.0245  130  TRP A N   
1043 C  CA  . TRP A 131 ? 0.1552 0.2362 0.1155 -0.0390 -0.0032 0.0406  130  TRP A CA  
1044 C  C   . TRP A 131 ? 0.2128 0.2467 0.1388 -0.0770 -0.0322 0.0425  130  TRP A C   
1045 O  O   . TRP A 131 ? 0.2519 0.2927 0.1534 -0.0828 -0.0574 0.0432  130  TRP A O   
1046 C  CB  . TRP A 131 ? 0.1467 0.2497 0.0933 -0.0394 -0.0083 0.0198  130  TRP A CB  
1047 C  CG  . TRP A 131 ? 0.1631 0.2208 0.1120 -0.0297 -0.0046 0.0278  130  TRP A CG  
1048 C  CD1 . TRP A 131 ? 0.1502 0.2094 0.1259 -0.0319 -0.0293 -0.0116 130  TRP A CD1 
1049 C  CD2 . TRP A 131 ? 0.1860 0.2027 0.0980 -0.0398 0.0212  0.0036  130  TRP A CD2 
1050 N  NE1 . TRP A 131 ? 0.1408 0.1977 0.1165 -0.0316 -0.0074 0.0088  130  TRP A NE1 
1051 C  CE2 . TRP A 131 ? 0.2141 0.2164 0.1084 -0.0421 0.0263  0.0337  130  TRP A CE2 
1052 C  CE3 . TRP A 131 ? 0.1526 0.2160 0.0899 -0.0040 -0.0134 0.0160  130  TRP A CE3 
1053 C  CZ2 . TRP A 131 ? 0.1661 0.2034 0.0988 -0.0126 0.0053  0.0728  130  TRP A CZ2 
1054 C  CZ3 . TRP A 131 ? 0.1983 0.2125 0.1209 0.0052  -0.0076 0.0076  130  TRP A CZ3 
1055 C  CH2 . TRP A 131 ? 0.2275 0.2109 0.1275 -0.0225 0.0250  0.0399  130  TRP A CH2 
1056 N  N   . GLU A 132 ? 0.1966 0.2370 0.1506 -0.0597 -0.0304 0.0405  131  GLU A N   
1057 C  CA  . GLU A 132 ? 0.1751 0.2373 0.1487 -0.0353 -0.0206 0.0341  131  GLU A CA  
1058 C  C   . GLU A 132 ? 0.1927 0.2441 0.1401 -0.0272 -0.0407 0.0116  131  GLU A C   
1059 O  O   . GLU A 132 ? 0.1863 0.2987 0.1538 -0.0525 -0.0350 0.0452  131  GLU A O   
1060 C  CB  . GLU A 132 ? 0.2526 0.2215 0.1681 -0.0386 -0.0271 0.0681  131  GLU A CB  
1061 C  CG  . GLU A 132 ? 0.3244 0.2344 0.1917 -0.0853 -0.0541 0.0813  131  GLU A CG  
1062 C  CD  . GLU A 132 ? 0.3912 0.2847 0.2168 -0.0442 -0.0347 0.0812  131  GLU A CD  
1063 O  OE1 . GLU A 132 ? 0.4149 0.3177 0.2111 -0.0565 -0.0186 0.0525  131  GLU A OE1 
1064 O  OE2 . GLU A 132 ? 0.3690 0.2729 0.2433 -0.0208 -0.0159 0.1069  131  GLU A OE2 
1065 N  N   . ARG A 133 ? 0.1807 0.2161 0.1105 -0.0325 0.0444  -0.0007 132  ARG A N   
1066 C  CA  . ARG A 133 ? 0.2163 0.2193 0.1280 -0.0211 0.0573  -0.0006 132  ARG A CA  
1067 C  C   . ARG A 133 ? 0.1911 0.2671 0.1098 -0.0210 0.0285  0.0010  132  ARG A C   
1068 O  O   . ARG A 133 ? 0.1831 0.2996 0.1147 -0.0245 -0.0369 0.0319  132  ARG A O   
1069 C  CB  . ARG A 133 ? 0.1583 0.2300 0.1395 -0.0041 0.0326  -0.0232 132  ARG A CB  
1070 C  CG  . ARG A 133 ? 0.1590 0.2115 0.1285 0.0041  0.0234  -0.0321 132  ARG A CG  
1071 C  CD  . ARG A 133 ? 0.1723 0.2373 0.1395 0.0235  0.0844  -0.0305 132  ARG A CD  
1072 N  NE  . ARG A 133 ? 0.1763 0.2823 0.1213 0.0192  0.0603  -0.0333 132  ARG A NE  
1073 C  CZ  . ARG A 133 ? 0.1721 0.2935 0.1380 0.0274  0.0391  -0.0352 132  ARG A CZ  
1074 N  NH1 . ARG A 133 ? 0.1519 0.2972 0.1158 -0.0007 -0.0136 -0.0217 132  ARG A NH1 
1075 N  NH2 . ARG A 133 ? 0.2415 0.3119 0.1654 0.0180  0.0041  -0.0346 132  ARG A NH2 
1076 N  N   . LEU A 134 ? 0.1689 0.2812 0.1283 -0.0389 -0.0146 -0.0256 133  LEU A N   
1077 C  CA  . LEU A 134 ? 0.1695 0.3200 0.1373 -0.0331 -0.0066 -0.0308 133  LEU A CA  
1078 C  C   . LEU A 134 ? 0.1757 0.3316 0.1607 -0.0419 -0.0088 -0.0049 133  LEU A C   
1079 O  O   . LEU A 134 ? 0.2184 0.3187 0.2047 -0.0730 -0.0266 0.0032  133  LEU A O   
1080 C  CB  . LEU A 134 ? 0.2349 0.3250 0.1341 -0.0367 -0.0075 -0.0308 133  LEU A CB  
1081 C  CG  . LEU A 134 ? 0.2507 0.3684 0.1135 -0.0615 -0.0175 -0.0213 133  LEU A CG  
1082 C  CD1 . LEU A 134 ? 0.2757 0.3886 0.1191 0.0005  -0.0163 -0.0449 133  LEU A CD1 
1083 C  CD2 . LEU A 134 ? 0.2368 0.3672 0.1182 -0.0714 -0.0207 -0.0260 133  LEU A CD2 
1084 N  N   . ASN A 135 ? 0.1526 0.3553 0.1521 0.0351  -0.0111 0.0144  134  ASN A N   
1085 C  CA  . ASN A 135 ? 0.1256 0.4051 0.1691 0.0037  0.0403  0.0143  134  ASN A CA  
1086 C  C   . ASN A 135 ? 0.1340 0.4588 0.2234 -0.0355 0.0406  -0.0208 134  ASN A C   
1087 O  O   . ASN A 135 ? 0.1997 0.4500 0.2241 -0.0852 0.0512  -0.0019 134  ASN A O   
1088 C  CB  . ASN A 135 ? 0.1817 0.4006 0.1734 0.0116  0.0527  0.0119  134  ASN A CB  
1089 C  CG  . ASN A 135 ? 0.2114 0.3806 0.1726 0.0195  0.0198  0.0159  134  ASN A CG  
1090 O  OD1 . ASN A 135 ? 0.1815 0.3836 0.1946 -0.0005 0.0131  -0.0007 134  ASN A OD1 
1091 N  ND2 . ASN A 135 ? 0.2103 0.3430 0.1890 0.0476  0.0324  0.0103  134  ASN A ND2 
1092 N  N   . ALA A 136 ? 0.1507 0.5158 0.2902 -0.0517 0.0410  -0.0730 135  ALA A N   
1093 C  CA  . ALA A 136 ? 0.1742 0.6178 0.3389 -0.0659 0.0094  -0.0984 135  ALA A CA  
1094 C  C   . ALA A 136 ? 0.2387 0.7291 0.3510 -0.0368 -0.0290 -0.1081 135  ALA A C   
1095 O  O   . ALA A 136 ? 0.2893 0.7473 0.3301 -0.0131 -0.0997 -0.0807 135  ALA A O   
1096 C  CB  . ALA A 136 ? 0.1910 0.6295 0.3860 -0.0876 0.0306  -0.1197 135  ALA A CB  
1097 N  N   . ASP A 137 ? 0.2008 0.7318 0.3810 -0.0461 -0.0090 -0.1292 136  ASP A N   
1098 C  CA  . ASP A 137 ? 0.2712 0.7863 0.4362 -0.0337 0.0287  -0.1125 136  ASP A CA  
1099 C  C   . ASP A 137 ? 0.2731 0.7074 0.4208 0.0055  0.0295  -0.1155 136  ASP A C   
1100 O  O   . ASP A 137 ? 0.2990 0.7267 0.4813 0.0383  0.0299  -0.1017 136  ASP A O   
1101 C  CB  . ASP A 137 ? 0.3619 0.8738 0.4967 -0.0610 0.0038  -0.0749 136  ASP A CB  
1102 C  CG  . ASP A 137 ? 0.4011 0.9461 0.5481 -0.0360 0.0324  -0.0450 136  ASP A CG  
1103 O  OD1 . ASP A 137 ? 0.4162 0.9856 0.5640 -0.0013 0.1130  -0.0572 136  ASP A OD1 
1104 O  OD2 . ASP A 137 ? 0.4474 0.9749 0.5761 -0.0397 0.0011  -0.0161 136  ASP A OD2 
1105 N  N   . GLU A 138 ? 0.2591 0.5909 0.3088 0.0067  0.0382  -0.1028 137  GLU A N   
1106 C  CA  . GLU A 138 ? 0.1937 0.4785 0.2224 0.0476  0.0236  -0.0451 137  GLU A CA  
1107 C  C   . GLU A 138 ? 0.2078 0.4188 0.1804 0.0116  -0.0462 -0.0110 137  GLU A C   
1108 O  O   . GLU A 138 ? 0.2832 0.4409 0.1998 -0.0732 0.0107  -0.0636 137  GLU A O   
1109 C  CB  . GLU A 138 ? 0.1827 0.4237 0.1732 0.0489  0.0210  -0.0213 137  GLU A CB  
1110 C  CG  . GLU A 138 ? 0.2690 0.4119 0.1564 0.0225  0.0001  0.0212  137  GLU A CG  
1111 C  CD  . GLU A 138 ? 0.3248 0.4077 0.1629 0.0186  -0.0644 0.0376  137  GLU A CD  
1112 O  OE1 . GLU A 138 ? 0.2736 0.3690 0.1576 0.0493  -0.0720 0.0659  137  GLU A OE1 
1113 O  OE2 . GLU A 138 ? 0.4902 0.4493 0.2139 -0.0196 -0.0642 -0.0004 137  GLU A OE2 
1114 N  N   . HIS A 139 ? 0.1783 0.3585 0.1713 0.0132  -0.0811 0.0270  138  HIS A N   
1115 C  CA  . HIS A 139 ? 0.1986 0.3951 0.1758 0.0391  -0.0612 0.0120  138  HIS A CA  
1116 C  C   . HIS A 139 ? 0.1880 0.3687 0.1605 0.0393  -0.0424 0.0137  138  HIS A C   
1117 O  O   . HIS A 139 ? 0.1840 0.3589 0.1633 0.0013  -0.0394 0.0118  138  HIS A O   
1118 C  CB  . HIS A 139 ? 0.2019 0.3862 0.2090 0.0605  -0.0146 0.0045  138  HIS A CB  
1119 C  CG  . HIS A 139 ? 0.1907 0.3783 0.2458 0.1034  -0.0413 0.0336  138  HIS A CG  
1120 N  ND1 . HIS A 139 ? 0.2771 0.3998 0.3149 0.1139  -0.0180 0.0312  138  HIS A ND1 
1121 C  CD2 . HIS A 139 ? 0.2596 0.3803 0.2548 0.0853  -0.0056 0.0275  138  HIS A CD2 
1122 C  CE1 . HIS A 139 ? 0.3512 0.4063 0.3237 0.0921  -0.0376 0.0387  138  HIS A CE1 
1123 N  NE2 . HIS A 139 ? 0.2931 0.3878 0.2810 0.0900  -0.0947 0.0511  138  HIS A NE2 
1124 N  N   . ILE A 140 ? 0.1531 0.3364 0.1353 0.0684  -0.0384 0.0203  139  ILE A N   
1125 C  CA  . ILE A 140 ? 0.1358 0.3225 0.1401 0.0429  -0.0064 0.0310  139  ILE A CA  
1126 C  C   . ILE A 140 ? 0.1164 0.3182 0.1698 0.0318  0.0079  0.0225  139  ILE A C   
1127 O  O   . ILE A 140 ? 0.0954 0.3338 0.1765 0.0308  0.0052  0.0383  139  ILE A O   
1128 C  CB  . ILE A 140 ? 0.1676 0.2694 0.1563 0.0265  -0.0229 0.0211  139  ILE A CB  
1129 C  CG1 . ILE A 140 ? 0.2330 0.2355 0.1413 0.0386  -0.0266 0.0054  139  ILE A CG1 
1130 C  CG2 . ILE A 140 ? 0.1796 0.2753 0.1508 0.0165  -0.0331 0.0451  139  ILE A CG2 
1131 C  CD1 . ILE A 140 ? 0.3125 0.2281 0.1551 0.0799  0.0155  0.0379  139  ILE A CD1 
1132 N  N   . GLU A 141 ? 0.1644 0.3022 0.1811 0.0322  -0.0234 0.0400  140  GLU A N   
1133 C  CA  . GLU A 141 ? 0.2060 0.2760 0.1639 0.0340  -0.0228 0.0652  140  GLU A CA  
1134 C  C   . GLU A 141 ? 0.1868 0.2434 0.1430 0.0394  -0.0080 0.0554  140  GLU A C   
1135 O  O   . GLU A 141 ? 0.1480 0.2448 0.1688 0.0382  -0.0484 0.0555  140  GLU A O   
1136 C  CB  . GLU A 141 ? 0.2111 0.2876 0.1922 0.0661  -0.0303 0.1050  140  GLU A CB  
1137 C  CG  . GLU A 141 ? 0.2094 0.3200 0.2532 0.0235  -0.0306 0.1414  140  GLU A CG  
1138 C  CD  . GLU A 141 ? 0.2829 0.3544 0.3584 0.0336  -0.0247 0.1711  140  GLU A CD  
1139 O  OE1 . GLU A 141 ? 0.2807 0.3667 0.3658 -0.0299 0.0307  0.1881  140  GLU A OE1 
1140 O  OE2 . GLU A 141 ? 0.3753 0.3533 0.4089 0.0393  0.0547  0.1778  140  GLU A OE2 
1141 N  N   . VAL A 142 ? 0.1689 0.2120 0.1018 0.0381  0.0006  0.0254  141  VAL A N   
1142 C  CA  . VAL A 142 ? 0.1745 0.2255 0.1160 -0.0015 -0.0046 0.0492  141  VAL A CA  
1143 C  C   . VAL A 142 ? 0.1661 0.2333 0.1248 0.0097  0.0035  0.0101  141  VAL A C   
1144 O  O   . VAL A 142 ? 0.1254 0.2489 0.1489 0.0308  -0.0163 0.0146  141  VAL A O   
1145 C  CB  . VAL A 142 ? 0.0767 0.2323 0.1350 -0.0346 -0.0255 0.0470  141  VAL A CB  
1146 C  CG1 . VAL A 142 ? 0.1879 0.2251 0.1509 0.0140  -0.0285 0.0771  141  VAL A CG1 
1147 C  CG2 . VAL A 142 ? 0.1155 0.2166 0.1456 -0.0631 -0.0221 0.0234  141  VAL A CG2 
1148 N  N   . PRO A 143 ? 0.1245 0.2520 0.1716 0.0384  0.0158  0.0215  142  PRO A N   
1149 C  CA  . PRO A 143 ? 0.1310 0.2467 0.1696 0.0340  0.0220  0.0091  142  PRO A CA  
1150 C  C   . PRO A 143 ? 0.1272 0.2435 0.1484 0.0135  0.0235  0.0176  142  PRO A C   
1151 O  O   . PRO A 143 ? 0.1258 0.2200 0.1345 -0.0027 0.0164  0.0074  142  PRO A O   
1152 C  CB  . PRO A 143 ? 0.1547 0.2269 0.1545 0.0879  0.0311  -0.0335 142  PRO A CB  
1153 C  CG  . PRO A 143 ? 0.1845 0.2445 0.1713 0.0415  -0.0008 -0.0070 142  PRO A CG  
1154 C  CD  . PRO A 143 ? 0.2047 0.2460 0.1647 0.0128  0.0085  0.0143  142  PRO A CD  
1155 N  N   . GLU A 144 ? 0.1441 0.2203 0.1360 0.0120  0.0232  0.0265  143  GLU A N   
1156 C  CA  . GLU A 144 ? 0.1406 0.2012 0.1372 0.0100  -0.0083 0.0463  143  GLU A CA  
1157 C  C   . GLU A 144 ? 0.1400 0.2027 0.1445 0.0184  -0.0255 0.0442  143  GLU A C   
1158 O  O   . GLU A 144 ? 0.1551 0.1954 0.1353 0.0253  -0.0199 0.0183  143  GLU A O   
1159 C  CB  . GLU A 144 ? 0.1796 0.2058 0.1672 0.0306  -0.0396 0.0519  143  GLU A CB  
1160 C  CG  . GLU A 144 ? 0.2308 0.2135 0.1978 0.0544  0.0144  0.0487  143  GLU A CG  
1161 C  CD  . GLU A 144 ? 0.2680 0.2001 0.2352 0.0171  0.0332  0.0305  143  GLU A CD  
1162 O  OE1 . GLU A 144 ? 0.1841 0.1988 0.2012 -0.0281 0.0155  0.0402  143  GLU A OE1 
1163 O  OE2 . GLU A 144 ? 0.3104 0.2173 0.2826 0.0349  0.1105  0.0129  143  GLU A OE2 
1164 N  N   . ASP A 145 ? 0.1488 0.2316 0.1340 0.0071  -0.0381 0.0524  144  ASP A N   
1165 C  CA  . ASP A 145 ? 0.1340 0.2226 0.1214 -0.0406 -0.0396 0.0030  144  ASP A CA  
1166 C  C   . ASP A 145 ? 0.1782 0.2198 0.0924 0.0004  -0.0149 0.0040  144  ASP A C   
1167 O  O   . ASP A 145 ? 0.1640 0.2096 0.1061 0.0004  -0.0249 0.0116  144  ASP A O   
1168 C  CB  . ASP A 145 ? 0.1271 0.2516 0.1381 -0.0518 -0.0572 0.0111  144  ASP A CB  
1169 C  CG  . ASP A 145 ? 0.1175 0.2869 0.1629 -0.0287 -0.0336 0.0222  144  ASP A CG  
1170 O  OD1 . ASP A 145 ? 0.1215 0.2806 0.1549 -0.0061 -0.0120 0.0239  144  ASP A OD1 
1171 O  OD2 . ASP A 145 ? 0.1496 0.2910 0.1623 0.0231  -0.0254 0.0111  144  ASP A OD2 
1172 N  N   . MET A 146 ? 0.1369 0.1953 0.0882 0.0429  -0.0361 0.0271  145  MET A N   
1173 C  CA  . MET A 146 ? 0.1097 0.2106 0.1055 0.0054  -0.0190 0.0232  145  MET A CA  
1174 C  C   . MET A 146 ? 0.1145 0.1735 0.1160 -0.0070 -0.0158 0.0105  145  MET A C   
1175 O  O   . MET A 146 ? 0.1228 0.1593 0.1498 0.0152  -0.0234 0.0016  145  MET A O   
1176 C  CB  . MET A 146 ? 0.1205 0.2047 0.1303 -0.0182 0.0680  0.0201  145  MET A CB  
1177 C  CG  . MET A 146 ? 0.1447 0.2528 0.1368 0.0145  0.0450  0.0111  145  MET A CG  
1178 S  SD  . MET A 146 ? 0.1934 0.2672 0.1531 0.0012  -0.0143 0.0082  145  MET A SD  
1179 C  CE  . MET A 146 ? 0.2438 0.3299 0.1646 0.0001  0.0181  -0.0287 145  MET A CE  
1180 N  N   . THR A 147 ? 0.1503 0.1325 0.1065 -0.0297 0.0157  0.0045  146  THR A N   
1181 C  CA  . THR A 147 ? 0.1572 0.1526 0.1337 -0.0371 -0.0330 -0.0097 146  THR A CA  
1182 C  C   . THR A 147 ? 0.1229 0.1736 0.1469 -0.0416 -0.0056 0.0042  146  THR A C   
1183 O  O   . THR A 147 ? 0.1241 0.1861 0.1573 0.0032  -0.0164 -0.0049 146  THR A O   
1184 C  CB  . THR A 147 ? 0.2052 0.1617 0.1831 0.0109  0.0364  -0.0355 146  THR A CB  
1185 O  OG1 . THR A 147 ? 0.3415 0.1650 0.1563 0.0579  -0.0338 -0.0386 146  THR A OG1 
1186 C  CG2 . THR A 147 ? 0.1965 0.1714 0.2326 0.0093  0.0332  -0.0258 146  THR A CG2 
1187 N  N   . ARG A 148 ? 0.1512 0.1962 0.1324 -0.0131 -0.0105 0.0269  147  ARG A N   
1188 C  CA  . ARG A 148 ? 0.1591 0.1971 0.1114 0.0494  -0.0126 0.0131  147  ARG A CA  
1189 C  C   . ARG A 148 ? 0.2111 0.1879 0.1180 0.0282  -0.0088 0.0109  147  ARG A C   
1190 O  O   . ARG A 148 ? 0.1829 0.1818 0.1419 -0.0024 -0.0098 0.0092  147  ARG A O   
1191 C  CB  . ARG A 148 ? 0.1874 0.2350 0.1256 0.0467  -0.0318 0.0275  147  ARG A CB  
1192 C  CG  . ARG A 148 ? 0.1673 0.2636 0.1328 0.0437  -0.0309 0.0294  147  ARG A CG  
1193 C  CD  . ARG A 148 ? 0.2083 0.2823 0.1414 0.0270  -0.0867 0.0255  147  ARG A CD  
1194 N  NE  . ARG A 148 ? 0.1772 0.2782 0.1650 0.0141  -0.0283 0.0131  147  ARG A NE  
1195 C  CZ  . ARG A 148 ? 0.2186 0.2654 0.1832 0.0590  -0.0097 0.0506  147  ARG A CZ  
1196 N  NH1 . ARG A 148 ? 0.2125 0.2666 0.1435 0.0394  0.0181  0.0238  147  ARG A NH1 
1197 N  NH2 . ARG A 148 ? 0.3239 0.2986 0.2067 0.0899  -0.0326 0.0698  147  ARG A NH2 
1198 N  N   . LEU A 149 ? 0.2324 0.1501 0.1343 -0.0166 -0.0085 0.0331  148  LEU A N   
1199 C  CA  . LEU A 149 ? 0.1692 0.1616 0.1520 -0.0307 -0.0018 0.0349  148  LEU A CA  
1200 C  C   . LEU A 149 ? 0.1909 0.1800 0.1068 -0.0074 0.0124  -0.0143 148  LEU A C   
1201 O  O   . LEU A 149 ? 0.1783 0.1850 0.1230 0.0408  0.0025  -0.0160 148  LEU A O   
1202 C  CB  . LEU A 149 ? 0.2049 0.1951 0.1796 -0.0363 0.0048  0.0298  148  LEU A CB  
1203 C  CG  . LEU A 149 ? 0.2663 0.1848 0.1838 -0.0338 0.0290  0.0085  148  LEU A CG  
1204 C  CD1 . LEU A 149 ? 0.2973 0.1926 0.1643 0.0194  0.0147  -0.0462 148  LEU A CD1 
1205 C  CD2 . LEU A 149 ? 0.4721 0.2268 0.2036 -0.0336 0.0152  -0.0363 148  LEU A CD2 
1206 N  N   . THR A 150 ? 0.1466 0.1855 0.1041 -0.0089 -0.0092 -0.0271 149  THR A N   
1207 C  CA  . THR A 150 ? 0.1150 0.2096 0.0972 -0.0195 -0.0408 -0.0064 149  THR A CA  
1208 C  C   . THR A 150 ? 0.1634 0.2221 0.1029 -0.0273 -0.0394 0.0151  149  THR A C   
1209 O  O   . THR A 150 ? 0.1365 0.2070 0.1048 -0.0337 -0.0059 -0.0239 149  THR A O   
1210 C  CB  . THR A 150 ? 0.1332 0.1795 0.1270 -0.0140 0.0222  -0.0023 149  THR A CB  
1211 O  OG1 . THR A 150 ? 0.1512 0.1416 0.1391 -0.0303 -0.0104 -0.0018 149  THR A OG1 
1212 C  CG2 . THR A 150 ? 0.1173 0.1871 0.1370 -0.0224 0.0184  -0.0205 149  THR A CG2 
1213 N  N   . LEU A 151 ? 0.1443 0.1940 0.0767 -0.0103 0.0210  -0.0023 150  LEU A N   
1214 C  CA  . LEU A 151 ? 0.2024 0.1648 0.1036 0.0050  0.0268  0.0233  150  LEU A CA  
1215 C  C   . LEU A 151 ? 0.1786 0.1558 0.1092 0.0249  -0.0206 -0.0094 150  LEU A C   
1216 O  O   . LEU A 151 ? 0.1862 0.1619 0.1248 0.0300  -0.0109 0.0036  150  LEU A O   
1217 C  CB  . LEU A 151 ? 0.1752 0.1343 0.1791 -0.0484 0.0167  0.0477  150  LEU A CB  
1218 C  CG  . LEU A 151 ? 0.2363 0.1578 0.2055 -0.0538 -0.0007 0.0549  150  LEU A CG  
1219 C  CD1 . LEU A 151 ? 0.1933 0.1697 0.2446 -0.0994 -0.0019 0.0448  150  LEU A CD1 
1220 C  CD2 . LEU A 151 ? 0.2490 0.1887 0.1943 -0.0915 0.0383  0.0469  150  LEU A CD2 
1221 N  N   . ASP A 152 ? 0.1559 0.2130 0.0914 0.0308  -0.0234 -0.0032 151  ASP A N   
1222 C  CA  . ASP A 152 ? 0.1089 0.2050 0.1055 0.0180  -0.0008 -0.0093 151  ASP A CA  
1223 C  C   . ASP A 152 ? 0.0654 0.1962 0.1142 0.0169  -0.0039 -0.0016 151  ASP A C   
1224 O  O   . ASP A 152 ? 0.1217 0.2467 0.1507 0.0433  -0.0188 -0.0077 151  ASP A O   
1225 C  CB  . ASP A 152 ? 0.1645 0.2379 0.1004 0.0236  -0.0123 0.0080  151  ASP A CB  
1226 C  CG  . ASP A 152 ? 0.2020 0.3054 0.1609 0.0421  -0.0172 0.0194  151  ASP A CG  
1227 O  OD1 . ASP A 152 ? 0.1679 0.3013 0.2209 0.0731  0.0574  0.1093  151  ASP A OD1 
1228 O  OD2 . ASP A 152 ? 0.1953 0.3826 0.1699 0.0930  -0.0058 0.0299  151  ASP A OD2 
1229 N  N   . THR A 153 ? 0.1347 0.1544 0.1241 0.0464  0.0290  0.0007  152  THR A N   
1230 C  CA  . THR A 153 ? 0.2288 0.1537 0.1448 0.0319  -0.0231 -0.0004 152  THR A CA  
1231 C  C   . THR A 153 ? 0.2114 0.1595 0.1413 0.0331  -0.0362 -0.0269 152  THR A C   
1232 O  O   . THR A 153 ? 0.1885 0.1682 0.1396 0.0363  -0.0579 -0.0232 152  THR A O   
1233 C  CB  . THR A 153 ? 0.1834 0.1214 0.1538 0.0018  -0.0248 0.0002  152  THR A CB  
1234 O  OG1 . THR A 153 ? 0.2215 0.1370 0.1663 -0.0301 0.0053  -0.0039 152  THR A OG1 
1235 C  CG2 . THR A 153 ? 0.2117 0.1307 0.1349 0.0130  -0.0543 -0.0106 152  THR A CG2 
1236 N  N   . ILE A 154 ? 0.1628 0.1606 0.1247 -0.0329 -0.0405 -0.0165 153  ILE A N   
1237 C  CA  . ILE A 154 ? 0.1251 0.2362 0.0859 -0.0034 -0.0044 -0.0365 153  ILE A CA  
1238 C  C   . ILE A 154 ? 0.1610 0.2422 0.0881 0.0020  -0.0139 -0.0347 153  ILE A C   
1239 O  O   . ILE A 154 ? 0.1578 0.2405 0.1243 0.0163  -0.0006 -0.0146 153  ILE A O   
1240 C  CB  . ILE A 154 ? 0.1511 0.2379 0.1122 0.0247  -0.0659 -0.0056 153  ILE A CB  
1241 C  CG1 . ILE A 154 ? 0.1692 0.2544 0.1212 0.0547  -0.0635 -0.0004 153  ILE A CG1 
1242 C  CG2 . ILE A 154 ? 0.1479 0.2525 0.1101 0.0806  -0.0313 0.0112  153  ILE A CG2 
1243 C  CD1 . ILE A 154 ? 0.2010 0.2783 0.1339 0.0582  -0.0775 -0.0220 153  ILE A CD1 
1244 N  N   . GLY A 155 ? 0.1541 0.2370 0.0916 0.0338  0.0111  -0.0574 154  GLY A N   
1245 C  CA  . GLY A 155 ? 0.2074 0.2278 0.1071 0.0568  0.0344  -0.0488 154  GLY A CA  
1246 C  C   . GLY A 155 ? 0.1885 0.2558 0.1136 0.0659  0.0342  -0.0443 154  GLY A C   
1247 O  O   . GLY A 155 ? 0.1789 0.2634 0.0992 0.0703  0.0131  -0.0092 154  GLY A O   
1248 N  N   . LEU A 156 ? 0.2020 0.2340 0.1347 0.0099  -0.0021 -0.0523 155  LEU A N   
1249 C  CA  . LEU A 156 ? 0.1909 0.2183 0.1375 0.0767  -0.0475 -0.0804 155  LEU A CA  
1250 C  C   . LEU A 156 ? 0.1919 0.2211 0.1367 0.0977  -0.0081 -0.0627 155  LEU A C   
1251 O  O   . LEU A 156 ? 0.2045 0.2527 0.1526 0.0773  0.0450  -0.0277 155  LEU A O   
1252 C  CB  . LEU A 156 ? 0.1564 0.2304 0.1552 0.0533  -0.0539 -0.0759 155  LEU A CB  
1253 C  CG  . LEU A 156 ? 0.1515 0.2216 0.1468 -0.0007 -0.0150 -0.0496 155  LEU A CG  
1254 C  CD1 . LEU A 156 ? 0.1789 0.2380 0.1616 0.0207  0.0343  -0.0163 155  LEU A CD1 
1255 C  CD2 . LEU A 156 ? 0.1575 0.2424 0.1673 -0.0018 -0.0518 -0.0568 155  LEU A CD2 
1256 N  N   . CYS A 157 ? 0.1960 0.2140 0.1288 0.0383  -0.0314 -0.0036 156  CYS A N   
1257 C  CA  . CYS A 157 ? 0.1718 0.2005 0.1710 0.0689  -0.0267 0.0147  156  CYS A CA  
1258 C  C   . CYS A 157 ? 0.1968 0.2231 0.1727 0.0880  -0.0036 0.0178  156  CYS A C   
1259 O  O   . CYS A 157 ? 0.1948 0.2502 0.1980 0.1149  -0.0159 -0.0094 156  CYS A O   
1260 C  CB  . CYS A 157 ? 0.1220 0.1853 0.1955 0.0258  0.0408  -0.0301 156  CYS A CB  
1261 S  SG  . CYS A 157 ? 0.2563 0.1790 0.2441 -0.0027 -0.0068 -0.0006 156  CYS A SG  
1262 N  N   . GLY A 158 ? 0.1859 0.2601 0.1641 0.0487  -0.0265 0.0193  157  GLY A N   
1263 C  CA  . GLY A 158 ? 0.1130 0.3043 0.1680 -0.0242 -0.0174 -0.0238 157  GLY A CA  
1264 C  C   . GLY A 158 ? 0.1502 0.3242 0.1575 0.0345  -0.0123 -0.0455 157  GLY A C   
1265 O  O   . GLY A 158 ? 0.1994 0.3912 0.1485 0.0477  -0.0277 -0.0261 157  GLY A O   
1266 N  N   . PHE A 159 ? 0.2165 0.2652 0.1737 0.0289  -0.0299 -0.0566 158  PHE A N   
1267 C  CA  . PHE A 159 ? 0.1890 0.2493 0.1757 0.0291  -0.0321 -0.0870 158  PHE A CA  
1268 C  C   . PHE A 159 ? 0.2041 0.2694 0.1902 0.0534  -0.0190 -0.0940 158  PHE A C   
1269 O  O   . PHE A 159 ? 0.2197 0.2778 0.1766 0.0340  -0.0638 -0.0967 158  PHE A O   
1270 C  CB  . PHE A 159 ? 0.2755 0.2408 0.1977 0.0160  -0.0274 -0.0692 158  PHE A CB  
1271 C  CG  . PHE A 159 ? 0.1898 0.2068 0.1884 0.0272  -0.0145 -0.0920 158  PHE A CG  
1272 C  CD1 . PHE A 159 ? 0.1390 0.1831 0.2124 -0.0086 -0.0182 -0.0530 158  PHE A CD1 
1273 C  CD2 . PHE A 159 ? 0.2300 0.2354 0.1900 0.0384  -0.0339 -0.0724 158  PHE A CD2 
1274 C  CE1 . PHE A 159 ? 0.1636 0.2069 0.2104 -0.0122 0.0129  -0.0488 158  PHE A CE1 
1275 C  CE2 . PHE A 159 ? 0.1918 0.2414 0.2224 -0.0035 -0.0560 -0.0709 158  PHE A CE2 
1276 C  CZ  . PHE A 159 ? 0.2075 0.2391 0.2289 0.0014  -0.0112 -0.0506 158  PHE A CZ  
1277 N  N   . ASN A 160 ? 0.1662 0.2852 0.2080 0.0427  -0.0493 -0.0859 159  ASN A N   
1278 C  CA  . ASN A 160 ? 0.1776 0.2970 0.1803 0.0659  0.0089  -0.0743 159  ASN A CA  
1279 C  C   . ASN A 160 ? 0.2104 0.2761 0.1868 0.0510  -0.0038 -0.0679 159  ASN A C   
1280 O  O   . ASN A 160 ? 0.2432 0.2884 0.1644 0.0267  -0.0201 -0.0553 159  ASN A O   
1281 C  CB  . ASN A 160 ? 0.2085 0.3488 0.1964 0.0604  0.0016  -0.1226 159  ASN A CB  
1282 C  CG  . ASN A 160 ? 0.2995 0.3987 0.2513 0.0569  0.0358  -0.1210 159  ASN A CG  
1283 O  OD1 . ASN A 160 ? 0.2752 0.3770 0.2506 0.0107  0.0193  -0.1251 159  ASN A OD1 
1284 N  ND2 . ASN A 160 ? 0.3517 0.4478 0.3068 0.0778  0.0126  -0.1361 159  ASN A ND2 
1285 N  N   . TYR A 161 ? 0.1829 0.2499 0.1663 0.0290  -0.0043 -0.0606 160  TYR A N   
1286 C  CA  . TYR A 161 ? 0.1308 0.2345 0.1588 -0.0132 -0.0254 -0.0359 160  TYR A CA  
1287 C  C   . TYR A 161 ? 0.1316 0.2503 0.1562 -0.0163 -0.0520 -0.0099 160  TYR A C   
1288 O  O   . TYR A 161 ? 0.1222 0.2838 0.1612 -0.0211 -0.0176 0.0044  160  TYR A O   
1289 C  CB  . TYR A 161 ? 0.1700 0.2310 0.1551 -0.0170 -0.0084 -0.0131 160  TYR A CB  
1290 C  CG  . TYR A 161 ? 0.2581 0.2434 0.1788 -0.0344 -0.0389 -0.0060 160  TYR A CG  
1291 C  CD1 . TYR A 161 ? 0.2566 0.2605 0.1965 -0.0642 -0.0219 -0.0245 160  TYR A CD1 
1292 C  CD2 . TYR A 161 ? 0.2861 0.2418 0.1922 -0.0381 -0.0453 -0.0070 160  TYR A CD2 
1293 C  CE1 . TYR A 161 ? 0.3293 0.2581 0.2069 -0.0308 0.0129  -0.0277 160  TYR A CE1 
1294 C  CE2 . TYR A 161 ? 0.3572 0.2387 0.2139 -0.0785 -0.0128 -0.0173 160  TYR A CE2 
1295 C  CZ  . TYR A 161 ? 0.4161 0.2577 0.2224 -0.0696 0.0074  -0.0156 160  TYR A CZ  
1296 O  OH  . TYR A 161 ? 0.4729 0.2429 0.2360 -0.1160 0.0086  -0.0372 160  TYR A OH  
1297 N  N   . ARG A 162 ? 0.1209 0.1867 0.1721 -0.0107 -0.0623 -0.0217 161  ARG A N   
1298 C  CA  . ARG A 162 ? 0.1398 0.1975 0.1604 0.0186  -0.0450 -0.0336 161  ARG A CA  
1299 C  C   . ARG A 162 ? 0.1292 0.2052 0.1546 0.0492  0.0056  -0.0158 161  ARG A C   
1300 O  O   . ARG A 162 ? 0.1617 0.2577 0.1690 0.0188  0.0060  -0.0175 161  ARG A O   
1301 C  CB  . ARG A 162 ? 0.1988 0.1831 0.1536 -0.0245 -0.0441 -0.0295 161  ARG A CB  
1302 C  CG  . ARG A 162 ? 0.2540 0.1702 0.1549 -0.0337 -0.0466 -0.0265 161  ARG A CG  
1303 C  CD  . ARG A 162 ? 0.2761 0.1751 0.1634 0.0024  -0.0302 0.0018  161  ARG A CD  
1304 N  NE  . ARG A 162 ? 0.2162 0.1988 0.1655 -0.0109 -0.0619 -0.0316 161  ARG A NE  
1305 C  CZ  . ARG A 162 ? 0.1943 0.1882 0.1373 0.0134  -0.0181 -0.0233 161  ARG A CZ  
1306 N  NH1 . ARG A 162 ? 0.1624 0.1885 0.1336 0.0138  -0.0321 -0.0400 161  ARG A NH1 
1307 N  NH2 . ARG A 162 ? 0.2193 0.1854 0.1672 0.0254  -0.0396 -0.0312 161  ARG A NH2 
1308 N  N   . PHE A 163 ? 0.1246 0.2291 0.1147 0.0403  0.0125  -0.0329 162  PHE A N   
1309 C  CA  . PHE A 163 ? 0.1593 0.2335 0.0924 0.0236  0.0223  -0.0546 162  PHE A CA  
1310 C  C   . PHE A 163 ? 0.1182 0.2570 0.1338 -0.0380 0.0131  -0.0317 162  PHE A C   
1311 O  O   . PHE A 163 ? 0.1640 0.2697 0.1687 0.0041  -0.0075 -0.0401 162  PHE A O   
1312 C  CB  . PHE A 163 ? 0.1799 0.2559 0.1046 0.0449  0.0072  -0.0673 162  PHE A CB  
1313 C  CG  . PHE A 163 ? 0.2065 0.2468 0.1604 0.0145  -0.0415 -0.0575 162  PHE A CG  
1314 C  CD1 . PHE A 163 ? 0.2843 0.2576 0.1929 -0.0163 -0.0964 -0.0332 162  PHE A CD1 
1315 C  CD2 . PHE A 163 ? 0.1852 0.2267 0.1620 0.0385  -0.0749 -0.0861 162  PHE A CD2 
1316 C  CE1 . PHE A 163 ? 0.3198 0.2568 0.2042 -0.0439 -0.0869 -0.0269 162  PHE A CE1 
1317 C  CE2 . PHE A 163 ? 0.1844 0.2373 0.1742 -0.0534 -0.0544 -0.0644 162  PHE A CE2 
1318 C  CZ  . PHE A 163 ? 0.2486 0.2519 0.2019 -0.0605 -0.0635 -0.0430 162  PHE A CZ  
1319 N  N   . ASN A 164 ? 0.1270 0.2558 0.1113 -0.0284 -0.0182 -0.0598 163  ASN A N   
1320 C  CA  . ASN A 164 ? 0.1144 0.2407 0.0953 -0.0095 0.0355  -0.0394 163  ASN A CA  
1321 C  C   . ASN A 164 ? 0.1924 0.2379 0.1078 0.0214  0.0275  -0.0117 163  ASN A C   
1322 O  O   . ASN A 164 ? 0.1665 0.2574 0.1019 0.0336  0.0029  -0.0204 163  ASN A O   
1323 C  CB  . ASN A 164 ? 0.1422 0.2471 0.1355 -0.0110 0.0435  -0.0542 163  ASN A CB  
1324 C  CG  . ASN A 164 ? 0.1120 0.2397 0.1370 -0.0154 0.0133  -0.0391 163  ASN A CG  
1325 O  OD1 . ASN A 164 ? 0.1763 0.2387 0.1583 -0.0111 0.0012  -0.0291 163  ASN A OD1 
1326 N  ND2 . ASN A 164 ? 0.1381 0.2395 0.1089 -0.0504 -0.0049 -0.0294 163  ASN A ND2 
1327 N  N   . SER A 165 ? 0.1717 0.2162 0.1126 0.0079  0.0493  -0.0083 164  SER A N   
1328 C  CA  . SER A 165 ? 0.1129 0.2460 0.1178 0.0111  0.0255  -0.0137 164  SER A CA  
1329 C  C   . SER A 165 ? 0.1517 0.2575 0.1431 -0.0111 -0.0134 0.0255  164  SER A C   
1330 O  O   . SER A 165 ? 0.1313 0.2729 0.1706 0.0368  -0.0011 0.0444  164  SER A O   
1331 C  CB  . SER A 165 ? 0.1588 0.2639 0.1077 -0.0004 0.0091  -0.0266 164  SER A CB  
1332 O  OG  . SER A 165 ? 0.1377 0.2599 0.1349 -0.0416 -0.0010 -0.0561 164  SER A OG  
1333 N  N   . PHE A 166 ? 0.1618 0.2440 0.1385 -0.0041 -0.0309 0.0229  165  PHE A N   
1334 C  CA  . PHE A 166 ? 0.1401 0.2610 0.1446 -0.0436 -0.0497 0.0411  165  PHE A CA  
1335 C  C   . PHE A 166 ? 0.2146 0.2884 0.1375 -0.0283 -0.0544 0.0215  165  PHE A C   
1336 O  O   . PHE A 166 ? 0.2611 0.3156 0.1560 -0.0673 -0.0562 0.0379  165  PHE A O   
1337 C  CB  . PHE A 166 ? 0.1735 0.2616 0.1502 0.0010  -0.0348 0.0125  165  PHE A CB  
1338 C  CG  . PHE A 166 ? 0.1616 0.2448 0.1414 -0.0057 0.0021  0.0169  165  PHE A CG  
1339 C  CD1 . PHE A 166 ? 0.1602 0.2420 0.1368 -0.0190 0.0159  0.0081  165  PHE A CD1 
1340 C  CD2 . PHE A 166 ? 0.1104 0.2246 0.1505 0.0136  -0.0131 0.0110  165  PHE A CD2 
1341 C  CE1 . PHE A 166 ? 0.2167 0.2335 0.1255 0.0095  -0.0052 -0.0038 165  PHE A CE1 
1342 C  CE2 . PHE A 166 ? 0.2160 0.2238 0.1429 -0.0044 -0.0148 -0.0068 165  PHE A CE2 
1343 C  CZ  . PHE A 166 ? 0.2232 0.2033 0.1280 -0.0386 0.0212  0.0128  165  PHE A CZ  
1344 N  N   . TYR A 167 ? 0.2125 0.2513 0.1328 0.0052  -0.0206 0.0241  166  TYR A N   
1345 C  CA  . TYR A 167 ? 0.2426 0.2480 0.1252 0.0444  -0.0043 0.0128  166  TYR A CA  
1346 C  C   . TYR A 167 ? 0.2280 0.2583 0.1606 0.0668  0.0015  0.0208  166  TYR A C   
1347 O  O   . TYR A 167 ? 0.3656 0.2458 0.1634 0.0235  0.0228  0.0302  166  TYR A O   
1348 C  CB  . TYR A 167 ? 0.2501 0.2122 0.1164 0.0388  0.0256  0.0305  166  TYR A CB  
1349 C  CG  . TYR A 167 ? 0.2250 0.1953 0.1262 0.0071  0.0195  0.0115  166  TYR A CG  
1350 C  CD1 . TYR A 167 ? 0.1520 0.2025 0.1412 -0.0129 -0.0018 -0.0006 166  TYR A CD1 
1351 C  CD2 . TYR A 167 ? 0.1362 0.1837 0.1474 0.0489  0.0119  -0.0283 166  TYR A CD2 
1352 C  CE1 . TYR A 167 ? 0.1607 0.2219 0.1168 -0.0426 -0.0154 -0.0496 166  TYR A CE1 
1353 C  CE2 . TYR A 167 ? 0.2062 0.1837 0.1383 0.0244  0.0386  -0.0379 166  TYR A CE2 
1354 C  CZ  . TYR A 167 ? 0.1732 0.2170 0.1419 -0.0353 0.0030  -0.0475 166  TYR A CZ  
1355 O  OH  . TYR A 167 ? 0.1716 0.2273 0.1569 -0.0022 0.0097  -0.0407 166  TYR A OH  
1356 N  N   . ARG A 168 ? 0.2278 0.2888 0.1691 0.1123  0.0226  -0.0344 167  ARG A N   
1357 C  CA  . ARG A 168 ? 0.1822 0.3391 0.2244 0.1201  -0.0454 -0.0249 167  ARG A CA  
1358 C  C   . ARG A 168 ? 0.2897 0.3795 0.2686 0.1784  -0.0619 0.0046  167  ARG A C   
1359 O  O   . ARG A 168 ? 0.3272 0.3903 0.2488 0.1397  0.0128  0.0381  167  ARG A O   
1360 C  CB  . ARG A 168 ? 0.2034 0.3394 0.2219 0.0507  -0.1003 0.0098  167  ARG A CB  
1361 C  CG  . ARG A 168 ? 0.2051 0.3512 0.2470 0.0418  -0.1249 0.0127  167  ARG A CG  
1362 C  CD  . ARG A 168 ? 0.2303 0.3804 0.3093 0.0166  -0.0624 -0.0246 167  ARG A CD  
1363 N  NE  . ARG A 168 ? 0.3389 0.3728 0.3297 0.0085  -0.0540 -0.0037 167  ARG A NE  
1364 C  CZ  . ARG A 168 ? 0.3946 0.4002 0.3511 0.0362  -0.0624 0.0120  167  ARG A CZ  
1365 N  NH1 . ARG A 168 ? 0.4190 0.3839 0.3651 0.0453  -0.0524 0.0353  167  ARG A NH1 
1366 N  NH2 . ARG A 168 ? 0.4026 0.4139 0.3445 0.0300  -0.0992 0.0046  167  ARG A NH2 
1367 N  N   . ASP A 169 ? 0.3946 0.4077 0.3213 0.2334  -0.0701 -0.0331 168  ASP A N   
1368 C  CA  . ASP A 169 ? 0.4932 0.4375 0.3758 0.2566  -0.1215 -0.0377 168  ASP A CA  
1369 C  C   . ASP A 169 ? 0.5803 0.4396 0.3818 0.2759  -0.1157 -0.0580 168  ASP A C   
1370 O  O   . ASP A 169 ? 0.6884 0.4566 0.3735 0.2333  -0.1195 -0.0926 168  ASP A O   
1371 C  CB  . ASP A 169 ? 0.5656 0.4664 0.4470 0.2726  -0.1413 -0.0384 168  ASP A CB  
1372 C  CG  . ASP A 169 ? 0.6607 0.5032 0.5185 0.2756  -0.1201 -0.0569 168  ASP A CG  
1373 O  OD1 . ASP A 169 ? 0.6832 0.5141 0.5283 0.1948  -0.1315 -0.0902 168  ASP A OD1 
1374 O  OD2 . ASP A 169 ? 0.7406 0.5625 0.5785 0.2392  -0.0686 -0.0530 168  ASP A OD2 
1375 N  N   . GLN A 170 ? 0.5791 0.4468 0.3900 0.2617  -0.1509 -0.0495 169  GLN A N   
1376 C  CA  . GLN A 170 ? 0.6329 0.4897 0.4408 0.1573  -0.1770 -0.0228 169  GLN A CA  
1377 C  C   . GLN A 170 ? 0.6421 0.4764 0.4093 0.0923  -0.1848 -0.0525 169  GLN A C   
1378 O  O   . GLN A 170 ? 0.6633 0.4685 0.4130 0.1053  -0.1504 -0.0720 169  GLN A O   
1379 C  CB  . GLN A 170 ? 0.7227 0.5448 0.4951 0.1071  -0.1603 0.0274  169  GLN A CB  
1380 C  CG  . GLN A 170 ? 0.7937 0.5998 0.5549 0.0900  -0.1375 0.0438  169  GLN A CG  
1381 C  CD  . GLN A 170 ? 0.8772 0.6607 0.6024 0.0895  -0.1180 0.0337  169  GLN A CD  
1382 O  OE1 . GLN A 170 ? 0.9126 0.6988 0.6152 0.0778  -0.1151 0.0404  169  GLN A OE1 
1383 N  NE2 . GLN A 170 ? 0.8877 0.6639 0.6217 0.0829  -0.1066 0.0153  169  GLN A NE2 
1384 N  N   . PRO A 171 ? 0.6643 0.4820 0.4001 0.0209  -0.1635 -0.0769 170  PRO A N   
1385 C  CA  . PRO A 171 ? 0.6703 0.4637 0.3790 -0.0131 -0.1764 -0.0867 170  PRO A CA  
1386 C  C   . PRO A 171 ? 0.6748 0.4105 0.3658 0.0245  -0.1614 -0.0724 170  PRO A C   
1387 O  O   . PRO A 171 ? 0.6703 0.3937 0.3434 -0.0187 -0.1694 -0.0388 170  PRO A O   
1388 C  CB  . PRO A 171 ? 0.6782 0.4957 0.3780 -0.0100 -0.1793 -0.0990 170  PRO A CB  
1389 C  CG  . PRO A 171 ? 0.6138 0.5091 0.3757 -0.0007 -0.1851 -0.1018 170  PRO A CG  
1390 C  CD  . PRO A 171 ? 0.6613 0.5035 0.3799 0.0045  -0.1593 -0.0984 170  PRO A CD  
1391 N  N   . HIS A 172 ? 0.6410 0.3542 0.3496 0.0539  -0.1710 -0.0762 171  HIS A N   
1392 C  CA  . HIS A 172 ? 0.6499 0.3323 0.3304 0.0924  -0.1563 -0.0800 171  HIS A CA  
1393 C  C   . HIS A 172 ? 0.6874 0.3393 0.2981 0.0541  -0.0780 -0.0411 171  HIS A C   
1394 O  O   . HIS A 172 ? 0.6276 0.3226 0.2809 0.0761  -0.0348 -0.0166 171  HIS A O   
1395 C  CB  . HIS A 172 ? 0.6323 0.3195 0.3234 0.1736  -0.1907 -0.0891 171  HIS A CB  
1396 C  CG  . HIS A 172 ? 0.7325 0.3346 0.3395 0.2112  -0.2235 -0.0815 171  HIS A CG  
1397 N  ND1 . HIS A 172 ? 0.7985 0.3212 0.3406 0.2076  -0.2108 -0.0763 171  HIS A ND1 
1398 C  CD2 . HIS A 172 ? 0.7223 0.3617 0.3443 0.2399  -0.2158 -0.0937 171  HIS A CD2 
1399 C  CE1 . HIS A 172 ? 0.7716 0.3391 0.3399 0.2249  -0.2011 -0.0984 171  HIS A CE1 
1400 N  NE2 . HIS A 172 ? 0.7731 0.3596 0.3377 0.2448  -0.2162 -0.0960 171  HIS A NE2 
1401 N  N   . PRO A 173 ? 0.7491 0.3419 0.2684 0.0191  -0.0031 0.0094  172  PRO A N   
1402 C  CA  . PRO A 173 ? 0.7227 0.3481 0.2679 0.0301  0.0115  0.0267  172  PRO A CA  
1403 C  C   . PRO A 173 ? 0.5901 0.3117 0.2922 0.0756  -0.0306 0.0287  172  PRO A C   
1404 O  O   . PRO A 173 ? 0.5343 0.2956 0.2822 0.0374  0.0000  0.0023  172  PRO A O   
1405 C  CB  . PRO A 173 ? 0.8226 0.3684 0.2751 0.0249  0.0245  0.0369  172  PRO A CB  
1406 C  CG  . PRO A 173 ? 0.8275 0.3653 0.2595 0.0278  0.0223  0.0268  172  PRO A CG  
1407 C  CD  . PRO A 173 ? 0.7835 0.3622 0.2542 0.0180  0.0419  0.0069  172  PRO A CD  
1408 N  N   . PHE A 174 ? 0.5377 0.2673 0.2862 0.1453  -0.0395 0.0353  173  PHE A N   
1409 C  CA  . PHE A 174 ? 0.4300 0.2967 0.2571 0.1877  -0.0770 0.0023  173  PHE A CA  
1410 C  C   . PHE A 174 ? 0.4709 0.3429 0.2817 0.0964  -0.0591 -0.0156 173  PHE A C   
1411 O  O   . PHE A 174 ? 0.5211 0.3744 0.2674 0.0295  -0.0104 -0.0548 173  PHE A O   
1412 C  CB  . PHE A 174 ? 0.5255 0.3098 0.2523 0.1916  -0.0975 0.0010  173  PHE A CB  
1413 C  CG  . PHE A 174 ? 0.6220 0.3542 0.2829 0.1888  -0.0996 -0.0180 173  PHE A CG  
1414 C  CD1 . PHE A 174 ? 0.5897 0.3658 0.2902 0.1688  -0.0933 -0.0292 173  PHE A CD1 
1415 C  CD2 . PHE A 174 ? 0.6892 0.3744 0.3157 0.1725  -0.1056 -0.0251 173  PHE A CD2 
1416 C  CE1 . PHE A 174 ? 0.6107 0.3695 0.2941 0.1071  -0.1189 -0.0381 173  PHE A CE1 
1417 C  CE2 . PHE A 174 ? 0.6320 0.3693 0.3096 0.1613  -0.1634 -0.0386 173  PHE A CE2 
1418 C  CZ  . PHE A 174 ? 0.6510 0.3715 0.3199 0.1045  -0.1440 -0.0553 173  PHE A CZ  
1419 N  N   . ILE A 175 ? 0.4454 0.3354 0.2974 0.1003  -0.0607 0.0100  174  ILE A N   
1420 C  CA  . ILE A 175 ? 0.4553 0.3191 0.3214 0.0560  -0.0845 0.0086  174  ILE A CA  
1421 C  C   . ILE A 175 ? 0.4496 0.3395 0.3242 0.0266  -0.1004 -0.0064 174  ILE A C   
1422 O  O   . ILE A 175 ? 0.3471 0.3659 0.3222 0.0021  -0.0740 -0.0265 174  ILE A O   
1423 C  CB  . ILE A 175 ? 0.5163 0.2838 0.3196 0.0715  -0.1182 0.0196  174  ILE A CB  
1424 C  CG1 . ILE A 175 ? 0.4991 0.2102 0.3278 0.0651  -0.1377 0.0237  174  ILE A CG1 
1425 C  CG2 . ILE A 175 ? 0.4606 0.3066 0.3095 0.0894  -0.1284 -0.0064 174  ILE A CG2 
1426 C  CD1 . ILE A 175 ? 0.4694 0.1886 0.3007 0.0187  -0.1813 0.0361  174  ILE A CD1 
1427 N  N   . THR A 176 ? 0.4955 0.3100 0.3280 0.0362  -0.1056 -0.0122 175  THR A N   
1428 C  CA  . THR A 176 ? 0.5140 0.2831 0.3170 0.0664  -0.1169 -0.0339 175  THR A CA  
1429 C  C   . THR A 176 ? 0.4562 0.2956 0.2786 0.0699  -0.0501 -0.0236 175  THR A C   
1430 O  O   . THR A 176 ? 0.4376 0.2775 0.3015 -0.0283 -0.0043 -0.0146 175  THR A O   
1431 C  CB  . THR A 176 ? 0.5965 0.2603 0.3436 0.0611  -0.1831 -0.0474 175  THR A CB  
1432 O  OG1 . THR A 176 ? 0.6441 0.2678 0.3567 0.0798  -0.1857 -0.0692 175  THR A OG1 
1433 C  CG2 . THR A 176 ? 0.6537 0.2831 0.3793 0.0564  -0.1425 -0.0404 175  THR A CG2 
1434 N  N   . SER A 177 ? 0.3673 0.3382 0.2457 0.0924  -0.0322 -0.0130 176  SER A N   
1435 C  CA  . SER A 177 ? 0.4333 0.3355 0.2215 0.0570  0.0612  -0.0252 176  SER A CA  
1436 C  C   . SER A 177 ? 0.4937 0.2818 0.1819 0.0311  0.0293  -0.0145 176  SER A C   
1437 O  O   . SER A 177 ? 0.5358 0.2367 0.1801 -0.0088 0.0338  -0.0250 176  SER A O   
1438 C  CB  . SER A 177 ? 0.4840 0.3787 0.2346 0.0448  0.1010  -0.0415 176  SER A CB  
1439 O  OG  . SER A 177 ? 0.5300 0.4022 0.2159 0.0599  0.1053  -0.0466 176  SER A OG  
1440 N  N   . MET A 178 ? 0.3736 0.2425 0.1797 0.0465  0.0072  -0.0014 177  MET A N   
1441 C  CA  . MET A 178 ? 0.3596 0.2199 0.2129 0.0769  0.0429  0.0187  177  MET A CA  
1442 C  C   . MET A 178 ? 0.3742 0.3084 0.2492 0.0311  0.0039  -0.0022 177  MET A C   
1443 O  O   . MET A 178 ? 0.3843 0.3471 0.2413 0.0152  -0.0113 0.0371  177  MET A O   
1444 C  CB  . MET A 178 ? 0.4116 0.2422 0.2341 0.0303  0.0151  0.0475  177  MET A CB  
1445 C  CG  . MET A 178 ? 0.3617 0.2372 0.2581 -0.0017 -0.0607 0.0339  177  MET A CG  
1446 S  SD  . MET A 178 ? 0.3651 0.2639 0.2939 0.0402  -0.0602 0.0224  177  MET A SD  
1447 C  CE  . MET A 178 ? 0.4184 0.2841 0.3030 0.0962  -0.0012 0.0349  177  MET A CE  
1448 N  N   . VAL A 179 ? 0.3942 0.3126 0.2422 0.0757  -0.0472 -0.0139 178  VAL A N   
1449 C  CA  . VAL A 179 ? 0.4479 0.3047 0.2739 0.0639  -0.0496 -0.0044 178  VAL A CA  
1450 C  C   . VAL A 179 ? 0.5126 0.3029 0.2741 0.0326  -0.0057 0.0044  178  VAL A C   
1451 O  O   . VAL A 179 ? 0.4331 0.3449 0.2823 0.0465  0.0375  -0.0076 178  VAL A O   
1452 C  CB  . VAL A 179 ? 0.3779 0.3160 0.2762 0.0488  -0.0727 -0.0082 178  VAL A CB  
1453 C  CG1 . VAL A 179 ? 0.3608 0.3405 0.2803 0.0469  -0.0554 -0.0075 178  VAL A CG1 
1454 C  CG2 . VAL A 179 ? 0.4480 0.3403 0.2728 0.0395  -0.0575 -0.0052 178  VAL A CG2 
1455 N  N   . ARG A 180 ? 0.5550 0.2764 0.2854 -0.0307 0.0106  0.0277  179  ARG A N   
1456 C  CA  . ARG A 180 ? 0.6080 0.2920 0.2863 0.0362  -0.0296 0.0655  179  ARG A CA  
1457 C  C   . ARG A 180 ? 0.6460 0.2689 0.2842 0.0490  -0.0547 0.0473  179  ARG A C   
1458 O  O   . ARG A 180 ? 0.6740 0.2419 0.2937 0.0494  -0.0627 0.0650  179  ARG A O   
1459 C  CB  . ARG A 180 ? 0.6609 0.3522 0.3019 0.0371  0.0349  0.1127  179  ARG A CB  
1460 C  CG  . ARG A 180 ? 0.7041 0.4377 0.3275 0.1095  0.0430  0.1460  179  ARG A CG  
1461 C  CD  . ARG A 180 ? 0.7895 0.5074 0.3623 0.1505  -0.0200 0.1330  179  ARG A CD  
1462 N  NE  . ARG A 180 ? 0.8234 0.5436 0.4020 0.1823  -0.0405 0.1197  179  ARG A NE  
1463 C  CZ  . ARG A 180 ? 0.8604 0.5706 0.4452 0.1688  -0.0609 0.1001  179  ARG A CZ  
1464 N  NH1 . ARG A 180 ? 0.8929 0.5805 0.4675 0.1240  -0.0699 0.0798  179  ARG A NH1 
1465 N  NH2 . ARG A 180 ? 0.8225 0.5892 0.4636 0.2088  -0.0669 0.0852  179  ARG A NH2 
1466 N  N   . ALA A 181 ? 0.5463 0.2804 0.2683 0.0629  -0.0047 0.0459  180  ALA A N   
1467 C  CA  . ALA A 181 ? 0.4666 0.2786 0.2381 0.0621  0.0452  0.0450  180  ALA A CA  
1468 C  C   . ALA A 181 ? 0.4124 0.2914 0.2231 0.0054  0.0636  0.0154  180  ALA A C   
1469 O  O   . ALA A 181 ? 0.4015 0.3211 0.2392 0.0009  -0.0031 -0.0015 180  ALA A O   
1470 C  CB  . ALA A 181 ? 0.4291 0.2908 0.2555 0.1291  0.0202  0.0666  180  ALA A CB  
1471 N  N   . LEU A 182 ? 0.3686 0.2664 0.2177 -0.0383 0.0756  -0.0246 181  LEU A N   
1472 C  CA  . LEU A 182 ? 0.3011 0.2294 0.2396 0.0133  0.0514  -0.0241 181  LEU A CA  
1473 C  C   . LEU A 182 ? 0.3492 0.2701 0.2693 0.0615  0.0305  -0.0224 181  LEU A C   
1474 O  O   . LEU A 182 ? 0.3656 0.3003 0.2742 -0.0082 0.0109  -0.0120 181  LEU A O   
1475 C  CB  . LEU A 182 ? 0.3326 0.2237 0.2372 -0.0410 0.0195  -0.0139 181  LEU A CB  
1476 C  CG  . LEU A 182 ? 0.3491 0.2353 0.2490 -0.0690 -0.0143 -0.0375 181  LEU A CG  
1477 C  CD1 . LEU A 182 ? 0.4346 0.2267 0.2341 -0.0445 0.0352  -0.0301 181  LEU A CD1 
1478 C  CD2 . LEU A 182 ? 0.3818 0.2446 0.2660 -0.0504 -0.0265 -0.0251 181  LEU A CD2 
1479 N  N   . ASP A 183 ? 0.3519 0.3063 0.2924 0.1037  -0.0410 0.0171  182  ASP A N   
1480 C  CA  . ASP A 183 ? 0.4444 0.3583 0.3318 0.0700  -0.0645 0.0062  182  ASP A CA  
1481 C  C   . ASP A 183 ? 0.4864 0.3121 0.3333 0.0124  -0.0682 0.0166  182  ASP A C   
1482 O  O   . ASP A 183 ? 0.5158 0.3231 0.3707 0.0230  -0.0362 0.0435  182  ASP A O   
1483 C  CB  . ASP A 183 ? 0.5487 0.4414 0.3663 0.1045  -0.1482 0.0039  182  ASP A CB  
1484 C  CG  . ASP A 183 ? 0.7608 0.5259 0.4247 0.1709  -0.1491 0.0148  182  ASP A CG  
1485 O  OD1 . ASP A 183 ? 0.8422 0.5571 0.4655 0.1879  -0.1553 0.0173  182  ASP A OD1 
1486 O  OD2 . ASP A 183 ? 0.8276 0.5671 0.4647 0.1834  -0.1638 0.0102  182  ASP A OD2 
1487 N  N   . GLU A 184 ? 0.3799 0.2936 0.3124 -0.0199 -0.0625 0.0405  183  GLU A N   
1488 C  CA  . GLU A 184 ? 0.4359 0.2961 0.3154 -0.0292 -0.1126 0.0375  183  GLU A CA  
1489 C  C   . GLU A 184 ? 0.4465 0.2993 0.2977 0.0351  -0.1380 0.0531  183  GLU A C   
1490 O  O   . GLU A 184 ? 0.4764 0.3129 0.3390 0.0736  -0.0869 0.0756  183  GLU A O   
1491 C  CB  . GLU A 184 ? 0.4356 0.3028 0.3354 -0.0455 -0.0675 0.0167  183  GLU A CB  
1492 C  CG  . GLU A 184 ? 0.4807 0.2844 0.3660 -0.0124 -0.0945 0.0074  183  GLU A CG  
1493 C  CD  . GLU A 184 ? 0.4943 0.2876 0.4020 0.0158  -0.0718 0.0194  183  GLU A CD  
1494 O  OE1 . GLU A 184 ? 0.5187 0.2745 0.4068 0.0269  -0.0443 0.0434  183  GLU A OE1 
1495 O  OE2 . GLU A 184 ? 0.4885 0.2751 0.4160 0.0255  -0.0475 -0.0062 183  GLU A OE2 
1496 N  N   . ALA A 185 ? 0.3632 0.2889 0.2576 0.0214  -0.0867 0.0256  184  ALA A N   
1497 C  CA  . ALA A 185 ? 0.3210 0.2496 0.2104 0.1006  0.0053  0.0270  184  ALA A CA  
1498 C  C   . ALA A 185 ? 0.4075 0.2868 0.2161 0.0216  0.0096  0.0153  184  ALA A C   
1499 O  O   . ALA A 185 ? 0.3809 0.2847 0.2180 -0.0198 -0.0184 -0.0318 184  ALA A O   
1500 C  CB  . ALA A 185 ? 0.3705 0.2292 0.1966 0.0956  0.0052  0.0105  184  ALA A CB  
1501 N  N   . MET A 186 ? 0.3085 0.3024 0.2202 0.0188  0.0195  0.0161  185  MET A N   
1502 C  CA  . MET A 186 ? 0.3579 0.3196 0.2481 -0.0245 0.0229  0.0178  185  MET A CA  
1503 C  C   . MET A 186 ? 0.3707 0.2582 0.2419 0.0545  0.0027  0.0343  185  MET A C   
1504 O  O   . MET A 186 ? 0.3790 0.2649 0.2329 0.0755  0.0138  0.0174  185  MET A O   
1505 C  CB  . MET A 186 ? 0.3367 0.3318 0.2587 -0.0561 0.0468  0.0256  185  MET A CB  
1506 C  CG  . MET A 186 ? 0.2495 0.3200 0.2484 -0.0253 0.0716  -0.0033 185  MET A CG  
1507 S  SD  . MET A 186 ? 0.3500 0.2763 0.2727 -0.0116 0.0624  0.0054  185  MET A SD  
1508 C  CE  . MET A 186 ? 0.4573 0.2786 0.3032 0.0763  0.0378  0.0229  185  MET A CE  
1509 N  N   . ASN A 187 ? 0.3909 0.2380 0.2839 0.1264  -0.0330 0.0683  186  ASN A N   
1510 C  CA  . ASN A 187 ? 0.3348 0.2250 0.3367 0.1171  -0.0514 0.0928  186  ASN A CA  
1511 C  C   . ASN A 187 ? 0.3828 0.2168 0.3609 0.0771  -0.0636 0.0550  186  ASN A C   
1512 O  O   . ASN A 187 ? 0.4357 0.2475 0.3763 0.0156  -0.0642 0.0388  186  ASN A O   
1513 C  CB  . ASN A 187 ? 0.3601 0.2736 0.3619 0.1049  -0.0438 0.1161  186  ASN A CB  
1514 C  CG  . ASN A 187 ? 0.4837 0.3244 0.4006 0.0941  0.0232  0.1093  186  ASN A CG  
1515 O  OD1 . ASN A 187 ? 0.5675 0.3329 0.3994 0.0743  0.0333  0.0987  186  ASN A OD1 
1516 N  ND2 . ASN A 187 ? 0.4553 0.3436 0.4264 0.1101  0.0402  0.1068  186  ASN A ND2 
1517 N  N   . LYS A 188 ? 0.3560 0.2199 0.3758 0.0356  -0.0375 0.0344  187  LYS A N   
1518 C  CA  . LYS A 188 ? 0.3423 0.2406 0.3783 0.0318  0.0000  0.0317  187  LYS A CA  
1519 C  C   . LYS A 188 ? 0.3628 0.2381 0.3516 0.0124  -0.0184 0.0110  187  LYS A C   
1520 O  O   . LYS A 188 ? 0.4242 0.2348 0.3632 0.0302  -0.0051 0.0151  187  LYS A O   
1521 C  CB  . LYS A 188 ? 0.3674 0.2846 0.4267 0.0562  0.1190  0.0216  187  LYS A CB  
1522 C  CG  . LYS A 188 ? 0.4650 0.3556 0.4892 0.1029  0.1368  0.0186  187  LYS A CG  
1523 C  CD  . LYS A 188 ? 0.4921 0.3918 0.5220 0.1048  0.1561  0.0082  187  LYS A CD  
1524 C  CE  . LYS A 188 ? 0.5927 0.4401 0.5667 0.0686  0.1118  0.0127  187  LYS A CE  
1525 N  NZ  . LYS A 188 ? 0.6384 0.4614 0.5963 0.0642  0.0888  0.0109  187  LYS A NZ  
1526 N  N   . LEU A 189 ? 0.3912 0.2369 0.3157 0.0024  -0.0241 0.0271  188  LEU A N   
1527 C  CA  . LEU A 189 ? 0.4187 0.2366 0.3442 0.0566  -0.0081 0.0088  188  LEU A CA  
1528 C  C   . LEU A 189 ? 0.4268 0.2481 0.4118 0.1135  0.0527  -0.0039 188  LEU A C   
1529 O  O   . LEU A 189 ? 0.4509 0.2568 0.4100 0.1586  0.0711  0.0031  188  LEU A O   
1530 C  CB  . LEU A 189 ? 0.3456 0.2289 0.3111 0.0594  -0.0495 0.0158  188  LEU A CB  
1531 C  CG  . LEU A 189 ? 0.3378 0.2426 0.3007 0.0481  -0.0486 0.0010  188  LEU A CG  
1532 C  CD1 . LEU A 189 ? 0.4293 0.2682 0.3084 0.0369  -0.0045 0.0298  188  LEU A CD1 
1533 C  CD2 . LEU A 189 ? 0.3732 0.2391 0.2886 0.0769  -0.0825 -0.0260 188  LEU A CD2 
1534 N  N   . GLN A 190 ? 0.4381 0.2622 0.4564 0.1193  0.1115  -0.0051 189  GLN A N   
1535 C  CA  . GLN A 190 ? 0.3781 0.2983 0.4865 0.1389  0.1589  -0.0137 189  GLN A CA  
1536 C  C   . GLN A 190 ? 0.3973 0.3344 0.5177 0.0991  0.1897  -0.0162 189  GLN A C   
1537 O  O   . GLN A 190 ? 0.4573 0.3838 0.5232 0.1168  0.1927  -0.0122 189  GLN A O   
1538 C  CB  . GLN A 190 ? 0.4252 0.3457 0.5290 0.1584  0.1717  -0.0269 189  GLN A CB  
1539 C  CG  . GLN A 190 ? 0.4794 0.4065 0.5580 0.1299  0.1400  -0.0163 189  GLN A CG  
1540 C  CD  . GLN A 190 ? 0.5384 0.4546 0.5715 0.1198  0.1802  -0.0057 189  GLN A CD  
1541 O  OE1 . GLN A 190 ? 0.5709 0.4862 0.5788 0.0572  0.2027  0.0049  189  GLN A OE1 
1542 N  NE2 . GLN A 190 ? 0.5871 0.4708 0.5796 0.1407  0.1378  0.0122  189  GLN A NE2 
1543 N  N   . ARG A 191 ? 0.3948 0.3269 0.5443 0.0394  0.2053  -0.0280 190  ARG A N   
1544 C  CA  . ARG A 191 ? 0.4820 0.3506 0.5821 0.0334  0.2117  -0.0404 190  ARG A CA  
1545 C  C   . ARG A 191 ? 0.6039 0.3525 0.6310 0.0107  0.2655  -0.0981 190  ARG A C   
1546 O  O   . ARG A 191 ? 0.6047 0.3530 0.6534 -0.0087 0.2992  -0.1203 190  ARG A O   
1547 C  CB  . ARG A 191 ? 0.5049 0.3754 0.5711 0.0620  0.1901  -0.0118 190  ARG A CB  
1548 C  CG  . ARG A 191 ? 0.5372 0.3819 0.5600 0.1235  0.1487  0.0170  190  ARG A CG  
1549 C  CD  . ARG A 191 ? 0.5051 0.3350 0.5320 0.1790  0.1314  0.0442  190  ARG A CD  
1550 N  NE  . ARG A 191 ? 0.5428 0.2960 0.5159 0.1463  0.0795  0.0770  190  ARG A NE  
1551 C  CZ  . ARG A 191 ? 0.5866 0.2492 0.4972 0.1160  0.0115  0.0388  190  ARG A CZ  
1552 N  NH1 . ARG A 191 ? 0.5527 0.2310 0.4892 0.0755  0.0027  0.0024  190  ARG A NH1 
1553 N  NH2 . ARG A 191 ? 0.6239 0.2749 0.5184 0.0636  -0.0738 0.0650  190  ARG A NH2 
1554 N  N   . ALA A 192 ? 0.6870 0.3805 0.6498 -0.0171 0.2888  -0.1226 191  ALA A N   
1555 C  CA  . ALA A 192 ? 0.7255 0.3941 0.6378 -0.0218 0.3359  -0.1495 191  ALA A CA  
1556 C  C   . ALA A 192 ? 0.7973 0.4346 0.6403 -0.0839 0.2794  -0.1224 191  ALA A C   
1557 O  O   . ALA A 192 ? 0.7938 0.4466 0.6231 -0.1027 0.2785  -0.1167 191  ALA A O   
1558 C  CB  . ALA A 192 ? 0.7167 0.3921 0.6379 0.0105  0.3113  -0.1513 191  ALA A CB  
1559 N  N   . ASN A 193 ? 0.7836 0.4534 0.6405 -0.0777 0.2408  -0.0996 192  ASN A N   
1560 C  CA  . ASN A 193 ? 0.7551 0.4767 0.6532 -0.0437 0.1680  -0.0852 192  ASN A CA  
1561 C  C   . ASN A 193 ? 0.6305 0.4784 0.6318 -0.0116 0.1256  -0.0900 192  ASN A C   
1562 O  O   . ASN A 193 ? 0.5963 0.4678 0.6296 0.0199  0.1148  -0.0888 192  ASN A O   
1563 C  CB  . ASN A 193 ? 0.8557 0.4844 0.6887 -0.0270 0.1321  -0.0754 192  ASN A CB  
1564 C  CG  . ASN A 193 ? 0.9733 0.4963 0.7324 -0.0676 0.0799  -0.0539 192  ASN A CG  
1565 O  OD1 . ASN A 193 ? 1.0581 0.5223 0.7632 -0.0341 0.0767  -0.0219 192  ASN A OD1 
1566 N  ND2 . ASN A 193 ? 0.9554 0.4598 0.7213 -0.1433 0.0435  -0.0880 192  ASN A ND2 
1567 N  N   . PRO A 194 ? 0.6297 0.4938 0.6245 -0.0252 0.0763  -0.0659 193  PRO A N   
1568 C  CA  . PRO A 194 ? 0.6445 0.5125 0.6115 -0.0295 0.0557  -0.0607 193  PRO A CA  
1569 C  C   . PRO A 194 ? 0.6504 0.5350 0.6099 -0.0741 0.0240  -0.0469 193  PRO A C   
1570 O  O   . PRO A 194 ? 0.6530 0.5411 0.5913 -0.0902 0.0165  -0.0419 193  PRO A O   
1571 C  CB  . PRO A 194 ? 0.6385 0.4995 0.6140 -0.0148 0.0472  -0.0606 193  PRO A CB  
1572 C  CG  . PRO A 194 ? 0.6304 0.5002 0.6217 0.0048  0.0345  -0.0620 193  PRO A CG  
1573 C  CD  . PRO A 194 ? 0.6193 0.4942 0.6192 -0.0203 0.0419  -0.0732 193  PRO A CD  
1574 N  N   . ASP A 195 ? 0.6942 0.5563 0.6292 -0.0905 0.0179  -0.0470 194  ASP A N   
1575 C  CA  . ASP A 195 ? 0.7256 0.5765 0.6540 -0.1154 -0.0231 -0.0604 194  ASP A CA  
1576 C  C   . ASP A 195 ? 0.7335 0.5478 0.6577 -0.1109 -0.0654 -0.0912 194  ASP A C   
1577 O  O   . ASP A 195 ? 0.7576 0.5335 0.6535 -0.1150 -0.0744 -0.1191 194  ASP A O   
1578 C  CB  . ASP A 195 ? 0.6871 0.6266 0.6687 -0.1263 -0.0138 -0.0538 194  ASP A CB  
1579 C  CG  . ASP A 195 ? 0.7096 0.6832 0.6835 -0.1187 0.0026  -0.0506 194  ASP A CG  
1580 O  OD1 . ASP A 195 ? 0.6937 0.7011 0.6913 -0.1011 0.0456  -0.0427 194  ASP A OD1 
1581 O  OD2 . ASP A 195 ? 0.7815 0.7124 0.6906 -0.1096 -0.0088 -0.0406 194  ASP A OD2 
1582 N  N   . ASP A 196 ? 0.7285 0.5358 0.6672 -0.0904 -0.0794 -0.0942 195  ASP A N   
1583 C  CA  . ASP A 196 ? 0.8046 0.5339 0.6874 -0.0588 -0.0538 -0.0710 195  ASP A CA  
1584 C  C   . ASP A 196 ? 0.8451 0.4980 0.6994 -0.0661 -0.0118 -0.0238 195  ASP A C   
1585 O  O   . ASP A 196 ? 0.8086 0.4800 0.6916 -0.0903 -0.0049 -0.0188 195  ASP A O   
1586 C  CB  . ASP A 196 ? 0.8356 0.5657 0.7059 -0.0522 -0.0436 -0.0771 195  ASP A CB  
1587 C  CG  . ASP A 196 ? 0.8770 0.5945 0.7293 -0.0357 -0.0465 -0.0795 195  ASP A CG  
1588 O  OD1 . ASP A 196 ? 0.9223 0.6040 0.7478 -0.0434 -0.0466 -0.0691 195  ASP A OD1 
1589 O  OD2 . ASP A 196 ? 0.8822 0.6125 0.7361 0.0099  -0.0327 -0.0817 195  ASP A OD2 
1590 N  N   . PRO A 197 ? 0.8829 0.4672 0.7139 -0.0950 -0.0122 0.0016  196  PRO A N   
1591 C  CA  . PRO A 197 ? 0.8899 0.4403 0.7151 -0.0928 -0.0124 0.0317  196  PRO A CA  
1592 C  C   . PRO A 197 ? 0.8511 0.3905 0.7165 -0.0430 -0.0143 0.0593  196  PRO A C   
1593 O  O   . PRO A 197 ? 0.8749 0.3632 0.7208 -0.0370 -0.0060 0.0708  196  PRO A O   
1594 C  CB  . PRO A 197 ? 0.9103 0.4650 0.7185 -0.1000 -0.0212 0.0214  196  PRO A CB  
1595 C  CG  . PRO A 197 ? 0.9002 0.4724 0.7196 -0.1053 -0.0146 0.0109  196  PRO A CG  
1596 C  CD  . PRO A 197 ? 0.8916 0.4757 0.7200 -0.1095 -0.0096 0.0043  196  PRO A CD  
1597 N  N   . ALA A 198 ? 0.7587 0.3675 0.7186 0.0106  -0.0104 0.0548  197  ALA A N   
1598 C  CA  . ALA A 198 ? 0.7526 0.3417 0.7221 0.0545  0.0058  0.0468  197  ALA A CA  
1599 C  C   . ALA A 198 ? 0.7310 0.3243 0.7171 0.0363  0.0090  0.0577  197  ALA A C   
1600 O  O   . ALA A 198 ? 0.7438 0.3206 0.7254 0.0093  -0.0105 0.0570  197  ALA A O   
1601 C  CB  . ALA A 198 ? 0.7424 0.3412 0.7255 0.0876  0.0167  0.0431  197  ALA A CB  
1602 N  N   . TYR A 199 ? 0.6490 0.3313 0.7124 0.0468  0.0573  0.0469  198  TYR A N   
1603 C  CA  . TYR A 199 ? 0.5894 0.3042 0.6973 0.0366  0.0865  0.0690  198  TYR A CA  
1604 C  C   . TYR A 199 ? 0.5745 0.3019 0.6526 -0.0381 0.0991  0.0668  198  TYR A C   
1605 O  O   . TYR A 199 ? 0.5582 0.2926 0.6406 -0.0761 0.1159  0.0382  198  TYR A O   
1606 C  CB  . TYR A 199 ? 0.6099 0.3254 0.7173 0.0790  0.1044  0.0766  198  TYR A CB  
1607 C  CG  . TYR A 199 ? 0.6571 0.3391 0.7372 0.1267  0.1068  0.0807  198  TYR A CG  
1608 C  CD1 . TYR A 199 ? 0.6654 0.3463 0.7480 0.1256  0.1164  0.0895  198  TYR A CD1 
1609 C  CD2 . TYR A 199 ? 0.6920 0.3647 0.7484 0.1222  0.0967  0.0880  198  TYR A CD2 
1610 C  CE1 . TYR A 199 ? 0.6966 0.3659 0.7617 0.1413  0.1057  0.0800  198  TYR A CE1 
1611 C  CE2 . TYR A 199 ? 0.7017 0.3722 0.7576 0.1571  0.1129  0.0691  198  TYR A CE2 
1612 C  CZ  . TYR A 199 ? 0.7204 0.3857 0.7715 0.1650  0.1113  0.0618  198  TYR A CZ  
1613 O  OH  . TYR A 199 ? 0.7930 0.4081 0.8008 0.1868  0.0759  0.0431  198  TYR A OH  
1614 N  N   . ASP A 200 ? 0.5874 0.3280 0.6298 -0.0507 0.1006  0.0907  199  ASP A N   
1615 C  CA  . ASP A 200 ? 0.6632 0.3431 0.6159 -0.0449 0.0802  0.1026  199  ASP A CA  
1616 C  C   . ASP A 200 ? 0.6775 0.3445 0.5905 -0.0219 0.0623  0.1053  199  ASP A C   
1617 O  O   . ASP A 200 ? 0.6781 0.3322 0.5857 -0.0237 0.0891  0.1024  199  ASP A O   
1618 C  CB  . ASP A 200 ? 0.7446 0.3452 0.6232 -0.0664 0.0748  0.1086  199  ASP A CB  
1619 C  CG  . ASP A 200 ? 0.8136 0.3505 0.6248 -0.0954 0.0804  0.1088  199  ASP A CG  
1620 O  OD1 . ASP A 200 ? 0.8248 0.3536 0.6132 -0.1571 0.1041  0.1199  199  ASP A OD1 
1621 O  OD2 . ASP A 200 ? 0.8571 0.3403 0.6326 -0.1110 0.0760  0.1110  199  ASP A OD2 
1622 N  N   . GLU A 201 ? 0.7426 0.3546 0.5736 0.0105  0.0316  0.1099  200  GLU A N   
1623 C  CA  . GLU A 201 ? 0.7649 0.3583 0.5464 0.0351  -0.0102 0.1050  200  GLU A CA  
1624 C  C   . GLU A 201 ? 0.7121 0.3170 0.4962 0.0835  -0.0080 0.1240  200  GLU A C   
1625 O  O   . GLU A 201 ? 0.7099 0.3518 0.4802 0.0979  -0.0080 0.1390  200  GLU A O   
1626 C  CB  . GLU A 201 ? 0.8239 0.3890 0.5685 0.0528  -0.0397 0.0951  200  GLU A CB  
1627 C  CG  . GLU A 201 ? 0.8561 0.4445 0.5919 0.0398  -0.0462 0.0767  200  GLU A CG  
1628 C  CD  . GLU A 201 ? 0.9285 0.4925 0.6086 0.0648  -0.0712 0.0653  200  GLU A CD  
1629 O  OE1 . GLU A 201 ? 0.9463 0.5049 0.6144 0.0456  -0.0542 0.0820  200  GLU A OE1 
1630 O  OE2 . GLU A 201 ? 0.9419 0.5065 0.6068 0.1331  -0.1112 0.0438  200  GLU A OE2 
1631 N  N   . ASN A 202 ? 0.6813 0.2905 0.4736 0.0731  0.0166  0.1112  201  ASN A N   
1632 C  CA  . ASN A 202 ? 0.7002 0.2955 0.4488 0.0385  0.0335  0.0844  201  ASN A CA  
1633 C  C   . ASN A 202 ? 0.7423 0.3099 0.3772 0.0533  0.0196  0.0430  201  ASN A C   
1634 O  O   . ASN A 202 ? 0.7530 0.3170 0.3687 0.0949  -0.0408 0.0382  201  ASN A O   
1635 C  CB  . ASN A 202 ? 0.6951 0.3156 0.5194 0.0545  0.0508  0.0723  201  ASN A CB  
1636 C  CG  . ASN A 202 ? 0.7559 0.3325 0.5802 0.0640  0.0903  0.0633  201  ASN A CG  
1637 O  OD1 . ASN A 202 ? 0.7835 0.3184 0.6096 0.0675  0.0867  0.0455  201  ASN A OD1 
1638 N  ND2 . ASN A 202 ? 0.7430 0.3503 0.5867 0.0559  0.1625  0.0799  201  ASN A ND2 
1639 N  N   . LYS A 203 ? 0.7291 0.3287 0.3141 0.0310  0.0489  -0.0182 202  LYS A N   
1640 C  CA  . LYS A 203 ? 0.7004 0.3626 0.3042 -0.0305 0.0400  -0.0300 202  LYS A CA  
1641 C  C   . LYS A 203 ? 0.7126 0.3841 0.2941 0.0186  -0.0204 -0.0092 202  LYS A C   
1642 O  O   . LYS A 203 ? 0.6920 0.3958 0.2932 0.0630  -0.0435 0.0090  202  LYS A O   
1643 C  CB  . LYS A 203 ? 0.7320 0.3862 0.3025 -0.0533 0.0504  -0.0680 202  LYS A CB  
1644 C  CG  . LYS A 203 ? 0.7902 0.4030 0.3254 -0.0888 0.0122  -0.0856 202  LYS A CG  
1645 C  CD  . LYS A 203 ? 0.8726 0.4532 0.3736 -0.0738 -0.0011 -0.0984 202  LYS A CD  
1646 C  CE  . LYS A 203 ? 0.9069 0.4781 0.4369 -0.0597 0.0066  -0.1234 202  LYS A CE  
1647 N  NZ  . LYS A 203 ? 0.9210 0.5091 0.4484 -0.0600 0.0168  -0.1309 202  LYS A NZ  
1648 N  N   . ARG A 204 ? 0.7374 0.3801 0.3194 0.0049  -0.0316 0.0309  203  ARG A N   
1649 C  CA  . ARG A 204 ? 0.7235 0.3913 0.3285 0.0430  -0.0202 0.0597  203  ARG A CA  
1650 C  C   . ARG A 204 ? 0.7538 0.3869 0.3323 0.0721  -0.0251 0.0861  203  ARG A C   
1651 O  O   . ARG A 204 ? 0.7961 0.3916 0.3405 0.0270  -0.0193 0.0902  203  ARG A O   
1652 C  CB  . ARG A 204 ? 0.7108 0.4413 0.3781 0.0577  -0.0291 0.0545  203  ARG A CB  
1653 C  CG  . ARG A 204 ? 0.7505 0.5036 0.4269 0.0314  -0.0678 0.0570  203  ARG A CG  
1654 C  CD  . ARG A 204 ? 0.8181 0.5703 0.4699 0.0144  -0.0923 0.0579  203  ARG A CD  
1655 N  NE  . ARG A 204 ? 0.9205 0.6319 0.5063 0.0188  -0.0921 0.0470  203  ARG A NE  
1656 C  CZ  . ARG A 204 ? 0.9814 0.6716 0.5268 0.0401  -0.0927 0.0390  203  ARG A CZ  
1657 N  NH1 . ARG A 204 ? 0.9996 0.6915 0.5342 0.0751  -0.0708 0.0461  203  ARG A NH1 
1658 N  NH2 . ARG A 204 ? 0.9685 0.6765 0.5335 0.0356  -0.1215 0.0332  203  ARG A NH2 
1659 N  N   . GLN A 205 ? 0.7747 0.3695 0.3391 0.0865  -0.0509 0.0814  204  GLN A N   
1660 C  CA  . GLN A 205 ? 0.7708 0.3574 0.3389 0.0957  -0.1079 0.0717  204  GLN A CA  
1661 C  C   . GLN A 205 ? 0.7832 0.3311 0.3270 0.1024  -0.1104 0.0671  204  GLN A C   
1662 O  O   . GLN A 205 ? 0.7941 0.3296 0.3320 0.1078  -0.1140 0.0797  204  GLN A O   
1663 C  CB  . GLN A 205 ? 0.7805 0.4017 0.3617 0.0725  -0.1395 0.0538  204  GLN A CB  
1664 C  CG  . GLN A 205 ? 0.7769 0.4618 0.3937 0.0937  -0.1250 0.0633  204  GLN A CG  
1665 C  CD  . GLN A 205 ? 0.7623 0.5100 0.3938 0.1177  -0.1370 0.0867  204  GLN A CD  
1666 O  OE1 . GLN A 205 ? 0.7889 0.5566 0.4129 0.1114  -0.1064 0.0658  204  GLN A OE1 
1667 N  NE2 . GLN A 205 ? 0.7063 0.5165 0.3795 0.1490  -0.1929 0.1038  204  GLN A NE2 
1668 N  N   . PHE A 206 ? 0.7654 0.3237 0.3112 0.1061  -0.1109 0.0709  205  PHE A N   
1669 C  CA  . PHE A 206 ? 0.7234 0.3216 0.2964 0.1045  -0.0568 0.0495  205  PHE A CA  
1670 C  C   . PHE A 206 ? 0.6825 0.3487 0.3023 0.0440  -0.0126 0.0302  205  PHE A C   
1671 O  O   . PHE A 206 ? 0.6177 0.3438 0.2813 0.0562  0.0206  0.0104  205  PHE A O   
1672 C  CB  . PHE A 206 ? 0.6990 0.3136 0.2950 0.0974  -0.0797 0.0463  205  PHE A CB  
1673 C  CG  . PHE A 206 ? 0.7076 0.3130 0.3018 0.1208  -0.0681 0.0322  205  PHE A CG  
1674 C  CD1 . PHE A 206 ? 0.7060 0.3014 0.2990 0.1394  -0.0612 -0.0103 205  PHE A CD1 
1675 C  CD2 . PHE A 206 ? 0.6264 0.3061 0.3176 0.1551  -0.0810 0.0375  205  PHE A CD2 
1676 C  CE1 . PHE A 206 ? 0.7046 0.3137 0.3201 0.1463  -0.0386 -0.0296 205  PHE A CE1 
1677 C  CE2 . PHE A 206 ? 0.6236 0.3076 0.3297 0.1575  -0.0445 0.0083  205  PHE A CE2 
1678 C  CZ  . PHE A 206 ? 0.6619 0.3144 0.3224 0.1848  -0.0050 -0.0118 205  PHE A CZ  
1679 N  N   . GLN A 207 ? 0.6680 0.3769 0.3300 -0.0178 -0.0035 0.0115  206  GLN A N   
1680 C  CA  . GLN A 207 ? 0.6870 0.4103 0.3588 -0.0117 -0.0156 0.0257  206  GLN A CA  
1681 C  C   . GLN A 207 ? 0.6598 0.4013 0.3444 0.0222  0.0187  0.0490  206  GLN A C   
1682 O  O   . GLN A 207 ? 0.6006 0.3717 0.3389 0.0660  0.0515  0.0265  206  GLN A O   
1683 C  CB  . GLN A 207 ? 0.7208 0.4622 0.4065 -0.0423 -0.0088 0.0478  206  GLN A CB  
1684 C  CG  . GLN A 207 ? 0.8302 0.5269 0.4666 0.0245  0.0169  0.0718  206  GLN A CG  
1685 C  CD  . GLN A 207 ? 0.9181 0.5947 0.5191 0.0746  0.0474  0.0669  206  GLN A CD  
1686 O  OE1 . GLN A 207 ? 0.9265 0.6343 0.5502 0.1122  0.0816  0.0726  206  GLN A OE1 
1687 N  NE2 . GLN A 207 ? 0.9460 0.6104 0.5209 0.0872  0.0441  0.0708  206  GLN A NE2 
1688 N  N   . GLU A 208 ? 0.6922 0.3973 0.3391 -0.0048 0.0023  0.0842  207  GLU A N   
1689 C  CA  . GLU A 208 ? 0.7081 0.3882 0.3531 -0.0038 -0.0143 0.0706  207  GLU A CA  
1690 C  C   . GLU A 208 ? 0.6696 0.3608 0.3227 0.0046  0.0492  0.0535  207  GLU A C   
1691 O  O   . GLU A 208 ? 0.5973 0.3256 0.3256 -0.0117 0.0552  0.0445  207  GLU A O   
1692 C  CB  . GLU A 208 ? 0.7700 0.4509 0.3979 0.0385  -0.0834 0.0723  207  GLU A CB  
1693 C  CG  . GLU A 208 ? 0.8756 0.5135 0.4779 0.0556  -0.0971 0.0578  207  GLU A CG  
1694 C  CD  . GLU A 208 ? 0.9879 0.5728 0.5524 0.0687  -0.1135 0.0386  207  GLU A CD  
1695 O  OE1 . GLU A 208 ? 1.0284 0.5577 0.5677 0.0398  -0.0913 0.0407  207  GLU A OE1 
1696 O  OE2 . GLU A 208 ? 1.0140 0.6201 0.5891 0.0836  -0.1171 0.0179  207  GLU A OE2 
1697 N  N   . ASP A 209 ? 0.6104 0.3394 0.2772 0.0172  0.0603  0.0543  208  ASP A N   
1698 C  CA  . ASP A 209 ? 0.5336 0.3496 0.2545 0.0417  0.0989  0.0335  208  ASP A CA  
1699 C  C   . ASP A 209 ? 0.5425 0.3153 0.2620 0.0442  0.0711  0.0094  208  ASP A C   
1700 O  O   . ASP A 209 ? 0.6217 0.2896 0.2588 0.0575  -0.0216 0.0079  208  ASP A O   
1701 C  CB  . ASP A 209 ? 0.5495 0.4001 0.2721 0.0983  0.0703  0.0347  208  ASP A CB  
1702 C  CG  . ASP A 209 ? 0.5538 0.4489 0.2758 0.0953  0.0500  0.0757  208  ASP A CG  
1703 O  OD1 . ASP A 209 ? 0.5471 0.4914 0.2888 0.0672  0.0781  0.1072  208  ASP A OD1 
1704 O  OD2 . ASP A 209 ? 0.6021 0.4433 0.2949 0.0669  0.0486  0.0979  208  ASP A OD2 
1705 N  N   . ILE A 210 ? 0.6010 0.2917 0.2816 0.0542  0.0322  -0.0016 209  ILE A N   
1706 C  CA  . ILE A 210 ? 0.6089 0.3001 0.2838 0.0279  0.0167  -0.0102 209  ILE A CA  
1707 C  C   . ILE A 210 ? 0.5775 0.3274 0.2836 -0.0411 0.0449  0.0090  209  ILE A C   
1708 O  O   . ILE A 210 ? 0.5812 0.3441 0.2683 -0.0380 0.0234  -0.0037 209  ILE A O   
1709 C  CB  . ILE A 210 ? 0.5774 0.2826 0.3045 0.0739  -0.0084 -0.0213 209  ILE A CB  
1710 C  CG1 . ILE A 210 ? 0.5774 0.2652 0.2872 0.0592  -0.0446 0.0017  209  ILE A CG1 
1711 C  CG2 . ILE A 210 ? 0.4753 0.2965 0.3351 0.0835  0.0175  -0.0353 209  ILE A CG2 
1712 C  CD1 . ILE A 210 ? 0.5269 0.2332 0.2842 -0.0041 -0.0804 0.0073  209  ILE A CD1 
1713 N  N   . LYS A 211 ? 0.6534 0.3218 0.2994 -0.0821 0.0121  0.0392  210  LYS A N   
1714 C  CA  . LYS A 211 ? 0.6338 0.3590 0.3112 -0.0778 0.0406  0.0354  210  LYS A CA  
1715 C  C   . LYS A 211 ? 0.6061 0.3627 0.3012 -0.0259 0.0408  0.0400  210  LYS A C   
1716 O  O   . LYS A 211 ? 0.6048 0.3711 0.3076 0.0073  0.0718  0.0189  210  LYS A O   
1717 C  CB  . LYS A 211 ? 0.6306 0.3941 0.3440 -0.1103 0.0526  0.0589  210  LYS A CB  
1718 C  CG  . LYS A 211 ? 0.6897 0.4460 0.3990 -0.0999 0.1181  0.0663  210  LYS A CG  
1719 C  CD  . LYS A 211 ? 0.7747 0.5036 0.4539 -0.0576 0.1374  0.0537  210  LYS A CD  
1720 C  CE  . LYS A 211 ? 0.7676 0.5265 0.4917 -0.0343 0.1752  0.0208  210  LYS A CE  
1721 N  NZ  . LYS A 211 ? 0.7752 0.5262 0.5078 -0.0605 0.1748  0.0185  210  LYS A NZ  
1722 N  N   . VAL A 212 ? 0.5791 0.3432 0.2832 -0.0064 -0.0056 0.0563  211  VAL A N   
1723 C  CA  . VAL A 212 ? 0.5484 0.3254 0.2760 0.0451  -0.0369 0.0266  211  VAL A CA  
1724 C  C   . VAL A 212 ? 0.6002 0.3104 0.2678 0.0402  0.0216  -0.0100 211  VAL A C   
1725 O  O   . VAL A 212 ? 0.6087 0.3074 0.2768 0.0498  0.0116  0.0048  211  VAL A O   
1726 C  CB  . VAL A 212 ? 0.5299 0.3148 0.2904 0.0829  -0.0287 0.0015  211  VAL A CB  
1727 C  CG1 . VAL A 212 ? 0.4955 0.3015 0.2986 0.1480  -0.0259 -0.0017 211  VAL A CG1 
1728 C  CG2 . VAL A 212 ? 0.5151 0.3043 0.2862 0.0974  -0.0060 -0.0119 211  VAL A CG2 
1729 N  N   . MET A 213 ? 0.5724 0.3157 0.2518 0.0907  -0.0044 -0.0246 212  MET A N   
1730 C  CA  . MET A 213 ? 0.5662 0.3387 0.2545 0.1475  0.0625  -0.0179 212  MET A CA  
1731 C  C   . MET A 213 ? 0.4959 0.3465 0.2546 0.1224  0.0639  -0.0317 212  MET A C   
1732 O  O   . MET A 213 ? 0.6042 0.3521 0.2346 0.0965  0.0713  -0.0703 212  MET A O   
1733 C  CB  . MET A 213 ? 0.6717 0.3633 0.2803 0.1372  0.0497  -0.0123 212  MET A CB  
1734 C  CG  . MET A 213 ? 0.7220 0.3914 0.2725 0.1124  0.1207  -0.0168 212  MET A CG  
1735 S  SD  . MET A 213 ? 0.7837 0.4278 0.3011 0.0766  0.0601  -0.0065 212  MET A SD  
1736 C  CE  . MET A 213 ? 0.8320 0.4344 0.3039 0.0284  -0.0383 -0.0158 212  MET A CE  
1737 N  N   . ASN A 214 ? 0.3808 0.3488 0.2602 0.0427  0.0808  -0.0276 213  ASN A N   
1738 C  CA  . ASN A 214 ? 0.3671 0.3852 0.3049 0.0099  0.0628  -0.0108 213  ASN A CA  
1739 C  C   . ASN A 214 ? 0.4830 0.3967 0.3361 -0.0386 0.0389  -0.0171 213  ASN A C   
1740 O  O   . ASN A 214 ? 0.4515 0.3917 0.3571 -0.0284 0.0228  -0.0644 213  ASN A O   
1741 C  CB  . ASN A 214 ? 0.3671 0.4245 0.3492 0.0239  0.0090  -0.0039 213  ASN A CB  
1742 C  CG  . ASN A 214 ? 0.4614 0.4848 0.4258 0.0551  -0.0143 -0.0252 213  ASN A CG  
1743 O  OD1 . ASN A 214 ? 0.5533 0.5279 0.4745 0.0574  -0.0343 -0.0310 213  ASN A OD1 
1744 N  ND2 . ASN A 214 ? 0.3604 0.4885 0.4171 0.0725  0.0073  -0.0398 213  ASN A ND2 
1745 N  N   . ASP A 215 ? 0.5715 0.3986 0.3236 -0.0975 0.0416  0.0239  214  ASP A N   
1746 C  CA  . ASP A 215 ? 0.6341 0.3884 0.3224 -0.0737 0.0535  0.0212  214  ASP A CA  
1747 C  C   . ASP A 215 ? 0.5454 0.3913 0.3102 -0.0734 0.0450  0.0235  214  ASP A C   
1748 O  O   . ASP A 215 ? 0.4664 0.3889 0.3221 -0.0736 0.0608  0.0181  214  ASP A O   
1749 C  CB  . ASP A 215 ? 0.7238 0.3864 0.3281 -0.0019 0.0656  0.0596  214  ASP A CB  
1750 C  CG  . ASP A 215 ? 0.8084 0.3938 0.3639 0.0117  0.0844  0.0628  214  ASP A CG  
1751 O  OD1 . ASP A 215 ? 0.8335 0.4090 0.3995 0.0254  0.1356  0.0532  214  ASP A OD1 
1752 O  OD2 . ASP A 215 ? 0.8711 0.3774 0.3778 0.0105  0.0893  0.0941  214  ASP A OD2 
1753 N  N   . LEU A 216 ? 0.4975 0.4126 0.2878 -0.0760 -0.0082 0.0084  215  LEU A N   
1754 C  CA  . LEU A 216 ? 0.4502 0.4042 0.2721 -0.0917 -0.0260 -0.0007 215  LEU A CA  
1755 C  C   . LEU A 216 ? 0.4692 0.3965 0.2535 -0.0678 -0.0229 -0.0340 215  LEU A C   
1756 O  O   . LEU A 216 ? 0.4583 0.3947 0.2402 -0.1003 -0.0101 -0.0643 215  LEU A O   
1757 C  CB  . LEU A 216 ? 0.4800 0.4058 0.2915 -0.1172 -0.0275 0.0157  215  LEU A CB  
1758 C  CG  . LEU A 216 ? 0.4959 0.4362 0.3172 -0.1427 -0.0260 0.0196  215  LEU A CG  
1759 C  CD1 . LEU A 216 ? 0.5722 0.4416 0.3188 -0.1318 -0.0139 -0.0012 215  LEU A CD1 
1760 C  CD2 . LEU A 216 ? 0.5233 0.4358 0.3185 -0.1417 -0.0340 0.0431  215  LEU A CD2 
1761 N  N   . VAL A 217 ? 0.5002 0.3852 0.2539 -0.0206 0.0219  -0.0602 216  VAL A N   
1762 C  CA  . VAL A 217 ? 0.5265 0.3990 0.2603 -0.0364 0.0085  -0.0516 216  VAL A CA  
1763 C  C   . VAL A 217 ? 0.5089 0.4287 0.3286 -0.0873 0.0416  -0.0117 216  VAL A C   
1764 O  O   . VAL A 217 ? 0.5189 0.4076 0.3303 -0.1044 0.0545  -0.0060 216  VAL A O   
1765 C  CB  . VAL A 217 ? 0.5105 0.3823 0.2486 -0.0466 0.0101  -0.0493 216  VAL A CB  
1766 C  CG1 . VAL A 217 ? 0.5089 0.3745 0.2437 -0.0777 0.0059  -0.0421 216  VAL A CG1 
1767 C  CG2 . VAL A 217 ? 0.4659 0.3659 0.2642 -0.0338 -0.0076 -0.0423 216  VAL A CG2 
1768 N  N   . ASP A 218 ? 0.5541 0.4389 0.3564 -0.1508 0.0494  -0.0004 217  ASP A N   
1769 C  CA  . ASP A 218 ? 0.6390 0.4600 0.3852 -0.1685 0.0442  -0.0104 217  ASP A CA  
1770 C  C   . ASP A 218 ? 0.6273 0.4392 0.3583 -0.1578 0.0355  -0.0129 217  ASP A C   
1771 O  O   . ASP A 218 ? 0.4816 0.4288 0.3407 -0.1026 0.0358  -0.0206 217  ASP A O   
1772 C  CB  . ASP A 218 ? 0.6543 0.5084 0.4536 -0.1923 0.0376  -0.0318 217  ASP A CB  
1773 C  CG  . ASP A 218 ? 0.7034 0.5537 0.5120 -0.1638 0.0352  -0.0454 217  ASP A CG  
1774 O  OD1 . ASP A 218 ? 0.7295 0.5838 0.5195 -0.1378 -0.0326 -0.0592 217  ASP A OD1 
1775 O  OD2 . ASP A 218 ? 0.6573 0.5567 0.5525 -0.1672 0.0651  -0.0447 217  ASP A OD2 
1776 N  N   . LYS A 219 ? 0.5807 0.4422 0.3475 -0.1326 0.0399  -0.0198 218  LYS A N   
1777 C  CA  . LYS A 219 ? 0.5686 0.4743 0.3146 -0.1253 0.0502  -0.0273 218  LYS A CA  
1778 C  C   . LYS A 219 ? 0.4639 0.4518 0.2933 -0.0884 0.0578  -0.0220 218  LYS A C   
1779 O  O   . LYS A 219 ? 0.4695 0.4668 0.3248 -0.0833 0.0483  -0.0128 218  LYS A O   
1780 C  CB  . LYS A 219 ? 0.6035 0.5139 0.3324 -0.1212 0.0450  -0.0271 218  LYS A CB  
1781 C  CG  . LYS A 219 ? 0.6729 0.5343 0.3698 -0.1297 0.0229  -0.0404 218  LYS A CG  
1782 C  CD  . LYS A 219 ? 0.7163 0.5542 0.3947 -0.1394 -0.0175 -0.0448 218  LYS A CD  
1783 C  CE  . LYS A 219 ? 0.6262 0.5462 0.4108 -0.1966 -0.0474 -0.0423 218  LYS A CE  
1784 N  NZ  . LYS A 219 ? 0.4108 0.5047 0.4100 -0.2628 -0.0417 -0.0230 218  LYS A NZ  
1785 N  N   . ILE A 220 ? 0.3796 0.4390 0.2334 -0.0626 0.0754  -0.0107 219  ILE A N   
1786 C  CA  . ILE A 220 ? 0.3450 0.4347 0.2333 -0.0246 0.0867  -0.0401 219  ILE A CA  
1787 C  C   . ILE A 220 ? 0.3621 0.4707 0.2649 -0.0004 0.0870  -0.0529 219  ILE A C   
1788 O  O   . ILE A 220 ? 0.3819 0.4967 0.2575 0.0466  0.0835  -0.0463 219  ILE A O   
1789 C  CB  . ILE A 220 ? 0.3342 0.4202 0.2270 -0.0811 0.1015  -0.0187 219  ILE A CB  
1790 C  CG1 . ILE A 220 ? 0.3026 0.4231 0.2061 -0.0714 0.0381  -0.0339 219  ILE A CG1 
1791 C  CG2 . ILE A 220 ? 0.3592 0.4222 0.2599 -0.1041 0.0186  -0.0278 219  ILE A CG2 
1792 C  CD1 . ILE A 220 ? 0.3348 0.4056 0.2177 -0.0601 0.0465  -0.0267 219  ILE A CD1 
1793 N  N   . ILE A 221 ? 0.3084 0.4851 0.3050 -0.0006 0.0343  -0.0887 220  ILE A N   
1794 C  CA  . ILE A 221 ? 0.2784 0.4945 0.3349 -0.0573 0.0216  -0.1014 220  ILE A CA  
1795 C  C   . ILE A 221 ? 0.3374 0.5385 0.3651 -0.0556 0.0657  -0.0653 220  ILE A C   
1796 O  O   . ILE A 221 ? 0.3707 0.5514 0.3776 -0.0318 0.0714  -0.0576 220  ILE A O   
1797 C  CB  . ILE A 221 ? 0.2526 0.4816 0.3595 -0.1126 0.0137  -0.1109 220  ILE A CB  
1798 C  CG1 . ILE A 221 ? 0.2394 0.4744 0.3611 -0.1493 0.0184  -0.1226 220  ILE A CG1 
1799 C  CG2 . ILE A 221 ? 0.3516 0.4864 0.3783 -0.0735 -0.0703 -0.1104 220  ILE A CG2 
1800 C  CD1 . ILE A 221 ? 0.2679 0.4859 0.4032 -0.1659 -0.0137 -0.1069 220  ILE A CD1 
1801 N  N   . ALA A 222 ? 0.4832 0.5545 0.3813 -0.0339 0.0681  -0.0409 221  ALA A N   
1802 C  CA  . ALA A 222 ? 0.6100 0.5699 0.3917 -0.0344 0.1134  -0.0223 221  ALA A CA  
1803 C  C   . ALA A 222 ? 0.6792 0.5870 0.3775 0.0070  0.1488  -0.0254 221  ALA A C   
1804 O  O   . ALA A 222 ? 0.7077 0.5949 0.3950 -0.0068 0.2038  -0.0192 221  ALA A O   
1805 C  CB  . ALA A 222 ? 0.6376 0.5566 0.4042 -0.0495 0.1153  -0.0002 221  ALA A CB  
1806 N  N   . ASP A 223 ? 0.6539 0.5952 0.3389 0.0369  0.1282  -0.0330 222  ASP A N   
1807 C  CA  . ASP A 223 ? 0.5771 0.5934 0.3172 0.0715  0.0813  -0.0360 222  ASP A CA  
1808 C  C   . ASP A 223 ? 0.5062 0.5653 0.2992 0.0644  0.1035  -0.0469 222  ASP A C   
1809 O  O   . ASP A 223 ? 0.5240 0.5238 0.2641 0.0361  0.0963  -0.0450 222  ASP A O   
1810 C  CB  . ASP A 223 ? 0.5857 0.6303 0.3579 0.1119  0.0375  -0.0331 222  ASP A CB  
1811 C  CG  . ASP A 223 ? 0.6407 0.6576 0.4148 0.1066  0.0434  -0.0401 222  ASP A CG  
1812 O  OD1 . ASP A 223 ? 0.6566 0.6599 0.4343 0.0447  0.0266  -0.0377 222  ASP A OD1 
1813 O  OD2 . ASP A 223 ? 0.5576 0.6672 0.4233 0.1799  0.0320  -0.0317 222  ASP A OD2 
1814 N  N   . ARG A 224 ? 0.3927 0.5656 0.2883 0.0714  0.0577  -0.0769 223  ARG A N   
1815 C  CA  . ARG A 224 ? 0.3351 0.5741 0.3039 0.1006  0.0907  -0.1014 223  ARG A CA  
1816 C  C   . ARG A 224 ? 0.3761 0.6068 0.3767 0.1101  0.1348  -0.1315 223  ARG A C   
1817 O  O   . ARG A 224 ? 0.4202 0.5931 0.3675 0.1330  0.1153  -0.1364 223  ARG A O   
1818 C  CB  . ARG A 224 ? 0.3025 0.5465 0.2692 0.1318  0.0519  -0.1015 223  ARG A CB  
1819 C  CG  . ARG A 224 ? 0.3377 0.5399 0.2689 0.0836  0.0053  -0.0902 223  ARG A CG  
1820 C  CD  . ARG A 224 ? 0.3216 0.5451 0.2693 0.0967  -0.0118 -0.1005 223  ARG A CD  
1821 N  NE  . ARG A 224 ? 0.2545 0.5680 0.2588 0.0744  -0.0183 -0.1146 223  ARG A NE  
1822 C  CZ  . ARG A 224 ? 0.2550 0.5652 0.2297 0.1054  -0.0525 -0.1392 223  ARG A CZ  
1823 N  NH1 . ARG A 224 ? 0.2857 0.5201 0.2185 0.0980  -0.0678 -0.1428 223  ARG A NH1 
1824 N  NH2 . ARG A 224 ? 0.2463 0.5620 0.2552 0.0984  -0.0785 -0.1223 223  ARG A NH2 
1825 N  N   . LYS A 225 ? 0.3725 0.6213 0.4684 0.0449  0.2078  -0.1252 224  LYS A N   
1826 C  CA  . LYS A 225 ? 0.5190 0.6521 0.5723 0.0015  0.2550  -0.1296 224  LYS A CA  
1827 C  C   . LYS A 225 ? 0.6077 0.6968 0.6039 -0.0516 0.2884  -0.0865 224  LYS A C   
1828 O  O   . LYS A 225 ? 0.6569 0.6984 0.6060 -0.0108 0.2937  -0.0789 224  LYS A O   
1829 C  CB  . LYS A 225 ? 0.5869 0.6347 0.6406 0.0152  0.2340  -0.1247 224  LYS A CB  
1830 C  CG  . LYS A 225 ? 0.6758 0.6189 0.6706 -0.0298 0.2520  -0.1201 224  LYS A CG  
1831 C  CD  . LYS A 225 ? 0.7083 0.6004 0.6854 -0.0496 0.2587  -0.1195 224  LYS A CD  
1832 C  CE  . LYS A 225 ? 0.7377 0.5802 0.6851 -0.0706 0.2728  -0.1020 224  LYS A CE  
1833 N  NZ  . LYS A 225 ? 0.6972 0.5536 0.6750 -0.0926 0.2997  -0.1025 224  LYS A NZ  
1834 N  N   . ALA A 226 ? 0.6234 0.7252 0.6282 -0.0795 0.2908  -0.0802 225  ALA A N   
1835 C  CA  . ALA A 226 ? 0.6936 0.7544 0.6622 -0.0660 0.2856  -0.0855 225  ALA A CA  
1836 C  C   . ALA A 226 ? 0.7972 0.7959 0.7196 -0.0087 0.2481  -0.0761 225  ALA A C   
1837 O  O   . ALA A 226 ? 0.8104 0.8013 0.7295 0.0208  0.2405  -0.0701 225  ALA A O   
1838 C  CB  . ALA A 226 ? 0.6695 0.7413 0.6450 -0.0693 0.3077  -0.0975 225  ALA A CB  
1839 N  N   . SER A 227 ? 0.8508 0.8280 0.7731 -0.0159 0.2074  -0.0537 226  SER A N   
1840 C  CA  . SER A 227 ? 0.9142 0.8592 0.8254 0.0223  0.1739  -0.0479 226  SER A CA  
1841 C  C   . SER A 227 ? 0.9865 0.8984 0.8584 0.0422  0.1631  -0.0364 226  SER A C   
1842 O  O   . SER A 227 ? 0.9738 0.9015 0.8462 0.0670  0.1850  -0.0399 226  SER A O   
1843 C  CB  . SER A 227 ? 0.8686 0.8555 0.8451 0.0280  0.1659  -0.0494 226  SER A CB  
1844 O  OG  . SER A 227 ? 0.8683 0.8531 0.8548 0.0230  0.1519  -0.0510 226  SER A OG  
1845 N  N   . GLY A 228 ? 1.0699 0.9298 0.9061 0.0206  0.1221  -0.0182 227  GLY A N   
1846 C  CA  . GLY A 228 ? 1.1210 0.9627 0.9407 0.0016  0.0930  -0.0065 227  GLY A CA  
1847 C  C   . GLY A 228 ? 1.1807 0.9977 0.9713 -0.0020 0.0666  0.0004  227  GLY A C   
1848 O  O   . GLY A 228 ? 1.2010 1.0073 0.9840 0.0185  0.0610  -0.0025 227  GLY A O   
1849 N  N   . GLU A 229 ? 1.1992 1.0162 0.9780 -0.0276 0.0488  0.0071  228  GLU A N   
1850 C  CA  . GLU A 229 ? 1.2092 1.0235 0.9785 -0.0515 0.0210  0.0173  228  GLU A CA  
1851 C  C   . GLU A 229 ? 1.2194 0.9983 0.9605 -0.0489 0.0235  0.0143  228  GLU A C   
1852 O  O   . GLU A 229 ? 1.2442 0.9993 0.9617 -0.0553 0.0294  0.0216  228  GLU A O   
1853 C  CB  . GLU A 229 ? 1.2062 1.0481 0.9924 -0.0643 -0.0090 0.0290  228  GLU A CB  
1854 C  CG  . GLU A 229 ? 1.2070 1.0668 1.0019 -0.0727 -0.0355 0.0428  228  GLU A CG  
1855 C  CD  . GLU A 229 ? 1.2077 1.0784 1.0090 -0.0885 -0.0546 0.0582  228  GLU A CD  
1856 O  OE1 . GLU A 229 ? 1.1900 1.0796 1.0073 -0.1011 -0.0579 0.0676  228  GLU A OE1 
1857 O  OE2 . GLU A 229 ? 1.2248 1.0825 1.0132 -0.0894 -0.0601 0.0629  228  GLU A OE2 
1858 N  N   . GLN A 230 ? 1.1846 0.9682 0.9398 -0.0328 0.0193  -0.0051 229  GLN A N   
1859 C  CA  . GLN A 230 ? 1.1136 0.9375 0.9170 -0.0090 0.0109  -0.0327 229  GLN A CA  
1860 C  C   . GLN A 230 ? 1.0669 0.8743 0.8818 -0.0053 0.0176  -0.0660 229  GLN A C   
1861 O  O   . GLN A 230 ? 1.0907 0.8768 0.8862 -0.0254 0.0252  -0.0681 229  GLN A O   
1862 C  CB  . GLN A 230 ? 1.0926 0.9612 0.9287 0.0122  -0.0117 -0.0248 229  GLN A CB  
1863 C  CG  . GLN A 230 ? 1.1193 0.9844 0.9400 0.0167  -0.0268 -0.0164 229  GLN A CG  
1864 C  CD  . GLN A 230 ? 1.1391 1.0020 0.9488 0.0208  -0.0231 -0.0081 229  GLN A CD  
1865 O  OE1 . GLN A 230 ? 1.1495 1.0066 0.9524 0.0127  -0.0022 -0.0046 229  GLN A OE1 
1866 N  NE2 . GLN A 230 ? 1.1386 1.0118 0.9524 0.0318  -0.0414 -0.0085 229  GLN A NE2 
1867 N  N   . SER A 231 ? 0.9838 0.7977 0.8366 0.0125  -0.0021 -0.0925 230  SER A N   
1868 C  CA  . SER A 231 ? 0.8951 0.7171 0.7872 0.0123  -0.0234 -0.1104 230  SER A CA  
1869 C  C   . SER A 231 ? 0.8086 0.6547 0.7297 0.0027  0.0024  -0.1050 230  SER A C   
1870 O  O   . SER A 231 ? 0.8014 0.6537 0.7187 0.0094  -0.0035 -0.1044 230  SER A O   
1871 C  CB  . SER A 231 ? 0.8852 0.6999 0.7935 0.0353  -0.0367 -0.1265 230  SER A CB  
1872 O  OG  . SER A 231 ? 0.8564 0.6875 0.7923 0.0497  -0.0444 -0.1358 230  SER A OG  
1873 N  N   . ASP A 232 ? 0.6957 0.5971 0.6813 0.0026  0.0447  -0.0927 231  ASP A N   
1874 C  CA  . ASP A 232 ? 0.6530 0.5513 0.6359 0.0294  0.0554  -0.0728 231  ASP A CA  
1875 C  C   . ASP A 232 ? 0.5648 0.5039 0.5736 0.0141  0.0312  -0.0513 231  ASP A C   
1876 O  O   . ASP A 232 ? 0.6043 0.5030 0.5944 -0.0134 0.0516  -0.0337 231  ASP A O   
1877 C  CB  . ASP A 232 ? 0.7490 0.5681 0.6636 0.0710  0.0789  -0.0619 231  ASP A CB  
1878 C  CG  . ASP A 232 ? 0.9127 0.5849 0.6901 0.0758  0.1100  -0.0483 231  ASP A CG  
1879 O  OD1 . ASP A 232 ? 0.9619 0.5806 0.6927 0.1014  0.1304  -0.0520 231  ASP A OD1 
1880 O  OD2 . ASP A 232 ? 0.9958 0.6001 0.7012 0.0711  0.1088  -0.0260 231  ASP A OD2 
1881 N  N   . ASP A 233 ? 0.4003 0.4377 0.4769 -0.0085 -0.0023 -0.0605 232  ASP A N   
1882 C  CA  . ASP A 233 ? 0.2822 0.4232 0.4041 0.0213  -0.0085 -0.0519 232  ASP A CA  
1883 C  C   . ASP A 233 ? 0.3068 0.4217 0.3590 0.0336  -0.0217 -0.0702 232  ASP A C   
1884 O  O   . ASP A 233 ? 0.2503 0.4671 0.3527 0.0416  -0.0473 -0.0521 232  ASP A O   
1885 C  CB  . ASP A 233 ? 0.2691 0.4325 0.3874 0.0579  0.0151  -0.0379 232  ASP A CB  
1886 C  CG  . ASP A 233 ? 0.2335 0.4054 0.3737 0.1106  0.0123  -0.0366 232  ASP A CG  
1887 O  OD1 . ASP A 233 ? 0.2135 0.3797 0.3769 0.1005  -0.0339 -0.0777 232  ASP A OD1 
1888 O  OD2 . ASP A 233 ? 0.2703 0.4069 0.3550 0.1349  0.0240  0.0117  232  ASP A OD2 
1889 N  N   . LEU A 234 ? 0.2710 0.3679 0.3166 0.0256  -0.0297 -0.0625 233  LEU A N   
1890 C  CA  . LEU A 234 ? 0.2388 0.3150 0.2733 0.0699  -0.0122 -0.0489 233  LEU A CA  
1891 C  C   . LEU A 234 ? 0.2079 0.2988 0.2242 0.0771  -0.0354 -0.0510 233  LEU A C   
1892 O  O   . LEU A 234 ? 0.1875 0.2710 0.2096 0.0806  -0.0420 -0.0403 233  LEU A O   
1893 C  CB  . LEU A 234 ? 0.2030 0.2928 0.2752 0.0687  -0.0124 -0.0156 233  LEU A CB  
1894 C  CG  . LEU A 234 ? 0.2730 0.3173 0.2641 0.1040  -0.0346 0.0127  233  LEU A CG  
1895 C  CD1 . LEU A 234 ? 0.3382 0.3315 0.2750 0.0341  -0.0497 0.0276  233  LEU A CD1 
1896 C  CD2 . LEU A 234 ? 0.2728 0.3145 0.2737 0.1684  -0.0118 -0.0166 233  LEU A CD2 
1897 N  N   . LEU A 235 ? 0.2783 0.3198 0.2256 0.1693  -0.0040 -0.0513 234  LEU A N   
1898 C  CA  . LEU A 235 ? 0.2238 0.3137 0.2258 0.1257  -0.0059 -0.0265 234  LEU A CA  
1899 C  C   . LEU A 235 ? 0.3086 0.3235 0.2599 0.1083  -0.0039 -0.0464 234  LEU A C   
1900 O  O   . LEU A 235 ? 0.3636 0.3034 0.2475 0.0850  0.0012  -0.0705 234  LEU A O   
1901 C  CB  . LEU A 235 ? 0.2855 0.3159 0.2318 0.0730  -0.0201 0.0076  234  LEU A CB  
1902 C  CG  . LEU A 235 ? 0.2864 0.3063 0.2120 0.0134  0.0070  0.0080  234  LEU A CG  
1903 C  CD1 . LEU A 235 ? 0.3843 0.2939 0.2334 -0.0071 0.0040  0.0025  234  LEU A CD1 
1904 C  CD2 . LEU A 235 ? 0.4127 0.3260 0.2291 0.0512  0.0763  0.0024  234  LEU A CD2 
1905 N  N   . THR A 236 ? 0.2593 0.3098 0.2789 0.1500  0.0010  -0.0799 235  THR A N   
1906 C  CA  . THR A 236 ? 0.2185 0.3218 0.3112 0.1358  -0.0314 -0.0645 235  THR A CA  
1907 C  C   . THR A 236 ? 0.2083 0.2992 0.3372 0.0702  -0.0594 -0.0671 235  THR A C   
1908 O  O   . THR A 236 ? 0.3123 0.2884 0.3561 0.0495  -0.0750 -0.0419 235  THR A O   
1909 C  CB  . THR A 236 ? 0.2157 0.3685 0.3229 0.1135  -0.0713 -0.0713 235  THR A CB  
1910 O  OG1 . THR A 236 ? 0.2564 0.4176 0.3178 0.1032  -0.0582 -0.0578 235  THR A OG1 
1911 C  CG2 . THR A 236 ? 0.2171 0.3827 0.3383 0.0732  -0.0694 -0.0758 235  THR A CG2 
1912 N  N   . HIS A 237 ? 0.1719 0.3026 0.3146 0.0617  -0.0464 -0.0688 236  HIS A N   
1913 C  CA  . HIS A 237 ? 0.1668 0.3156 0.3189 0.0452  -0.0482 -0.0323 236  HIS A CA  
1914 C  C   . HIS A 237 ? 0.1543 0.3581 0.2895 0.0009  -0.0579 -0.0070 236  HIS A C   
1915 O  O   . HIS A 237 ? 0.2033 0.3851 0.2750 0.0046  -0.0710 -0.0016 236  HIS A O   
1916 C  CB  . HIS A 237 ? 0.1839 0.2878 0.3573 0.0196  -0.0324 -0.0216 236  HIS A CB  
1917 C  CG  . HIS A 237 ? 0.3941 0.3277 0.4159 0.0102  -0.0370 -0.0237 236  HIS A CG  
1918 N  ND1 . HIS A 237 ? 0.4324 0.3212 0.4415 0.0087  -0.0236 -0.0436 236  HIS A ND1 
1919 C  CD2 . HIS A 237 ? 0.4683 0.3304 0.4552 0.0104  -0.0718 -0.0169 236  HIS A CD2 
1920 C  CE1 . HIS A 237 ? 0.5159 0.3295 0.4793 -0.0026 -0.0328 -0.0339 236  HIS A CE1 
1921 N  NE2 . HIS A 237 ? 0.4760 0.3096 0.4735 0.0150  -0.0610 -0.0359 236  HIS A NE2 
1922 N  N   . MET A 238 ? 0.2200 0.3613 0.2430 -0.0300 -0.0303 0.0237  237  MET A N   
1923 C  CA  . MET A 238 ? 0.2322 0.3741 0.2160 -0.0369 -0.0092 -0.0033 237  MET A CA  
1924 C  C   . MET A 238 ? 0.3016 0.3933 0.2356 -0.0493 -0.0334 -0.0189 237  MET A C   
1925 O  O   . MET A 238 ? 0.3673 0.4217 0.2524 -0.0767 -0.0438 0.0003  237  MET A O   
1926 C  CB  . MET A 238 ? 0.1640 0.3486 0.2103 0.0313  0.0539  -0.0175 237  MET A CB  
1927 C  CG  . MET A 238 ? 0.1096 0.3374 0.2119 0.0604  -0.0207 0.0262  237  MET A CG  
1928 S  SD  . MET A 238 ? 0.2562 0.3768 0.2101 0.0537  -0.0203 -0.0315 237  MET A SD  
1929 C  CE  . MET A 238 ? 0.2459 0.3398 0.2376 0.0123  0.0238  -0.0267 237  MET A CE  
1930 N  N   . LEU A 239 ? 0.2688 0.3678 0.2316 0.0101  -0.0380 -0.0387 238  LEU A N   
1931 C  CA  . LEU A 239 ? 0.2282 0.3710 0.2310 0.0640  0.0230  -0.0452 238  LEU A CA  
1932 C  C   . LEU A 239 ? 0.3059 0.4495 0.2691 0.0170  0.0128  -0.0244 238  LEU A C   
1933 O  O   . LEU A 239 ? 0.3694 0.4863 0.2868 -0.0137 0.0212  -0.0188 238  LEU A O   
1934 C  CB  . LEU A 239 ? 0.2784 0.3426 0.2231 0.0672  0.0261  -0.0276 238  LEU A CB  
1935 C  CG  . LEU A 239 ? 0.3279 0.3577 0.2453 -0.0298 0.0489  -0.0566 238  LEU A CG  
1936 C  CD1 . LEU A 239 ? 0.3599 0.3456 0.2377 0.0063  0.0337  -0.0681 238  LEU A CD1 
1937 C  CD2 . LEU A 239 ? 0.4376 0.3750 0.2645 0.0108  0.0405  -0.0603 238  LEU A CD2 
1938 N  N   . ASN A 240 ? 0.3330 0.4847 0.3001 0.0504  -0.0098 -0.0545 239  ASN A N   
1939 C  CA  . ASN A 240 ? 0.2873 0.5292 0.3234 0.0589  -0.0123 -0.0865 239  ASN A CA  
1940 C  C   . ASN A 240 ? 0.2350 0.5190 0.3366 0.0239  -0.0305 -0.0955 239  ASN A C   
1941 O  O   . ASN A 240 ? 0.2203 0.5307 0.3685 0.0570  0.0427  -0.0967 239  ASN A O   
1942 C  CB  . ASN A 240 ? 0.3245 0.5723 0.3313 0.0833  -0.0186 -0.1113 239  ASN A CB  
1943 C  CG  . ASN A 240 ? 0.4414 0.6247 0.3568 0.0368  0.0375  -0.1210 239  ASN A CG  
1944 O  OD1 . ASN A 240 ? 0.5493 0.6553 0.3697 0.0227  0.1204  -0.1302 239  ASN A OD1 
1945 N  ND2 . ASN A 240 ? 0.5081 0.6358 0.3557 -0.0100 -0.0551 -0.1100 239  ASN A ND2 
1946 N  N   . GLY A 241 ? 0.2677 0.5019 0.2961 0.0132  -0.0239 -0.0792 240  GLY A N   
1947 C  CA  . GLY A 241 ? 0.2878 0.4841 0.2739 0.0094  -0.0548 -0.0644 240  GLY A CA  
1948 C  C   . GLY A 241 ? 0.2881 0.4690 0.2860 0.0435  -0.0365 -0.0357 240  GLY A C   
1949 O  O   . GLY A 241 ? 0.3462 0.4675 0.2858 0.0059  -0.0528 -0.0355 240  GLY A O   
1950 N  N   . LYS A 242 ? 0.2781 0.4502 0.3108 0.1093  -0.0175 0.0093  241  LYS A N   
1951 C  CA  . LYS A 242 ? 0.2977 0.4591 0.3198 0.1195  0.0221  0.0305  241  LYS A CA  
1952 C  C   . LYS A 242 ? 0.2721 0.4265 0.3238 0.0963  0.0317  0.0259  241  LYS A C   
1953 O  O   . LYS A 242 ? 0.2946 0.4111 0.3180 0.1030  0.0143  0.0113  241  LYS A O   
1954 C  CB  . LYS A 242 ? 0.4139 0.5010 0.3432 0.1394  0.0870  0.0448  241  LYS A CB  
1955 C  CG  . LYS A 242 ? 0.5547 0.5399 0.3869 0.1250  0.0605  0.0474  241  LYS A CG  
1956 C  CD  . LYS A 242 ? 0.6588 0.5672 0.4057 0.1407  0.0843  0.0364  241  LYS A CD  
1957 C  CE  . LYS A 242 ? 0.8051 0.5958 0.4339 0.1269  0.1089  0.0197  241  LYS A CE  
1958 N  NZ  . LYS A 242 ? 0.9127 0.6129 0.4438 0.1254  0.1118  -0.0042 241  LYS A NZ  
1959 N  N   . ASP A 243 ? 0.2083 0.3861 0.3249 0.0858  -0.0070 0.0348  242  ASP A N   
1960 C  CA  . ASP A 243 ? 0.2235 0.4036 0.3185 0.0718  -0.0309 0.0613  242  ASP A CA  
1961 C  C   . ASP A 243 ? 0.1653 0.4957 0.3532 0.0795  0.0177  0.1280  242  ASP A C   
1962 O  O   . ASP A 243 ? 0.2594 0.5705 0.3741 0.0618  -0.0120 0.1165  242  ASP A O   
1963 C  CB  . ASP A 243 ? 0.2467 0.3667 0.2897 0.0608  -0.0646 0.0367  242  ASP A CB  
1964 C  CG  . ASP A 243 ? 0.2047 0.3466 0.2860 0.0616  -0.0165 0.0453  242  ASP A CG  
1965 O  OD1 . ASP A 243 ? 0.2425 0.3440 0.2788 0.0294  -0.0241 0.0603  242  ASP A OD1 
1966 O  OD2 . ASP A 243 ? 0.2527 0.3449 0.2945 0.0856  -0.0037 0.0539  242  ASP A OD2 
1967 N  N   . PRO A 244 ? 0.2584 0.5136 0.4214 0.0604  -0.0230 0.1722  243  PRO A N   
1968 C  CA  . PRO A 244 ? 0.2861 0.5301 0.4400 0.0728  0.0103  0.2259  243  PRO A CA  
1969 C  C   . PRO A 244 ? 0.2896 0.5731 0.4763 0.1108  -0.0075 0.2495  243  PRO A C   
1970 O  O   . PRO A 244 ? 0.3794 0.6081 0.4953 0.1548  0.0246  0.2797  243  PRO A O   
1971 C  CB  . PRO A 244 ? 0.4005 0.5287 0.4586 0.0509  -0.0500 0.2086  243  PRO A CB  
1972 C  CG  . PRO A 244 ? 0.4176 0.5245 0.4459 0.0072  -0.0540 0.1842  243  PRO A CG  
1973 C  CD  . PRO A 244 ? 0.3572 0.5022 0.4326 0.0435  -0.0071 0.1781  243  PRO A CD  
1974 N  N   . GLU A 245 ? 0.3962 0.6015 0.4840 0.0791  -0.0803 0.2240  244  GLU A N   
1975 C  CA  . GLU A 245 ? 0.4174 0.6141 0.4672 0.0713  -0.1325 0.2041  244  GLU A CA  
1976 C  C   . GLU A 245 ? 0.4339 0.6108 0.4613 0.0667  -0.1623 0.1666  244  GLU A C   
1977 O  O   . GLU A 245 ? 0.5241 0.6347 0.4719 0.0512  -0.1857 0.1762  244  GLU A O   
1978 C  CB  . GLU A 245 ? 0.4955 0.6480 0.4632 0.0525  -0.1439 0.1989  244  GLU A CB  
1979 C  CG  . GLU A 245 ? 0.6008 0.6936 0.4827 0.0366  -0.1112 0.1954  244  GLU A CG  
1980 C  CD  . GLU A 245 ? 0.6711 0.7476 0.5020 -0.0143 -0.1094 0.1797  244  GLU A CD  
1981 O  OE1 . GLU A 245 ? 0.5240 0.7575 0.4946 -0.0283 -0.1469 0.1895  244  GLU A OE1 
1982 O  OE2 . GLU A 245 ? 0.7533 0.7759 0.5215 -0.0264 -0.0618 0.1631  244  GLU A OE2 
1983 N  N   . THR A 246 ? 0.3237 0.5794 0.4283 0.0647  -0.0905 0.1362  245  THR A N   
1984 C  CA  . THR A 246 ? 0.2927 0.5745 0.4152 0.0026  -0.0272 0.0889  245  THR A CA  
1985 C  C   . THR A 246 ? 0.1972 0.6423 0.4361 -0.0353 -0.0094 0.0579  245  THR A C   
1986 O  O   . THR A 246 ? 0.2048 0.6679 0.4600 -0.0168 -0.1011 0.0401  245  THR A O   
1987 C  CB  . THR A 246 ? 0.3267 0.5073 0.3757 -0.0468 -0.0257 0.0551  245  THR A CB  
1988 O  OG1 . THR A 246 ? 0.2953 0.4544 0.3368 -0.0429 -0.0678 0.0203  245  THR A OG1 
1989 C  CG2 . THR A 246 ? 0.3599 0.5039 0.3759 -0.0818 -0.0448 0.0640  245  THR A CG2 
1990 N  N   . GLY A 247 ? 0.2738 0.6310 0.4213 -0.0362 0.0091  0.0268  246  GLY A N   
1991 C  CA  . GLY A 247 ? 0.2689 0.6201 0.4089 0.0113  0.0652  0.0426  246  GLY A CA  
1992 C  C   . GLY A 247 ? 0.3139 0.5952 0.4240 0.0806  0.0423  0.0372  246  GLY A C   
1993 O  O   . GLY A 247 ? 0.3263 0.6143 0.4033 0.1179  0.1054  0.0414  246  GLY A O   
1994 N  N   . GLU A 248 ? 0.2657 0.5571 0.4269 0.0638  -0.0522 0.0166  247  GLU A N   
1995 C  CA  . GLU A 248 ? 0.1830 0.4892 0.3712 -0.0248 -0.1182 0.0221  247  GLU A CA  
1996 C  C   . GLU A 248 ? 0.1542 0.4827 0.3557 -0.0204 -0.0544 0.0567  247  GLU A C   
1997 O  O   . GLU A 248 ? 0.1501 0.4879 0.3614 -0.0094 -0.0596 0.0870  247  GLU A O   
1998 C  CB  . GLU A 248 ? 0.2068 0.4920 0.3757 -0.0243 -0.1310 -0.0138 247  GLU A CB  
1999 C  CG  . GLU A 248 ? 0.3491 0.4645 0.3523 -0.0427 -0.1327 -0.0797 247  GLU A CG  
2000 C  CD  . GLU A 248 ? 0.3821 0.4693 0.3758 -0.0090 -0.1252 -0.0883 247  GLU A CD  
2001 O  OE1 . GLU A 248 ? 0.3479 0.4627 0.3821 0.0688  -0.1114 -0.0979 247  GLU A OE1 
2002 O  OE2 . GLU A 248 ? 0.3453 0.4570 0.3819 -0.0513 -0.1294 -0.1153 247  GLU A OE2 
2003 N  N   . PRO A 249 ? 0.1453 0.4460 0.3157 0.0154  -0.0009 0.0373  248  PRO A N   
2004 C  CA  . PRO A 249 ? 0.1613 0.3893 0.2738 0.0568  0.0054  0.0366  248  PRO A CA  
2005 C  C   . PRO A 249 ? 0.1843 0.3550 0.2506 0.0748  0.0182  0.0411  248  PRO A C   
2006 O  O   . PRO A 249 ? 0.1956 0.3601 0.2678 0.0071  -0.0129 0.0340  248  PRO A O   
2007 C  CB  . PRO A 249 ? 0.1867 0.4171 0.3166 0.0580  0.0147  0.0226  248  PRO A CB  
2008 C  CG  . PRO A 249 ? 0.2696 0.4534 0.3117 0.0622  0.0511  0.0314  248  PRO A CG  
2009 C  CD  . PRO A 249 ? 0.1871 0.4575 0.3166 0.0295  0.0309  0.0383  248  PRO A CD  
2010 N  N   . LEU A 250 ? 0.1238 0.3203 0.2178 0.0850  0.0093  0.0312  249  LEU A N   
2011 C  CA  . LEU A 250 ? 0.1035 0.2690 0.2297 0.0002  -0.0046 0.0185  249  LEU A CA  
2012 C  C   . LEU A 250 ? 0.1537 0.2965 0.2420 0.0362  0.0192  0.0254  249  LEU A C   
2013 O  O   . LEU A 250 ? 0.2487 0.2948 0.2311 0.0404  0.0503  -0.0093 249  LEU A O   
2014 C  CB  . LEU A 250 ? 0.1227 0.2756 0.2426 0.0009  -0.0028 0.0242  249  LEU A CB  
2015 C  CG  . LEU A 250 ? 0.1273 0.2717 0.2438 -0.0559 -0.0017 -0.0120 249  LEU A CG  
2016 C  CD1 . LEU A 250 ? 0.1380 0.2644 0.2530 -0.0291 -0.0198 -0.0177 249  LEU A CD1 
2017 C  CD2 . LEU A 250 ? 0.1947 0.2768 0.2272 -0.0211 -0.0201 -0.0342 249  LEU A CD2 
2018 N  N   . ASP A 251 ? 0.2121 0.3081 0.2644 0.0298  0.0484  0.0315  250  ASP A N   
2019 C  CA  . ASP A 251 ? 0.2131 0.3452 0.2980 -0.0519 0.0383  0.0428  250  ASP A CA  
2020 C  C   . ASP A 251 ? 0.2168 0.3561 0.2962 -0.0430 0.0440  0.0535  250  ASP A C   
2021 O  O   . ASP A 251 ? 0.1789 0.3272 0.3017 -0.0257 0.0051  0.0768  250  ASP A O   
2022 C  CB  . ASP A 251 ? 0.2973 0.3872 0.3147 -0.0076 0.0120  0.0046  250  ASP A CB  
2023 C  CG  . ASP A 251 ? 0.3118 0.4152 0.3327 0.0155  -0.0337 -0.0366 250  ASP A CG  
2024 O  OD1 . ASP A 251 ? 0.2048 0.4201 0.3073 -0.0008 0.0510  -0.0485 250  ASP A OD1 
2025 O  OD2 . ASP A 251 ? 0.4376 0.4514 0.4021 0.0858  -0.0542 -0.0333 250  ASP A OD2 
2026 N  N   . ASP A 252 ? 0.2077 0.3867 0.2812 -0.0187 0.0897  0.0458  251  ASP A N   
2027 C  CA  . ASP A 252 ? 0.2695 0.4427 0.2907 0.0232  0.1169  0.0481  251  ASP A CA  
2028 C  C   . ASP A 252 ? 0.2632 0.4129 0.2709 0.0206  0.1180  0.0221  251  ASP A C   
2029 O  O   . ASP A 252 ? 0.2570 0.3999 0.2752 0.0419  0.0537  0.0349  251  ASP A O   
2030 C  CB  . ASP A 252 ? 0.3106 0.5194 0.3256 0.0746  0.1499  0.0476  251  ASP A CB  
2031 C  CG  . ASP A 252 ? 0.4505 0.5765 0.3610 0.1185  0.1966  0.0701  251  ASP A CG  
2032 O  OD1 . ASP A 252 ? 0.5300 0.5842 0.3776 0.1347  0.1881  0.0781  251  ASP A OD1 
2033 O  OD2 . ASP A 252 ? 0.4624 0.6122 0.3761 0.1463  0.2147  0.0715  251  ASP A OD2 
2034 N  N   . GLU A 253 ? 0.3729 0.3927 0.2722 -0.0262 0.1323  0.0182  252  GLU A N   
2035 C  CA  . GLU A 253 ? 0.3079 0.3721 0.2487 -0.0891 0.1104  -0.0037 252  GLU A CA  
2036 C  C   . GLU A 253 ? 0.2783 0.3248 0.2132 -0.0635 0.0380  0.0199  252  GLU A C   
2037 O  O   . GLU A 253 ? 0.2954 0.3281 0.1980 -0.0244 0.0254  0.0390  252  GLU A O   
2038 C  CB  . GLU A 253 ? 0.3381 0.3985 0.2830 -0.1346 0.1440  -0.0110 252  GLU A CB  
2039 C  CG  . GLU A 253 ? 0.4052 0.4344 0.3151 -0.2151 0.1254  -0.0380 252  GLU A CG  
2040 C  CD  . GLU A 253 ? 0.5496 0.5082 0.3559 -0.2338 0.1470  -0.0242 252  GLU A CD  
2041 O  OE1 . GLU A 253 ? 0.6125 0.5284 0.3793 -0.2465 0.1393  -0.0256 252  GLU A OE1 
2042 O  OE2 . GLU A 253 ? 0.5833 0.5288 0.3686 -0.1872 0.1267  -0.0410 252  GLU A OE2 
2043 N  N   . ASN A 254 ? 0.2040 0.2707 0.1909 -0.0800 0.0510  0.0035  253  ASN A N   
2044 C  CA  . ASN A 254 ? 0.1769 0.2413 0.1711 -0.0679 0.0243  -0.0017 253  ASN A CA  
2045 C  C   . ASN A 254 ? 0.1852 0.2433 0.1729 -0.0416 0.0069  -0.0007 253  ASN A C   
2046 O  O   . ASN A 254 ? 0.1460 0.2645 0.2002 -0.0164 0.0115  -0.0189 253  ASN A O   
2047 C  CB  . ASN A 254 ? 0.2378 0.2553 0.1663 -0.0745 0.0824  -0.0166 253  ASN A CB  
2048 C  CG  . ASN A 254 ? 0.1564 0.2779 0.1795 -0.0328 0.0180  -0.0183 253  ASN A CG  
2049 O  OD1 . ASN A 254 ? 0.1501 0.2972 0.2211 -0.0304 0.0338  -0.0109 253  ASN A OD1 
2050 N  ND2 . ASN A 254 ? 0.0870 0.2991 0.1652 -0.0134 -0.0095 -0.0322 253  ASN A ND2 
2051 N  N   . ILE A 255 ? 0.1996 0.2402 0.1569 -0.0081 0.0411  -0.0100 254  ILE A N   
2052 C  CA  . ILE A 255 ? 0.1982 0.2661 0.1690 0.0185  0.0180  -0.0726 254  ILE A CA  
2053 C  C   . ILE A 255 ? 0.1953 0.2632 0.1615 -0.0205 0.0172  -0.0185 254  ILE A C   
2054 O  O   . ILE A 255 ? 0.2177 0.2647 0.1575 0.0268  0.0222  -0.0028 254  ILE A O   
2055 C  CB  . ILE A 255 ? 0.1860 0.2876 0.1604 0.0265  -0.0151 -0.0891 254  ILE A CB  
2056 C  CG1 . ILE A 255 ? 0.2740 0.2906 0.1818 0.1000  0.0305  -0.0857 254  ILE A CG1 
2057 C  CG2 . ILE A 255 ? 0.2864 0.2629 0.1812 0.0474  0.0162  -0.1104 254  ILE A CG2 
2058 C  CD1 . ILE A 255 ? 0.2807 0.3292 0.2030 0.0884  0.0387  -0.0954 254  ILE A CD1 
2059 N  N   . ARG A 256 ? 0.1843 0.2894 0.1740 0.0016  0.0671  0.0154  255  ARG A N   
2060 C  CA  . ARG A 256 ? 0.1317 0.2997 0.1843 -0.0080 0.0309  0.0433  255  ARG A CA  
2061 C  C   . ARG A 256 ? 0.1355 0.2624 0.1781 0.0134  -0.0026 0.0199  255  ARG A C   
2062 O  O   . ARG A 256 ? 0.1561 0.2492 0.1641 0.0234  0.0199  0.0228  255  ARG A O   
2063 C  CB  . ARG A 256 ? 0.1873 0.3464 0.2044 -0.0338 0.0560  0.0883  255  ARG A CB  
2064 C  CG  . ARG A 256 ? 0.3480 0.4177 0.2781 -0.0443 0.0677  0.1300  255  ARG A CG  
2065 C  CD  . ARG A 256 ? 0.5447 0.4836 0.3612 -0.0368 0.1267  0.1659  255  ARG A CD  
2066 N  NE  . ARG A 256 ? 0.6333 0.5392 0.4070 -0.0653 0.1480  0.1923  255  ARG A NE  
2067 C  CZ  . ARG A 256 ? 0.7615 0.5688 0.4537 -0.0169 0.1343  0.2012  255  ARG A CZ  
2068 N  NH1 . ARG A 256 ? 0.7438 0.5830 0.4650 0.0189  0.1544  0.1995  255  ARG A NH1 
2069 N  NH2 . ARG A 256 ? 0.7817 0.5831 0.4691 0.0473  0.0947  0.2068  255  ARG A NH2 
2070 N  N   . TYR A 257 ? 0.1909 0.2125 0.1745 0.0039  -0.0123 0.0091  256  TYR A N   
2071 C  CA  . TYR A 257 ? 0.1589 0.1817 0.1755 -0.0412 0.0563  -0.0338 256  TYR A CA  
2072 C  C   . TYR A 257 ? 0.1252 0.1786 0.1455 -0.0036 0.0205  -0.0238 256  TYR A C   
2073 O  O   . TYR A 257 ? 0.1476 0.1914 0.1508 0.0081  0.0057  -0.0227 256  TYR A O   
2074 C  CB  . TYR A 257 ? 0.1556 0.1880 0.1857 -0.0638 0.0544  -0.0518 256  TYR A CB  
2075 C  CG  . TYR A 257 ? 0.2028 0.2072 0.2348 -0.1164 0.0479  -0.0217 256  TYR A CG  
2076 C  CD1 . TYR A 257 ? 0.2808 0.2273 0.2529 -0.1217 0.0659  -0.0293 256  TYR A CD1 
2077 C  CD2 . TYR A 257 ? 0.2506 0.2220 0.2667 -0.1358 0.0478  -0.0280 256  TYR A CD2 
2078 C  CE1 . TYR A 257 ? 0.2793 0.2561 0.2544 -0.1209 0.0796  -0.0041 256  TYR A CE1 
2079 C  CE2 . TYR A 257 ? 0.2183 0.2665 0.2808 -0.1331 0.0272  -0.0141 256  TYR A CE2 
2080 C  CZ  . TYR A 257 ? 0.3278 0.2761 0.2847 -0.1487 0.0540  -0.0043 256  TYR A CZ  
2081 O  OH  . TYR A 257 ? 0.4119 0.3459 0.3139 -0.1331 0.0692  -0.0076 256  TYR A OH  
2082 N  N   . GLN A 258 ? 0.1936 0.2115 0.1328 0.0587  0.0043  -0.0179 257  GLN A N   
2083 C  CA  . GLN A 258 ? 0.1452 0.2283 0.1171 0.0618  -0.0396 0.0211  257  GLN A CA  
2084 C  C   . GLN A 258 ? 0.1617 0.2166 0.1194 0.0087  -0.0288 -0.0351 257  GLN A C   
2085 O  O   . GLN A 258 ? 0.1660 0.1969 0.1363 -0.0318 0.0082  -0.0229 257  GLN A O   
2086 C  CB  . GLN A 258 ? 0.1286 0.2545 0.1102 0.0610  -0.0021 0.0358  257  GLN A CB  
2087 C  CG  . GLN A 258 ? 0.1554 0.2616 0.1279 0.0718  -0.0093 0.0287  257  GLN A CG  
2088 C  CD  . GLN A 258 ? 0.1653 0.2510 0.1254 0.0390  -0.0062 0.0245  257  GLN A CD  
2089 O  OE1 . GLN A 258 ? 0.1627 0.2523 0.1059 0.0151  0.0157  0.0014  257  GLN A OE1 
2090 N  NE2 . GLN A 258 ? 0.1185 0.2196 0.1283 0.0242  0.0054  0.0290  257  GLN A NE2 
2091 N  N   . ILE A 259 ? 0.1977 0.1987 0.1011 0.0049  -0.0234 -0.0496 258  ILE A N   
2092 C  CA  . ILE A 259 ? 0.1734 0.2170 0.1184 0.0298  0.0389  -0.0358 258  ILE A CA  
2093 C  C   . ILE A 259 ? 0.1705 0.2221 0.1307 0.0139  0.0250  -0.0190 258  ILE A C   
2094 O  O   . ILE A 259 ? 0.1488 0.2452 0.1468 0.0143  0.0126  -0.0286 258  ILE A O   
2095 C  CB  . ILE A 259 ? 0.1602 0.2533 0.1401 0.0721  0.0218  -0.0225 258  ILE A CB  
2096 C  CG1 . ILE A 259 ? 0.2298 0.2601 0.1538 0.0754  0.0583  -0.0305 258  ILE A CG1 
2097 C  CG2 . ILE A 259 ? 0.1677 0.2433 0.1293 0.0402  -0.0148 -0.0346 258  ILE A CG2 
2098 C  CD1 . ILE A 259 ? 0.2703 0.2658 0.1445 0.0325  0.0699  -0.0201 258  ILE A CD1 
2099 N  N   . ILE A 260 ? 0.1842 0.2170 0.1278 0.0049  0.0396  -0.0040 259  ILE A N   
2100 C  CA  . ILE A 260 ? 0.1702 0.1865 0.1447 -0.0065 0.0626  -0.0179 259  ILE A CA  
2101 C  C   . ILE A 260 ? 0.1401 0.1936 0.1418 -0.0108 0.0338  0.0059  259  ILE A C   
2102 O  O   . ILE A 260 ? 0.1503 0.2140 0.1200 -0.0121 0.0272  0.0156  259  ILE A O   
2103 C  CB  . ILE A 260 ? 0.1932 0.1734 0.2090 0.0364  0.1043  -0.0193 259  ILE A CB  
2104 C  CG1 . ILE A 260 ? 0.3352 0.1868 0.2797 -0.0535 0.0913  -0.0226 259  ILE A CG1 
2105 C  CG2 . ILE A 260 ? 0.3398 0.1754 0.2261 -0.0306 0.0882  -0.0402 259  ILE A CG2 
2106 C  CD1 . ILE A 260 ? 0.4436 0.1963 0.3232 -0.1145 0.0872  0.0155  259  ILE A CD1 
2107 N  N   . THR A 261 ? 0.1772 0.1581 0.1150 0.0064  0.0192  0.0071  260  THR A N   
2108 C  CA  . THR A 261 ? 0.1273 0.1812 0.1556 -0.0169 0.0341  -0.0315 260  THR A CA  
2109 C  C   . THR A 261 ? 0.1804 0.1758 0.1663 0.0037  0.0402  -0.0651 260  THR A C   
2110 O  O   . THR A 261 ? 0.2025 0.1888 0.1676 -0.0256 0.0039  -0.0526 260  THR A O   
2111 C  CB  . THR A 261 ? 0.1604 0.1923 0.1574 -0.0488 0.0028  -0.0022 260  THR A CB  
2112 O  OG1 . THR A 261 ? 0.1460 0.2050 0.1612 -0.0246 0.0409  0.0071  260  THR A OG1 
2113 C  CG2 . THR A 261 ? 0.1931 0.1616 0.1908 -0.0643 0.0284  -0.0174 260  THR A CG2 
2114 N  N   . PHE A 262 ? 0.1832 0.1602 0.1314 -0.0055 0.0132  -0.0639 261  PHE A N   
2115 C  CA  . PHE A 262 ? 0.2008 0.1657 0.1400 -0.0205 0.0124  -0.0263 261  PHE A CA  
2116 C  C   . PHE A 262 ? 0.1845 0.1818 0.1374 -0.0379 0.0405  -0.0264 261  PHE A C   
2117 O  O   . PHE A 262 ? 0.2111 0.1783 0.1644 -0.0652 0.0259  -0.0479 261  PHE A O   
2118 C  CB  . PHE A 262 ? 0.1920 0.1522 0.1553 -0.0381 0.0493  -0.0150 261  PHE A CB  
2119 C  CG  . PHE A 262 ? 0.1249 0.1418 0.2144 -0.0102 -0.0210 0.0011  261  PHE A CG  
2120 C  CD1 . PHE A 262 ? 0.1998 0.1800 0.2188 -0.0054 0.0240  -0.0098 261  PHE A CD1 
2121 C  CD2 . PHE A 262 ? 0.2754 0.2094 0.2235 -0.0241 -0.0051 -0.0068 261  PHE A CD2 
2122 C  CE1 . PHE A 262 ? 0.1870 0.1824 0.2327 -0.0150 -0.0168 -0.0429 261  PHE A CE1 
2123 C  CE2 . PHE A 262 ? 0.1947 0.2139 0.2517 -0.0829 0.0042  -0.0189 261  PHE A CE2 
2124 C  CZ  . PHE A 262 ? 0.2360 0.1977 0.2435 -0.0121 0.0395  -0.0501 261  PHE A CZ  
2125 N  N   . LEU A 263 ? 0.2328 0.1702 0.1282 0.0074  -0.0073 -0.0199 262  LEU A N   
2126 C  CA  . LEU A 263 ? 0.2378 0.2365 0.1403 -0.0311 0.0097  -0.0114 262  LEU A CA  
2127 C  C   . LEU A 263 ? 0.1589 0.2861 0.1630 0.0019  0.0340  -0.0008 262  LEU A C   
2128 O  O   . LEU A 263 ? 0.1646 0.3347 0.1881 -0.0507 0.0033  -0.0241 262  LEU A O   
2129 C  CB  . LEU A 263 ? 0.1701 0.2487 0.1228 -0.0337 0.0156  0.0010  262  LEU A CB  
2130 C  CG  . LEU A 263 ? 0.1560 0.2191 0.1253 -0.0470 0.0379  -0.0333 262  LEU A CG  
2131 C  CD1 . LEU A 263 ? 0.1909 0.2212 0.1500 -0.0129 0.0685  -0.0071 262  LEU A CD1 
2132 C  CD2 . LEU A 263 ? 0.1935 0.2178 0.1387 -0.0531 0.0130  -0.0428 262  LEU A CD2 
2133 N  N   . ILE A 264 ? 0.1631 0.2885 0.1550 -0.0010 0.0410  -0.0050 263  ILE A N   
2134 C  CA  . ILE A 264 ? 0.1667 0.2626 0.1828 0.0031  0.0347  0.0156  263  ILE A CA  
2135 C  C   . ILE A 264 ? 0.0973 0.2627 0.1607 -0.0381 0.0459  -0.0272 263  ILE A C   
2136 O  O   . ILE A 264 ? 0.1320 0.3333 0.1800 -0.0523 0.0586  -0.0221 263  ILE A O   
2137 C  CB  . ILE A 264 ? 0.1861 0.2432 0.2201 0.0129  0.0693  0.0491  263  ILE A CB  
2138 C  CG1 . ILE A 264 ? 0.2531 0.2424 0.2624 0.0223  0.0535  0.0491  263  ILE A CG1 
2139 C  CG2 . ILE A 264 ? 0.1967 0.2215 0.2407 0.0370  0.0377  0.0133  263  ILE A CG2 
2140 C  CD1 . ILE A 264 ? 0.3269 0.2522 0.2862 0.0079  0.0033  -0.0008 263  ILE A CD1 
2141 N  N   . ALA A 265 ? 0.1528 0.2409 0.1658 -0.0455 0.0430  -0.0121 264  ALA A N   
2142 C  CA  . ALA A 265 ? 0.2040 0.2259 0.1516 -0.0398 0.0637  -0.0103 264  ALA A CA  
2143 C  C   . ALA A 265 ? 0.1753 0.2156 0.1672 -0.0481 0.0452  -0.0019 264  ALA A C   
2144 O  O   . ALA A 265 ? 0.1973 0.2339 0.2093 -0.0224 0.0145  -0.0031 264  ALA A O   
2145 C  CB  . ALA A 265 ? 0.2310 0.2360 0.1356 0.0074  -0.0221 -0.0391 264  ALA A CB  
2146 N  N   . GLY A 266 ? 0.1879 0.2103 0.1887 -0.0140 0.0342  -0.0094 265  GLY A N   
2147 C  CA  . GLY A 266 ? 0.1716 0.2302 0.2134 -0.0513 -0.0203 -0.0104 265  GLY A CA  
2148 C  C   . GLY A 266 ? 0.1616 0.2434 0.2138 -0.0058 -0.0200 -0.0100 265  GLY A C   
2149 O  O   . GLY A 266 ? 0.2329 0.2446 0.2185 -0.0068 -0.0134 -0.0355 265  GLY A O   
2150 N  N   . HIS A 267 ? 0.1693 0.2291 0.1947 0.1082  0.0004  0.0280  266  HIS A N   
2151 C  CA  . HIS A 267 ? 0.1303 0.2624 0.1862 0.0737  -0.0124 0.0308  266  HIS A CA  
2152 C  C   . HIS A 267 ? 0.2128 0.2419 0.2012 0.0338  -0.0312 0.0035  266  HIS A C   
2153 O  O   . HIS A 267 ? 0.1724 0.2233 0.1906 -0.0043 -0.0118 -0.0028 266  HIS A O   
2154 C  CB  . HIS A 267 ? 0.1874 0.2719 0.1646 0.0631  -0.0204 0.0883  266  HIS A CB  
2155 C  CG  . HIS A 267 ? 0.1879 0.2935 0.1808 0.0416  0.0022  0.0733  266  HIS A CG  
2156 N  ND1 . HIS A 267 ? 0.2317 0.2930 0.1923 0.0338  0.0018  0.0239  266  HIS A ND1 
2157 C  CD2 . HIS A 267 ? 0.2406 0.3100 0.1640 0.0634  0.0459  0.0764  266  HIS A CD2 
2158 C  CE1 . HIS A 267 ? 0.2061 0.3143 0.1865 0.0667  0.0096  0.0425  266  HIS A CE1 
2159 N  NE2 . HIS A 267 ? 0.2484 0.3233 0.1653 0.0423  0.0428  0.0520  266  HIS A NE2 
2160 N  N   . GLU A 268 ? 0.1670 0.2496 0.1936 0.0106  -0.0690 0.0005  267  GLU A N   
2161 C  CA  . GLU A 268 ? 0.1672 0.2369 0.2149 0.0183  -0.0237 -0.0033 267  GLU A CA  
2162 C  C   . GLU A 268 ? 0.1766 0.2569 0.2189 0.0320  0.0120  0.0177  267  GLU A C   
2163 O  O   . GLU A 268 ? 0.2033 0.2970 0.2363 0.0398  0.0653  0.0858  267  GLU A O   
2164 C  CB  . GLU A 268 ? 0.1180 0.2141 0.2602 0.0508  0.0163  0.0162  267  GLU A CB  
2165 C  CG  . GLU A 268 ? 0.2229 0.2631 0.2636 0.0761  0.0297  0.0226  267  GLU A CG  
2166 C  CD  . GLU A 268 ? 0.3991 0.3172 0.2813 0.0482  0.0085  0.0047  267  GLU A CD  
2167 O  OE1 . GLU A 268 ? 0.4083 0.3433 0.2128 0.1388  -0.0397 -0.0331 267  GLU A OE1 
2168 O  OE2 . GLU A 268 ? 0.4875 0.3141 0.3316 0.0278  -0.0093 -0.0021 267  GLU A OE2 
2169 N  N   . THR A 269 ? 0.1083 0.1929 0.1750 0.0032  0.0134  0.0022  268  THR A N   
2170 C  CA  . THR A 269 ? 0.1349 0.1787 0.1639 -0.0047 -0.0082 0.0267  268  THR A CA  
2171 C  C   . THR A 269 ? 0.1676 0.1743 0.1696 -0.0207 0.0006  0.0300  268  THR A C   
2172 O  O   . THR A 269 ? 0.1609 0.1808 0.2129 0.0164  0.0151  0.0062  268  THR A O   
2173 C  CB  . THR A 269 ? 0.1889 0.1843 0.1849 0.0319  -0.0436 0.0082  268  THR A CB  
2174 O  OG1 . THR A 269 ? 0.1929 0.2087 0.2248 0.0353  0.0031  0.0441  268  THR A OG1 
2175 C  CG2 . THR A 269 ? 0.1871 0.1586 0.1853 0.0151  -0.0438 -0.0102 268  THR A CG2 
2176 N  N   . THR A 270 ? 0.1397 0.1690 0.1496 -0.0267 -0.0123 0.0161  269  THR A N   
2177 C  CA  . THR A 270 ? 0.0990 0.1570 0.1402 0.0096  -0.0206 -0.0121 269  THR A CA  
2178 C  C   . THR A 270 ? 0.2064 0.1775 0.1339 0.0569  0.0015  0.0200  269  THR A C   
2179 O  O   . THR A 270 ? 0.1892 0.1875 0.1340 0.0383  0.0181  0.0186  269  THR A O   
2180 C  CB  . THR A 270 ? 0.0848 0.1756 0.1788 0.0150  -0.0610 -0.0125 269  THR A CB  
2181 O  OG1 . THR A 270 ? 0.1152 0.1821 0.1799 0.0308  -0.0172 0.0153  269  THR A OG1 
2182 C  CG2 . THR A 270 ? 0.1129 0.1605 0.1608 0.0097  -0.0473 -0.0297 269  THR A CG2 
2183 N  N   A SER A 271 ? 0.2271 0.1704 0.1266 0.0724  0.0171  0.0335  270  SER A N   
2184 N  N   B SER A 271 ? 0.2145 0.1723 0.1157 0.0694  0.0106  0.0345  270  SER A N   
2185 C  CA  A SER A 271 ? 0.2014 0.1943 0.1129 0.0487  0.0046  0.0285  270  SER A CA  
2186 C  CA  B SER A 271 ? 0.2049 0.1816 0.0923 0.0536  -0.0046 0.0443  270  SER A CA  
2187 C  C   A SER A 271 ? 0.2176 0.2199 0.1406 0.0168  -0.0080 0.0215  270  SER A C   
2188 C  C   B SER A 271 ? 0.2135 0.1951 0.1156 0.0341  0.0049  0.0397  270  SER A C   
2189 O  O   A SER A 271 ? 0.1530 0.2336 0.1603 0.0096  -0.0150 0.0094  270  SER A O   
2190 O  O   B SER A 271 ? 0.1764 0.1908 0.1240 0.0331  0.0062  0.0495  270  SER A O   
2191 C  CB  A SER A 271 ? 0.2161 0.1956 0.1286 0.0177  -0.0036 0.0219  270  SER A CB  
2192 C  CB  B SER A 271 ? 0.2109 0.1780 0.0927 0.0360  -0.0300 0.0489  270  SER A CB  
2193 O  OG  A SER A 271 ? 0.1962 0.1886 0.1260 -0.0255 0.0234  0.0150  270  SER A OG  
2194 O  OG  B SER A 271 ? 0.2201 0.1765 0.0924 0.0277  -0.0308 0.0511  270  SER A OG  
2195 N  N   . GLY A 272 ? 0.2063 0.1954 0.1054 0.0414  0.0479  0.0332  271  GLY A N   
2196 C  CA  . GLY A 272 ? 0.1291 0.1503 0.0963 0.0354  0.0363  0.0415  271  GLY A CA  
2197 C  C   . GLY A 272 ? 0.1703 0.1992 0.0987 0.0201  0.0364  0.0201  271  GLY A C   
2198 O  O   . GLY A 272 ? 0.1297 0.2448 0.1281 0.0342  0.0224  0.0293  271  GLY A O   
2199 N  N   . LEU A 273 ? 0.1987 0.1682 0.1133 0.0260  -0.0026 0.0057  272  LEU A N   
2200 C  CA  . LEU A 273 ? 0.1970 0.1710 0.1268 0.0202  -0.0235 0.0250  272  LEU A CA  
2201 C  C   . LEU A 273 ? 0.1194 0.1975 0.1169 0.0201  -0.0017 0.0129  272  LEU A C   
2202 O  O   . LEU A 273 ? 0.1156 0.1914 0.1272 0.0100  0.0058  0.0227  272  LEU A O   
2203 C  CB  . LEU A 273 ? 0.1373 0.1732 0.1512 0.0363  0.0297  0.0296  272  LEU A CB  
2204 C  CG  . LEU A 273 ? 0.1480 0.1646 0.1550 0.0048  -0.0232 0.0273  272  LEU A CG  
2205 C  CD1 . LEU A 273 ? 0.1992 0.2118 0.1245 0.0046  -0.0196 0.0526  272  LEU A CD1 
2206 C  CD2 . LEU A 273 ? 0.1630 0.1378 0.1900 0.0348  -0.0401 -0.0005 272  LEU A CD2 
2207 N  N   . LEU A 274 ? 0.1407 0.2036 0.0847 0.0006  0.0061  0.0020  273  LEU A N   
2208 C  CA  . LEU A 274 ? 0.1028 0.1822 0.1067 0.0183  -0.0291 -0.0118 273  LEU A CA  
2209 C  C   . LEU A 274 ? 0.1587 0.1914 0.1307 0.0558  -0.0035 0.0145  273  LEU A C   
2210 O  O   . LEU A 274 ? 0.1636 0.2046 0.1440 -0.0033 0.0021  0.0229  273  LEU A O   
2211 C  CB  . LEU A 274 ? 0.1424 0.1425 0.0916 0.0230  0.0220  0.0055  273  LEU A CB  
2212 C  CG  . LEU A 274 ? 0.1192 0.1389 0.1585 -0.0075 0.0288  -0.0009 273  LEU A CG  
2213 C  CD1 . LEU A 274 ? 0.1287 0.1199 0.1500 0.0300  0.0385  0.0042  273  LEU A CD1 
2214 C  CD2 . LEU A 274 ? 0.2039 0.1643 0.1819 0.0142  -0.0201 -0.0091 273  LEU A CD2 
2215 N  N   . SER A 275 ? 0.1476 0.1914 0.1467 0.0986  0.0018  0.0135  274  SER A N   
2216 C  CA  . SER A 275 ? 0.1417 0.2114 0.1272 0.0446  0.0516  0.0608  274  SER A CA  
2217 C  C   . SER A 275 ? 0.1332 0.2601 0.1393 0.0165  0.0539  0.0596  274  SER A C   
2218 O  O   . SER A 275 ? 0.0998 0.2996 0.1520 0.0436  0.0310  0.0693  274  SER A O   
2219 C  CB  . SER A 275 ? 0.1439 0.2279 0.1296 -0.0214 0.0493  0.0609  274  SER A CB  
2220 O  OG  . SER A 275 ? 0.1293 0.2595 0.1502 -0.0053 0.0384  0.0651  274  SER A OG  
2221 N  N   . PHE A 276 ? 0.1502 0.2323 0.1147 0.0396  0.0089  0.0526  275  PHE A N   
2222 C  CA  . PHE A 276 ? 0.1447 0.2371 0.1299 -0.0213 0.0278  0.0524  275  PHE A CA  
2223 C  C   . PHE A 276 ? 0.1263 0.2531 0.1721 0.0030  0.0124  0.0523  275  PHE A C   
2224 O  O   . PHE A 276 ? 0.1394 0.2669 0.1829 0.0036  0.0160  0.0502  275  PHE A O   
2225 C  CB  . PHE A 276 ? 0.1512 0.2096 0.1354 0.0022  0.0044  0.0238  275  PHE A CB  
2226 C  CG  . PHE A 276 ? 0.0992 0.1908 0.1350 0.0486  0.0139  0.0121  275  PHE A CG  
2227 C  CD1 . PHE A 276 ? 0.1497 0.1774 0.1482 0.0351  0.0033  0.0154  275  PHE A CD1 
2228 C  CD2 . PHE A 276 ? 0.1219 0.1810 0.1162 0.0079  0.0111  0.0234  275  PHE A CD2 
2229 C  CE1 . PHE A 276 ? 0.1509 0.2142 0.1652 -0.0249 0.0165  0.0216  275  PHE A CE1 
2230 C  CE2 . PHE A 276 ? 0.1474 0.2018 0.1374 0.0231  -0.0186 0.0510  275  PHE A CE2 
2231 C  CZ  . PHE A 276 ? 0.1192 0.2252 0.1666 -0.0109 -0.0129 0.0531  275  PHE A CZ  
2232 N  N   . ALA A 277 ? 0.1440 0.2086 0.1592 -0.0139 -0.0099 0.0421  276  ALA A N   
2233 C  CA  . ALA A 277 ? 0.0587 0.2112 0.1720 0.0138  -0.0199 0.0123  276  ALA A CA  
2234 C  C   . ALA A 277 ? 0.0772 0.2453 0.1545 -0.0435 -0.0005 0.0310  276  ALA A C   
2235 O  O   . ALA A 277 ? 0.1123 0.2829 0.2007 -0.0729 0.0068  0.0223  276  ALA A O   
2236 C  CB  . ALA A 277 ? 0.1227 0.2171 0.2005 0.0277  0.0178  0.0131  276  ALA A CB  
2237 N  N   . LEU A 278 ? 0.1528 0.2744 0.1356 0.0250  0.0277  0.0547  277  LEU A N   
2238 C  CA  . LEU A 278 ? 0.1026 0.3164 0.1235 -0.0006 0.0216  0.0517  277  LEU A CA  
2239 C  C   . LEU A 278 ? 0.1029 0.3346 0.1513 -0.0113 -0.0268 0.0383  277  LEU A C   
2240 O  O   . LEU A 278 ? 0.0984 0.3465 0.1629 -0.0255 -0.0260 0.0235  277  LEU A O   
2241 C  CB  . LEU A 278 ? 0.1296 0.3317 0.1481 -0.0255 -0.0478 0.0579  277  LEU A CB  
2242 C  CG  . LEU A 278 ? 0.2383 0.3246 0.1615 -0.0438 -0.0231 0.0801  277  LEU A CG  
2243 C  CD1 . LEU A 278 ? 0.2525 0.3152 0.1767 -0.0360 -0.0453 0.0878  277  LEU A CD1 
2244 C  CD2 . LEU A 278 ? 0.2159 0.3147 0.1642 0.0064  -0.0045 0.0688  277  LEU A CD2 
2245 N  N   . TYR A 279 ? 0.1249 0.3111 0.1405 -0.0050 0.0236  0.0076  278  TYR A N   
2246 C  CA  . TYR A 279 ? 0.1288 0.3077 0.1806 0.0104  0.0140  0.0299  278  TYR A CA  
2247 C  C   . TYR A 279 ? 0.0913 0.3138 0.1553 0.0351  -0.0068 0.0475  278  TYR A C   
2248 O  O   . TYR A 279 ? 0.1066 0.3944 0.1878 0.0199  -0.0005 0.0737  278  TYR A O   
2249 C  CB  . TYR A 279 ? 0.1756 0.2915 0.1904 0.0180  0.0245  0.0291  278  TYR A CB  
2250 C  CG  . TYR A 279 ? 0.1188 0.2867 0.2021 0.0853  0.0162  0.0320  278  TYR A CG  
2251 C  CD1 . TYR A 279 ? 0.1081 0.3131 0.2008 0.0652  -0.0027 0.0486  278  TYR A CD1 
2252 C  CD2 . TYR A 279 ? 0.1197 0.3170 0.1957 0.0064  0.0576  0.0515  278  TYR A CD2 
2253 C  CE1 . TYR A 279 ? 0.1199 0.3327 0.2229 0.0672  0.0439  0.0367  278  TYR A CE1 
2254 C  CE2 . TYR A 279 ? 0.1310 0.3482 0.2140 0.0426  0.0374  0.0369  278  TYR A CE2 
2255 C  CZ  . TYR A 279 ? 0.1372 0.3367 0.2213 0.0634  0.0668  0.0331  278  TYR A CZ  
2256 O  OH  . TYR A 279 ? 0.1769 0.3937 0.2297 0.0609  0.0549  0.0238  278  TYR A OH  
2257 N  N   . PHE A 280 ? 0.1147 0.3610 0.1303 0.0211  -0.0031 0.0839  279  PHE A N   
2258 C  CA  . PHE A 280 ? 0.1581 0.3702 0.1356 -0.0046 -0.0130 0.0850  279  PHE A CA  
2259 C  C   . PHE A 280 ? 0.1807 0.3789 0.1410 -0.0302 -0.0244 0.0854  279  PHE A C   
2260 O  O   . PHE A 280 ? 0.1973 0.4173 0.1766 -0.0986 -0.0161 0.0610  279  PHE A O   
2261 C  CB  . PHE A 280 ? 0.1306 0.3456 0.1238 0.0402  -0.0156 0.0588  279  PHE A CB  
2262 C  CG  . PHE A 280 ? 0.1809 0.3674 0.1576 0.0450  0.0024  0.0491  279  PHE A CG  
2263 C  CD1 . PHE A 280 ? 0.1739 0.3659 0.1725 0.0600  0.0077  0.0384  279  PHE A CD1 
2264 C  CD2 . PHE A 280 ? 0.2548 0.3524 0.1675 0.0519  0.0133  0.0708  279  PHE A CD2 
2265 C  CE1 . PHE A 280 ? 0.2142 0.3662 0.1745 0.0506  0.0184  0.0568  279  PHE A CE1 
2266 C  CE2 . PHE A 280 ? 0.2353 0.3370 0.1697 0.0474  0.0566  0.0466  279  PHE A CE2 
2267 C  CZ  . PHE A 280 ? 0.2021 0.3508 0.1888 0.0495  0.0343  0.0550  279  PHE A CZ  
2268 N  N   . LEU A 281 ? 0.1916 0.3584 0.1460 -0.0031 0.0021  0.0878  280  LEU A N   
2269 C  CA  . LEU A 281 ? 0.1192 0.3751 0.1731 0.0043  0.0046  0.0464  280  LEU A CA  
2270 C  C   . LEU A 281 ? 0.1075 0.4071 0.1929 0.0176  0.0151  0.0468  280  LEU A C   
2271 O  O   . LEU A 281 ? 0.1274 0.4228 0.2160 -0.0160 -0.0172 0.0644  280  LEU A O   
2272 C  CB  . LEU A 281 ? 0.1149 0.3747 0.2013 0.0175  -0.0154 0.0373  280  LEU A CB  
2273 C  CG  . LEU A 281 ? 0.1077 0.3953 0.2094 0.0001  0.0278  0.0341  280  LEU A CG  
2274 C  CD1 . LEU A 281 ? 0.1699 0.4294 0.2264 0.0278  0.0016  0.0001  280  LEU A CD1 
2275 C  CD2 . LEU A 281 ? 0.2171 0.3805 0.2235 -0.0389 0.0408  0.0660  280  LEU A CD2 
2276 N  N   . VAL A 282 ? 0.1664 0.4172 0.2105 -0.0120 -0.0143 0.0914  281  VAL A N   
2277 C  CA  . VAL A 282 ? 0.1295 0.4343 0.1971 -0.0140 -0.0179 0.1263  281  VAL A CA  
2278 C  C   . VAL A 282 ? 0.1298 0.4076 0.2191 0.0377  -0.0200 0.0928  281  VAL A C   
2279 O  O   . VAL A 282 ? 0.1241 0.4556 0.2285 0.0024  -0.0163 0.0841  281  VAL A O   
2280 C  CB  . VAL A 282 ? 0.1277 0.4668 0.2087 -0.0305 -0.0042 0.0924  281  VAL A CB  
2281 C  CG1 . VAL A 282 ? 0.1797 0.4612 0.2300 0.0176  0.0727  0.0857  281  VAL A CG1 
2282 C  CG2 . VAL A 282 ? 0.1583 0.4347 0.2061 -0.0483 -0.0197 0.1045  281  VAL A CG2 
2283 N  N   . LYS A 283 ? 0.1480 0.4513 0.1987 0.0268  0.0159  0.1186  282  LYS A N   
2284 C  CA  . LYS A 283 ? 0.2166 0.4517 0.2186 0.0087  0.0570  0.1074  282  LYS A CA  
2285 C  C   . LYS A 283 ? 0.1400 0.4618 0.2312 0.0078  0.0368  0.0974  282  LYS A C   
2286 O  O   . LYS A 283 ? 0.2123 0.5099 0.2445 0.0444  0.0656  0.0861  282  LYS A O   
2287 C  CB  . LYS A 283 ? 0.2163 0.4532 0.1990 0.0351  0.0490  0.1093  282  LYS A CB  
2288 C  CG  . LYS A 283 ? 0.1443 0.4319 0.2240 0.0660  0.0148  0.1281  282  LYS A CG  
2289 C  CD  . LYS A 283 ? 0.1568 0.4565 0.2220 0.0467  0.0158  0.1193  282  LYS A CD  
2290 C  CE  . LYS A 283 ? 0.1647 0.4344 0.2417 0.0918  -0.0076 0.0946  282  LYS A CE  
2291 N  NZ  . LYS A 283 ? 0.1541 0.4235 0.2423 0.0974  0.0295  0.0888  282  LYS A NZ  
2292 N  N   . ASN A 284 ? 0.1363 0.4780 0.2295 -0.0421 -0.0187 0.0904  283  ASN A N   
2293 C  CA  . ASN A 284 ? 0.1575 0.4760 0.2355 -0.0729 -0.0223 0.0923  283  ASN A CA  
2294 C  C   . ASN A 284 ? 0.2420 0.4898 0.2855 -0.1180 -0.0445 0.1183  283  ASN A C   
2295 O  O   . ASN A 284 ? 0.2151 0.4886 0.2594 -0.1473 -0.0515 0.1217  283  ASN A O   
2296 C  CB  . ASN A 284 ? 0.1826 0.4788 0.2080 -0.0590 0.0035  0.0909  283  ASN A CB  
2297 C  CG  . ASN A 284 ? 0.1758 0.4668 0.1821 -0.0427 0.0391  0.0695  283  ASN A CG  
2298 O  OD1 . ASN A 284 ? 0.2104 0.4918 0.1875 -0.0026 0.0108  0.0777  283  ASN A OD1 
2299 N  ND2 . ASN A 284 ? 0.1365 0.4291 0.1703 -0.0549 0.0142  0.0629  283  ASN A ND2 
2300 N  N   . PRO A 285 ? 0.2563 0.5046 0.3347 -0.1171 -0.1252 0.1230  284  PRO A N   
2301 C  CA  . PRO A 285 ? 0.3647 0.5255 0.3566 -0.1046 -0.1622 0.1379  284  PRO A CA  
2302 C  C   . PRO A 285 ? 0.3071 0.5601 0.3529 -0.1264 -0.1479 0.1513  284  PRO A C   
2303 O  O   . PRO A 285 ? 0.3364 0.5366 0.3484 -0.1702 -0.1546 0.1454  284  PRO A O   
2304 C  CB  . PRO A 285 ? 0.3587 0.5065 0.3733 -0.0971 -0.1881 0.1391  284  PRO A CB  
2305 C  CG  . PRO A 285 ? 0.3586 0.5132 0.3840 -0.0755 -0.1388 0.1225  284  PRO A CG  
2306 C  CD  . PRO A 285 ? 0.3064 0.5003 0.3591 -0.0627 -0.1124 0.1291  284  PRO A CD  
2307 N  N   . HIS A 286 ? 0.2297 0.5989 0.3455 -0.1009 -0.0937 0.1532  285  HIS A N   
2308 C  CA  . HIS A 286 ? 0.2094 0.5842 0.3494 -0.1258 -0.0434 0.1370  285  HIS A CA  
2309 C  C   . HIS A 286 ? 0.2143 0.5046 0.3114 -0.1398 -0.0615 0.1348  285  HIS A C   
2310 O  O   . HIS A 286 ? 0.2267 0.5000 0.3036 -0.1448 -0.0808 0.1408  285  HIS A O   
2311 C  CB  . HIS A 286 ? 0.2036 0.6819 0.3893 -0.0896 -0.0238 0.1336  285  HIS A CB  
2312 C  CG  . HIS A 286 ? 0.3439 0.8128 0.4659 -0.1292 -0.1075 0.1076  285  HIS A CG  
2313 N  ND1 . HIS A 286 ? 0.4216 0.8463 0.4990 -0.1180 -0.1513 0.1004  285  HIS A ND1 
2314 C  CD2 . HIS A 286 ? 0.3208 0.8518 0.4950 -0.1253 -0.1289 0.1010  285  HIS A CD2 
2315 C  CE1 . HIS A 286 ? 0.4090 0.8556 0.5053 -0.0884 -0.1989 0.0965  285  HIS A CE1 
2316 N  NE2 . HIS A 286 ? 0.3645 0.8609 0.5192 -0.1040 -0.1890 0.0916  285  HIS A NE2 
2317 N  N   . VAL A 287 ? 0.2266 0.4650 0.2854 -0.1556 -0.0649 0.1135  286  VAL A N   
2318 C  CA  . VAL A 287 ? 0.1968 0.4165 0.2436 -0.1357 -0.0547 0.0972  286  VAL A CA  
2319 C  C   . VAL A 287 ? 0.2031 0.4228 0.2450 -0.1367 -0.0632 0.1190  286  VAL A C   
2320 O  O   . VAL A 287 ? 0.1639 0.4340 0.2499 -0.0963 -0.0419 0.1314  286  VAL A O   
2321 C  CB  . VAL A 287 ? 0.1734 0.4315 0.2136 -0.1115 -0.0115 0.0912  286  VAL A CB  
2322 C  CG1 . VAL A 287 ? 0.2211 0.4417 0.2001 -0.1100 -0.0644 0.1102  286  VAL A CG1 
2323 C  CG2 . VAL A 287 ? 0.2166 0.4530 0.1969 -0.0533 0.0172  0.0675  286  VAL A CG2 
2324 N  N   . LEU A 288 ? 0.1984 0.3998 0.2444 -0.1356 -0.0595 0.0994  287  LEU A N   
2325 C  CA  . LEU A 288 ? 0.2514 0.4152 0.2462 -0.1641 -0.0546 0.1248  287  LEU A CA  
2326 C  C   . LEU A 288 ? 0.2278 0.4238 0.2572 -0.1527 -0.0760 0.0984  287  LEU A C   
2327 O  O   . LEU A 288 ? 0.2955 0.4279 0.2663 -0.1646 -0.1075 0.1049  287  LEU A O   
2328 C  CB  . LEU A 288 ? 0.2720 0.4428 0.2528 -0.1795 -0.0555 0.1228  287  LEU A CB  
2329 C  CG  . LEU A 288 ? 0.3501 0.4387 0.2733 -0.2025 -0.0712 0.1339  287  LEU A CG  
2330 C  CD1 . LEU A 288 ? 0.3406 0.4273 0.3041 -0.2144 -0.0676 0.1095  287  LEU A CD1 
2331 C  CD2 . LEU A 288 ? 0.3563 0.4505 0.2699 -0.1658 -0.0896 0.1331  287  LEU A CD2 
2332 N  N   . GLN A 289 ? 0.1940 0.4249 0.2897 -0.1188 -0.0782 0.0913  288  GLN A N   
2333 C  CA  . GLN A 289 ? 0.1950 0.4211 0.3184 -0.1365 -0.0321 0.0815  288  GLN A CA  
2334 C  C   . GLN A 289 ? 0.2756 0.4042 0.2949 -0.1581 -0.0456 0.0841  288  GLN A C   
2335 O  O   . GLN A 289 ? 0.3131 0.4010 0.3060 -0.1759 -0.0862 0.0817  288  GLN A O   
2336 C  CB  . GLN A 289 ? 0.3465 0.4439 0.3957 -0.1751 -0.0148 0.0664  288  GLN A CB  
2337 C  CG  . GLN A 289 ? 0.3385 0.4390 0.4728 -0.2168 0.0447  0.0483  288  GLN A CG  
2338 C  CD  . GLN A 289 ? 0.5858 0.4834 0.5484 -0.2286 0.0001  0.0085  288  GLN A CD  
2339 O  OE1 . GLN A 289 ? 0.6672 0.4970 0.5757 -0.2291 -0.0367 0.0011  288  GLN A OE1 
2340 N  NE2 . GLN A 289 ? 0.6930 0.5212 0.5782 -0.1910 0.0020  -0.0080 288  GLN A NE2 
2341 N  N   . LYS A 290 ? 0.2648 0.3936 0.2767 -0.1192 -0.0556 0.0843  289  LYS A N   
2342 C  CA  . LYS A 290 ? 0.2642 0.3587 0.2495 -0.1357 -0.0236 0.1053  289  LYS A CA  
2343 C  C   . LYS A 290 ? 0.2938 0.3423 0.2390 -0.0983 -0.0004 0.1007  289  LYS A C   
2344 O  O   . LYS A 290 ? 0.2861 0.3479 0.2435 -0.0845 -0.0050 0.0908  289  LYS A O   
2345 C  CB  . LYS A 290 ? 0.2699 0.3789 0.2570 -0.0725 -0.0397 0.0937  289  LYS A CB  
2346 C  CG  . LYS A 290 ? 0.3858 0.3953 0.2563 -0.0990 0.0027  0.1050  289  LYS A CG  
2347 C  CD  . LYS A 290 ? 0.3824 0.4069 0.2506 -0.1255 -0.0474 0.1084  289  LYS A CD  
2348 C  CE  . LYS A 290 ? 0.3533 0.4404 0.2414 -0.1385 -0.0533 0.1006  289  LYS A CE  
2349 N  NZ  . LYS A 290 ? 0.4069 0.4573 0.2710 -0.1336 -0.0915 0.0896  289  LYS A NZ  
2350 N  N   . ALA A 291 ? 0.3010 0.3335 0.2005 -0.1234 -0.0031 0.0944  290  ALA A N   
2351 C  CA  . ALA A 291 ? 0.2782 0.3077 0.2072 -0.1437 0.0158  0.0694  290  ALA A CA  
2352 C  C   . ALA A 291 ? 0.2534 0.3260 0.1922 -0.1403 -0.0413 0.0606  290  ALA A C   
2353 O  O   . ALA A 291 ? 0.2854 0.3435 0.1969 -0.1828 -0.0500 0.0524  290  ALA A O   
2354 C  CB  . ALA A 291 ? 0.2752 0.2952 0.2110 -0.1248 0.0335  0.0758  290  ALA A CB  
2355 N  N   . ALA A 292 ? 0.1675 0.3178 0.2111 -0.0997 -0.0688 0.0414  291  ALA A N   
2356 C  CA  . ALA A 292 ? 0.2848 0.3292 0.1886 -0.1464 -0.0797 0.0748  291  ALA A CA  
2357 C  C   . ALA A 292 ? 0.3487 0.3674 0.2131 -0.1793 -0.0775 0.0753  291  ALA A C   
2358 O  O   . ALA A 292 ? 0.3691 0.3573 0.2310 -0.1892 -0.1116 0.0612  291  ALA A O   
2359 C  CB  . ALA A 292 ? 0.3029 0.3314 0.1833 -0.1762 -0.0846 0.0755  291  ALA A CB  
2360 N  N   . GLU A 293 ? 0.2852 0.3790 0.2124 -0.1821 -0.0484 0.0909  292  GLU A N   
2361 C  CA  . GLU A 293 ? 0.2621 0.4056 0.2478 -0.1780 -0.0351 0.0849  292  GLU A CA  
2362 C  C   . GLU A 293 ? 0.2901 0.3700 0.2785 -0.1892 -0.0494 0.0613  292  GLU A C   
2363 O  O   . GLU A 293 ? 0.3006 0.3560 0.2862 -0.1861 -0.0739 0.0540  292  GLU A O   
2364 C  CB  . GLU A 293 ? 0.2779 0.4805 0.2795 -0.1958 -0.0406 0.0918  292  GLU A CB  
2365 C  CG  . GLU A 293 ? 0.2838 0.5278 0.3120 -0.1998 -0.0188 0.0911  292  GLU A CG  
2366 C  CD  . GLU A 293 ? 0.4087 0.6149 0.3494 -0.2534 -0.0104 0.1214  292  GLU A CD  
2367 O  OE1 . GLU A 293 ? 0.5540 0.6340 0.3768 -0.2193 0.0005  0.1368  292  GLU A OE1 
2368 O  OE2 . GLU A 293 ? 0.3697 0.6133 0.3501 -0.2408 -0.0017 0.1156  292  GLU A OE2 
2369 N  N   . GLU A 294 ? 0.2449 0.3374 0.2739 -0.1614 -0.0546 0.0663  293  GLU A N   
2370 C  CA  . GLU A 294 ? 0.2790 0.3045 0.2503 -0.1677 -0.0656 0.0552  293  GLU A CA  
2371 C  C   . GLU A 294 ? 0.3696 0.3015 0.2390 -0.1761 -0.0900 0.0722  293  GLU A C   
2372 O  O   . GLU A 294 ? 0.4002 0.3064 0.2280 -0.1634 -0.0744 0.0640  293  GLU A O   
2373 C  CB  . GLU A 294 ? 0.2790 0.2785 0.2238 -0.1610 -0.0606 0.0386  293  GLU A CB  
2374 C  CG  . GLU A 294 ? 0.3350 0.2864 0.2074 -0.1698 -0.0707 0.0466  293  GLU A CG  
2375 C  CD  . GLU A 294 ? 0.2885 0.2876 0.1867 -0.1649 -0.0454 0.0663  293  GLU A CD  
2376 O  OE1 . GLU A 294 ? 0.3224 0.2980 0.1824 -0.1678 -0.0389 0.0726  293  GLU A OE1 
2377 O  OE2 . GLU A 294 ? 0.3050 0.3384 0.2040 -0.1219 -0.0410 0.0256  293  GLU A OE2 
2378 N  N   . ALA A 295 ? 0.3536 0.2859 0.2305 -0.1639 -0.1024 0.0827  294  ALA A N   
2379 C  CA  . ALA A 295 ? 0.3687 0.2749 0.2217 -0.1753 -0.0780 0.0803  294  ALA A CA  
2380 C  C   . ALA A 295 ? 0.3949 0.3024 0.2232 -0.1856 -0.1184 0.0721  294  ALA A C   
2381 O  O   . ALA A 295 ? 0.4618 0.3051 0.2223 -0.2048 -0.1134 0.0680  294  ALA A O   
2382 C  CB  . ALA A 295 ? 0.3310 0.2715 0.2123 -0.0864 -0.0365 0.0752  294  ALA A CB  
2383 N  N   . ALA A 296 ? 0.3906 0.3116 0.2257 -0.1881 -0.1160 0.0705  295  ALA A N   
2384 C  CA  . ALA A 296 ? 0.3777 0.3393 0.2574 -0.1880 -0.1014 0.0257  295  ALA A CA  
2385 C  C   . ALA A 296 ? 0.4231 0.3467 0.2691 -0.1781 -0.0941 0.0226  295  ALA A C   
2386 O  O   . ALA A 296 ? 0.3726 0.3268 0.2965 -0.1385 -0.0763 0.0118  295  ALA A O   
2387 C  CB  . ALA A 296 ? 0.3729 0.3664 0.2551 -0.1959 -0.0906 0.0169  295  ALA A CB  
2388 N  N   . ARG A 297 ? 0.4674 0.3456 0.2674 -0.1700 -0.0740 0.0376  296  ARG A N   
2389 C  CA  . ARG A 297 ? 0.4680 0.3256 0.2713 -0.1756 -0.0664 0.0363  296  ARG A CA  
2390 C  C   . ARG A 297 ? 0.4690 0.3103 0.2632 -0.1294 -0.0977 0.0527  296  ARG A C   
2391 O  O   . ARG A 297 ? 0.4740 0.3444 0.2638 -0.1513 -0.1259 0.0642  296  ARG A O   
2392 C  CB  . ARG A 297 ? 0.5154 0.3315 0.2887 -0.1950 -0.0284 0.0195  296  ARG A CB  
2393 C  CG  . ARG A 297 ? 0.5670 0.3687 0.3116 -0.1939 0.0106  0.0210  296  ARG A CG  
2394 C  CD  . ARG A 297 ? 0.6679 0.4180 0.3729 -0.2165 0.0556  0.0204  296  ARG A CD  
2395 N  NE  . ARG A 297 ? 0.7869 0.4611 0.4105 -0.2629 0.0610  0.0450  296  ARG A NE  
2396 C  CZ  . ARG A 297 ? 0.9371 0.5013 0.4411 -0.2231 0.1122  0.0982  296  ARG A CZ  
2397 N  NH1 . ARG A 297 ? 0.9010 0.5385 0.4437 -0.2244 0.1180  0.1285  296  ARG A NH1 
2398 N  NH2 . ARG A 297 ? 0.9363 0.4744 0.4492 -0.1652 0.1850  0.1138  296  ARG A NH2 
2399 N  N   . VAL A 298 ? 0.3835 0.2617 0.2424 -0.1585 -0.1137 0.0333  297  VAL A N   
2400 C  CA  . VAL A 298 ? 0.3693 0.2406 0.2346 -0.1279 -0.0622 0.0283  297  VAL A CA  
2401 C  C   . VAL A 298 ? 0.4408 0.2532 0.2729 -0.0992 -0.0769 0.0323  297  VAL A C   
2402 O  O   . VAL A 298 ? 0.4868 0.2502 0.2688 -0.1016 -0.1009 0.0062  297  VAL A O   
2403 C  CB  . VAL A 298 ? 0.3446 0.2288 0.2238 -0.1527 -0.0460 0.0019  297  VAL A CB  
2404 C  CG1 . VAL A 298 ? 0.2933 0.2181 0.2237 -0.1306 -0.0559 -0.0032 297  VAL A CG1 
2405 C  CG2 . VAL A 298 ? 0.4413 0.2159 0.2164 -0.1494 -0.0201 -0.0268 297  VAL A CG2 
2406 N  N   . LEU A 299 ? 0.4160 0.2465 0.2788 -0.1054 -0.1354 0.0307  298  LEU A N   
2407 C  CA  . LEU A 299 ? 0.4383 0.2206 0.2442 -0.1148 -0.0857 0.0265  298  LEU A CA  
2408 C  C   . LEU A 299 ? 0.5147 0.2572 0.2471 -0.1200 -0.1165 0.0167  298  LEU A C   
2409 O  O   . LEU A 299 ? 0.4696 0.2959 0.2144 -0.1162 -0.0977 -0.0017 298  LEU A O   
2410 C  CB  . LEU A 299 ? 0.3944 0.2066 0.2393 -0.1040 -0.0585 0.0029  298  LEU A CB  
2411 C  CG  . LEU A 299 ? 0.3004 0.2110 0.2419 -0.0946 -0.0796 0.0220  298  LEU A CG  
2412 C  CD1 . LEU A 299 ? 0.3583 0.1821 0.2436 -0.0782 -0.0328 0.0386  298  LEU A CD1 
2413 C  CD2 . LEU A 299 ? 0.4267 0.2350 0.2388 -0.0565 -0.0855 0.0166  298  LEU A CD2 
2414 N  N   . VAL A 300 ? 0.5738 0.2461 0.2547 -0.1355 -0.1169 -0.0051 299  VAL A N   
2415 C  CA  . VAL A 300 ? 0.6172 0.2436 0.2528 -0.1573 -0.1049 0.0108  299  VAL A CA  
2416 C  C   . VAL A 300 ? 0.6107 0.2659 0.2637 -0.1614 -0.1027 -0.0086 299  VAL A C   
2417 O  O   . VAL A 300 ? 0.5773 0.2959 0.2543 -0.2012 -0.0857 0.0063  299  VAL A O   
2418 C  CB  . VAL A 300 ? 0.6160 0.2675 0.2559 -0.1492 -0.0813 0.0293  299  VAL A CB  
2419 C  CG1 . VAL A 300 ? 0.5930 0.2664 0.2402 -0.1944 -0.0347 0.0332  299  VAL A CG1 
2420 C  CG2 . VAL A 300 ? 0.6296 0.2789 0.2624 -0.1382 -0.0673 0.0299  299  VAL A CG2 
2421 N  N   . ASP A 301 ? 0.5978 0.2784 0.2662 -0.1218 -0.0980 0.0115  300  ASP A N   
2422 C  CA  . ASP A 301 ? 0.5803 0.2962 0.2514 -0.0716 -0.1101 -0.0001 300  ASP A CA  
2423 C  C   . ASP A 301 ? 0.5513 0.3095 0.2338 -0.0859 -0.1158 0.0088  300  ASP A C   
2424 O  O   . ASP A 301 ? 0.5512 0.3273 0.2499 -0.0051 -0.0553 0.0222  300  ASP A O   
2425 C  CB  . ASP A 301 ? 0.5237 0.2839 0.2484 -0.0260 -0.1327 -0.0082 300  ASP A CB  
2426 C  CG  . ASP A 301 ? 0.6014 0.2957 0.2720 -0.0290 -0.1415 -0.0476 300  ASP A CG  
2427 O  OD1 . ASP A 301 ? 0.5693 0.2769 0.3010 -0.0848 -0.1452 -0.0553 300  ASP A OD1 
2428 O  OD2 . ASP A 301 ? 0.7524 0.2962 0.2717 0.0225  -0.1379 -0.0351 300  ASP A OD2 
2429 N  N   . PRO A 302 ? 0.5527 0.3073 0.2286 -0.1318 -0.1163 -0.0172 301  PRO A N   
2430 C  CA  . PRO A 302 ? 0.5339 0.2887 0.2252 -0.1508 -0.1123 -0.0040 301  PRO A CA  
2431 C  C   . PRO A 302 ? 0.5874 0.2975 0.2209 -0.1389 -0.0868 0.0167  301  PRO A C   
2432 O  O   . PRO A 302 ? 0.5831 0.3217 0.2380 -0.1164 -0.0840 0.0316  301  PRO A O   
2433 C  CB  . PRO A 302 ? 0.5347 0.2823 0.2323 -0.1449 -0.1055 -0.0181 301  PRO A CB  
2434 C  CG  . PRO A 302 ? 0.5450 0.2958 0.2541 -0.1696 -0.0830 -0.0316 301  PRO A CG  
2435 C  CD  . PRO A 302 ? 0.5578 0.2868 0.2321 -0.1542 -0.0739 -0.0355 301  PRO A CD  
2436 N  N   . VAL A 303 ? 0.5741 0.3167 0.2354 -0.1442 -0.0696 0.0137  302  VAL A N   
2437 C  CA  . VAL A 303 ? 0.5330 0.3736 0.2497 -0.1288 -0.1323 0.0535  302  VAL A CA  
2438 C  C   . VAL A 303 ? 0.5253 0.3311 0.2767 -0.0943 -0.1183 0.0591  302  VAL A C   
2439 O  O   . VAL A 303 ? 0.4720 0.3228 0.2813 -0.0403 -0.1619 0.0360  302  VAL A O   
2440 C  CB  . VAL A 303 ? 0.6036 0.4290 0.2497 -0.1356 -0.1217 0.0678  302  VAL A CB  
2441 C  CG1 . VAL A 303 ? 0.6678 0.4477 0.2743 -0.1373 -0.0976 0.0679  302  VAL A CG1 
2442 C  CG2 . VAL A 303 ? 0.6346 0.4525 0.2861 -0.1460 -0.1051 0.0778  302  VAL A CG2 
2443 N  N   . PRO A 304 ? 0.4679 0.2892 0.2875 -0.0852 -0.1121 0.0654  303  PRO A N   
2444 C  CA  . PRO A 304 ? 0.4160 0.2586 0.2707 -0.0613 -0.0981 0.0397  303  PRO A CA  
2445 C  C   . PRO A 304 ? 0.4112 0.2189 0.2290 0.0004  -0.1199 0.0190  303  PRO A C   
2446 O  O   . PRO A 304 ? 0.3576 0.2336 0.2113 -0.0100 -0.0493 0.0067  303  PRO A O   
2447 C  CB  . PRO A 304 ? 0.4485 0.2769 0.2950 -0.0490 -0.1051 0.0526  303  PRO A CB  
2448 C  CG  . PRO A 304 ? 0.4265 0.2950 0.3201 -0.0232 -0.1149 0.0789  303  PRO A CG  
2449 C  CD  . PRO A 304 ? 0.4334 0.2971 0.3076 -0.0342 -0.1156 0.0650  303  PRO A CD  
2450 N  N   . SER A 305 ? 0.3263 0.1818 0.2214 0.0346  -0.1395 0.0218  304  SER A N   
2451 C  CA  . SER A 305 ? 0.3562 0.1396 0.2268 0.0296  -0.1111 0.0344  304  SER A CA  
2452 C  C   . SER A 305 ? 0.3204 0.1608 0.2275 -0.0068 -0.1094 0.0059  304  SER A C   
2453 O  O   . SER A 305 ? 0.3481 0.1408 0.2134 0.0129  -0.0372 -0.0292 304  SER A O   
2454 C  CB  . SER A 305 ? 0.3266 0.1282 0.2481 0.0059  -0.0489 0.0244  304  SER A CB  
2455 O  OG  . SER A 305 ? 0.3680 0.1562 0.2515 0.0061  -0.0711 -0.0022 304  SER A OG  
2456 N  N   . TYR A 306 ? 0.2531 0.1801 0.2301 0.0034  -0.1112 0.0085  305  TYR A N   
2457 C  CA  . TYR A 306 ? 0.2813 0.1812 0.2364 -0.0154 -0.0913 0.0101  305  TYR A CA  
2458 C  C   . TYR A 306 ? 0.3325 0.1622 0.2351 0.0019  -0.0648 -0.0055 305  TYR A C   
2459 O  O   . TYR A 306 ? 0.3647 0.1561 0.2310 0.0035  -0.0571 -0.0033 305  TYR A O   
2460 C  CB  . TYR A 306 ? 0.2556 0.2245 0.2546 -0.0576 -0.0704 -0.0084 305  TYR A CB  
2461 C  CG  . TYR A 306 ? 0.2828 0.2747 0.2593 -0.0543 -0.0473 -0.0132 305  TYR A CG  
2462 C  CD1 . TYR A 306 ? 0.2144 0.2966 0.2775 -0.0595 -0.0432 -0.0147 305  TYR A CD1 
2463 C  CD2 . TYR A 306 ? 0.2781 0.3319 0.2682 -0.0655 -0.0690 -0.0241 305  TYR A CD2 
2464 C  CE1 . TYR A 306 ? 0.2959 0.3185 0.2922 -0.0608 -0.0604 -0.0667 305  TYR A CE1 
2465 C  CE2 . TYR A 306 ? 0.2497 0.3502 0.2641 -0.0696 -0.0678 -0.0614 305  TYR A CE2 
2466 C  CZ  . TYR A 306 ? 0.3492 0.3595 0.2821 -0.0595 -0.0549 -0.0810 305  TYR A CZ  
2467 O  OH  . TYR A 306 ? 0.4902 0.3951 0.3107 -0.0428 -0.0266 -0.1143 305  TYR A OH  
2468 N  N   . LYS A 307 ? 0.3855 0.1584 0.2472 -0.0169 -0.0976 0.0004  306  LYS A N   
2469 C  CA  . LYS A 307 ? 0.3779 0.1458 0.2718 0.0220  -0.0601 0.0210  306  LYS A CA  
2470 C  C   . LYS A 307 ? 0.4101 0.1539 0.2336 -0.0120 -0.0663 0.0242  306  LYS A C   
2471 O  O   . LYS A 307 ? 0.5038 0.1731 0.1952 -0.0614 -0.0930 0.0240  306  LYS A O   
2472 C  CB  . LYS A 307 ? 0.3847 0.1519 0.3816 0.0979  -0.0244 -0.0077 306  LYS A CB  
2473 C  CG  . LYS A 307 ? 0.5276 0.1962 0.4574 0.0940  -0.0561 -0.0292 306  LYS A CG  
2474 C  CD  . LYS A 307 ? 0.6451 0.2535 0.5141 0.1186  -0.0394 -0.0440 306  LYS A CD  
2475 C  CE  . LYS A 307 ? 0.7267 0.2989 0.5555 0.1124  -0.0307 -0.0459 306  LYS A CE  
2476 N  NZ  . LYS A 307 ? 0.7724 0.3539 0.5823 0.0976  -0.0194 -0.0412 306  LYS A NZ  
2477 N  N   . GLN A 308 ? 0.4010 0.1322 0.2430 -0.0224 -0.0620 0.0249  307  GLN A N   
2478 C  CA  . GLN A 308 ? 0.3249 0.1375 0.2359 -0.0179 -0.0749 0.0093  307  GLN A CA  
2479 C  C   . GLN A 308 ? 0.3428 0.1623 0.2408 -0.0706 -0.0903 0.0059  307  GLN A C   
2480 O  O   . GLN A 308 ? 0.3856 0.2007 0.2605 -0.0761 -0.1166 0.0163  307  GLN A O   
2481 C  CB  . GLN A 308 ? 0.3588 0.1286 0.2295 -0.0547 -0.0992 0.0018  307  GLN A CB  
2482 C  CG  . GLN A 308 ? 0.3740 0.1256 0.2453 -0.0662 -0.0730 0.0013  307  GLN A CG  
2483 C  CD  . GLN A 308 ? 0.4013 0.1563 0.2815 -0.0941 -0.1039 0.0149  307  GLN A CD  
2484 O  OE1 . GLN A 308 ? 0.4535 0.2011 0.2924 -0.1215 -0.1003 0.0097  307  GLN A OE1 
2485 N  NE2 . GLN A 308 ? 0.4793 0.1649 0.3013 -0.0764 -0.0465 0.0426  307  GLN A NE2 
2486 N  N   . VAL A 309 ? 0.3378 0.1469 0.2238 -0.0804 -0.0992 0.0019  308  VAL A N   
2487 C  CA  . VAL A 309 ? 0.3517 0.1537 0.2004 -0.0486 -0.1028 0.0071  308  VAL A CA  
2488 C  C   . VAL A 309 ? 0.3326 0.1563 0.1979 -0.0543 -0.0734 -0.0124 308  VAL A C   
2489 O  O   . VAL A 309 ? 0.3630 0.1527 0.1959 -0.0488 -0.0317 0.0094  308  VAL A O   
2490 C  CB  . VAL A 309 ? 0.3342 0.1489 0.1953 0.0020  -0.0619 0.0020  308  VAL A CB  
2491 C  CG1 . VAL A 309 ? 0.2841 0.1564 0.1954 0.0118  -0.0229 0.0175  308  VAL A CG1 
2492 C  CG2 . VAL A 309 ? 0.3352 0.1526 0.2003 -0.0133 -0.0065 -0.0246 308  VAL A CG2 
2493 N  N   . LYS A 310 ? 0.3458 0.1595 0.1881 -0.0336 -0.0643 -0.0072 309  LYS A N   
2494 C  CA  . LYS A 310 ? 0.3296 0.1910 0.2187 -0.0155 -0.0576 0.0251  309  LYS A CA  
2495 C  C   . LYS A 310 ? 0.3018 0.2241 0.2098 -0.0443 -0.0318 0.0396  309  LYS A C   
2496 O  O   . LYS A 310 ? 0.3396 0.2379 0.1864 -0.0875 -0.0229 0.0199  309  LYS A O   
2497 C  CB  . LYS A 310 ? 0.3596 0.2152 0.2457 -0.0610 -0.0700 0.0335  309  LYS A CB  
2498 C  CG  . LYS A 310 ? 0.3640 0.2397 0.3104 -0.0783 -0.0828 0.0010  309  LYS A CG  
2499 C  CD  . LYS A 310 ? 0.4502 0.2194 0.3915 -0.1025 -0.0444 -0.0151 309  LYS A CD  
2500 C  CE  . LYS A 310 ? 0.5639 0.2756 0.4337 -0.0983 -0.0240 -0.0386 309  LYS A CE  
2501 N  NZ  . LYS A 310 ? 0.6529 0.2879 0.4588 -0.1600 -0.0387 -0.0816 309  LYS A NZ  
2502 N  N   . GLN A 311 ? 0.3069 0.2184 0.2243 -0.0568 -0.0405 0.0455  310  GLN A N   
2503 C  CA  . GLN A 311 ? 0.2499 0.2211 0.2465 -0.0842 -0.0170 0.0310  310  GLN A CA  
2504 C  C   . GLN A 311 ? 0.2888 0.1936 0.2266 -0.0617 -0.0446 0.0205  310  GLN A C   
2505 O  O   . GLN A 311 ? 0.3635 0.1912 0.2408 -0.0795 -0.0547 0.0115  310  GLN A O   
2506 C  CB  . GLN A 311 ? 0.2967 0.2580 0.2546 -0.0516 0.0252  0.0218  310  GLN A CB  
2507 C  CG  . GLN A 311 ? 0.4595 0.2920 0.2959 -0.0578 0.0282  0.0379  310  GLN A CG  
2508 C  CD  . GLN A 311 ? 0.4951 0.3708 0.3395 -0.0534 0.0418  0.0281  310  GLN A CD  
2509 O  OE1 . GLN A 311 ? 0.5081 0.4094 0.3516 -0.0961 0.0494  0.0462  310  GLN A OE1 
2510 N  NE2 . GLN A 311 ? 0.4985 0.3710 0.3537 -0.0228 0.0227  0.0199  310  GLN A NE2 
2511 N  N   . LEU A 312 ? 0.3146 0.1992 0.1739 -0.0813 -0.0393 0.0328  311  LEU A N   
2512 C  CA  . LEU A 312 ? 0.3311 0.1760 0.1739 -0.0880 -0.0547 0.0095  311  LEU A CA  
2513 C  C   . LEU A 312 ? 0.3478 0.2214 0.1925 -0.0614 -0.0353 0.0030  311  LEU A C   
2514 O  O   . LEU A 312 ? 0.3316 0.2265 0.2034 -0.0306 -0.0609 -0.0146 311  LEU A O   
2515 C  CB  . LEU A 312 ? 0.3048 0.1999 0.1550 -0.0797 -0.0527 0.0335  311  LEU A CB  
2516 C  CG  . LEU A 312 ? 0.2395 0.1945 0.1707 -0.0962 -0.0266 0.0526  311  LEU A CG  
2517 C  CD1 . LEU A 312 ? 0.2774 0.1819 0.1664 -0.0612 0.0016  0.0561  311  LEU A CD1 
2518 C  CD2 . LEU A 312 ? 0.2854 0.2204 0.1961 -0.0975 -0.0622 0.0640  311  LEU A CD2 
2519 N  N   . LYS A 313 ? 0.3393 0.2301 0.2028 -0.0413 -0.0648 -0.0082 312  LYS A N   
2520 C  CA  . LYS A 313 ? 0.2827 0.2406 0.2247 -0.0061 -0.0496 0.0428  312  LYS A CA  
2521 C  C   . LYS A 313 ? 0.2422 0.2496 0.2003 -0.0231 -0.0392 0.0435  312  LYS A C   
2522 O  O   . LYS A 313 ? 0.2916 0.2409 0.1676 -0.0467 -0.0324 0.0641  312  LYS A O   
2523 C  CB  . LYS A 313 ? 0.2982 0.2500 0.2730 -0.0086 -0.0574 0.0603  312  LYS A CB  
2524 C  CG  . LYS A 313 ? 0.4619 0.3154 0.3266 -0.0028 -0.0743 0.0636  312  LYS A CG  
2525 C  CD  . LYS A 313 ? 0.5455 0.4047 0.4125 -0.0131 -0.0941 0.0363  312  LYS A CD  
2526 C  CE  . LYS A 313 ? 0.5947 0.4748 0.4716 -0.0664 -0.0941 0.0170  312  LYS A CE  
2527 N  NZ  . LYS A 313 ? 0.6703 0.5136 0.5130 -0.0640 -0.0512 0.0234  312  LYS A NZ  
2528 N  N   . TYR A 314 ? 0.2913 0.2778 0.2120 -0.0537 -0.0582 0.0701  313  TYR A N   
2529 C  CA  . TYR A 314 ? 0.1968 0.2956 0.1885 -0.0826 -0.0085 0.0334  313  TYR A CA  
2530 C  C   . TYR A 314 ? 0.2507 0.2718 0.1669 -0.0835 -0.0061 0.0388  313  TYR A C   
2531 O  O   . TYR A 314 ? 0.2708 0.2776 0.1613 -0.0739 -0.0079 0.0331  313  TYR A O   
2532 C  CB  . TYR A 314 ? 0.2524 0.3268 0.2170 -0.0923 0.0531  0.0309  313  TYR A CB  
2533 C  CG  . TYR A 314 ? 0.2005 0.3524 0.2181 -0.0764 0.0383  0.0505  313  TYR A CG  
2534 C  CD1 . TYR A 314 ? 0.2581 0.3681 0.2369 -0.0592 0.0397  0.0251  313  TYR A CD1 
2535 C  CD2 . TYR A 314 ? 0.1676 0.3618 0.2430 -0.1133 0.0216  0.0437  313  TYR A CD2 
2536 C  CE1 . TYR A 314 ? 0.2794 0.3880 0.2360 -0.0709 0.0351  0.0407  313  TYR A CE1 
2537 C  CE2 . TYR A 314 ? 0.1617 0.3627 0.2258 -0.1105 0.0077  0.0534  313  TYR A CE2 
2538 C  CZ  . TYR A 314 ? 0.2270 0.3808 0.2513 -0.1073 0.0433  0.0498  313  TYR A CZ  
2539 O  OH  . TYR A 314 ? 0.2429 0.3794 0.2505 -0.0599 0.0455  0.0502  313  TYR A OH  
2540 N  N   . VAL A 315 ? 0.2670 0.2353 0.1580 -0.1310 -0.0049 0.0509  314  VAL A N   
2541 C  CA  . VAL A 315 ? 0.2074 0.2179 0.1575 -0.1071 -0.0455 0.0686  314  VAL A CA  
2542 C  C   . VAL A 315 ? 0.2506 0.2470 0.1441 -0.0976 -0.0360 0.0626  314  VAL A C   
2543 O  O   . VAL A 315 ? 0.2072 0.2585 0.1544 -0.0293 -0.0163 0.0687  314  VAL A O   
2544 C  CB  . VAL A 315 ? 0.2896 0.1794 0.1875 -0.0797 -0.0766 0.0409  314  VAL A CB  
2545 C  CG1 . VAL A 315 ? 0.2488 0.1910 0.1891 -0.0105 -0.0286 0.0260  314  VAL A CG1 
2546 C  CG2 . VAL A 315 ? 0.3580 0.1819 0.2049 -0.0986 -0.1030 0.0100  314  VAL A CG2 
2547 N  N   . GLY A 316 ? 0.2139 0.2447 0.1127 -0.0651 -0.0643 0.0432  315  GLY A N   
2548 C  CA  . GLY A 316 ? 0.2086 0.2338 0.1308 -0.0967 -0.0289 0.0210  315  GLY A CA  
2549 C  C   . GLY A 316 ? 0.1793 0.2209 0.1295 -0.0824 0.0194  0.0261  315  GLY A C   
2550 O  O   . GLY A 316 ? 0.1419 0.2240 0.1635 -0.0609 -0.0431 0.0426  315  GLY A O   
2551 N  N   . MET A 317 ? 0.1992 0.2262 0.1424 -0.0420 0.0040  0.0542  316  MET A N   
2552 C  CA  . MET A 317 ? 0.2375 0.2381 0.1614 -0.0665 -0.0218 0.0640  316  MET A CA  
2553 C  C   . MET A 317 ? 0.1800 0.2538 0.1601 -0.0373 -0.0079 0.0462  316  MET A C   
2554 O  O   . MET A 317 ? 0.1319 0.2668 0.1696 -0.0604 0.0190  0.0391  316  MET A O   
2555 C  CB  . MET A 317 ? 0.3028 0.2544 0.1959 -0.0826 -0.0119 0.0893  316  MET A CB  
2556 C  CG  . MET A 317 ? 0.3437 0.2901 0.2840 -0.1057 0.0035  0.1402  316  MET A CG  
2557 S  SD  . MET A 317 ? 0.4316 0.3401 0.3950 -0.0499 -0.0013 0.1851  316  MET A SD  
2558 C  CE  . MET A 317 ? 0.4870 0.3758 0.4083 -0.0666 0.0556  0.1505  316  MET A CE  
2559 N  N   . VAL A 318 ? 0.1168 0.2462 0.1353 -0.0311 -0.0006 0.0711  317  VAL A N   
2560 C  CA  . VAL A 318 ? 0.1466 0.2575 0.1605 -0.0357 -0.0471 0.0576  317  VAL A CA  
2561 C  C   . VAL A 318 ? 0.1885 0.2583 0.1647 -0.0301 -0.0477 0.0332  317  VAL A C   
2562 O  O   . VAL A 318 ? 0.1811 0.2609 0.1569 -0.0594 -0.0530 0.0512  317  VAL A O   
2563 C  CB  . VAL A 318 ? 0.1447 0.2451 0.1556 -0.0821 -0.0629 0.0670  317  VAL A CB  
2564 C  CG1 . VAL A 318 ? 0.2053 0.2375 0.1493 -0.0896 -0.0574 0.0783  317  VAL A CG1 
2565 C  CG2 . VAL A 318 ? 0.1604 0.2915 0.1673 -0.0955 -0.0563 0.0882  317  VAL A CG2 
2566 N  N   . LEU A 319 ? 0.1020 0.2572 0.1700 0.0081  0.0032  0.0083  318  LEU A N   
2567 C  CA  . LEU A 319 ? 0.0917 0.2322 0.1448 -0.0368 0.0379  0.0209  318  LEU A CA  
2568 C  C   . LEU A 319 ? 0.1588 0.2662 0.1490 -0.0404 0.0477  0.0369  318  LEU A C   
2569 O  O   . LEU A 319 ? 0.1516 0.2674 0.1514 -0.0223 -0.0012 0.0480  318  LEU A O   
2570 C  CB  . LEU A 319 ? 0.1639 0.2399 0.1457 -0.0392 0.0447  0.0249  318  LEU A CB  
2571 C  CG  . LEU A 319 ? 0.1601 0.2306 0.1203 0.0126  0.0655  0.0320  318  LEU A CG  
2572 C  CD1 . LEU A 319 ? 0.2375 0.2310 0.1318 0.0193  0.0849  0.0326  318  LEU A CD1 
2573 C  CD2 . LEU A 319 ? 0.2232 0.2258 0.1290 0.0319  0.0322  0.0664  318  LEU A CD2 
2574 N  N   . ASN A 320 ? 0.1254 0.2919 0.1365 -0.0300 0.0034  0.0413  319  ASN A N   
2575 C  CA  . ASN A 320 ? 0.1034 0.2772 0.1415 0.0043  0.0171  0.0811  319  ASN A CA  
2576 C  C   . ASN A 320 ? 0.0918 0.2444 0.1462 -0.0481 -0.0347 0.0582  319  ASN A C   
2577 O  O   . ASN A 320 ? 0.1757 0.2496 0.1389 -0.0430 -0.0340 0.0097  319  ASN A O   
2578 C  CB  . ASN A 320 ? 0.1106 0.2668 0.1722 0.0578  -0.0077 0.0719  319  ASN A CB  
2579 C  CG  . ASN A 320 ? 0.1534 0.2686 0.2313 0.0836  -0.0017 0.0930  319  ASN A CG  
2580 O  OD1 . ASN A 320 ? 0.2135 0.2945 0.2520 0.0600  0.0468  0.0916  319  ASN A OD1 
2581 N  ND2 . ASN A 320 ? 0.2791 0.2967 0.2823 0.0591  -0.0696 0.0732  319  ASN A ND2 
2582 N  N   . GLU A 321 ? 0.1026 0.2647 0.1407 0.0015  -0.0286 0.0788  320  GLU A N   
2583 C  CA  . GLU A 321 ? 0.0913 0.2689 0.1667 0.0097  -0.0020 0.0667  320  GLU A CA  
2584 C  C   . GLU A 321 ? 0.1499 0.2749 0.1334 -0.0053 -0.0153 0.0620  320  GLU A C   
2585 O  O   . GLU A 321 ? 0.1920 0.2837 0.1478 -0.0389 -0.0168 0.0514  320  GLU A O   
2586 C  CB  . GLU A 321 ? 0.1234 0.2992 0.1857 0.0588  0.0200  0.0279  320  GLU A CB  
2587 C  CG  . GLU A 321 ? 0.1384 0.3050 0.2144 0.0032  0.0106  0.0384  320  GLU A CG  
2588 C  CD  . GLU A 321 ? 0.0879 0.3128 0.2243 -0.0001 -0.0124 0.0511  320  GLU A CD  
2589 O  OE1 . GLU A 321 ? 0.1418 0.2790 0.2087 -0.0047 -0.0232 0.0588  320  GLU A OE1 
2590 O  OE2 . GLU A 321 ? 0.1220 0.3169 0.2246 0.0028  0.0182  0.0419  320  GLU A OE2 
2591 N  N   . ALA A 322 ? 0.1628 0.2496 0.1050 -0.0107 -0.0049 0.0778  321  ALA A N   
2592 C  CA  . ALA A 322 ? 0.1699 0.2586 0.0876 0.0099  -0.0220 0.0337  321  ALA A CA  
2593 C  C   . ALA A 322 ? 0.1428 0.2384 0.1278 -0.0138 -0.0468 0.0319  321  ALA A C   
2594 O  O   . ALA A 322 ? 0.1573 0.2562 0.1675 0.0033  -0.0409 0.0058  321  ALA A O   
2595 C  CB  . ALA A 322 ? 0.1738 0.2651 0.0995 0.0398  -0.0211 0.0531  321  ALA A CB  
2596 N  N   . LEU A 323 ? 0.0763 0.2420 0.1307 0.0117  -0.0314 0.0090  322  LEU A N   
2597 C  CA  . LEU A 323 ? 0.0716 0.2414 0.1300 0.0181  0.0250  0.0178  322  LEU A CA  
2598 C  C   . LEU A 323 ? 0.1766 0.2528 0.1511 0.0468  0.0294  0.0473  322  LEU A C   
2599 O  O   . LEU A 323 ? 0.2102 0.2484 0.1562 0.0611  0.0249  0.0346  322  LEU A O   
2600 C  CB  . LEU A 323 ? 0.0940 0.2171 0.1412 -0.0074 0.0545  -0.0156 322  LEU A CB  
2601 C  CG  . LEU A 323 ? 0.1084 0.1797 0.1532 -0.0438 0.0574  0.0146  322  LEU A CG  
2602 C  CD1 . LEU A 323 ? 0.1710 0.2262 0.1806 0.0042  -0.0123 -0.0291 322  LEU A CD1 
2603 C  CD2 . LEU A 323 ? 0.1597 0.1750 0.1801 -0.0740 0.0567  0.0260  322  LEU A CD2 
2604 N  N   . ARG A 324 ? 0.1124 0.2504 0.1446 0.0563  0.0471  0.0746  323  ARG A N   
2605 C  CA  . ARG A 324 ? 0.1313 0.2323 0.1265 0.0381  0.0546  0.0631  323  ARG A CA  
2606 C  C   . ARG A 324 ? 0.1248 0.2925 0.1278 0.0590  0.0098  0.0566  323  ARG A C   
2607 O  O   . ARG A 324 ? 0.1247 0.3098 0.1439 0.0430  0.0201  0.0414  323  ARG A O   
2608 C  CB  . ARG A 324 ? 0.1808 0.2191 0.1252 0.0021  0.0646  0.0606  323  ARG A CB  
2609 C  CG  . ARG A 324 ? 0.1837 0.2473 0.1330 0.0047  0.0642  0.0671  323  ARG A CG  
2610 C  CD  . ARG A 324 ? 0.1296 0.3101 0.1471 0.0051  0.0381  0.0820  323  ARG A CD  
2611 N  NE  . ARG A 324 ? 0.1033 0.2963 0.1740 -0.0297 0.0198  0.0778  323  ARG A NE  
2612 C  CZ  . ARG A 324 ? 0.1107 0.3592 0.1667 0.0186  0.0027  0.0657  323  ARG A CZ  
2613 N  NH1 . ARG A 324 ? 0.1438 0.3782 0.1650 0.0590  0.0501  0.0565  323  ARG A NH1 
2614 N  NH2 . ARG A 324 ? 0.1241 0.3839 0.1533 0.0374  -0.0102 0.0679  323  ARG A NH2 
2615 N  N   . LEU A 325 ? 0.1189 0.3021 0.1474 0.0580  -0.0168 0.0531  324  LEU A N   
2616 C  CA  . LEU A 325 ? 0.1099 0.3061 0.1599 0.0499  -0.0268 0.0373  324  LEU A CA  
2617 C  C   . LEU A 325 ? 0.1806 0.2798 0.1434 0.0651  0.0630  0.0208  324  LEU A C   
2618 O  O   . LEU A 325 ? 0.2161 0.2621 0.1632 0.0423  0.0295  0.0250  324  LEU A O   
2619 C  CB  . LEU A 325 ? 0.1216 0.3303 0.2116 0.0355  0.0228  0.0284  324  LEU A CB  
2620 C  CG  . LEU A 325 ? 0.1426 0.3373 0.2072 0.0635  0.0664  0.0052  324  LEU A CG  
2621 C  CD1 . LEU A 325 ? 0.1751 0.3605 0.2103 -0.0156 -0.0230 0.0146  324  LEU A CD1 
2622 C  CD2 . LEU A 325 ? 0.2338 0.3328 0.2043 0.1242  0.0679  0.0282  324  LEU A CD2 
2623 N  N   . TRP A 326 ? 0.1277 0.2584 0.1420 0.0682  0.0529  0.0491  325  TRP A N   
2624 C  CA  . TRP A 326 ? 0.1429 0.2467 0.1267 0.0614  0.0562  0.0620  325  TRP A CA  
2625 C  C   . TRP A 326 ? 0.1068 0.2437 0.1057 0.0548  0.0303  0.0193  325  TRP A C   
2626 O  O   . TRP A 326 ? 0.1809 0.2515 0.1269 0.0671  0.0676  0.0131  325  TRP A O   
2627 C  CB  . TRP A 326 ? 0.1694 0.2469 0.1472 0.0652  0.0071  0.0798  325  TRP A CB  
2628 C  CG  . TRP A 326 ? 0.1342 0.2304 0.1499 0.0717  -0.0231 0.0507  325  TRP A CG  
2629 C  CD1 . TRP A 326 ? 0.1244 0.2311 0.1684 0.0809  -0.0086 0.0453  325  TRP A CD1 
2630 C  CD2 . TRP A 326 ? 0.1646 0.2297 0.1721 0.0748  -0.0164 0.0327  325  TRP A CD2 
2631 N  NE1 . TRP A 326 ? 0.2187 0.2525 0.1736 0.1210  -0.0107 0.0169  325  TRP A NE1 
2632 C  CE2 . TRP A 326 ? 0.1955 0.2430 0.1973 0.0659  -0.0269 0.0172  325  TRP A CE2 
2633 C  CE3 . TRP A 326 ? 0.2065 0.2287 0.1723 0.1230  -0.0164 0.0230  325  TRP A CE3 
2634 C  CZ2 . TRP A 326 ? 0.2237 0.2679 0.2167 0.0341  -0.0199 0.0271  325  TRP A CZ2 
2635 C  CZ3 . TRP A 326 ? 0.2731 0.2492 0.2059 0.1461  -0.0237 0.0274  325  TRP A CZ3 
2636 C  CH2 . TRP A 326 ? 0.2436 0.2687 0.1997 0.0949  -0.0369 0.0354  325  TRP A CH2 
2637 N  N   . PRO A 327 ? 0.1338 0.2344 0.1038 0.0517  0.0469  0.0053  326  PRO A N   
2638 C  CA  . PRO A 327 ? 0.1420 0.2023 0.1052 0.0267  0.0322  0.0350  326  PRO A CA  
2639 C  C   . PRO A 327 ? 0.1905 0.2069 0.0891 0.0622  0.0352  0.0485  326  PRO A C   
2640 O  O   . PRO A 327 ? 0.1891 0.2057 0.1218 0.0358  0.0335  0.0179  326  PRO A O   
2641 C  CB  . PRO A 327 ? 0.2189 0.2062 0.0928 0.0455  0.0227  0.0272  326  PRO A CB  
2642 C  CG  . PRO A 327 ? 0.1823 0.2560 0.0828 0.0623  -0.0041 0.0188  326  PRO A CG  
2643 C  CD  . PRO A 327 ? 0.1478 0.2575 0.0975 0.0267  -0.0005 0.0215  326  PRO A CD  
2644 N  N   . THR A 328 ? 0.1866 0.1997 0.0779 0.0058  0.0420  0.0377  327  THR A N   
2645 C  CA  . THR A 328 ? 0.1623 0.2004 0.0831 -0.0026 0.0560  0.0203  327  THR A CA  
2646 C  C   . THR A 328 ? 0.2397 0.2595 0.0907 0.0062  -0.0070 0.0302  327  THR A C   
2647 O  O   . THR A 328 ? 0.1987 0.2683 0.0977 0.0135  -0.0378 0.0096  327  THR A O   
2648 C  CB  . THR A 328 ? 0.1160 0.2516 0.1365 0.0436  0.0036  -0.0138 327  THR A CB  
2649 O  OG1 . THR A 328 ? 0.1421 0.2676 0.1663 0.0434  0.0241  -0.0213 327  THR A OG1 
2650 C  CG2 . THR A 328 ? 0.1245 0.3001 0.1439 0.0411  -0.0340 0.0078  327  THR A CG2 
2651 N  N   . ALA A 329 ? 0.1627 0.2707 0.1151 0.0334  0.0310  -0.0053 328  ALA A N   
2652 C  CA  . ALA A 329 ? 0.1219 0.2217 0.1463 0.0554  0.0452  -0.0319 328  ALA A CA  
2653 C  C   . ALA A 329 ? 0.1774 0.2315 0.1041 0.0655  0.0372  0.0241  328  ALA A C   
2654 O  O   . ALA A 329 ? 0.3137 0.2619 0.1026 0.1020  0.0257  0.0187  328  ALA A O   
2655 C  CB  . ALA A 329 ? 0.1435 0.2594 0.1832 0.0741  0.0467  -0.0262 328  ALA A CB  
2656 N  N   . PRO A 330 ? 0.1772 0.1888 0.1075 0.0635  0.0186  0.0512  329  PRO A N   
2657 C  CA  . PRO A 330 ? 0.1791 0.1787 0.1036 0.0495  -0.0134 0.0005  329  PRO A CA  
2658 C  C   . PRO A 330 ? 0.1869 0.1618 0.1075 0.0516  0.0432  0.0012  329  PRO A C   
2659 O  O   . PRO A 330 ? 0.2219 0.1491 0.1302 0.0181  0.0352  0.0162  329  PRO A O   
2660 C  CB  . PRO A 330 ? 0.2093 0.1925 0.1235 0.0608  -0.0290 0.0184  329  PRO A CB  
2661 C  CG  . PRO A 330 ? 0.2063 0.1608 0.1388 0.0399  0.0117  0.0293  329  PRO A CG  
2662 C  CD  . PRO A 330 ? 0.1533 0.1710 0.1279 0.0258  0.0054  0.0348  329  PRO A CD  
2663 N  N   . ALA A 331 ? 0.1885 0.1717 0.1135 0.0485  0.0049  0.0041  330  ALA A N   
2664 C  CA  . ALA A 331 ? 0.1841 0.1321 0.1145 0.0888  0.0175  -0.0012 330  ALA A CA  
2665 C  C   . ALA A 331 ? 0.1650 0.1531 0.1170 0.0334  -0.0134 0.0109  330  ALA A C   
2666 O  O   . ALA A 331 ? 0.2403 0.1571 0.1214 0.0039  0.0207  0.0053  330  ALA A O   
2667 C  CB  . ALA A 331 ? 0.2000 0.1220 0.1415 0.0753  0.0031  0.0159  330  ALA A CB  
2668 N  N   . PHE A 332 ? 0.1427 0.1715 0.1295 0.0304  0.0223  -0.0046 331  PHE A N   
2669 C  CA  . PHE A 332 ? 0.2000 0.1477 0.1604 0.0252  -0.0218 0.0081  331  PHE A CA  
2670 C  C   . PHE A 332 ? 0.2105 0.1755 0.1636 -0.0054 -0.0167 0.0075  331  PHE A C   
2671 O  O   . PHE A 332 ? 0.2226 0.2162 0.1668 -0.0231 -0.0195 0.0097  331  PHE A O   
2672 C  CB  . PHE A 332 ? 0.2509 0.1390 0.1653 0.0018  0.0198  0.0165  331  PHE A CB  
2673 C  CG  . PHE A 332 ? 0.1987 0.1582 0.1597 0.0244  -0.0268 0.0055  331  PHE A CG  
2674 C  CD1 . PHE A 332 ? 0.1362 0.1613 0.1643 0.0308  0.0227  0.0074  331  PHE A CD1 
2675 C  CD2 . PHE A 332 ? 0.2089 0.1904 0.1202 0.0064  0.0245  0.0205  331  PHE A CD2 
2676 C  CE1 . PHE A 332 ? 0.1709 0.1944 0.1399 0.0339  0.0168  -0.0013 331  PHE A CE1 
2677 C  CE2 . PHE A 332 ? 0.1620 0.2335 0.1453 0.0612  0.0114  0.0105  331  PHE A CE2 
2678 C  CZ  . PHE A 332 ? 0.1840 0.2116 0.1537 0.0288  0.0189  0.0191  331  PHE A CZ  
2679 N  N   . SER A 333 ? 0.1880 0.1773 0.1740 -0.0084 -0.0254 0.0168  332  SER A N   
2680 C  CA  . SER A 333 ? 0.1907 0.1505 0.1293 0.0028  -0.0149 0.0145  332  SER A CA  
2681 C  C   . SER A 333 ? 0.2089 0.1645 0.1333 0.0229  -0.0035 0.0127  332  SER A C   
2682 O  O   . SER A 333 ? 0.2227 0.1195 0.1251 0.0147  -0.0104 0.0177  332  SER A O   
2683 C  CB  . SER A 333 ? 0.2108 0.1501 0.1254 -0.0459 0.0050  -0.0307 332  SER A CB  
2684 O  OG  . SER A 333 ? 0.2179 0.1575 0.1491 0.0112  -0.0304 -0.0138 332  SER A OG  
2685 N  N   . LEU A 334 ? 0.1757 0.1680 0.1270 0.0107  -0.0277 0.0263  333  LEU A N   
2686 C  CA  . LEU A 334 ? 0.2063 0.1392 0.1542 -0.0193 -0.0108 0.0108  333  LEU A CA  
2687 C  C   . LEU A 334 ? 0.2331 0.1782 0.1423 -0.0445 -0.0239 0.0047  333  LEU A C   
2688 O  O   . LEU A 334 ? 0.2609 0.1735 0.1564 -0.0212 -0.0468 0.0137  333  LEU A O   
2689 C  CB  . LEU A 334 ? 0.1859 0.1122 0.1780 -0.0348 0.0010  0.0062  333  LEU A CB  
2690 C  CG  . LEU A 334 ? 0.1826 0.1248 0.1861 -0.0154 0.0035  -0.0051 333  LEU A CG  
2691 C  CD1 . LEU A 334 ? 0.3016 0.1590 0.1796 -0.0046 0.0219  0.0018  333  LEU A CD1 
2692 C  CD2 . LEU A 334 ? 0.1997 0.1363 0.1834 0.0184  -0.0346 -0.0228 333  LEU A CD2 
2693 N  N   . TYR A 335 ? 0.1935 0.1853 0.1140 -0.0172 -0.0026 0.0052  334  TYR A N   
2694 C  CA  . TYR A 335 ? 0.2254 0.2104 0.1379 -0.0405 -0.0513 -0.0012 334  TYR A CA  
2695 C  C   . TYR A 335 ? 0.2826 0.2231 0.1173 -0.0148 -0.0113 -0.0166 334  TYR A C   
2696 O  O   . TYR A 335 ? 0.2218 0.1917 0.1214 -0.0182 -0.0163 -0.0206 334  TYR A O   
2697 C  CB  . TYR A 335 ? 0.2100 0.2058 0.1708 -0.0135 -0.0364 -0.0017 334  TYR A CB  
2698 C  CG  . TYR A 335 ? 0.1868 0.1864 0.1840 -0.0113 -0.0030 -0.0084 334  TYR A CG  
2699 C  CD1 . TYR A 335 ? 0.1809 0.1671 0.1704 -0.0007 -0.0211 -0.0194 334  TYR A CD1 
2700 C  CD2 . TYR A 335 ? 0.2165 0.2026 0.1878 0.0023  0.0076  -0.0328 334  TYR A CD2 
2701 C  CE1 . TYR A 335 ? 0.1282 0.1763 0.1824 -0.0404 -0.0459 -0.0189 334  TYR A CE1 
2702 C  CE2 . TYR A 335 ? 0.2235 0.2002 0.2014 0.0246  -0.0142 -0.0466 334  TYR A CE2 
2703 C  CZ  . TYR A 335 ? 0.1658 0.1995 0.2017 -0.0298 -0.0092 -0.0373 334  TYR A CZ  
2704 O  OH  . TYR A 335 ? 0.1969 0.2513 0.2135 -0.0521 -0.0499 -0.0580 334  TYR A OH  
2705 N  N   . ALA A 336 ? 0.2291 0.2485 0.0966 -0.0364 -0.0215 -0.0101 335  ALA A N   
2706 C  CA  . ALA A 336 ? 0.2297 0.2364 0.0958 0.0004  -0.0152 -0.0117 335  ALA A CA  
2707 C  C   . ALA A 336 ? 0.2887 0.2564 0.1382 -0.0375 -0.0125 -0.0227 335  ALA A C   
2708 O  O   . ALA A 336 ? 0.2547 0.2832 0.1427 -0.0648 -0.0020 -0.0313 335  ALA A O   
2709 C  CB  . ALA A 336 ? 0.3480 0.2222 0.1047 0.0234  0.0008  -0.0088 335  ALA A CB  
2710 N  N   . LYS A 337 ? 0.2376 0.2430 0.1684 0.0022  -0.0366 -0.0192 336  LYS A N   
2711 C  CA  . LYS A 337 ? 0.2554 0.2378 0.1888 0.0258  -0.0510 -0.0497 336  LYS A CA  
2712 C  C   . LYS A 337 ? 0.2973 0.3053 0.2448 0.0225  -0.0768 -0.0708 336  LYS A C   
2713 O  O   . LYS A 337 ? 0.3000 0.3363 0.2811 0.0500  -0.0555 -0.0984 336  LYS A O   
2714 C  CB  . LYS A 337 ? 0.3058 0.2066 0.1935 0.0650  -0.0486 -0.0565 336  LYS A CB  
2715 C  CG  . LYS A 337 ? 0.3012 0.1802 0.2117 0.0361  -0.0515 -0.0747 336  LYS A CG  
2716 C  CD  . LYS A 337 ? 0.1986 0.1981 0.2533 0.0316  -0.0565 -0.0297 336  LYS A CD  
2717 C  CE  . LYS A 337 ? 0.1769 0.2624 0.2856 -0.0156 -0.0031 -0.0253 336  LYS A CE  
2718 N  NZ  . LYS A 337 ? 0.1471 0.3038 0.2838 -0.0227 0.0164  -0.0218 336  LYS A NZ  
2719 N  N   . GLU A 338 ? 0.2110 0.2960 0.2058 0.0509  -0.0569 -0.0326 337  GLU A N   
2720 C  CA  . GLU A 338 ? 0.2548 0.3307 0.2088 0.1065  -0.0892 -0.0617 337  GLU A CA  
2721 C  C   . GLU A 338 ? 0.3055 0.3326 0.1920 0.0848  -0.0818 -0.0578 337  GLU A C   
2722 O  O   . GLU A 338 ? 0.3312 0.3078 0.1920 0.0971  -0.0920 -0.0491 337  GLU A O   
2723 C  CB  . GLU A 338 ? 0.2976 0.4070 0.2602 0.1605  -0.0912 -0.0895 337  GLU A CB  
2724 C  CG  . GLU A 338 ? 0.4860 0.4759 0.3265 0.1285  -0.0922 -0.0963 337  GLU A CG  
2725 C  CD  . GLU A 338 ? 0.5492 0.5349 0.3803 0.1123  -0.1240 -0.1169 337  GLU A CD  
2726 O  OE1 . GLU A 338 ? 0.6311 0.5434 0.3884 0.1376  -0.1120 -0.1252 337  GLU A OE1 
2727 O  OE2 . GLU A 338 ? 0.4513 0.5693 0.4247 0.0674  -0.1694 -0.1278 337  GLU A OE2 
2728 N  N   . ASP A 339 ? 0.3850 0.3624 0.1761 0.0650  -0.0724 -0.0581 338  ASP A N   
2729 C  CA  . ASP A 339 ? 0.3674 0.3605 0.1851 0.0337  -0.0511 -0.0749 338  ASP A CA  
2730 C  C   . ASP A 339 ? 0.3996 0.3423 0.2145 0.0412  -0.0398 -0.0487 338  ASP A C   
2731 O  O   . ASP A 339 ? 0.4266 0.3494 0.2316 0.0576  -0.0462 -0.0518 338  ASP A O   
2732 C  CB  . ASP A 339 ? 0.4185 0.3938 0.1841 -0.0149 -0.0937 -0.0991 338  ASP A CB  
2733 C  CG  . ASP A 339 ? 0.4120 0.4129 0.1954 -0.0317 -0.0907 -0.1136 338  ASP A CG  
2734 O  OD1 . ASP A 339 ? 0.4160 0.4227 0.2117 -0.0110 -0.0363 -0.1101 338  ASP A OD1 
2735 O  OD2 . ASP A 339 ? 0.4334 0.4516 0.2125 -0.0394 -0.1032 -0.1008 338  ASP A OD2 
2736 N  N   . THR A 340 ? 0.3482 0.3058 0.2171 0.0382  -0.0703 -0.0129 339  THR A N   
2737 C  CA  . THR A 340 ? 0.3444 0.3384 0.2291 0.0798  -0.0235 -0.0324 339  THR A CA  
2738 C  C   . THR A 340 ? 0.3781 0.3460 0.2601 0.0767  0.0142  -0.0139 339  THR A C   
2739 O  O   . THR A 340 ? 0.4869 0.3464 0.3230 0.0945  0.0539  0.0000  339  THR A O   
2740 C  CB  . THR A 340 ? 0.3895 0.3260 0.2060 0.0323  -0.0137 -0.0367 339  THR A CB  
2741 O  OG1 . THR A 340 ? 0.3936 0.3252 0.2063 0.0082  0.0244  -0.0108 339  THR A OG1 
2742 C  CG2 . THR A 340 ? 0.3704 0.3291 0.1801 0.0081  0.0079  -0.0581 339  THR A CG2 
2743 N  N   . VAL A 341 ? 0.2952 0.3441 0.2155 0.0531  0.0293  -0.0276 340  VAL A N   
2744 C  CA  . VAL A 341 ? 0.2847 0.3398 0.1929 0.0524  0.0204  -0.0428 340  VAL A CA  
2745 C  C   . VAL A 341 ? 0.3707 0.3376 0.2197 0.0693  -0.0104 -0.0067 340  VAL A C   
2746 O  O   . VAL A 341 ? 0.3916 0.3428 0.2238 0.0926  -0.0537 -0.0368 340  VAL A O   
2747 C  CB  . VAL A 341 ? 0.2918 0.3610 0.1798 -0.0029 0.0446  -0.0395 340  VAL A CB  
2748 C  CG1 . VAL A 341 ? 0.3679 0.3634 0.1838 -0.0070 0.0536  -0.0129 340  VAL A CG1 
2749 C  CG2 . VAL A 341 ? 0.3097 0.3828 0.1723 -0.0322 0.0546  -0.0884 340  VAL A CG2 
2750 N  N   . LEU A 342 ? 0.3121 0.3191 0.2312 0.0946  0.0131  0.0226  341  LEU A N   
2751 C  CA  . LEU A 342 ? 0.4025 0.3323 0.2356 0.1109  -0.0109 0.0699  341  LEU A CA  
2752 C  C   . LEU A 342 ? 0.4223 0.3436 0.2434 0.0961  -0.0033 0.0611  341  LEU A C   
2753 O  O   . LEU A 342 ? 0.4638 0.3554 0.2575 0.0907  -0.0222 0.0663  341  LEU A O   
2754 C  CB  . LEU A 342 ? 0.4455 0.3266 0.2662 0.1142  -0.0546 0.0620  341  LEU A CB  
2755 C  CG  . LEU A 342 ? 0.3992 0.3356 0.2892 0.1287  -0.0603 0.0695  341  LEU A CG  
2756 C  CD1 . LEU A 342 ? 0.4560 0.2961 0.2926 0.0514  -0.0568 0.0325  341  LEU A CD1 
2757 C  CD2 . LEU A 342 ? 0.3675 0.3321 0.2995 0.1767  -0.0430 0.0713  341  LEU A CD2 
2758 N  N   . GLY A 343 ? 0.4458 0.3320 0.2201 0.0641  0.0152  0.0732  342  GLY A N   
2759 C  CA  . GLY A 343 ? 0.4523 0.3669 0.2114 0.0848  0.0069  0.0292  342  GLY A CA  
2760 C  C   . GLY A 343 ? 0.4448 0.4033 0.2069 0.0726  -0.0071 0.0314  342  GLY A C   
2761 O  O   . GLY A 343 ? 0.5200 0.4156 0.2207 -0.0039 0.0211  0.0462  342  GLY A O   
2762 N  N   . GLY A 344 ? 0.3772 0.4016 0.1809 0.1179  -0.0895 0.0239  343  GLY A N   
2763 C  CA  . GLY A 344 ? 0.4045 0.4175 0.1832 0.1026  -0.0078 0.0110  343  GLY A CA  
2764 C  C   . GLY A 344 ? 0.4052 0.4589 0.1828 0.0774  0.0549  -0.0097 343  GLY A C   
2765 O  O   . GLY A 344 ? 0.4752 0.4733 0.1483 0.0527  0.0687  -0.0130 343  GLY A O   
2766 N  N   . GLU A 345 ? 0.4109 0.4500 0.2000 0.0906  0.0281  0.0134  344  GLU A N   
2767 C  CA  . GLU A 345 ? 0.3990 0.4565 0.2408 0.0594  0.0635  0.0083  344  GLU A CA  
2768 C  C   . GLU A 345 ? 0.4366 0.4220 0.1916 0.0101  0.0810  -0.0031 344  GLU A C   
2769 O  O   . GLU A 345 ? 0.4202 0.4533 0.1817 -0.0223 0.0835  0.0080  344  GLU A O   
2770 C  CB  . GLU A 345 ? 0.4199 0.4870 0.3100 0.0923  0.0682  0.0263  344  GLU A CB  
2771 C  CG  . GLU A 345 ? 0.4846 0.5202 0.3574 0.1015  0.1298  0.0499  344  GLU A CG  
2772 C  CD  . GLU A 345 ? 0.5749 0.5584 0.3876 0.1130  0.1679  0.0585  344  GLU A CD  
2773 O  OE1 . GLU A 345 ? 0.5578 0.5500 0.3850 0.1034  0.1537  0.0454  344  GLU A OE1 
2774 O  OE2 . GLU A 345 ? 0.6974 0.5914 0.4234 0.1318  0.1481  0.0513  344  GLU A OE2 
2775 N  N   . TYR A 346 ? 0.4290 0.3719 0.1686 0.0201  0.0606  -0.0254 345  TYR A N   
2776 C  CA  . TYR A 346 ? 0.4227 0.3214 0.1853 0.0231  0.0469  -0.0361 345  TYR A CA  
2777 C  C   . TYR A 346 ? 0.4276 0.3120 0.1905 0.0719  0.0319  -0.0325 345  TYR A C   
2778 O  O   . TYR A 346 ? 0.4290 0.3022 0.1709 0.0910  0.0719  0.0145  345  TYR A O   
2779 C  CB  . TYR A 346 ? 0.3723 0.2947 0.1810 0.0697  0.0253  -0.0032 345  TYR A CB  
2780 C  CG  . TYR A 346 ? 0.3497 0.3141 0.2032 0.0576  0.0515  0.0188  345  TYR A CG  
2781 C  CD1 . TYR A 346 ? 0.3925 0.3207 0.2078 0.0769  0.0357  0.0485  345  TYR A CD1 
2782 C  CD2 . TYR A 346 ? 0.3698 0.3190 0.1934 0.0357  0.0114  0.0218  345  TYR A CD2 
2783 C  CE1 . TYR A 346 ? 0.3877 0.3328 0.1963 0.0355  0.0373  0.0421  345  TYR A CE1 
2784 C  CE2 . TYR A 346 ? 0.4194 0.3267 0.1982 0.0375  -0.0024 0.0298  345  TYR A CE2 
2785 C  CZ  . TYR A 346 ? 0.3973 0.3587 0.2116 0.0506  0.0307  0.0298  345  TYR A CZ  
2786 O  OH  . TYR A 346 ? 0.4050 0.3848 0.2248 0.0539  0.0465  0.0342  345  TYR A OH  
2787 N  N   . PRO A 347 ? 0.3762 0.3285 0.1994 0.0498  0.0392  -0.0782 346  PRO A N   
2788 C  CA  . PRO A 347 ? 0.4114 0.3415 0.2146 0.0511  0.0232  -0.0718 346  PRO A CA  
2789 C  C   . PRO A 347 ? 0.4389 0.3094 0.1912 0.0840  0.0028  -0.0550 346  PRO A C   
2790 O  O   . PRO A 347 ? 0.4784 0.3004 0.1797 0.1307  0.0142  -0.0542 346  PRO A O   
2791 C  CB  . PRO A 347 ? 0.4317 0.3757 0.2547 0.0663  0.0113  -0.0924 346  PRO A CB  
2792 C  CG  . PRO A 347 ? 0.4451 0.3896 0.2539 0.0548  0.0239  -0.1279 346  PRO A CG  
2793 C  CD  . PRO A 347 ? 0.3617 0.3552 0.2277 0.0135  0.0356  -0.1016 346  PRO A CD  
2794 N  N   . LEU A 348 ? 0.4316 0.2840 0.1917 0.0631  -0.0363 -0.0651 347  LEU A N   
2795 C  CA  . LEU A 348 ? 0.3104 0.2583 0.1770 0.0762  -0.0202 -0.0591 347  LEU A CA  
2796 C  C   . LEU A 348 ? 0.3505 0.2811 0.2052 0.0286  -0.0092 -0.0496 347  LEU A C   
2797 O  O   . LEU A 348 ? 0.3715 0.3218 0.2227 0.0052  -0.0255 -0.0411 347  LEU A O   
2798 C  CB  . LEU A 348 ? 0.3308 0.2629 0.1694 0.0500  -0.0523 -0.0915 347  LEU A CB  
2799 C  CG  . LEU A 348 ? 0.3387 0.2723 0.1899 0.0353  -0.0290 -0.0822 347  LEU A CG  
2800 C  CD1 . LEU A 348 ? 0.3530 0.2749 0.1840 0.0578  -0.0149 -0.0772 347  LEU A CD1 
2801 C  CD2 . LEU A 348 ? 0.3557 0.2857 0.2136 0.0291  -0.0534 -0.0535 347  LEU A CD2 
2802 N  N   . GLU A 349 ? 0.3112 0.2604 0.2132 0.0228  0.0378  -0.0629 348  GLU A N   
2803 C  CA  . GLU A 349 ? 0.3411 0.2602 0.2290 -0.0120 -0.0173 -0.0771 348  GLU A CA  
2804 C  C   . GLU A 349 ? 0.3068 0.2219 0.2345 -0.0262 -0.0297 -0.0674 348  GLU A C   
2805 O  O   . GLU A 349 ? 0.3403 0.1884 0.2233 -0.0252 -0.0676 -0.0440 348  GLU A O   
2806 C  CB  . GLU A 349 ? 0.3617 0.2919 0.2423 -0.0229 0.0424  -0.0907 348  GLU A CB  
2807 C  CG  . GLU A 349 ? 0.4229 0.3128 0.2759 -0.0512 0.0724  -0.1340 348  GLU A CG  
2808 C  CD  . GLU A 349 ? 0.6869 0.3904 0.3503 -0.0187 0.1130  -0.1182 348  GLU A CD  
2809 O  OE1 . GLU A 349 ? 0.8353 0.4210 0.3988 -0.0868 0.0797  -0.0696 348  GLU A OE1 
2810 O  OE2 . GLU A 349 ? 0.7834 0.4327 0.3993 0.0255  0.0502  -0.1312 348  GLU A OE2 
2811 N  N   . LYS A 350 ? 0.3398 0.2452 0.2479 -0.0119 -0.0355 -0.0802 349  LYS A N   
2812 C  CA  . LYS A 350 ? 0.2577 0.2632 0.2719 0.0372  -0.0511 -0.0818 349  LYS A CA  
2813 C  C   . LYS A 350 ? 0.2656 0.2614 0.2565 0.0127  -0.0690 -0.0679 349  LYS A C   
2814 O  O   . LYS A 350 ? 0.3516 0.2557 0.2515 -0.0321 -0.0379 -0.0932 349  LYS A O   
2815 C  CB  . LYS A 350 ? 0.2769 0.2940 0.2921 0.0764  -0.0416 -0.0992 349  LYS A CB  
2816 C  CG  . LYS A 350 ? 0.3457 0.3434 0.3391 0.0770  -0.0511 -0.1003 349  LYS A CG  
2817 C  CD  . LYS A 350 ? 0.3158 0.3944 0.3617 0.1149  -0.0876 -0.1072 349  LYS A CD  
2818 C  CE  . LYS A 350 ? 0.3177 0.4616 0.4010 0.1109  -0.1051 -0.0847 349  LYS A CE  
2819 N  NZ  . LYS A 350 ? 0.4857 0.4911 0.4320 0.0802  -0.0927 -0.0863 349  LYS A NZ  
2820 N  N   . GLY A 351 ? 0.2266 0.2533 0.2410 0.0234  -0.0572 -0.0387 350  GLY A N   
2821 C  CA  . GLY A 351 ? 0.2543 0.2229 0.2358 0.0581  -0.0541 -0.0184 350  GLY A CA  
2822 C  C   . GLY A 351 ? 0.2934 0.1939 0.2125 0.0576  -0.0474 -0.0233 350  GLY A C   
2823 O  O   . GLY A 351 ? 0.3092 0.1515 0.2167 0.0547  -0.0725 0.0045  350  GLY A O   
2824 N  N   . ASP A 352 ? 0.3102 0.2078 0.1974 -0.0039 -0.0093 -0.0430 351  ASP A N   
2825 C  CA  . ASP A 352 ? 0.2565 0.2385 0.1684 0.0380  -0.0360 -0.0489 351  ASP A CA  
2826 C  C   . ASP A 352 ? 0.2798 0.2401 0.1784 0.0483  -0.0401 -0.0380 351  ASP A C   
2827 O  O   . ASP A 352 ? 0.2940 0.2502 0.1758 0.0055  0.0045  -0.0371 351  ASP A O   
2828 C  CB  . ASP A 352 ? 0.3263 0.2348 0.1548 -0.0057 -0.0224 -0.0868 351  ASP A CB  
2829 C  CG  . ASP A 352 ? 0.4126 0.2679 0.1962 0.0502  -0.0351 -0.0703 351  ASP A CG  
2830 O  OD1 . ASP A 352 ? 0.4198 0.2538 0.2113 0.0981  -0.0652 -0.0751 351  ASP A OD1 
2831 O  OD2 . ASP A 352 ? 0.4013 0.2833 0.1873 0.0630  -0.0275 -0.0651 351  ASP A OD2 
2832 N  N   . GLU A 353 ? 0.2816 0.2315 0.1752 0.0493  -0.0262 -0.0179 352  GLU A N   
2833 C  CA  . GLU A 353 ? 0.2818 0.2470 0.1654 -0.0289 0.0313  -0.0012 352  GLU A CA  
2834 C  C   . GLU A 353 ? 0.2785 0.2056 0.1589 0.0295  0.0121  -0.0240 352  GLU A C   
2835 O  O   . GLU A 353 ? 0.2999 0.1836 0.1669 0.0170  0.0378  -0.0400 352  GLU A O   
2836 C  CB  . GLU A 353 ? 0.3674 0.2931 0.1872 -0.0842 0.0342  0.0159  352  GLU A CB  
2837 C  CG  . GLU A 353 ? 0.5496 0.3468 0.2532 -0.0609 -0.0187 0.0385  352  GLU A CG  
2838 C  CD  . GLU A 353 ? 0.6043 0.3697 0.3067 -0.0792 -0.0336 0.0619  352  GLU A CD  
2839 O  OE1 . GLU A 353 ? 0.4895 0.3401 0.2797 -0.0453 -0.1236 0.0422  352  GLU A OE1 
2840 O  OE2 . GLU A 353 ? 0.6494 0.4043 0.3570 -0.1024 -0.0133 0.0870  352  GLU A OE2 
2841 N  N   . LEU A 354 ? 0.2191 0.1528 0.1589 0.0050  0.0023  -0.0235 353  LEU A N   
2842 C  CA  . LEU A 354 ? 0.2678 0.1558 0.1361 -0.0002 0.0064  -0.0135 353  LEU A CA  
2843 C  C   . LEU A 354 ? 0.2219 0.2096 0.1383 0.0115  0.0009  -0.0044 353  LEU A C   
2844 O  O   . LEU A 354 ? 0.1982 0.2314 0.1426 0.0220  0.0165  -0.0288 353  LEU A O   
2845 C  CB  . LEU A 354 ? 0.2525 0.1519 0.1313 0.0321  -0.0146 0.0133  353  LEU A CB  
2846 C  CG  . LEU A 354 ? 0.3319 0.1649 0.1735 0.1204  0.0412  0.0215  353  LEU A CG  
2847 C  CD1 . LEU A 354 ? 0.2784 0.1905 0.1782 0.0859  0.0596  0.0298  353  LEU A CD1 
2848 C  CD2 . LEU A 354 ? 0.3062 0.2213 0.1854 0.1292  0.0689  -0.0019 353  LEU A CD2 
2849 N  N   . MET A 355 ? 0.2205 0.1817 0.1322 0.0818  0.0018  0.0032  354  MET A N   
2850 C  CA  . MET A 355 ? 0.2629 0.1650 0.1181 0.0456  -0.0313 0.0345  354  MET A CA  
2851 C  C   . MET A 355 ? 0.2242 0.1836 0.1375 0.0360  -0.0131 -0.0099 354  MET A C   
2852 O  O   . MET A 355 ? 0.2812 0.1868 0.1677 0.0599  0.0528  -0.0010 354  MET A O   
2853 C  CB  . MET A 355 ? 0.2352 0.1465 0.1500 0.0861  -0.0069 0.0400  354  MET A CB  
2854 C  CG  . MET A 355 ? 0.2180 0.2061 0.1547 0.0485  0.0183  0.0313  354  MET A CG  
2855 S  SD  . MET A 355 ? 0.2576 0.2404 0.1856 0.0431  0.0149  0.0100  354  MET A SD  
2856 C  CE  . MET A 355 ? 0.2179 0.2940 0.2291 0.0153  0.0096  -0.0160 354  MET A CE  
2857 N  N   . VAL A 356 ? 0.2073 0.1997 0.1484 -0.0159 -0.0027 0.0025  355  VAL A N   
2858 C  CA  . VAL A 356 ? 0.2023 0.1664 0.1587 0.0432  0.0265  -0.0191 355  VAL A CA  
2859 C  C   . VAL A 356 ? 0.1684 0.1884 0.1569 0.0335  0.0209  -0.0176 355  VAL A C   
2860 O  O   . VAL A 356 ? 0.1954 0.1896 0.1299 0.0553  0.0233  -0.0071 355  VAL A O   
2861 C  CB  . VAL A 356 ? 0.2017 0.1598 0.1642 0.0550  0.0210  -0.0172 355  VAL A CB  
2862 C  CG1 . VAL A 356 ? 0.2262 0.1607 0.1352 0.0116  0.0298  -0.0267 355  VAL A CG1 
2863 C  CG2 . VAL A 356 ? 0.2079 0.1738 0.1581 0.0929  -0.0350 0.0167  355  VAL A CG2 
2864 N  N   . LEU A 357 ? 0.1351 0.1706 0.1694 0.0360  0.0153  -0.0137 356  LEU A N   
2865 C  CA  . LEU A 357 ? 0.1239 0.1712 0.1642 0.0550  -0.0094 0.0078  356  LEU A CA  
2866 C  C   . LEU A 357 ? 0.1654 0.1775 0.1587 0.0131  0.0029  0.0116  356  LEU A C   
2867 O  O   . LEU A 357 ? 0.1932 0.1896 0.1748 0.0053  0.0198  0.0093  356  LEU A O   
2868 C  CB  . LEU A 357 ? 0.2087 0.1968 0.1713 0.1050  0.0524  0.0315  356  LEU A CB  
2869 C  CG  . LEU A 357 ? 0.2125 0.2116 0.1731 0.1207  0.0576  0.0542  356  LEU A CG  
2870 C  CD1 . LEU A 357 ? 0.2604 0.2096 0.1443 0.0719  0.0188  0.0697  356  LEU A CD1 
2871 C  CD2 . LEU A 357 ? 0.2256 0.1863 0.1978 0.1138  0.0598  0.0546  356  LEU A CD2 
2872 N  N   . ILE A 358 ? 0.2025 0.1834 0.1349 0.0362  0.0032  0.0305  357  ILE A N   
2873 C  CA  . ILE A 358 ? 0.1675 0.1577 0.1366 0.0470  0.0400  0.0344  357  ILE A CA  
2874 C  C   . ILE A 358 ? 0.1655 0.1773 0.1376 0.0349  0.0442  0.0655  357  ILE A C   
2875 O  O   . ILE A 358 ? 0.1547 0.2092 0.1644 0.0543  0.0229  0.0478  357  ILE A O   
2876 C  CB  . ILE A 358 ? 0.1708 0.1227 0.1339 0.0759  0.0581  0.0306  357  ILE A CB  
2877 C  CG1 . ILE A 358 ? 0.1613 0.1412 0.1212 0.0697  0.0423  -0.0142 357  ILE A CG1 
2878 C  CG2 . ILE A 358 ? 0.2763 0.1186 0.1286 0.0494  0.0096  0.0450  357  ILE A CG2 
2879 C  CD1 . ILE A 358 ? 0.2323 0.1454 0.0964 0.1039  0.0228  0.0148  357  ILE A CD1 
2880 N  N   . PRO A 359 ? 0.1836 0.1790 0.1398 -0.0063 0.0640  0.0614  358  PRO A N   
2881 C  CA  . PRO A 359 ? 0.1408 0.1955 0.1550 0.0170  0.0408  0.0783  358  PRO A CA  
2882 C  C   . PRO A 359 ? 0.1521 0.1717 0.1578 0.0381  0.0316  0.0265  358  PRO A C   
2883 O  O   . PRO A 359 ? 0.1546 0.1813 0.1679 0.0308  0.0435  0.0278  358  PRO A O   
2884 C  CB  . PRO A 359 ? 0.1468 0.1964 0.1474 0.0202  0.0150  0.0992  358  PRO A CB  
2885 C  CG  . PRO A 359 ? 0.1427 0.1755 0.1454 0.0683  0.0373  0.0732  358  PRO A CG  
2886 C  CD  . PRO A 359 ? 0.2194 0.1705 0.1281 0.0152  0.0057  0.0693  358  PRO A CD  
2887 N  N   . GLN A 360 ? 0.1817 0.1437 0.1825 0.0385  0.0262  0.0034  359  GLN A N   
2888 C  CA  . GLN A 360 ? 0.2366 0.1364 0.1842 0.0345  0.0718  -0.0291 359  GLN A CA  
2889 C  C   . GLN A 360 ? 0.2693 0.1874 0.1580 0.0707  0.0412  0.0012  359  GLN A C   
2890 O  O   . GLN A 360 ? 0.2707 0.2154 0.1531 0.1091  0.0476  0.0301  359  GLN A O   
2891 C  CB  . GLN A 360 ? 0.2476 0.1693 0.2515 0.0202  0.1422  -0.0164 359  GLN A CB  
2892 C  CG  . GLN A 360 ? 0.3141 0.2030 0.3118 0.0484  0.0987  -0.0325 359  GLN A CG  
2893 C  CD  . GLN A 360 ? 0.3187 0.2509 0.3269 0.0977  0.0414  0.0068  359  GLN A CD  
2894 O  OE1 . GLN A 360 ? 0.2617 0.2438 0.3285 0.0556  0.0509  0.0231  359  GLN A OE1 
2895 N  NE2 . GLN A 360 ? 0.3415 0.2705 0.3246 0.1349  0.0204  0.0292  359  GLN A NE2 
2896 N  N   . LEU A 361 ? 0.1515 0.1989 0.1379 0.0656  0.0253  0.0086  360  LEU A N   
2897 C  CA  . LEU A 361 ? 0.1874 0.1900 0.1638 0.0836  0.0305  0.0189  360  LEU A CA  
2898 C  C   . LEU A 361 ? 0.1704 0.1974 0.1644 -0.0062 0.0330  0.0023  360  LEU A C   
2899 O  O   . LEU A 361 ? 0.1650 0.2107 0.2001 0.0372  0.0261  -0.0236 360  LEU A O   
2900 C  CB  . LEU A 361 ? 0.1590 0.1982 0.1341 0.1031  0.0010  0.0199  360  LEU A CB  
2901 C  CG  . LEU A 361 ? 0.1275 0.1985 0.1257 0.0858  0.0364  0.0452  360  LEU A CG  
2902 C  CD1 . LEU A 361 ? 0.2057 0.1987 0.1119 0.0553  0.0254  0.0716  360  LEU A CD1 
2903 C  CD2 . LEU A 361 ? 0.1767 0.2043 0.1480 0.1102  -0.0007 0.0232  360  LEU A CD2 
2904 N  N   . HIS A 362 ? 0.1520 0.1774 0.1393 0.0106  0.0034  0.0018  361  HIS A N   
2905 C  CA  . HIS A 362 ? 0.1567 0.1886 0.1313 0.0331  0.0581  0.0132  361  HIS A CA  
2906 C  C   . HIS A 362 ? 0.1817 0.2090 0.1535 0.0515  0.0453  0.0370  361  HIS A C   
2907 O  O   . HIS A 362 ? 0.2055 0.2046 0.1609 0.0398  0.0632  0.0359  361  HIS A O   
2908 C  CB  . HIS A 362 ? 0.1549 0.2104 0.1221 0.0535  0.0628  -0.0085 361  HIS A CB  
2909 C  CG  . HIS A 362 ? 0.1419 0.1904 0.1326 0.0366  0.0461  -0.0018 361  HIS A CG  
2910 N  ND1 . HIS A 362 ? 0.1170 0.2063 0.1504 0.0291  0.0099  0.0132  361  HIS A ND1 
2911 C  CD2 . HIS A 362 ? 0.1423 0.1733 0.1172 0.0235  0.0368  -0.0223 361  HIS A CD2 
2912 C  CE1 . HIS A 362 ? 0.0978 0.1767 0.1415 0.0018  -0.0311 0.0036  361  HIS A CE1 
2913 N  NE2 . HIS A 362 ? 0.1416 0.1746 0.1032 -0.0008 0.0010  0.0035  361  HIS A NE2 
2914 N  N   . ARG A 363 ? 0.1407 0.2406 0.1511 0.0636  0.0669  0.0566  362  ARG A N   
2915 C  CA  . ARG A 363 ? 0.1432 0.2388 0.1416 0.0881  0.0288  0.0786  362  ARG A CA  
2916 C  C   . ARG A 363 ? 0.1579 0.2557 0.1725 0.0452  0.0143  0.0670  362  ARG A C   
2917 O  O   . ARG A 363 ? 0.1596 0.2838 0.1926 0.0553  0.0462  0.0638  362  ARG A O   
2918 C  CB  . ARG A 363 ? 0.1541 0.2581 0.1244 0.1048  0.0328  0.0646  362  ARG A CB  
2919 C  CG  . ARG A 363 ? 0.1635 0.2929 0.1484 0.0573  -0.0076 0.0928  362  ARG A CG  
2920 C  CD  . ARG A 363 ? 0.2034 0.2986 0.1523 0.0814  -0.0186 0.0797  362  ARG A CD  
2921 N  NE  . ARG A 363 ? 0.2013 0.2882 0.1455 0.0753  0.0032  0.0748  362  ARG A NE  
2922 C  CZ  . ARG A 363 ? 0.1633 0.2749 0.1514 0.0154  0.0242  0.0588  362  ARG A CZ  
2923 N  NH1 . ARG A 363 ? 0.1543 0.2703 0.1740 0.0286  0.0324  0.0386  362  ARG A NH1 
2924 N  NH2 . ARG A 363 ? 0.1813 0.2984 0.1561 0.0452  0.0500  0.0424  362  ARG A NH2 
2925 N  N   . ASP A 364 ? 0.1991 0.2192 0.1706 0.0088  -0.0079 0.0710  363  ASP A N   
2926 C  CA  . ASP A 364 ? 0.2307 0.2391 0.1799 0.0380  -0.0198 0.0629  363  ASP A CA  
2927 C  C   . ASP A 364 ? 0.1896 0.3060 0.1894 0.0654  0.0388  0.0567  363  ASP A C   
2928 O  O   . ASP A 364 ? 0.1720 0.3151 0.1770 0.0556  0.0342  0.0612  363  ASP A O   
2929 C  CB  . ASP A 364 ? 0.2084 0.2475 0.1719 0.0353  -0.0743 0.0336  363  ASP A CB  
2930 C  CG  . ASP A 364 ? 0.1939 0.2698 0.1834 0.0737  0.0330  0.0446  363  ASP A CG  
2931 O  OD1 . ASP A 364 ? 0.1832 0.3118 0.1851 0.0861  0.0521  0.0366  363  ASP A OD1 
2932 O  OD2 . ASP A 364 ? 0.2282 0.2594 0.1809 0.0551  0.0195  0.0458  363  ASP A OD2 
2933 N  N   . LYS A 365 ? 0.2203 0.3478 0.2029 0.0608  0.0377  0.0734  364  LYS A N   
2934 C  CA  . LYS A 365 ? 0.2232 0.3587 0.2429 0.0878  0.0298  0.0798  364  LYS A CA  
2935 C  C   . LYS A 365 ? 0.2672 0.3371 0.2159 0.0599  0.0436  0.0629  364  LYS A C   
2936 O  O   . LYS A 365 ? 0.2910 0.3422 0.2047 0.0781  0.0457  0.0603  364  LYS A O   
2937 C  CB  . LYS A 365 ? 0.2082 0.3764 0.3072 0.1420  0.0371  0.0905  364  LYS A CB  
2938 C  CG  . LYS A 365 ? 0.2344 0.4043 0.3523 0.1632  0.0120  0.0701  364  LYS A CG  
2939 C  CD  . LYS A 365 ? 0.2777 0.4582 0.4158 0.1906  -0.0011 0.0760  364  LYS A CD  
2940 C  CE  . LYS A 365 ? 0.3659 0.5306 0.4653 0.2244  0.0151  0.0891  364  LYS A CE  
2941 N  NZ  . LYS A 365 ? 0.4296 0.5517 0.4887 0.1703  0.0383  0.0701  364  LYS A NZ  
2942 N  N   . THR A 366 ? 0.1768 0.3039 0.1893 0.0498  0.0610  0.0452  365  THR A N   
2943 C  CA  . THR A 366 ? 0.2115 0.3024 0.1782 0.0498  0.0722  0.0359  365  THR A CA  
2944 C  C   . THR A 366 ? 0.2825 0.2999 0.1816 0.0441  0.0433  0.0697  365  THR A C   
2945 O  O   . THR A 366 ? 0.2242 0.3090 0.2070 0.0533  0.0689  0.0750  365  THR A O   
2946 C  CB  . THR A 366 ? 0.2982 0.2743 0.2099 0.0160  0.0714  0.0072  365  THR A CB  
2947 O  OG1 . THR A 366 ? 0.3306 0.2845 0.2152 0.0165  0.0304  0.0581  365  THR A OG1 
2948 C  CG2 . THR A 366 ? 0.3444 0.2619 0.2222 0.0443  0.1141  -0.0375 365  THR A CG2 
2949 N  N   . ILE A 367 ? 0.2608 0.2805 0.1655 0.0438  0.0489  0.0611  366  ILE A N   
2950 C  CA  . ILE A 367 ? 0.2447 0.2622 0.1965 0.0520  0.0768  0.0683  366  ILE A CA  
2951 C  C   . ILE A 367 ? 0.2440 0.2612 0.2174 0.0154  0.0358  0.0459  366  ILE A C   
2952 O  O   . ILE A 367 ? 0.3194 0.2152 0.2530 -0.0120 0.0437  0.0219  366  ILE A O   
2953 C  CB  . ILE A 367 ? 0.1967 0.2720 0.2106 0.0728  0.1044  0.0748  366  ILE A CB  
2954 C  CG1 . ILE A 367 ? 0.2042 0.3004 0.2099 0.0259  0.0381  0.1079  366  ILE A CG1 
2955 C  CG2 . ILE A 367 ? 0.2294 0.2646 0.2431 0.0652  0.1295  0.0736  366  ILE A CG2 
2956 C  CD1 . ILE A 367 ? 0.2240 0.3176 0.2143 0.0155  0.0198  0.1369  366  ILE A CD1 
2957 N  N   . TRP A 368 ? 0.1191 0.3276 0.1847 -0.0325 -0.0080 0.0092  367  TRP A N   
2958 C  CA  . TRP A 368 ? 0.1817 0.3802 0.2127 0.0065  0.0560  0.0314  367  TRP A CA  
2959 C  C   . TRP A 368 ? 0.2365 0.4603 0.2424 -0.0209 0.0591  0.0241  367  TRP A C   
2960 O  O   . TRP A 368 ? 0.3018 0.5149 0.2800 -0.0682 0.1104  -0.0019 367  TRP A O   
2961 C  CB  . TRP A 368 ? 0.1770 0.3149 0.2129 0.0484  0.0964  0.0668  367  TRP A CB  
2962 C  CG  . TRP A 368 ? 0.1372 0.2925 0.2078 0.0735  0.0499  0.0745  367  TRP A CG  
2963 C  CD1 . TRP A 368 ? 0.1855 0.2749 0.1994 0.0455  0.0759  0.0791  367  TRP A CD1 
2964 C  CD2 . TRP A 368 ? 0.2305 0.2897 0.1830 0.0511  0.0382  0.0441  367  TRP A CD2 
2965 N  NE1 . TRP A 368 ? 0.2008 0.2677 0.1920 0.0544  0.1035  0.0641  367  TRP A NE1 
2966 C  CE2 . TRP A 368 ? 0.1860 0.2689 0.1875 0.0276  0.0687  0.0491  367  TRP A CE2 
2967 C  CE3 . TRP A 368 ? 0.2207 0.2999 0.1633 0.0802  -0.0144 0.0175  367  TRP A CE3 
2968 C  CZ2 . TRP A 368 ? 0.2284 0.2712 0.1684 0.0052  0.0251  0.0647  367  TRP A CZ2 
2969 C  CZ3 . TRP A 368 ? 0.2484 0.3217 0.1548 0.0112  -0.0763 0.0392  367  TRP A CZ3 
2970 C  CH2 . TRP A 368 ? 0.2116 0.3130 0.1661 0.0082  -0.0223 0.0639  367  TRP A CH2 
2971 N  N   . GLY A 369 ? 0.1947 0.4811 0.2405 0.0090  0.0679  0.0558  368  GLY A N   
2972 C  CA  . GLY A 369 ? 0.2108 0.5182 0.2711 0.0600  0.0550  0.0817  368  GLY A CA  
2973 C  C   . GLY A 369 ? 0.2942 0.5930 0.2888 0.0719  0.0990  0.0835  368  GLY A C   
2974 O  O   . GLY A 369 ? 0.4085 0.5605 0.2682 0.0792  0.1291  0.0805  368  GLY A O   
2975 N  N   . ASP A 370 ? 0.2892 0.6678 0.3295 0.1132  0.1213  0.0983  369  ASP A N   
2976 C  CA  . ASP A 370 ? 0.3936 0.7255 0.3521 0.0894  0.1691  0.1137  369  ASP A CA  
2977 C  C   . ASP A 370 ? 0.4098 0.7155 0.3427 0.0646  0.1480  0.1484  369  ASP A C   
2978 O  O   . ASP A 370 ? 0.4689 0.7316 0.3845 0.0883  0.1348  0.1376  369  ASP A O   
2979 C  CB  . ASP A 370 ? 0.4824 0.7749 0.3608 0.0882  0.1928  0.1195  369  ASP A CB  
2980 C  CG  . ASP A 370 ? 0.6840 0.8356 0.3967 0.0668  0.1927  0.1420  369  ASP A CG  
2981 O  OD1 . ASP A 370 ? 0.7292 0.8417 0.4232 0.0667  0.2033  0.1396  369  ASP A OD1 
2982 O  OD2 . ASP A 370 ? 0.7673 0.8741 0.3806 0.0348  0.1980  0.1551  369  ASP A OD2 
2983 N  N   . ASP A 371 ? 0.3445 0.6646 0.3405 -0.0057 0.1371  0.1424  370  ASP A N   
2984 C  CA  . ASP A 371 ? 0.3289 0.6608 0.3354 -0.0312 0.0890  0.1076  370  ASP A CA  
2985 C  C   . ASP A 371 ? 0.2252 0.6211 0.3522 -0.0232 0.1095  0.0494  370  ASP A C   
2986 O  O   . ASP A 371 ? 0.2364 0.6229 0.3327 -0.0465 0.1029  0.0330  370  ASP A O   
2987 C  CB  . ASP A 371 ? 0.3355 0.6708 0.3410 -0.0869 0.0504  0.1172  370  ASP A CB  
2988 C  CG  . ASP A 371 ? 0.4424 0.6993 0.3547 -0.1385 0.0282  0.1234  370  ASP A CG  
2989 O  OD1 . ASP A 371 ? 0.4358 0.7121 0.3413 -0.1438 0.0245  0.1426  370  ASP A OD1 
2990 O  OD2 . ASP A 371 ? 0.5221 0.7068 0.3864 -0.1586 0.0088  0.1173  370  ASP A OD2 
2991 N  N   . VAL A 372 ? 0.2124 0.5821 0.3592 -0.0117 0.1187  0.0115  371  VAL A N   
2992 C  CA  . VAL A 372 ? 0.2725 0.5181 0.3550 0.0090  0.0951  0.0036  371  VAL A CA  
2993 C  C   . VAL A 372 ? 0.1848 0.4731 0.3117 0.0117  0.0837  -0.0050 371  VAL A C   
2994 O  O   . VAL A 372 ? 0.2027 0.4356 0.2769 0.0277  0.0701  -0.0017 371  VAL A O   
2995 C  CB  . VAL A 372 ? 0.3415 0.4786 0.4014 0.0416  0.0709  -0.0065 371  VAL A CB  
2996 C  CG1 . VAL A 372 ? 0.3654 0.4753 0.4096 0.1329  0.0607  -0.0314 371  VAL A CG1 
2997 C  CG2 . VAL A 372 ? 0.3316 0.4556 0.4123 -0.0260 0.0956  0.0070  371  VAL A CG2 
2998 N  N   . GLU A 373 ? 0.1730 0.4659 0.2902 0.0242  0.0389  -0.0101 372  GLU A N   
2999 C  CA  . GLU A 373 ? 0.2329 0.4598 0.2780 0.0570  0.0265  -0.0075 372  GLU A CA  
3000 C  C   . GLU A 373 ? 0.2824 0.4814 0.2445 0.0595  -0.0030 0.0333  372  GLU A C   
3001 O  O   . GLU A 373 ? 0.3180 0.4981 0.2415 0.0460  0.0201  0.0645  372  GLU A O   
3002 C  CB  . GLU A 373 ? 0.2518 0.4554 0.3114 0.0166  0.0272  -0.0231 372  GLU A CB  
3003 C  CG  . GLU A 373 ? 0.3223 0.4845 0.3265 0.0379  0.0182  -0.0367 372  GLU A CG  
3004 C  CD  . GLU A 373 ? 0.3774 0.5091 0.3393 0.0441  -0.0234 -0.0268 372  GLU A CD  
3005 O  OE1 . GLU A 373 ? 0.4150 0.5152 0.3568 0.0710  -0.0381 -0.0007 372  GLU A OE1 
3006 O  OE2 . GLU A 373 ? 0.3353 0.5292 0.3305 0.0142  -0.0312 -0.0103 372  GLU A OE2 
3007 N  N   . GLU A 374 ? 0.2034 0.5011 0.2169 0.0477  0.0113  0.0557  373  GLU A N   
3008 C  CA  . GLU A 374 ? 0.1890 0.5114 0.2179 0.0176  0.0539  0.0577  373  GLU A CA  
3009 C  C   . GLU A 374 ? 0.1609 0.4685 0.1935 0.0350  0.0203  0.0480  373  GLU A C   
3010 O  O   . GLU A 374 ? 0.2045 0.4651 0.1893 0.0355  0.0166  0.0390  373  GLU A O   
3011 C  CB  . GLU A 374 ? 0.2600 0.5271 0.2550 -0.0195 0.1140  0.0610  373  GLU A CB  
3012 C  CG  . GLU A 374 ? 0.4054 0.6201 0.3121 -0.0617 0.1249  0.0273  373  GLU A CG  
3013 C  CD  . GLU A 374 ? 0.6035 0.6770 0.3921 -0.0803 0.0843  -0.0214 373  GLU A CD  
3014 O  OE1 . GLU A 374 ? 0.6682 0.6887 0.4396 -0.0824 0.0655  -0.0391 373  GLU A OE1 
3015 O  OE2 . GLU A 374 ? 0.6842 0.7060 0.4170 -0.0999 0.0248  -0.0269 373  GLU A OE2 
3016 N  N   . PHE A 375 ? 0.1804 0.4356 0.1725 0.0494  0.0361  0.0426  374  PHE A N   
3017 C  CA  . PHE A 375 ? 0.1618 0.3873 0.1875 0.0473  0.0481  0.0567  374  PHE A CA  
3018 C  C   . PHE A 375 ? 0.1875 0.4047 0.2033 0.0225  0.0069  0.0885  374  PHE A C   
3019 O  O   . PHE A 375 ? 0.2330 0.3885 0.2598 -0.0200 0.0153  0.0751  374  PHE A O   
3020 C  CB  . PHE A 375 ? 0.1564 0.3553 0.1952 0.0188  0.0009  0.0565  374  PHE A CB  
3021 C  CG  . PHE A 375 ? 0.1032 0.3350 0.2033 0.0048  0.0036  0.0564  374  PHE A CG  
3022 C  CD1 . PHE A 375 ? 0.0893 0.2884 0.1940 -0.0395 0.0076  0.0514  374  PHE A CD1 
3023 C  CD2 . PHE A 375 ? 0.1410 0.3503 0.2141 0.0073  -0.0135 0.0596  374  PHE A CD2 
3024 C  CE1 . PHE A 375 ? 0.0908 0.3123 0.1945 -0.0145 0.0058  0.0800  374  PHE A CE1 
3025 C  CE2 . PHE A 375 ? 0.1828 0.3420 0.2255 -0.0371 0.0374  0.0658  374  PHE A CE2 
3026 C  CZ  . PHE A 375 ? 0.1787 0.3292 0.2211 -0.0096 0.0305  0.0766  374  PHE A CZ  
3027 N  N   . ARG A 376 ? 0.1644 0.4215 0.1672 -0.0095 -0.0118 0.0982  375  ARG A N   
3028 C  CA  . ARG A 376 ? 0.1852 0.4247 0.1533 -0.0174 0.0047  0.0944  375  ARG A CA  
3029 C  C   . ARG A 376 ? 0.1399 0.4119 0.1538 -0.0266 -0.0200 0.0500  375  ARG A C   
3030 O  O   . ARG A 376 ? 0.1709 0.4249 0.1546 -0.0058 -0.0024 0.0412  375  ARG A O   
3031 C  CB  . ARG A 376 ? 0.3760 0.4606 0.1731 -0.0543 0.0232  0.1118  375  ARG A CB  
3032 C  CG  . ARG A 376 ? 0.4569 0.5432 0.2259 -0.0412 0.0651  0.1110  375  ARG A CG  
3033 C  CD  . ARG A 376 ? 0.5295 0.5916 0.2822 -0.0636 0.1145  0.0977  375  ARG A CD  
3034 N  NE  . ARG A 376 ? 0.6356 0.6155 0.3259 -0.0842 0.1585  0.0795  375  ARG A NE  
3035 C  CZ  . ARG A 376 ? 0.7515 0.6238 0.3635 -0.1139 0.2161  0.0657  375  ARG A CZ  
3036 N  NH1 . ARG A 376 ? 0.7782 0.6301 0.3772 -0.0848 0.2251  0.0499  375  ARG A NH1 
3037 N  NH2 . ARG A 376 ? 0.7547 0.6135 0.3729 -0.1670 0.2311  0.0407  375  ARG A NH2 
3038 N  N   . PRO A 377 ? 0.1274 0.3647 0.1677 -0.0376 -0.0337 0.0495  376  PRO A N   
3039 C  CA  . PRO A 377 ? 0.1771 0.3292 0.1676 -0.0335 0.0021  0.0625  376  PRO A CA  
3040 C  C   . PRO A 377 ? 0.1237 0.3149 0.1612 -0.0222 0.0166  0.0690  376  PRO A C   
3041 O  O   . PRO A 377 ? 0.1937 0.2706 0.1481 -0.0210 0.0078  0.0714  376  PRO A O   
3042 C  CB  . PRO A 377 ? 0.1941 0.3457 0.1613 -0.0159 -0.0322 0.0528  376  PRO A CB  
3043 C  CG  . PRO A 377 ? 0.1150 0.3776 0.1842 -0.0047 -0.0293 0.0308  376  PRO A CG  
3044 C  CD  . PRO A 377 ? 0.1285 0.3797 0.1682 -0.0659 -0.0348 0.0231  376  PRO A CD  
3045 N  N   . GLU A 378 ? 0.2167 0.3314 0.1763 -0.0089 0.0288  0.0735  377  GLU A N   
3046 C  CA  . GLU A 378 ? 0.2107 0.3754 0.2082 -0.0947 -0.0130 0.0763  377  GLU A CA  
3047 C  C   . GLU A 378 ? 0.1727 0.3865 0.1963 -0.0729 -0.0139 0.0637  377  GLU A C   
3048 O  O   . GLU A 378 ? 0.2038 0.3910 0.1994 -0.0881 -0.0245 0.0700  377  GLU A O   
3049 C  CB  . GLU A 378 ? 0.2159 0.4082 0.2537 -0.1296 -0.0470 0.1051  377  GLU A CB  
3050 C  CG  . GLU A 378 ? 0.2818 0.4225 0.2669 -0.1425 -0.0963 0.1126  377  GLU A CG  
3051 C  CD  . GLU A 378 ? 0.2741 0.4475 0.2894 -0.1281 -0.0574 0.0972  377  GLU A CD  
3052 O  OE1 . GLU A 378 ? 0.2770 0.4078 0.3016 -0.0816 -0.0100 0.1095  377  GLU A OE1 
3053 O  OE2 . GLU A 378 ? 0.2463 0.4881 0.2994 -0.1361 -0.0525 0.0670  377  GLU A OE2 
3054 N  N   . ARG A 379 ? 0.1736 0.3455 0.1959 -0.0685 0.0004  0.0396  378  ARG A N   
3055 C  CA  . ARG A 379 ? 0.2616 0.3394 0.1975 -0.0328 -0.0493 0.0369  378  ARG A CA  
3056 C  C   . ARG A 379 ? 0.2135 0.3217 0.1831 -0.0777 -0.0341 0.0397  378  ARG A C   
3057 O  O   . ARG A 379 ? 0.2133 0.3428 0.2033 -0.0615 -0.0380 0.0491  378  ARG A O   
3058 C  CB  . ARG A 379 ? 0.2730 0.3575 0.2292 0.0500  -0.0391 -0.0226 378  ARG A CB  
3059 C  CG  . ARG A 379 ? 0.4035 0.3722 0.2389 0.0319  0.0090  -0.0187 378  ARG A CG  
3060 C  CD  . ARG A 379 ? 0.3881 0.3325 0.2262 -0.0662 0.0767  -0.0091 378  ARG A CD  
3061 N  NE  . ARG A 379 ? 0.3788 0.3599 0.2458 -0.1299 0.0321  0.0490  378  ARG A NE  
3062 C  CZ  . ARG A 379 ? 0.3519 0.4284 0.2585 -0.0766 0.0139  0.0799  378  ARG A CZ  
3063 N  NH1 . ARG A 379 ? 0.3086 0.4237 0.2205 -0.0882 0.0446  0.0876  378  ARG A NH1 
3064 N  NH2 . ARG A 379 ? 0.3382 0.4936 0.3037 -0.0576 -0.0578 0.0894  378  ARG A NH2 
3065 N  N   . PHE A 380 ? 0.2048 0.2917 0.1604 -0.1328 -0.0124 0.0378  379  PHE A N   
3066 C  CA  . PHE A 380 ? 0.1799 0.2827 0.1826 -0.1116 0.0256  0.0385  379  PHE A CA  
3067 C  C   . PHE A 380 ? 0.1995 0.2777 0.2020 -0.0641 0.0225  0.0254  379  PHE A C   
3068 O  O   . PHE A 380 ? 0.2450 0.2860 0.2239 -0.0756 0.0266  0.0108  379  PHE A O   
3069 C  CB  . PHE A 380 ? 0.1860 0.2944 0.1594 -0.1093 -0.0095 0.0735  379  PHE A CB  
3070 C  CG  . PHE A 380 ? 0.2396 0.2813 0.1938 -0.0547 0.0094  0.1115  379  PHE A CG  
3071 C  CD1 . PHE A 380 ? 0.1898 0.2642 0.2007 -0.0761 0.0217  0.0975  379  PHE A CD1 
3072 C  CD2 . PHE A 380 ? 0.2381 0.2798 0.2052 -0.0398 0.0188  0.1311  379  PHE A CD2 
3073 C  CE1 . PHE A 380 ? 0.2641 0.2586 0.1879 -0.0581 -0.0071 0.1075  379  PHE A CE1 
3074 C  CE2 . PHE A 380 ? 0.1782 0.2803 0.1949 -0.0392 0.0013  0.1152  379  PHE A CE2 
3075 C  CZ  . PHE A 380 ? 0.2286 0.2833 0.2024 -0.0242 0.0049  0.1031  379  PHE A CZ  
3076 N  N   . GLU A 381 ? 0.1735 0.2494 0.2086 -0.0710 -0.0236 0.0014  380  GLU A N   
3077 C  CA  . GLU A 381 ? 0.2219 0.3134 0.2217 -0.0556 -0.0569 0.0104  380  GLU A CA  
3078 C  C   . GLU A 381 ? 0.2065 0.2886 0.2040 -0.0337 0.0007  -0.0006 380  GLU A C   
3079 O  O   . GLU A 381 ? 0.2936 0.3010 0.1915 -0.0356 -0.0320 -0.0287 380  GLU A O   
3080 C  CB  . GLU A 381 ? 0.2222 0.3953 0.2682 -0.1174 -0.0857 0.0169  380  GLU A CB  
3081 C  CG  . GLU A 381 ? 0.4412 0.4782 0.3437 -0.1859 -0.0878 0.0750  380  GLU A CG  
3082 C  CD  . GLU A 381 ? 0.6029 0.5338 0.3769 -0.2067 -0.1111 0.0885  380  GLU A CD  
3083 O  OE1 . GLU A 381 ? 0.7656 0.5569 0.3821 -0.2255 -0.0365 0.1171  380  GLU A OE1 
3084 O  OE2 . GLU A 381 ? 0.5577 0.5198 0.3613 -0.2205 -0.2097 0.0731  380  GLU A OE2 
3085 N  N   . ASN A 382 ? 0.1953 0.2909 0.2064 -0.0462 0.0099  0.0212  381  ASN A N   
3086 C  CA  . ASN A 382 ? 0.1905 0.2593 0.2156 -0.0477 -0.0045 0.0320  381  ASN A CA  
3087 C  C   . ASN A 382 ? 0.2090 0.2328 0.2012 -0.0276 -0.0002 0.0174  381  ASN A C   
3088 O  O   . ASN A 382 ? 0.1807 0.1982 0.1885 -0.0105 -0.0232 0.0325  381  ASN A O   
3089 C  CB  . ASN A 382 ? 0.1853 0.2719 0.2126 -0.0207 -0.0106 0.0369  381  ASN A CB  
3090 C  CG  . ASN A 382 ? 0.2624 0.2630 0.2092 0.0237  -0.0065 0.0496  381  ASN A CG  
3091 O  OD1 . ASN A 382 ? 0.2762 0.2317 0.2101 0.0372  0.0236  0.0426  381  ASN A OD1 
3092 N  ND2 . ASN A 382 ? 0.3198 0.2633 0.2148 -0.0459 0.0228  0.0360  381  ASN A ND2 
3093 N  N   . PRO A 383 ? 0.2106 0.2391 0.1891 -0.0036 0.0274  0.0105  382  PRO A N   
3094 C  CA  . PRO A 383 ? 0.2161 0.2450 0.1706 -0.0109 0.0092  0.0042  382  PRO A CA  
3095 C  C   . PRO A 383 ? 0.2121 0.2080 0.1731 -0.0020 -0.0306 0.0275  382  PRO A C   
3096 O  O   . PRO A 383 ? 0.1665 0.1987 0.2054 0.0115  -0.0010 0.0256  382  PRO A O   
3097 C  CB  . PRO A 383 ? 0.2632 0.2862 0.1741 -0.0276 -0.0170 -0.0217 382  PRO A CB  
3098 C  CG  . PRO A 383 ? 0.2316 0.2848 0.1899 -0.0613 -0.0448 -0.0230 382  PRO A CG  
3099 C  CD  . PRO A 383 ? 0.1765 0.2546 0.1763 -0.0924 0.0267  0.0021  382  PRO A CD  
3100 N  N   . SER A 384 ? 0.1717 0.1992 0.1640 0.0145  0.0046  0.0457  383  SER A N   
3101 C  CA  . SER A 384 ? 0.1862 0.1907 0.1801 0.0044  -0.0124 0.0533  383  SER A CA  
3102 C  C   . SER A 384 ? 0.2185 0.1989 0.1700 0.0291  -0.0310 0.0284  383  SER A C   
3103 O  O   . SER A 384 ? 0.2027 0.2448 0.1897 0.0295  0.0139  0.0218  383  SER A O   
3104 C  CB  . SER A 384 ? 0.1943 0.1631 0.2061 0.0197  0.0337  0.0464  383  SER A CB  
3105 O  OG  . SER A 384 ? 0.2301 0.2299 0.2137 0.0299  0.0365  0.0407  383  SER A OG  
3106 N  N   . ALA A 385 ? 0.1614 0.1917 0.2044 0.0225  -0.0244 0.0074  384  ALA A N   
3107 C  CA  . ALA A 385 ? 0.2234 0.1904 0.2320 0.0104  0.0027  0.0154  384  ALA A CA  
3108 C  C   . ALA A 385 ? 0.1797 0.1821 0.2222 0.0332  -0.0074 0.0196  384  ALA A C   
3109 O  O   . ALA A 385 ? 0.2448 0.2373 0.2460 0.0488  0.0488  0.0122  384  ALA A O   
3110 C  CB  . ALA A 385 ? 0.2247 0.1651 0.2369 -0.0245 0.0360  0.0269  384  ALA A CB  
3111 N  N   . ILE A 386 ? 0.1815 0.1483 0.1718 0.0132  -0.0183 0.0389  385  ILE A N   
3112 C  CA  . ILE A 386 ? 0.2279 0.1684 0.1598 -0.0297 -0.0324 0.0291  385  ILE A CA  
3113 C  C   . ILE A 386 ? 0.2321 0.1599 0.1623 0.0059  -0.0325 0.0298  385  ILE A C   
3114 O  O   . ILE A 386 ? 0.2568 0.1406 0.1745 0.0253  -0.0029 0.0279  385  ILE A O   
3115 C  CB  . ILE A 386 ? 0.2979 0.1734 0.1679 -0.0268 -0.0772 0.0258  385  ILE A CB  
3116 C  CG1 . ILE A 386 ? 0.3681 0.2125 0.1790 0.0150  -0.0365 0.0200  385  ILE A CG1 
3117 C  CG2 . ILE A 386 ? 0.2870 0.1678 0.1785 -0.0466 -0.1256 0.0263  385  ILE A CG2 
3118 C  CD1 . ILE A 386 ? 0.4467 0.2180 0.1884 0.0064  -0.0098 0.0184  385  ILE A CD1 
3119 N  N   . PRO A 387 ? 0.1891 0.1406 0.1698 0.0518  0.0316  0.0147  386  PRO A N   
3120 C  CA  . PRO A 387 ? 0.1661 0.1758 0.1713 0.0529  -0.0011 -0.0232 386  PRO A CA  
3121 C  C   . PRO A 387 ? 0.1134 0.2002 0.1901 0.0558  -0.0018 -0.0164 386  PRO A C   
3122 O  O   . PRO A 387 ? 0.1609 0.2005 0.1964 0.0557  -0.0049 -0.0076 386  PRO A O   
3123 C  CB  . PRO A 387 ? 0.1256 0.2223 0.1798 0.0045  0.0382  -0.0115 386  PRO A CB  
3124 C  CG  . PRO A 387 ? 0.1404 0.2130 0.1709 0.0264  0.0386  -0.0093 386  PRO A CG  
3125 C  CD  . PRO A 387 ? 0.2073 0.1704 0.1932 0.0067  0.0421  -0.0197 386  PRO A CD  
3126 N  N   . GLN A 388 ? 0.0622 0.1951 0.2086 0.0230  -0.0035 0.0144  387  GLN A N   
3127 C  CA  . GLN A 388 ? 0.0590 0.1560 0.1677 0.0310  -0.0219 0.0158  387  GLN A CA  
3128 C  C   . GLN A 388 ? 0.1427 0.1294 0.1553 0.0803  -0.0062 0.0102  387  GLN A C   
3129 O  O   . GLN A 388 ? 0.1886 0.1390 0.1624 0.0479  0.0444  -0.0118 387  GLN A O   
3130 C  CB  . GLN A 388 ? 0.0963 0.1219 0.1950 0.0523  -0.0198 0.0192  387  GLN A CB  
3131 C  CG  . GLN A 388 ? 0.2052 0.1489 0.1717 0.0822  -0.0228 0.0289  387  GLN A CG  
3132 C  CD  . GLN A 388 ? 0.1905 0.1698 0.1656 0.0408  -0.0016 0.0551  387  GLN A CD  
3133 O  OE1 . GLN A 388 ? 0.2078 0.1616 0.1793 0.0418  -0.0184 0.0498  387  GLN A OE1 
3134 N  NE2 . GLN A 388 ? 0.1830 0.1422 0.1714 -0.0099 -0.0215 0.0572  387  GLN A NE2 
3135 N  N   . HIS A 389 ? 0.1913 0.1522 0.1552 0.0485  -0.0029 0.0167  388  HIS A N   
3136 C  CA  . HIS A 389 ? 0.1438 0.1714 0.1518 -0.0102 -0.0469 0.0249  388  HIS A CA  
3137 C  C   . HIS A 389 ? 0.1437 0.1868 0.1519 0.0179  0.0168  0.0087  388  HIS A C   
3138 O  O   . HIS A 389 ? 0.1731 0.2004 0.1655 0.0295  0.0238  0.0107  388  HIS A O   
3139 C  CB  . HIS A 389 ? 0.1551 0.1817 0.1786 0.0511  -0.0245 0.0182  388  HIS A CB  
3140 C  CG  . HIS A 389 ? 0.1391 0.1953 0.1995 0.0126  -0.0199 0.0203  388  HIS A CG  
3141 N  ND1 . HIS A 389 ? 0.1366 0.1907 0.1972 0.0400  0.0164  0.0077  388  HIS A ND1 
3142 C  CD2 . HIS A 389 ? 0.2316 0.2003 0.1978 -0.0155 -0.0262 0.0321  388  HIS A CD2 
3143 C  CE1 . HIS A 389 ? 0.1880 0.2392 0.2133 -0.0202 -0.0150 0.0278  388  HIS A CE1 
3144 N  NE2 . HIS A 389 ? 0.2095 0.2406 0.1854 -0.0132 0.0036  0.0394  388  HIS A NE2 
3145 N  N   . ALA A 390 ? 0.1416 0.2121 0.1254 -0.0096 0.0234  0.0085  389  ALA A N   
3146 C  CA  . ALA A 390 ? 0.0920 0.1968 0.1344 0.0092  0.0074  0.0403  389  ALA A CA  
3147 C  C   . ALA A 390 ? 0.1944 0.1970 0.1165 -0.0150 0.0152  0.0594  389  ALA A C   
3148 O  O   . ALA A 390 ? 0.2207 0.2067 0.1066 -0.0069 -0.0014 0.0265  389  ALA A O   
3149 C  CB  . ALA A 390 ? 0.1227 0.2046 0.1530 -0.0027 0.0196  0.0993  389  ALA A CB  
3150 N  N   . PHE A 391 ? 0.1378 0.1844 0.1020 0.0266  0.0204  0.0163  390  PHE A N   
3151 C  CA  . PHE A 391 ? 0.2252 0.1642 0.1057 0.0165  0.0075  0.0131  390  PHE A CA  
3152 C  C   . PHE A 391 ? 0.1325 0.1469 0.1262 0.0246  0.0421  0.0254  390  PHE A C   
3153 O  O   . PHE A 391 ? 0.1516 0.1634 0.1701 0.0223  0.0508  0.0192  390  PHE A O   
3154 C  CB  . PHE A 391 ? 0.1739 0.1673 0.1089 0.0227  -0.0544 0.0309  390  PHE A CB  
3155 C  CG  . PHE A 391 ? 0.0979 0.1636 0.1191 0.0469  -0.0358 0.0252  390  PHE A CG  
3156 C  CD1 . PHE A 391 ? 0.1121 0.1818 0.1204 0.0085  -0.0366 0.0529  390  PHE A CD1 
3157 C  CD2 . PHE A 391 ? 0.1751 0.1480 0.1287 0.0115  0.0014  0.0190  390  PHE A CD2 
3158 C  CE1 . PHE A 391 ? 0.1485 0.1945 0.1357 0.0248  0.0019  0.0035  390  PHE A CE1 
3159 C  CE2 . PHE A 391 ? 0.2233 0.1254 0.1421 -0.0126 0.0368  0.0344  390  PHE A CE2 
3160 C  CZ  . PHE A 391 ? 0.1660 0.1724 0.1609 0.0065  0.0230  0.0374  390  PHE A CZ  
3161 N  N   . LYS A 392 ? 0.1587 0.1371 0.1239 -0.0071 0.0514  0.0255  391  LYS A N   
3162 C  CA  . LYS A 392 ? 0.1835 0.1451 0.1011 0.0017  -0.0028 0.0211  391  LYS A CA  
3163 C  C   . LYS A 392 ? 0.1824 0.1618 0.1091 0.0087  0.0287  0.0158  391  LYS A C   
3164 O  O   . LYS A 392 ? 0.1520 0.1533 0.1034 0.0286  0.0277  0.0311  391  LYS A O   
3165 C  CB  . LYS A 392 ? 0.1744 0.1878 0.1048 0.0117  0.0233  0.0128  391  LYS A CB  
3166 C  CG  . LYS A 392 ? 0.1646 0.2023 0.1312 0.0455  0.0526  0.0281  391  LYS A CG  
3167 C  CD  . LYS A 392 ? 0.1916 0.2171 0.1659 0.0209  0.0081  0.0444  391  LYS A CD  
3168 C  CE  . LYS A 392 ? 0.1824 0.1922 0.1800 0.0443  0.0050  0.0466  391  LYS A CE  
3169 N  NZ  . LYS A 392 ? 0.2160 0.1726 0.1940 -0.0072 -0.0217 0.0287  391  LYS A NZ  
3170 N  N   . PRO A 393 ? 0.1381 0.1502 0.1219 0.0077  0.0075  0.0292  392  PRO A N   
3171 C  CA  . PRO A 393 ? 0.1040 0.1586 0.1456 0.0522  -0.0015 0.0218  392  PRO A CA  
3172 C  C   . PRO A 393 ? 0.1505 0.1527 0.1298 0.0458  0.0279  0.0100  392  PRO A C   
3173 O  O   . PRO A 393 ? 0.1508 0.1927 0.1171 0.0242  0.0001  0.0013  392  PRO A O   
3174 C  CB  . PRO A 393 ? 0.1364 0.1343 0.1466 -0.0152 -0.0047 0.0223  392  PRO A CB  
3175 C  CG  . PRO A 393 ? 0.1340 0.1175 0.1398 0.0287  -0.0444 0.0346  392  PRO A CG  
3176 C  CD  . PRO A 393 ? 0.1793 0.1249 0.1176 -0.0521 -0.0267 0.0080  392  PRO A CD  
3177 N  N   A HIS A 394 ? 0.0995 0.1466 0.1366 0.0675  0.0133  -0.0092 393  HIS A N   
3178 N  N   B HIS A 394 ? 0.1078 0.1538 0.1288 0.0396  -0.0009 -0.0035 393  HIS A N   
3179 C  CA  A HIS A 394 ? 0.1296 0.1374 0.1469 0.0620  0.0383  -0.0272 393  HIS A CA  
3180 C  CA  B HIS A 394 ? 0.1149 0.1436 0.1321 0.0264  -0.0082 -0.0071 393  HIS A CA  
3181 C  C   A HIS A 394 ? 0.1624 0.1238 0.1221 0.0610  0.0343  -0.0123 393  HIS A C   
3182 C  C   B HIS A 394 ? 0.1346 0.1422 0.1129 0.0036  0.0055  0.0185  393  HIS A C   
3183 O  O   A HIS A 394 ? 0.2194 0.1189 0.1281 0.0426  0.0211  0.0211  393  HIS A O   
3184 O  O   B HIS A 394 ? 0.1149 0.1616 0.1096 -0.0411 0.0171  0.0559  393  HIS A O   
3185 C  CB  A HIS A 394 ? 0.1778 0.1590 0.1545 0.0211  0.0009  -0.0724 393  HIS A CB  
3186 C  CB  B HIS A 394 ? 0.1105 0.1499 0.1418 -0.0113 -0.0616 -0.0399 393  HIS A CB  
3187 C  CG  A HIS A 394 ? 0.2200 0.1535 0.1866 0.0114  -0.0293 -0.0972 393  HIS A CG  
3188 C  CG  B HIS A 394 ? 0.1929 0.1612 0.1766 0.0016  -0.0644 -0.0406 393  HIS A CG  
3189 N  ND1 A HIS A 394 ? 0.1577 0.1612 0.2138 0.0288  -0.0257 -0.0970 393  HIS A ND1 
3190 N  ND1 B HIS A 394 ? 0.1344 0.1579 0.1957 0.0065  -0.0925 -0.0230 393  HIS A ND1 
3191 C  CD2 A HIS A 394 ? 0.2328 0.1638 0.1876 0.0082  -0.0672 -0.0872 393  HIS A CD2 
3192 C  CD2 B HIS A 394 ? 0.2456 0.1722 0.1953 -0.0154 -0.0916 -0.0418 393  HIS A CD2 
3193 C  CE1 A HIS A 394 ? 0.1863 0.1816 0.2105 0.0271  -0.0137 -0.1025 393  HIS A CE1 
3194 C  CE1 B HIS A 394 ? 0.1425 0.1719 0.2007 0.0225  -0.0960 -0.0022 393  HIS A CE1 
3195 N  NE2 A HIS A 394 ? 0.2377 0.1515 0.2037 0.0215  -0.0507 -0.0944 393  HIS A NE2 
3196 N  NE2 B HIS A 394 ? 0.2189 0.1865 0.2146 0.0077  -0.0779 -0.0137 393  HIS A NE2 
3197 N  N   . GLY A 395 ? 0.1943 0.1155 0.1149 0.0175  -0.0066 0.0066  394  GLY A N   
3198 C  CA  . GLY A 395 ? 0.1697 0.1380 0.1018 -0.0038 -0.0210 -0.0264 394  GLY A CA  
3199 C  C   . GLY A 395 ? 0.1979 0.1527 0.1221 0.0068  -0.0090 0.0197  394  GLY A C   
3200 O  O   . GLY A 395 ? 0.1594 0.1686 0.1429 -0.0096 0.0002  0.0502  394  GLY A O   
3201 N  N   . ASN A 396 ? 0.1860 0.1551 0.0880 0.0526  -0.0379 -0.0006 395  ASN A N   
3202 C  CA  . ASN A 396 ? 0.1746 0.1647 0.0998 0.0645  -0.0042 0.0272  395  ASN A CA  
3203 C  C   . ASN A 396 ? 0.1718 0.1377 0.1249 0.0833  0.0011  0.0311  395  ASN A C   
3204 O  O   . ASN A 396 ? 0.1691 0.1233 0.1547 -0.0001 0.0038  0.0284  395  ASN A O   
3205 C  CB  . ASN A 396 ? 0.1971 0.1786 0.1027 0.0481  0.0062  0.0211  395  ASN A CB  
3206 C  CG  . ASN A 396 ? 0.1878 0.1895 0.1365 0.0575  -0.0002 0.0228  395  ASN A CG  
3207 O  OD1 . ASN A 396 ? 0.2170 0.1862 0.1254 0.0430  0.0009  0.0325  395  ASN A OD1 
3208 N  ND2 . ASN A 396 ? 0.1946 0.1954 0.1536 0.0043  -0.0213 0.0163  395  ASN A ND2 
3209 N  N   . GLY A 397 ? 0.1842 0.1612 0.1520 0.0898  -0.0217 0.0308  396  GLY A N   
3210 C  CA  . GLY A 397 ? 0.1647 0.1747 0.1639 0.0927  0.0200  0.0335  396  GLY A CA  
3211 C  C   . GLY A 397 ? 0.2314 0.1238 0.1471 0.0457  0.0466  0.0246  396  GLY A C   
3212 O  O   . GLY A 397 ? 0.1914 0.1257 0.1683 0.0199  0.0436  -0.0292 396  GLY A O   
3213 N  N   . GLN A 398 ? 0.1701 0.1288 0.1556 0.0243  0.0387  0.0137  397  GLN A N   
3214 C  CA  . GLN A 398 ? 0.1378 0.1475 0.1638 -0.0076 0.0395  0.0157  397  GLN A CA  
3215 C  C   . GLN A 398 ? 0.1547 0.1319 0.1688 -0.0101 0.0202  0.0210  397  GLN A C   
3216 O  O   . GLN A 398 ? 0.1443 0.1586 0.1719 -0.0408 0.0289  -0.0223 397  GLN A O   
3217 C  CB  . GLN A 398 ? 0.1196 0.1394 0.1859 0.0082  0.0028  -0.0342 397  GLN A CB  
3218 C  CG  . GLN A 398 ? 0.1485 0.1281 0.2073 0.0223  -0.0626 -0.0503 397  GLN A CG  
3219 C  CD  . GLN A 398 ? 0.1947 0.1489 0.2072 0.0545  -0.0366 -0.0257 397  GLN A CD  
3220 O  OE1 . GLN A 398 ? 0.2262 0.2205 0.2016 -0.0006 -0.0282 -0.0110 397  GLN A OE1 
3221 N  NE2 . GLN A 398 ? 0.1986 0.1811 0.2315 -0.0170 -0.0256 -0.0330 397  GLN A NE2 
3222 N  N   . ARG A 399 ? 0.0927 0.1295 0.1765 -0.0122 -0.0083 0.0014  398  ARG A N   
3223 C  CA  . ARG A 399 ? 0.2005 0.0944 0.1634 -0.0119 -0.0087 -0.0020 398  ARG A CA  
3224 C  C   . ARG A 399 ? 0.1962 0.0863 0.1344 0.0209  0.0010  -0.0097 398  ARG A C   
3225 O  O   . ARG A 399 ? 0.1553 0.1047 0.1518 -0.0145 0.0166  0.0004  398  ARG A O   
3226 C  CB  . ARG A 399 ? 0.1455 0.1244 0.1597 -0.0448 -0.0031 -0.0193 398  ARG A CB  
3227 C  CG  . ARG A 399 ? 0.0830 0.1280 0.1271 -0.0517 0.0267  0.0075  398  ARG A CG  
3228 C  CD  . ARG A 399 ? 0.1128 0.1365 0.1293 -0.0326 0.0598  0.0184  398  ARG A CD  
3229 N  NE  . ARG A 399 ? 0.1268 0.1398 0.1279 -0.0179 0.0326  0.0327  398  ARG A NE  
3230 C  CZ  . ARG A 399 ? 0.1522 0.1674 0.1245 -0.0455 -0.0124 -0.0079 398  ARG A CZ  
3231 N  NH1 . ARG A 399 ? 0.1328 0.1767 0.1273 -0.0464 0.0265  -0.0223 398  ARG A NH1 
3232 N  NH2 . ARG A 399 ? 0.1611 0.1622 0.1291 -0.0061 0.0141  -0.0277 398  ARG A NH2 
3233 N  N   . ALA A 400 ? 0.1473 0.1070 0.1529 -0.0096 0.0060  -0.0372 399  ALA A N   
3234 C  CA  . ALA A 400 ? 0.1583 0.0963 0.1453 -0.0251 -0.0095 -0.0179 399  ALA A CA  
3235 C  C   . ALA A 400 ? 0.1693 0.1300 0.1534 -0.0426 0.0042  0.0035  399  ALA A C   
3236 O  O   . ALA A 400 ? 0.1236 0.1441 0.1953 -0.0044 0.0380  0.0043  399  ALA A O   
3237 C  CB  . ALA A 400 ? 0.1634 0.1438 0.1388 -0.0505 -0.0194 -0.0110 399  ALA A CB  
3238 N  N   . CYS A 401 ? 0.1320 0.1248 0.1320 -0.0122 -0.0313 0.0116  400  CYS A N   
3239 C  CA  . CYS A 401 ? 0.0726 0.1628 0.1499 0.0326  -0.0178 0.0023  400  CYS A CA  
3240 C  C   . CYS A 401 ? 0.1010 0.1846 0.1632 -0.0166 0.0573  -0.0044 400  CYS A C   
3241 O  O   . CYS A 401 ? 0.2214 0.1508 0.2292 0.0148  0.1078  0.0180  400  CYS A O   
3242 C  CB  . CYS A 401 ? 0.1179 0.1911 0.1491 0.0653  -0.0335 -0.0276 400  CYS A CB  
3243 S  SG  . CYS A 401 ? 0.1458 0.1924 0.1648 0.0129  -0.0062 -0.0530 400  CYS A SG  
3244 N  N   . ILE A 402 ? 0.1848 0.1922 0.1556 0.0043  0.0168  -0.0346 401  ILE A N   
3245 C  CA  . ILE A 402 ? 0.1156 0.1645 0.1538 0.0021  0.0113  -0.0602 401  ILE A CA  
3246 C  C   . ILE A 402 ? 0.1847 0.1384 0.1334 0.0354  0.0344  -0.0640 401  ILE A C   
3247 O  O   . ILE A 402 ? 0.1910 0.1426 0.1663 0.0327  0.0365  -0.0533 401  ILE A O   
3248 C  CB  . ILE A 402 ? 0.1058 0.1835 0.1486 0.0545  0.0118  -0.0090 401  ILE A CB  
3249 C  CG1 . ILE A 402 ? 0.0607 0.2083 0.1584 0.0088  0.0220  -0.0251 401  ILE A CG1 
3250 C  CG2 . ILE A 402 ? 0.0891 0.1767 0.1658 0.0400  -0.0212 -0.0096 401  ILE A CG2 
3251 C  CD1 . ILE A 402 ? 0.1021 0.2426 0.1945 0.0406  0.0343  -0.0274 401  ILE A CD1 
3252 N  N   . GLY A 403 ? 0.1569 0.1341 0.1289 -0.0288 0.0133  -0.0369 402  GLY A N   
3253 C  CA  . GLY A 403 ? 0.1777 0.1551 0.1658 -0.0358 -0.0083 -0.0522 402  GLY A CA  
3254 C  C   . GLY A 403 ? 0.1512 0.1698 0.1767 0.0068  -0.0103 -0.0327 402  GLY A C   
3255 O  O   . GLY A 403 ? 0.1715 0.1688 0.1801 -0.0199 -0.0278 -0.0091 402  GLY A O   
3256 N  N   . GLN A 404 ? 0.1629 0.1708 0.1486 0.0148  0.0209  -0.0119 403  GLN A N   
3257 C  CA  . GLN A 404 ? 0.1645 0.1751 0.1306 -0.0383 0.0354  -0.0029 403  GLN A CA  
3258 C  C   . GLN A 404 ? 0.1552 0.1835 0.1406 -0.0149 -0.0139 -0.0159 403  GLN A C   
3259 O  O   . GLN A 404 ? 0.1837 0.1795 0.1730 -0.0046 -0.0249 0.0118  403  GLN A O   
3260 C  CB  . GLN A 404 ? 0.2400 0.2448 0.1504 -0.1059 0.0742  -0.0118 403  GLN A CB  
3261 C  CG  . GLN A 404 ? 0.3293 0.3397 0.1767 -0.1497 0.0485  0.0018  403  GLN A CG  
3262 C  CD  . GLN A 404 ? 0.4095 0.3761 0.2538 -0.1049 0.0557  -0.0123 403  GLN A CD  
3263 O  OE1 . GLN A 404 ? 0.3605 0.3875 0.2023 -0.0581 -0.0167 -0.0675 403  GLN A OE1 
3264 N  NE2 . GLN A 404 ? 0.4652 0.3842 0.3044 -0.1054 0.0682  0.0372  403  GLN A NE2 
3265 N  N   . GLN A 405 ? 0.2767 0.1515 0.1350 0.0112  -0.0246 -0.0345 404  GLN A N   
3266 C  CA  . GLN A 405 ? 0.3078 0.1698 0.1802 0.0056  -0.0392 -0.0406 404  GLN A CA  
3267 C  C   . GLN A 405 ? 0.1929 0.1581 0.2032 0.0112  -0.0455 -0.0216 404  GLN A C   
3268 O  O   . GLN A 405 ? 0.1885 0.1475 0.2313 0.0032  -0.0046 -0.0235 404  GLN A O   
3269 C  CB  . GLN A 405 ? 0.4004 0.2139 0.1991 0.0068  -0.0481 -0.0171 404  GLN A CB  
3270 C  CG  . GLN A 405 ? 0.5882 0.2794 0.2719 0.0566  0.0443  0.0128  404  GLN A CG  
3271 C  CD  . GLN A 405 ? 0.8566 0.3570 0.3236 0.0913  0.1143  0.0219  404  GLN A CD  
3272 O  OE1 . GLN A 405 ? 0.9449 0.4087 0.3775 0.1120  0.0940  0.0485  404  GLN A OE1 
3273 N  NE2 . GLN A 405 ? 0.9173 0.3982 0.3439 0.0436  0.1672  0.0381  404  GLN A NE2 
3274 N  N   . PHE A 406 ? 0.2121 0.1334 0.1885 0.0397  -0.0439 0.0165  405  PHE A N   
3275 C  CA  . PHE A 406 ? 0.1885 0.1746 0.1805 0.0451  -0.0590 -0.0130 405  PHE A CA  
3276 C  C   . PHE A 406 ? 0.1583 0.1772 0.1683 0.0074  -0.0513 -0.0172 405  PHE A C   
3277 O  O   . PHE A 406 ? 0.1945 0.1754 0.1925 -0.0170 -0.0084 -0.0222 405  PHE A O   
3278 C  CB  . PHE A 406 ? 0.1542 0.2173 0.1469 -0.0081 -0.0358 -0.0272 405  PHE A CB  
3279 C  CG  . PHE A 406 ? 0.1668 0.2155 0.1674 0.0007  -0.0343 -0.0309 405  PHE A CG  
3280 C  CD1 . PHE A 406 ? 0.1054 0.2091 0.1506 0.0165  -0.0350 -0.0226 405  PHE A CD1 
3281 C  CD2 . PHE A 406 ? 0.2316 0.2024 0.1599 0.0074  -0.0470 -0.0653 405  PHE A CD2 
3282 C  CE1 . PHE A 406 ? 0.1833 0.1990 0.1679 0.0122  0.0120  -0.0234 405  PHE A CE1 
3283 C  CE2 . PHE A 406 ? 0.2463 0.2076 0.1767 0.0335  -0.0549 -0.0146 405  PHE A CE2 
3284 C  CZ  . PHE A 406 ? 0.2190 0.2152 0.1707 0.0381  -0.0185 0.0160  405  PHE A CZ  
3285 N  N   . ALA A 407 ? 0.1622 0.1515 0.1480 -0.0129 0.0020  -0.0378 406  ALA A N   
3286 C  CA  . ALA A 407 ? 0.1772 0.1384 0.1505 0.0157  -0.0188 -0.0209 406  ALA A CA  
3287 C  C   . ALA A 407 ? 0.1812 0.1606 0.1377 -0.0131 -0.0007 -0.0003 406  ALA A C   
3288 O  O   . ALA A 407 ? 0.1927 0.1792 0.1481 -0.0224 -0.0125 -0.0002 406  ALA A O   
3289 C  CB  . ALA A 407 ? 0.1306 0.1333 0.1359 0.0784  -0.0139 -0.0079 406  ALA A CB  
3290 N  N   . LEU A 408 ? 0.1589 0.1530 0.1407 -0.0238 0.0157  0.0232  407  LEU A N   
3291 C  CA  . LEU A 408 ? 0.2284 0.1691 0.1273 -0.0706 -0.0111 0.0282  407  LEU A CA  
3292 C  C   . LEU A 408 ? 0.2058 0.1714 0.1541 -0.0640 -0.0278 0.0036  407  LEU A C   
3293 O  O   . LEU A 408 ? 0.1863 0.1769 0.1455 -0.0951 -0.0280 -0.0006 407  LEU A O   
3294 C  CB  . LEU A 408 ? 0.2589 0.2130 0.1057 -0.0627 -0.0569 0.0235  407  LEU A CB  
3295 C  CG  . LEU A 408 ? 0.3641 0.2854 0.1548 0.0029  -0.0041 0.0174  407  LEU A CG  
3296 C  CD1 . LEU A 408 ? 0.4614 0.2877 0.1577 -0.0262 0.0302  0.0469  407  LEU A CD1 
3297 C  CD2 . LEU A 408 ? 0.4807 0.3218 0.1851 0.0492  -0.0124 -0.0176 407  LEU A CD2 
3298 N  N   . HIS A 409 ? 0.2771 0.1644 0.1661 -0.0381 -0.0342 0.0100  408  HIS A N   
3299 C  CA  . HIS A 409 ? 0.1594 0.1425 0.1660 0.0291  -0.0489 -0.0278 408  HIS A CA  
3300 C  C   . HIS A 409 ? 0.1503 0.1664 0.1734 0.0294  -0.0560 -0.0003 408  HIS A C   
3301 O  O   . HIS A 409 ? 0.1842 0.1750 0.1809 0.0047  -0.0391 0.0039  408  HIS A O   
3302 C  CB  . HIS A 409 ? 0.1837 0.1227 0.2012 0.0340  -0.0333 -0.0623 408  HIS A CB  
3303 C  CG  . HIS A 409 ? 0.2761 0.1833 0.2267 0.0330  -0.0415 -0.0600 408  HIS A CG  
3304 N  ND1 . HIS A 409 ? 0.2780 0.1757 0.2210 -0.0234 -0.0628 -0.0453 408  HIS A ND1 
3305 C  CD2 . HIS A 409 ? 0.2538 0.1975 0.2316 0.0656  -0.0703 -0.0748 408  HIS A CD2 
3306 C  CE1 . HIS A 409 ? 0.2708 0.1953 0.2179 0.0193  -0.0136 -0.0390 408  HIS A CE1 
3307 N  NE2 . HIS A 409 ? 0.2264 0.2017 0.2342 0.0923  -0.0267 -0.0353 408  HIS A NE2 
3308 N  N   . GLU A 410 ? 0.1447 0.1696 0.1684 -0.0061 -0.0283 0.0233  409  GLU A N   
3309 C  CA  . GLU A 410 ? 0.1849 0.1563 0.1815 0.0041  -0.0273 0.0392  409  GLU A CA  
3310 C  C   . GLU A 410 ? 0.1454 0.1523 0.1746 -0.0341 0.0034  -0.0053 409  GLU A C   
3311 O  O   . GLU A 410 ? 0.1712 0.1333 0.1790 -0.0244 -0.0336 -0.0499 409  GLU A O   
3312 C  CB  . GLU A 410 ? 0.2088 0.1496 0.1875 -0.0031 -0.0344 0.0481  409  GLU A CB  
3313 C  CG  . GLU A 410 ? 0.1521 0.1266 0.2073 -0.0279 -0.0248 0.0661  409  GLU A CG  
3314 C  CD  . GLU A 410 ? 0.2025 0.2218 0.2458 -0.0019 0.0191  0.0366  409  GLU A CD  
3315 O  OE1 . GLU A 410 ? 0.2637 0.2280 0.2656 -0.0094 0.0194  0.0095  409  GLU A OE1 
3316 O  OE2 . GLU A 410 ? 0.2495 0.2485 0.2720 -0.0128 0.0396  0.0325  409  GLU A OE2 
3317 N  N   . ALA A 411 ? 0.1590 0.1297 0.1594 -0.0132 0.0436  0.0257  410  ALA A N   
3318 C  CA  . ALA A 411 ? 0.1504 0.1439 0.1645 -0.0434 0.0341  -0.0023 410  ALA A CA  
3319 C  C   . ALA A 411 ? 0.1777 0.1554 0.1675 -0.0287 -0.0088 0.0244  410  ALA A C   
3320 O  O   . ALA A 411 ? 0.1832 0.1785 0.1890 -0.0051 0.0085  0.0407  410  ALA A O   
3321 C  CB  . ALA A 411 ? 0.2106 0.1683 0.1527 0.0400  0.0180  -0.0155 410  ALA A CB  
3322 N  N   . THR A 412 ? 0.1889 0.1615 0.1434 -0.0083 -0.0449 0.0113  411  THR A N   
3323 C  CA  . THR A 412 ? 0.2112 0.1731 0.1489 -0.0303 -0.0399 0.0067  411  THR A CA  
3324 C  C   . THR A 412 ? 0.1464 0.2076 0.1502 -0.0223 -0.0196 0.0101  411  THR A C   
3325 O  O   . THR A 412 ? 0.1843 0.1981 0.1487 -0.0518 -0.0103 0.0408  411  THR A O   
3326 C  CB  . THR A 412 ? 0.2257 0.1540 0.1617 -0.0515 -0.0433 0.0076  411  THR A CB  
3327 O  OG1 . THR A 412 ? 0.2027 0.1796 0.1514 -0.0351 -0.0167 0.0389  411  THR A OG1 
3328 C  CG2 . THR A 412 ? 0.1625 0.1368 0.1850 -0.0685 -0.0307 0.0269  411  THR A CG2 
3329 N  N   . LEU A 413 ? 0.1844 0.2107 0.1338 -0.0355 0.0012  0.0166  412  LEU A N   
3330 C  CA  . LEU A 413 ? 0.2142 0.1946 0.1300 -0.0167 0.0026  0.0098  412  LEU A CA  
3331 C  C   . LEU A 413 ? 0.1776 0.1958 0.1795 -0.0693 -0.0116 0.0262  412  LEU A C   
3332 O  O   . LEU A 413 ? 0.2532 0.1834 0.1696 -0.0656 -0.0515 0.0251  412  LEU A O   
3333 C  CB  . LEU A 413 ? 0.1978 0.1835 0.1521 -0.0113 0.0303  -0.0265 412  LEU A CB  
3334 C  CG  . LEU A 413 ? 0.3090 0.1889 0.1751 -0.0816 0.0517  -0.0392 412  LEU A CG  
3335 C  CD1 . LEU A 413 ? 0.3723 0.2179 0.1785 -0.0381 0.0267  -0.0306 412  LEU A CD1 
3336 C  CD2 . LEU A 413 ? 0.2689 0.1794 0.1965 -0.0951 0.0693  -0.0546 412  LEU A CD2 
3337 N  N   . VAL A 414 ? 0.1939 0.1968 0.1991 -0.0739 0.0045  0.0512  413  VAL A N   
3338 C  CA  . VAL A 414 ? 0.1432 0.1951 0.2232 -0.0868 0.0030  0.0499  413  VAL A CA  
3339 C  C   . VAL A 414 ? 0.1709 0.1856 0.1888 -0.0372 0.0089  0.0309  413  VAL A C   
3340 O  O   . VAL A 414 ? 0.1846 0.1816 0.2021 -0.0581 -0.0137 0.0222  413  VAL A O   
3341 C  CB  . VAL A 414 ? 0.1326 0.2237 0.2460 -0.0766 -0.0142 0.0790  413  VAL A CB  
3342 C  CG1 . VAL A 414 ? 0.2067 0.2374 0.3208 -0.0660 -0.0034 0.1004  413  VAL A CG1 
3343 C  CG2 . VAL A 414 ? 0.2259 0.2679 0.2155 -0.0482 -0.0351 0.0538  413  VAL A CG2 
3344 N  N   . LEU A 415 ? 0.2288 0.1965 0.1524 -0.0310 0.0408  0.0085  414  LEU A N   
3345 C  CA  . LEU A 415 ? 0.2486 0.2272 0.1334 -0.0372 -0.0102 0.0411  414  LEU A CA  
3346 C  C   . LEU A 415 ? 0.3301 0.2494 0.1621 -0.0326 -0.0221 0.0348  414  LEU A C   
3347 O  O   . LEU A 415 ? 0.3020 0.2532 0.1529 -0.0528 -0.0249 0.0521  414  LEU A O   
3348 C  CB  . LEU A 415 ? 0.2098 0.2645 0.1336 -0.0025 -0.0161 0.0148  414  LEU A CB  
3349 C  CG  . LEU A 415 ? 0.2179 0.2727 0.1301 0.0474  -0.0726 0.0331  414  LEU A CG  
3350 C  CD1 . LEU A 415 ? 0.2455 0.2936 0.1668 0.0515  -0.0860 0.0255  414  LEU A CD1 
3351 C  CD2 . LEU A 415 ? 0.2040 0.2737 0.1379 -0.0015 -0.0576 -0.0060 414  LEU A CD2 
3352 N  N   . GLY A 416 ? 0.2531 0.2251 0.1745 -0.0439 -0.0440 0.0423  415  GLY A N   
3353 C  CA  . GLY A 416 ? 0.2158 0.2100 0.1611 -0.0873 -0.0193 0.0527  415  GLY A CA  
3354 C  C   . GLY A 416 ? 0.2086 0.2199 0.1489 -0.1143 -0.0092 0.0411  415  GLY A C   
3355 O  O   . GLY A 416 ? 0.2689 0.2735 0.1619 -0.1282 -0.0550 0.0383  415  GLY A O   
3356 N  N   . MET A 417 ? 0.1928 0.2203 0.1231 -0.0795 -0.0350 0.0348  416  MET A N   
3357 C  CA  . MET A 417 ? 0.1795 0.2353 0.1241 -0.0380 -0.0365 0.0278  416  MET A CA  
3358 C  C   . MET A 417 ? 0.2115 0.2410 0.1327 -0.0176 -0.0363 0.0236  416  MET A C   
3359 O  O   . MET A 417 ? 0.2007 0.2679 0.1655 -0.0244 -0.0501 0.0326  416  MET A O   
3360 C  CB  . MET A 417 ? 0.2100 0.2382 0.1661 -0.0185 0.0226  0.0199  416  MET A CB  
3361 C  CG  . MET A 417 ? 0.1941 0.2303 0.1972 -0.0041 0.0172  0.0159  416  MET A CG  
3362 S  SD  . MET A 417 ? 0.3221 0.2357 0.2560 -0.0262 -0.0062 0.0093  416  MET A SD  
3363 C  CE  . MET A 417 ? 0.3342 0.3055 0.2261 0.0587  -0.0301 0.0167  416  MET A CE  
3364 N  N   . MET A 418 ? 0.2497 0.2543 0.1426 -0.0034 -0.0026 0.0426  417  MET A N   
3365 C  CA  . MET A 418 ? 0.2207 0.2671 0.1761 -0.0469 0.0080  0.0359  417  MET A CA  
3366 C  C   . MET A 418 ? 0.2253 0.2690 0.1895 -0.1023 0.0033  0.0809  417  MET A C   
3367 O  O   . MET A 418 ? 0.2680 0.2998 0.1846 -0.1195 -0.0269 0.0716  417  MET A O   
3368 C  CB  . MET A 418 ? 0.1750 0.2535 0.1932 -0.0425 -0.0374 0.0174  417  MET A CB  
3369 C  CG  . MET A 418 ? 0.2261 0.2338 0.1975 -0.1039 -0.0339 0.0054  417  MET A CG  
3370 S  SD  . MET A 418 ? 0.2479 0.2756 0.2324 -0.0621 -0.0004 0.0093  417  MET A SD  
3371 C  CE  . MET A 418 ? 0.3173 0.2726 0.2598 -0.0395 0.0152  -0.0010 417  MET A CE  
3372 N  N   . LEU A 419 ? 0.1899 0.2651 0.1771 -0.0445 0.0348  0.0919  418  LEU A N   
3373 C  CA  . LEU A 419 ? 0.1961 0.3008 0.1772 -0.1013 0.0373  0.0534  418  LEU A CA  
3374 C  C   . LEU A 419 ? 0.2350 0.3047 0.1694 -0.0796 0.0143  0.0436  418  LEU A C   
3375 O  O   . LEU A 419 ? 0.2869 0.3287 0.1710 -0.0835 -0.0186 0.0371  418  LEU A O   
3376 C  CB  . LEU A 419 ? 0.2537 0.2835 0.1624 -0.0622 -0.0229 0.0468  418  LEU A CB  
3377 C  CG  . LEU A 419 ? 0.3113 0.3000 0.2126 -0.0667 -0.0454 0.0169  418  LEU A CG  
3378 C  CD1 . LEU A 419 ? 0.3017 0.3059 0.1892 -0.0941 -0.0509 0.0105  418  LEU A CD1 
3379 C  CD2 . LEU A 419 ? 0.3968 0.3016 0.2601 -0.0296 -0.0642 0.0111  418  LEU A CD2 
3380 N  N   . LYS A 420 ? 0.2964 0.3119 0.1718 -0.0802 -0.0143 0.0390  419  LYS A N   
3381 C  CA  . LYS A 420 ? 0.3034 0.2975 0.1715 -0.0756 -0.0320 0.0137  419  LYS A CA  
3382 C  C   . LYS A 420 ? 0.2952 0.3022 0.1758 -0.1127 -0.0464 0.0192  419  LYS A C   
3383 O  O   . LYS A 420 ? 0.3481 0.2956 0.1964 -0.1321 -0.0579 0.0270  419  LYS A O   
3384 C  CB  . LYS A 420 ? 0.4272 0.2786 0.1783 -0.0696 -0.0257 -0.0298 419  LYS A CB  
3385 C  CG  . LYS A 420 ? 0.3511 0.2722 0.1995 -0.0608 -0.0580 -0.0356 419  LYS A CG  
3386 C  CD  . LYS A 420 ? 0.3869 0.2578 0.2238 -0.0774 -0.0326 -0.0316 419  LYS A CD  
3387 C  CE  . LYS A 420 ? 0.4067 0.2804 0.2262 -0.0386 -0.0466 -0.0100 419  LYS A CE  
3388 N  NZ  . LYS A 420 ? 0.3781 0.2791 0.2480 -0.0591 -0.0286 0.0152  419  LYS A NZ  
3389 N  N   . HIS A 421 ? 0.3006 0.3113 0.1484 -0.1299 -0.0291 0.0374  420  HIS A N   
3390 C  CA  . HIS A 421 ? 0.2165 0.3270 0.1541 -0.1034 -0.0216 0.0727  420  HIS A CA  
3391 C  C   . HIS A 421 ? 0.2347 0.3503 0.1843 -0.0878 -0.0477 0.0758  420  HIS A C   
3392 O  O   . HIS A 421 ? 0.2672 0.3575 0.2028 -0.1225 -0.0620 0.0698  420  HIS A O   
3393 C  CB  . HIS A 421 ? 0.2325 0.3236 0.1699 -0.0924 -0.0563 0.0626  420  HIS A CB  
3394 C  CG  . HIS A 421 ? 0.2874 0.3384 0.1904 -0.0982 -0.0348 0.0343  420  HIS A CG  
3395 N  ND1 . HIS A 421 ? 0.3341 0.3370 0.2082 -0.1448 -0.0409 0.0145  420  HIS A ND1 
3396 C  CD2 . HIS A 421 ? 0.3607 0.3332 0.1908 -0.1259 -0.0244 0.0128  420  HIS A CD2 
3397 C  CE1 . HIS A 421 ? 0.3756 0.3381 0.2071 -0.1427 -0.0515 0.0018  420  HIS A CE1 
3398 N  NE2 . HIS A 421 ? 0.3968 0.3311 0.1887 -0.1162 -0.0280 0.0210  420  HIS A NE2 
3399 N  N   . PHE A 422 ? 0.2146 0.3347 0.1909 -0.1310 -0.0186 0.0654  421  PHE A N   
3400 C  CA  . PHE A 422 ? 0.1753 0.3269 0.2277 -0.1234 -0.0150 0.0604  421  PHE A CA  
3401 C  C   . PHE A 422 ? 0.2063 0.3443 0.2627 -0.1447 -0.0163 0.0515  421  PHE A C   
3402 O  O   . PHE A 422 ? 0.2203 0.3627 0.2632 -0.1325 -0.0339 0.0584  421  PHE A O   
3403 C  CB  . PHE A 422 ? 0.2350 0.3337 0.2286 -0.1277 -0.0429 0.0719  421  PHE A CB  
3404 C  CG  . PHE A 422 ? 0.1904 0.3363 0.2037 -0.1095 -0.0288 0.0794  421  PHE A CG  
3405 C  CD1 . PHE A 422 ? 0.2187 0.3509 0.1886 -0.1051 -0.0440 0.0810  421  PHE A CD1 
3406 C  CD2 . PHE A 422 ? 0.1952 0.3170 0.2018 -0.0824 -0.0745 0.0469  421  PHE A CD2 
3407 C  CE1 . PHE A 422 ? 0.2560 0.3407 0.1891 -0.0566 -0.0567 0.0806  421  PHE A CE1 
3408 C  CE2 . PHE A 422 ? 0.1592 0.3249 0.1850 -0.0364 -0.0350 0.0697  421  PHE A CE2 
3409 C  CZ  . PHE A 422 ? 0.1964 0.3291 0.1827 -0.0289 -0.0663 0.0694  421  PHE A CZ  
3410 N  N   . ASP A 423 ? 0.1740 0.3431 0.2641 -0.1189 0.0073  0.0075  422  ASP A N   
3411 C  CA  . ASP A 423 ? 0.1804 0.3627 0.2636 -0.0876 0.0360  0.0101  422  ASP A CA  
3412 C  C   . ASP A 423 ? 0.2597 0.3336 0.2318 -0.0608 0.0457  0.0205  422  ASP A C   
3413 O  O   . ASP A 423 ? 0.3569 0.3380 0.2168 -0.0701 0.0597  0.0128  422  ASP A O   
3414 C  CB  . ASP A 423 ? 0.2427 0.3698 0.2936 -0.1701 -0.0299 0.0348  422  ASP A CB  
3415 C  CG  . ASP A 423 ? 0.3469 0.4250 0.3333 -0.1711 -0.0643 0.0699  422  ASP A CG  
3416 O  OD1 . ASP A 423 ? 0.4320 0.4071 0.3571 -0.1391 -0.1097 0.1550  422  ASP A OD1 
3417 O  OD2 . ASP A 423 ? 0.4466 0.4684 0.3566 -0.1295 -0.0283 0.0402  422  ASP A OD2 
3418 N  N   . PHE A 424 ? 0.2152 0.3550 0.2105 -0.0040 0.0342  0.0364  423  PHE A N   
3419 C  CA  . PHE A 424 ? 0.1355 0.3722 0.2251 -0.0191 0.0066  0.0498  423  PHE A CA  
3420 C  C   . PHE A 424 ? 0.1717 0.3925 0.2358 0.0060  0.0622  0.0616  423  PHE A C   
3421 O  O   . PHE A 424 ? 0.2899 0.3936 0.2747 -0.0422 0.0922  0.1085  423  PHE A O   
3422 C  CB  . PHE A 424 ? 0.1451 0.3831 0.2388 -0.0351 -0.0162 0.0577  423  PHE A CB  
3423 C  CG  . PHE A 424 ? 0.1774 0.3708 0.2359 -0.0101 -0.0306 0.0389  423  PHE A CG  
3424 C  CD1 . PHE A 424 ? 0.2147 0.3436 0.2356 -0.0467 -0.0723 0.0279  423  PHE A CD1 
3425 C  CD2 . PHE A 424 ? 0.1051 0.3412 0.2242 0.0018  -0.0493 0.0272  423  PHE A CD2 
3426 C  CE1 . PHE A 424 ? 0.1702 0.3369 0.2441 -0.0652 -0.0856 0.0369  423  PHE A CE1 
3427 C  CE2 . PHE A 424 ? 0.1183 0.3575 0.2183 -0.0398 -0.0236 0.0221  423  PHE A CE2 
3428 C  CZ  . PHE A 424 ? 0.2260 0.3467 0.2423 -0.0371 -0.1043 0.0377  423  PHE A CZ  
3429 N  N   . GLU A 425 ? 0.2139 0.4026 0.2221 -0.0395 0.0334  0.0363  424  GLU A N   
3430 C  CA  . GLU A 425 ? 0.1862 0.4331 0.2352 0.0035  0.0015  0.0057  424  GLU A CA  
3431 C  C   . GLU A 425 ? 0.1358 0.4207 0.2137 0.0074  0.0417  0.0210  424  GLU A C   
3432 O  O   . GLU A 425 ? 0.1372 0.4404 0.2249 -0.0255 0.0360  0.0239  424  GLU A O   
3433 C  CB  . GLU A 425 ? 0.1973 0.4842 0.2841 -0.0062 0.0155  -0.0132 424  GLU A CB  
3434 C  CG  . GLU A 425 ? 0.2895 0.5384 0.3254 0.0028  -0.0442 -0.0199 424  GLU A CG  
3435 C  CD  . GLU A 425 ? 0.2782 0.5798 0.3774 0.0248  -0.0693 -0.0458 424  GLU A CD  
3436 O  OE1 . GLU A 425 ? 0.2430 0.5908 0.3596 0.0063  -0.0631 -0.0595 424  GLU A OE1 
3437 O  OE2 . GLU A 425 ? 0.2679 0.6104 0.4259 0.0545  -0.1035 -0.0362 424  GLU A OE2 
3438 N  N   . ASP A 426 ? 0.2169 0.4246 0.1826 0.0302  0.0137  0.0268  425  ASP A N   
3439 C  CA  . ASP A 426 ? 0.1799 0.4301 0.1774 0.0243  0.0490  0.0273  425  ASP A CA  
3440 C  C   . ASP A 426 ? 0.1362 0.4717 0.1903 0.0439  0.0292  0.0582  425  ASP A C   
3441 O  O   . ASP A 426 ? 0.1481 0.5002 0.2132 0.0504  0.0343  0.0820  425  ASP A O   
3442 C  CB  . ASP A 426 ? 0.2106 0.4169 0.1699 0.0315  0.0368  0.0129  425  ASP A CB  
3443 C  CG  . ASP A 426 ? 0.1828 0.4338 0.1699 0.0472  0.0149  0.0196  425  ASP A CG  
3444 O  OD1 . ASP A 426 ? 0.1741 0.4566 0.1927 0.0322  -0.0209 0.0384  425  ASP A OD1 
3445 O  OD2 . ASP A 426 ? 0.2340 0.4506 0.1688 0.0544  -0.0344 0.0199  425  ASP A OD2 
3446 N  N   . HIS A 427 ? 0.1417 0.4966 0.2101 0.0045  -0.0090 0.0555  426  HIS A N   
3447 C  CA  . HIS A 427 ? 0.1463 0.4864 0.2200 0.0310  -0.0372 0.0499  426  HIS A CA  
3448 C  C   . HIS A 427 ? 0.1938 0.5289 0.2279 0.0542  -0.0555 0.0608  426  HIS A C   
3449 O  O   . HIS A 427 ? 0.1974 0.5717 0.2402 0.0456  -0.0551 0.0638  426  HIS A O   
3450 C  CB  . HIS A 427 ? 0.1488 0.4771 0.2207 0.0453  -0.0240 0.0234  426  HIS A CB  
3451 C  CG  . HIS A 427 ? 0.1918 0.4516 0.2146 0.0399  -0.0153 0.0336  426  HIS A CG  
3452 N  ND1 . HIS A 427 ? 0.1686 0.4303 0.2175 0.0641  -0.0087 0.0322  426  HIS A ND1 
3453 C  CD2 . HIS A 427 ? 0.2032 0.4511 0.2180 0.0686  -0.0465 0.0236  426  HIS A CD2 
3454 C  CE1 . HIS A 427 ? 0.1907 0.4384 0.2220 0.0557  -0.0113 0.0192  426  HIS A CE1 
3455 N  NE2 . HIS A 427 ? 0.1893 0.4492 0.2138 0.0573  -0.0452 0.0111  426  HIS A NE2 
3456 N  N   . THR A 428 ? 0.1803 0.5624 0.2191 0.0233  -0.0153 0.0590  427  THR A N   
3457 C  CA  . THR A 428 ? 0.1620 0.5491 0.2064 0.0459  0.0268  0.0555  427  THR A CA  
3458 C  C   . THR A 428 ? 0.1638 0.5457 0.2074 0.0396  0.0237  0.0539  427  THR A C   
3459 O  O   . THR A 428 ? 0.1724 0.5315 0.2148 0.0754  0.0228  0.0481  427  THR A O   
3460 C  CB  . THR A 428 ? 0.1915 0.5496 0.2077 0.0334  0.0019  0.0364  427  THR A CB  
3461 O  OG1 . THR A 428 ? 0.1437 0.5379 0.2198 0.0506  0.0067  0.0390  427  THR A OG1 
3462 C  CG2 . THR A 428 ? 0.2440 0.5360 0.1795 0.0426  0.0416  -0.0011 427  THR A CG2 
3463 N  N   . ASN A 429 ? 0.1477 0.5321 0.2050 0.0290  -0.0210 0.0538  428  ASN A N   
3464 C  CA  . ASN A 429 ? 0.1433 0.5269 0.2027 0.0379  0.0232  0.0339  428  ASN A CA  
3465 C  C   . ASN A 429 ? 0.1478 0.4984 0.2102 0.0246  0.0097  0.0381  428  ASN A C   
3466 O  O   . ASN A 429 ? 0.2147 0.5002 0.2393 0.0490  -0.0004 0.0147  428  ASN A O   
3467 C  CB  . ASN A 429 ? 0.1482 0.5448 0.2246 0.0360  0.0270  0.0392  428  ASN A CB  
3468 C  CG  . ASN A 429 ? 0.1785 0.5976 0.2773 0.0349  0.0576  0.0111  428  ASN A CG  
3469 O  OD1 . ASN A 429 ? 0.2261 0.6394 0.3038 0.0402  0.0641  0.0095  428  ASN A OD1 
3470 N  ND2 . ASN A 429 ? 0.1871 0.5850 0.2860 -0.0050 0.0755  -0.0066 428  ASN A ND2 
3471 N  N   . TYR A 430 ? 0.1131 0.4293 0.1995 0.0194  0.0124  0.0563  429  TYR A N   
3472 C  CA  . TYR A 430 ? 0.1205 0.4223 0.1962 0.0513  0.0214  0.0297  429  TYR A CA  
3473 C  C   . TYR A 430 ? 0.1575 0.4375 0.2241 0.0709  0.0261  -0.0040 429  TYR A C   
3474 O  O   . TYR A 430 ? 0.2098 0.4441 0.2443 0.0619  0.0129  -0.0167 429  TYR A O   
3475 C  CB  . TYR A 430 ? 0.1187 0.3829 0.1900 0.0679  0.0176  0.0299  429  TYR A CB  
3476 C  CG  . TYR A 430 ? 0.1017 0.3377 0.1838 0.0543  -0.0005 0.0356  429  TYR A CG  
3477 C  CD1 . TYR A 430 ? 0.1355 0.3283 0.1765 0.0975  0.0061  0.0258  429  TYR A CD1 
3478 C  CD2 . TYR A 430 ? 0.1318 0.3540 0.1850 0.0782  -0.0337 0.0038  429  TYR A CD2 
3479 C  CE1 . TYR A 430 ? 0.1211 0.3110 0.1671 0.0382  -0.0313 -0.0007 429  TYR A CE1 
3480 C  CE2 . TYR A 430 ? 0.1300 0.3371 0.1936 0.0067  -0.0176 0.0032  429  TYR A CE2 
3481 C  CZ  . TYR A 430 ? 0.1181 0.3379 0.1990 0.0604  -0.0415 -0.0052 429  TYR A CZ  
3482 O  OH  . TYR A 430 ? 0.1547 0.3386 0.1944 0.1000  -0.0494 -0.0316 429  TYR A OH  
3483 N  N   . GLU A 431 ? 0.1537 0.4335 0.2490 0.0913  0.0160  -0.0282 430  GLU A N   
3484 C  CA  . GLU A 431 ? 0.2253 0.4518 0.2703 0.0998  0.0102  -0.0325 430  GLU A CA  
3485 C  C   . GLU A 431 ? 0.1369 0.4254 0.2435 0.0466  -0.0069 -0.0055 430  GLU A C   
3486 O  O   . GLU A 431 ? 0.1853 0.4535 0.2406 0.0706  -0.0011 -0.0088 430  GLU A O   
3487 C  CB  . GLU A 431 ? 0.2748 0.4894 0.3165 0.0979  0.0189  -0.0677 430  GLU A CB  
3488 C  CG  . GLU A 431 ? 0.3779 0.5364 0.3981 0.0963  0.0120  -0.1054 430  GLU A CG  
3489 C  CD  . GLU A 431 ? 0.5791 0.6028 0.4757 0.0623  -0.0207 -0.1070 430  GLU A CD  
3490 O  OE1 . GLU A 431 ? 0.6115 0.6278 0.5057 0.0896  -0.0186 -0.0794 430  GLU A OE1 
3491 O  OE2 . GLU A 431 ? 0.6933 0.6299 0.5208 0.0547  0.0105  -0.1217 430  GLU A OE2 
3492 N  N   . LEU A 432 ? 0.1039 0.3757 0.2237 0.0272  -0.0219 0.0212  431  LEU A N   
3493 C  CA  . LEU A 432 ? 0.1414 0.3543 0.1960 0.0450  -0.0448 0.0429  431  LEU A CA  
3494 C  C   . LEU A 432 ? 0.1430 0.3612 0.2212 0.0518  -0.0019 0.0455  431  LEU A C   
3495 O  O   . LEU A 432 ? 0.2272 0.3483 0.2707 0.1046  -0.0064 0.0508  431  LEU A O   
3496 C  CB  . LEU A 432 ? 0.1252 0.3229 0.2025 0.0649  -0.0366 0.0388  431  LEU A CB  
3497 C  CG  . LEU A 432 ? 0.1762 0.3081 0.1846 0.1109  -0.0371 0.0221  431  LEU A CG  
3498 C  CD1 . LEU A 432 ? 0.1714 0.3227 0.2258 0.1268  -0.0023 0.0133  431  LEU A CD1 
3499 C  CD2 . LEU A 432 ? 0.2670 0.3051 0.1821 0.0954  -0.0200 0.0737  431  LEU A CD2 
3500 N  N   . ASP A 433 ? 0.1311 0.3554 0.2011 0.0298  0.0074  0.0592  432  ASP A N   
3501 C  CA  . ASP A 433 ? 0.1413 0.3519 0.2082 0.0810  -0.0263 0.0521  432  ASP A CA  
3502 C  C   . ASP A 433 ? 0.1516 0.3732 0.2042 0.0714  -0.0214 0.0494  432  ASP A C   
3503 O  O   . ASP A 433 ? 0.1870 0.4006 0.2051 0.0888  -0.0164 0.0573  432  ASP A O   
3504 C  CB  . ASP A 433 ? 0.2942 0.3630 0.2474 0.1118  -0.0637 0.0613  432  ASP A CB  
3505 C  CG  . ASP A 433 ? 0.3931 0.3673 0.2679 0.1208  -0.0863 0.0765  432  ASP A CG  
3506 O  OD1 . ASP A 433 ? 0.4336 0.3792 0.2723 0.0996  -0.0335 0.0462  432  ASP A OD1 
3507 O  OD2 . ASP A 433 ? 0.4780 0.3834 0.3170 0.1038  -0.1228 0.0714  432  ASP A OD2 
3508 N  N   . ILE A 434 ? 0.1180 0.3236 0.1703 0.0329  -0.0038 0.0469  433  ILE A N   
3509 C  CA  . ILE A 434 ? 0.0955 0.2817 0.1741 0.0559  0.0002  0.0419  433  ILE A CA  
3510 C  C   . ILE A 434 ? 0.1366 0.2559 0.1735 0.0823  0.0248  0.0173  433  ILE A C   
3511 O  O   . ILE A 434 ? 0.2135 0.2377 0.1901 0.0894  0.0032  0.0258  433  ILE A O   
3512 C  CB  . ILE A 434 ? 0.1441 0.3042 0.1884 0.0424  0.0091  0.0491  433  ILE A CB  
3513 C  CG1 . ILE A 434 ? 0.2022 0.3201 0.1630 0.0707  -0.0115 0.0617  433  ILE A CG1 
3514 C  CG2 . ILE A 434 ? 0.1221 0.2886 0.1798 0.0638  0.0165  0.0471  433  ILE A CG2 
3515 C  CD1 . ILE A 434 ? 0.2283 0.3618 0.1321 0.0690  -0.0107 0.0419  433  ILE A CD1 
3516 N  N   . LYS A 435 ? 0.1515 0.2480 0.1266 0.0389  0.0283  0.0132  434  LYS A N   
3517 C  CA  . LYS A 435 ? 0.1881 0.2450 0.1192 0.0036  -0.0095 0.0458  434  LYS A CA  
3518 C  C   . LYS A 435 ? 0.2317 0.2382 0.1419 0.0333  -0.0153 0.0421  434  LYS A C   
3519 O  O   . LYS A 435 ? 0.2348 0.2244 0.1686 0.0742  -0.0183 0.0403  434  LYS A O   
3520 C  CB  . LYS A 435 ? 0.2289 0.2722 0.1259 -0.0346 -0.0040 0.0656  434  LYS A CB  
3521 C  CG  . LYS A 435 ? 0.2027 0.3091 0.1222 -0.0325 -0.0458 0.0727  434  LYS A CG  
3522 C  CD  . LYS A 435 ? 0.3436 0.3361 0.1837 0.0178  -0.0207 0.0352  434  LYS A CD  
3523 C  CE  . LYS A 435 ? 0.4237 0.3319 0.2410 0.0671  -0.0333 0.0249  434  LYS A CE  
3524 N  NZ  . LYS A 435 ? 0.5514 0.3726 0.2858 0.0749  -0.0216 0.0046  434  LYS A NZ  
3525 N  N   . GLU A 436 ? 0.2155 0.2444 0.1252 0.0530  -0.0265 0.0351  435  GLU A N   
3526 C  CA  . GLU A 436 ? 0.1925 0.2464 0.1262 0.0510  0.0053  0.0029  435  GLU A CA  
3527 C  C   . GLU A 436 ? 0.1814 0.2273 0.1456 0.0914  0.0461  0.0318  435  GLU A C   
3528 O  O   . GLU A 436 ? 0.1973 0.2179 0.1786 0.0388  0.0351  0.0567  435  GLU A O   
3529 C  CB  . GLU A 436 ? 0.2248 0.2413 0.1031 0.0420  -0.0125 -0.0250 435  GLU A CB  
3530 C  CG  . GLU A 436 ? 0.2422 0.2546 0.1241 0.0482  0.0302  -0.0151 435  GLU A CG  
3531 C  CD  . GLU A 436 ? 0.2251 0.2348 0.1587 0.0503  0.0101  0.0156  435  GLU A CD  
3532 O  OE1 . GLU A 436 ? 0.1941 0.2461 0.1631 0.0180  -0.0246 -0.0111 435  GLU A OE1 
3533 O  OE2 . GLU A 436 ? 0.1961 0.2197 0.1858 0.0528  0.0211  0.0446  435  GLU A OE2 
3534 N  N   . THR A 437 ? 0.1759 0.2552 0.1642 0.0471  0.0435  0.0233  436  THR A N   
3535 C  CA  . THR A 437 ? 0.1875 0.2673 0.1622 0.0957  0.0471  0.0287  436  THR A CA  
3536 C  C   . THR A 437 ? 0.1784 0.2401 0.1611 0.1172  0.0416  0.0445  436  THR A C   
3537 O  O   . THR A 437 ? 0.2348 0.2449 0.1854 0.0853  0.1044  0.0229  436  THR A O   
3538 C  CB  . THR A 437 ? 0.2318 0.2920 0.1806 0.0936  -0.0052 0.0433  436  THR A CB  
3539 O  OG1 . THR A 437 ? 0.2897 0.3266 0.2072 0.0482  0.0434  0.0293  436  THR A OG1 
3540 C  CG2 . THR A 437 ? 0.2413 0.2930 0.1716 0.1080  -0.0409 0.0575  436  THR A CG2 
3541 N  N   . LEU A 438 ? 0.1991 0.1996 0.1464 0.0849  0.0520  0.0779  437  LEU A N   
3542 C  CA  . LEU A 438 ? 0.1858 0.2023 0.1567 -0.0007 0.0622  0.0611  437  LEU A CA  
3543 C  C   . LEU A 438 ? 0.3036 0.2124 0.1595 -0.0629 0.0516  0.0654  437  LEU A C   
3544 O  O   . LEU A 438 ? 0.2534 0.2274 0.2032 -0.0056 0.0360  0.0357  437  LEU A O   
3545 C  CB  . LEU A 438 ? 0.1609 0.2434 0.1997 -0.0263 0.0626  0.0818  437  LEU A CB  
3546 C  CG  . LEU A 438 ? 0.1873 0.2734 0.2318 0.0506  0.0574  0.0179  437  LEU A CG  
3547 C  CD1 . LEU A 438 ? 0.2313 0.3213 0.2212 -0.0374 0.0675  0.0217  437  LEU A CD1 
3548 C  CD2 . LEU A 438 ? 0.2680 0.1702 0.2619 0.0911  -0.0135 0.0177  437  LEU A CD2 
3549 N  N   . THR A 439 ? 0.3333 0.1816 0.1860 0.0255  0.0328  0.0279  438  THR A N   
3550 C  CA  . THR A 439 ? 0.1977 0.1957 0.1882 0.1133  0.0242  -0.0114 438  THR A CA  
3551 C  C   . THR A 439 ? 0.1693 0.2228 0.1935 0.0605  0.0134  -0.0087 438  THR A C   
3552 O  O   . THR A 439 ? 0.1991 0.2398 0.1924 0.0490  0.0105  0.0243  438  THR A O   
3553 C  CB  . THR A 439 ? 0.1686 0.2266 0.1844 0.1138  0.0145  0.0235  438  THR A CB  
3554 O  OG1 . THR A 439 ? 0.2687 0.2317 0.1890 0.0474  0.0053  0.0471  438  THR A OG1 
3555 C  CG2 . THR A 439 ? 0.1705 0.2300 0.1766 0.1099  -0.0275 0.0092  438  THR A CG2 
3556 N  N   . LEU A 440 ? 0.1055 0.1944 0.1697 0.0416  0.0407  -0.0367 439  LEU A N   
3557 C  CA  . LEU A 440 ? 0.0953 0.2101 0.1521 0.0158  0.0440  -0.0205 439  LEU A CA  
3558 C  C   . LEU A 440 ? 0.1243 0.2264 0.1870 0.0468  -0.0320 0.0183  439  LEU A C   
3559 O  O   . LEU A 440 ? 0.1635 0.1843 0.1873 0.0506  0.0061  0.0174  439  LEU A O   
3560 C  CB  . LEU A 440 ? 0.1081 0.2308 0.1569 0.0207  0.0494  -0.0325 439  LEU A CB  
3561 C  CG  . LEU A 440 ? 0.2170 0.2225 0.1460 0.0418  0.0418  -0.0262 439  LEU A CG  
3562 C  CD1 . LEU A 440 ? 0.2151 0.2236 0.1565 0.0868  0.0415  0.0260  439  LEU A CD1 
3563 C  CD2 . LEU A 440 ? 0.2597 0.1964 0.1544 0.0331  0.0294  -0.0355 439  LEU A CD2 
3564 N  N   . LYS A 441 ? 0.1053 0.2477 0.1795 0.0082  0.0037  0.0243  440  LYS A N   
3565 C  CA  . LYS A 441 ? 0.1345 0.2557 0.1570 0.0441  0.0078  0.0518  440  LYS A CA  
3566 C  C   . LYS A 441 ? 0.1581 0.2664 0.1751 0.0299  -0.0003 0.0573  440  LYS A C   
3567 O  O   . LYS A 441 ? 0.2220 0.2643 0.1981 0.0447  0.0040  0.0458  440  LYS A O   
3568 C  CB  . LYS A 441 ? 0.2801 0.2857 0.1413 0.0199  0.0375  0.0299  440  LYS A CB  
3569 C  CG  . LYS A 441 ? 0.3906 0.3234 0.1452 0.0317  0.0441  0.0558  440  LYS A CG  
3570 C  CD  . LYS A 441 ? 0.3944 0.3928 0.1884 0.0242  0.0210  0.0148  440  LYS A CD  
3571 C  CE  . LYS A 441 ? 0.4073 0.4149 0.1882 0.0140  0.0317  0.0142  440  LYS A CE  
3572 N  NZ  . LYS A 441 ? 0.4217 0.4083 0.2263 -0.0529 -0.0094 0.0115  440  LYS A NZ  
3573 N  N   . PRO A 442 ? 0.1623 0.2798 0.1758 0.0702  0.0055  0.0774  441  PRO A N   
3574 C  CA  . PRO A 442 ? 0.1624 0.2709 0.1675 0.0598  -0.0059 0.0796  441  PRO A CA  
3575 C  C   . PRO A 442 ? 0.2504 0.2608 0.1845 0.0462  0.0161  0.0509  441  PRO A C   
3576 O  O   . PRO A 442 ? 0.2277 0.2787 0.1966 0.0185  -0.0202 0.0052  441  PRO A O   
3577 C  CB  . PRO A 442 ? 0.2035 0.3020 0.1909 0.0649  -0.0171 0.0706  441  PRO A CB  
3578 C  CG  . PRO A 442 ? 0.2036 0.2867 0.2052 0.0731  0.0002  0.0541  441  PRO A CG  
3579 C  CD  . PRO A 442 ? 0.1121 0.2645 0.2043 -0.0095 -0.0009 0.0504  441  PRO A CD  
3580 N  N   . GLU A 443 ? 0.2096 0.2601 0.1810 0.0412  -0.0060 0.0702  442  GLU A N   
3581 C  CA  . GLU A 443 ? 0.2318 0.2657 0.1890 0.0352  -0.0319 0.0644  442  GLU A CA  
3582 C  C   . GLU A 443 ? 0.1542 0.3050 0.1880 0.0574  -0.0404 0.0543  442  GLU A C   
3583 O  O   . GLU A 443 ? 0.1263 0.3378 0.1958 0.0619  0.0004  0.0270  442  GLU A O   
3584 C  CB  . GLU A 443 ? 0.2736 0.2856 0.2184 -0.0242 -0.0581 0.0624  442  GLU A CB  
3585 C  CG  . GLU A 443 ? 0.3953 0.3220 0.2511 -0.0224 -0.0565 0.0701  442  GLU A CG  
3586 C  CD  . GLU A 443 ? 0.5720 0.3494 0.2765 -0.0384 -0.0514 0.0845  442  GLU A CD  
3587 O  OE1 . GLU A 443 ? 0.5830 0.3499 0.2801 -0.0380 -0.0603 0.0476  442  GLU A OE1 
3588 O  OE2 . GLU A 443 ? 0.7369 0.3775 0.3181 -0.0775 -0.0570 0.0799  442  GLU A OE2 
3589 N  N   . GLY A 444 ? 0.1793 0.3134 0.1795 0.0958  -0.0241 0.0429  443  GLY A N   
3590 C  CA  . GLY A 444 ? 0.1754 0.3280 0.2023 0.0949  -0.0514 0.0378  443  GLY A CA  
3591 C  C   . GLY A 444 ? 0.2175 0.3563 0.1827 0.0423  -0.0304 0.0531  443  GLY A C   
3592 O  O   . GLY A 444 ? 0.2874 0.3530 0.1632 0.0085  -0.0403 0.0525  443  GLY A O   
3593 N  N   . PHE A 445 ? 0.2064 0.3357 0.1747 0.0265  -0.0023 0.0530  444  PHE A N   
3594 C  CA  . PHE A 445 ? 0.1891 0.3248 0.1597 -0.0106 0.0313  0.0325  444  PHE A CA  
3595 C  C   . PHE A 445 ? 0.1215 0.2974 0.1752 0.0207  0.0016  0.0169  444  PHE A C   
3596 O  O   . PHE A 445 ? 0.1585 0.2853 0.1829 0.0731  -0.0123 0.0108  444  PHE A O   
3597 C  CB  . PHE A 445 ? 0.1570 0.3485 0.1727 -0.0062 0.0575  0.0493  444  PHE A CB  
3598 C  CG  . PHE A 445 ? 0.1126 0.3541 0.1761 0.0217  0.0391  0.0582  444  PHE A CG  
3599 C  CD1 . PHE A 445 ? 0.1752 0.3978 0.1848 0.0347  0.0412  0.0716  444  PHE A CD1 
3600 C  CD2 . PHE A 445 ? 0.1649 0.3787 0.1869 0.0195  0.0409  0.0859  444  PHE A CD2 
3601 C  CE1 . PHE A 445 ? 0.1887 0.4029 0.1912 0.0855  0.0184  0.0874  444  PHE A CE1 
3602 C  CE2 . PHE A 445 ? 0.1754 0.3902 0.1700 0.0906  0.0318  0.1103  444  PHE A CE2 
3603 C  CZ  . PHE A 445 ? 0.1760 0.4039 0.1817 0.0893  0.0184  0.1019  444  PHE A CZ  
3604 N  N   . VAL A 446 ? 0.1668 0.2718 0.1950 -0.0150 -0.0381 0.0259  445  VAL A N   
3605 C  CA  . VAL A 446 ? 0.1383 0.3081 0.2014 -0.0177 -0.0216 0.0255  445  VAL A CA  
3606 C  C   . VAL A 446 ? 0.1176 0.3415 0.2060 -0.0341 -0.0331 0.0234  445  VAL A C   
3607 O  O   . VAL A 446 ? 0.1295 0.3907 0.2294 -0.0205 0.0337  0.0217  445  VAL A O   
3608 C  CB  . VAL A 446 ? 0.0867 0.2889 0.2194 0.0459  -0.0111 0.0170  445  VAL A CB  
3609 C  CG1 . VAL A 446 ? 0.1175 0.2765 0.2316 0.0061  0.0168  0.0225  445  VAL A CG1 
3610 C  CG2 . VAL A 446 ? 0.1373 0.2982 0.2435 0.0411  -0.0423 0.0080  445  VAL A CG2 
3611 N  N   . VAL A 447 ? 0.1818 0.3336 0.1841 0.0005  -0.0430 0.0087  446  VAL A N   
3612 C  CA  . VAL A 447 ? 0.1628 0.3430 0.1672 -0.0074 -0.0551 0.0281  446  VAL A CA  
3613 C  C   . VAL A 447 ? 0.1347 0.3769 0.1651 -0.0449 -0.0372 0.0459  446  VAL A C   
3614 O  O   . VAL A 447 ? 0.1460 0.4022 0.1669 -0.0441 -0.0080 0.0380  446  VAL A O   
3615 C  CB  . VAL A 447 ? 0.1207 0.3528 0.1523 -0.0383 0.0093  0.0332  446  VAL A CB  
3616 C  CG1 . VAL A 447 ? 0.2377 0.3467 0.1350 0.0147  -0.0207 0.0479  446  VAL A CG1 
3617 C  CG2 . VAL A 447 ? 0.1368 0.3489 0.1691 -0.0558 -0.0304 0.0044  446  VAL A CG2 
3618 N  N   . LYS A 448 ? 0.1186 0.3761 0.1665 -0.0058 -0.0023 0.0542  447  LYS A N   
3619 C  CA  . LYS A 448 ? 0.1523 0.3700 0.1857 0.0433  -0.0255 0.0337  447  LYS A CA  
3620 C  C   . LYS A 448 ? 0.2883 0.3769 0.1836 0.0101  0.0221  0.0236  447  LYS A C   
3621 O  O   . LYS A 448 ? 0.3242 0.3757 0.1980 -0.0366 0.0195  0.0277  447  LYS A O   
3622 C  CB  . LYS A 448 ? 0.1566 0.4209 0.2271 0.0395  0.0042  0.0519  447  LYS A CB  
3623 C  CG  . LYS A 448 ? 0.2135 0.4454 0.2577 0.0607  -0.0719 0.0727  447  LYS A CG  
3624 C  CD  . LYS A 448 ? 0.3380 0.4925 0.3039 0.0684  -0.1164 0.0932  447  LYS A CD  
3625 C  CE  . LYS A 448 ? 0.4296 0.5482 0.3598 0.0838  -0.1787 0.0782  447  LYS A CE  
3626 N  NZ  . LYS A 448 ? 0.5131 0.5772 0.3866 0.0765  -0.1618 0.0758  447  LYS A NZ  
3627 N  N   . ALA A 449 ? 0.2432 0.3468 0.1708 0.0283  -0.0297 -0.0067 448  ALA A N   
3628 C  CA  . ALA A 449 ? 0.3093 0.3784 0.1997 -0.0077 -0.0029 -0.0005 448  ALA A CA  
3629 C  C   . ALA A 449 ? 0.4138 0.4012 0.2355 -0.0148 -0.0232 0.0191  448  ALA A C   
3630 O  O   . ALA A 449 ? 0.6068 0.4200 0.2513 -0.0695 -0.0620 0.0296  448  ALA A O   
3631 C  CB  . ALA A 449 ? 0.2900 0.3683 0.2015 0.0103  0.0746  -0.0059 448  ALA A CB  
3632 N  N   . LYS A 450 ? 0.2123 0.4177 0.2778 -0.0121 -0.0151 0.0103  449  LYS A N   
3633 C  CA  . LYS A 450 ? 0.1968 0.4644 0.3183 -0.0201 -0.0577 0.0249  449  LYS A CA  
3634 C  C   . LYS A 450 ? 0.2352 0.4203 0.2909 -0.0729 -0.0975 0.0090  449  LYS A C   
3635 O  O   . LYS A 450 ? 0.2531 0.3840 0.2958 -0.0738 -0.1427 0.0346  449  LYS A O   
3636 C  CB  . LYS A 450 ? 0.3299 0.5436 0.3818 -0.0188 -0.0472 0.0516  449  LYS A CB  
3637 C  CG  . LYS A 450 ? 0.5655 0.6020 0.4309 0.0632  -0.0674 0.0976  449  LYS A CG  
3638 C  CD  . LYS A 450 ? 0.7072 0.6386 0.4779 0.1006  -0.0712 0.1180  449  LYS A CD  
3639 C  CE  . LYS A 450 ? 0.8028 0.6571 0.5014 0.1204  -0.0893 0.1279  449  LYS A CE  
3640 N  NZ  . LYS A 450 ? 0.8735 0.6667 0.5090 0.1387  -0.0798 0.1390  449  LYS A NZ  
3641 N  N   . SER A 451 ? 0.2506 0.4127 0.2686 -0.0250 -0.0534 0.0144  450  SER A N   
3642 C  CA  . SER A 451 ? 0.2119 0.4258 0.2495 -0.0649 -0.0513 0.0204  450  SER A CA  
3643 C  C   . SER A 451 ? 0.1816 0.3883 0.2610 -0.0543 -0.1054 0.0210  450  SER A C   
3644 O  O   . SER A 451 ? 0.2460 0.4460 0.2785 -0.1020 -0.1126 0.0388  450  SER A O   
3645 C  CB  . SER A 451 ? 0.3036 0.4388 0.2183 -0.1210 -0.0177 0.0004  450  SER A CB  
3646 O  OG  . SER A 451 ? 0.4167 0.4731 0.2240 -0.1498 -0.0368 0.0064  450  SER A OG  
3647 N  N   . LYS A 452 ? 0.2716 0.3818 0.2742 -0.1509 -0.0741 0.0125  451  LYS A N   
3648 C  CA  . LYS A 452 ? 0.3104 0.3891 0.2845 -0.1604 -0.0722 0.0262  451  LYS A CA  
3649 C  C   . LYS A 452 ? 0.3423 0.3697 0.3381 -0.1314 -0.0664 -0.0218 451  LYS A C   
3650 O  O   . LYS A 452 ? 0.3572 0.3878 0.3738 -0.1629 -0.0437 0.0099  451  LYS A O   
3651 C  CB  . LYS A 452 ? 0.3851 0.3969 0.2811 -0.1461 -0.0653 0.0695  451  LYS A CB  
3652 C  CG  . LYS A 452 ? 0.3339 0.4212 0.2638 -0.1292 -0.0819 0.0888  451  LYS A CG  
3653 C  CD  . LYS A 452 ? 0.3229 0.4563 0.2855 -0.1157 -0.0580 0.0736  451  LYS A CD  
3654 C  CE  . LYS A 452 ? 0.3264 0.4785 0.3203 -0.1192 -0.0180 0.0409  451  LYS A CE  
3655 N  NZ  . LYS A 452 ? 0.4123 0.4871 0.3593 -0.1050 -0.0440 0.0292  451  LYS A NZ  
3656 N  N   . LYS A 453 ? 0.3031 0.3885 0.3206 -0.0808 -0.0681 -0.0539 452  LYS A N   
3657 C  CA  . LYS A 453 ? 0.3604 0.4272 0.3342 -0.0891 -0.1534 -0.0616 452  LYS A CA  
3658 C  C   . LYS A 453 ? 0.4070 0.4173 0.3196 -0.1600 -0.1230 -0.0447 452  LYS A C   
3659 O  O   . LYS A 453 ? 0.4466 0.4246 0.3514 -0.1845 -0.0960 -0.0419 452  LYS A O   
3660 C  CB  . LYS A 453 ? 0.3806 0.4607 0.3641 -0.0582 -0.1752 -0.0663 452  LYS A CB  
3661 C  CG  . LYS A 453 ? 0.4306 0.4875 0.3996 -0.0167 -0.1750 -0.0804 452  LYS A CG  
3662 C  CD  . LYS A 453 ? 0.5809 0.5056 0.4292 0.0168  -0.1155 -0.0971 452  LYS A CD  
3663 C  CE  . LYS A 453 ? 0.7325 0.5297 0.4574 0.0566  -0.0762 -0.1076 452  LYS A CE  
3664 N  NZ  . LYS A 453 ? 0.7830 0.5488 0.4766 0.0581  -0.0647 -0.1201 452  LYS A NZ  
3665 N  N   . ILE A 454 ? 0.3523 0.4042 0.2747 -0.1430 -0.0775 0.0051  453  ILE A N   
3666 C  CA  . ILE A 454 ? 0.3606 0.3892 0.2477 -0.1338 -0.0877 -0.0137 453  ILE A CA  
3667 C  C   . ILE A 454 ? 0.4167 0.3688 0.2551 -0.1102 -0.0904 -0.0417 453  ILE A C   
3668 O  O   . ILE A 454 ? 0.4018 0.3169 0.2344 -0.1100 -0.0932 -0.0539 453  ILE A O   
3669 C  CB  . ILE A 454 ? 0.3935 0.4041 0.2369 -0.0925 -0.0653 0.0084  453  ILE A CB  
3670 C  CG1 . ILE A 454 ? 0.3447 0.4036 0.2080 -0.1124 -0.0139 -0.0059 453  ILE A CG1 
3671 C  CG2 . ILE A 454 ? 0.2944 0.4033 0.2416 -0.0399 -0.0889 0.0246  453  ILE A CG2 
3672 C  CD1 . ILE A 454 ? 0.3177 0.4061 0.1920 -0.1196 0.0186  -0.0052 453  ILE A CD1 
3673 N  N   . PRO A 455 ? 0.4963 0.3944 0.2844 -0.1462 -0.0436 -0.0685 454  PRO A N   
3674 C  CA  . PRO A 455 ? 0.5024 0.4144 0.3095 -0.1381 -0.0132 -0.0912 454  PRO A CA  
3675 C  C   . PRO A 455 ? 0.4800 0.4202 0.3255 -0.1172 0.0261  -0.0839 454  PRO A C   
3676 O  O   . PRO A 455 ? 0.4870 0.4203 0.3445 -0.1066 0.0800  -0.0762 454  PRO A O   
3677 C  CB  . PRO A 455 ? 0.5566 0.4190 0.3226 -0.1777 -0.0173 -0.1328 454  PRO A CB  
3678 C  CG  . PRO A 455 ? 0.5826 0.4111 0.3259 -0.2190 0.0055  -0.1164 454  PRO A CG  
3679 C  CD  . PRO A 455 ? 0.5596 0.4035 0.2901 -0.1848 -0.0342 -0.1130 454  PRO A CD  
3680 N  N   . LEU A 456 ? 0.4864 0.4107 0.3403 -0.1082 -0.0156 -0.0734 455  LEU A N   
3681 C  CA  . LEU A 456 ? 0.5328 0.4020 0.3546 -0.1104 -0.0315 -0.0602 455  LEU A CA  
3682 C  C   . LEU A 456 ? 0.6926 0.4061 0.3619 -0.1011 -0.0370 -0.0457 455  LEU A C   
3683 O  O   . LEU A 456 ? 0.7878 0.4059 0.3647 -0.0763 -0.0429 -0.0482 455  LEU A O   
3684 C  CB  . LEU A 456 ? 0.4182 0.3981 0.3410 -0.1309 -0.0635 -0.0485 455  LEU A CB  
3685 C  CG  . LEU A 456 ? 0.3247 0.3988 0.3142 -0.0947 -0.0534 -0.0247 455  LEU A CG  
3686 C  CD1 . LEU A 456 ? 0.3906 0.3935 0.3269 -0.0932 0.0095  -0.0266 455  LEU A CD1 
3687 C  CD2 . LEU A 456 ? 0.2471 0.4092 0.2942 -0.0549 -0.1077 0.0220  455  LEU A CD2 
3688 O  OXT . LEU A 456 ? 0.6816 0.3922 0.3586 -0.0722 -0.0069 -0.0164 455  LEU A OXT 
3689 N  N   . THR B 2   ? 0.9797 0.7897 0.6885 -0.1510 0.0910  0.0750  1    THR B N   
3690 C  CA  . THR B 2   ? 0.9680 0.7999 0.6940 -0.1480 0.0756  0.0530  1    THR B CA  
3691 C  C   . THR B 2   ? 0.8797 0.7780 0.6612 -0.1554 0.0712  0.0568  1    THR B C   
3692 O  O   . THR B 2   ? 0.8388 0.7583 0.6582 -0.1728 0.0854  0.0740  1    THR B O   
3693 C  CB  . THR B 2   ? 1.0162 0.8236 0.7233 -0.1481 0.0504  0.0314  1    THR B CB  
3694 O  OG1 . THR B 2   ? 1.0475 0.8478 0.7421 -0.1636 0.0607  0.0221  1    THR B OG1 
3695 C  CG2 . THR B 2   ? 0.9981 0.8259 0.7285 -0.1319 0.0156  0.0215  1    THR B CG2 
3696 N  N   . ILE B 3   ? 0.8087 0.7728 0.6312 -0.1344 0.0391  0.0622  2    ILE B N   
3697 C  CA  . ILE B 3   ? 0.7395 0.7619 0.5988 -0.0939 0.0336  0.0701  2    ILE B CA  
3698 C  C   . ILE B 3   ? 0.8121 0.7495 0.5519 -0.0384 0.0291  0.0740  2    ILE B C   
3699 O  O   . ILE B 3   ? 0.8539 0.7432 0.5189 -0.0582 0.0689  0.1040  2    ILE B O   
3700 C  CB  . ILE B 3   ? 0.6401 0.7705 0.6103 -0.1059 0.0296  0.0851  2    ILE B CB  
3701 C  CG1 . ILE B 3   ? 0.6191 0.7899 0.6081 -0.0803 0.0003  0.0878  2    ILE B CG1 
3702 C  CG2 . ILE B 3   ? 0.5904 0.7588 0.6166 -0.1271 0.0508  0.0923  2    ILE B CG2 
3703 C  CD1 . ILE B 3   ? 0.6039 0.8019 0.6110 -0.0836 -0.0164 0.0992  2    ILE B CD1 
3704 N  N   . LYS B 4   ? 0.7740 0.7317 0.5110 0.0139  -0.0028 0.0590  3    LYS B N   
3705 C  CA  . LYS B 4   ? 0.7484 0.7021 0.4884 0.0515  -0.0163 0.0272  3    LYS B CA  
3706 C  C   . LYS B 4   ? 0.7134 0.6505 0.4414 0.0908  -0.0133 0.0094  3    LYS B C   
3707 O  O   . LYS B 4   ? 0.7437 0.6534 0.4218 0.1441  -0.0065 -0.0057 3    LYS B O   
3708 C  CB  . LYS B 4   ? 0.7506 0.7228 0.5083 0.0616  -0.0366 0.0292  3    LYS B CB  
3709 C  CG  . LYS B 4   ? 0.7049 0.7404 0.5305 0.0651  -0.0383 0.0315  3    LYS B CG  
3710 C  CD  . LYS B 4   ? 0.6864 0.7554 0.5480 0.0471  -0.0701 0.0303  3    LYS B CD  
3711 C  CE  . LYS B 4   ? 0.6337 0.7648 0.5674 0.0470  -0.0776 0.0180  3    LYS B CE  
3712 N  NZ  . LYS B 4   ? 0.5621 0.7758 0.5795 0.0659  -0.1125 0.0133  3    LYS B NZ  
3713 N  N   . GLU B 5   ? 0.6908 0.5949 0.4136 0.0955  -0.0182 0.0164  4    GLU B N   
3714 C  CA  . GLU B 5   ? 0.6317 0.5425 0.4070 0.0976  0.0051  0.0300  4    GLU B CA  
3715 C  C   . GLU B 5   ? 0.4629 0.4840 0.3258 0.0911  0.0053  0.0519  4    GLU B C   
3716 O  O   . GLU B 5   ? 0.4301 0.4943 0.2982 0.0891  0.0373  0.0930  4    GLU B O   
3717 C  CB  . GLU B 5   ? 0.7389 0.5666 0.4877 0.0850  0.0206  0.0137  4    GLU B CB  
3718 C  CG  . GLU B 5   ? 0.8174 0.5960 0.5667 0.0833  0.0470  -0.0045 4    GLU B CG  
3719 C  CD  . GLU B 5   ? 0.9261 0.6361 0.6314 0.0999  0.0814  -0.0188 4    GLU B CD  
3720 O  OE1 . GLU B 5   ? 0.9661 0.6694 0.6660 0.0766  0.0911  -0.0163 4    GLU B OE1 
3721 O  OE2 . GLU B 5   ? 0.9672 0.6230 0.6418 0.1263  0.0792  -0.0224 4    GLU B OE2 
3722 N  N   . MET B 6   ? 0.3737 0.4187 0.2911 0.0436  -0.0228 0.0351  5    MET B N   
3723 C  CA  . MET B 6   ? 0.3379 0.3406 0.2687 -0.0636 0.0203  0.0339  5    MET B CA  
3724 C  C   . MET B 6   ? 0.2606 0.2410 0.2390 -0.0417 0.0264  0.0443  5    MET B C   
3725 O  O   . MET B 6   ? 0.3628 0.2194 0.2469 0.0256  0.0761  0.0458  5    MET B O   
3726 C  CB  . MET B 6   ? 0.3593 0.3767 0.3121 -0.1455 -0.0360 0.0054  5    MET B CB  
3727 C  CG  . MET B 6   ? 0.3865 0.3621 0.3134 -0.1006 -0.0151 0.0070  5    MET B CG  
3728 S  SD  . MET B 6   ? 0.2790 0.2893 0.2724 -0.0055 0.0223  0.0011  5    MET B SD  
3729 C  CE  . MET B 6   ? 0.3642 0.3125 0.2444 -0.0213 -0.0833 -0.0328 5    MET B CE  
3730 N  N   . PRO B 7   ? 0.2766 0.2012 0.2065 -0.0058 0.0121  0.0213  6    PRO B N   
3731 C  CA  . PRO B 7   ? 0.2467 0.2398 0.1999 0.0418  0.0313  0.0096  6    PRO B CA  
3732 C  C   . PRO B 7   ? 0.1944 0.2380 0.1689 -0.0123 0.0510  0.0055  6    PRO B C   
3733 O  O   . PRO B 7   ? 0.1732 0.2779 0.1815 -0.0221 0.0353  -0.0143 6    PRO B O   
3734 C  CB  . PRO B 7   ? 0.3281 0.2521 0.2288 0.0566  0.0245  0.0149  6    PRO B CB  
3735 C  CG  . PRO B 7   ? 0.2799 0.1981 0.2516 0.0123  -0.0201 0.0527  6    PRO B CG  
3736 C  CD  . PRO B 7   ? 0.3204 0.2234 0.1973 0.0237  -0.0321 0.0524  6    PRO B CD  
3737 N  N   . GLN B 8   ? 0.2537 0.2084 0.1433 -0.0118 0.0095  0.0005  7    GLN B N   
3738 C  CA  . GLN B 8   ? 0.1947 0.1944 0.1946 0.0011  0.0311  0.0284  7    GLN B CA  
3739 C  C   . GLN B 8   ? 0.2053 0.2075 0.2054 -0.0127 0.0300  0.0444  7    GLN B C   
3740 O  O   . GLN B 8   ? 0.1995 0.1998 0.2442 -0.0389 0.0848  0.0277  7    GLN B O   
3741 C  CB  . GLN B 8   ? 0.1412 0.1818 0.2021 0.0080  0.0289  0.0493  7    GLN B CB  
3742 C  CG  . GLN B 8   ? 0.1905 0.1682 0.2137 0.0515  0.0849  0.0788  7    GLN B CG  
3743 C  CD  . GLN B 8   ? 0.2916 0.2379 0.2396 0.0580  0.0910  0.1014  7    GLN B CD  
3744 O  OE1 . GLN B 8   ? 0.3535 0.3040 0.2942 0.0626  0.0691  0.1319  7    GLN B OE1 
3745 N  NE2 . GLN B 8   ? 0.3144 0.2226 0.2367 0.0196  0.0618  0.0672  7    GLN B NE2 
3746 N  N   . PRO B 9   ? 0.1700 0.2014 0.2043 -0.0242 0.0616  0.0538  8    PRO B N   
3747 C  CA  . PRO B 9   ? 0.1899 0.1809 0.2083 -0.0327 0.0396  0.0591  8    PRO B CA  
3748 C  C   . PRO B 9   ? 0.2276 0.1755 0.2204 -0.0090 0.0685  0.0173  8    PRO B C   
3749 O  O   . PRO B 9   ? 0.1998 0.1854 0.2258 -0.0383 0.0780  -0.0006 8    PRO B O   
3750 C  CB  . PRO B 9   ? 0.1203 0.2037 0.1991 0.0198  0.0207  0.0607  8    PRO B CB  
3751 C  CG  . PRO B 9   ? 0.1362 0.1869 0.1795 0.0035  -0.0043 0.0570  8    PRO B CG  
3752 C  CD  . PRO B 9   ? 0.1924 0.2143 0.1610 -0.0717 0.0184  0.0747  8    PRO B CD  
3753 N  N   . LYS B 10  ? 0.2325 0.1420 0.2262 -0.0201 0.0271  0.0150  9    LYS B N   
3754 C  CA  . LYS B 10  ? 0.1345 0.1129 0.2080 0.0122  0.0240  0.0407  9    LYS B CA  
3755 C  C   . LYS B 10  ? 0.1691 0.1101 0.2101 -0.0273 0.0438  0.0588  9    LYS B C   
3756 O  O   . LYS B 10  ? 0.2359 0.0857 0.2144 -0.0046 0.0328  0.0517  9    LYS B O   
3757 C  CB  . LYS B 10  ? 0.1658 0.1374 0.1879 -0.0132 0.0019  0.0396  9    LYS B CB  
3758 C  CG  . LYS B 10  ? 0.1229 0.1693 0.1902 -0.0144 -0.0326 0.0653  9    LYS B CG  
3759 C  CD  . LYS B 10  ? 0.1309 0.2437 0.1848 0.0113  -0.0185 0.0627  9    LYS B CD  
3760 C  CE  . LYS B 10  ? 0.1478 0.3409 0.2239 -0.0194 -0.0535 0.0521  9    LYS B CE  
3761 N  NZ  . LYS B 10  ? 0.2639 0.4187 0.2252 -0.0723 -0.0267 0.0245  9    LYS B NZ  
3762 N  N   . THR B 11  ? 0.1637 0.1544 0.2478 0.0310  0.0097  0.0217  10   THR B N   
3763 C  CA  . THR B 11  ? 0.1554 0.1645 0.2118 0.0633  0.0093  0.0083  10   THR B CA  
3764 C  C   . THR B 11  ? 0.1002 0.1847 0.2207 -0.0066 -0.0098 0.0153  10   THR B C   
3765 O  O   . THR B 11  ? 0.1423 0.1571 0.2324 0.0033  0.0031  -0.0004 10   THR B O   
3766 C  CB  . THR B 11  ? 0.1793 0.2129 0.2430 -0.0281 -0.0129 0.0394  10   THR B CB  
3767 O  OG1 . THR B 11  ? 0.2124 0.2086 0.2357 -0.0458 -0.0073 0.0776  10   THR B OG1 
3768 C  CG2 . THR B 11  ? 0.1904 0.2261 0.2590 -0.0295 0.0060  0.0335  10   THR B CG2 
3769 N  N   . PHE B 12  ? 0.1623 0.1943 0.2131 0.0386  0.0395  0.0258  11   PHE B N   
3770 C  CA  . PHE B 12  ? 0.1754 0.1686 0.2132 0.0297  0.0158  0.0422  11   PHE B CA  
3771 C  C   . PHE B 12  ? 0.2433 0.2048 0.2530 0.0213  0.0091  0.0606  11   PHE B C   
3772 O  O   . PHE B 12  ? 0.2143 0.2142 0.2684 -0.0214 0.0289  0.0386  11   PHE B O   
3773 C  CB  . PHE B 12  ? 0.2223 0.1715 0.1907 0.0496  0.0145  0.0426  11   PHE B CB  
3774 C  CG  . PHE B 12  ? 0.1781 0.1504 0.1962 0.0158  0.0149  0.0442  11   PHE B CG  
3775 C  CD1 . PHE B 12  ? 0.2181 0.1390 0.2169 0.0124  0.0379  0.0351  11   PHE B CD1 
3776 C  CD2 . PHE B 12  ? 0.1712 0.1744 0.1967 0.0007  0.0309  0.0574  11   PHE B CD2 
3777 C  CE1 . PHE B 12  ? 0.2420 0.1136 0.2185 -0.0178 0.0455  0.0162  11   PHE B CE1 
3778 C  CE2 . PHE B 12  ? 0.1926 0.1610 0.2152 -0.0145 -0.0071 0.0281  11   PHE B CE2 
3779 C  CZ  . PHE B 12  ? 0.2654 0.1279 0.2151 -0.0104 0.0347  0.0267  11   PHE B CZ  
3780 N  N   . GLY B 13  ? 0.1682 0.2123 0.2659 0.0602  0.0105  0.0618  12   GLY B N   
3781 C  CA  . GLY B 13  ? 0.1462 0.2263 0.2969 0.0570  0.0907  0.0662  12   GLY B CA  
3782 C  C   . GLY B 13  ? 0.1384 0.2392 0.3012 0.0487  0.0742  0.0757  12   GLY B C   
3783 O  O   . GLY B 13  ? 0.2566 0.2370 0.2880 0.0019  0.0477  0.0690  12   GLY B O   
3784 N  N   . GLU B 14  ? 0.1615 0.2294 0.3129 0.0824  0.0805  0.0749  13   GLU B N   
3785 C  CA  . GLU B 14  ? 0.1736 0.2840 0.3510 0.0853  0.0951  0.0885  13   GLU B CA  
3786 C  C   . GLU B 14  ? 0.1675 0.2464 0.3566 0.0656  0.0804  0.0882  13   GLU B C   
3787 O  O   . GLU B 14  ? 0.1926 0.2537 0.3687 0.0491  0.0655  0.0778  13   GLU B O   
3788 C  CB  . GLU B 14  ? 0.2840 0.3887 0.4241 0.1084  0.1079  0.1225  13   GLU B CB  
3789 C  CG  . GLU B 14  ? 0.4700 0.5129 0.4770 0.1011  0.0981  0.1107  13   GLU B CG  
3790 C  CD  . GLU B 14  ? 0.6756 0.6420 0.5216 0.0776  0.1222  0.1180  13   GLU B CD  
3791 O  OE1 . GLU B 14  ? 0.7199 0.6953 0.5461 0.0642  0.1112  0.1036  13   GLU B OE1 
3792 O  OE2 . GLU B 14  ? 0.7605 0.6902 0.5384 0.0414  0.1235  0.1364  13   GLU B OE2 
3793 N  N   . LEU B 15  ? 0.1780 0.2174 0.3192 0.0443  0.0757  0.0756  14   LEU B N   
3794 C  CA  . LEU B 15  ? 0.2223 0.2237 0.3109 0.0192  0.0603  0.0445  14   LEU B CA  
3795 C  C   . LEU B 15  ? 0.2047 0.2225 0.3117 0.0146  0.0560  0.0296  14   LEU B C   
3796 O  O   . LEU B 15  ? 0.1521 0.2178 0.3214 0.0064  0.0534  0.0149  14   LEU B O   
3797 C  CB  . LEU B 15  ? 0.2301 0.2457 0.2689 0.0115  0.0646  0.0154  14   LEU B CB  
3798 C  CG  . LEU B 15  ? 0.2705 0.3173 0.2672 0.0641  0.0929  0.0086  14   LEU B CG  
3799 C  CD1 . LEU B 15  ? 0.3849 0.3204 0.2538 0.0767  0.0497  -0.0182 14   LEU B CD1 
3800 C  CD2 . LEU B 15  ? 0.3101 0.3380 0.2842 0.0712  0.1414  0.0155  14   LEU B CD2 
3801 N  N   . LYS B 16  ? 0.1597 0.2215 0.2977 0.0254  0.0743  0.0275  15   LYS B N   
3802 C  CA  . LYS B 16  ? 0.0977 0.2374 0.2959 0.0066  0.0087  0.0315  15   LYS B CA  
3803 C  C   . LYS B 16  ? 0.0726 0.2013 0.2268 -0.0214 0.0244  0.0371  15   LYS B C   
3804 O  O   . LYS B 16  ? 0.1527 0.1944 0.2153 -0.0731 0.0465  0.0447  15   LYS B O   
3805 C  CB  . LYS B 16  ? 0.1329 0.2735 0.3539 0.0150  -0.0520 0.0669  15   LYS B CB  
3806 C  CG  . LYS B 16  ? 0.1761 0.2999 0.4003 0.0069  -0.1178 0.0667  15   LYS B CG  
3807 C  CD  . LYS B 16  ? 0.2483 0.3579 0.4244 0.1013  -0.1159 0.0796  15   LYS B CD  
3808 C  CE  . LYS B 16  ? 0.2996 0.4193 0.4704 0.0647  -0.1229 0.0630  15   LYS B CE  
3809 N  NZ  . LYS B 16  ? 0.4059 0.4654 0.4854 0.0906  -0.1143 0.0417  15   LYS B NZ  
3810 N  N   . ASN B 17  ? 0.1120 0.2011 0.2075 0.0028  0.0294  0.0550  16   ASN B N   
3811 C  CA  . ASN B 17  ? 0.1662 0.1857 0.1937 0.0175  0.0250  0.0223  16   ASN B CA  
3812 C  C   . ASN B 17  ? 0.1638 0.1912 0.1940 -0.0073 0.0226  0.0160  16   ASN B C   
3813 O  O   . ASN B 17  ? 0.1934 0.1984 0.1910 0.0248  -0.0101 0.0574  16   ASN B O   
3814 C  CB  . ASN B 17  ? 0.1821 0.1769 0.2057 -0.0270 0.0356  0.0306  16   ASN B CB  
3815 C  CG  . ASN B 17  ? 0.1315 0.2067 0.2149 -0.0074 0.0639  0.0132  16   ASN B CG  
3816 O  OD1 . ASN B 17  ? 0.1458 0.2166 0.2093 -0.0116 0.0465  -0.0110 16   ASN B OD1 
3817 N  ND2 . ASN B 17  ? 0.1222 0.1962 0.2223 -0.0076 0.0831  0.0381  16   ASN B ND2 
3818 N  N   . LEU B 18  ? 0.1913 0.1886 0.2135 0.0245  0.0628  0.0140  17   LEU B N   
3819 C  CA  . LEU B 18  ? 0.1447 0.2166 0.2077 0.0014  0.0900  0.0308  17   LEU B CA  
3820 C  C   . LEU B 18  ? 0.2070 0.2075 0.2271 0.0144  0.0561  0.0473  17   LEU B C   
3821 O  O   . LEU B 18  ? 0.2168 0.2164 0.1909 0.0057  0.0197  0.0261  17   LEU B O   
3822 C  CB  . LEU B 18  ? 0.1565 0.2264 0.2088 0.0206  0.1042  0.0183  17   LEU B CB  
3823 C  CG  . LEU B 18  ? 0.2377 0.2173 0.2333 0.0297  0.1346  0.0551  17   LEU B CG  
3824 C  CD1 . LEU B 18  ? 0.2624 0.2324 0.2501 -0.0448 0.1042  0.0832  17   LEU B CD1 
3825 C  CD2 . LEU B 18  ? 0.2347 0.2254 0.2560 0.0574  0.0914  0.0097  17   LEU B CD2 
3826 N  N   . PRO B 19  ? 0.1636 0.1599 0.2580 0.0010  0.0367  0.0816  18   PRO B N   
3827 C  CA  . PRO B 19  ? 0.2052 0.1720 0.2585 0.0035  0.0114  0.0589  18   PRO B CA  
3828 C  C   . PRO B 19  ? 0.2244 0.2004 0.2252 0.0176  0.0315  0.0438  18   PRO B C   
3829 O  O   . PRO B 19  ? 0.2573 0.2116 0.1973 0.0024  0.0518  0.0463  18   PRO B O   
3830 C  CB  . PRO B 19  ? 0.1880 0.1747 0.2648 0.0147  0.0221  0.0511  18   PRO B CB  
3831 C  CG  . PRO B 19  ? 0.1945 0.1676 0.2512 0.0371  0.0332  0.0524  18   PRO B CG  
3832 C  CD  . PRO B 19  ? 0.1931 0.1779 0.2598 -0.0061 0.0523  0.0788  18   PRO B CD  
3833 N  N   . LEU B 20  ? 0.1969 0.1790 0.2163 0.0321  0.0363  0.0321  19   LEU B N   
3834 C  CA  . LEU B 20  ? 0.1889 0.1982 0.1880 0.0031  0.0693  0.0258  19   LEU B CA  
3835 C  C   . LEU B 20  ? 0.2482 0.2110 0.1931 -0.0179 0.0308  0.0186  19   LEU B C   
3836 O  O   . LEU B 20  ? 0.3335 0.2137 0.2134 -0.0413 -0.0230 0.0229  19   LEU B O   
3837 C  CB  . LEU B 20  ? 0.1260 0.2200 0.1818 0.0458  0.0570  0.0307  19   LEU B CB  
3838 C  CG  . LEU B 20  ? 0.2097 0.1971 0.1757 -0.0191 0.0502  0.0501  19   LEU B CG  
3839 C  CD1 . LEU B 20  ? 0.2458 0.2037 0.1762 0.0212  0.0429  0.0377  19   LEU B CD1 
3840 C  CD2 . LEU B 20  ? 0.2664 0.2298 0.1965 0.0095  -0.0099 0.0474  19   LEU B CD2 
3841 N  N   . LEU B 21  ? 0.1709 0.2171 0.2042 -0.0141 0.0519  0.0096  20   LEU B N   
3842 C  CA  . LEU B 21  ? 0.1722 0.2236 0.1981 -0.0252 0.0379  0.0271  20   LEU B CA  
3843 C  C   . LEU B 21  ? 0.2292 0.1856 0.2074 0.0018  -0.0004 0.0334  20   LEU B C   
3844 O  O   . LEU B 21  ? 0.2061 0.1919 0.1983 0.0155  0.0040  0.0307  20   LEU B O   
3845 C  CB  . LEU B 21  ? 0.1872 0.2490 0.1996 -0.0126 -0.0047 0.0401  20   LEU B CB  
3846 C  CG  . LEU B 21  ? 0.2201 0.2433 0.2268 -0.0287 -0.0379 0.0433  20   LEU B CG  
3847 C  CD1 . LEU B 21  ? 0.2465 0.2810 0.2282 -0.0226 -0.0696 0.0561  20   LEU B CD1 
3848 C  CD2 . LEU B 21  ? 0.3494 0.2737 0.2322 -0.0084 -0.0322 0.0051  20   LEU B CD2 
3849 N  N   . ASN B 22  ? 0.2445 0.1688 0.2259 -0.0203 0.0010  0.0199  21   ASN B N   
3850 C  CA  . ASN B 22  ? 0.2334 0.1498 0.2235 -0.0421 -0.0170 -0.0059 21   ASN B CA  
3851 C  C   . ASN B 22  ? 0.2461 0.1528 0.2181 -0.0052 -0.0053 0.0013  21   ASN B C   
3852 O  O   . ASN B 22  ? 0.2342 0.1782 0.2464 -0.0286 -0.0328 0.0149  21   ASN B O   
3853 C  CB  . ASN B 22  ? 0.2737 0.1614 0.2422 0.0478  0.0119  -0.0167 21   ASN B CB  
3854 C  CG  . ASN B 22  ? 0.4320 0.2140 0.2663 -0.0098 -0.0309 -0.0081 21   ASN B CG  
3855 O  OD1 . ASN B 22  ? 0.4162 0.2630 0.2754 -0.0232 0.0055  -0.0361 21   ASN B OD1 
3856 N  ND2 . ASN B 22  ? 0.5537 0.2395 0.2874 -0.0377 -0.0437 -0.0159 21   ASN B ND2 
3857 N  N   . THR B 23  ? 0.2162 0.1354 0.1713 -0.0112 -0.0009 0.0339  22   THR B N   
3858 C  CA  . THR B 23  ? 0.2293 0.1784 0.2067 -0.0078 -0.0604 0.0165  22   THR B CA  
3859 C  C   . THR B 23  ? 0.2564 0.1805 0.2145 -0.0040 -0.0716 -0.0085 22   THR B C   
3860 O  O   . THR B 23  ? 0.2618 0.1892 0.2443 -0.0333 -0.0348 -0.0144 22   THR B O   
3861 C  CB  . THR B 23  ? 0.2225 0.2335 0.2277 -0.0429 -0.0707 0.0258  22   THR B CB  
3862 O  OG1 . THR B 23  ? 0.2513 0.2858 0.2522 -0.0262 -0.0768 0.0140  22   THR B OG1 
3863 C  CG2 . THR B 23  ? 0.1972 0.2141 0.2156 -0.0718 -0.0268 0.0249  22   THR B CG2 
3864 N  N   . ASP B 24  ? 0.3386 0.1770 0.2065 -0.0088 -0.0659 -0.0429 23   ASP B N   
3865 C  CA  . ASP B 24  ? 0.3990 0.2046 0.2297 0.0260  -0.1120 -0.0413 23   ASP B CA  
3866 C  C   . ASP B 24  ? 0.2604 0.1627 0.2009 0.0282  -0.0916 -0.0340 23   ASP B C   
3867 O  O   . ASP B 24  ? 0.2812 0.1700 0.1847 -0.0249 -0.0378 -0.0012 23   ASP B O   
3868 C  CB  . ASP B 24  ? 0.4972 0.2826 0.2764 0.0101  -0.1841 -0.0349 23   ASP B CB  
3869 C  CG  . ASP B 24  ? 0.5211 0.3806 0.3334 -0.0213 -0.2358 -0.0166 23   ASP B CG  
3870 O  OD1 . ASP B 24  ? 0.5426 0.4335 0.3865 -0.0221 -0.2449 0.0056  23   ASP B OD1 
3871 O  OD2 . ASP B 24  ? 0.7041 0.4466 0.3714 -0.0482 -0.2223 -0.0107 23   ASP B OD2 
3872 N  N   . LYS B 25  ? 0.2334 0.1642 0.2104 0.0190  -0.0844 0.0097  24   LYS B N   
3873 C  CA  . LYS B 25  ? 0.1065 0.1864 0.2060 -0.0083 -0.0684 0.0090  24   LYS B CA  
3874 C  C   . LYS B 25  ? 0.0835 0.1593 0.1956 -0.0391 0.0068  0.0127  24   LYS B C   
3875 O  O   . LYS B 25  ? 0.1312 0.1291 0.2437 -0.0212 0.0092  0.0274  24   LYS B O   
3876 C  CB  . LYS B 25  ? 0.1262 0.1935 0.2275 -0.0149 -0.0863 0.0146  24   LYS B CB  
3877 C  CG  . LYS B 25  ? 0.1746 0.2315 0.2355 -0.0322 -0.1155 0.0267  24   LYS B CG  
3878 C  CD  . LYS B 25  ? 0.1569 0.2792 0.2485 0.0027  -0.1097 0.0256  24   LYS B CD  
3879 C  CE  . LYS B 25  ? 0.1281 0.2830 0.2577 -0.0481 -0.0815 0.0150  24   LYS B CE  
3880 N  NZ  . LYS B 25  ? 0.1597 0.3112 0.2956 -0.1055 -0.0555 0.0366  24   LYS B NZ  
3881 N  N   . PRO B 26  ? 0.1394 0.1431 0.1594 -0.0634 0.0106  -0.0132 25   PRO B N   
3882 C  CA  . PRO B 26  ? 0.2013 0.1635 0.1420 -0.0305 -0.0294 -0.0168 25   PRO B CA  
3883 C  C   . PRO B 26  ? 0.1202 0.1371 0.1678 -0.0585 0.0192  -0.0108 25   PRO B C   
3884 O  O   . PRO B 26  ? 0.1579 0.1467 0.1537 -0.0069 0.0182  -0.0042 25   PRO B O   
3885 C  CB  . PRO B 26  ? 0.2109 0.2005 0.1432 -0.0231 0.0093  -0.0055 25   PRO B CB  
3886 C  CG  . PRO B 26  ? 0.1676 0.1738 0.1604 0.0010  -0.0183 0.0213  25   PRO B CG  
3887 C  CD  . PRO B 26  ? 0.1328 0.1500 0.1567 0.0028  0.0014  0.0144  25   PRO B CD  
3888 N  N   . VAL B 27  ? 0.1804 0.1146 0.1816 -0.0669 -0.0127 -0.0214 26   VAL B N   
3889 C  CA  . VAL B 27  ? 0.1347 0.1348 0.1771 -0.0790 -0.0162 -0.0056 26   VAL B CA  
3890 C  C   . VAL B 27  ? 0.1444 0.1321 0.1800 -0.0811 -0.0172 0.0084  26   VAL B C   
3891 O  O   . VAL B 27  ? 0.2158 0.1123 0.1988 -0.0292 -0.0185 0.0296  26   VAL B O   
3892 C  CB  . VAL B 27  ? 0.1314 0.1200 0.1855 -0.0749 0.0045  -0.0026 26   VAL B CB  
3893 C  CG1 . VAL B 27  ? 0.2317 0.1199 0.1780 -0.0276 0.0290  0.0137  26   VAL B CG1 
3894 C  CG2 . VAL B 27  ? 0.1338 0.1857 0.2141 -0.0828 0.0016  -0.0031 26   VAL B CG2 
3895 N  N   . GLN B 28  ? 0.1094 0.1357 0.1875 -0.0577 -0.0069 0.0245  27   GLN B N   
3896 C  CA  . GLN B 28  ? 0.1244 0.1507 0.1720 -0.0162 0.0048  0.0485  27   GLN B CA  
3897 C  C   . GLN B 28  ? 0.1813 0.1483 0.1853 -0.0183 0.0034  0.0260  27   GLN B C   
3898 O  O   . GLN B 28  ? 0.1474 0.1677 0.1729 -0.0111 -0.0053 0.0271  27   GLN B O   
3899 C  CB  . GLN B 28  ? 0.1853 0.1691 0.1463 -0.0134 -0.0231 0.0585  27   GLN B CB  
3900 C  CG  . GLN B 28  ? 0.1971 0.1685 0.1374 0.0370  -0.0290 0.0473  27   GLN B CG  
3901 C  CD  . GLN B 28  ? 0.1338 0.1781 0.1610 0.0197  -0.0083 0.0469  27   GLN B CD  
3902 O  OE1 . GLN B 28  ? 0.1622 0.2095 0.1875 0.0261  -0.0222 0.0154  27   GLN B OE1 
3903 N  NE2 . GLN B 28  ? 0.1303 0.1784 0.1779 -0.0335 0.0189  0.0345  27   GLN B NE2 
3904 N  N   . ALA B 29  ? 0.2262 0.1075 0.1858 -0.0069 -0.0708 0.0137  28   ALA B N   
3905 C  CA  . ALA B 29  ? 0.2320 0.0770 0.2089 0.0086  -0.0710 0.0150  28   ALA B CA  
3906 C  C   . ALA B 29  ? 0.2171 0.1173 0.2136 0.0081  -0.0261 0.0193  28   ALA B C   
3907 O  O   . ALA B 29  ? 0.1751 0.1418 0.2122 0.0107  0.0093  0.0548  28   ALA B O   
3908 C  CB  . ALA B 29  ? 0.1883 0.0708 0.2261 -0.0068 -0.0353 0.0347  28   ALA B CB  
3909 N  N   . LEU B 30  ? 0.1529 0.1212 0.2091 -0.0190 -0.0119 -0.0103 29   LEU B N   
3910 C  CA  . LEU B 30  ? 0.1119 0.1329 0.1848 -0.0418 0.0221  -0.0156 29   LEU B CA  
3911 C  C   . LEU B 30  ? 0.1647 0.1564 0.1787 0.0136  0.0273  -0.0013 29   LEU B C   
3912 O  O   . LEU B 30  ? 0.1997 0.1626 0.1574 -0.0089 0.0182  -0.0252 29   LEU B O   
3913 C  CB  . LEU B 30  ? 0.0691 0.1687 0.1757 0.0169  0.0332  0.0166  29   LEU B CB  
3914 C  CG  . LEU B 30  ? 0.1152 0.1631 0.1626 0.0267  0.0629  0.0623  29   LEU B CG  
3915 C  CD1 . LEU B 30  ? 0.1633 0.1439 0.1496 0.0047  0.0590  0.0595  29   LEU B CD1 
3916 C  CD2 . LEU B 30  ? 0.1455 0.1833 0.2008 0.0001  0.0516  0.0746  29   LEU B CD2 
3917 N  N   . MET B 31  ? 0.1505 0.1509 0.1966 0.0442  -0.0007 -0.0043 30   MET B N   
3918 C  CA  . MET B 31  ? 0.1746 0.1288 0.2022 0.0532  0.0141  0.0177  30   MET B CA  
3919 C  C   . MET B 31  ? 0.1647 0.1385 0.2208 0.0168  0.0082  0.0081  30   MET B C   
3920 O  O   . MET B 31  ? 0.2369 0.1456 0.1883 -0.0235 0.0004  -0.0162 30   MET B O   
3921 C  CB  . MET B 31  ? 0.1921 0.1263 0.1973 -0.0197 0.0096  0.0416  30   MET B CB  
3922 C  CG  . MET B 31  ? 0.1883 0.1562 0.1842 -0.0430 -0.0104 0.0399  30   MET B CG  
3923 S  SD  . MET B 31  ? 0.2122 0.1802 0.1781 0.0020  -0.0279 0.0137  30   MET B SD  
3924 C  CE  . MET B 31  ? 0.2633 0.1676 0.2031 0.0372  -0.0192 0.0036  30   MET B CE  
3925 N  N   . LYS B 32  ? 0.1675 0.1701 0.2476 -0.0381 0.0074  0.0052  31   LYS B N   
3926 C  CA  . LYS B 32  ? 0.1371 0.2042 0.2510 -0.0495 -0.0129 0.0275  31   LYS B CA  
3927 C  C   . LYS B 32  ? 0.1537 0.1888 0.2351 -0.0169 -0.0171 0.0213  31   LYS B C   
3928 O  O   . LYS B 32  ? 0.1420 0.1980 0.2256 0.0224  0.0143  0.0212  31   LYS B O   
3929 C  CB  . LYS B 32  ? 0.1283 0.2919 0.3066 -0.0238 -0.0884 0.0346  31   LYS B CB  
3930 C  CG  . LYS B 32  ? 0.3022 0.3733 0.4015 -0.0410 -0.0981 0.0340  31   LYS B CG  
3931 C  CD  . LYS B 32  ? 0.4844 0.4261 0.4704 -0.0436 -0.1304 0.0286  31   LYS B CD  
3932 C  CE  . LYS B 32  ? 0.5901 0.4682 0.5380 -0.0657 -0.1610 0.0083  31   LYS B CE  
3933 N  NZ  . LYS B 32  ? 0.6701 0.4752 0.5850 -0.0945 -0.1890 0.0105  31   LYS B NZ  
3934 N  N   . ILE B 33  ? 0.1897 0.1694 0.2167 0.0019  -0.0383 0.0203  32   ILE B N   
3935 C  CA  . ILE B 33  ? 0.1886 0.1381 0.2073 0.0536  -0.0223 0.0277  32   ILE B CA  
3936 C  C   . ILE B 33  ? 0.1582 0.1515 0.2091 -0.0069 -0.0368 0.0453  32   ILE B C   
3937 O  O   . ILE B 33  ? 0.2368 0.1738 0.2189 -0.0095 -0.0031 0.0175  32   ILE B O   
3938 C  CB  . ILE B 33  ? 0.2325 0.1065 0.2023 0.0099  -0.0168 -0.0038 32   ILE B CB  
3939 C  CG1 . ILE B 33  ? 0.2656 0.1204 0.2433 0.0107  0.0417  -0.0388 32   ILE B CG1 
3940 C  CG2 . ILE B 33  ? 0.2194 0.1336 0.1825 0.0329  0.0275  0.0198  32   ILE B CG2 
3941 C  CD1 . ILE B 33  ? 0.2484 0.1323 0.2618 0.0524  0.0146  -0.0523 32   ILE B CD1 
3942 N  N   . ALA B 34  ? 0.1823 0.1551 0.2206 -0.0134 0.0037  0.0397  33   ALA B N   
3943 C  CA  . ALA B 34  ? 0.0996 0.1499 0.2117 0.0055  0.0488  0.0306  33   ALA B CA  
3944 C  C   . ALA B 34  ? 0.1424 0.1584 0.2275 0.0042  0.0174  0.0089  33   ALA B C   
3945 O  O   . ALA B 34  ? 0.2156 0.1679 0.2229 0.0236  0.0540  0.0133  33   ALA B O   
3946 C  CB  . ALA B 34  ? 0.1328 0.1464 0.2041 -0.0173 0.0373  0.0120  33   ALA B CB  
3947 N  N   . ASP B 35  ? 0.1678 0.1841 0.2345 -0.0421 0.0206  -0.0079 34   ASP B N   
3948 C  CA  . ASP B 35  ? 0.1642 0.2292 0.2534 -0.0090 0.0431  0.0145  34   ASP B CA  
3949 C  C   . ASP B 35  ? 0.1938 0.2319 0.2477 0.0252  0.0776  0.0180  34   ASP B C   
3950 O  O   . ASP B 35  ? 0.2400 0.2434 0.2673 -0.0002 0.0890  0.0340  34   ASP B O   
3951 C  CB  . ASP B 35  ? 0.2827 0.2702 0.2981 -0.0351 0.0104  0.0167  34   ASP B CB  
3952 C  CG  . ASP B 35  ? 0.3217 0.3395 0.3250 -0.0287 0.0161  0.0140  34   ASP B CG  
3953 O  OD1 . ASP B 35  ? 0.3320 0.3550 0.3415 0.0033  0.0687  0.0222  34   ASP B OD1 
3954 O  OD2 . ASP B 35  ? 0.3670 0.3756 0.3364 -0.0162 0.0223  0.0020  34   ASP B OD2 
3955 N  N   . GLU B 36  ? 0.1887 0.2240 0.2426 0.0436  0.0599  -0.0142 35   GLU B N   
3956 C  CA  A GLU B 36  ? 0.1851 0.2211 0.2576 -0.0044 0.0316  -0.0255 35   GLU B CA  
3957 C  CA  B GLU B 36  ? 0.2086 0.2291 0.2445 0.0082  0.0514  -0.0134 35   GLU B CA  
3958 C  C   . GLU B 36  ? 0.2225 0.2433 0.2323 0.0106  0.0541  -0.0119 35   GLU B C   
3959 O  O   . GLU B 36  ? 0.2462 0.2795 0.2338 0.0016  0.1009  -0.0041 35   GLU B O   
3960 C  CB  A GLU B 36  ? 0.2301 0.2072 0.3046 0.0064  -0.0375 -0.0447 35   GLU B CB  
3961 C  CB  B GLU B 36  ? 0.2180 0.2207 0.2542 -0.0006 0.0326  -0.0084 35   GLU B CB  
3962 C  CG  A GLU B 36  ? 0.3682 0.2506 0.3757 0.0259  -0.0891 -0.0455 35   GLU B CG  
3963 C  CG  B GLU B 36  ? 0.2588 0.2311 0.2563 -0.0067 0.0329  0.0090  35   GLU B CG  
3964 C  CD  A GLU B 36  ? 0.4898 0.3046 0.4392 0.0209  -0.1561 -0.0616 35   GLU B CD  
3965 C  CD  B GLU B 36  ? 0.3737 0.2581 0.2892 0.0030  0.0587  0.0447  35   GLU B CD  
3966 O  OE1 A GLU B 36  ? 0.5052 0.3415 0.4841 0.0551  -0.1535 -0.0821 35   GLU B OE1 
3967 O  OE1 B GLU B 36  ? 0.3724 0.2633 0.3193 -0.0220 0.1207  0.0639  35   GLU B OE1 
3968 O  OE2 A GLU B 36  ? 0.4975 0.3134 0.4549 -0.0551 -0.1828 -0.0555 35   GLU B OE2 
3969 O  OE2 B GLU B 36  ? 0.4688 0.2648 0.3075 -0.0080 0.0705  0.0569  35   GLU B OE2 
3970 N  N   . LEU B 37  ? 0.1664 0.2060 0.2197 -0.0137 -0.0084 -0.0231 36   LEU B N   
3971 C  CA  . LEU B 37  ? 0.1897 0.1997 0.1936 -0.0041 0.0028  -0.0261 36   LEU B CA  
3972 C  C   . LEU B 37  ? 0.2029 0.2184 0.1863 -0.0349 0.0348  -0.0045 36   LEU B C   
3973 O  O   . LEU B 37  ? 0.2363 0.2367 0.2027 -0.0013 0.0149  -0.0326 36   LEU B O   
3974 C  CB  . LEU B 37  ? 0.1748 0.1849 0.2170 -0.0321 0.0531  -0.0207 36   LEU B CB  
3975 C  CG  . LEU B 37  ? 0.1350 0.1989 0.2038 -0.0384 0.0461  -0.0033 36   LEU B CG  
3976 C  CD1 . LEU B 37  ? 0.1942 0.2044 0.2107 -0.0113 0.0639  -0.0195 36   LEU B CD1 
3977 C  CD2 . LEU B 37  ? 0.1824 0.2313 0.2192 -0.0415 0.0808  -0.0020 36   LEU B CD2 
3978 N  N   . GLY B 38  ? 0.1867 0.2221 0.1832 -0.0247 0.0349  0.0101  37   GLY B N   
3979 C  CA  . GLY B 38  ? 0.2610 0.2263 0.1856 -0.0627 0.0118  -0.0085 37   GLY B CA  
3980 C  C   . GLY B 38  ? 0.2605 0.2207 0.1818 -0.0392 0.0106  -0.0025 37   GLY B C   
3981 O  O   . GLY B 38  ? 0.2413 0.2505 0.1864 -0.0373 0.0293  0.0074  37   GLY B O   
3982 N  N   . GLU B 39  ? 0.2100 0.1730 0.1855 0.0069  -0.0009 -0.0061 38   GLU B N   
3983 C  CA  . GLU B 39  ? 0.2085 0.1743 0.1759 0.0053  0.0361  -0.0099 38   GLU B CA  
3984 C  C   . GLU B 39  ? 0.2040 0.1581 0.1834 -0.0011 0.0363  0.0057  38   GLU B C   
3985 O  O   . GLU B 39  ? 0.2473 0.1290 0.1691 0.0220  0.0404  0.0027  38   GLU B O   
3986 C  CB  . GLU B 39  ? 0.2686 0.2123 0.1365 0.0204  0.0358  -0.0017 38   GLU B CB  
3987 C  CG  . GLU B 39  ? 0.2228 0.2631 0.1240 -0.0096 -0.0128 -0.0079 38   GLU B CG  
3988 C  CD  . GLU B 39  ? 0.2824 0.3312 0.1365 -0.0388 0.0682  -0.0022 38   GLU B CD  
3989 O  OE1 . GLU B 39  ? 0.2883 0.3668 0.1433 -0.0753 0.0609  -0.0044 38   GLU B OE1 
3990 O  OE2 . GLU B 39  ? 0.4482 0.3296 0.1291 -0.0626 0.0526  -0.0076 38   GLU B OE2 
3991 N  N   . ILE B 40  ? 0.1929 0.1586 0.1865 0.0133  0.0260  0.0171  39   ILE B N   
3992 C  CA  . ILE B 40  ? 0.1346 0.1908 0.1670 0.0255  -0.0225 0.0128  39   ILE B CA  
3993 C  C   . ILE B 40  ? 0.2225 0.1936 0.1831 0.0244  -0.0068 0.0300  39   ILE B C   
3994 O  O   . ILE B 40  ? 0.2507 0.2115 0.1715 0.0282  0.0036  0.0580  39   ILE B O   
3995 C  CB  . ILE B 40  ? 0.1235 0.2350 0.1448 0.0034  0.0281  0.0145  39   ILE B CB  
3996 C  CG1 . ILE B 40  ? 0.1240 0.2510 0.1765 0.0135  -0.0356 -0.0141 39   ILE B CG1 
3997 C  CG2 . ILE B 40  ? 0.2862 0.2136 0.1068 0.0078  0.0450  0.0423  39   ILE B CG2 
3998 C  CD1 . ILE B 40  ? 0.2178 0.2859 0.1532 0.0241  -0.0265 -0.0076 39   ILE B CD1 
3999 N  N   . PHE B 41  ? 0.1856 0.1764 0.1892 0.0058  0.0333  0.0003  40   PHE B N   
4000 C  CA  . PHE B 41  ? 0.1697 0.1825 0.2077 0.0338  0.0454  0.0051  40   PHE B CA  
4001 C  C   . PHE B 41  ? 0.1848 0.2024 0.2236 -0.0029 -0.0086 0.0181  40   PHE B C   
4002 O  O   . PHE B 41  ? 0.1403 0.2077 0.2216 -0.0092 0.0081  0.0365  40   PHE B O   
4003 C  CB  . PHE B 41  ? 0.0970 0.2096 0.1762 0.0087  0.0063  0.0292  40   PHE B CB  
4004 C  CG  . PHE B 41  ? 0.1178 0.2000 0.1662 0.0095  0.0299  0.0367  40   PHE B CG  
4005 C  CD1 . PHE B 41  ? 0.1127 0.2114 0.1650 -0.0040 0.0457  0.0251  40   PHE B CD1 
4006 C  CD2 . PHE B 41  ? 0.1272 0.1906 0.1615 -0.0197 0.0142  0.0626  40   PHE B CD2 
4007 C  CE1 . PHE B 41  ? 0.1187 0.1708 0.1793 0.0078  0.0328  0.0063  40   PHE B CE1 
4008 C  CE2 . PHE B 41  ? 0.1576 0.1789 0.1756 0.0174  0.0500  0.0453  40   PHE B CE2 
4009 C  CZ  . PHE B 41  ? 0.1010 0.1907 0.1809 0.0291  0.0326  0.0268  40   PHE B CZ  
4010 N  N   . LYS B 42  ? 0.1801 0.1764 0.2271 0.0115  -0.0331 0.0094  41   LYS B N   
4011 C  CA  . LYS B 42  ? 0.1792 0.2037 0.2105 0.0519  -0.0357 0.0189  41   LYS B CA  
4012 C  C   . LYS B 42  ? 0.2317 0.2059 0.1878 0.0023  -0.0064 0.0152  41   LYS B C   
4013 O  O   . LYS B 42  ? 0.2039 0.2187 0.1786 -0.0163 0.0020  0.0272  41   LYS B O   
4014 C  CB  . LYS B 42  ? 0.2021 0.2346 0.2344 0.1066  -0.0582 0.0328  41   LYS B CB  
4015 C  CG  . LYS B 42  ? 0.2618 0.2857 0.2751 0.1059  -0.0679 0.0733  41   LYS B CG  
4016 C  CD  . LYS B 42  ? 0.3786 0.3187 0.3502 0.1367  -0.0980 0.1004  41   LYS B CD  
4017 C  CE  . LYS B 42  ? 0.5604 0.3559 0.3848 0.1288  -0.1265 0.1107  41   LYS B CE  
4018 N  NZ  . LYS B 42  ? 0.6412 0.3773 0.4189 0.1425  -0.1289 0.1361  41   LYS B NZ  
4019 N  N   . PHE B 43  ? 0.1891 0.1912 0.1794 -0.0008 0.0005  0.0219  42   PHE B N   
4020 C  CA  . PHE B 43  ? 0.1710 0.1944 0.1741 0.0096  0.0521  0.0394  42   PHE B CA  
4021 C  C   . PHE B 43  ? 0.1259 0.1974 0.2086 -0.0071 0.0504  0.0223  42   PHE B C   
4022 O  O   . PHE B 43  ? 0.1343 0.2143 0.2053 -0.0435 0.0095  0.0015  42   PHE B O   
4023 C  CB  . PHE B 43  ? 0.1851 0.1835 0.1588 -0.0478 0.0209  0.0541  42   PHE B CB  
4024 C  CG  . PHE B 43  ? 0.2592 0.1893 0.1769 -0.0098 0.0005  0.0477  42   PHE B CG  
4025 C  CD1 . PHE B 43  ? 0.2632 0.2215 0.1808 -0.0051 -0.0479 0.0262  42   PHE B CD1 
4026 C  CD2 . PHE B 43  ? 0.2544 0.1754 0.1879 0.0061  -0.0274 0.0396  42   PHE B CD2 
4027 C  CE1 . PHE B 43  ? 0.3307 0.2326 0.1901 -0.0843 -0.0112 0.0100  42   PHE B CE1 
4028 C  CE2 . PHE B 43  ? 0.2571 0.1930 0.1931 -0.0532 -0.0165 0.0151  42   PHE B CE2 
4029 C  CZ  . PHE B 43  ? 0.3117 0.2224 0.1823 -0.0825 -0.0131 0.0199  42   PHE B CZ  
4030 N  N   . GLU B 44  ? 0.1299 0.2276 0.2140 0.0214  0.0577  0.0290  43   GLU B N   
4031 C  CA  . GLU B 44  ? 0.1560 0.2358 0.2340 0.0575  0.0392  0.0464  43   GLU B CA  
4032 C  C   . GLU B 44  ? 0.1594 0.2258 0.2512 0.0244  0.0727  0.0017  43   GLU B C   
4033 O  O   . GLU B 44  ? 0.1838 0.2079 0.2755 0.0097  0.0404  -0.0160 43   GLU B O   
4034 C  CB  . GLU B 44  ? 0.2299 0.2895 0.2392 0.0819  -0.0152 0.0858  43   GLU B CB  
4035 C  CG  . GLU B 44  ? 0.3025 0.3532 0.2957 0.0408  -0.0438 0.0855  43   GLU B CG  
4036 C  CD  . GLU B 44  ? 0.4253 0.4081 0.3464 0.0402  -0.0660 0.1024  43   GLU B CD  
4037 O  OE1 . GLU B 44  ? 0.4626 0.4157 0.3538 0.0678  0.0156  0.0951  43   GLU B OE1 
4038 O  OE2 . GLU B 44  ? 0.4541 0.4576 0.3829 0.0753  -0.1103 0.1333  43   GLU B OE2 
4039 N  N   . ALA B 45  ? 0.1431 0.2185 0.2526 0.0345  0.0701  -0.0436 44   ALA B N   
4040 C  CA  . ALA B 45  ? 0.1855 0.2070 0.2583 0.0440  0.0657  -0.0087 44   ALA B CA  
4041 C  C   . ALA B 45  ? 0.1509 0.2051 0.2838 0.0167  0.0424  -0.0041 44   ALA B C   
4042 O  O   . ALA B 45  ? 0.1707 0.2025 0.3111 -0.0113 0.0377  0.0102  44   ALA B O   
4043 C  CB  . ALA B 45  ? 0.2192 0.1815 0.2743 0.0377  0.0326  0.0028  44   ALA B CB  
4044 N  N   . PRO B 46  ? 0.1631 0.2243 0.3071 0.0153  0.0253  0.0067  45   PRO B N   
4045 C  CA  . PRO B 46  ? 0.1860 0.2333 0.3350 0.0480  0.0553  -0.0242 45   PRO B CA  
4046 C  C   . PRO B 46  ? 0.2097 0.2980 0.3659 0.0276  0.1014  -0.0273 45   PRO B C   
4047 O  O   . PRO B 46  ? 0.1975 0.3273 0.3687 0.0042  0.1133  -0.0174 45   PRO B O   
4048 C  CB  . PRO B 46  ? 0.2494 0.2192 0.3425 0.0938  0.0367  -0.0010 45   PRO B CB  
4049 C  CG  . PRO B 46  ? 0.2083 0.2522 0.3464 0.0385  0.0425  -0.0072 45   PRO B CG  
4050 C  CD  . PRO B 46  ? 0.1917 0.2215 0.3226 0.0053  0.0479  -0.0165 45   PRO B CD  
4051 N  N   . GLY B 47  ? 0.2292 0.3170 0.3970 0.0663  0.0570  -0.0260 46   GLY B N   
4052 C  CA  . GLY B 47  ? 0.2085 0.3026 0.4297 0.0433  0.0512  -0.0388 46   GLY B CA  
4053 C  C   . GLY B 47  ? 0.1390 0.2833 0.4341 0.0184  0.0369  -0.0276 46   GLY B C   
4054 O  O   . GLY B 47  ? 0.1810 0.3148 0.4798 0.0293  0.0348  -0.0366 46   GLY B O   
4055 N  N   . ARG B 48  ? 0.1553 0.2751 0.3699 0.0462  0.0377  -0.0068 47   ARG B N   
4056 C  CA  . ARG B 48  ? 0.2263 0.2819 0.3397 0.0596  0.0241  0.0295  47   ARG B CA  
4057 C  C   . ARG B 48  ? 0.1767 0.2714 0.3215 0.0283  0.0043  0.0101  47   ARG B C   
4058 O  O   . ARG B 48  ? 0.2083 0.2945 0.3117 0.0243  0.0359  -0.0044 47   ARG B O   
4059 C  CB  . ARG B 48  ? 0.3969 0.3088 0.3267 0.0959  -0.0003 0.0883  47   ARG B CB  
4060 C  CG  . ARG B 48  ? 0.5144 0.3507 0.3152 0.1348  -0.0079 0.0980  47   ARG B CG  
4061 C  CD  . ARG B 48  ? 0.4704 0.3623 0.2749 0.1490  -0.0652 0.1037  47   ARG B CD  
4062 N  NE  . ARG B 48  ? 0.3972 0.3317 0.2465 0.1043  -0.0490 0.0979  47   ARG B NE  
4063 C  CZ  . ARG B 48  ? 0.4533 0.3499 0.2135 -0.0037 -0.0054 0.0332  47   ARG B CZ  
4064 N  NH1 . ARG B 48  ? 0.5095 0.3749 0.2314 -0.0362 0.0492  0.0165  47   ARG B NH1 
4065 N  NH2 . ARG B 48  ? 0.3518 0.3091 0.1589 -0.0382 -0.0560 -0.0225 47   ARG B NH2 
4066 N  N   . VAL B 49  ? 0.1465 0.2735 0.3115 0.0096  0.0211  -0.0158 48   VAL B N   
4067 C  CA  . VAL B 49  ? 0.1791 0.2651 0.2976 0.0262  0.0506  -0.0084 48   VAL B CA  
4068 C  C   . VAL B 49  ? 0.1572 0.2264 0.2782 0.0337  0.0293  0.0166  48   VAL B C   
4069 O  O   . VAL B 49  ? 0.1617 0.2354 0.3027 0.0266  0.0280  0.0355  48   VAL B O   
4070 C  CB  . VAL B 49  ? 0.2609 0.3242 0.3229 0.0012  0.0898  -0.0035 48   VAL B CB  
4071 C  CG1 . VAL B 49  ? 0.4080 0.3625 0.3497 0.0323  0.0692  0.0072  48   VAL B CG1 
4072 C  CG2 . VAL B 49  ? 0.3237 0.3309 0.3015 0.0315  0.0919  0.0139  48   VAL B CG2 
4073 N  N   . THR B 50  ? 0.1170 0.2057 0.2389 0.0096  0.0142  0.0291  49   THR B N   
4074 C  CA  . THR B 50  ? 0.1631 0.1960 0.2284 -0.0010 0.0422  0.0337  49   THR B CA  
4075 C  C   . THR B 50  ? 0.1695 0.1739 0.2210 0.0038  0.0387  0.0097  49   THR B C   
4076 O  O   . THR B 50  ? 0.2622 0.1875 0.2354 -0.0034 -0.0148 -0.0156 49   THR B O   
4077 C  CB  . THR B 50  ? 0.2361 0.2098 0.1989 -0.0327 -0.0330 0.0279  49   THR B CB  
4078 O  OG1 . THR B 50  ? 0.2146 0.2169 0.2013 -0.0068 0.0047  0.0586  49   THR B OG1 
4079 C  CG2 . THR B 50  ? 0.1890 0.2053 0.1999 -0.0860 -0.0782 -0.0041 49   THR B CG2 
4080 N  N   . ARG B 51  ? 0.1711 0.1519 0.2034 0.0363  0.0037  0.0068  50   ARG B N   
4081 C  CA  . ARG B 51  ? 0.1877 0.1890 0.1707 0.0592  -0.0198 0.0145  50   ARG B CA  
4082 C  C   . ARG B 51  ? 0.1378 0.1959 0.1961 0.0610  -0.0101 0.0142  50   ARG B C   
4083 O  O   . ARG B 51  ? 0.1830 0.2218 0.2287 0.0185  -0.0702 0.0416  50   ARG B O   
4084 C  CB  . ARG B 51  ? 0.1710 0.2230 0.1704 0.0736  -0.0457 0.0558  50   ARG B CB  
4085 C  CG  . ARG B 51  ? 0.1785 0.2424 0.2028 0.0642  -0.0465 0.0757  50   ARG B CG  
4086 C  CD  . ARG B 51  ? 0.1616 0.2252 0.2338 0.0544  -0.0362 0.0802  50   ARG B CD  
4087 N  NE  . ARG B 51  ? 0.2202 0.2468 0.2414 0.0394  -0.0125 0.0670  50   ARG B NE  
4088 C  CZ  . ARG B 51  ? 0.2485 0.2490 0.2273 0.0203  -0.0412 0.0837  50   ARG B CZ  
4089 N  NH1 . ARG B 51  ? 0.2587 0.2478 0.2078 0.0115  -0.0475 0.0697  50   ARG B NH1 
4090 N  NH2 . ARG B 51  ? 0.2552 0.2370 0.2409 0.0298  -0.0244 0.0999  50   ARG B NH2 
4091 N  N   . TYR B 52  ? 0.1098 0.1696 0.1906 0.0243  -0.0234 0.0102  51   TYR B N   
4092 C  CA  . TYR B 52  ? 0.1782 0.1437 0.1718 0.0114  -0.0157 -0.0109 51   TYR B CA  
4093 C  C   . TYR B 52  ? 0.2022 0.1445 0.1521 0.0016  0.0019  -0.0071 51   TYR B C   
4094 O  O   . TYR B 52  ? 0.2035 0.1547 0.1573 -0.0042 0.0296  0.0200  51   TYR B O   
4095 C  CB  . TYR B 52  ? 0.1369 0.1210 0.1347 -0.0337 -0.0016 -0.0291 51   TYR B CB  
4096 C  CG  . TYR B 52  ? 0.1353 0.1657 0.1444 -0.0282 0.0734  -0.0238 51   TYR B CG  
4097 C  CD1 . TYR B 52  ? 0.1792 0.1560 0.1692 -0.0055 0.0713  -0.0237 51   TYR B CD1 
4098 C  CD2 . TYR B 52  ? 0.1286 0.1920 0.1229 -0.0419 0.0299  -0.0213 51   TYR B CD2 
4099 C  CE1 . TYR B 52  ? 0.1759 0.1663 0.1592 0.0090  0.0183  -0.0076 51   TYR B CE1 
4100 C  CE2 . TYR B 52  ? 0.1768 0.1744 0.1425 -0.0114 0.0341  -0.0219 51   TYR B CE2 
4101 C  CZ  . TYR B 52  ? 0.1915 0.1583 0.1594 -0.0128 0.0316  -0.0007 51   TYR B CZ  
4102 O  OH  . TYR B 52  ? 0.1960 0.1859 0.1669 0.0027  -0.0071 0.0006  51   TYR B OH  
4103 N  N   . LEU B 53  ? 0.1637 0.1444 0.1371 0.0164  -0.0518 -0.0041 52   LEU B N   
4104 C  CA  . LEU B 53  ? 0.1338 0.1533 0.1456 0.0001  -0.0145 -0.0069 52   LEU B CA  
4105 C  C   . LEU B 53  ? 0.1280 0.1838 0.1482 0.0108  -0.0299 -0.0197 52   LEU B C   
4106 O  O   . LEU B 53  ? 0.1831 0.2189 0.1499 -0.0029 -0.0041 -0.0436 52   LEU B O   
4107 C  CB  . LEU B 53  ? 0.1155 0.2080 0.1703 -0.0263 -0.0551 0.0013  52   LEU B CB  
4108 C  CG  . LEU B 53  ? 0.1623 0.2308 0.1775 -0.0388 -0.0440 0.0538  52   LEU B CG  
4109 C  CD1 . LEU B 53  ? 0.2216 0.2279 0.1969 0.0050  -0.0233 0.0392  52   LEU B CD1 
4110 C  CD2 . LEU B 53  ? 0.2772 0.2350 0.1610 -0.0067 -0.0216 0.0578  52   LEU B CD2 
4111 N  N   . SER B 54  ? 0.1463 0.1590 0.1494 -0.0181 0.0104  -0.0104 53   SER B N   
4112 C  CA  . SER B 54  ? 0.1366 0.1593 0.1568 -0.0253 -0.0276 -0.0165 53   SER B CA  
4113 C  C   . SER B 54  ? 0.1476 0.1588 0.1473 0.0214  -0.0383 0.0030  53   SER B C   
4114 O  O   . SER B 54  ? 0.1808 0.1826 0.1670 0.0406  -0.0130 0.0233  53   SER B O   
4115 C  CB  . SER B 54  ? 0.1897 0.1811 0.1757 -0.0278 -0.0517 -0.0465 53   SER B CB  
4116 O  OG  . SER B 54  ? 0.1937 0.2285 0.1885 -0.0590 -0.0297 0.0123  53   SER B OG  
4117 N  N   . SER B 55  ? 0.1596 0.1811 0.1478 -0.0085 -0.0129 -0.0192 54   SER B N   
4118 C  CA  . SER B 55  ? 0.2519 0.2053 0.1180 -0.0120 -0.0325 -0.0221 54   SER B CA  
4119 C  C   . SER B 55  ? 0.2483 0.2072 0.1417 -0.0298 -0.0062 -0.0166 54   SER B C   
4120 O  O   . SER B 55  ? 0.2261 0.2368 0.1506 -0.0613 -0.0026 -0.0120 54   SER B O   
4121 C  CB  . SER B 55  ? 0.1998 0.2312 0.0922 0.0214  -0.0360 -0.0003 54   SER B CB  
4122 O  OG  . SER B 55  ? 0.2329 0.2257 0.1004 0.0148  -0.0345 0.0156  54   SER B OG  
4123 N  N   . GLN B 56  ? 0.1979 0.1677 0.1363 -0.0472 -0.0040 -0.0121 55   GLN B N   
4124 C  CA  . GLN B 56  ? 0.1883 0.1460 0.1500 0.0132  -0.0190 -0.0329 55   GLN B CA  
4125 C  C   . GLN B 56  ? 0.1874 0.2010 0.1334 -0.0057 -0.0165 -0.0261 55   GLN B C   
4126 O  O   . GLN B 56  ? 0.1644 0.2371 0.1267 -0.0317 -0.0344 -0.0129 55   GLN B O   
4127 C  CB  . GLN B 56  ? 0.1887 0.1373 0.1801 0.0030  -0.0133 -0.0095 55   GLN B CB  
4128 C  CG  . GLN B 56  ? 0.1531 0.1916 0.2269 -0.0210 -0.0448 -0.0136 55   GLN B CG  
4129 C  CD  . GLN B 56  ? 0.2174 0.2248 0.2315 -0.0511 -0.0388 0.0071  55   GLN B CD  
4130 O  OE1 . GLN B 56  ? 0.2650 0.2515 0.1916 0.0087  -0.0337 -0.0136 55   GLN B OE1 
4131 N  NE2 . GLN B 56  ? 0.2060 0.2534 0.2711 -0.0769 -0.0126 0.0574  55   GLN B NE2 
4132 N  N   . ARG B 57  ? 0.1921 0.2176 0.1305 0.0674  0.0137  -0.0195 56   ARG B N   
4133 C  CA  . ARG B 57  ? 0.2325 0.2757 0.1314 0.0287  -0.0315 0.0034  56   ARG B CA  
4134 C  C   . ARG B 57  ? 0.1731 0.2795 0.1415 -0.0063 -0.0606 -0.0070 56   ARG B C   
4135 O  O   . ARG B 57  ? 0.1954 0.2471 0.1864 0.0413  -0.0571 -0.0011 56   ARG B O   
4136 C  CB  . ARG B 57  ? 0.3113 0.3520 0.1217 0.0415  0.0031  0.0280  56   ARG B CB  
4137 C  CG  . ARG B 57  ? 0.3996 0.3905 0.2001 0.0541  0.0774  0.0683  56   ARG B CG  
4138 C  CD  . ARG B 57  ? 0.5031 0.3743 0.2286 0.0247  0.1099  0.0977  56   ARG B CD  
4139 N  NE  . ARG B 57  ? 0.5446 0.3528 0.2453 -0.0540 0.0653  0.0828  56   ARG B NE  
4140 C  CZ  . ARG B 57  ? 0.4496 0.3629 0.2257 -0.0406 0.0145  0.0488  56   ARG B CZ  
4141 N  NH1 . ARG B 57  ? 0.3632 0.3557 0.2248 -0.0032 -0.0179 0.0356  56   ARG B NH1 
4142 N  NH2 . ARG B 57  ? 0.4492 0.3893 0.2049 -0.0751 0.0351  0.0199  56   ARG B NH2 
4143 N  N   . LEU B 58  ? 0.1733 0.2641 0.1256 -0.0267 0.0045  0.0261  57   LEU B N   
4144 C  CA  . LEU B 58  ? 0.1458 0.2354 0.1137 -0.0288 0.0124  0.0343  57   LEU B CA  
4145 C  C   . LEU B 58  ? 0.1970 0.2158 0.1229 -0.0636 0.0146  0.0060  57   LEU B C   
4146 O  O   . LEU B 58  ? 0.1589 0.2318 0.1570 -0.0020 -0.0128 0.0147  57   LEU B O   
4147 C  CB  . LEU B 58  ? 0.1653 0.2322 0.1376 -0.0388 0.0181  0.0567  57   LEU B CB  
4148 C  CG  . LEU B 58  ? 0.1979 0.2231 0.1474 -0.0299 -0.0096 0.0299  57   LEU B CG  
4149 C  CD1 . LEU B 58  ? 0.2267 0.2410 0.1600 0.0144  0.0020  0.0507  57   LEU B CD1 
4150 C  CD2 . LEU B 58  ? 0.2010 0.2410 0.1872 0.0076  -0.0388 0.0137  57   LEU B CD2 
4151 N  N   . ILE B 59  ? 0.2378 0.2019 0.1085 -0.0028 0.0200  0.0041  58   ILE B N   
4152 C  CA  . ILE B 59  ? 0.1620 0.2016 0.1202 -0.0330 -0.0310 -0.0074 58   ILE B CA  
4153 C  C   . ILE B 59  ? 0.1709 0.2311 0.1409 -0.0212 0.0106  0.0072  58   ILE B C   
4154 O  O   . ILE B 59  ? 0.1510 0.2521 0.1676 -0.0273 -0.0035 0.0364  58   ILE B O   
4155 C  CB  . ILE B 59  ? 0.1942 0.1243 0.0995 0.0186  -0.0278 0.0061  58   ILE B CB  
4156 C  CG1 . ILE B 59  ? 0.2047 0.1304 0.1234 -0.0039 -0.0432 -0.0233 58   ILE B CG1 
4157 C  CG2 . ILE B 59  ? 0.1730 0.1403 0.1083 0.0513  -0.0312 0.0141  58   ILE B CG2 
4158 C  CD1 . ILE B 59  ? 0.2479 0.1014 0.1132 -0.0105 -0.0362 -0.0179 58   ILE B CD1 
4159 N  N   . LYS B 60  ? 0.1922 0.2660 0.1343 -0.0380 -0.0155 0.0205  59   LYS B N   
4160 C  CA  . LYS B 60  ? 0.1957 0.2715 0.1549 -0.0013 0.0019  -0.0185 59   LYS B CA  
4161 C  C   . LYS B 60  ? 0.1695 0.2506 0.1660 -0.0230 -0.0072 -0.0068 59   LYS B C   
4162 O  O   . LYS B 60  ? 0.1597 0.2566 0.1779 -0.0522 0.0123  0.0105  59   LYS B O   
4163 C  CB  . LYS B 60  ? 0.2544 0.3400 0.1332 0.0653  0.0235  -0.0161 59   LYS B CB  
4164 C  CG  . LYS B 60  ? 0.2394 0.3848 0.1661 0.0994  0.0198  -0.0833 59   LYS B CG  
4165 C  CD  . LYS B 60  ? 0.2515 0.4116 0.1902 0.0653  0.0448  -0.1042 59   LYS B CD  
4166 C  CE  . LYS B 60  ? 0.3189 0.4676 0.1846 0.0118  0.0553  -0.1152 59   LYS B CE  
4167 N  NZ  . LYS B 60  ? 0.4241 0.5421 0.1999 -0.0403 0.0204  -0.1351 59   LYS B NZ  
4168 N  N   . GLU B 61  ? 0.1653 0.2392 0.1655 0.0328  -0.0139 -0.0176 60   GLU B N   
4169 C  CA  . GLU B 61  ? 0.1744 0.2491 0.1573 0.0177  0.0161  -0.0063 60   GLU B CA  
4170 C  C   . GLU B 61  ? 0.1959 0.2412 0.1637 0.0027  0.0391  0.0099  60   GLU B C   
4171 O  O   . GLU B 61  ? 0.2700 0.2443 0.1780 0.0142  0.0085  0.0246  60   GLU B O   
4172 C  CB  . GLU B 61  ? 0.2162 0.2700 0.1400 0.0024  -0.0028 0.0084  60   GLU B CB  
4173 C  CG  . GLU B 61  ? 0.2889 0.3031 0.1194 -0.0320 0.0234  0.0279  60   GLU B CG  
4174 C  CD  . GLU B 61  ? 0.4218 0.3427 0.1532 -0.0089 0.0579  0.0163  60   GLU B CD  
4175 O  OE1 . GLU B 61  ? 0.4299 0.3249 0.1562 0.0272  0.0935  -0.0120 60   GLU B OE1 
4176 O  OE2 . GLU B 61  ? 0.4898 0.3861 0.1781 0.0176  0.0049  0.0268  60   GLU B OE2 
4177 N  N   . ALA B 62  ? 0.2266 0.2047 0.1690 0.0082  -0.0185 0.0126  61   ALA B N   
4178 C  CA  . ALA B 62  ? 0.2163 0.2256 0.1720 -0.0619 0.0116  -0.0260 61   ALA B CA  
4179 C  C   . ALA B 62  ? 0.1854 0.2347 0.1811 -0.0488 0.0029  -0.0158 61   ALA B C   
4180 O  O   . ALA B 62  ? 0.1454 0.2556 0.1736 0.0002  0.0035  0.0017  61   ALA B O   
4181 C  CB  . ALA B 62  ? 0.1535 0.2134 0.2047 -0.0724 0.0241  -0.0489 61   ALA B CB  
4182 N  N   . CYS B 63  ? 0.1975 0.2401 0.1820 -0.0348 -0.0011 0.0053  62   CYS B N   
4183 C  CA  . CYS B 63  ? 0.1829 0.2293 0.1808 -0.0360 -0.0445 0.0264  62   CYS B CA  
4184 C  C   . CYS B 63  ? 0.1625 0.2368 0.1700 -0.0224 -0.0308 0.0178  62   CYS B C   
4185 O  O   . CYS B 63  ? 0.1512 0.2374 0.1374 -0.0040 0.0010  0.0065  62   CYS B O   
4186 C  CB  . CYS B 63  ? 0.1713 0.2542 0.1841 -0.0583 0.0012  0.0080  62   CYS B CB  
4187 S  SG  . CYS B 63  ? 0.1964 0.2531 0.1934 -0.0589 0.0130  0.0091  62   CYS B SG  
4188 N  N   . ASP B 64  ? 0.1516 0.2335 0.1615 -0.0210 -0.0375 0.0014  63   ASP B N   
4189 C  CA  . ASP B 64  ? 0.1801 0.2629 0.1556 -0.0104 -0.0467 -0.0318 63   ASP B CA  
4190 C  C   . ASP B 64  ? 0.1789 0.2709 0.1509 -0.0723 -0.0004 -0.0205 63   ASP B C   
4191 O  O   . ASP B 64  ? 0.1808 0.2720 0.1502 -0.0209 0.0007  -0.0205 63   ASP B O   
4192 C  CB  . ASP B 64  ? 0.2288 0.2710 0.1407 -0.0107 -0.0825 -0.0363 63   ASP B CB  
4193 C  CG  . ASP B 64  ? 0.2861 0.2880 0.1530 0.0059  -0.0330 -0.0718 63   ASP B CG  
4194 O  OD1 . ASP B 64  ? 0.3267 0.2966 0.1522 -0.0023 -0.0097 -0.0568 63   ASP B OD1 
4195 O  OD2 . ASP B 64  ? 0.3112 0.2765 0.1805 -0.0103 -0.0380 -0.1022 63   ASP B OD2 
4196 N  N   . GLU B 65  ? 0.1012 0.2843 0.1630 -0.0648 0.0024  0.0166  64   GLU B N   
4197 C  CA  . GLU B 65  ? 0.1631 0.2834 0.1717 -0.0184 0.0033  0.0073  64   GLU B CA  
4198 C  C   . GLU B 65  ? 0.1743 0.2643 0.1971 -0.0221 0.0044  -0.0213 64   GLU B C   
4199 O  O   . GLU B 65  ? 0.1986 0.2522 0.2106 -0.0153 0.0013  -0.0428 64   GLU B O   
4200 C  CB  . GLU B 65  ? 0.2157 0.3162 0.1775 -0.0047 -0.0325 0.0313  64   GLU B CB  
4201 C  CG  . GLU B 65  ? 0.2582 0.3154 0.1625 0.0026  -0.0285 0.0440  64   GLU B CG  
4202 C  CD  . GLU B 65  ? 0.3376 0.2621 0.1914 0.0232  -0.0154 0.0104  64   GLU B CD  
4203 O  OE1 . GLU B 65  ? 0.5365 0.2792 0.2036 0.0074  -0.0173 -0.0310 64   GLU B OE1 
4204 O  OE2 . GLU B 65  ? 0.1519 0.2374 0.1970 -0.0092 0.0231  0.0020  64   GLU B OE2 
4205 N  N   . SER B 66  ? 0.2154 0.2637 0.1915 -0.0444 -0.0589 -0.0302 65   SER B N   
4206 C  CA  . SER B 66  ? 0.2184 0.2730 0.1989 -0.0084 -0.0374 -0.0498 65   SER B CA  
4207 C  C   . SER B 66  ? 0.1957 0.2565 0.2065 0.0152  -0.0609 0.0034  65   SER B C   
4208 O  O   . SER B 66  ? 0.1743 0.2603 0.2399 -0.0434 -0.0685 0.0177  65   SER B O   
4209 C  CB  . SER B 66  ? 0.3453 0.3058 0.2116 -0.0108 -0.0160 -0.0631 65   SER B CB  
4210 O  OG  . SER B 66  ? 0.3484 0.3181 0.2136 -0.0469 -0.0183 -0.0895 65   SER B OG  
4211 N  N   . ARG B 67  ? 0.2824 0.2460 0.1715 -0.0082 -0.0102 -0.0253 66   ARG B N   
4212 C  CA  . ARG B 67  ? 0.2956 0.2465 0.1563 -0.0041 0.0135  -0.0458 66   ARG B CA  
4213 C  C   . ARG B 67  ? 0.2305 0.2540 0.1531 -0.0285 -0.0038 -0.0322 66   ARG B C   
4214 O  O   . ARG B 67  ? 0.2074 0.2735 0.1677 -0.0257 -0.0682 -0.0001 66   ARG B O   
4215 C  CB  . ARG B 67  ? 0.2175 0.2490 0.1361 -0.0010 0.0475  -0.0317 66   ARG B CB  
4216 C  CG  . ARG B 67  ? 0.2847 0.2771 0.1528 0.0109  0.0945  -0.0392 66   ARG B CG  
4217 C  CD  . ARG B 67  ? 0.3299 0.2898 0.1312 -0.0026 0.0728  -0.0190 66   ARG B CD  
4218 N  NE  . ARG B 67  ? 0.3107 0.3067 0.1473 -0.0176 0.0050  -0.0092 66   ARG B NE  
4219 C  CZ  . ARG B 67  ? 0.3223 0.3199 0.1691 0.0450  0.0023  -0.0084 66   ARG B CZ  
4220 N  NH1 . ARG B 67  ? 0.2302 0.3113 0.1702 0.0333  0.0052  -0.0368 66   ARG B NH1 
4221 N  NH2 . ARG B 67  ? 0.3607 0.3345 0.1748 0.0464  -0.0338 -0.0005 66   ARG B NH2 
4222 N  N   . PHE B 68  ? 0.1820 0.2316 0.1219 -0.0233 -0.0335 0.0057  67   PHE B N   
4223 C  CA  . PHE B 68  ? 0.1698 0.2291 0.1178 -0.0481 -0.0117 -0.0112 67   PHE B CA  
4224 C  C   . PHE B 68  ? 0.1871 0.2405 0.1310 -0.0278 -0.0035 -0.0063 67   PHE B C   
4225 O  O   . PHE B 68  ? 0.2355 0.1967 0.1639 -0.0373 0.0117  -0.0119 67   PHE B O   
4226 C  CB  . PHE B 68  ? 0.1505 0.2308 0.1472 -0.0474 0.0029  0.0195  67   PHE B CB  
4227 C  CG  . PHE B 68  ? 0.1673 0.2689 0.1601 -0.0299 0.0226  0.0403  67   PHE B CG  
4228 C  CD1 . PHE B 68  ? 0.1672 0.2855 0.1875 0.0068  -0.0033 0.0398  67   PHE B CD1 
4229 C  CD2 . PHE B 68  ? 0.1796 0.2824 0.1617 -0.0108 -0.0046 0.0340  67   PHE B CD2 
4230 C  CE1 . PHE B 68  ? 0.2312 0.2713 0.1898 0.0206  -0.0152 0.0663  67   PHE B CE1 
4231 C  CE2 . PHE B 68  ? 0.1669 0.2734 0.1814 -0.0072 -0.0001 0.0639  67   PHE B CE2 
4232 C  CZ  . PHE B 68  ? 0.2558 0.2860 0.1857 0.0207  -0.0024 0.0659  67   PHE B CZ  
4233 N  N   . ASP B 69  ? 0.1220 0.2615 0.1285 -0.0237 0.0110  0.0004  68   ASP B N   
4234 C  CA  . ASP B 69  ? 0.1634 0.2445 0.1334 -0.0402 0.0036  0.0092  68   ASP B CA  
4235 C  C   . ASP B 69  ? 0.1856 0.2130 0.1297 -0.0305 -0.0087 0.0149  68   ASP B C   
4236 O  O   . ASP B 69  ? 0.1210 0.2079 0.1548 -0.0024 -0.0068 0.0152  68   ASP B O   
4237 C  CB  . ASP B 69  ? 0.0751 0.2559 0.1594 -0.0317 0.0205  -0.0004 68   ASP B CB  
4238 C  CG  . ASP B 69  ? 0.0710 0.2588 0.1902 0.0023  -0.0280 0.0017  68   ASP B CG  
4239 O  OD1 . ASP B 69  ? 0.1316 0.2408 0.1861 0.0398  -0.0651 0.0007  68   ASP B OD1 
4240 O  OD2 . ASP B 69  ? 0.1408 0.3164 0.1977 -0.0244 -0.0153 0.0304  68   ASP B OD2 
4241 N  N   . LYS B 70  ? 0.1600 0.1875 0.0885 -0.0143 -0.0517 -0.0107 69   LYS B N   
4242 C  CA  . LYS B 70  ? 0.1799 0.1464 0.0887 -0.0039 -0.0387 -0.0016 69   LYS B CA  
4243 C  C   . LYS B 70  ? 0.1633 0.1621 0.1306 -0.0293 -0.0592 0.0151  69   LYS B C   
4244 O  O   . LYS B 70  ? 0.1623 0.2170 0.1378 -0.0007 -0.0593 0.0261  69   LYS B O   
4245 C  CB  . LYS B 70  ? 0.1608 0.1559 0.0818 0.0355  -0.0081 0.0064  69   LYS B CB  
4246 C  CG  . LYS B 70  ? 0.1533 0.1865 0.0693 -0.0093 -0.0084 0.0167  69   LYS B CG  
4247 C  CD  . LYS B 70  ? 0.1672 0.1979 0.0575 0.0021  -0.0224 0.0205  69   LYS B CD  
4248 C  CE  . LYS B 70  ? 0.1786 0.1970 0.0617 0.0219  -0.0041 0.0319  69   LYS B CE  
4249 N  NZ  . LYS B 70  ? 0.1493 0.1869 0.0817 -0.0015 -0.0384 0.0032  69   LYS B NZ  
4250 N  N   . ASN B 71  ? 0.1913 0.1127 0.1399 -0.0246 -0.0442 -0.0059 70   ASN B N   
4251 C  CA  . ASN B 71  ? 0.1937 0.1120 0.1345 -0.0682 -0.0315 -0.0116 70   ASN B CA  
4252 C  C   . ASN B 71  ? 0.1423 0.1143 0.1275 -0.0243 -0.0070 0.0150  70   ASN B C   
4253 O  O   . ASN B 71  ? 0.1338 0.1483 0.1707 -0.0123 -0.0380 0.0020  70   ASN B O   
4254 C  CB  . ASN B 71  ? 0.1769 0.1142 0.1600 -0.0164 -0.0150 -0.0039 70   ASN B CB  
4255 C  CG  . ASN B 71  ? 0.2157 0.1284 0.1849 -0.0238 0.0094  0.0293  70   ASN B CG  
4256 O  OD1 . ASN B 71  ? 0.2443 0.1309 0.2135 0.0336  -0.0055 0.0254  70   ASN B OD1 
4257 N  ND2 . ASN B 71  ? 0.1764 0.1510 0.1914 0.0021  -0.0200 0.0323  70   ASN B ND2 
4258 N  N   . LEU B 72  ? 0.1460 0.1524 0.1339 0.0173  -0.0171 -0.0071 71   LEU B N   
4259 C  CA  . LEU B 72  ? 0.1611 0.1544 0.1574 -0.0056 0.0058  -0.0163 71   LEU B CA  
4260 C  C   . LEU B 72  ? 0.1437 0.1758 0.1715 -0.0244 -0.0169 -0.0226 71   LEU B C   
4261 O  O   . LEU B 72  ? 0.1887 0.1815 0.1843 0.0054  -0.0212 -0.0115 71   LEU B O   
4262 C  CB  . LEU B 72  ? 0.1604 0.1661 0.1781 0.0578  0.0106  0.0264  71   LEU B CB  
4263 C  CG  . LEU B 72  ? 0.2178 0.1841 0.1950 0.0506  0.0214  0.0106  71   LEU B CG  
4264 C  CD1 . LEU B 72  ? 0.2605 0.2037 0.1946 0.1010  -0.0141 0.0015  71   LEU B CD1 
4265 C  CD2 . LEU B 72  ? 0.1629 0.1395 0.1948 0.0063  0.0080  -0.0075 71   LEU B CD2 
4266 N  N   . SER B 73  ? 0.0968 0.1789 0.1869 -0.0293 -0.0402 -0.0284 72   SER B N   
4267 C  CA  . SER B 73  ? 0.1234 0.2097 0.1560 -0.0142 -0.0269 -0.0180 72   SER B CA  
4268 C  C   . SER B 73  ? 0.1471 0.1676 0.1855 -0.0040 -0.0237 -0.0174 72   SER B C   
4269 O  O   . SER B 73  ? 0.1631 0.1994 0.1968 0.0153  -0.0192 -0.0142 72   SER B O   
4270 C  CB  . SER B 73  ? 0.1832 0.2050 0.1325 0.0051  -0.0242 0.0011  72   SER B CB  
4271 O  OG  . SER B 73  ? 0.1787 0.1848 0.1214 -0.0176 -0.0078 -0.0181 72   SER B OG  
4272 N  N   . GLN B 74  ? 0.2072 0.1678 0.1900 -0.0409 -0.0044 -0.0280 73   GLN B N   
4273 C  CA  . GLN B 74  ? 0.2321 0.1408 0.2122 -0.0585 -0.0157 -0.0219 73   GLN B CA  
4274 C  C   . GLN B 74  ? 0.2259 0.1345 0.2021 -0.0356 -0.0461 -0.0175 73   GLN B C   
4275 O  O   . GLN B 74  ? 0.2270 0.1391 0.2009 0.0069  -0.0379 -0.0384 73   GLN B O   
4276 C  CB  . GLN B 74  ? 0.2717 0.1134 0.2224 0.0250  0.0110  -0.0325 73   GLN B CB  
4277 C  CG  . GLN B 74  ? 0.2782 0.2061 0.2812 0.0247  -0.0062 -0.0044 73   GLN B CG  
4278 C  CD  . GLN B 74  ? 0.3524 0.2952 0.3279 0.0511  -0.0146 0.0198  73   GLN B CD  
4279 O  OE1 . GLN B 74  ? 0.4038 0.3237 0.3708 -0.0003 -0.0258 0.0056  73   GLN B OE1 
4280 N  NE2 . GLN B 74  ? 0.2733 0.3370 0.3440 0.1211  -0.0345 0.0680  73   GLN B NE2 
4281 N  N   . ALA B 75  ? 0.1765 0.1502 0.2057 0.0310  -0.0431 0.0187  74   ALA B N   
4282 C  CA  . ALA B 75  ? 0.1413 0.1521 0.1852 0.0216  0.0179  0.0316  74   ALA B CA  
4283 C  C   . ALA B 75  ? 0.1364 0.1664 0.2119 -0.0114 -0.0084 -0.0042 74   ALA B C   
4284 O  O   . ALA B 75  ? 0.2462 0.1726 0.2030 -0.0110 -0.0277 0.0197  74   ALA B O   
4285 C  CB  . ALA B 75  ? 0.1749 0.1520 0.1743 0.0328  0.0329  0.0072  74   ALA B CB  
4286 N  N   . LEU B 76  ? 0.1427 0.1487 0.2026 -0.0041 -0.0462 -0.0112 75   LEU B N   
4287 C  CA  . LEU B 76  ? 0.1053 0.1543 0.1854 -0.0037 -0.0020 -0.0089 75   LEU B CA  
4288 C  C   . LEU B 76  ? 0.1588 0.1549 0.1900 0.0243  -0.0290 -0.0046 75   LEU B C   
4289 O  O   . LEU B 76  ? 0.1509 0.1594 0.1845 0.0005  0.0002  0.0147  75   LEU B O   
4290 C  CB  . LEU B 76  ? 0.2020 0.1122 0.1914 -0.0013 0.0580  -0.0138 75   LEU B CB  
4291 C  CG  . LEU B 76  ? 0.2084 0.1112 0.1785 0.0181  -0.0151 -0.0069 75   LEU B CG  
4292 C  CD1 . LEU B 76  ? 0.2049 0.0945 0.1911 -0.0089 0.0167  -0.0193 75   LEU B CD1 
4293 C  CD2 . LEU B 76  ? 0.2089 0.1243 0.2037 0.0364  -0.0405 0.0329  75   LEU B CD2 
4294 N  N   . LYS B 77  ? 0.1245 0.1398 0.2131 0.0360  -0.0399 -0.0333 76   LYS B N   
4295 C  CA  . LYS B 77  ? 0.1617 0.2010 0.2024 0.0138  -0.0153 -0.0086 76   LYS B CA  
4296 C  C   . LYS B 77  ? 0.1649 0.1924 0.2020 0.0339  -0.0247 -0.0388 76   LYS B C   
4297 O  O   . LYS B 77  ? 0.1263 0.1943 0.2310 0.0456  0.0134  -0.0497 76   LYS B O   
4298 C  CB  . LYS B 77  ? 0.1829 0.2216 0.1834 -0.0099 -0.0315 0.0278  76   LYS B CB  
4299 C  CG  . LYS B 77  ? 0.2410 0.2253 0.1767 0.0057  -0.1006 0.0452  76   LYS B CG  
4300 C  CD  . LYS B 77  ? 0.3239 0.2406 0.1954 0.0174  -0.1284 0.0433  76   LYS B CD  
4301 C  CE  . LYS B 77  ? 0.4180 0.2520 0.2399 0.0354  -0.1539 0.0434  76   LYS B CE  
4302 N  NZ  . LYS B 77  ? 0.5129 0.2214 0.2637 0.0379  -0.1561 0.0430  76   LYS B NZ  
4303 N  N   . PHE B 78  ? 0.1812 0.1553 0.1947 0.0278  -0.0655 -0.0237 77   PHE B N   
4304 C  CA  . PHE B 78  ? 0.2343 0.1810 0.2054 -0.0654 -0.0462 -0.0164 77   PHE B CA  
4305 C  C   . PHE B 78  ? 0.2518 0.2003 0.1961 -0.0319 -0.0390 -0.0125 77   PHE B C   
4306 O  O   . PHE B 78  ? 0.2019 0.2427 0.2001 -0.0425 -0.0180 -0.0035 77   PHE B O   
4307 C  CB  . PHE B 78  ? 0.1977 0.1759 0.2479 -0.0477 -0.0441 0.0017  77   PHE B CB  
4308 C  CG  . PHE B 78  ? 0.2601 0.1795 0.2590 -0.0332 -0.0107 -0.0274 77   PHE B CG  
4309 C  CD1 . PHE B 78  ? 0.3244 0.1810 0.2855 -0.0595 -0.0244 -0.0050 77   PHE B CD1 
4310 C  CD2 . PHE B 78  ? 0.3031 0.1588 0.2380 -0.0460 -0.0136 -0.0281 77   PHE B CD2 
4311 C  CE1 . PHE B 78  ? 0.4568 0.2305 0.2892 -0.0147 0.0012  -0.0051 77   PHE B CE1 
4312 C  CE2 . PHE B 78  ? 0.3831 0.2171 0.2706 -0.0090 -0.0604 -0.0212 77   PHE B CE2 
4313 C  CZ  . PHE B 78  ? 0.4723 0.2250 0.2910 -0.0113 -0.0246 -0.0133 77   PHE B CZ  
4314 N  N   . VAL B 79  ? 0.2554 0.1515 0.1874 -0.0472 -0.0417 0.0288  78   VAL B N   
4315 C  CA  . VAL B 79  ? 0.1834 0.1616 0.2211 -0.0035 0.0087  -0.0061 78   VAL B CA  
4316 C  C   . VAL B 79  ? 0.1572 0.1851 0.2204 -0.0064 -0.0024 -0.0126 78   VAL B C   
4317 O  O   . VAL B 79  ? 0.1766 0.2007 0.1732 -0.0209 -0.0149 -0.0132 78   VAL B O   
4318 C  CB  . VAL B 79  ? 0.1747 0.1570 0.2351 0.0018  0.0272  0.0086  78   VAL B CB  
4319 C  CG1 . VAL B 79  ? 0.2130 0.1257 0.2479 0.0188  0.0308  -0.0162 78   VAL B CG1 
4320 C  CG2 . VAL B 79  ? 0.0724 0.1722 0.2369 -0.0067 -0.0079 0.0219  78   VAL B CG2 
4321 N  N   . ARG B 80  ? 0.1393 0.2007 0.2318 0.0170  -0.0379 -0.0202 79   ARG B N   
4322 C  CA  . ARG B 80  ? 0.0870 0.2246 0.2356 0.0302  -0.0514 -0.0203 79   ARG B CA  
4323 C  C   . ARG B 80  ? 0.1692 0.2163 0.2365 0.0558  -0.0539 -0.0316 79   ARG B C   
4324 O  O   . ARG B 80  ? 0.1782 0.2200 0.2196 0.0757  -0.0463 -0.0177 79   ARG B O   
4325 C  CB  . ARG B 80  ? 0.0932 0.2051 0.2154 0.0013  -0.0675 -0.0182 79   ARG B CB  
4326 C  CG  . ARG B 80  ? 0.1253 0.2185 0.2080 -0.0411 -0.0774 -0.0263 79   ARG B CG  
4327 C  CD  . ARG B 80  ? 0.0996 0.2278 0.2141 -0.0208 -0.0696 -0.0181 79   ARG B CD  
4328 N  NE  . ARG B 80  ? 0.1438 0.2338 0.2556 -0.0388 -0.0791 -0.0431 79   ARG B NE  
4329 C  CZ  . ARG B 80  ? 0.1273 0.2303 0.2529 0.0055  -0.0325 -0.0235 79   ARG B CZ  
4330 N  NH1 . ARG B 80  ? 0.1449 0.1988 0.2409 0.0469  -0.0204 0.0044  79   ARG B NH1 
4331 N  NH2 . ARG B 80  ? 0.1674 0.2500 0.2655 0.0733  -0.0031 -0.0131 79   ARG B NH2 
4332 N  N   . ASP B 81  ? 0.2316 0.1817 0.2228 0.0314  -0.0365 -0.0065 80   ASP B N   
4333 C  CA  . ASP B 81  ? 0.2595 0.1944 0.2431 0.0063  0.0099  -0.0245 80   ASP B CA  
4334 C  C   . ASP B 81  ? 0.2880 0.2060 0.2263 0.0133  0.0077  -0.0482 80   ASP B C   
4335 O  O   . ASP B 81  ? 0.2704 0.2383 0.2476 0.0586  0.0259  -0.0822 80   ASP B O   
4336 C  CB  . ASP B 81  ? 0.3444 0.1733 0.2798 -0.0347 0.0006  -0.0277 80   ASP B CB  
4337 C  CG  . ASP B 81  ? 0.3832 0.1963 0.3583 -0.0760 -0.0202 -0.0036 80   ASP B CG  
4338 O  OD1 . ASP B 81  ? 0.4027 0.2245 0.3850 -0.0763 -0.0350 0.0091  80   ASP B OD1 
4339 O  OD2 . ASP B 81  ? 0.5163 0.1828 0.3906 -0.0686 0.0039  0.0337  80   ASP B OD2 
4340 N  N   . PHE B 82  ? 0.2866 0.1842 0.1820 -0.0101 -0.0443 -0.0238 81   PHE B N   
4341 C  CA  . PHE B 82  ? 0.2469 0.1984 0.1680 0.0035  -0.0541 -0.0070 81   PHE B CA  
4342 C  C   . PHE B 82  ? 0.2618 0.2026 0.1632 0.0091  -0.0369 0.0133  81   PHE B C   
4343 O  O   . PHE B 82  ? 0.2129 0.2092 0.1667 0.0268  0.0100  0.0341  81   PHE B O   
4344 C  CB  . PHE B 82  ? 0.2333 0.2221 0.1545 -0.0194 -0.0062 -0.0123 81   PHE B CB  
4345 C  CG  . PHE B 82  ? 0.2138 0.2237 0.1630 -0.0308 -0.0179 -0.0049 81   PHE B CG  
4346 C  CD1 . PHE B 82  ? 0.2486 0.2314 0.1944 -0.0623 -0.0107 -0.0394 81   PHE B CD1 
4347 C  CD2 . PHE B 82  ? 0.2634 0.2475 0.1675 -0.0160 -0.0180 -0.0011 81   PHE B CD2 
4348 C  CE1 . PHE B 82  ? 0.2554 0.2115 0.2072 -0.0400 -0.0512 -0.0159 81   PHE B CE1 
4349 C  CE2 . PHE B 82  ? 0.2591 0.2488 0.2097 -0.0298 -0.0938 0.0216  81   PHE B CE2 
4350 C  CZ  . PHE B 82  ? 0.2714 0.2587 0.2173 -0.0284 -0.0778 0.0083  81   PHE B CZ  
4351 N  N   . ALA B 83  ? 0.1994 0.1830 0.1335 -0.0186 -0.0326 -0.0052 82   ALA B N   
4352 C  CA  . ALA B 83  ? 0.1883 0.2173 0.1578 -0.0226 0.0132  -0.0269 82   ALA B CA  
4353 C  C   . ALA B 83  ? 0.1664 0.1990 0.1602 -0.0444 0.0055  -0.0282 82   ALA B C   
4354 O  O   . ALA B 83  ? 0.1657 0.1959 0.1658 -0.0377 0.0006  -0.0051 82   ALA B O   
4355 C  CB  . ALA B 83  ? 0.1346 0.2199 0.1516 0.0052  0.0446  -0.0383 82   ALA B CB  
4356 N  N   . GLY B 84  ? 0.1369 0.1979 0.1786 -0.0125 0.0005  -0.0281 83   GLY B N   
4357 C  CA  . GLY B 84  ? 0.1256 0.1739 0.1900 -0.0279 -0.0511 -0.0376 83   GLY B CA  
4358 C  C   . GLY B 84  ? 0.1779 0.1829 0.2066 0.0018  -0.0473 -0.0159 83   GLY B C   
4359 O  O   . GLY B 84  ? 0.2069 0.2094 0.2152 0.0421  -0.0091 -0.0108 83   GLY B O   
4360 N  N   . ASP B 85  ? 0.1267 0.1523 0.1984 -0.0156 -0.0286 -0.0009 84   ASP B N   
4361 C  CA  . ASP B 85  ? 0.1057 0.1543 0.1974 -0.0104 -0.0432 0.0152  84   ASP B CA  
4362 C  C   . ASP B 85  ? 0.1595 0.2071 0.1911 -0.0177 -0.0052 0.0165  84   ASP B C   
4363 O  O   . ASP B 85  ? 0.1156 0.2423 0.1996 -0.0334 0.0257  0.0219  84   ASP B O   
4364 C  CB  . ASP B 85  ? 0.0604 0.1693 0.2203 -0.0182 0.0136  0.0131  84   ASP B CB  
4365 C  CG  . ASP B 85  ? 0.0650 0.2063 0.2049 -0.0136 -0.0374 0.0037  84   ASP B CG  
4366 O  OD1 . ASP B 85  ? 0.1980 0.2130 0.1875 -0.0123 -0.0686 0.0131  84   ASP B OD1 
4367 O  OD2 . ASP B 85  ? 0.1085 0.2111 0.2685 -0.0382 -0.0518 0.0227  84   ASP B OD2 
4368 N  N   . GLY B 86  ? 0.1428 0.2116 0.1710 0.0240  0.0273  0.0007  85   GLY B N   
4369 C  CA  . GLY B 86  ? 0.0875 0.2132 0.1527 0.0624  0.0106  -0.0104 85   GLY B CA  
4370 C  C   . GLY B 86  ? 0.1042 0.1942 0.1488 0.0283  0.0407  -0.0109 85   GLY B C   
4371 O  O   . GLY B 86  ? 0.1716 0.1920 0.1287 -0.0182 -0.0169 0.0389  85   GLY B O   
4372 N  N   . LEU B 87  ? 0.1203 0.1498 0.1444 0.0524  0.0205  -0.0229 86   LEU B N   
4373 C  CA  . LEU B 87  ? 0.1219 0.1257 0.1700 0.0152  0.0008  -0.0070 86   LEU B CA  
4374 C  C   . LEU B 87  ? 0.1667 0.1404 0.1685 0.0045  -0.0371 0.0253  86   LEU B C   
4375 O  O   . LEU B 87  ? 0.1901 0.1895 0.1423 -0.0455 0.0082  0.0240  86   LEU B O   
4376 C  CB  . LEU B 87  ? 0.2101 0.0997 0.1827 -0.0295 -0.0107 -0.0034 86   LEU B CB  
4377 C  CG  . LEU B 87  ? 0.2159 0.0948 0.1865 -0.0171 0.0068  0.0106  86   LEU B CG  
4378 C  CD1 . LEU B 87  ? 0.2642 0.0797 0.1911 -0.0025 0.0258  0.0367  86   LEU B CD1 
4379 C  CD2 . LEU B 87  ? 0.1339 0.1400 0.1894 -0.0153 -0.0119 0.0249  86   LEU B CD2 
4380 N  N   . ALA B 88  ? 0.1137 0.1250 0.1863 -0.0314 -0.0189 0.0128  87   ALA B N   
4381 C  CA  . ALA B 88  ? 0.0745 0.1830 0.1709 -0.0519 -0.0181 -0.0011 87   ALA B CA  
4382 C  C   . ALA B 88  ? 0.1945 0.1450 0.1636 -0.0146 -0.0013 -0.0144 87   ALA B C   
4383 O  O   . ALA B 88  ? 0.2043 0.1314 0.1574 0.0030  0.0138  -0.0068 87   ALA B O   
4384 C  CB  . ALA B 88  ? 0.0841 0.2363 0.1715 -0.0568 -0.0120 -0.0024 87   ALA B CB  
4385 N  N   . THR B 89  ? 0.1406 0.1317 0.1679 0.0036  -0.0060 0.0075  88   THR B N   
4386 C  CA  . THR B 89  ? 0.1406 0.1201 0.1503 -0.0038 -0.0214 0.0042  88   THR B CA  
4387 C  C   . THR B 89  ? 0.1573 0.1358 0.1592 -0.0233 -0.0316 -0.0132 88   THR B C   
4388 O  O   . THR B 89  ? 0.1378 0.1876 0.1944 -0.0063 -0.0277 -0.0088 88   THR B O   
4389 C  CB  . THR B 89  ? 0.1226 0.1652 0.1693 -0.0151 -0.0044 0.0053  88   THR B CB  
4390 O  OG1 . THR B 89  ? 0.1429 0.2052 0.1611 0.0210  0.0083  -0.0247 88   THR B OG1 
4391 C  CG2 . THR B 89  ? 0.1203 0.1908 0.1512 -0.0140 -0.0202 0.0169  88   THR B CG2 
4392 N  N   . SER B 90  ? 0.0918 0.1410 0.1850 -0.0421 -0.0162 0.0009  89   SER B N   
4393 C  CA  . SER B 90  ? 0.0817 0.1585 0.1920 -0.0508 -0.0254 0.0235  89   SER B CA  
4394 C  C   . SER B 90  ? 0.1130 0.1679 0.1653 0.0235  -0.0145 0.0210  89   SER B C   
4395 O  O   . SER B 90  ? 0.1492 0.1817 0.1568 0.0053  -0.0130 -0.0241 89   SER B O   
4396 C  CB  . SER B 90  ? 0.1305 0.1369 0.2920 0.0079  -0.0590 0.0112  89   SER B CB  
4397 O  OG  . SER B 90  ? 0.2817 0.2061 0.3082 -0.0410 -0.0211 -0.0133 89   SER B OG  
4398 N  N   . TRP B 91  ? 0.1407 0.1578 0.1408 0.0293  -0.0314 0.0288  90   TRP B N   
4399 C  CA  . TRP B 91  ? 0.1655 0.1359 0.1592 0.0309  -0.0220 0.0418  90   TRP B CA  
4400 C  C   . TRP B 91  ? 0.1497 0.1259 0.1519 0.0311  0.0336  0.0175  90   TRP B C   
4401 O  O   . TRP B 91  ? 0.1777 0.1412 0.1634 -0.0016 -0.0073 0.0411  90   TRP B O   
4402 C  CB  . TRP B 91  ? 0.1739 0.1421 0.1910 0.0376  -0.0389 0.0550  90   TRP B CB  
4403 C  CG  . TRP B 91  ? 0.1903 0.1472 0.1849 0.0183  -0.0136 0.0034  90   TRP B CG  
4404 C  CD1 . TRP B 91  ? 0.1229 0.1468 0.2072 0.0257  -0.0175 0.0174  90   TRP B CD1 
4405 C  CD2 . TRP B 91  ? 0.2032 0.1499 0.1939 -0.0311 -0.0193 0.0210  90   TRP B CD2 
4406 N  NE1 . TRP B 91  ? 0.1726 0.1468 0.1837 -0.0263 -0.0043 0.0649  90   TRP B NE1 
4407 C  CE2 . TRP B 91  ? 0.1814 0.1491 0.1910 -0.0097 -0.0206 0.0400  90   TRP B CE2 
4408 C  CE3 . TRP B 91  ? 0.2020 0.1467 0.2186 0.0156  -0.0314 0.0294  90   TRP B CE3 
4409 C  CZ2 . TRP B 91  ? 0.1835 0.1644 0.1941 -0.0379 0.0021  0.0196  90   TRP B CZ2 
4410 C  CZ3 . TRP B 91  ? 0.2034 0.1384 0.1955 0.0260  -0.0511 -0.0035 90   TRP B CZ3 
4411 C  CH2 . TRP B 91  ? 0.1675 0.1536 0.1928 -0.0019 -0.0119 0.0039  90   TRP B CH2 
4412 N  N   . THR B 92  ? 0.1222 0.1257 0.1507 0.0069  -0.0050 -0.0015 91   THR B N   
4413 C  CA  . THR B 92  ? 0.1632 0.1196 0.1773 0.0377  0.0212  0.0067  91   THR B CA  
4414 C  C   . THR B 92  ? 0.1836 0.1401 0.2183 0.0070  -0.0137 0.0150  91   THR B C   
4415 O  O   . THR B 92  ? 0.1652 0.1776 0.2165 -0.0044 -0.0479 0.0302  91   THR B O   
4416 C  CB  . THR B 92  ? 0.1549 0.1308 0.1829 -0.0186 0.0219  0.0044  91   THR B CB  
4417 O  OG1 . THR B 92  ? 0.1788 0.1570 0.1483 -0.0118 -0.0011 0.0214  91   THR B OG1 
4418 C  CG2 . THR B 92  ? 0.1810 0.1536 0.1897 -0.0030 0.0539  0.0062  91   THR B CG2 
4419 N  N   . HIS B 93  ? 0.0912 0.1207 0.2194 0.0094  -0.0159 0.0172  92   HIS B N   
4420 C  CA  . HIS B 93  ? 0.1175 0.1311 0.1796 0.0242  0.0105  0.0493  92   HIS B CA  
4421 C  C   . HIS B 93  ? 0.1452 0.1499 0.1817 -0.0153 -0.0066 0.0177  92   HIS B C   
4422 O  O   . HIS B 93  ? 0.1525 0.1412 0.1929 0.0156  -0.0027 0.0128  92   HIS B O   
4423 C  CB  . HIS B 93  ? 0.1390 0.1114 0.2048 0.0084  -0.0376 0.0692  92   HIS B CB  
4424 C  CG  . HIS B 93  ? 0.1731 0.1155 0.1894 -0.0330 -0.0140 0.0376  92   HIS B CG  
4425 N  ND1 . HIS B 93  ? 0.1970 0.1399 0.1999 -0.0055 -0.0135 0.0376  92   HIS B ND1 
4426 C  CD2 . HIS B 93  ? 0.2279 0.1093 0.1830 -0.0431 -0.0377 0.0042  92   HIS B CD2 
4427 C  CE1 . HIS B 93  ? 0.2675 0.1588 0.2069 0.0250  -0.0170 0.0395  92   HIS B CE1 
4428 N  NE2 . HIS B 93  ? 0.2623 0.1379 0.1761 0.0247  -0.0002 0.0109  92   HIS B NE2 
4429 N  N   . GLU B 94  ? 0.2075 0.1287 0.1632 -0.0425 -0.0360 0.0345  93   GLU B N   
4430 C  CA  . GLU B 94  ? 0.2550 0.1418 0.1617 -0.0957 -0.0203 0.0319  93   GLU B CA  
4431 C  C   . GLU B 94  ? 0.1536 0.1564 0.1682 -0.0568 -0.0197 0.0280  93   GLU B C   
4432 O  O   . GLU B 94  ? 0.1421 0.1604 0.1787 0.0107  -0.0202 0.0162  93   GLU B O   
4433 C  CB  . GLU B 94  ? 0.2344 0.1115 0.1691 -0.0292 -0.0314 0.0151  93   GLU B CB  
4434 C  CG  . GLU B 94  ? 0.2188 0.1259 0.1663 0.0173  -0.0500 0.0337  93   GLU B CG  
4435 C  CD  . GLU B 94  ? 0.2162 0.1607 0.2005 0.0353  -0.0209 0.0169  93   GLU B CD  
4436 O  OE1 . GLU B 94  ? 0.2280 0.1640 0.1893 0.0756  -0.0231 0.0102  93   GLU B OE1 
4437 O  OE2 . GLU B 94  ? 0.1983 0.2051 0.2486 0.0335  -0.0167 -0.0120 93   GLU B OE2 
4438 N  N   . LYS B 95  ? 0.1615 0.1783 0.1875 -0.0220 -0.0241 0.0542  94   LYS B N   
4439 C  CA  . LYS B 95  ? 0.0744 0.1876 0.1729 -0.0384 -0.0080 0.0587  94   LYS B CA  
4440 C  C   . LYS B 95  ? 0.1503 0.1992 0.1856 -0.0007 -0.0252 0.0327  94   LYS B C   
4441 O  O   . LYS B 95  ? 0.1363 0.2116 0.1688 -0.0386 -0.0267 0.0455  94   LYS B O   
4442 C  CB  . LYS B 95  ? 0.0842 0.1882 0.1965 -0.0548 0.0001  0.0343  94   LYS B CB  
4443 C  CG  . LYS B 95  ? 0.1142 0.2023 0.2231 -0.0668 0.0456  0.0280  94   LYS B CG  
4444 C  CD  . LYS B 95  ? 0.1436 0.2181 0.2713 -0.0808 0.0515  0.0343  94   LYS B CD  
4445 C  CE  . LYS B 95  ? 0.1727 0.2271 0.3263 0.0064  0.0832  0.0160  94   LYS B CE  
4446 N  NZ  . LYS B 95  ? 0.2227 0.2223 0.3388 0.0183  0.0560  -0.0121 94   LYS B NZ  
4447 N  N   . ASN B 96  ? 0.1314 0.1856 0.1778 0.0169  -0.0291 0.0115  95   ASN B N   
4448 C  CA  . ASN B 96  ? 0.1669 0.1848 0.1825 0.0274  0.0182  -0.0038 95   ASN B CA  
4449 C  C   . ASN B 96  ? 0.1330 0.1956 0.1768 0.0170  0.0174  0.0030  95   ASN B C   
4450 O  O   . ASN B 96  ? 0.1557 0.2099 0.1665 0.0009  -0.0196 0.0091  95   ASN B O   
4451 C  CB  . ASN B 96  ? 0.1855 0.1958 0.1852 -0.0061 0.0618  -0.0058 95   ASN B CB  
4452 C  CG  . ASN B 96  ? 0.1878 0.1965 0.2266 -0.0450 0.0478  0.0085  95   ASN B CG  
4453 O  OD1 . ASN B 96  ? 0.2432 0.2011 0.2496 -0.0426 0.1048  -0.0230 95   ASN B OD1 
4454 N  ND2 . ASN B 96  ? 0.1843 0.1991 0.2005 0.0479  -0.0091 0.0368  95   ASN B ND2 
4455 N  N   . TRP B 97  ? 0.0904 0.1987 0.1808 -0.0121 0.0300  0.0047  96   TRP B N   
4456 C  CA  . TRP B 97  ? 0.1143 0.1647 0.1798 -0.0590 0.0035  0.0208  96   TRP B CA  
4457 C  C   . TRP B 97  ? 0.1043 0.1507 0.1798 -0.0565 -0.0449 -0.0099 96   TRP B C   
4458 O  O   . TRP B 97  ? 0.1368 0.1251 0.2144 -0.0187 -0.0345 -0.0018 96   TRP B O   
4459 C  CB  . TRP B 97  ? 0.1464 0.1553 0.1537 -0.0010 -0.0216 0.0382  96   TRP B CB  
4460 C  CG  . TRP B 97  ? 0.0954 0.1814 0.1477 -0.0062 -0.0136 0.0101  96   TRP B CG  
4461 C  CD1 . TRP B 97  ? 0.1163 0.2027 0.1782 -0.0346 0.0262  -0.0011 96   TRP B CD1 
4462 C  CD2 . TRP B 97  ? 0.1502 0.2096 0.1418 -0.0527 0.0005  -0.0008 96   TRP B CD2 
4463 N  NE1 . TRP B 97  ? 0.1304 0.2053 0.1405 -0.0119 -0.0065 -0.0077 96   TRP B NE1 
4464 C  CE2 . TRP B 97  ? 0.1370 0.2145 0.1157 -0.0320 -0.0120 0.0106  96   TRP B CE2 
4465 C  CE3 . TRP B 97  ? 0.1560 0.2093 0.1475 -0.0188 -0.0077 -0.0361 96   TRP B CE3 
4466 C  CZ2 . TRP B 97  ? 0.1607 0.2172 0.1430 -0.0242 -0.0256 0.0126  96   TRP B CZ2 
4467 C  CZ3 . TRP B 97  ? 0.1573 0.2489 0.1377 -0.0290 0.0446  -0.0017 96   TRP B CZ3 
4468 C  CH2 . TRP B 97  ? 0.1440 0.2389 0.1661 0.0032  0.0490  -0.0188 96   TRP B CH2 
4469 N  N   . LYS B 98  ? 0.1086 0.1409 0.1832 -0.0692 -0.0198 -0.0156 97   LYS B N   
4470 C  CA  . LYS B 98  ? 0.1345 0.1387 0.1931 -0.0759 -0.0273 -0.0154 97   LYS B CA  
4471 C  C   . LYS B 98  ? 0.1533 0.1533 0.2021 -0.0587 -0.0276 0.0078  97   LYS B C   
4472 O  O   . LYS B 98  ? 0.1267 0.1444 0.2077 -0.0322 -0.0187 0.0089  97   LYS B O   
4473 C  CB  . LYS B 98  ? 0.2391 0.1333 0.1980 -0.0797 -0.0528 -0.0215 97   LYS B CB  
4474 C  CG  . LYS B 98  ? 0.2294 0.1872 0.2541 -0.0604 0.0132  -0.0012 97   LYS B CG  
4475 C  CD  . LYS B 98  ? 0.3643 0.2187 0.2905 -0.0451 0.0219  -0.0105 97   LYS B CD  
4476 C  CE  . LYS B 98  ? 0.4099 0.2868 0.2870 -0.0106 -0.0154 -0.0207 97   LYS B CE  
4477 N  NZ  . LYS B 98  ? 0.5579 0.3075 0.2939 0.0218  -0.0372 -0.0305 97   LYS B NZ  
4478 N  N   . LYS B 99  ? 0.1408 0.1473 0.1854 -0.0292 0.0093  0.0002  98   LYS B N   
4479 C  CA  . LYS B 99  ? 0.1075 0.1557 0.2090 0.0076  0.0123  0.0007  98   LYS B CA  
4480 C  C   . LYS B 99  ? 0.1158 0.1521 0.2146 -0.0212 0.0000  -0.0078 98   LYS B C   
4481 O  O   . LYS B 99  ? 0.1753 0.1694 0.2207 0.0117  -0.0051 0.0016  98   LYS B O   
4482 C  CB  . LYS B 99  ? 0.1363 0.2052 0.2435 0.0189  0.0102  -0.0166 98   LYS B CB  
4483 C  CG  . LYS B 99  ? 0.1712 0.2510 0.2736 -0.0030 0.0100  -0.0150 98   LYS B CG  
4484 C  CD  . LYS B 99  ? 0.0997 0.2437 0.2740 -0.0054 0.0298  -0.0319 98   LYS B CD  
4485 C  CE  . LYS B 99  ? 0.1223 0.2605 0.2504 0.0297  0.0131  -0.0187 98   LYS B CE  
4486 N  NZ  . LYS B 99  ? 0.1613 0.2368 0.2550 0.0207  0.0411  -0.0383 98   LYS B NZ  
4487 N  N   . ALA B 100 ? 0.1054 0.1711 0.2024 -0.0577 -0.0104 -0.0096 99   ALA B N   
4488 C  CA  . ALA B 100 ? 0.1389 0.1686 0.1625 -0.0060 -0.0805 -0.0008 99   ALA B CA  
4489 C  C   . ALA B 100 ? 0.1790 0.1558 0.1788 0.0238  -0.0641 0.0038  99   ALA B C   
4490 O  O   . ALA B 100 ? 0.1412 0.1788 0.2090 0.0023  -0.0261 -0.0040 99   ALA B O   
4491 C  CB  . ALA B 100 ? 0.1472 0.1611 0.1787 -0.0190 -0.0355 -0.0138 99   ALA B CB  
4492 N  N   . HIS B 101 ? 0.1663 0.1293 0.1773 -0.0075 -0.0233 -0.0183 100  HIS B N   
4493 C  CA  . HIS B 101 ? 0.2007 0.1136 0.2299 -0.0026 0.0035  -0.0025 100  HIS B CA  
4494 C  C   . HIS B 101 ? 0.1446 0.0996 0.2635 0.0061  -0.0467 0.0142  100  HIS B C   
4495 O  O   . HIS B 101 ? 0.1722 0.1295 0.2927 -0.0148 -0.0125 0.0294  100  HIS B O   
4496 C  CB  . HIS B 101 ? 0.1635 0.1184 0.2389 0.0595  0.0150  -0.0003 100  HIS B CB  
4497 C  CG  . HIS B 101 ? 0.2192 0.2016 0.2828 0.0833  -0.0069 -0.0393 100  HIS B CG  
4498 N  ND1 . HIS B 101 ? 0.1630 0.2417 0.2875 0.0301  -0.0169 -0.0597 100  HIS B ND1 
4499 C  CD2 . HIS B 101 ? 0.2772 0.2725 0.3135 0.0937  -0.0052 -0.0793 100  HIS B CD2 
4500 C  CE1 . HIS B 101 ? 0.2257 0.2569 0.3103 -0.0054 -0.0747 -0.0701 100  HIS B CE1 
4501 N  NE2 . HIS B 101 ? 0.3401 0.2786 0.3394 0.0609  -0.0597 -0.0854 100  HIS B NE2 
4502 N  N   . ASN B 102 ? 0.0914 0.1279 0.2467 -0.0165 -0.0358 -0.0087 101  ASN B N   
4503 C  CA  . ASN B 102 ? 0.1923 0.1496 0.2544 -0.0621 -0.0296 0.0095  101  ASN B CA  
4504 C  C   . ASN B 102 ? 0.1874 0.1546 0.2606 -0.0528 -0.0151 0.0362  101  ASN B C   
4505 O  O   . ASN B 102 ? 0.1626 0.1651 0.2900 -0.0499 -0.0281 0.0589  101  ASN B O   
4506 C  CB  . ASN B 102 ? 0.0728 0.1889 0.2317 -0.0211 -0.0365 0.0042  101  ASN B CB  
4507 C  CG  . ASN B 102 ? 0.1493 0.2266 0.2394 -0.0168 0.0231  -0.0204 101  ASN B CG  
4508 O  OD1 . ASN B 102 ? 0.1274 0.2536 0.2597 -0.0135 0.0078  -0.0168 101  ASN B OD1 
4509 N  ND2 . ASN B 102 ? 0.1945 0.2262 0.2133 -0.0279 0.0047  -0.0085 101  ASN B ND2 
4510 N  N   . ILE B 103 ? 0.1449 0.1526 0.2457 -0.0456 -0.0193 0.0443  102  ILE B N   
4511 C  CA  . ILE B 103 ? 0.1190 0.1786 0.2392 0.0175  0.0012  0.0626  102  ILE B CA  
4512 C  C   . ILE B 103 ? 0.1314 0.1907 0.2503 0.0030  -0.0464 0.1036  102  ILE B C   
4513 O  O   . ILE B 103 ? 0.1854 0.2285 0.2824 0.0049  -0.0796 0.0602  102  ILE B O   
4514 C  CB  . ILE B 103 ? 0.1024 0.2212 0.2320 0.0365  -0.0257 0.0764  102  ILE B CB  
4515 C  CG1 . ILE B 103 ? 0.0976 0.2062 0.2319 0.0496  -0.0354 0.0384  102  ILE B CG1 
4516 C  CG2 . ILE B 103 ? 0.2177 0.2447 0.2422 -0.0035 -0.0071 0.1189  102  ILE B CG2 
4517 C  CD1 . ILE B 103 ? 0.0922 0.2198 0.2427 0.0363  -0.0415 0.0382  102  ILE B CD1 
4518 N  N   . LEU B 104 ? 0.1178 0.1764 0.2448 -0.0251 -0.0435 0.0895  103  LEU B N   
4519 C  CA  . LEU B 104 ? 0.1125 0.1938 0.2773 -0.0248 -0.0626 0.0550  103  LEU B CA  
4520 C  C   . LEU B 104 ? 0.1390 0.1836 0.3349 -0.0391 -0.0775 0.0327  103  LEU B C   
4521 O  O   . LEU B 104 ? 0.1216 0.1825 0.3724 -0.0330 -0.0636 0.0351  103  LEU B O   
4522 C  CB  . LEU B 104 ? 0.1826 0.2093 0.2571 -0.0421 -0.0396 0.0749  103  LEU B CB  
4523 C  CG  . LEU B 104 ? 0.2251 0.1846 0.2290 -0.0214 0.0029  0.0809  103  LEU B CG  
4524 C  CD1 . LEU B 104 ? 0.2764 0.2061 0.2474 -0.0198 0.0572  0.0690  103  LEU B CD1 
4525 C  CD2 . LEU B 104 ? 0.3460 0.1794 0.2193 -0.0648 -0.0077 0.0938  103  LEU B CD2 
4526 N  N   . LEU B 105 ? 0.1312 0.1682 0.3513 0.0001  -0.0730 0.0069  104  LEU B N   
4527 C  CA  . LEU B 105 ? 0.2020 0.2033 0.3630 0.0047  -0.0531 -0.0404 104  LEU B CA  
4528 C  C   . LEU B 105 ? 0.1546 0.1846 0.3885 0.0481  -0.0880 -0.0270 104  LEU B C   
4529 O  O   . LEU B 105 ? 0.2377 0.1486 0.3662 0.0570  -0.1408 -0.0518 104  LEU B O   
4530 C  CB  . LEU B 105 ? 0.1832 0.2500 0.3618 0.0156  -0.0474 -0.0930 104  LEU B CB  
4531 C  CG  . LEU B 105 ? 0.2348 0.2924 0.3787 -0.0344 -0.0293 -0.1458 104  LEU B CG  
4532 C  CD1 . LEU B 105 ? 0.1983 0.3123 0.3832 -0.0631 0.0359  -0.1615 104  LEU B CD1 
4533 C  CD2 . LEU B 105 ? 0.3085 0.3240 0.3930 0.0237  -0.0477 -0.1582 104  LEU B CD2 
4534 N  N   . PRO B 106 ? 0.2311 0.1834 0.4462 -0.0253 -0.1164 0.0497  105  PRO B N   
4535 C  CA  . PRO B 106 ? 0.2290 0.2119 0.4757 0.0033  -0.1402 0.0858  105  PRO B CA  
4536 C  C   . PRO B 106 ? 0.2625 0.1959 0.4685 0.0011  -0.1590 0.0780  105  PRO B C   
4537 O  O   . PRO B 106 ? 0.3659 0.1820 0.5043 -0.0406 -0.1700 0.0877  105  PRO B O   
4538 C  CB  . PRO B 106 ? 0.2438 0.2392 0.5003 -0.0444 -0.1152 0.1075  105  PRO B CB  
4539 C  CG  . PRO B 106 ? 0.2106 0.2449 0.4879 -0.0230 -0.1357 0.0975  105  PRO B CG  
4540 C  CD  . PRO B 106 ? 0.2074 0.1991 0.4738 -0.0465 -0.0906 0.0932  105  PRO B CD  
4541 N  N   . SER B 107 ? 0.1789 0.1766 0.4144 -0.0083 -0.1083 0.0574  106  SER B N   
4542 C  CA  . SER B 107 ? 0.1937 0.2202 0.3709 0.0274  -0.0417 0.0324  106  SER B CA  
4543 C  C   . SER B 107 ? 0.1971 0.2101 0.3465 0.0028  -0.0391 -0.0064 106  SER B C   
4544 O  O   . SER B 107 ? 0.2018 0.1758 0.3348 0.0093  -0.0138 -0.0040 106  SER B O   
4545 C  CB  . SER B 107 ? 0.2404 0.3307 0.3574 0.0656  0.0111  -0.0041 106  SER B CB  
4546 O  OG  . SER B 107 ? 0.3560 0.4216 0.4026 0.0729  0.0429  0.0010  106  SER B OG  
4547 N  N   . PHE B 108 ? 0.1823 0.2805 0.3342 -0.0121 -0.0316 -0.0352 107  PHE B N   
4548 C  CA  . PHE B 108 ? 0.2310 0.3399 0.3579 -0.0370 -0.0881 -0.0524 107  PHE B CA  
4549 C  C   . PHE B 108 ? 0.3862 0.4017 0.3825 0.0739  -0.1212 -0.0981 107  PHE B C   
4550 O  O   . PHE B 108 ? 0.5070 0.4892 0.3879 0.0968  -0.1062 -0.0648 107  PHE B O   
4551 C  CB  . PHE B 108 ? 0.2581 0.3532 0.3617 -0.1289 -0.0783 -0.0165 107  PHE B CB  
4552 C  CG  . PHE B 108 ? 0.2475 0.3393 0.3400 -0.1307 -0.0540 0.0383  107  PHE B CG  
4553 C  CD1 . PHE B 108 ? 0.2680 0.3386 0.3245 -0.1319 -0.0755 0.0629  107  PHE B CD1 
4554 C  CD2 . PHE B 108 ? 0.2197 0.3124 0.3342 -0.1172 -0.0937 0.1110  107  PHE B CD2 
4555 C  CE1 . PHE B 108 ? 0.2513 0.3098 0.3163 -0.1290 -0.1283 0.0987  107  PHE B CE1 
4556 C  CE2 . PHE B 108 ? 0.2029 0.3005 0.3231 -0.1072 -0.1072 0.1289  107  PHE B CE2 
4557 C  CZ  . PHE B 108 ? 0.2882 0.2998 0.3166 -0.1335 -0.1104 0.1115  107  PHE B CZ  
4558 N  N   . SER B 109 ? 0.4247 0.3972 0.4333 0.1168  -0.1673 -0.1467 108  SER B N   
4559 C  CA  . SER B 109 ? 0.4567 0.3939 0.4941 0.1123  -0.1531 -0.1674 108  SER B CA  
4560 C  C   . SER B 109 ? 0.4929 0.4225 0.5092 0.1414  -0.1492 -0.1859 108  SER B C   
4561 O  O   . SER B 109 ? 0.4126 0.4554 0.4873 0.1703  -0.1872 -0.2305 108  SER B O   
4562 C  CB  . SER B 109 ? 0.6174 0.3863 0.5104 0.0894  -0.1868 -0.1586 108  SER B CB  
4563 O  OG  . SER B 109 ? 0.5738 0.3519 0.5074 0.0425  -0.2138 -0.1631 108  SER B OG  
4564 N  N   . GLN B 110 ? 0.5825 0.4064 0.5270 0.1094  -0.1397 -0.1683 109  GLN B N   
4565 C  CA  . GLN B 110 ? 0.6265 0.3978 0.5688 0.1361  -0.1257 -0.1475 109  GLN B CA  
4566 C  C   . GLN B 110 ? 0.5169 0.3383 0.5825 0.0916  -0.1068 -0.1177 109  GLN B C   
4567 O  O   . GLN B 110 ? 0.4811 0.2667 0.5595 0.0691  -0.1055 -0.1241 109  GLN B O   
4568 C  CB  . GLN B 110 ? 0.7811 0.4742 0.6118 0.0753  -0.1311 -0.1310 109  GLN B CB  
4569 C  CG  . GLN B 110 ? 0.8986 0.5374 0.6590 0.0856  -0.0727 -0.0997 109  GLN B CG  
4570 C  CD  . GLN B 110 ? 0.9495 0.5835 0.7024 0.1131  -0.0355 -0.0712 109  GLN B CD  
4571 O  OE1 . GLN B 110 ? 0.9519 0.6189 0.7111 0.1594  -0.0112 -0.0860 109  GLN B OE1 
4572 N  NE2 . GLN B 110 ? 0.9681 0.5736 0.7234 0.0844  -0.0288 -0.0402 109  GLN B NE2 
4573 N  N   . GLN B 111 ? 0.5343 0.3781 0.6038 0.1501  -0.0822 -0.1004 110  GLN B N   
4574 C  CA  . GLN B 111 ? 0.5769 0.4123 0.6206 0.0898  -0.0693 -0.1048 110  GLN B CA  
4575 C  C   . GLN B 111 ? 0.4851 0.3803 0.5849 0.0793  -0.1063 -0.0830 110  GLN B C   
4576 O  O   . GLN B 111 ? 0.3039 0.3947 0.5700 0.1134  -0.1094 -0.0753 110  GLN B O   
4577 C  CB  . GLN B 111 ? 0.6900 0.4880 0.6677 0.0429  -0.0436 -0.1116 110  GLN B CB  
4578 C  CG  . GLN B 111 ? 0.7930 0.5408 0.7095 0.0188  -0.0120 -0.1230 110  GLN B CG  
4579 C  CD  . GLN B 111 ? 0.9335 0.5871 0.7397 0.0286  0.0172  -0.1313 110  GLN B CD  
4580 O  OE1 . GLN B 111 ? 0.9877 0.6185 0.7460 0.0263  0.0074  -0.1416 110  GLN B OE1 
4581 N  NE2 . GLN B 111 ? 0.9661 0.5948 0.7545 0.0317  0.0364  -0.1273 110  GLN B NE2 
4582 N  N   . ALA B 112 ? 0.4731 0.2872 0.5501 0.0558  -0.1823 -0.0627 111  ALA B N   
4583 C  CA  . ALA B 112 ? 0.4251 0.2293 0.5209 0.0285  -0.2063 -0.0348 111  ALA B CA  
4584 C  C   . ALA B 112 ? 0.3143 0.2047 0.4765 -0.0328 -0.1984 -0.0137 111  ALA B C   
4585 O  O   . ALA B 112 ? 0.3195 0.2395 0.5166 -0.0488 -0.1135 -0.0167 111  ALA B O   
4586 C  CB  . ALA B 112 ? 0.4189 0.2247 0.5210 0.0021  -0.2389 -0.0217 111  ALA B CB  
4587 N  N   . MET B 113 ? 0.2873 0.1779 0.4121 -0.0491 -0.1715 0.0053  112  MET B N   
4588 C  CA  . MET B 113 ? 0.2643 0.1726 0.3558 -0.0568 -0.0900 0.0311  112  MET B CA  
4589 C  C   . MET B 113 ? 0.1937 0.1571 0.2948 -0.0731 -0.0807 0.0001  112  MET B C   
4590 O  O   . MET B 113 ? 0.2757 0.1412 0.2715 -0.0851 -0.0460 -0.0274 112  MET B O   
4591 C  CB  . MET B 113 ? 0.4879 0.1938 0.3526 0.0023  -0.0485 0.0289  112  MET B CB  
4592 C  CG  . MET B 113 ? 0.5362 0.2328 0.3700 0.0141  -0.0245 0.0038  112  MET B CG  
4593 S  SD  . MET B 113 ? 0.3867 0.2413 0.3575 -0.0552 0.0088  -0.0127 112  MET B SD  
4594 C  CE  . MET B 113 ? 0.5718 0.2875 0.4005 -0.0039 0.0398  0.0128  112  MET B CE  
4595 N  N   . LYS B 114 ? 0.2559 0.1597 0.3105 -0.0815 -0.0652 0.0112  113  LYS B N   
4596 C  CA  . LYS B 114 ? 0.2886 0.1735 0.2857 -0.0222 -0.0278 0.0073  113  LYS B CA  
4597 C  C   . LYS B 114 ? 0.2721 0.2235 0.2944 -0.0374 -0.0060 0.0011  113  LYS B C   
4598 O  O   . LYS B 114 ? 0.2546 0.2553 0.2617 -0.0724 -0.0050 -0.0094 113  LYS B O   
4599 C  CB  . LYS B 114 ? 0.3297 0.1624 0.2782 0.0025  -0.0196 -0.0179 113  LYS B CB  
4600 C  CG  . LYS B 114 ? 0.3094 0.1768 0.2870 -0.0024 -0.0290 -0.0367 113  LYS B CG  
4601 C  CD  . LYS B 114 ? 0.3973 0.1855 0.3275 -0.0791 -0.0346 -0.0593 113  LYS B CD  
4602 C  CE  . LYS B 114 ? 0.4725 0.2114 0.3630 -0.1280 -0.0123 -0.0746 113  LYS B CE  
4603 N  NZ  . LYS B 114 ? 0.5896 0.2459 0.3761 -0.0864 0.0077  -0.1163 113  LYS B NZ  
4604 N  N   . GLY B 115 ? 0.1753 0.2321 0.3149 0.0156  0.0031  -0.0157 114  GLY B N   
4605 C  CA  . GLY B 115 ? 0.1917 0.2569 0.3191 -0.0584 0.0715  -0.0593 114  GLY B CA  
4606 C  C   . GLY B 115 ? 0.2372 0.2481 0.3114 -0.0509 0.0130  -0.0483 114  GLY B C   
4607 O  O   . GLY B 115 ? 0.3390 0.2737 0.2961 -0.0500 0.0659  -0.0351 114  GLY B O   
4608 N  N   . TYR B 116 ? 0.1764 0.1925 0.2864 -0.0296 -0.0119 0.0047  115  TYR B N   
4609 C  CA  . TYR B 116 ? 0.1517 0.1977 0.2580 -0.0114 -0.0217 0.0061  115  TYR B CA  
4610 C  C   . TYR B 116 ? 0.1468 0.1884 0.2206 -0.0244 -0.0144 0.0017  115  TYR B C   
4611 O  O   . TYR B 116 ? 0.1804 0.2300 0.1975 -0.0161 -0.0139 0.0305  115  TYR B O   
4612 C  CB  . TYR B 116 ? 0.1413 0.1905 0.2729 -0.0262 -0.0090 0.0035  115  TYR B CB  
4613 C  CG  . TYR B 116 ? 0.1864 0.2215 0.2873 -0.0525 -0.0176 -0.0367 115  TYR B CG  
4614 C  CD1 . TYR B 116 ? 0.1924 0.2656 0.3084 -0.0275 -0.0199 -0.0249 115  TYR B CD1 
4615 C  CD2 . TYR B 116 ? 0.1891 0.2286 0.2989 -0.0325 0.0167  -0.0243 115  TYR B CD2 
4616 C  CE1 . TYR B 116 ? 0.1558 0.3045 0.3106 0.0297  -0.0418 -0.0064 115  TYR B CE1 
4617 C  CE2 . TYR B 116 ? 0.1556 0.2575 0.3081 -0.0435 -0.0049 -0.0592 115  TYR B CE2 
4618 C  CZ  . TYR B 116 ? 0.1280 0.2881 0.3239 0.0219  -0.0227 -0.0197 115  TYR B CZ  
4619 O  OH  . TYR B 116 ? 0.1499 0.3070 0.3461 0.0516  -0.0421 -0.0109 115  TYR B OH  
4620 N  N   . HIS B 117 ? 0.1540 0.1665 0.2227 -0.0313 0.0259  -0.0420 116  HIS B N   
4621 C  CA  . HIS B 117 ? 0.1427 0.1593 0.1906 0.0095  0.0059  -0.0595 116  HIS B CA  
4622 C  C   . HIS B 117 ? 0.1481 0.1705 0.1511 -0.0591 0.0376  -0.0365 116  HIS B C   
4623 O  O   . HIS B 117 ? 0.1132 0.2087 0.1661 -0.0295 0.0270  -0.0191 116  HIS B O   
4624 C  CB  . HIS B 117 ? 0.2014 0.1164 0.1785 0.0641  0.0192  -0.0489 116  HIS B CB  
4625 C  CG  . HIS B 117 ? 0.1812 0.1493 0.1687 0.0314  0.0091  -0.0414 116  HIS B CG  
4626 N  ND1 . HIS B 117 ? 0.2163 0.1419 0.1537 0.0408  0.0322  -0.0323 116  HIS B ND1 
4627 C  CD2 . HIS B 117 ? 0.1926 0.1563 0.1505 0.0848  -0.0054 -0.0344 116  HIS B CD2 
4628 C  CE1 . HIS B 117 ? 0.2390 0.1469 0.1788 0.0761  -0.0318 -0.0256 116  HIS B CE1 
4629 N  NE2 . HIS B 117 ? 0.1728 0.1735 0.1621 0.0455  -0.0092 -0.0356 116  HIS B NE2 
4630 N  N   . ALA B 118 ? 0.2166 0.2041 0.0952 0.0100  0.0290  -0.0279 117  ALA B N   
4631 C  CA  . ALA B 118 ? 0.2572 0.2090 0.1528 -0.0385 0.0080  -0.0049 117  ALA B CA  
4632 C  C   . ALA B 118 ? 0.1900 0.2147 0.1615 -0.0492 0.0102  -0.0098 117  ALA B C   
4633 O  O   . ALA B 118 ? 0.1769 0.2025 0.1882 -0.0276 -0.0159 0.0057  117  ALA B O   
4634 C  CB  . ALA B 118 ? 0.2848 0.2273 0.1512 -0.0971 -0.0150 0.0174  117  ALA B CB  
4635 N  N   . MET B 119 ? 0.1877 0.1830 0.1599 0.0009  0.0291  -0.0021 118  MET B N   
4636 C  CA  A MET B 119 ? 0.1601 0.2056 0.1850 0.0345  0.0334  0.0060  118  MET B CA  
4637 C  CA  B MET B 119 ? 0.1929 0.2145 0.1807 -0.0094 0.0493  -0.0075 118  MET B CA  
4638 C  C   . MET B 119 ? 0.1699 0.2131 0.1541 0.0062  0.0353  -0.0068 118  MET B C   
4639 O  O   . MET B 119 ? 0.2225 0.2459 0.1410 -0.0317 -0.0135 -0.0135 118  MET B O   
4640 C  CB  A MET B 119 ? 0.1113 0.2254 0.2179 0.0517  0.0183  0.0376  118  MET B CB  
4641 C  CB  B MET B 119 ? 0.2254 0.2506 0.2149 -0.0554 0.0850  -0.0104 118  MET B CB  
4642 C  CG  A MET B 119 ? 0.1455 0.2412 0.2390 0.0542  0.0072  0.0316  118  MET B CG  
4643 C  CG  B MET B 119 ? 0.3052 0.2843 0.2265 -0.0763 0.1199  -0.0154 118  MET B CG  
4644 S  SD  A MET B 119 ? 0.2801 0.2425 0.2791 -0.0005 0.0090  0.0436  118  MET B SD  
4645 S  SD  B MET B 119 ? 0.4037 0.3133 0.2741 -0.1551 0.1360  -0.0106 118  MET B SD  
4646 C  CE  A MET B 119 ? 0.3100 0.2530 0.2839 -0.0355 0.0166  0.0232  118  MET B CE  
4647 C  CE  B MET B 119 ? 0.3937 0.3189 0.2756 -0.1484 0.1294  0.0098  118  MET B CE  
4648 N  N   . MET B 120 ? 0.1877 0.2007 0.1256 0.0142  0.0361  -0.0067 119  MET B N   
4649 C  CA  . MET B 120 ? 0.1547 0.2069 0.0948 0.0361  0.0040  -0.0140 119  MET B CA  
4650 C  C   . MET B 120 ? 0.1156 0.2107 0.1257 0.0318  0.0000  -0.0109 119  MET B C   
4651 O  O   . MET B 120 ? 0.1528 0.2047 0.1465 -0.0267 -0.0190 -0.0068 119  MET B O   
4652 C  CB  . MET B 120 ? 0.1297 0.1849 0.0694 -0.0178 0.0174  -0.0220 119  MET B CB  
4653 C  CG  . MET B 120 ? 0.1901 0.2194 0.0865 0.0078  -0.0119 -0.0147 119  MET B CG  
4654 S  SD  . MET B 120 ? 0.1806 0.2459 0.1313 0.0003  -0.0167 -0.0169 119  MET B SD  
4655 C  CE  . MET B 120 ? 0.1130 0.2326 0.1165 0.0249  -0.0039 0.0238  119  MET B CE  
4656 N  N   . VAL B 121 ? 0.1720 0.1905 0.1319 0.0040  -0.0119 -0.0068 120  VAL B N   
4657 C  CA  . VAL B 121 ? 0.1418 0.1612 0.1333 0.0280  -0.0248 0.0033  120  VAL B CA  
4658 C  C   . VAL B 121 ? 0.1220 0.1774 0.1265 0.0102  -0.0187 0.0078  120  VAL B C   
4659 O  O   . VAL B 121 ? 0.1364 0.2129 0.1361 0.0021  -0.0158 -0.0004 120  VAL B O   
4660 C  CB  . VAL B 121 ? 0.1890 0.1740 0.1410 -0.0188 -0.0237 0.0255  120  VAL B CB  
4661 C  CG1 . VAL B 121 ? 0.2101 0.1732 0.1788 0.0022  -0.0494 0.0315  120  VAL B CG1 
4662 C  CG2 . VAL B 121 ? 0.2059 0.1716 0.1507 -0.0090 -0.0141 0.0217  120  VAL B CG2 
4663 N  N   . ASP B 122 ? 0.2006 0.1369 0.1204 0.0476  0.0263  0.0016  121  ASP B N   
4664 C  CA  . ASP B 122 ? 0.2035 0.1793 0.1090 0.0044  0.0397  0.0026  121  ASP B CA  
4665 C  C   . ASP B 122 ? 0.2407 0.1930 0.1350 0.0011  0.0113  -0.0151 121  ASP B C   
4666 O  O   . ASP B 122 ? 0.2058 0.1890 0.1385 -0.0049 -0.0044 -0.0081 121  ASP B O   
4667 C  CB  . ASP B 122 ? 0.1872 0.2113 0.1112 0.0124  0.0638  -0.0075 121  ASP B CB  
4668 C  CG  . ASP B 122 ? 0.2408 0.2268 0.1411 -0.0085 0.0120  0.0201  121  ASP B CG  
4669 O  OD1 . ASP B 122 ? 0.2436 0.2018 0.1467 -0.0149 0.0076  0.0039  121  ASP B OD1 
4670 O  OD2 . ASP B 122 ? 0.2208 0.2458 0.1527 0.0011  0.0307  -0.0007 121  ASP B OD2 
4671 N  N   . ILE B 123 ? 0.1875 0.1764 0.1338 0.0012  0.0227  -0.0070 122  ILE B N   
4672 C  CA  . ILE B 123 ? 0.1915 0.1873 0.1532 -0.0154 -0.0069 0.0078  122  ILE B CA  
4673 C  C   . ILE B 123 ? 0.1314 0.2192 0.1189 0.0170  -0.0252 -0.0231 122  ILE B C   
4674 O  O   . ILE B 123 ? 0.1260 0.2244 0.1169 0.0114  -0.0154 0.0179  122  ILE B O   
4675 C  CB  . ILE B 123 ? 0.0898 0.1524 0.1838 -0.0269 0.0025  0.0011  122  ILE B CB  
4676 C  CG1 . ILE B 123 ? 0.1181 0.1690 0.1511 0.0163  0.0197  -0.0163 122  ILE B CG1 
4677 C  CG2 . ILE B 123 ? 0.1358 0.1376 0.1948 -0.0470 -0.0211 0.0236  122  ILE B CG2 
4678 C  CD1 . ILE B 123 ? 0.1627 0.1304 0.1623 -0.0116 0.0682  -0.0616 122  ILE B CD1 
4679 N  N   . ALA B 124 ? 0.1520 0.2404 0.1208 0.0060  -0.0134 -0.0443 123  ALA B N   
4680 C  CA  . ALA B 124 ? 0.1345 0.2360 0.0943 0.0168  -0.0201 -0.0652 123  ALA B CA  
4681 C  C   . ALA B 124 ? 0.1578 0.2097 0.1032 0.0145  -0.0177 -0.0241 123  ALA B C   
4682 O  O   . ALA B 124 ? 0.1826 0.1822 0.1262 -0.0248 -0.0064 -0.0254 123  ALA B O   
4683 C  CB  . ALA B 124 ? 0.1402 0.2355 0.1089 0.0022  -0.0280 -0.0726 123  ALA B CB  
4684 N  N   . VAL B 125 ? 0.1731 0.2064 0.1102 -0.0204 -0.0220 -0.0273 124  VAL B N   
4685 C  CA  . VAL B 125 ? 0.2165 0.1707 0.1103 -0.0113 -0.0209 0.0051  124  VAL B CA  
4686 C  C   . VAL B 125 ? 0.1772 0.2111 0.1215 -0.0014 -0.0101 -0.0011 124  VAL B C   
4687 O  O   . VAL B 125 ? 0.1793 0.2066 0.1448 -0.0110 0.0181  0.0066  124  VAL B O   
4688 C  CB  . VAL B 125 ? 0.1950 0.1628 0.1103 -0.0414 -0.0361 0.0116  124  VAL B CB  
4689 C  CG1 . VAL B 125 ? 0.2105 0.2252 0.1190 -0.0254 -0.0693 0.0374  124  VAL B CG1 
4690 C  CG2 . VAL B 125 ? 0.2741 0.1195 0.1312 -0.0319 -0.0157 0.0056  124  VAL B CG2 
4691 N  N   . GLN B 126 ? 0.1736 0.2159 0.1113 0.0349  0.0312  -0.0028 125  GLN B N   
4692 C  CA  . GLN B 126 ? 0.1223 0.2323 0.1093 0.0079  0.0525  -0.0258 125  GLN B CA  
4693 C  C   . GLN B 126 ? 0.1723 0.2289 0.1070 -0.0217 0.0455  -0.0195 125  GLN B C   
4694 O  O   . GLN B 126 ? 0.1954 0.2387 0.1319 -0.0322 0.0090  -0.0213 125  GLN B O   
4695 C  CB  . GLN B 126 ? 0.1084 0.2253 0.1006 0.0448  0.0340  -0.0135 125  GLN B CB  
4696 C  CG  . GLN B 126 ? 0.0813 0.2105 0.1284 0.0173  0.0394  -0.0239 125  GLN B CG  
4697 C  CD  . GLN B 126 ? 0.1233 0.2182 0.1221 0.0198  0.0389  -0.0331 125  GLN B CD  
4698 O  OE1 . GLN B 126 ? 0.1424 0.2184 0.1281 0.0028  0.0071  -0.0058 125  GLN B OE1 
4699 N  NE2 . GLN B 126 ? 0.1399 0.2249 0.1183 0.0129  0.0117  -0.0042 125  GLN B NE2 
4700 N  N   . LEU B 127 ? 0.1930 0.1988 0.0971 -0.0174 0.0264  -0.0384 126  LEU B N   
4701 C  CA  . LEU B 127 ? 0.1828 0.1763 0.0786 -0.0261 -0.0155 -0.0091 126  LEU B CA  
4702 C  C   . LEU B 127 ? 0.1574 0.1539 0.1267 0.0053  -0.0030 -0.0251 126  LEU B C   
4703 O  O   . LEU B 127 ? 0.1865 0.1670 0.1378 0.0084  0.0026  -0.0386 126  LEU B O   
4704 C  CB  . LEU B 127 ? 0.1946 0.1431 0.0511 -0.0005 -0.0084 0.0094  126  LEU B CB  
4705 C  CG  . LEU B 127 ? 0.2260 0.1216 0.1005 -0.0583 0.0167  0.0148  126  LEU B CG  
4706 C  CD1 . LEU B 127 ? 0.2340 0.1500 0.1568 -0.0513 0.0351  0.0165  126  LEU B CD1 
4707 C  CD2 . LEU B 127 ? 0.2664 0.1682 0.1312 -0.0559 0.0744  -0.0120 126  LEU B CD2 
4708 N  N   . VAL B 128 ? 0.1693 0.1330 0.1185 0.0250  -0.0255 0.0009  127  VAL B N   
4709 C  CA  . VAL B 128 ? 0.1649 0.1446 0.1109 0.0576  -0.0313 -0.0336 127  VAL B CA  
4710 C  C   . VAL B 128 ? 0.2597 0.1782 0.1384 0.0298  0.0052  -0.0325 127  VAL B C   
4711 O  O   . VAL B 128 ? 0.2564 0.1878 0.1515 0.0100  -0.0103 -0.0503 127  VAL B O   
4712 C  CB  . VAL B 128 ? 0.1742 0.1883 0.0924 0.0364  -0.0368 -0.0262 127  VAL B CB  
4713 C  CG1 . VAL B 128 ? 0.1721 0.1854 0.1068 0.0639  -0.0522 -0.0356 127  VAL B CG1 
4714 C  CG2 . VAL B 128 ? 0.1534 0.2140 0.1034 -0.0009 -0.0338 0.0235  127  VAL B CG2 
4715 N  N   . GLN B 129 ? 0.1768 0.1856 0.1262 0.0258  0.0149  0.0021  128  GLN B N   
4716 C  CA  . GLN B 129 ? 0.1927 0.1998 0.1063 0.0004  0.0206  -0.0018 128  GLN B CA  
4717 C  C   . GLN B 129 ? 0.2164 0.2049 0.1214 0.0029  0.0033  0.0189  128  GLN B C   
4718 O  O   . GLN B 129 ? 0.1988 0.2111 0.1397 -0.0056 -0.0250 -0.0114 128  GLN B O   
4719 C  CB  . GLN B 129 ? 0.2470 0.2251 0.1034 -0.0022 0.0055  0.0009  128  GLN B CB  
4720 C  CG  . GLN B 129 ? 0.4429 0.2839 0.1720 -0.0647 -0.0025 0.0084  128  GLN B CG  
4721 C  CD  . GLN B 129 ? 0.7751 0.3510 0.2595 -0.0584 -0.0396 0.0056  128  GLN B CD  
4722 O  OE1 . GLN B 129 ? 0.8510 0.3952 0.3116 -0.0432 -0.0245 -0.0037 128  GLN B OE1 
4723 N  NE2 . GLN B 129 ? 0.9158 0.3725 0.2618 -0.0586 -0.0630 0.0478  128  GLN B NE2 
4724 N  N   . LYS B 130 ? 0.1722 0.1662 0.1201 0.0414  0.0134  0.0173  129  LYS B N   
4725 C  CA  . LYS B 130 ? 0.1596 0.1584 0.1407 0.0415  0.0145  0.0110  129  LYS B CA  
4726 C  C   . LYS B 130 ? 0.1741 0.1890 0.1375 0.0445  0.0259  -0.0121 129  LYS B C   
4727 O  O   . LYS B 130 ? 0.1907 0.1906 0.1460 0.0154  0.0044  0.0152  129  LYS B O   
4728 C  CB  . LYS B 130 ? 0.1756 0.1297 0.1385 0.0599  0.0098  -0.0075 129  LYS B CB  
4729 C  CG  . LYS B 130 ? 0.2297 0.1101 0.1498 0.0158  -0.0537 -0.0148 129  LYS B CG  
4730 C  CD  . LYS B 130 ? 0.2636 0.1333 0.1714 -0.0112 -0.1081 -0.0265 129  LYS B CD  
4731 C  CE  . LYS B 130 ? 0.3131 0.1747 0.1645 -0.0057 -0.0637 -0.0409 129  LYS B CE  
4732 N  NZ  . LYS B 130 ? 0.2820 0.2080 0.1537 0.0206  -0.0318 -0.0475 129  LYS B NZ  
4733 N  N   . TRP B 131 ? 0.1865 0.1781 0.1385 0.0426  0.0276  -0.0255 130  TRP B N   
4734 C  CA  . TRP B 131 ? 0.1747 0.1765 0.1226 0.0571  0.0023  -0.0244 130  TRP B CA  
4735 C  C   . TRP B 131 ? 0.1740 0.1953 0.1162 0.0160  -0.0058 0.0047  130  TRP B C   
4736 O  O   . TRP B 131 ? 0.1816 0.2026 0.1256 -0.0318 -0.0179 -0.0132 130  TRP B O   
4737 C  CB  . TRP B 131 ? 0.1881 0.1710 0.1186 0.0680  -0.0282 -0.0088 130  TRP B CB  
4738 C  CG  . TRP B 131 ? 0.1501 0.2118 0.1200 0.0295  -0.0121 -0.0194 130  TRP B CG  
4739 C  CD1 . TRP B 131 ? 0.2165 0.2302 0.1557 -0.0174 0.0026  0.0030  130  TRP B CD1 
4740 C  CD2 . TRP B 131 ? 0.1497 0.2094 0.1083 0.0060  -0.0068 -0.0114 130  TRP B CD2 
4741 N  NE1 . TRP B 131 ? 0.1515 0.2200 0.1410 -0.0033 -0.0015 -0.0139 130  TRP B NE1 
4742 C  CE2 . TRP B 131 ? 0.2198 0.2154 0.1190 0.0037  0.0363  -0.0304 130  TRP B CE2 
4743 C  CE3 . TRP B 131 ? 0.1142 0.1912 0.1090 -0.0259 -0.0391 -0.0331 130  TRP B CE3 
4744 C  CZ2 . TRP B 131 ? 0.1829 0.1995 0.1226 -0.0150 0.0416  -0.0181 130  TRP B CZ2 
4745 C  CZ3 . TRP B 131 ? 0.1862 0.1885 0.1191 -0.0045 -0.0001 -0.0393 130  TRP B CZ3 
4746 C  CH2 . TRP B 131 ? 0.1761 0.2159 0.1306 -0.0152 0.0212  -0.0108 130  TRP B CH2 
4747 N  N   . GLU B 132 ? 0.2436 0.1719 0.1189 0.0268  0.0358  0.0015  131  GLU B N   
4748 C  CA  . GLU B 132 ? 0.2503 0.2065 0.1435 -0.0138 -0.0353 -0.0416 131  GLU B CA  
4749 C  C   . GLU B 132 ? 0.1845 0.2487 0.1261 -0.0313 -0.0418 -0.0348 131  GLU B C   
4750 O  O   . GLU B 132 ? 0.1865 0.2999 0.1251 -0.0259 -0.0351 -0.0628 131  GLU B O   
4751 C  CB  . GLU B 132 ? 0.1890 0.1772 0.1693 -0.0194 -0.0528 -0.0611 131  GLU B CB  
4752 C  CG  . GLU B 132 ? 0.2616 0.1967 0.1851 0.0561  -0.0389 -0.0900 131  GLU B CG  
4753 C  CD  . GLU B 132 ? 0.3242 0.1872 0.2291 0.0251  -0.0616 -0.0642 131  GLU B CD  
4754 O  OE1 . GLU B 132 ? 0.2666 0.1741 0.2419 0.0155  -0.0520 -0.0477 131  GLU B OE1 
4755 O  OE2 . GLU B 132 ? 0.3543 0.1967 0.2695 -0.0425 0.0053  -0.0702 131  GLU B OE2 
4756 N  N   . ARG B 133 ? 0.1793 0.2339 0.0803 0.0246  -0.0077 -0.0191 132  ARG B N   
4757 C  CA  . ARG B 133 ? 0.1841 0.2461 0.1158 0.0165  0.0026  -0.0147 132  ARG B CA  
4758 C  C   . ARG B 133 ? 0.1720 0.2466 0.1256 0.0441  -0.0095 -0.0189 132  ARG B C   
4759 O  O   . ARG B 133 ? 0.1819 0.2920 0.1378 0.0317  -0.0020 -0.0363 132  ARG B O   
4760 C  CB  . ARG B 133 ? 0.1514 0.2356 0.1316 0.0161  0.0057  -0.0063 132  ARG B CB  
4761 C  CG  . ARG B 133 ? 0.1197 0.1931 0.1111 0.0078  0.0325  0.0096  132  ARG B CG  
4762 C  CD  . ARG B 133 ? 0.1572 0.2044 0.1279 -0.0184 0.0329  -0.0020 132  ARG B CD  
4763 N  NE  . ARG B 133 ? 0.2648 0.2451 0.1347 -0.0284 0.0419  0.0161  132  ARG B NE  
4764 C  CZ  . ARG B 133 ? 0.2356 0.2696 0.1551 -0.0205 0.0261  0.0279  132  ARG B CZ  
4765 N  NH1 . ARG B 133 ? 0.1755 0.2730 0.1627 0.0064  -0.0038 0.0181  132  ARG B NH1 
4766 N  NH2 . ARG B 133 ? 0.2676 0.2867 0.1673 -0.0496 -0.0067 0.0329  132  ARG B NH2 
4767 N  N   . LEU B 134 ? 0.1678 0.2645 0.1315 0.0091  -0.0124 -0.0271 133  LEU B N   
4768 C  CA  . LEU B 134 ? 0.1764 0.2557 0.1412 -0.0339 -0.0040 -0.0078 133  LEU B CA  
4769 C  C   . LEU B 134 ? 0.1460 0.2446 0.1833 -0.0419 -0.0194 -0.0210 133  LEU B C   
4770 O  O   . LEU B 134 ? 0.2236 0.2584 0.2195 -0.0008 0.0495  -0.0165 133  LEU B O   
4771 C  CB  . LEU B 134 ? 0.2214 0.2537 0.1296 0.0155  0.0238  -0.0314 133  LEU B CB  
4772 C  CG  . LEU B 134 ? 0.2141 0.2572 0.0894 0.0158  0.0178  -0.0491 133  LEU B CG  
4773 C  CD1 . LEU B 134 ? 0.2745 0.2833 0.1073 -0.0343 0.0049  -0.0155 133  LEU B CD1 
4774 C  CD2 . LEU B 134 ? 0.2449 0.2587 0.1024 -0.0091 0.0176  -0.0604 133  LEU B CD2 
4775 N  N   . ASN B 135 ? 0.1552 0.2484 0.1543 -0.0726 -0.0266 -0.0605 134  ASN B N   
4776 C  CA  . ASN B 135 ? 0.1314 0.2880 0.1520 -0.0329 0.0161  -0.0469 134  ASN B CA  
4777 C  C   . ASN B 135 ? 0.2086 0.3509 0.2197 0.0155  0.0183  -0.0172 134  ASN B C   
4778 O  O   . ASN B 135 ? 0.2203 0.3512 0.2082 0.0168  0.0738  -0.0282 134  ASN B O   
4779 C  CB  . ASN B 135 ? 0.1582 0.2982 0.1414 -0.0074 0.0158  -0.0577 134  ASN B CB  
4780 C  CG  . ASN B 135 ? 0.1389 0.3094 0.1608 -0.0051 0.0191  -0.0264 134  ASN B CG  
4781 O  OD1 . ASN B 135 ? 0.1858 0.3530 0.1619 -0.0184 0.0084  -0.0136 134  ASN B OD1 
4782 N  ND2 . ASN B 135 ? 0.1430 0.2709 0.1888 0.0099  -0.0173 -0.0413 134  ASN B ND2 
4783 N  N   . ALA B 136 ? 0.1735 0.3916 0.2658 0.0124  0.0166  0.0371  135  ALA B N   
4784 C  CA  . ALA B 136 ? 0.2235 0.4232 0.3205 0.0223  0.0092  0.0630  135  ALA B CA  
4785 C  C   . ALA B 136 ? 0.2358 0.4698 0.3417 -0.0170 -0.0363 0.0678  135  ALA B C   
4786 O  O   . ALA B 136 ? 0.2107 0.4648 0.3572 -0.0639 -0.0931 0.0790  135  ALA B O   
4787 C  CB  . ALA B 136 ? 0.2240 0.4265 0.3535 0.0280  0.0469  0.0559  135  ALA B CB  
4788 N  N   . ASP B 137 ? 0.2770 0.5126 0.3491 -0.0165 0.0256  0.0689  136  ASP B N   
4789 C  CA  . ASP B 137 ? 0.3133 0.5491 0.3812 -0.0554 -0.0030 0.0567  136  ASP B CA  
4790 C  C   . ASP B 137 ? 0.2484 0.4813 0.3360 -0.0792 -0.0172 0.0589  136  ASP B C   
4791 O  O   . ASP B 137 ? 0.2934 0.5027 0.3805 -0.1332 -0.0033 0.0807  136  ASP B O   
4792 C  CB  . ASP B 137 ? 0.4110 0.6515 0.4396 -0.0021 -0.0320 0.0594  136  ASP B CB  
4793 C  CG  . ASP B 137 ? 0.4368 0.7335 0.4832 -0.0057 0.0239  0.0493  136  ASP B CG  
4794 O  OD1 . ASP B 137 ? 0.4411 0.7622 0.5103 -0.0224 0.0802  0.0413  136  ASP B OD1 
4795 O  OD2 . ASP B 137 ? 0.4903 0.7651 0.4914 0.0155  -0.0194 0.0485  136  ASP B OD2 
4796 N  N   . GLU B 138 ? 0.2169 0.4314 0.2445 -0.0699 -0.0603 0.0373  137  GLU B N   
4797 C  CA  . GLU B 138 ? 0.1736 0.3824 0.1649 -0.0292 -0.0293 0.0195  137  GLU B CA  
4798 C  C   . GLU B 138 ? 0.2441 0.3588 0.1602 -0.0212 -0.0611 -0.0015 137  GLU B C   
4799 O  O   . GLU B 138 ? 0.2941 0.3860 0.1715 0.0433  -0.0225 -0.0072 137  GLU B O   
4800 C  CB  . GLU B 138 ? 0.1526 0.3648 0.1486 -0.0784 -0.0367 -0.0116 137  GLU B CB  
4801 C  CG  . GLU B 138 ? 0.2229 0.3430 0.0986 -0.0712 -0.0152 0.0023  137  GLU B CG  
4802 C  CD  . GLU B 138 ? 0.2404 0.3283 0.1348 -0.0324 -0.0101 -0.0307 137  GLU B CD  
4803 O  OE1 . GLU B 138 ? 0.2311 0.3415 0.1472 -0.0183 -0.0472 -0.0689 137  GLU B OE1 
4804 O  OE2 . GLU B 138 ? 0.2913 0.3229 0.1759 -0.0221 0.0095  -0.0212 137  GLU B OE2 
4805 N  N   . HIS B 139 ? 0.2191 0.3257 0.1545 -0.0451 -0.0574 0.0019  138  HIS B N   
4806 C  CA  . HIS B 139 ? 0.2383 0.2943 0.1449 -0.0337 -0.0599 -0.0056 138  HIS B CA  
4807 C  C   . HIS B 139 ? 0.1863 0.2713 0.1248 -0.0268 -0.0125 -0.0159 138  HIS B C   
4808 O  O   . HIS B 139 ? 0.1910 0.2690 0.1063 0.0140  -0.0125 -0.0076 138  HIS B O   
4809 C  CB  . HIS B 139 ? 0.3060 0.2890 0.1761 -0.0280 -0.0472 -0.0134 138  HIS B CB  
4810 C  CG  . HIS B 139 ? 0.3209 0.2630 0.2182 -0.0792 -0.0812 -0.0659 138  HIS B CG  
4811 N  ND1 . HIS B 139 ? 0.3642 0.2539 0.2660 -0.0588 -0.0616 -0.0973 138  HIS B ND1 
4812 C  CD2 . HIS B 139 ? 0.3400 0.2507 0.2413 -0.0592 -0.0586 -0.0706 138  HIS B CD2 
4813 C  CE1 . HIS B 139 ? 0.4283 0.2713 0.2728 -0.0266 -0.0304 -0.0908 138  HIS B CE1 
4814 N  NE2 . HIS B 139 ? 0.3464 0.2727 0.2528 -0.0512 -0.0977 -0.0869 138  HIS B NE2 
4815 N  N   . ILE B 140 ? 0.1219 0.2587 0.1479 0.0061  -0.0344 -0.0353 139  ILE B N   
4816 C  CA  . ILE B 140 ? 0.1209 0.2026 0.1535 0.0045  -0.0454 -0.0439 139  ILE B CA  
4817 C  C   . ILE B 140 ? 0.1031 0.1954 0.1465 0.0136  -0.0428 -0.0275 139  ILE B C   
4818 O  O   . ILE B 140 ? 0.2064 0.1820 0.1292 -0.0029 -0.0328 0.0031  139  ILE B O   
4819 C  CB  . ILE B 140 ? 0.2589 0.1603 0.1767 -0.0464 -0.0747 -0.0420 139  ILE B CB  
4820 C  CG1 . ILE B 140 ? 0.2013 0.1093 0.1788 -0.0401 -0.0295 -0.0507 139  ILE B CG1 
4821 C  CG2 . ILE B 140 ? 0.2453 0.1644 0.1544 -0.0420 -0.0801 -0.0396 139  ILE B CG2 
4822 C  CD1 . ILE B 140 ? 0.2022 0.1515 0.2411 0.0024  0.0034  -0.0469 139  ILE B CD1 
4823 N  N   . GLU B 141 ? 0.1673 0.1886 0.1490 0.0144  -0.0103 -0.0644 140  GLU B N   
4824 C  CA  . GLU B 141 ? 0.1740 0.1850 0.1551 0.0093  -0.0066 -0.0730 140  GLU B CA  
4825 C  C   . GLU B 141 ? 0.1706 0.1842 0.1458 0.0186  -0.0151 -0.0472 140  GLU B C   
4826 O  O   . GLU B 141 ? 0.1250 0.1992 0.1692 0.0194  -0.0174 -0.0366 140  GLU B O   
4827 C  CB  . GLU B 141 ? 0.1886 0.2029 0.1785 -0.0351 -0.0219 -0.0880 140  GLU B CB  
4828 C  CG  . GLU B 141 ? 0.2177 0.2524 0.2235 -0.0481 -0.0085 -0.1000 140  GLU B CG  
4829 C  CD  . GLU B 141 ? 0.2030 0.2848 0.3056 -0.0570 0.0089  -0.1236 140  GLU B CD  
4830 O  OE1 . GLU B 141 ? 0.2309 0.3137 0.3176 -0.0447 0.0525  -0.1202 140  GLU B OE1 
4831 O  OE2 . GLU B 141 ? 0.3527 0.2955 0.3468 -0.0176 0.0306  -0.1285 140  GLU B OE2 
4832 N  N   . VAL B 142 ? 0.1380 0.1659 0.1463 0.0275  0.0033  -0.0380 141  VAL B N   
4833 C  CA  . VAL B 142 ? 0.1555 0.1458 0.1290 0.0188  -0.0046 -0.0216 141  VAL B CA  
4834 C  C   . VAL B 142 ? 0.1531 0.1714 0.1340 -0.0129 0.0102  -0.0116 141  VAL B C   
4835 O  O   . VAL B 142 ? 0.1490 0.1951 0.1398 0.0112  -0.0323 -0.0146 141  VAL B O   
4836 C  CB  . VAL B 142 ? 0.0636 0.1432 0.1523 0.0174  -0.0080 -0.0261 141  VAL B CB  
4837 C  CG1 . VAL B 142 ? 0.1535 0.1466 0.1336 -0.0105 -0.0427 -0.0069 141  VAL B CG1 
4838 C  CG2 . VAL B 142 ? 0.1207 0.1249 0.1867 0.0464  -0.0058 -0.0388 141  VAL B CG2 
4839 N  N   . PRO B 143 ? 0.1308 0.1635 0.1593 -0.0283 -0.0266 -0.0194 142  PRO B N   
4840 C  CA  . PRO B 143 ? 0.1323 0.1750 0.1405 -0.0440 -0.0167 -0.0189 142  PRO B CA  
4841 C  C   . PRO B 143 ? 0.0585 0.1820 0.1395 0.0032  -0.0230 -0.0405 142  PRO B C   
4842 O  O   . PRO B 143 ? 0.0627 0.2017 0.1383 0.0317  -0.0080 -0.0345 142  PRO B O   
4843 C  CB  . PRO B 143 ? 0.1776 0.1805 0.1423 -0.0372 -0.0483 -0.0163 142  PRO B CB  
4844 C  CG  . PRO B 143 ? 0.1859 0.1933 0.1715 -0.0712 -0.0601 -0.0209 142  PRO B CG  
4845 C  CD  . PRO B 143 ? 0.1393 0.1696 0.1725 0.0065  -0.0390 0.0031  142  PRO B CD  
4846 N  N   . GLU B 144 ? 0.1576 0.1819 0.1363 0.0373  -0.0009 -0.0410 143  GLU B N   
4847 C  CA  . GLU B 144 ? 0.1495 0.1718 0.1550 0.0152  0.0035  -0.0446 143  GLU B CA  
4848 C  C   . GLU B 144 ? 0.1312 0.1672 0.1627 -0.0212 -0.0162 -0.0364 143  GLU B C   
4849 O  O   . GLU B 144 ? 0.1688 0.1702 0.1640 -0.0082 -0.0186 -0.0012 143  GLU B O   
4850 C  CB  . GLU B 144 ? 0.1728 0.1646 0.1563 -0.0687 -0.0079 -0.0540 143  GLU B CB  
4851 C  CG  . GLU B 144 ? 0.2473 0.1717 0.2022 -0.0423 0.0080  -0.0465 143  GLU B CG  
4852 C  CD  . GLU B 144 ? 0.2118 0.1754 0.2399 -0.0189 0.0272  -0.0347 143  GLU B CD  
4853 O  OE1 . GLU B 144 ? 0.1615 0.1674 0.2170 -0.0218 0.0164  -0.0371 143  GLU B OE1 
4854 O  OE2 . GLU B 144 ? 0.3967 0.2276 0.2787 -0.0251 0.1255  -0.0012 143  GLU B OE2 
4855 N  N   . ASP B 145 ? 0.1293 0.1530 0.1446 0.0404  -0.0461 -0.0101 144  ASP B N   
4856 C  CA  . ASP B 145 ? 0.1324 0.1633 0.1559 0.0183  -0.0434 -0.0091 144  ASP B CA  
4857 C  C   . ASP B 145 ? 0.1504 0.1657 0.1271 0.0357  -0.0286 -0.0276 144  ASP B C   
4858 O  O   . ASP B 145 ? 0.1497 0.1333 0.1562 -0.0033 -0.0072 -0.0253 144  ASP B O   
4859 C  CB  . ASP B 145 ? 0.1439 0.1780 0.1436 -0.0089 -0.0571 0.0001  144  ASP B CB  
4860 C  CG  . ASP B 145 ? 0.0984 0.2028 0.1516 0.0061  -0.0504 -0.0076 144  ASP B CG  
4861 O  OD1 . ASP B 145 ? 0.1260 0.2073 0.1514 0.0077  -0.0090 -0.0293 144  ASP B OD1 
4862 O  OD2 . ASP B 145 ? 0.1663 0.1751 0.1550 0.0005  -0.0668 -0.0062 144  ASP B OD2 
4863 N  N   . MET B 146 ? 0.1266 0.1691 0.1191 0.0135  -0.0165 -0.0497 145  MET B N   
4864 C  CA  . MET B 146 ? 0.0897 0.1793 0.0987 0.0054  0.0070  -0.0229 145  MET B CA  
4865 C  C   . MET B 146 ? 0.1220 0.1546 0.1218 -0.0116 -0.0152 -0.0234 145  MET B C   
4866 O  O   . MET B 146 ? 0.1246 0.1760 0.1519 0.0523  -0.0161 -0.0276 145  MET B O   
4867 C  CB  . MET B 146 ? 0.1492 0.1694 0.1198 0.0051  0.0598  -0.0091 145  MET B CB  
4868 C  CG  . MET B 146 ? 0.2030 0.1515 0.1299 0.0252  0.0517  -0.0069 145  MET B CG  
4869 S  SD  . MET B 146 ? 0.2065 0.1728 0.1322 0.0187  -0.0209 -0.0060 145  MET B SD  
4870 C  CE  . MET B 146 ? 0.1731 0.2418 0.1196 0.0828  0.0173  -0.0080 145  MET B CE  
4871 N  N   . THR B 147 ? 0.1464 0.1459 0.1193 -0.0049 0.0165  -0.0402 146  THR B N   
4872 C  CA  . THR B 147 ? 0.1655 0.1172 0.1635 0.0111  -0.0215 -0.0146 146  THR B CA  
4873 C  C   . THR B 147 ? 0.1541 0.1470 0.1646 -0.0299 -0.0137 -0.0275 146  THR B C   
4874 O  O   . THR B 147 ? 0.1653 0.1412 0.1730 -0.0272 0.0096  -0.0193 146  THR B O   
4875 C  CB  . THR B 147 ? 0.1591 0.1297 0.2213 0.0801  0.0094  -0.0042 146  THR B CB  
4876 O  OG1 . THR B 147 ? 0.2677 0.1431 0.2285 -0.0157 0.0208  0.0067  146  THR B OG1 
4877 C  CG2 . THR B 147 ? 0.1639 0.1872 0.2664 0.0582  -0.0143 -0.0017 146  THR B CG2 
4878 N  N   . ARG B 148 ? 0.1380 0.1610 0.1448 -0.0035 0.0036  -0.0001 147  ARG B N   
4879 C  CA  . ARG B 148 ? 0.1356 0.1818 0.1257 -0.0306 0.0007  -0.0122 147  ARG B CA  
4880 C  C   . ARG B 148 ? 0.1510 0.2047 0.1276 -0.0569 -0.0142 -0.0235 147  ARG B C   
4881 O  O   . ARG B 148 ? 0.1702 0.2340 0.1559 -0.0292 0.0017  -0.0032 147  ARG B O   
4882 C  CB  . ARG B 148 ? 0.1705 0.1877 0.1412 -0.0340 -0.0714 -0.0468 147  ARG B CB  
4883 C  CG  . ARG B 148 ? 0.1190 0.1918 0.1467 -0.0250 -0.0503 -0.0564 147  ARG B CG  
4884 C  CD  . ARG B 148 ? 0.1224 0.2156 0.1710 -0.0085 -0.0147 -0.0640 147  ARG B CD  
4885 N  NE  . ARG B 148 ? 0.2056 0.2532 0.1914 -0.0200 -0.0171 -0.0909 147  ARG B NE  
4886 C  CZ  . ARG B 148 ? 0.2463 0.2674 0.1986 -0.0454 -0.0357 -0.1051 147  ARG B CZ  
4887 N  NH1 . ARG B 148 ? 0.2099 0.2344 0.1550 -0.0173 -0.0023 -0.0397 147  ARG B NH1 
4888 N  NH2 . ARG B 148 ? 0.3039 0.3324 0.2312 -0.0433 -0.0397 -0.1195 147  ARG B NH2 
4889 N  N   . LEU B 149 ? 0.2002 0.1529 0.1200 0.0197  -0.0059 -0.0622 148  LEU B N   
4890 C  CA  . LEU B 149 ? 0.1842 0.1718 0.1157 0.0531  -0.0126 -0.0706 148  LEU B CA  
4891 C  C   . LEU B 149 ? 0.1476 0.1943 0.1202 -0.0078 -0.0302 -0.0001 148  LEU B C   
4892 O  O   . LEU B 149 ? 0.1098 0.1884 0.1567 -0.0175 -0.0077 0.0325  148  LEU B O   
4893 C  CB  . LEU B 149 ? 0.1715 0.1686 0.1537 0.0586  0.0251  -0.0682 148  LEU B CB  
4894 C  CG  . LEU B 149 ? 0.2820 0.1856 0.1663 0.0542  -0.0076 -0.0899 148  LEU B CG  
4895 C  CD1 . LEU B 149 ? 0.2591 0.1450 0.1631 -0.0102 -0.0351 -0.0801 148  LEU B CD1 
4896 C  CD2 . LEU B 149 ? 0.4129 0.2133 0.1831 0.0581  -0.0174 -0.0860 148  LEU B CD2 
4897 N  N   . THR B 150 ? 0.1441 0.1580 0.1142 0.0277  -0.0017 -0.0026 149  THR B N   
4898 C  CA  . THR B 150 ? 0.1242 0.1899 0.0846 0.0322  0.0181  -0.0005 149  THR B CA  
4899 C  C   . THR B 150 ? 0.1692 0.1787 0.0919 0.0621  -0.0265 -0.0299 149  THR B C   
4900 O  O   . THR B 150 ? 0.1831 0.1952 0.1069 0.0297  -0.0506 -0.0214 149  THR B O   
4901 C  CB  . THR B 150 ? 0.1337 0.1626 0.1235 0.0539  0.0524  0.0224  149  THR B CB  
4902 O  OG1 . THR B 150 ? 0.1748 0.1347 0.1521 0.0107  0.0264  -0.0037 149  THR B OG1 
4903 C  CG2 . THR B 150 ? 0.1510 0.1747 0.1477 0.0049  0.0463  0.0006  149  THR B CG2 
4904 N  N   . LEU B 151 ? 0.1298 0.1717 0.1007 0.0560  0.0192  -0.0237 150  LEU B N   
4905 C  CA  . LEU B 151 ? 0.1880 0.1557 0.1190 0.0518  0.0170  -0.0488 150  LEU B CA  
4906 C  C   . LEU B 151 ? 0.1631 0.1941 0.1210 0.0256  -0.0050 -0.0183 150  LEU B C   
4907 O  O   . LEU B 151 ? 0.1503 0.1949 0.1321 -0.0091 -0.0128 -0.0207 150  LEU B O   
4908 C  CB  . LEU B 151 ? 0.2472 0.1463 0.1319 0.0593  0.0130  -0.0555 150  LEU B CB  
4909 C  CG  . LEU B 151 ? 0.2582 0.1816 0.1553 0.0281  0.0022  -0.0483 150  LEU B CG  
4910 C  CD1 . LEU B 151 ? 0.2305 0.2178 0.2182 0.0964  0.0396  -0.0295 150  LEU B CD1 
4911 C  CD2 . LEU B 151 ? 0.3511 0.2195 0.1924 0.0222  0.0677  -0.0462 150  LEU B CD2 
4912 N  N   . ASP B 152 ? 0.1945 0.2303 0.1230 0.0118  -0.0071 0.0005  151  ASP B N   
4913 C  CA  . ASP B 152 ? 0.1460 0.2155 0.1118 -0.0115 -0.0297 0.0244  151  ASP B CA  
4914 C  C   . ASP B 152 ? 0.1481 0.2089 0.0959 -0.0413 -0.0455 0.0009  151  ASP B C   
4915 O  O   . ASP B 152 ? 0.1734 0.1919 0.1201 -0.0567 0.0031  0.0039  151  ASP B O   
4916 C  CB  . ASP B 152 ? 0.1174 0.2800 0.1266 -0.0308 -0.0416 -0.0082 151  ASP B CB  
4917 C  CG  . ASP B 152 ? 0.1516 0.3271 0.1706 -0.0660 -0.0307 -0.0364 151  ASP B CG  
4918 O  OD1 . ASP B 152 ? 0.1854 0.3309 0.2093 -0.0217 0.0374  -0.0875 151  ASP B OD1 
4919 O  OD2 . ASP B 152 ? 0.2258 0.3834 0.1517 -0.0597 -0.0111 -0.0374 151  ASP B OD2 
4920 N  N   . THR B 153 ? 0.1856 0.1866 0.0903 -0.0121 -0.0283 -0.0157 152  THR B N   
4921 C  CA  . THR B 153 ? 0.1657 0.1862 0.1126 -0.0230 -0.0009 -0.0237 152  THR B CA  
4922 C  C   . THR B 153 ? 0.1850 0.1882 0.1042 -0.0273 -0.0045 0.0050  152  THR B C   
4923 O  O   . THR B 153 ? 0.1435 0.1583 0.1298 -0.0123 0.0149  0.0043  152  THR B O   
4924 C  CB  . THR B 153 ? 0.1304 0.2039 0.1300 -0.0003 -0.0002 -0.0458 152  THR B CB  
4925 O  OG1 . THR B 153 ? 0.1209 0.2067 0.1775 0.0481  -0.0201 -0.0342 152  THR B OG1 
4926 C  CG2 . THR B 153 ? 0.1309 0.2138 0.1574 -0.0239 -0.0290 -0.0162 152  THR B CG2 
4927 N  N   . ILE B 154 ? 0.1146 0.1735 0.1031 0.0060  -0.0221 0.0005  153  ILE B N   
4928 C  CA  . ILE B 154 ? 0.1539 0.2080 0.0991 0.0440  -0.0219 0.0242  153  ILE B CA  
4929 C  C   . ILE B 154 ? 0.2051 0.2284 0.1074 0.0319  -0.0521 0.0000  153  ILE B C   
4930 O  O   . ILE B 154 ? 0.1785 0.2236 0.1278 0.0188  -0.0173 -0.0034 153  ILE B O   
4931 C  CB  . ILE B 154 ? 0.0849 0.2275 0.1162 -0.0008 -0.0322 -0.0212 153  ILE B CB  
4932 C  CG1 . ILE B 154 ? 0.1602 0.2415 0.1139 -0.0332 -0.0287 -0.0399 153  ILE B CG1 
4933 C  CG2 . ILE B 154 ? 0.1497 0.2189 0.1292 0.0114  -0.0063 -0.0444 153  ILE B CG2 
4934 C  CD1 . ILE B 154 ? 0.1626 0.2418 0.1541 -0.0256 -0.0454 -0.0185 153  ILE B CD1 
4935 N  N   . GLY B 155 ? 0.1601 0.2283 0.0936 -0.0156 0.0024  0.0020  154  GLY B N   
4936 C  CA  . GLY B 155 ? 0.1191 0.2314 0.0992 -0.0499 0.0318  0.0200  154  GLY B CA  
4937 C  C   . GLY B 155 ? 0.1296 0.2498 0.1093 -0.0403 -0.0021 0.0176  154  GLY B C   
4938 O  O   . GLY B 155 ? 0.1059 0.2661 0.1131 -0.0262 0.0080  0.0054  154  GLY B O   
4939 N  N   . LEU B 156 ? 0.1628 0.2339 0.0962 -0.0411 -0.0005 0.0340  155  LEU B N   
4940 C  CA  . LEU B 156 ? 0.1729 0.2072 0.1064 0.0220  -0.0280 0.0385  155  LEU B CA  
4941 C  C   . LEU B 156 ? 0.1770 0.2183 0.1236 -0.0137 -0.0141 0.0260  155  LEU B C   
4942 O  O   . LEU B 156 ? 0.1893 0.2341 0.1474 -0.0165 -0.0020 0.0308  155  LEU B O   
4943 C  CB  . LEU B 156 ? 0.1903 0.2070 0.1173 0.0520  -0.0003 0.0372  155  LEU B CB  
4944 C  CG  . LEU B 156 ? 0.1572 0.2215 0.1424 0.0614  -0.0004 0.0412  155  LEU B CG  
4945 C  CD1 . LEU B 156 ? 0.1930 0.2392 0.1342 0.0651  0.0134  0.0345  155  LEU B CD1 
4946 C  CD2 . LEU B 156 ? 0.1984 0.2180 0.1587 0.0257  -0.0338 0.0499  155  LEU B CD2 
4947 N  N   . CYS B 157 ? 0.2153 0.2253 0.1162 -0.0481 0.0057  0.0084  156  CYS B N   
4948 C  CA  . CYS B 157 ? 0.1196 0.2282 0.1451 -0.0613 0.0261  -0.0099 156  CYS B CA  
4949 C  C   . CYS B 157 ? 0.1564 0.2245 0.1583 -0.0718 -0.0298 0.0129  156  CYS B C   
4950 O  O   . CYS B 157 ? 0.1305 0.2379 0.1998 -0.0236 -0.0026 0.0279  156  CYS B O   
4951 C  CB  . CYS B 157 ? 0.1282 0.2283 0.1649 0.0186  0.0509  0.0002  156  CYS B CB  
4952 S  SG  . CYS B 157 ? 0.2099 0.2149 0.2183 0.0028  0.0364  -0.0110 156  CYS B SG  
4953 N  N   . GLY B 158 ? 0.1631 0.2062 0.1290 -0.0200 -0.0132 0.0249  157  GLY B N   
4954 C  CA  . GLY B 158 ? 0.1249 0.2299 0.1050 0.0147  -0.0108 0.0256  157  GLY B CA  
4955 C  C   . GLY B 158 ? 0.2056 0.2346 0.1353 0.0031  0.0157  0.0217  157  GLY B C   
4956 O  O   . GLY B 158 ? 0.2026 0.2537 0.1472 0.0308  -0.0068 0.0125  157  GLY B O   
4957 N  N   . PHE B 159 ? 0.1848 0.2266 0.1364 -0.0030 0.0070  0.0431  158  PHE B N   
4958 C  CA  . PHE B 159 ? 0.1557 0.2227 0.1365 -0.0248 0.0369  0.0342  158  PHE B CA  
4959 C  C   . PHE B 159 ? 0.1686 0.2555 0.1181 -0.0105 0.0116  0.0109  158  PHE B C   
4960 O  O   . PHE B 159 ? 0.1906 0.2668 0.1354 0.0104  -0.0015 0.0200  158  PHE B O   
4961 C  CB  . PHE B 159 ? 0.1801 0.2073 0.1562 -0.0107 -0.0080 0.0620  158  PHE B CB  
4962 C  CG  . PHE B 159 ? 0.2050 0.2094 0.1688 -0.0348 -0.0103 0.0552  158  PHE B CG  
4963 C  CD1 . PHE B 159 ? 0.2434 0.1844 0.2027 -0.0099 -0.0204 0.0687  158  PHE B CD1 
4964 C  CD2 . PHE B 159 ? 0.1860 0.2293 0.1815 -0.0534 -0.0005 0.0811  158  PHE B CD2 
4965 C  CE1 . PHE B 159 ? 0.2354 0.2182 0.2047 -0.0069 0.0166  0.0613  158  PHE B CE1 
4966 C  CE2 . PHE B 159 ? 0.2353 0.2394 0.2056 -0.0113 0.0041  0.0634  158  PHE B CE2 
4967 C  CZ  . PHE B 159 ? 0.1988 0.2309 0.2082 -0.0266 -0.0056 0.0438  158  PHE B CZ  
4968 N  N   . ASN B 160 ? 0.1628 0.2584 0.1115 -0.0402 -0.0005 0.0147  159  ASN B N   
4969 C  CA  . ASN B 160 ? 0.1762 0.2890 0.1264 -0.0658 0.0116  0.0399  159  ASN B CA  
4970 C  C   . ASN B 160 ? 0.1873 0.3026 0.1336 -0.0255 0.0299  0.0095  159  ASN B C   
4971 O  O   . ASN B 160 ? 0.1866 0.3389 0.1454 -0.0176 0.0328  -0.0071 159  ASN B O   
4972 C  CB  . ASN B 160 ? 0.2089 0.3169 0.1693 -0.0675 0.0213  0.0706  159  ASN B CB  
4973 C  CG  . ASN B 160 ? 0.2892 0.3591 0.2602 -0.0307 0.0490  0.0937  159  ASN B CG  
4974 O  OD1 . ASN B 160 ? 0.2755 0.3577 0.2845 0.0093  0.0275  0.0779  159  ASN B OD1 
4975 N  ND2 . ASN B 160 ? 0.3321 0.3878 0.3099 -0.0017 0.0543  0.1254  159  ASN B ND2 
4976 N  N   . TYR B 161 ? 0.1505 0.3041 0.1251 -0.0107 -0.0252 -0.0157 160  TYR B N   
4977 C  CA  . TYR B 161 ? 0.0993 0.2709 0.1503 0.0230  -0.0469 -0.0326 160  TYR B CA  
4978 C  C   . TYR B 161 ? 0.1148 0.2739 0.1416 0.0580  -0.0442 -0.0192 160  TYR B C   
4979 O  O   . TYR B 161 ? 0.1678 0.3177 0.1157 0.0381  0.0074  -0.0060 160  TYR B O   
4980 C  CB  . TYR B 161 ? 0.2189 0.3263 0.1876 0.0571  -0.0775 -0.0453 160  TYR B CB  
4981 C  CG  . TYR B 161 ? 0.3404 0.3536 0.2104 0.1004  -0.0893 -0.0626 160  TYR B CG  
4982 C  CD1 . TYR B 161 ? 0.4189 0.3550 0.1904 0.1576  -0.0792 -0.0417 160  TYR B CD1 
4983 C  CD2 . TYR B 161 ? 0.3787 0.3522 0.2217 0.1367  -0.1208 -0.0712 160  TYR B CD2 
4984 C  CE1 . TYR B 161 ? 0.4587 0.3499 0.2156 0.2295  -0.0856 -0.0571 160  TYR B CE1 
4985 C  CE2 . TYR B 161 ? 0.4828 0.3700 0.2402 0.1485  -0.1109 -0.0758 160  TYR B CE2 
4986 C  CZ  . TYR B 161 ? 0.5302 0.3761 0.2352 0.1975  -0.0994 -0.0650 160  TYR B CZ  
4987 O  OH  . TYR B 161 ? 0.6505 0.3973 0.2663 0.2121  -0.1153 -0.0490 160  TYR B OH  
4988 N  N   . ARG B 162 ? 0.1081 0.2795 0.1373 0.0325  -0.0448 0.0012  161  ARG B N   
4989 C  CA  . ARG B 162 ? 0.1270 0.2339 0.1560 0.0299  -0.0744 0.0077  161  ARG B CA  
4990 C  C   . ARG B 162 ? 0.1254 0.2231 0.1435 0.0261  -0.0186 0.0104  161  ARG B C   
4991 O  O   . ARG B 162 ? 0.1691 0.2373 0.1311 0.0096  0.0137  -0.0218 161  ARG B O   
4992 C  CB  . ARG B 162 ? 0.1255 0.2578 0.1911 0.0667  -0.0616 -0.0321 161  ARG B CB  
4993 C  CG  . ARG B 162 ? 0.2009 0.2608 0.2014 0.0693  -0.0589 -0.0160 161  ARG B CG  
4994 C  CD  . ARG B 162 ? 0.2628 0.2663 0.1871 0.0464  -0.0146 -0.0354 161  ARG B CD  
4995 N  NE  . ARG B 162 ? 0.1862 0.2663 0.1762 0.0048  0.0106  -0.0155 161  ARG B NE  
4996 C  CZ  . ARG B 162 ? 0.1903 0.2489 0.1446 -0.0062 0.0056  0.0101  161  ARG B CZ  
4997 N  NH1 . ARG B 162 ? 0.1794 0.2307 0.1231 0.0316  -0.0125 0.0154  161  ARG B NH1 
4998 N  NH2 . ARG B 162 ? 0.1886 0.2580 0.1520 -0.0473 0.0092  0.0131  161  ARG B NH2 
4999 N  N   . PHE B 163 ? 0.1425 0.2250 0.1540 0.0129  -0.0288 0.0197  162  PHE B N   
5000 C  CA  . PHE B 163 ? 0.1951 0.2530 0.1309 -0.0052 -0.0487 0.0432  162  PHE B CA  
5001 C  C   . PHE B 163 ? 0.1250 0.2624 0.1302 0.0172  -0.0093 -0.0016 162  PHE B C   
5002 O  O   . PHE B 163 ? 0.1555 0.2767 0.1135 0.0077  -0.0112 -0.0082 162  PHE B O   
5003 C  CB  . PHE B 163 ? 0.2143 0.2843 0.1270 0.0646  -0.0297 0.0185  162  PHE B CB  
5004 C  CG  . PHE B 163 ? 0.2120 0.3264 0.1533 0.0679  0.0005  -0.0099 162  PHE B CG  
5005 C  CD1 . PHE B 163 ? 0.3906 0.4028 0.1618 0.1035  -0.0664 -0.0401 162  PHE B CD1 
5006 C  CD2 . PHE B 163 ? 0.1770 0.3351 0.1398 -0.0107 -0.0110 0.0099  162  PHE B CD2 
5007 C  CE1 . PHE B 163 ? 0.4072 0.4323 0.1573 0.1288  -0.0470 -0.0562 162  PHE B CE1 
5008 C  CE2 . PHE B 163 ? 0.2634 0.3615 0.1645 0.0233  0.0323  0.0021  162  PHE B CE2 
5009 C  CZ  . PHE B 163 ? 0.3182 0.4032 0.1635 0.0634  -0.0082 -0.0477 162  PHE B CZ  
5010 N  N   . ASN B 164 ? 0.1454 0.2314 0.0916 0.0024  -0.0011 0.0240  163  ASN B N   
5011 C  CA  . ASN B 164 ? 0.1426 0.2552 0.0679 -0.0183 0.0025  0.0217  163  ASN B CA  
5012 C  C   . ASN B 164 ? 0.1802 0.2458 0.0805 -0.0203 -0.0058 0.0061  163  ASN B C   
5013 O  O   . ASN B 164 ? 0.1700 0.2378 0.1044 -0.0028 -0.0251 -0.0085 163  ASN B O   
5014 C  CB  . ASN B 164 ? 0.1303 0.2815 0.0924 -0.0099 -0.0159 0.0555  163  ASN B CB  
5015 C  CG  . ASN B 164 ? 0.2117 0.3365 0.1200 -0.0190 -0.0048 0.0169  163  ASN B CG  
5016 O  OD1 . ASN B 164 ? 0.2029 0.3728 0.1401 0.0228  0.0526  0.0318  163  ASN B OD1 
5017 N  ND2 . ASN B 164 ? 0.1640 0.3353 0.1082 -0.0692 0.0146  -0.0166 163  ASN B ND2 
5018 N  N   . SER B 165 ? 0.1543 0.2313 0.1028 0.0054  -0.0005 0.0207  164  SER B N   
5019 C  CA  . SER B 165 ? 0.1301 0.2301 0.1175 -0.0221 0.0051  0.0174  164  SER B CA  
5020 C  C   . SER B 165 ? 0.1448 0.2103 0.1353 -0.0183 -0.0210 -0.0188 164  SER B C   
5021 O  O   . SER B 165 ? 0.1499 0.2130 0.1581 -0.0090 -0.0017 -0.0366 164  SER B O   
5022 C  CB  . SER B 165 ? 0.2038 0.2156 0.0992 -0.0194 -0.0412 0.0229  164  SER B CB  
5023 O  OG  . SER B 165 ? 0.2006 0.2300 0.1115 0.0173  -0.0456 0.0382  164  SER B OG  
5024 N  N   . PHE B 166 ? 0.1612 0.2228 0.1388 0.0534  -0.0313 -0.0029 165  PHE B N   
5025 C  CA  . PHE B 166 ? 0.1878 0.2344 0.1294 0.0388  -0.0174 -0.0429 165  PHE B CA  
5026 C  C   . PHE B 166 ? 0.2497 0.2382 0.1446 0.0444  -0.0199 -0.0521 165  PHE B C   
5027 O  O   . PHE B 166 ? 0.2433 0.2633 0.1898 0.0353  -0.0414 -0.0555 165  PHE B O   
5028 C  CB  . PHE B 166 ? 0.1286 0.2619 0.1305 0.0083  -0.0451 -0.0545 165  PHE B CB  
5029 C  CG  . PHE B 166 ? 0.1492 0.2332 0.1416 0.0220  -0.0225 -0.0398 165  PHE B CG  
5030 C  CD1 . PHE B 166 ? 0.2007 0.2102 0.1562 0.0657  -0.0088 -0.0328 165  PHE B CD1 
5031 C  CD2 . PHE B 166 ? 0.1839 0.2201 0.1341 -0.0129 -0.0079 -0.0461 165  PHE B CD2 
5032 C  CE1 . PHE B 166 ? 0.2183 0.2125 0.1678 0.0108  0.0195  -0.0225 165  PHE B CE1 
5033 C  CE2 . PHE B 166 ? 0.1618 0.2243 0.1708 0.0420  0.0040  -0.0157 165  PHE B CE2 
5034 C  CZ  . PHE B 166 ? 0.1534 0.2267 0.1591 0.0479  0.0109  -0.0119 165  PHE B CZ  
5035 N  N   . TYR B 167 ? 0.1801 0.2217 0.1288 0.0043  0.0296  -0.0423 166  TYR B N   
5036 C  CA  . TYR B 167 ? 0.2153 0.2172 0.1368 -0.0900 0.0067  -0.0129 166  TYR B CA  
5037 C  C   . TYR B 167 ? 0.2543 0.2595 0.1763 -0.0670 -0.0240 0.0019  166  TYR B C   
5038 O  O   . TYR B 167 ? 0.3493 0.2622 0.1478 -0.0365 -0.0563 -0.0029 166  TYR B O   
5039 C  CB  . TYR B 167 ? 0.1704 0.2003 0.1268 -0.0230 -0.0078 0.0021  166  TYR B CB  
5040 C  CG  . TYR B 167 ? 0.1962 0.2011 0.1181 -0.0261 -0.0336 -0.0071 166  TYR B CG  
5041 C  CD1 . TYR B 167 ? 0.1700 0.1995 0.1299 -0.0290 -0.0220 -0.0103 166  TYR B CD1 
5042 C  CD2 . TYR B 167 ? 0.2154 0.2132 0.1404 -0.0306 0.0132  0.0108  166  TYR B CD2 
5043 C  CE1 . TYR B 167 ? 0.1785 0.2156 0.1279 -0.0015 0.0020  -0.0079 166  TYR B CE1 
5044 C  CE2 . TYR B 167 ? 0.1512 0.1945 0.1419 -0.0337 0.0149  -0.0090 166  TYR B CE2 
5045 C  CZ  . TYR B 167 ? 0.1767 0.2169 0.1283 -0.0206 -0.0175 0.0014  166  TYR B CZ  
5046 O  OH  . TYR B 167 ? 0.2115 0.2163 0.1205 -0.0805 -0.0264 -0.0094 166  TYR B OH  
5047 N  N   . ARG B 168 ? 0.2101 0.2648 0.2154 -0.0477 -0.0364 0.0508  167  ARG B N   
5048 C  CA  . ARG B 168 ? 0.2645 0.2816 0.2464 -0.0554 -0.0767 0.0057  167  ARG B CA  
5049 C  C   . ARG B 168 ? 0.3414 0.2903 0.2587 -0.0792 -0.0969 -0.0190 167  ARG B C   
5050 O  O   . ARG B 168 ? 0.3213 0.2952 0.2277 -0.0777 -0.0122 -0.0735 167  ARG B O   
5051 C  CB  . ARG B 168 ? 0.3043 0.3120 0.2563 -0.0422 -0.0655 0.0187  167  ARG B CB  
5052 C  CG  . ARG B 168 ? 0.1708 0.3460 0.2693 -0.0062 -0.0925 0.0127  167  ARG B CG  
5053 C  CD  . ARG B 168 ? 0.1569 0.3579 0.2893 -0.0191 -0.0552 0.0286  167  ARG B CD  
5054 N  NE  . ARG B 168 ? 0.3164 0.3871 0.3250 0.0379  -0.0229 0.0178  167  ARG B NE  
5055 C  CZ  . ARG B 168 ? 0.3989 0.4025 0.3615 -0.0135 0.0054  0.0095  167  ARG B CZ  
5056 N  NH1 . ARG B 168 ? 0.4817 0.3767 0.3934 0.0350  -0.0227 0.0225  167  ARG B NH1 
5057 N  NH2 . ARG B 168 ? 0.3736 0.4097 0.3579 -0.0835 0.0226  0.0101  167  ARG B NH2 
5058 N  N   . ASP B 169 ? 0.4475 0.2849 0.3253 -0.1505 -0.0643 0.0151  168  ASP B N   
5059 C  CA  . ASP B 169 ? 0.5007 0.3436 0.3676 -0.1474 -0.1153 0.0311  168  ASP B CA  
5060 C  C   . ASP B 169 ? 0.5534 0.3365 0.3627 -0.1632 -0.1228 0.0170  168  ASP B C   
5061 O  O   . ASP B 169 ? 0.5198 0.3122 0.3399 -0.2010 -0.0760 0.0341  168  ASP B O   
5062 C  CB  . ASP B 169 ? 0.4883 0.3986 0.4158 -0.2105 -0.1375 0.0487  168  ASP B CB  
5063 C  CG  . ASP B 169 ? 0.6143 0.4404 0.4673 -0.2354 -0.1255 0.0528  168  ASP B CG  
5064 O  OD1 . ASP B 169 ? 0.6924 0.4583 0.5120 -0.1843 -0.1465 0.0358  168  ASP B OD1 
5065 O  OD2 . ASP B 169 ? 0.6734 0.5061 0.4925 -0.2064 -0.1118 0.0484  168  ASP B OD2 
5066 N  N   . GLN B 170 ? 0.5416 0.3630 0.3805 -0.1327 -0.2034 -0.0025 169  GLN B N   
5067 C  CA  . GLN B 170 ? 0.5496 0.3909 0.4137 -0.0934 -0.2187 -0.0018 169  GLN B CA  
5068 C  C   . GLN B 170 ? 0.4744 0.3549 0.3709 -0.0373 -0.2055 0.0175  169  GLN B C   
5069 O  O   . GLN B 170 ? 0.4952 0.3526 0.3644 -0.0039 -0.1958 0.0342  169  GLN B O   
5070 C  CB  . GLN B 170 ? 0.6305 0.4794 0.5032 -0.1089 -0.2016 0.0005  169  GLN B CB  
5071 C  CG  . GLN B 170 ? 0.7565 0.5780 0.6191 -0.1050 -0.1793 0.0036  169  GLN B CG  
5072 C  CD  . GLN B 170 ? 0.8960 0.6375 0.7005 -0.1208 -0.1739 0.0080  169  GLN B CD  
5073 O  OE1 . GLN B 170 ? 0.9518 0.6630 0.7105 -0.1312 -0.1790 0.0011  169  GLN B OE1 
5074 N  NE2 . GLN B 170 ? 0.9101 0.6544 0.7359 -0.1364 -0.1543 0.0045  169  GLN B NE2 
5075 N  N   . PRO B 171 ? 0.4503 0.3369 0.3458 -0.0427 -0.1686 0.0252  170  PRO B N   
5076 C  CA  . PRO B 171 ? 0.4711 0.3404 0.3285 0.0034  -0.1519 0.0339  170  PRO B CA  
5077 C  C   . PRO B 171 ? 0.4837 0.3131 0.3130 0.0122  -0.1522 0.0304  170  PRO B C   
5078 O  O   . PRO B 171 ? 0.4914 0.2733 0.2945 0.0769  -0.0975 -0.0048 170  PRO B O   
5079 C  CB  . PRO B 171 ? 0.4276 0.3470 0.3367 0.0129  -0.1583 0.0386  170  PRO B CB  
5080 C  CG  . PRO B 171 ? 0.5032 0.3502 0.3422 0.0054  -0.1641 0.0357  170  PRO B CG  
5081 C  CD  . PRO B 171 ? 0.4853 0.3306 0.3126 -0.0184 -0.1708 0.0500  170  PRO B CD  
5082 N  N   . HIS B 172 ? 0.4619 0.3126 0.2992 -0.0125 -0.2066 0.0307  171  HIS B N   
5083 C  CA  . HIS B 172 ? 0.4919 0.3109 0.2890 -0.0382 -0.1036 0.0314  171  HIS B CA  
5084 C  C   . HIS B 172 ? 0.4832 0.2966 0.2410 -0.0048 -0.0278 0.0035  171  HIS B C   
5085 O  O   . HIS B 172 ? 0.3980 0.2642 0.2337 -0.0598 0.0154  -0.0172 171  HIS B O   
5086 C  CB  . HIS B 172 ? 0.5298 0.2921 0.3085 -0.1234 -0.1118 0.0469  171  HIS B CB  
5087 C  CG  . HIS B 172 ? 0.5857 0.3046 0.3077 -0.1359 -0.1348 0.0671  171  HIS B CG  
5088 N  ND1 . HIS B 172 ? 0.6405 0.3087 0.3130 -0.1130 -0.1482 0.0737  171  HIS B ND1 
5089 C  CD2 . HIS B 172 ? 0.6228 0.3055 0.3078 -0.2002 -0.1515 0.0661  171  HIS B CD2 
5090 C  CE1 . HIS B 172 ? 0.5919 0.2933 0.3152 -0.1631 -0.1570 0.0930  171  HIS B CE1 
5091 N  NE2 . HIS B 172 ? 0.6026 0.3158 0.3122 -0.2227 -0.1382 0.0689  171  HIS B NE2 
5092 N  N   . PRO B 173 ? 0.4901 0.3385 0.1966 0.0104  0.0601  -0.0078 172  PRO B N   
5093 C  CA  . PRO B 173 ? 0.4563 0.3370 0.1906 0.0047  0.0333  -0.0150 172  PRO B CA  
5094 C  C   . PRO B 173 ? 0.4090 0.3141 0.2205 -0.0678 0.0472  -0.0194 172  PRO B C   
5095 O  O   . PRO B 173 ? 0.3315 0.2909 0.2273 -0.0876 0.0345  -0.0340 172  PRO B O   
5096 C  CB  . PRO B 173 ? 0.5303 0.3565 0.1864 0.0464  0.0535  -0.0170 172  PRO B CB  
5097 C  CG  . PRO B 173 ? 0.5745 0.3748 0.1832 0.0241  0.0760  -0.0084 172  PRO B CG  
5098 C  CD  . PRO B 173 ? 0.5809 0.3627 0.1773 0.0334  0.0774  -0.0041 172  PRO B CD  
5099 N  N   . PHE B 174 ? 0.3128 0.2863 0.2086 -0.0859 0.0148  -0.0056 173  PHE B N   
5100 C  CA  . PHE B 174 ? 0.3264 0.2738 0.1934 -0.0569 -0.0548 -0.0315 173  PHE B CA  
5101 C  C   . PHE B 174 ? 0.2988 0.2537 0.1826 -0.0170 -0.0555 -0.0009 173  PHE B C   
5102 O  O   . PHE B 174 ? 0.3606 0.2636 0.2007 0.0085  -0.0337 0.0097  173  PHE B O   
5103 C  CB  . PHE B 174 ? 0.3440 0.2891 0.1991 -0.0591 -0.0726 -0.0342 173  PHE B CB  
5104 C  CG  . PHE B 174 ? 0.3504 0.2812 0.2358 -0.0187 -0.0380 -0.0378 173  PHE B CG  
5105 C  CD1 . PHE B 174 ? 0.3143 0.2753 0.2460 -0.0056 -0.0337 -0.0396 173  PHE B CD1 
5106 C  CD2 . PHE B 174 ? 0.3265 0.2613 0.2517 -0.0448 -0.0209 -0.0385 173  PHE B CD2 
5107 C  CE1 . PHE B 174 ? 0.3570 0.2765 0.2604 0.0348  -0.0126 -0.0463 173  PHE B CE1 
5108 C  CE2 . PHE B 174 ? 0.2852 0.2690 0.2750 0.0151  -0.0007 -0.0339 173  PHE B CE2 
5109 C  CZ  . PHE B 174 ? 0.3402 0.2715 0.2821 0.0379  -0.0066 -0.0262 173  PHE B CZ  
5110 N  N   . ILE B 175 ? 0.3231 0.2363 0.1878 -0.0017 -0.0265 -0.0055 174  ILE B N   
5111 C  CA  . ILE B 175 ? 0.3268 0.2226 0.2163 0.0018  -0.0311 -0.0136 174  ILE B CA  
5112 C  C   . ILE B 175 ? 0.3074 0.2105 0.2287 0.0376  -0.0372 -0.0037 174  ILE B C   
5113 O  O   . ILE B 175 ? 0.3010 0.1958 0.2126 0.0468  -0.0395 0.0128  174  ILE B O   
5114 C  CB  . ILE B 175 ? 0.3517 0.2042 0.2273 -0.0480 -0.0071 -0.0139 174  ILE B CB  
5115 C  CG1 . ILE B 175 ? 0.3832 0.1975 0.2318 -0.0681 -0.0394 -0.0406 174  ILE B CG1 
5116 C  CG2 . ILE B 175 ? 0.3062 0.1782 0.2236 -0.0658 0.0519  -0.0188 174  ILE B CG2 
5117 C  CD1 . ILE B 175 ? 0.3194 0.2194 0.2304 -0.0771 -0.0543 -0.0373 174  ILE B CD1 
5118 N  N   . THR B 176 ? 0.3056 0.2213 0.2502 0.0101  -0.0316 0.0057  175  THR B N   
5119 C  CA  . THR B 176 ? 0.3833 0.2414 0.2398 -0.0181 -0.0814 0.0095  175  THR B CA  
5120 C  C   . THR B 176 ? 0.3464 0.2718 0.2636 -0.0049 -0.0267 0.0023  175  THR B C   
5121 O  O   . THR B 176 ? 0.2597 0.2380 0.2655 0.0484  -0.0249 0.0082  175  THR B O   
5122 C  CB  . THR B 176 ? 0.4453 0.2584 0.2197 -0.0435 -0.1405 0.0069  175  THR B CB  
5123 O  OG1 . THR B 176 ? 0.5011 0.2997 0.2500 -0.0521 -0.1065 0.0098  175  THR B OG1 
5124 C  CG2 . THR B 176 ? 0.4996 0.2697 0.1987 -0.0523 -0.1135 0.0247  175  THR B CG2 
5125 N  N   . SER B 177 ? 0.3190 0.2978 0.2598 -0.0211 -0.0126 -0.0164 176  SER B N   
5126 C  CA  . SER B 177 ? 0.2952 0.2714 0.2390 -0.0046 0.0822  0.0050  176  SER B CA  
5127 C  C   . SER B 177 ? 0.2881 0.2317 0.2016 0.0079  0.0474  -0.0093 176  SER B C   
5128 O  O   . SER B 177 ? 0.3631 0.2065 0.1783 0.0608  0.0195  -0.0254 176  SER B O   
5129 C  CB  . SER B 177 ? 0.3583 0.2999 0.2448 0.0645  0.1384  -0.0084 176  SER B CB  
5130 O  OG  . SER B 177 ? 0.3964 0.3245 0.2304 0.0686  0.1342  0.0181  176  SER B OG  
5131 N  N   . MET B 178 ? 0.2200 0.2135 0.1733 -0.0231 0.0267  -0.0451 177  MET B N   
5132 C  CA  . MET B 178 ? 0.2972 0.2112 0.1832 -0.0402 0.0330  -0.0654 177  MET B CA  
5133 C  C   . MET B 178 ? 0.2180 0.2346 0.2066 -0.0870 -0.0404 -0.0297 177  MET B C   
5134 O  O   . MET B 178 ? 0.2567 0.2640 0.1891 -0.0376 -0.0090 -0.0327 177  MET B O   
5135 C  CB  . MET B 178 ? 0.2835 0.1992 0.1905 -0.0541 -0.0044 -0.0859 177  MET B CB  
5136 C  CG  . MET B 178 ? 0.3289 0.1709 0.2277 -0.0292 -0.0378 -0.0729 177  MET B CG  
5137 S  SD  . MET B 178 ? 0.2658 0.2333 0.2692 -0.0041 -0.0414 -0.0424 177  MET B SD  
5138 C  CE  . MET B 178 ? 0.1785 0.2573 0.2722 -0.0534 -0.0106 -0.0563 177  MET B CE  
5139 N  N   . VAL B 179 ? 0.2416 0.2382 0.2324 -0.0924 -0.0265 -0.0197 178  VAL B N   
5140 C  CA  . VAL B 179 ? 0.2233 0.2401 0.2491 -0.0496 0.0065  0.0001  178  VAL B CA  
5141 C  C   . VAL B 179 ? 0.3252 0.2378 0.2576 -0.0117 0.0106  -0.0032 178  VAL B C   
5142 O  O   . VAL B 179 ? 0.2213 0.2172 0.2525 0.0055  0.0082  0.0132  178  VAL B O   
5143 C  CB  . VAL B 179 ? 0.1426 0.2585 0.2419 0.0051  -0.0102 0.0311  178  VAL B CB  
5144 C  CG1 . VAL B 179 ? 0.1604 0.3049 0.2652 0.0017  0.0169  0.0322  178  VAL B CG1 
5145 C  CG2 . VAL B 179 ? 0.2570 0.2669 0.2268 -0.0097 -0.0067 0.0116  178  VAL B CG2 
5146 N  N   . ARG B 180 ? 0.3330 0.2113 0.2377 0.0134  0.0062  -0.0388 179  ARG B N   
5147 C  CA  . ARG B 180 ? 0.3684 0.2007 0.2213 0.0387  -0.0285 -0.0785 179  ARG B CA  
5148 C  C   . ARG B 180 ? 0.4011 0.2153 0.1996 0.0280  -0.0197 -0.0514 179  ARG B C   
5149 O  O   . ARG B 180 ? 0.4651 0.2217 0.2206 0.0359  -0.0452 -0.0302 179  ARG B O   
5150 C  CB  . ARG B 180 ? 0.4255 0.2202 0.2233 0.0477  0.0181  -0.1046 179  ARG B CB  
5151 C  CG  . ARG B 180 ? 0.4823 0.2475 0.2350 -0.0228 -0.0293 -0.1157 179  ARG B CG  
5152 C  CD  . ARG B 180 ? 0.4959 0.3110 0.2541 -0.0544 -0.0105 -0.1142 179  ARG B CD  
5153 N  NE  . ARG B 180 ? 0.4555 0.3532 0.2711 -0.0703 0.0096  -0.1078 179  ARG B NE  
5154 C  CZ  . ARG B 180 ? 0.4089 0.3738 0.3096 -0.0512 0.0189  -0.1081 179  ARG B CZ  
5155 N  NH1 . ARG B 180 ? 0.4337 0.3755 0.3391 0.0239  0.0426  -0.1397 179  ARG B NH1 
5156 N  NH2 . ARG B 180 ? 0.3465 0.3868 0.3120 -0.0396 0.0405  -0.0487 179  ARG B NH2 
5157 N  N   . ALA B 181 ? 0.3142 0.2536 0.1925 -0.0501 -0.0348 -0.0376 180  ALA B N   
5158 C  CA  . ALA B 181 ? 0.2106 0.2701 0.2116 -0.0486 -0.0170 -0.0133 180  ALA B CA  
5159 C  C   . ALA B 181 ? 0.2738 0.2494 0.2001 0.0265  -0.0001 -0.0395 180  ALA B C   
5160 O  O   . ALA B 181 ? 0.3171 0.2311 0.2125 0.0358  -0.0398 -0.0299 180  ALA B O   
5161 C  CB  . ALA B 181 ? 0.1401 0.2730 0.2494 -0.0800 -0.0266 0.0138  180  ALA B CB  
5162 N  N   . LEU B 182 ? 0.2689 0.2124 0.1997 0.0283  0.0110  -0.0367 181  LEU B N   
5163 C  CA  . LEU B 182 ? 0.3074 0.2080 0.2025 -0.0382 0.0098  -0.0145 181  LEU B CA  
5164 C  C   . LEU B 182 ? 0.3079 0.2455 0.2204 -0.0345 0.0027  0.0019  181  LEU B C   
5165 O  O   . LEU B 182 ? 0.2657 0.2913 0.2283 0.0053  -0.0146 0.0004  181  LEU B O   
5166 C  CB  . LEU B 182 ? 0.3002 0.1820 0.2115 0.0101  -0.0002 -0.0260 181  LEU B CB  
5167 C  CG  . LEU B 182 ? 0.2399 0.1834 0.2004 0.0327  -0.0313 0.0008  181  LEU B CG  
5168 C  CD1 . LEU B 182 ? 0.3315 0.2159 0.2141 0.0060  -0.0187 0.0078  181  LEU B CD1 
5169 C  CD2 . LEU B 182 ? 0.2215 0.2190 0.2032 0.0265  -0.0438 -0.0135 181  LEU B CD2 
5170 N  N   . ASP B 183 ? 0.3082 0.2516 0.2607 0.0110  -0.0251 -0.0151 182  ASP B N   
5171 C  CA  . ASP B 183 ? 0.3769 0.2858 0.2819 -0.0146 -0.0543 -0.0243 182  ASP B CA  
5172 C  C   . ASP B 183 ? 0.3487 0.2577 0.2672 0.0208  -0.0584 -0.0139 182  ASP B C   
5173 O  O   . ASP B 183 ? 0.3395 0.2650 0.2902 0.0093  -0.0305 0.0062  182  ASP B O   
5174 C  CB  . ASP B 183 ? 0.4097 0.3533 0.3285 -0.0122 -0.0846 -0.0596 182  ASP B CB  
5175 C  CG  . ASP B 183 ? 0.6042 0.4575 0.4028 -0.0714 -0.0725 -0.0757 182  ASP B CG  
5176 O  OD1 . ASP B 183 ? 0.6777 0.4924 0.4607 -0.0535 -0.0841 -0.0824 182  ASP B OD1 
5177 O  OD2 . ASP B 183 ? 0.7089 0.5033 0.4427 -0.1008 -0.0344 -0.0680 182  ASP B OD2 
5178 N  N   . GLU B 184 ? 0.2233 0.2344 0.2748 0.0506  -0.0504 -0.0211 183  GLU B N   
5179 C  CA  . GLU B 184 ? 0.1811 0.2039 0.2713 0.0342  -0.0523 -0.0174 183  GLU B CA  
5180 C  C   . GLU B 184 ? 0.2916 0.1788 0.2430 -0.0340 -0.0602 -0.0288 183  GLU B C   
5181 O  O   . GLU B 184 ? 0.3850 0.1950 0.2473 -0.0022 -0.0307 -0.0146 183  GLU B O   
5182 C  CB  . GLU B 184 ? 0.2758 0.2080 0.2844 0.0409  0.0030  -0.0268 183  GLU B CB  
5183 C  CG  . GLU B 184 ? 0.3127 0.2008 0.3140 0.0432  -0.0441 -0.0004 183  GLU B CG  
5184 C  CD  . GLU B 184 ? 0.3900 0.2094 0.3257 0.0222  -0.0627 -0.0051 183  GLU B CD  
5185 O  OE1 . GLU B 184 ? 0.4117 0.2067 0.3128 0.0244  -0.0504 -0.0303 183  GLU B OE1 
5186 O  OE2 . GLU B 184 ? 0.4460 0.2164 0.3162 0.0579  -0.0520 0.0259  183  GLU B OE2 
5187 N  N   . ALA B 185 ? 0.2825 0.2097 0.2431 -0.0578 -0.0367 -0.0106 184  ALA B N   
5188 C  CA  . ALA B 185 ? 0.3034 0.1910 0.2100 -0.0898 0.0284  -0.0171 184  ALA B CA  
5189 C  C   . ALA B 185 ? 0.3121 0.2291 0.2033 0.0042  0.0232  -0.0271 184  ALA B C   
5190 O  O   . ALA B 185 ? 0.3655 0.2601 0.1892 0.0184  0.0221  -0.0072 184  ALA B O   
5191 C  CB  . ALA B 185 ? 0.3301 0.1916 0.2338 0.0019  -0.0327 -0.0144 184  ALA B CB  
5192 N  N   . MET B 186 ? 0.1906 0.2053 0.2043 0.0668  0.0174  -0.0173 185  MET B N   
5193 C  CA  . MET B 186 ? 0.1941 0.2109 0.2251 0.0380  0.0332  -0.0273 185  MET B CA  
5194 C  C   . MET B 186 ? 0.2688 0.2132 0.2463 -0.0014 0.0184  -0.0228 185  MET B C   
5195 O  O   . MET B 186 ? 0.2904 0.2173 0.2074 0.0233  0.0491  -0.0026 185  MET B O   
5196 C  CB  . MET B 186 ? 0.2283 0.2326 0.2385 0.0132  0.0431  -0.0324 185  MET B CB  
5197 C  CG  . MET B 186 ? 0.2000 0.2384 0.2214 0.0033  0.0238  -0.0102 185  MET B CG  
5198 S  SD  . MET B 186 ? 0.2469 0.2310 0.2379 0.0079  0.0135  -0.0074 185  MET B SD  
5199 C  CE  . MET B 186 ? 0.2804 0.2029 0.2698 -0.0042 -0.0558 -0.0463 185  MET B CE  
5200 N  N   . ASN B 187 ? 0.2442 0.2235 0.2861 -0.0069 -0.0619 -0.0204 186  ASN B N   
5201 C  CA  . ASN B 187 ? 0.3466 0.2336 0.3145 0.0010  -0.0995 -0.0229 186  ASN B CA  
5202 C  C   . ASN B 187 ? 0.3703 0.1889 0.3102 0.0319  -0.0690 -0.0331 186  ASN B C   
5203 O  O   . ASN B 187 ? 0.3781 0.1864 0.3075 0.0208  -0.0561 -0.0297 186  ASN B O   
5204 C  CB  . ASN B 187 ? 0.3973 0.2935 0.3234 0.0484  -0.1157 -0.0178 186  ASN B CB  
5205 C  CG  . ASN B 187 ? 0.4211 0.4338 0.3787 0.1049  -0.0878 -0.0420 186  ASN B CG  
5206 O  OD1 . ASN B 187 ? 0.4176 0.4500 0.3993 0.1022  -0.0981 -0.0315 186  ASN B OD1 
5207 N  ND2 . ASN B 187 ? 0.4072 0.5142 0.3904 0.0988  -0.0743 -0.0517 186  ASN B ND2 
5208 N  N   . LYS B 188 ? 0.3403 0.1858 0.3105 0.0607  -0.0187 -0.0296 187  LYS B N   
5209 C  CA  . LYS B 188 ? 0.3770 0.2347 0.3345 0.0419  -0.0209 -0.0329 187  LYS B CA  
5210 C  C   . LYS B 188 ? 0.3822 0.2371 0.3079 0.0084  -0.0582 -0.0201 187  LYS B C   
5211 O  O   . LYS B 188 ? 0.3717 0.2503 0.3183 0.0356  -0.0277 -0.0182 187  LYS B O   
5212 C  CB  . LYS B 188 ? 0.3979 0.2813 0.3750 0.0202  0.0216  -0.0338 187  LYS B CB  
5213 C  CG  . LYS B 188 ? 0.4937 0.3429 0.4356 0.0027  0.0431  -0.0330 187  LYS B CG  
5214 C  CD  . LYS B 188 ? 0.5021 0.3789 0.4700 -0.0351 0.0872  -0.0350 187  LYS B CD  
5215 C  CE  . LYS B 188 ? 0.4823 0.3798 0.4742 -0.0175 0.1495  -0.0484 187  LYS B CE  
5216 N  NZ  . LYS B 188 ? 0.4537 0.3889 0.4648 0.0414  0.2345  -0.0549 187  LYS B NZ  
5217 N  N   . LEU B 189 ? 0.4290 0.2239 0.2645 -0.0357 -0.0541 -0.0417 188  LEU B N   
5218 C  CA  . LEU B 189 ? 0.3903 0.2308 0.2673 -0.0250 -0.0505 0.0019  188  LEU B CA  
5219 C  C   . LEU B 189 ? 0.2797 0.2566 0.2811 -0.0192 -0.0060 0.0160  188  LEU B C   
5220 O  O   . LEU B 189 ? 0.4087 0.2357 0.3023 -0.0384 0.0079  0.0112  188  LEU B O   
5221 C  CB  . LEU B 189 ? 0.3682 0.2471 0.2719 -0.0309 -0.0781 -0.0204 188  LEU B CB  
5222 C  CG  . LEU B 189 ? 0.3893 0.2208 0.2625 0.0351  -0.0985 -0.0029 188  LEU B CG  
5223 C  CD1 . LEU B 189 ? 0.4405 0.1915 0.2660 0.0396  -0.0850 0.0005  188  LEU B CD1 
5224 C  CD2 . LEU B 189 ? 0.4459 0.2637 0.2651 0.0031  -0.1191 0.0131  188  LEU B CD2 
5225 N  N   . GLN B 190 ? 0.2427 0.3033 0.2904 -0.0221 0.0267  -0.0148 189  GLN B N   
5226 C  CA  . GLN B 190 ? 0.2473 0.3562 0.3073 -0.0199 0.0656  -0.0137 189  GLN B CA  
5227 C  C   . GLN B 190 ? 0.2443 0.3307 0.3288 0.0552  0.0895  0.0266  189  GLN B C   
5228 O  O   . GLN B 190 ? 0.3526 0.3179 0.3578 0.0667  0.1093  0.0327  189  GLN B O   
5229 C  CB  . GLN B 190 ? 0.3165 0.4195 0.3288 -0.0203 0.0914  -0.0215 189  GLN B CB  
5230 C  CG  . GLN B 190 ? 0.3806 0.4586 0.3588 -0.0018 0.0577  -0.0426 189  GLN B CG  
5231 C  CD  . GLN B 190 ? 0.4008 0.4977 0.3977 -0.0389 0.1079  -0.0412 189  GLN B CD  
5232 O  OE1 . GLN B 190 ? 0.5279 0.5103 0.4211 -0.0254 0.0966  -0.0400 189  GLN B OE1 
5233 N  NE2 . GLN B 190 ? 0.2883 0.4986 0.4204 -0.0252 0.1334  -0.0544 189  GLN B NE2 
5234 N  N   . ARG B 191 ? 0.2506 0.3211 0.2986 0.0571  0.1043  0.0539  190  ARG B N   
5235 C  CA  . ARG B 191 ? 0.3355 0.2967 0.3092 0.0592  0.0797  0.0745  190  ARG B CA  
5236 C  C   . ARG B 191 ? 0.3879 0.3031 0.3614 0.0970  0.0833  0.0745  190  ARG B C   
5237 O  O   . ARG B 191 ? 0.3573 0.3024 0.3988 0.1117  0.0769  0.0828  190  ARG B O   
5238 C  CB  . ARG B 191 ? 0.3723 0.2505 0.2767 0.0279  0.0678  0.0918  190  ARG B CB  
5239 C  CG  . ARG B 191 ? 0.3806 0.2035 0.2711 0.0422  0.0577  0.0705  190  ARG B CG  
5240 C  CD  . ARG B 191 ? 0.3684 0.1561 0.2734 0.0639  0.0085  0.0499  190  ARG B CD  
5241 N  NE  . ARG B 191 ? 0.4139 0.1699 0.2466 0.0153  -0.0138 0.0003  190  ARG B NE  
5242 C  CZ  . ARG B 191 ? 0.3799 0.1776 0.2865 -0.0001 -0.0140 0.0129  190  ARG B CZ  
5243 N  NH1 . ARG B 191 ? 0.4074 0.2049 0.3068 0.0251  0.0276  0.0117  190  ARG B NH1 
5244 N  NH2 . ARG B 191 ? 0.4005 0.1830 0.2984 0.0114  -0.0349 0.0077  190  ARG B NH2 
5245 N  N   . ALA B 192 ? 0.4576 0.3298 0.3488 0.1115  0.1505  0.0818  191  ALA B N   
5246 C  CA  . ALA B 192 ? 0.5152 0.3726 0.3471 0.1142  0.1565  0.0675  191  ALA B CA  
5247 C  C   . ALA B 192 ? 0.5580 0.4006 0.3419 0.1435  0.0952  0.0416  191  ALA B C   
5248 O  O   . ALA B 192 ? 0.5350 0.4133 0.3290 0.1731  0.1052  0.0375  191  ALA B O   
5249 C  CB  . ALA B 192 ? 0.5837 0.3804 0.3485 0.0536  0.1635  0.1083  191  ALA B CB  
5250 N  N   A ASN B 193 ? 0.5426 0.3923 0.3409 0.1516  0.0710  0.0282  192  ASN B N   
5251 N  N   B ASN B 193 ? 0.5432 0.3897 0.3298 0.1477  0.0864  0.0344  192  ASN B N   
5252 C  CA  A ASN B 193 ? 0.5203 0.3799 0.3513 0.1618  0.0479  0.0191  192  ASN B CA  
5253 C  CA  B ASN B 193 ? 0.5199 0.3773 0.3360 0.1492  0.0809  0.0285  192  ASN B CA  
5254 C  C   A ASN B 193 ? 0.4873 0.3814 0.3510 0.1265  0.0325  0.0248  192  ASN B C   
5255 C  C   B ASN B 193 ? 0.4930 0.3776 0.3464 0.1221  0.0415  0.0322  192  ASN B C   
5256 O  O   A ASN B 193 ? 0.4878 0.3826 0.3707 0.0878  0.0232  0.0374  192  ASN B O   
5257 O  O   B ASN B 193 ? 0.4981 0.3790 0.3765 0.0772  0.0232  0.0454  192  ASN B O   
5258 C  CB  A ASN B 193 ? 0.5521 0.3720 0.3668 0.1801  0.0218  0.0202  192  ASN B CB  
5259 C  CB  B ASN B 193 ? 0.5329 0.3757 0.3375 0.1386  0.0895  0.0393  192  ASN B CB  
5260 C  CG  A ASN B 193 ? 0.5785 0.3615 0.3771 0.2123  -0.0104 0.0078  192  ASN B CG  
5261 C  CG  B ASN B 193 ? 0.5363 0.3755 0.3329 0.1458  0.1034  0.0265  192  ASN B CG  
5262 O  OD1 A ASN B 193 ? 0.5247 0.3418 0.3612 0.2389  -0.0369 0.0109  192  ASN B OD1 
5263 O  OD1 B ASN B 193 ? 0.5593 0.3736 0.3397 0.1967  0.1330  0.0254  192  ASN B OD1 
5264 N  ND2 A ASN B 193 ? 0.6439 0.3953 0.4007 0.1758  -0.0105 0.0095  192  ASN B ND2 
5265 N  ND2 B ASN B 193 ? 0.5551 0.3795 0.3311 0.0938  0.0866  0.0284  192  ASN B ND2 
5266 N  N   . PRO B 194 ? 0.4562 0.3916 0.3420 0.1059  0.0348  0.0139  193  PRO B N   
5267 C  CA  . PRO B 194 ? 0.4483 0.3944 0.3385 0.0791  0.0395  0.0179  193  PRO B CA  
5268 C  C   . PRO B 194 ? 0.4364 0.3998 0.3496 0.1175  0.0301  -0.0018 193  PRO B C   
5269 O  O   . PRO B 194 ? 0.3996 0.4006 0.3204 0.0689  0.0090  -0.0103 193  PRO B O   
5270 C  CB  . PRO B 194 ? 0.4547 0.4078 0.3289 0.0937  0.0110  0.0394  193  PRO B CB  
5271 C  CG  . PRO B 194 ? 0.4340 0.4123 0.3392 0.0989  0.0080  0.0534  193  PRO B CG  
5272 C  CD  . PRO B 194 ? 0.4629 0.4165 0.3440 0.1183  0.0093  0.0351  193  PRO B CD  
5273 N  N   . ASP B 195 ? 0.4477 0.4203 0.3727 0.1612  0.0282  0.0003  194  ASP B N   
5274 C  CA  . ASP B 195 ? 0.4484 0.4430 0.3983 0.1817  0.0043  0.0133  194  ASP B CA  
5275 C  C   . ASP B 195 ? 0.5086 0.3877 0.3856 0.1751  0.0403  0.0182  194  ASP B C   
5276 O  O   . ASP B 195 ? 0.5322 0.3800 0.3951 0.1960  0.0594  0.0465  194  ASP B O   
5277 C  CB  . ASP B 195 ? 0.5371 0.5216 0.4321 0.1852  -0.0553 0.0215  194  ASP B CB  
5278 C  CG  . ASP B 195 ? 0.6435 0.5913 0.4723 0.1943  -0.0837 0.0167  194  ASP B CG  
5279 O  OD1 . ASP B 195 ? 0.6018 0.6092 0.4727 0.1727  -0.0500 -0.0073 194  ASP B OD1 
5280 O  OD2 . ASP B 195 ? 0.7661 0.6366 0.5008 0.1868  -0.1228 0.0281  194  ASP B OD2 
5281 N  N   . ASP B 196 ? 0.5113 0.3508 0.3699 0.1262  0.0316  0.0008  195  ASP B N   
5282 C  CA  . ASP B 196 ? 0.5661 0.3027 0.3888 0.0793  0.0611  0.0114  195  ASP B CA  
5283 C  C   . ASP B 196 ? 0.5710 0.2322 0.3793 0.1034  0.0508  -0.0041 195  ASP B C   
5284 O  O   . ASP B 196 ? 0.5032 0.2234 0.3603 0.0871  0.0387  0.0156  195  ASP B O   
5285 C  CB  . ASP B 196 ? 0.6088 0.3244 0.4075 0.0026  0.0872  0.0080  195  ASP B CB  
5286 C  CG  . ASP B 196 ? 0.6751 0.3529 0.4329 -0.0835 0.0980  0.0320  195  ASP B CG  
5287 O  OD1 . ASP B 196 ? 0.6895 0.3234 0.4289 -0.1172 0.1316  0.0254  195  ASP B OD1 
5288 O  OD2 . ASP B 196 ? 0.7104 0.4011 0.4539 -0.1286 0.0583  0.0404  195  ASP B OD2 
5289 N  N   . PRO B 197 ? 0.5709 0.2106 0.4021 0.1383  0.0650  -0.0167 196  PRO B N   
5290 C  CA  . PRO B 197 ? 0.5813 0.1986 0.4334 0.1283  0.0246  -0.0283 196  PRO B CA  
5291 C  C   . PRO B 197 ? 0.5423 0.1744 0.4480 0.0429  0.0308  -0.0565 196  PRO B C   
5292 O  O   . PRO B 197 ? 0.5598 0.1629 0.4455 0.0024  -0.0075 -0.0621 196  PRO B O   
5293 C  CB  . PRO B 197 ? 0.5949 0.2251 0.4343 0.1544  0.0322  -0.0312 196  PRO B CB  
5294 C  CG  . PRO B 197 ? 0.6295 0.2236 0.4208 0.1382  0.0839  -0.0192 196  PRO B CG  
5295 C  CD  . PRO B 197 ? 0.6239 0.2104 0.4168 0.1218  0.0892  -0.0161 196  PRO B CD  
5296 N  N   . ALA B 198 ? 0.4669 0.1804 0.4673 0.0247  0.0367  -0.0535 197  ALA B N   
5297 C  CA  . ALA B 198 ? 0.4252 0.2059 0.4622 0.0088  0.0421  -0.0275 197  ALA B CA  
5298 C  C   . ALA B 198 ? 0.4325 0.2075 0.4286 -0.0060 0.0262  -0.0186 197  ALA B C   
5299 O  O   . ALA B 198 ? 0.4323 0.2484 0.4573 -0.0165 -0.0072 -0.0207 197  ALA B O   
5300 C  CB  . ALA B 198 ? 0.3989 0.2199 0.4768 0.0025  0.0768  -0.0113 197  ALA B CB  
5301 N  N   . TYR B 199 ? 0.3512 0.1913 0.3786 -0.0503 0.0432  -0.0378 198  TYR B N   
5302 C  CA  . TYR B 199 ? 0.3614 0.1738 0.3521 -0.0085 0.0584  -0.0718 198  TYR B CA  
5303 C  C   . TYR B 199 ? 0.3340 0.1757 0.3424 0.0275  0.0563  -0.0737 198  TYR B C   
5304 O  O   . TYR B 199 ? 0.3820 0.1719 0.3389 0.0573  -0.0113 -0.0582 198  TYR B O   
5305 C  CB  . TYR B 199 ? 0.2557 0.1687 0.3243 -0.0005 0.0843  -0.0842 198  TYR B CB  
5306 C  CG  . TYR B 199 ? 0.2943 0.1855 0.3689 -0.0029 0.0771  -0.0722 198  TYR B CG  
5307 C  CD1 . TYR B 199 ? 0.3219 0.1968 0.3890 -0.0181 0.1149  -0.0661 198  TYR B CD1 
5308 C  CD2 . TYR B 199 ? 0.3340 0.2230 0.3850 -0.0420 0.1284  -0.0537 198  TYR B CD2 
5309 C  CE1 . TYR B 199 ? 0.4539 0.2178 0.4133 0.0110  0.1062  -0.0433 198  TYR B CE1 
5310 C  CE2 . TYR B 199 ? 0.4298 0.2408 0.4040 -0.0142 0.1445  -0.0348 198  TYR B CE2 
5311 C  CZ  . TYR B 199 ? 0.4279 0.2440 0.4253 -0.0339 0.1420  -0.0268 198  TYR B CZ  
5312 O  OH  . TYR B 199 ? 0.4416 0.2632 0.4716 -0.0732 0.1247  -0.0148 198  TYR B OH  
5313 N  N   . ASP B 200 ? 0.4063 0.1862 0.3379 0.0678  0.0541  -0.0674 199  ASP B N   
5314 C  CA  . ASP B 200 ? 0.4540 0.2362 0.3497 0.1171  0.0578  -0.0327 199  ASP B CA  
5315 C  C   . ASP B 200 ? 0.4760 0.2692 0.3640 0.0739  -0.0087 -0.0233 199  ASP B C   
5316 O  O   . ASP B 200 ? 0.4364 0.2772 0.3525 0.0594  -0.0276 -0.0365 199  ASP B O   
5317 C  CB  . ASP B 200 ? 0.4688 0.2528 0.3301 0.1427  0.1024  -0.0437 199  ASP B CB  
5318 C  CG  . ASP B 200 ? 0.5719 0.2721 0.3336 0.1355  0.1024  -0.0335 199  ASP B CG  
5319 O  OD1 . ASP B 200 ? 0.5127 0.2876 0.3458 0.1041  0.1240  0.0061  199  ASP B OD1 
5320 O  OD2 . ASP B 200 ? 0.6784 0.2975 0.3428 0.1505  0.0570  -0.0135 199  ASP B OD2 
5321 N  N   . GLU B 201 ? 0.5394 0.2599 0.3760 0.0484  -0.0255 -0.0308 200  GLU B N   
5322 C  CA  . GLU B 201 ? 0.5504 0.2633 0.3968 -0.0209 -0.0914 -0.0392 200  GLU B CA  
5323 C  C   . GLU B 201 ? 0.5135 0.2101 0.3798 -0.0392 -0.0533 -0.0506 200  GLU B C   
5324 O  O   . GLU B 201 ? 0.4979 0.2168 0.3880 -0.0612 -0.0254 -0.0416 200  GLU B O   
5325 C  CB  . GLU B 201 ? 0.6462 0.3060 0.4282 -0.0665 -0.1099 -0.0304 200  GLU B CB  
5326 C  CG  . GLU B 201 ? 0.7292 0.3615 0.4765 -0.0644 -0.1062 -0.0208 200  GLU B CG  
5327 C  CD  . GLU B 201 ? 0.8575 0.4115 0.5243 -0.0800 -0.1001 -0.0077 200  GLU B CD  
5328 O  OE1 . GLU B 201 ? 0.9327 0.4204 0.5456 -0.1051 -0.0821 -0.0263 200  GLU B OE1 
5329 O  OE2 . GLU B 201 ? 0.9090 0.4545 0.5444 -0.0997 -0.1040 0.0065  200  GLU B OE2 
5330 N  N   . ASN B 202 ? 0.4429 0.1729 0.3600 -0.0172 -0.0268 -0.0574 201  ASN B N   
5331 C  CA  . ASN B 202 ? 0.3961 0.1548 0.3500 0.0111  -0.0148 -0.0574 201  ASN B CA  
5332 C  C   . ASN B 202 ? 0.4365 0.1806 0.3188 -0.0002 -0.0020 -0.0304 201  ASN B C   
5333 O  O   . ASN B 202 ? 0.4335 0.2078 0.3217 -0.0037 0.0032  -0.0580 201  ASN B O   
5334 C  CB  . ASN B 202 ? 0.4054 0.1702 0.4006 0.0410  -0.0174 -0.0590 201  ASN B CB  
5335 C  CG  . ASN B 202 ? 0.4177 0.2219 0.4462 0.0473  -0.0234 -0.0309 201  ASN B CG  
5336 O  OD1 . ASN B 202 ? 0.4283 0.2944 0.4835 0.0289  -0.0200 0.0002  201  ASN B OD1 
5337 N  ND2 . ASN B 202 ? 0.4914 0.2263 0.4551 0.0677  -0.0069 -0.0214 201  ASN B ND2 
5338 N  N   . LYS B 203 ? 0.3772 0.1982 0.2839 0.0300  -0.0056 -0.0009 202  LYS B N   
5339 C  CA  . LYS B 203 ? 0.4455 0.2326 0.2806 0.0297  -0.0024 0.0257  202  LYS B CA  
5340 C  C   . LYS B 203 ? 0.4860 0.2542 0.2656 0.0104  -0.0023 0.0140  202  LYS B C   
5341 O  O   . LYS B 203 ? 0.4754 0.2450 0.2665 0.0417  -0.0164 0.0158  202  LYS B O   
5342 C  CB  . LYS B 203 ? 0.3944 0.2312 0.2719 0.0741  -0.0166 0.0420  202  LYS B CB  
5343 C  CG  . LYS B 203 ? 0.4209 0.2459 0.2808 0.0651  -0.0553 0.0287  202  LYS B CG  
5344 C  CD  . LYS B 203 ? 0.4386 0.2872 0.2642 0.0280  -0.0676 0.0375  202  LYS B CD  
5345 C  CE  . LYS B 203 ? 0.4096 0.3111 0.2806 0.0447  -0.0796 0.0514  202  LYS B CE  
5346 N  NZ  . LYS B 203 ? 0.3968 0.3458 0.2969 0.0511  -0.1338 0.0323  202  LYS B NZ  
5347 N  N   . ARG B 204 ? 0.4902 0.2731 0.2619 0.0074  0.0065  0.0084  203  ARG B N   
5348 C  CA  . ARG B 204 ? 0.4873 0.2863 0.2503 -0.0269 0.0325  -0.0190 203  ARG B CA  
5349 C  C   . ARG B 204 ? 0.4234 0.2552 0.2597 -0.0268 0.0485  -0.0392 203  ARG B C   
5350 O  O   . ARG B 204 ? 0.4172 0.2496 0.2695 -0.1055 0.0647  -0.0377 203  ARG B O   
5351 C  CB  . ARG B 204 ? 0.6190 0.3252 0.2703 -0.0311 0.0005  -0.0316 203  ARG B CB  
5352 C  CG  . ARG B 204 ? 0.7206 0.4196 0.3332 0.0340  -0.0479 -0.0140 203  ARG B CG  
5353 C  CD  . ARG B 204 ? 0.7595 0.5140 0.3859 0.0827  -0.0832 0.0066  203  ARG B CD  
5354 N  NE  . ARG B 204 ? 0.7801 0.5949 0.4314 0.0927  -0.1117 0.0282  203  ARG B NE  
5355 C  CZ  . ARG B 204 ? 0.7895 0.6482 0.4728 0.1142  -0.1265 0.0323  203  ARG B CZ  
5356 N  NH1 . ARG B 204 ? 0.7753 0.6612 0.4874 0.1159  -0.0989 0.0395  203  ARG B NH1 
5357 N  NH2 . ARG B 204 ? 0.7638 0.6651 0.4885 0.1143  -0.1451 0.0264  203  ARG B NH2 
5358 N  N   . GLN B 205 ? 0.4222 0.2246 0.2550 0.0108  0.0093  -0.0507 204  GLN B N   
5359 C  CA  . GLN B 205 ? 0.3699 0.2099 0.2579 0.0055  -0.0430 -0.0524 204  GLN B CA  
5360 C  C   . GLN B 205 ? 0.3725 0.2219 0.2242 0.0168  -0.0332 -0.0459 204  GLN B C   
5361 O  O   . GLN B 205 ? 0.4185 0.2551 0.2093 0.0322  -0.0022 -0.0368 204  GLN B O   
5362 C  CB  . GLN B 205 ? 0.3081 0.2264 0.2908 -0.0158 -0.0305 -0.0470 204  GLN B CB  
5363 C  CG  . GLN B 205 ? 0.3503 0.2826 0.3147 -0.0381 -0.0331 -0.0269 204  GLN B CG  
5364 C  CD  . GLN B 205 ? 0.4218 0.2977 0.3094 -0.0361 -0.0428 -0.0532 204  GLN B CD  
5365 O  OE1 . GLN B 205 ? 0.4109 0.3035 0.3183 0.0296  -0.0157 -0.0407 204  GLN B OE1 
5366 N  NE2 . GLN B 205 ? 0.5234 0.2898 0.3123 -0.0828 -0.0847 -0.0618 204  GLN B NE2 
5367 N  N   . PHE B 206 ? 0.3634 0.2327 0.2055 0.0064  -0.0474 -0.0477 205  PHE B N   
5368 C  CA  . PHE B 206 ? 0.3589 0.2419 0.2329 -0.0416 -0.0356 -0.0480 205  PHE B CA  
5369 C  C   . PHE B 206 ? 0.3072 0.2402 0.2657 -0.0069 -0.0053 -0.0202 205  PHE B C   
5370 O  O   . PHE B 206 ? 0.3144 0.2049 0.2577 -0.0243 -0.0061 -0.0050 205  PHE B O   
5371 C  CB  . PHE B 206 ? 0.3799 0.2440 0.2145 -0.0627 -0.0420 -0.0539 205  PHE B CB  
5372 C  CG  . PHE B 206 ? 0.3459 0.2498 0.2255 -0.0167 -0.0570 -0.0523 205  PHE B CG  
5373 C  CD1 . PHE B 206 ? 0.3413 0.2567 0.2294 -0.0153 -0.0997 -0.0586 205  PHE B CD1 
5374 C  CD2 . PHE B 206 ? 0.3250 0.2411 0.2313 -0.0261 -0.0855 -0.0306 205  PHE B CD2 
5375 C  CE1 . PHE B 206 ? 0.3166 0.2578 0.2398 -0.0435 -0.0577 -0.0603 205  PHE B CE1 
5376 C  CE2 . PHE B 206 ? 0.2892 0.2321 0.2397 -0.0391 -0.0608 -0.0498 205  PHE B CE2 
5377 C  CZ  . PHE B 206 ? 0.3500 0.2550 0.2424 -0.0923 0.0041  -0.0493 205  PHE B CZ  
5378 N  N   . GLN B 207 ? 0.2278 0.2650 0.2897 0.0247  0.0077  0.0035  206  GLN B N   
5379 C  CA  . GLN B 207 ? 0.2618 0.3059 0.2734 0.0392  0.0606  0.0276  206  GLN B CA  
5380 C  C   . GLN B 207 ? 0.3381 0.2958 0.2866 0.0264  0.0516  -0.0134 206  GLN B C   
5381 O  O   . GLN B 207 ? 0.3804 0.2733 0.2981 -0.0103 0.0803  -0.0440 206  GLN B O   
5382 C  CB  . GLN B 207 ? 0.2840 0.3373 0.2863 0.1130  0.0424  0.0377  206  GLN B CB  
5383 C  CG  . GLN B 207 ? 0.4026 0.3995 0.3238 0.0653  0.0577  0.0195  206  GLN B CG  
5384 C  CD  . GLN B 207 ? 0.4883 0.4351 0.3444 0.0261  0.0890  0.0115  206  GLN B CD  
5385 O  OE1 . GLN B 207 ? 0.5487 0.4839 0.3665 -0.0104 0.0861  0.0173  206  GLN B OE1 
5386 N  NE2 . GLN B 207 ? 0.4584 0.4101 0.3427 0.0466  0.1174  -0.0139 206  GLN B NE2 
5387 N  N   . GLU B 208 ? 0.2526 0.2922 0.2754 0.0443  0.0129  -0.0422 207  GLU B N   
5388 C  CA  . GLU B 208 ? 0.3472 0.2893 0.3146 0.0256  -0.0054 -0.0289 207  GLU B CA  
5389 C  C   . GLU B 208 ? 0.3458 0.2570 0.3031 0.0605  0.0220  -0.0251 207  GLU B C   
5390 O  O   . GLU B 208 ? 0.3297 0.2315 0.2892 0.0925  0.0198  -0.0355 207  GLU B O   
5391 C  CB  . GLU B 208 ? 0.4715 0.3685 0.3707 -0.0786 -0.0830 -0.0310 207  GLU B CB  
5392 C  CG  . GLU B 208 ? 0.6446 0.4309 0.4802 -0.1299 -0.0903 -0.0452 207  GLU B CG  
5393 C  CD  . GLU B 208 ? 0.8333 0.4962 0.5906 -0.1405 -0.0712 -0.0437 207  GLU B CD  
5394 O  OE1 . GLU B 208 ? 0.9186 0.5418 0.6298 -0.1259 -0.0713 -0.0652 207  GLU B OE1 
5395 O  OE2 . GLU B 208 ? 0.8478 0.5234 0.6332 -0.1502 -0.0503 -0.0271 207  GLU B OE2 
5396 N  N   . ASP B 209 ? 0.3154 0.2219 0.2834 0.0548  0.0351  -0.0479 208  ASP B N   
5397 C  CA  . ASP B 209 ? 0.2504 0.2358 0.2629 0.0428  0.0311  -0.0076 208  ASP B CA  
5398 C  C   . ASP B 209 ? 0.2961 0.2641 0.2567 0.0418  0.0158  -0.0070 208  ASP B C   
5399 O  O   . ASP B 209 ? 0.2896 0.2405 0.2330 0.0459  0.0008  0.0016  208  ASP B O   
5400 C  CB  . ASP B 209 ? 0.2723 0.2400 0.2650 -0.0469 0.0111  0.0271  208  ASP B CB  
5401 C  CG  . ASP B 209 ? 0.4125 0.2724 0.2646 -0.0236 0.0011  0.0146  208  ASP B CG  
5402 O  OD1 . ASP B 209 ? 0.4129 0.2778 0.2724 0.0555  0.0431  0.0041  208  ASP B OD1 
5403 O  OD2 . ASP B 209 ? 0.4049 0.2188 0.2500 -0.0211 -0.0070 0.0050  208  ASP B OD2 
5404 N  N   . ILE B 210 ? 0.2821 0.2903 0.2609 0.0381  -0.0038 -0.0011 209  ILE B N   
5405 C  CA  . ILE B 210 ? 0.2679 0.3068 0.2422 -0.0206 0.0084  0.0221  209  ILE B CA  
5406 C  C   . ILE B 210 ? 0.3444 0.2906 0.2256 0.0104  0.0199  0.0111  209  ILE B C   
5407 O  O   . ILE B 210 ? 0.3882 0.2812 0.2249 0.0339  0.0103  0.0447  209  ILE B O   
5408 C  CB  . ILE B 210 ? 0.3017 0.3258 0.2628 -0.0478 0.0194  0.0408  209  ILE B CB  
5409 C  CG1 . ILE B 210 ? 0.3223 0.3254 0.2354 -0.0284 0.0023  0.0408  209  ILE B CG1 
5410 C  CG2 . ILE B 210 ? 0.2795 0.3316 0.2820 -0.0689 0.0179  0.0302  209  ILE B CG2 
5411 C  CD1 . ILE B 210 ? 0.3961 0.3088 0.2349 0.0180  -0.0408 0.0180  209  ILE B CD1 
5412 N  N   . LYS B 211 ? 0.3871 0.2700 0.2046 0.0490  0.0131  -0.0365 210  LYS B N   
5413 C  CA  . LYS B 211 ? 0.4229 0.2684 0.1915 0.0840  0.0383  -0.0649 210  LYS B CA  
5414 C  C   . LYS B 211 ? 0.4090 0.2972 0.1844 0.0526  0.0105  -0.0401 210  LYS B C   
5415 O  O   . LYS B 211 ? 0.4225 0.3439 0.2101 0.0220  0.0693  -0.0065 210  LYS B O   
5416 C  CB  . LYS B 211 ? 0.4448 0.3015 0.2228 0.0931  0.0691  -0.0933 210  LYS B CB  
5417 C  CG  . LYS B 211 ? 0.6317 0.3904 0.2575 0.1236  0.0713  -0.0989 210  LYS B CG  
5418 C  CD  . LYS B 211 ? 0.7933 0.4677 0.2853 0.1544  0.0943  -0.0824 210  LYS B CD  
5419 C  CE  . LYS B 211 ? 0.8693 0.5059 0.3229 0.1881  0.0841  -0.0306 210  LYS B CE  
5420 N  NZ  . LYS B 211 ? 0.9539 0.5354 0.3656 0.1971  0.0678  0.0175  210  LYS B NZ  
5421 N  N   . VAL B 212 ? 0.3403 0.2844 0.1825 0.0456  -0.0074 -0.0600 211  VAL B N   
5422 C  CA  . VAL B 212 ? 0.3115 0.2741 0.2270 0.0055  -0.0333 -0.0518 211  VAL B CA  
5423 C  C   . VAL B 212 ? 0.3715 0.2972 0.2082 0.0069  0.0142  -0.0389 211  VAL B C   
5424 O  O   . VAL B 212 ? 0.3653 0.3053 0.2014 -0.0296 0.0157  -0.0439 211  VAL B O   
5425 C  CB  . VAL B 212 ? 0.2857 0.2428 0.2555 0.0099  -0.0017 -0.0451 211  VAL B CB  
5426 C  CG1 . VAL B 212 ? 0.3182 0.2357 0.2530 0.0070  -0.0336 -0.0436 211  VAL B CG1 
5427 C  CG2 . VAL B 212 ? 0.3316 0.2202 0.2837 -0.0099 0.0296  -0.0196 211  VAL B CG2 
5428 N  N   . MET B 213 ? 0.3539 0.3044 0.2115 -0.0237 -0.0017 -0.0209 212  MET B N   
5429 C  CA  . MET B 213 ? 0.3519 0.2814 0.1941 -0.0581 0.0469  -0.0303 212  MET B CA  
5430 C  C   . MET B 213 ? 0.3303 0.3061 0.2118 -0.0273 0.0295  -0.0361 212  MET B C   
5431 O  O   . MET B 213 ? 0.4295 0.3107 0.2037 -0.0592 0.0253  0.0004  212  MET B O   
5432 C  CB  . MET B 213 ? 0.4244 0.2831 0.2065 -0.0305 0.0285  0.0031  212  MET B CB  
5433 C  CG  . MET B 213 ? 0.4991 0.2957 0.1928 0.0247  0.0603  0.0027  212  MET B CG  
5434 S  SD  . MET B 213 ? 0.5638 0.3115 0.2395 0.0507  0.0358  -0.0128 212  MET B SD  
5435 C  CE  . MET B 213 ? 0.5119 0.3139 0.2278 0.1802  -0.1172 -0.0208 212  MET B CE  
5436 N  N   . ASN B 214 ? 0.2918 0.3236 0.2249 0.0062  0.0288  -0.0341 213  ASN B N   
5437 C  CA  . ASN B 214 ? 0.3667 0.3374 0.2198 -0.0109 0.0255  -0.0280 213  ASN B CA  
5438 C  C   . ASN B 214 ? 0.4080 0.3230 0.2504 -0.0002 0.0316  0.0102  213  ASN B C   
5439 O  O   . ASN B 214 ? 0.3278 0.3566 0.2910 0.0085  0.0350  0.0461  213  ASN B O   
5440 C  CB  . ASN B 214 ? 0.2848 0.3897 0.2263 -0.0249 -0.0405 -0.0301 213  ASN B CB  
5441 C  CG  . ASN B 214 ? 0.4367 0.4327 0.2756 -0.0891 -0.0385 -0.0301 213  ASN B CG  
5442 O  OD1 . ASN B 214 ? 0.5880 0.4531 0.3173 -0.0651 -0.0441 -0.0500 213  ASN B OD1 
5443 N  ND2 . ASN B 214 ? 0.3692 0.4424 0.2567 -0.2007 0.0165  0.0044  213  ASN B ND2 
5444 N  N   . ASP B 215 ? 0.4517 0.2852 0.2167 -0.0031 0.0439  -0.0226 214  ASP B N   
5445 C  CA  . ASP B 215 ? 0.5189 0.3077 0.2267 0.0228  0.0660  -0.0171 214  ASP B CA  
5446 C  C   . ASP B 215 ? 0.4469 0.3060 0.2373 0.0490  0.0687  -0.0043 214  ASP B C   
5447 O  O   . ASP B 215 ? 0.4311 0.2995 0.2698 0.0566  0.0760  0.0266  214  ASP B O   
5448 C  CB  . ASP B 215 ? 0.5931 0.3308 0.2139 0.0221  0.1026  -0.0703 214  ASP B CB  
5449 C  CG  . ASP B 215 ? 0.7490 0.3926 0.2507 -0.0348 0.0454  -0.0481 214  ASP B CG  
5450 O  OD1 . ASP B 215 ? 0.7487 0.4191 0.2747 -0.0204 0.0531  -0.0343 214  ASP B OD1 
5451 O  OD2 . ASP B 215 ? 0.8570 0.4082 0.2641 -0.0779 0.0128  -0.0899 214  ASP B OD2 
5452 N  N   . LEU B 216 ? 0.4173 0.3139 0.2262 0.0004  0.0347  -0.0027 215  LEU B N   
5453 C  CA  . LEU B 216 ? 0.3577 0.3051 0.2380 -0.0346 -0.0230 0.0035  215  LEU B CA  
5454 C  C   . LEU B 216 ? 0.3304 0.3087 0.2488 -0.0332 -0.0141 0.0099  215  LEU B C   
5455 O  O   . LEU B 216 ? 0.3484 0.3118 0.2518 -0.0303 0.0091  -0.0007 215  LEU B O   
5456 C  CB  . LEU B 216 ? 0.3843 0.3168 0.2578 -0.0398 -0.0259 0.0181  215  LEU B CB  
5457 C  CG  . LEU B 216 ? 0.4447 0.3346 0.2871 0.0088  0.0210  0.0333  215  LEU B CG  
5458 C  CD1 . LEU B 216 ? 0.5067 0.3485 0.3130 -0.0116 0.0095  0.0327  215  LEU B CD1 
5459 C  CD2 . LEU B 216 ? 0.5472 0.3496 0.3270 0.0196  0.0493  0.0085  215  LEU B CD2 
5460 N  N   . VAL B 217 ? 0.2689 0.2808 0.2038 -0.0223 0.0078  0.0175  216  VAL B N   
5461 C  CA  . VAL B 217 ? 0.3111 0.2850 0.2522 -0.0234 -0.0292 0.0268  216  VAL B CA  
5462 C  C   . VAL B 217 ? 0.2697 0.2867 0.3250 -0.0360 0.0145  0.0298  216  VAL B C   
5463 O  O   . VAL B 217 ? 0.3291 0.2785 0.3353 -0.0092 -0.0050 0.0278  216  VAL B O   
5464 C  CB  . VAL B 217 ? 0.3377 0.2943 0.2418 -0.0313 -0.0490 0.0407  216  VAL B CB  
5465 C  CG1 . VAL B 217 ? 0.2882 0.3006 0.2347 -0.0234 -0.0463 0.0884  216  VAL B CG1 
5466 C  CG2 . VAL B 217 ? 0.3727 0.2956 0.2658 -0.0266 -0.0138 0.0193  216  VAL B CG2 
5467 N  N   . ASP B 218 ? 0.3796 0.3057 0.3922 0.0148  0.0696  0.0374  217  ASP B N   
5468 C  CA  . ASP B 218 ? 0.4011 0.3406 0.4402 0.0498  0.0986  0.0241  217  ASP B CA  
5469 C  C   . ASP B 218 ? 0.4196 0.3647 0.4332 0.0226  0.0846  0.0211  217  ASP B C   
5470 O  O   . ASP B 218 ? 0.4363 0.3786 0.4330 -0.0197 0.1118  0.0456  217  ASP B O   
5471 C  CB  . ASP B 218 ? 0.4944 0.3787 0.5092 0.0675  0.0570  0.0212  217  ASP B CB  
5472 C  CG  . ASP B 218 ? 0.4654 0.4216 0.5764 0.0705  0.0491  0.0041  217  ASP B CG  
5473 O  OD1 . ASP B 218 ? 0.3825 0.4357 0.5892 0.0542  0.0128  -0.0053 217  ASP B OD1 
5474 O  OD2 . ASP B 218 ? 0.4554 0.4418 0.6168 0.1337  0.0517  0.0213  217  ASP B OD2 
5475 N  N   . LYS B 219 ? 0.4046 0.3613 0.4116 0.0280  0.0824  -0.0108 218  LYS B N   
5476 C  CA  . LYS B 219 ? 0.4259 0.3484 0.3803 -0.0086 0.0836  -0.0332 218  LYS B CA  
5477 C  C   . LYS B 219 ? 0.3980 0.3328 0.3116 -0.0536 0.0881  -0.0369 218  LYS B C   
5478 O  O   . LYS B 219 ? 0.3817 0.2883 0.3105 -0.0677 0.1087  -0.0322 218  LYS B O   
5479 C  CB  . LYS B 219 ? 0.4065 0.3630 0.4300 -0.0637 0.0642  -0.0465 218  LYS B CB  
5480 C  CG  . LYS B 219 ? 0.5289 0.4050 0.4772 -0.1073 0.0318  -0.0442 218  LYS B CG  
5481 C  CD  . LYS B 219 ? 0.6143 0.4423 0.5160 -0.1342 0.0122  -0.0463 218  LYS B CD  
5482 C  CE  . LYS B 219 ? 0.7044 0.4868 0.5626 -0.1379 0.0155  -0.0232 218  LYS B CE  
5483 N  NZ  . LYS B 219 ? 0.7322 0.5164 0.6132 -0.1580 0.0229  -0.0138 218  LYS B NZ  
5484 N  N   . ILE B 220 ? 0.2631 0.3444 0.2328 -0.0347 0.0886  -0.0416 219  ILE B N   
5485 C  CA  . ILE B 220 ? 0.2534 0.3393 0.2316 -0.0011 0.0705  -0.0114 219  ILE B CA  
5486 C  C   . ILE B 220 ? 0.3112 0.3736 0.2533 0.0334  0.0439  0.0302  219  ILE B C   
5487 O  O   . ILE B 220 ? 0.3153 0.3699 0.2411 -0.0121 0.0315  0.0354  219  ILE B O   
5488 C  CB  . ILE B 220 ? 0.2410 0.3418 0.2353 0.0076  0.0519  -0.0090 219  ILE B CB  
5489 C  CG1 . ILE B 220 ? 0.1973 0.3644 0.2278 0.0069  0.0112  0.0433  219  ILE B CG1 
5490 C  CG2 . ILE B 220 ? 0.2508 0.3044 0.2739 0.0755  0.0588  -0.0320 219  ILE B CG2 
5491 C  CD1 . ILE B 220 ? 0.1219 0.3938 0.2291 0.0178  0.0187  0.0645  219  ILE B CD1 
5492 N  N   . ILE B 221 ? 0.2245 0.4033 0.2717 0.0722  0.0261  0.0747  220  ILE B N   
5493 C  CA  . ILE B 221 ? 0.2250 0.4471 0.3082 0.0479  0.0442  0.0747  220  ILE B CA  
5494 C  C   . ILE B 221 ? 0.3223 0.4794 0.3055 0.0182  0.0818  0.0620  220  ILE B C   
5495 O  O   . ILE B 221 ? 0.3217 0.4771 0.3148 0.0131  0.0375  0.0518  220  ILE B O   
5496 C  CB  . ILE B 221 ? 0.2400 0.4771 0.3502 0.0600  0.0432  0.0970  220  ILE B CB  
5497 C  CG1 . ILE B 221 ? 0.2811 0.4941 0.3730 0.1135  0.0230  0.1427  220  ILE B CG1 
5498 C  CG2 . ILE B 221 ? 0.2888 0.4849 0.3724 0.0280  0.0346  0.0871  220  ILE B CG2 
5499 C  CD1 . ILE B 221 ? 0.2907 0.5212 0.4057 0.0872  0.0000  0.1393  220  ILE B CD1 
5500 N  N   . ALA B 222 ? 0.4780 0.4871 0.2916 0.0015  0.1541  0.0362  221  ALA B N   
5501 C  CA  . ALA B 222 ? 0.5795 0.5019 0.3014 0.0177  0.1769  0.0419  221  ALA B CA  
5502 C  C   . ALA B 222 ? 0.5971 0.5147 0.3033 0.0173  0.1633  0.0768  221  ALA B C   
5503 O  O   . ALA B 222 ? 0.5598 0.5316 0.3049 0.0260  0.1726  0.0896  221  ALA B O   
5504 C  CB  . ALA B 222 ? 0.5662 0.4914 0.3077 -0.0022 0.1414  0.0105  221  ALA B CB  
5505 N  N   . ASP B 223 ? 0.5994 0.5148 0.2988 0.0202  0.1498  0.0675  222  ASP B N   
5506 C  CA  . ASP B 223 ? 0.5753 0.5274 0.3277 0.0093  0.1181  0.0301  222  ASP B CA  
5507 C  C   . ASP B 223 ? 0.5596 0.5215 0.3097 0.0216  0.1189  0.0386  222  ASP B C   
5508 O  O   . ASP B 223 ? 0.6255 0.5153 0.3111 0.0239  0.1078  0.0461  222  ASP B O   
5509 C  CB  . ASP B 223 ? 0.5714 0.5507 0.3836 0.0180  0.1031  -0.0001 222  ASP B CB  
5510 C  CG  . ASP B 223 ? 0.5555 0.5898 0.4206 0.0081  0.0887  -0.0309 222  ASP B CG  
5511 O  OD1 . ASP B 223 ? 0.5132 0.6056 0.4381 0.0677  0.1266  -0.0366 222  ASP B OD1 
5512 O  OD2 . ASP B 223 ? 0.5132 0.5947 0.4117 -0.0298 0.0449  -0.0652 222  ASP B OD2 
5513 N  N   . ARG B 224 ? 0.4233 0.5089 0.2611 0.0320  0.1046  0.0400  223  ARG B N   
5514 C  CA  . ARG B 224 ? 0.4143 0.4969 0.3081 -0.0356 0.1763  0.0524  223  ARG B CA  
5515 C  C   . ARG B 224 ? 0.4350 0.5382 0.3944 -0.0902 0.2194  0.0700  223  ARG B C   
5516 O  O   . ARG B 224 ? 0.5006 0.5272 0.3980 -0.0870 0.2324  0.0806  223  ARG B O   
5517 C  CB  . ARG B 224 ? 0.4173 0.4640 0.2755 -0.0257 0.1255  0.0538  223  ARG B CB  
5518 C  CG  . ARG B 224 ? 0.2961 0.4263 0.2685 -0.0443 0.1016  0.0700  223  ARG B CG  
5519 C  CD  . ARG B 224 ? 0.3030 0.4131 0.2557 -0.0270 0.0520  0.0744  223  ARG B CD  
5520 N  NE  . ARG B 224 ? 0.2077 0.4076 0.2327 -0.0489 0.0515  0.0833  223  ARG B NE  
5521 C  CZ  . ARG B 224 ? 0.1622 0.4040 0.2311 -0.0280 -0.0085 0.0737  223  ARG B CZ  
5522 N  NH1 . ARG B 224 ? 0.1882 0.3948 0.2484 -0.0541 -0.0321 0.0843  223  ARG B NH1 
5523 N  NH2 . ARG B 224 ? 0.1583 0.4163 0.2345 -0.0035 -0.0644 0.0441  223  ARG B NH2 
5524 N  N   . LYS B 225 ? 0.4493 0.6010 0.4712 -0.0675 0.2573  0.0724  224  LYS B N   
5525 C  CA  . LYS B 225 ? 0.6191 0.6644 0.5466 -0.0309 0.2612  0.0649  224  LYS B CA  
5526 C  C   . LYS B 225 ? 0.7310 0.7057 0.5770 -0.0199 0.2717  0.0447  224  LYS B C   
5527 O  O   . LYS B 225 ? 0.8152 0.7182 0.5854 -0.0206 0.2565  0.0304  224  LYS B O   
5528 C  CB  . LYS B 225 ? 0.7251 0.6938 0.5913 0.0080  0.2413  0.0632  224  LYS B CB  
5529 C  CG  . LYS B 225 ? 0.9152 0.7299 0.6334 0.0561  0.2116  0.0516  224  LYS B CG  
5530 C  CD  . LYS B 225 ? 1.0400 0.7709 0.6642 0.0635  0.2031  0.0409  224  LYS B CD  
5531 C  CE  . LYS B 225 ? 1.1144 0.8022 0.6760 0.0560  0.1967  0.0296  224  LYS B CE  
5532 N  NZ  . LYS B 225 ? 1.1794 0.8213 0.6845 0.0245  0.1780  0.0324  224  LYS B NZ  
5533 N  N   . ALA B 226 ? 0.7664 0.7223 0.5996 -0.0221 0.2933  0.0562  225  ALA B N   
5534 C  CA  . ALA B 226 ? 0.8148 0.7332 0.6103 -0.0329 0.3208  0.0831  225  ALA B CA  
5535 C  C   . ALA B 226 ? 0.9115 0.7488 0.6716 -0.0277 0.2825  0.0770  225  ALA B C   
5536 O  O   . ALA B 226 ? 0.9296 0.7432 0.6723 -0.0337 0.2771  0.0594  225  ALA B O   
5537 C  CB  . ALA B 226 ? 0.8049 0.7290 0.5747 -0.0472 0.3703  0.0956  225  ALA B CB  
5538 N  N   . SER B 227 ? 0.9843 0.7733 0.7300 -0.0290 0.2555  0.0793  226  SER B N   
5539 C  CA  . SER B 227 ? 1.0084 0.8121 0.8000 -0.0398 0.2200  0.0718  226  SER B CA  
5540 C  C   . SER B 227 ? 1.0912 0.8416 0.8454 -0.0327 0.1887  0.0717  226  SER B C   
5541 O  O   . SER B 227 ? 1.0748 0.8417 0.8517 -0.0449 0.2005  0.0784  226  SER B O   
5542 C  CB  . SER B 227 ? 0.9708 0.8179 0.8241 -0.0398 0.2166  0.0628  226  SER B CB  
5543 O  OG  . SER B 227 ? 1.0003 0.8310 0.8409 -0.0548 0.2067  0.0579  226  SER B OG  
5544 N  N   . GLY B 228 ? 1.1526 0.8694 0.8822 -0.0145 0.1497  0.0628  227  GLY B N   
5545 C  CA  . GLY B 228 ? 1.1838 0.8962 0.9126 0.0121  0.1257  0.0591  227  GLY B CA  
5546 C  C   . GLY B 228 ? 1.1959 0.9141 0.9400 0.0399  0.1050  0.0594  227  GLY B C   
5547 O  O   . GLY B 228 ? 1.2035 0.9055 0.9528 0.0280  0.0936  0.0565  227  GLY B O   
5548 N  N   . GLU B 229 ? 1.1798 0.9379 0.9463 0.0679  0.0939  0.0659  228  GLU B N   
5549 C  CA  . GLU B 229 ? 1.1968 0.9577 0.9492 0.0670  0.0726  0.0753  228  GLU B CA  
5550 C  C   . GLU B 229 ? 1.2128 0.9562 0.9457 0.0432  0.0626  0.0591  228  GLU B C   
5551 O  O   . GLU B 229 ? 1.2519 0.9625 0.9509 0.0428  0.0662  0.0525  228  GLU B O   
5552 C  CB  . GLU B 229 ? 1.1931 0.9749 0.9558 0.0769  0.0590  0.0898  228  GLU B CB  
5553 C  CG  . GLU B 229 ? 1.2071 0.9836 0.9614 0.0950  0.0496  0.0972  228  GLU B CG  
5554 C  CD  . GLU B 229 ? 1.2468 0.9836 0.9616 0.1179  0.0436  0.1071  228  GLU B CD  
5555 O  OE1 . GLU B 229 ? 1.2623 0.9817 0.9567 0.1092  0.0267  0.1045  228  GLU B OE1 
5556 O  OE2 . GLU B 229 ? 1.2485 0.9810 0.9661 0.1503  0.0538  0.1168  228  GLU B OE2 
5557 N  N   . GLN B 230 ? 1.1542 0.9391 0.9300 0.0230  0.0501  0.0567  229  GLN B N   
5558 C  CA  . GLN B 230 ? 1.0838 0.9199 0.9125 -0.0039 0.0487  0.0606  229  GLN B CA  
5559 C  C   . GLN B 230 ? 1.0153 0.8735 0.8700 0.0076  0.0597  0.0831  229  GLN B C   
5560 O  O   . GLN B 230 ? 1.0247 0.8758 0.8743 0.0201  0.0627  0.0812  229  GLN B O   
5561 C  CB  . GLN B 230 ? 1.0547 0.9405 0.9337 -0.0403 0.0430  0.0511  229  GLN B CB  
5562 C  CG  . GLN B 230 ? 1.0425 0.9583 0.9509 -0.0627 0.0388  0.0465  229  GLN B CG  
5563 C  CD  . GLN B 230 ? 1.0348 0.9774 0.9629 -0.0696 0.0490  0.0414  229  GLN B CD  
5564 O  OE1 . GLN B 230 ? 1.0331 0.9863 0.9669 -0.0710 0.0576  0.0421  229  GLN B OE1 
5565 N  NE2 . GLN B 230 ? 1.0264 0.9812 0.9629 -0.0663 0.0525  0.0337  229  GLN B NE2 
5566 N  N   . SER B 231 ? 0.9205 0.8167 0.8179 0.0116  0.0657  0.1120  230  SER B N   
5567 C  CA  . SER B 231 ? 0.8048 0.7541 0.7754 0.0471  0.0422  0.1261  230  SER B CA  
5568 C  C   . SER B 231 ? 0.7734 0.6984 0.7330 0.0906  0.0466  0.1252  230  SER B C   
5569 O  O   . SER B 231 ? 0.7033 0.7010 0.7138 0.1189  0.0048  0.1412  230  SER B O   
5570 C  CB  . SER B 231 ? 0.6962 0.7400 0.7695 0.0389  0.0318  0.1394  230  SER B CB  
5571 O  OG  . SER B 231 ? 0.5381 0.7284 0.7617 0.0481  0.0114  0.1493  230  SER B OG  
5572 N  N   . ASP B 232 ? 0.6702 0.6331 0.7058 0.1203  0.0973  0.1055  231  ASP B N   
5573 C  CA  . ASP B 232 ? 0.6205 0.5883 0.6943 0.1130  0.0962  0.0786  231  ASP B CA  
5574 C  C   . ASP B 232 ? 0.4661 0.5341 0.6481 0.0748  0.0969  0.0618  231  ASP B C   
5575 O  O   . ASP B 232 ? 0.5647 0.5603 0.6855 0.0894  0.1336  0.0263  231  ASP B O   
5576 C  CB  . ASP B 232 ? 0.7683 0.6050 0.7205 0.1181  0.0524  0.0673  231  ASP B CB  
5577 C  CG  . ASP B 232 ? 0.9074 0.6259 0.7456 0.1207  0.0115  0.0669  231  ASP B CG  
5578 O  OD1 . ASP B 232 ? 0.9547 0.6212 0.7477 0.1184  0.0133  0.0743  231  ASP B OD1 
5579 O  OD2 . ASP B 232 ? 0.9596 0.6407 0.7535 0.1088  -0.0219 0.0618  231  ASP B OD2 
5580 N  N   . ASP B 233 ? 0.2148 0.4389 0.5494 -0.0020 0.0377  0.0996  232  ASP B N   
5581 C  CA  . ASP B 233 ? 0.1517 0.3744 0.4342 -0.0297 -0.0231 0.0871  232  ASP B CA  
5582 C  C   . ASP B 233 ? 0.1701 0.3243 0.3771 -0.0626 -0.0185 0.0747  232  ASP B C   
5583 O  O   . ASP B 233 ? 0.1880 0.3204 0.3899 -0.0803 -0.0402 0.0521  232  ASP B O   
5584 C  CB  . ASP B 233 ? 0.1540 0.3731 0.3778 -0.0569 -0.0843 0.0842  232  ASP B CB  
5585 C  CG  . ASP B 233 ? 0.2058 0.3776 0.3602 -0.0657 -0.0826 0.0925  232  ASP B CG  
5586 O  OD1 . ASP B 233 ? 0.2697 0.4195 0.3572 -0.0467 -0.0859 0.0885  232  ASP B OD1 
5587 O  OD2 . ASP B 233 ? 0.2522 0.3470 0.3509 -0.0393 -0.0747 0.0831  232  ASP B OD2 
5588 N  N   . LEU B 234 ? 0.2267 0.2918 0.3320 -0.0632 -0.0413 0.0549  233  LEU B N   
5589 C  CA  . LEU B 234 ? 0.1815 0.2913 0.2490 -0.0952 -0.0601 0.0400  233  LEU B CA  
5590 C  C   . LEU B 234 ? 0.2207 0.2881 0.2139 -0.0404 -0.0610 0.0217  233  LEU B C   
5591 O  O   . LEU B 234 ? 0.2245 0.2995 0.2265 -0.0651 -0.0665 0.0354  233  LEU B O   
5592 C  CB  . LEU B 234 ? 0.2547 0.2638 0.2562 -0.1404 -0.0768 0.0569  233  LEU B CB  
5593 C  CG  . LEU B 234 ? 0.3365 0.3106 0.2650 -0.1209 -0.0886 0.0057  233  LEU B CG  
5594 C  CD1 . LEU B 234 ? 0.3645 0.3431 0.2604 -0.0873 -0.1074 -0.0034 233  LEU B CD1 
5595 C  CD2 . LEU B 234 ? 0.3139 0.3272 0.2853 -0.1358 -0.0715 0.0137  233  LEU B CD2 
5596 N  N   . LEU B 235 ? 0.2476 0.2742 0.1845 -0.1117 -0.0057 0.0071  234  LEU B N   
5597 C  CA  . LEU B 235 ? 0.1948 0.2661 0.1790 -0.0616 -0.0249 -0.0144 234  LEU B CA  
5598 C  C   . LEU B 235 ? 0.1801 0.2776 0.1982 -0.0035 -0.0463 0.0124  234  LEU B C   
5599 O  O   . LEU B 235 ? 0.1876 0.3069 0.2168 -0.0061 -0.0554 0.0315  234  LEU B O   
5600 C  CB  . LEU B 235 ? 0.2604 0.2434 0.1888 -0.0342 -0.0488 -0.0305 234  LEU B CB  
5601 C  CG  . LEU B 235 ? 0.2472 0.2299 0.1841 -0.0564 -0.0512 -0.0287 234  LEU B CG  
5602 C  CD1 . LEU B 235 ? 0.3712 0.2739 0.1982 -0.0117 -0.0138 -0.0296 234  LEU B CD1 
5603 C  CD2 . LEU B 235 ? 0.2819 0.2005 0.2144 -0.0665 -0.0990 0.0032  234  LEU B CD2 
5604 N  N   . THR B 236 ? 0.2017 0.2635 0.2147 -0.0679 -0.0909 0.0141  235  THR B N   
5605 C  CA  . THR B 236 ? 0.2037 0.2728 0.2551 -0.0439 -0.0588 0.0229  235  THR B CA  
5606 C  C   . THR B 236 ? 0.1777 0.2975 0.2668 -0.0244 -0.0329 0.0246  235  THR B C   
5607 O  O   . THR B 236 ? 0.2313 0.3438 0.2845 -0.0572 -0.0840 0.0318  235  THR B O   
5608 C  CB  . THR B 236 ? 0.1588 0.2784 0.2893 -0.0690 -0.0721 -0.0190 235  THR B CB  
5609 O  OG1 . THR B 236 ? 0.2116 0.3021 0.2842 -0.0116 -0.0681 -0.0081 235  THR B OG1 
5610 C  CG2 . THR B 236 ? 0.1886 0.2991 0.2930 -0.0068 -0.0509 -0.0420 235  THR B CG2 
5611 N  N   . HIS B 237 ? 0.1973 0.3219 0.2614 -0.0396 0.0008  0.0532  236  HIS B N   
5612 C  CA  . HIS B 237 ? 0.1997 0.3379 0.2716 -0.0032 -0.0457 0.0219  236  HIS B CA  
5613 C  C   . HIS B 237 ? 0.2457 0.3741 0.2597 -0.0084 -0.0186 0.0081  236  HIS B C   
5614 O  O   . HIS B 237 ? 0.1966 0.3901 0.2769 -0.0281 0.0047  0.0129  236  HIS B O   
5615 C  CB  . HIS B 237 ? 0.2817 0.3163 0.3255 -0.0423 -0.0753 -0.0063 236  HIS B CB  
5616 C  CG  . HIS B 237 ? 0.4437 0.3078 0.3726 -0.0592 -0.1118 -0.0217 236  HIS B CG  
5617 N  ND1 . HIS B 237 ? 0.4942 0.3047 0.4097 -0.0668 -0.0875 -0.0415 236  HIS B ND1 
5618 C  CD2 . HIS B 237 ? 0.6171 0.3302 0.4157 -0.0296 -0.1287 -0.0105 236  HIS B CD2 
5619 C  CE1 . HIS B 237 ? 0.5223 0.3193 0.4340 -0.0615 -0.1201 -0.0390 236  HIS B CE1 
5620 N  NE2 . HIS B 237 ? 0.6665 0.3187 0.4454 -0.0618 -0.1197 -0.0233 236  HIS B NE2 
5621 N  N   . MET B 238 ? 0.2222 0.3898 0.2250 -0.0188 -0.0537 0.0068  237  MET B N   
5622 C  CA  . MET B 238 ? 0.2079 0.3937 0.2259 -0.0254 -0.0446 0.0312  237  MET B CA  
5623 C  C   . MET B 238 ? 0.2600 0.4415 0.2475 0.0463  -0.0973 0.0348  237  MET B C   
5624 O  O   . MET B 238 ? 0.2758 0.4647 0.2719 0.0388  -0.1035 0.0104  237  MET B O   
5625 C  CB  . MET B 238 ? 0.1537 0.3839 0.2228 -0.0488 -0.0270 0.0598  237  MET B CB  
5626 C  CG  . MET B 238 ? 0.1639 0.3805 0.2377 -0.0865 -0.0515 0.0326  237  MET B CG  
5627 S  SD  . MET B 238 ? 0.2528 0.3714 0.2129 -0.0364 -0.0274 0.0548  237  MET B SD  
5628 C  CE  . MET B 238 ? 0.1754 0.3665 0.2171 -0.0863 0.0228  0.0799  237  MET B CE  
5629 N  N   . LEU B 239 ? 0.2610 0.4584 0.2424 0.0487  -0.0421 0.0151  238  LEU B N   
5630 C  CA  . LEU B 239 ? 0.2642 0.4762 0.2655 0.0839  -0.0388 0.0336  238  LEU B CA  
5631 C  C   . LEU B 239 ? 0.2293 0.4807 0.3229 0.0403  0.0288  0.0358  238  LEU B C   
5632 O  O   . LEU B 239 ? 0.2558 0.4891 0.3808 0.0612  0.0801  0.0226  238  LEU B O   
5633 C  CB  . LEU B 239 ? 0.3103 0.4772 0.2306 0.1092  -0.0991 0.0354  238  LEU B CB  
5634 C  CG  . LEU B 239 ? 0.4222 0.4699 0.2460 0.1613  -0.1085 0.0381  238  LEU B CG  
5635 C  CD1 . LEU B 239 ? 0.4229 0.4610 0.2127 0.1622  -0.0818 0.0233  238  LEU B CD1 
5636 C  CD2 . LEU B 239 ? 0.5034 0.4727 0.2686 0.1673  -0.1217 0.0542  238  LEU B CD2 
5637 N  N   . ASN B 240 ? 0.3257 0.4710 0.3136 -0.0127 0.0334  0.0573  239  ASN B N   
5638 C  CA  . ASN B 240 ? 0.2956 0.4933 0.3058 -0.0376 -0.0083 0.0817  239  ASN B CA  
5639 C  C   . ASN B 240 ? 0.2372 0.4660 0.2843 -0.0456 -0.0685 0.0981  239  ASN B C   
5640 O  O   . ASN B 240 ? 0.2149 0.4983 0.3126 -0.0762 -0.0687 0.1095  239  ASN B O   
5641 C  CB  . ASN B 240 ? 0.3429 0.5254 0.3200 -0.0073 -0.0200 0.0760  239  ASN B CB  
5642 C  CG  . ASN B 240 ? 0.4315 0.5766 0.3523 0.0053  -0.0184 0.0583  239  ASN B CG  
5643 O  OD1 . ASN B 240 ? 0.4323 0.6039 0.3628 0.0142  -0.0211 0.0341  239  ASN B OD1 
5644 N  ND2 . ASN B 240 ? 0.4429 0.5818 0.3649 0.0143  -0.0426 0.0444  239  ASN B ND2 
5645 N  N   . GLY B 241 ? 0.2610 0.4031 0.2595 0.0168  -0.0548 0.1082  240  GLY B N   
5646 C  CA  . GLY B 241 ? 0.2164 0.3468 0.2450 -0.0368 -0.0693 0.0915  240  GLY B CA  
5647 C  C   . GLY B 241 ? 0.2049 0.3118 0.2763 -0.0488 -0.0585 0.0785  240  GLY B C   
5648 O  O   . GLY B 241 ? 0.2263 0.3007 0.2916 -0.0208 -0.0952 0.0626  240  GLY B O   
5649 N  N   . LYS B 242 ? 0.1570 0.2875 0.2760 -0.0550 -0.0875 0.0942  241  LYS B N   
5650 C  CA  . LYS B 242 ? 0.1777 0.2765 0.2859 -0.0596 -0.0294 0.0928  241  LYS B CA  
5651 C  C   . LYS B 242 ? 0.1346 0.2617 0.2805 -0.0172 -0.0424 0.0866  241  LYS B C   
5652 O  O   . LYS B 242 ? 0.1692 0.3314 0.3216 0.0136  -0.0616 0.1019  241  LYS B O   
5653 C  CB  . LYS B 242 ? 0.2936 0.2961 0.3010 -0.0340 -0.0643 0.0924  241  LYS B CB  
5654 C  CG  . LYS B 242 ? 0.4890 0.3429 0.3257 0.0325  -0.0172 0.0909  241  LYS B CG  
5655 C  CD  . LYS B 242 ? 0.5675 0.3673 0.3495 0.0643  0.0087  0.0965  241  LYS B CD  
5656 C  CE  . LYS B 242 ? 0.5787 0.3907 0.3781 0.0464  -0.0074 0.0803  241  LYS B CE  
5657 N  NZ  . LYS B 242 ? 0.6434 0.4035 0.4002 0.0498  -0.0476 0.0550  241  LYS B NZ  
5658 N  N   . ASP B 243 ? 0.1269 0.2213 0.2488 -0.0444 -0.0792 0.0786  242  ASP B N   
5659 C  CA  . ASP B 243 ? 0.1801 0.1955 0.2529 -0.0283 -0.0233 0.0644  242  ASP B CA  
5660 C  C   . ASP B 243 ? 0.1682 0.2132 0.2865 0.0015  -0.0136 0.0225  242  ASP B C   
5661 O  O   . ASP B 243 ? 0.1434 0.2096 0.2789 -0.0447 -0.0141 0.0285  242  ASP B O   
5662 C  CB  . ASP B 243 ? 0.1471 0.1925 0.1979 -0.0438 -0.0293 0.0887  242  ASP B CB  
5663 C  CG  . ASP B 243 ? 0.1524 0.2082 0.2171 -0.0536 -0.0021 0.0307  242  ASP B CG  
5664 O  OD1 . ASP B 243 ? 0.1409 0.2186 0.2156 -0.0523 -0.0239 -0.0080 242  ASP B OD1 
5665 O  OD2 . ASP B 243 ? 0.1550 0.1892 0.2209 0.0222  -0.0134 -0.0006 242  ASP B OD2 
5666 N  N   . PRO B 244 ? 0.1029 0.2172 0.3243 0.0082  0.0048  0.0072  243  PRO B N   
5667 C  CA  . PRO B 244 ? 0.0891 0.2263 0.3324 0.0192  -0.0191 -0.0294 243  PRO B CA  
5668 C  C   . PRO B 244 ? 0.0819 0.2033 0.3148 -0.0165 0.0124  -0.0105 243  PRO B C   
5669 O  O   . PRO B 244 ? 0.1459 0.2142 0.3336 0.0062  0.0463  0.0125  243  PRO B O   
5670 C  CB  . PRO B 244 ? 0.1164 0.2539 0.3349 0.0681  -0.0173 -0.0322 243  PRO B CB  
5671 C  CG  . PRO B 244 ? 0.1688 0.2701 0.3790 0.0748  -0.0053 -0.0417 243  PRO B CG  
5672 C  CD  . PRO B 244 ? 0.1590 0.2062 0.3637 0.0557  0.0050  -0.0040 243  PRO B CD  
5673 N  N   . GLU B 245 ? 0.1338 0.2094 0.2988 -0.0088 0.0372  -0.0016 244  GLU B N   
5674 C  CA  . GLU B 245 ? 0.1006 0.2317 0.2734 -0.0224 0.0354  0.0043  244  GLU B CA  
5675 C  C   . GLU B 245 ? 0.1629 0.2331 0.2493 0.0361  0.0065  0.0093  244  GLU B C   
5676 O  O   . GLU B 245 ? 0.2063 0.2431 0.2568 0.0669  -0.0255 -0.0206 244  GLU B O   
5677 C  CB  . GLU B 245 ? 0.1276 0.2828 0.2704 -0.0453 0.0575  0.0184  244  GLU B CB  
5678 C  CG  . GLU B 245 ? 0.3021 0.3376 0.2923 -0.0379 0.0112  0.0037  244  GLU B CG  
5679 C  CD  . GLU B 245 ? 0.3600 0.4194 0.3116 -0.0454 -0.0394 0.0067  244  GLU B CD  
5680 O  OE1 . GLU B 245 ? 0.2477 0.4226 0.2975 -0.1085 -0.0229 -0.0077 244  GLU B OE1 
5681 O  OE2 . GLU B 245 ? 0.5228 0.4631 0.3612 -0.0694 -0.0449 0.0044  244  GLU B OE2 
5682 N  N   . THR B 246 ? 0.1821 0.2228 0.1981 0.0677  0.0134  -0.0088 245  THR B N   
5683 C  CA  . THR B 246 ? 0.1904 0.2306 0.2258 0.0288  0.0175  0.0221  245  THR B CA  
5684 C  C   . THR B 246 ? 0.1340 0.2635 0.2314 0.0096  0.0126  0.0140  245  THR B C   
5685 O  O   . THR B 246 ? 0.1394 0.2805 0.2508 0.0270  -0.0001 0.0113  245  THR B O   
5686 C  CB  . THR B 246 ? 0.2231 0.2022 0.2235 0.0612  0.0080  0.0409  245  THR B CB  
5687 O  OG1 . THR B 246 ? 0.2131 0.2154 0.2389 0.0645  0.0032  0.0361  245  THR B OG1 
5688 C  CG2 . THR B 246 ? 0.2445 0.1766 0.2260 0.0232  0.0497  0.0704  245  THR B CG2 
5689 N  N   . GLY B 247 ? 0.1583 0.2405 0.2146 0.0085  0.0115  -0.0038 246  GLY B N   
5690 C  CA  . GLY B 247 ? 0.1730 0.2395 0.2192 -0.0258 0.0225  0.0020  246  GLY B CA  
5691 C  C   . GLY B 247 ? 0.1788 0.2204 0.2340 -0.0088 -0.0285 0.0463  246  GLY B C   
5692 O  O   . GLY B 247 ? 0.1741 0.1964 0.2672 0.0116  -0.0020 0.0512  246  GLY B O   
5693 N  N   . GLU B 248 ? 0.1597 0.2318 0.2423 -0.0111 -0.0552 0.0652  247  GLU B N   
5694 C  CA  . GLU B 248 ? 0.1688 0.2164 0.1948 -0.0014 -0.0540 0.0402  247  GLU B CA  
5695 C  C   . GLU B 248 ? 0.1610 0.2617 0.2012 0.0138  -0.0175 0.0565  247  GLU B C   
5696 O  O   . GLU B 248 ? 0.1421 0.2707 0.1999 -0.0489 -0.0189 0.0614  247  GLU B O   
5697 C  CB  . GLU B 248 ? 0.2051 0.2092 0.1701 -0.0043 -0.0264 0.0631  247  GLU B CB  
5698 C  CG  . GLU B 248 ? 0.1677 0.2648 0.1894 -0.0031 -0.0126 0.0538  247  GLU B CG  
5699 C  CD  . GLU B 248 ? 0.1596 0.2693 0.2230 0.0223  -0.0474 0.0451  247  GLU B CD  
5700 O  OE1 . GLU B 248 ? 0.2592 0.2573 0.2330 -0.0068 -0.0005 0.0227  247  GLU B OE1 
5701 O  OE2 . GLU B 248 ? 0.1555 0.3227 0.2244 0.0086  -0.0345 0.0365  247  GLU B OE2 
5702 N  N   . PRO B 249 ? 0.1488 0.3060 0.2031 0.0155  -0.0107 0.0476  248  PRO B N   
5703 C  CA  . PRO B 249 ? 0.1536 0.3225 0.2008 -0.0474 0.0056  0.0689  248  PRO B CA  
5704 C  C   . PRO B 249 ? 0.1022 0.2970 0.2263 -0.0402 -0.0323 0.0477  248  PRO B C   
5705 O  O   . PRO B 249 ? 0.1383 0.3468 0.2384 -0.0106 -0.0293 0.0464  248  PRO B O   
5706 C  CB  . PRO B 249 ? 0.1267 0.3514 0.2271 0.0178  0.0308  0.0437  248  PRO B CB  
5707 C  CG  . PRO B 249 ? 0.1985 0.3654 0.2128 0.0143  0.0339  0.0184  248  PRO B CG  
5708 C  CD  . PRO B 249 ? 0.2421 0.3545 0.1925 -0.0234 -0.0334 0.0425  248  PRO B CD  
5709 N  N   . LEU B 250 ? 0.1338 0.2660 0.2220 -0.0940 -0.0142 0.0489  249  LEU B N   
5710 C  CA  . LEU B 250 ? 0.1167 0.2838 0.2280 -0.0608 -0.0049 0.0308  249  LEU B CA  
5711 C  C   . LEU B 250 ? 0.1416 0.2887 0.1979 -0.0467 0.0151  0.0050  249  LEU B C   
5712 O  O   . LEU B 250 ? 0.2178 0.2899 0.1905 -0.0495 0.0225  0.0029  249  LEU B O   
5713 C  CB  . LEU B 250 ? 0.1318 0.2910 0.2765 0.0004  0.0200  0.0292  249  LEU B CB  
5714 C  CG  . LEU B 250 ? 0.0866 0.2990 0.2934 0.0372  0.0060  0.0201  249  LEU B CG  
5715 C  CD1 . LEU B 250 ? 0.0934 0.3030 0.3264 0.0472  -0.0101 0.0102  249  LEU B CD1 
5716 C  CD2 . LEU B 250 ? 0.1672 0.3000 0.2674 -0.0756 0.0102  0.0038  249  LEU B CD2 
5717 N  N   . ASP B 251 ? 0.1943 0.3244 0.1965 -0.0512 0.0196  0.0289  250  ASP B N   
5718 C  CA  . ASP B 251 ? 0.2482 0.3651 0.2136 -0.0578 -0.0227 0.0143  250  ASP B CA  
5719 C  C   . ASP B 251 ? 0.2628 0.3691 0.2188 -0.0346 0.0162  -0.0054 250  ASP B C   
5720 O  O   . ASP B 251 ? 0.1835 0.3340 0.2191 0.0241  0.0053  -0.0202 250  ASP B O   
5721 C  CB  . ASP B 251 ? 0.2666 0.4069 0.2468 -0.0462 -0.0342 0.0204  250  ASP B CB  
5722 C  CG  . ASP B 251 ? 0.4260 0.4586 0.2719 -0.0360 -0.0616 0.0276  250  ASP B CG  
5723 O  OD1 . ASP B 251 ? 0.3622 0.4405 0.2471 0.0065  -0.0798 0.0047  250  ASP B OD1 
5724 O  OD2 . ASP B 251 ? 0.6049 0.5046 0.3455 -0.0618 -0.0365 0.0519  250  ASP B OD2 
5725 N  N   . ASP B 252 ? 0.2585 0.3838 0.2202 -0.0377 0.0542  -0.0129 251  ASP B N   
5726 C  CA  . ASP B 252 ? 0.2645 0.4012 0.2388 -0.1073 0.0715  -0.0057 251  ASP B CA  
5727 C  C   . ASP B 252 ? 0.1967 0.3704 0.2201 -0.0659 0.0625  -0.0062 251  ASP B C   
5728 O  O   . ASP B 252 ? 0.2255 0.3726 0.2094 -0.0485 0.0175  -0.0423 251  ASP B O   
5729 C  CB  . ASP B 252 ? 0.2916 0.4750 0.2836 -0.1132 0.0579  0.0028  251  ASP B CB  
5730 C  CG  . ASP B 252 ? 0.4438 0.5531 0.3216 -0.0556 0.1102  -0.0110 251  ASP B CG  
5731 O  OD1 . ASP B 252 ? 0.5258 0.5651 0.3272 -0.0634 0.1066  -0.0228 251  ASP B OD1 
5732 O  OD2 . ASP B 252 ? 0.4813 0.5983 0.3547 -0.0449 0.1234  -0.0077 251  ASP B OD2 
5733 N  N   . GLU B 253 ? 0.2975 0.3598 0.2322 0.0262  0.1130  0.0078  252  GLU B N   
5734 C  CA  . GLU B 253 ? 0.2804 0.3692 0.2419 0.0691  0.0828  0.0383  252  GLU B CA  
5735 C  C   . GLU B 253 ? 0.2377 0.3155 0.2250 0.0384  0.0074  0.0190  252  GLU B C   
5736 O  O   . GLU B 253 ? 0.2182 0.2926 0.2065 0.0186  0.0338  0.0226  252  GLU B O   
5737 C  CB  . GLU B 253 ? 0.3331 0.4418 0.3191 0.1359  0.1170  0.0541  252  GLU B CB  
5738 C  CG  . GLU B 253 ? 0.3975 0.4976 0.3818 0.2114  0.1138  0.0678  252  GLU B CG  
5739 C  CD  . GLU B 253 ? 0.5200 0.5563 0.4448 0.2251  0.1504  0.0626  252  GLU B CD  
5740 O  OE1 . GLU B 253 ? 0.6274 0.5830 0.4809 0.2378  0.1739  0.0707  252  GLU B OE1 
5741 O  OE2 . GLU B 253 ? 0.4875 0.5990 0.4694 0.2246  0.1345  0.0411  252  GLU B OE2 
5742 N  N   . ASN B 254 ? 0.1593 0.2891 0.1904 0.0324  -0.0188 -0.0138 253  ASN B N   
5743 C  CA  . ASN B 254 ? 0.1665 0.2386 0.1720 0.0510  0.0179  -0.0265 253  ASN B CA  
5744 C  C   . ASN B 254 ? 0.1794 0.2244 0.1466 0.0227  0.0271  -0.0010 253  ASN B C   
5745 O  O   . ASN B 254 ? 0.1759 0.2342 0.1485 -0.0169 0.0255  -0.0119 253  ASN B O   
5746 C  CB  . ASN B 254 ? 0.1175 0.2288 0.1781 0.0523  0.0189  0.0035  253  ASN B CB  
5747 C  CG  . ASN B 254 ? 0.1895 0.1907 0.1815 0.0117  0.0110  0.0109  253  ASN B CG  
5748 O  OD1 . ASN B 254 ? 0.1643 0.1688 0.2280 -0.0059 0.0083  0.0354  253  ASN B OD1 
5749 N  ND2 . ASN B 254 ? 0.1304 0.1806 0.1751 -0.0347 0.0212  0.0244  253  ASN B ND2 
5750 N  N   . ILE B 255 ? 0.2083 0.2614 0.1424 -0.0609 0.0053  -0.0013 254  ILE B N   
5751 C  CA  . ILE B 255 ? 0.1934 0.2982 0.1617 -0.0775 -0.0313 0.0488  254  ILE B CA  
5752 C  C   . ILE B 255 ? 0.2348 0.3210 0.1575 -0.0561 -0.0109 0.0092  254  ILE B C   
5753 O  O   . ILE B 255 ? 0.2117 0.3285 0.1616 -0.0387 0.0125  0.0105  254  ILE B O   
5754 C  CB  . ILE B 255 ? 0.1788 0.3318 0.1811 -0.0929 -0.0501 0.0842  254  ILE B CB  
5755 C  CG1 . ILE B 255 ? 0.2042 0.3197 0.1985 -0.1145 -0.0035 0.0918  254  ILE B CG1 
5756 C  CG2 . ILE B 255 ? 0.1692 0.3670 0.1986 -0.0693 -0.0073 0.0681  254  ILE B CG2 
5757 C  CD1 . ILE B 255 ? 0.2284 0.3271 0.2250 -0.1183 -0.0052 0.0673  254  ILE B CD1 
5758 N  N   . ARG B 256 ? 0.1485 0.3101 0.1807 -0.0334 0.0358  -0.0144 255  ARG B N   
5759 C  CA  . ARG B 256 ? 0.1331 0.2851 0.1805 0.0336  0.0469  -0.0356 255  ARG B CA  
5760 C  C   . ARG B 256 ? 0.0578 0.2222 0.1624 0.0015  0.0122  -0.0140 255  ARG B C   
5761 O  O   . ARG B 256 ? 0.0997 0.2730 0.1712 0.0097  -0.0023 -0.0143 255  ARG B O   
5762 C  CB  . ARG B 256 ? 0.1746 0.3072 0.2121 0.0326  0.0947  -0.0499 255  ARG B CB  
5763 C  CG  . ARG B 256 ? 0.3275 0.3357 0.2675 -0.0020 0.0533  -0.1068 255  ARG B CG  
5764 C  CD  . ARG B 256 ? 0.4778 0.3756 0.3378 0.0019  0.0423  -0.1520 255  ARG B CD  
5765 N  NE  . ARG B 256 ? 0.5629 0.4287 0.3865 0.0182  0.0279  -0.1286 255  ARG B NE  
5766 C  CZ  . ARG B 256 ? 0.6213 0.4500 0.3957 0.0098  0.0556  -0.1029 255  ARG B CZ  
5767 N  NH1 . ARG B 256 ? 0.6112 0.4527 0.3936 0.0237  0.1230  -0.1119 255  ARG B NH1 
5768 N  NH2 . ARG B 256 ? 0.4938 0.4479 0.4024 -0.0574 0.0569  -0.0575 255  ARG B NH2 
5769 N  N   . TYR B 257 ? 0.1547 0.2264 0.1373 -0.0158 0.0008  -0.0293 256  TYR B N   
5770 C  CA  . TYR B 257 ? 0.1625 0.2203 0.1461 0.0248  0.0442  -0.0032 256  TYR B CA  
5771 C  C   . TYR B 257 ? 0.2007 0.2159 0.1428 0.0268  -0.0115 0.0160  256  TYR B C   
5772 O  O   . TYR B 257 ? 0.1551 0.1972 0.1582 -0.0004 0.0124  0.0162  256  TYR B O   
5773 C  CB  . TYR B 257 ? 0.2055 0.2205 0.1521 0.0151  0.0175  -0.0044 256  TYR B CB  
5774 C  CG  . TYR B 257 ? 0.2027 0.2270 0.1859 0.0047  0.0146  -0.0047 256  TYR B CG  
5775 C  CD1 . TYR B 257 ? 0.2649 0.2370 0.1994 0.0277  0.0153  -0.0296 256  TYR B CD1 
5776 C  CD2 . TYR B 257 ? 0.1932 0.2459 0.2224 0.0623  0.0336  -0.0204 256  TYR B CD2 
5777 C  CE1 . TYR B 257 ? 0.2246 0.2579 0.2403 0.0320  -0.0033 -0.0582 256  TYR B CE1 
5778 C  CE2 . TYR B 257 ? 0.2355 0.2687 0.2520 0.0822  0.0128  -0.0321 256  TYR B CE2 
5779 C  CZ  . TYR B 257 ? 0.2547 0.2514 0.2708 0.1141  -0.0160 -0.0529 256  TYR B CZ  
5780 O  OH  . TYR B 257 ? 0.2973 0.2803 0.3205 0.1288  -0.0165 -0.0657 256  TYR B OH  
5781 N  N   . GLN B 258 ? 0.2590 0.2239 0.1182 -0.0175 0.0067  0.0054  257  GLN B N   
5782 C  CA  . GLN B 258 ? 0.2241 0.2051 0.1465 -0.0246 -0.0345 -0.0046 257  GLN B CA  
5783 C  C   . GLN B 258 ? 0.2031 0.1800 0.1280 0.0095  -0.0191 0.0003  257  GLN B C   
5784 O  O   . GLN B 258 ? 0.1727 0.1636 0.1638 0.0306  -0.0430 0.0030  257  GLN B O   
5785 C  CB  . GLN B 258 ? 0.1782 0.2255 0.1484 -0.0579 -0.0275 0.0131  257  GLN B CB  
5786 C  CG  . GLN B 258 ? 0.1671 0.2119 0.1180 -0.0370 -0.0250 0.0367  257  GLN B CG  
5787 C  CD  . GLN B 258 ? 0.1491 0.2286 0.1496 -0.0110 -0.0200 0.0208  257  GLN B CD  
5788 O  OE1 . GLN B 258 ? 0.1181 0.2244 0.1552 -0.0155 0.0002  0.0126  257  GLN B OE1 
5789 N  NE2 . GLN B 258 ? 0.1679 0.1959 0.1408 -0.0229 -0.0219 0.0099  257  GLN B NE2 
5790 N  N   . ILE B 259 ? 0.1990 0.1866 0.1432 -0.0067 0.0056  0.0287  258  ILE B N   
5791 C  CA  . ILE B 259 ? 0.1670 0.2101 0.1432 -0.0212 -0.0307 0.0573  258  ILE B CA  
5792 C  C   . ILE B 259 ? 0.1299 0.2108 0.1719 -0.0172 -0.0055 0.0368  258  ILE B C   
5793 O  O   . ILE B 259 ? 0.1414 0.2414 0.1682 0.0133  0.0129  0.0321  258  ILE B O   
5794 C  CB  . ILE B 259 ? 0.1269 0.2677 0.1419 -0.0466 -0.0159 0.0593  258  ILE B CB  
5795 C  CG1 . ILE B 259 ? 0.1767 0.2883 0.1628 -0.0795 0.0449  0.0508  258  ILE B CG1 
5796 C  CG2 . ILE B 259 ? 0.1781 0.2750 0.1620 -0.0458 -0.0321 0.0517  258  ILE B CG2 
5797 C  CD1 . ILE B 259 ? 0.2719 0.3127 0.1638 -0.1013 0.0483  0.0603  258  ILE B CD1 
5798 N  N   . ILE B 260 ? 0.1714 0.2053 0.1662 0.0122  -0.0085 0.0098  259  ILE B N   
5799 C  CA  . ILE B 260 ? 0.1566 0.1723 0.1778 -0.0209 0.0305  -0.0197 259  ILE B CA  
5800 C  C   . ILE B 260 ? 0.1619 0.2021 0.1521 0.0220  0.0016  -0.0139 259  ILE B C   
5801 O  O   . ILE B 260 ? 0.1342 0.1786 0.1341 0.0458  -0.0131 0.0017  259  ILE B O   
5802 C  CB  . ILE B 260 ? 0.1907 0.1462 0.2425 -0.0467 0.1070  -0.0329 259  ILE B CB  
5803 C  CG1 . ILE B 260 ? 0.3142 0.1585 0.2762 -0.0274 0.0834  -0.0196 259  ILE B CG1 
5804 C  CG2 . ILE B 260 ? 0.2212 0.1406 0.2845 0.0016  0.1088  -0.0395 259  ILE B CG2 
5805 C  CD1 . ILE B 260 ? 0.4582 0.1877 0.3093 -0.0077 0.0904  -0.0313 259  ILE B CD1 
5806 N  N   . THR B 261 ? 0.1216 0.1838 0.1220 0.0012  -0.0051 -0.0288 260  THR B N   
5807 C  CA  . THR B 261 ? 0.1352 0.1844 0.1467 0.0185  -0.0234 0.0028  260  THR B CA  
5808 C  C   . THR B 261 ? 0.1618 0.1616 0.1393 -0.0104 0.0098  -0.0070 260  THR B C   
5809 O  O   . THR B 261 ? 0.1539 0.1467 0.1524 0.0321  -0.0080 0.0020  260  THR B O   
5810 C  CB  . THR B 261 ? 0.1107 0.1821 0.1590 0.0467  -0.0389 0.0099  260  THR B CB  
5811 O  OG1 . THR B 261 ? 0.1834 0.1444 0.1819 0.0213  -0.0270 -0.0064 260  THR B OG1 
5812 C  CG2 . THR B 261 ? 0.1162 0.2025 0.1766 0.0098  0.0051  0.0395  260  THR B CG2 
5813 N  N   . PHE B 262 ? 0.2178 0.1490 0.1466 0.0038  -0.0032 0.0257  261  PHE B N   
5814 C  CA  . PHE B 262 ? 0.1550 0.1956 0.1663 -0.0488 -0.0130 0.0170  261  PHE B CA  
5815 C  C   . PHE B 262 ? 0.1764 0.2016 0.1818 -0.0243 -0.0255 0.0214  261  PHE B C   
5816 O  O   . PHE B 262 ? 0.1874 0.1697 0.2248 0.0390  -0.0585 0.0237  261  PHE B O   
5817 C  CB  . PHE B 262 ? 0.1567 0.1848 0.1663 -0.0580 -0.0029 0.0143  261  PHE B CB  
5818 C  CG  . PHE B 262 ? 0.1236 0.2360 0.2161 -0.0537 -0.0394 0.0034  261  PHE B CG  
5819 C  CD1 . PHE B 262 ? 0.1958 0.2565 0.2461 -0.0536 -0.0257 -0.0099 261  PHE B CD1 
5820 C  CD2 . PHE B 262 ? 0.1599 0.2689 0.2059 -0.0799 0.0023  -0.0028 261  PHE B CD2 
5821 C  CE1 . PHE B 262 ? 0.1625 0.2599 0.2435 -0.0008 -0.0157 -0.0240 261  PHE B CE1 
5822 C  CE2 . PHE B 262 ? 0.1022 0.2816 0.2173 -0.0460 -0.0502 -0.0081 261  PHE B CE2 
5823 C  CZ  . PHE B 262 ? 0.1154 0.2684 0.2393 0.0273  -0.0194 0.0136  261  PHE B CZ  
5824 N  N   . LEU B 263 ? 0.1620 0.2192 0.1512 -0.0374 -0.0383 -0.0038 262  LEU B N   
5825 C  CA  . LEU B 263 ? 0.1764 0.2689 0.1430 -0.0047 0.0323  -0.0233 262  LEU B CA  
5826 C  C   . LEU B 263 ? 0.2201 0.2693 0.1679 -0.0007 0.0288  -0.0172 262  LEU B C   
5827 O  O   . LEU B 263 ? 0.2240 0.2821 0.1702 0.0138  -0.0274 0.0025  262  LEU B O   
5828 C  CB  . LEU B 263 ? 0.1473 0.2805 0.1029 0.0151  0.0312  -0.0300 262  LEU B CB  
5829 C  CG  . LEU B 263 ? 0.1603 0.2715 0.1040 0.0003  -0.0026 0.0018  262  LEU B CG  
5830 C  CD1 . LEU B 263 ? 0.1821 0.2598 0.1159 0.0332  0.0011  0.0016  262  LEU B CD1 
5831 C  CD2 . LEU B 263 ? 0.1998 0.2886 0.1092 0.0259  -0.0455 0.0284  262  LEU B CD2 
5832 N  N   . ILE B 264 ? 0.1563 0.2359 0.1730 0.0183  -0.0024 -0.0478 263  ILE B N   
5833 C  CA  . ILE B 264 ? 0.1734 0.2151 0.1802 -0.0226 0.0303  -0.0468 263  ILE B CA  
5834 C  C   . ILE B 264 ? 0.1382 0.2587 0.1839 -0.0309 0.0255  -0.0108 263  ILE B C   
5835 O  O   . ILE B 264 ? 0.1640 0.2909 0.1980 -0.0149 0.0413  0.0170  263  ILE B O   
5836 C  CB  . ILE B 264 ? 0.2115 0.1876 0.2083 -0.0082 0.0831  -0.0099 263  ILE B CB  
5837 C  CG1 . ILE B 264 ? 0.1848 0.2000 0.2525 -0.0082 0.0566  0.0094  263  ILE B CG1 
5838 C  CG2 . ILE B 264 ? 0.2678 0.1617 0.2413 -0.0178 0.0659  0.0201  263  ILE B CG2 
5839 C  CD1 . ILE B 264 ? 0.2400 0.1885 0.2709 -0.0057 -0.0012 0.0339  263  ILE B CD1 
5840 N  N   . ALA B 265 ? 0.1016 0.2355 0.1736 -0.0320 0.0271  -0.0442 264  ALA B N   
5841 C  CA  . ALA B 265 ? 0.1954 0.2510 0.1712 0.0092  0.0240  -0.0468 264  ALA B CA  
5842 C  C   . ALA B 265 ? 0.1907 0.2092 0.1680 0.0014  0.0075  -0.0052 264  ALA B C   
5843 O  O   . ALA B 265 ? 0.2361 0.2323 0.1991 -0.0134 0.0069  0.0140  264  ALA B O   
5844 C  CB  . ALA B 265 ? 0.2305 0.2527 0.1438 -0.0064 -0.0550 -0.0670 264  ALA B CB  
5845 N  N   . GLY B 266 ? 0.1920 0.1709 0.1829 -0.0149 -0.0374 0.0418  265  GLY B N   
5846 C  CA  . GLY B 266 ? 0.2210 0.1864 0.2026 -0.0461 -0.0296 0.0503  265  GLY B CA  
5847 C  C   . GLY B 266 ? 0.1751 0.1845 0.1813 -0.0292 -0.0452 0.0603  265  GLY B C   
5848 O  O   . GLY B 266 ? 0.2065 0.1915 0.1887 0.0375  -0.0437 0.0706  265  GLY B O   
5849 N  N   . HIS B 267 ? 0.1625 0.2109 0.1793 -0.0843 0.0119  0.0073  266  HIS B N   
5850 C  CA  . HIS B 267 ? 0.1483 0.2393 0.1707 -0.0633 0.0201  -0.0040 266  HIS B CA  
5851 C  C   . HIS B 267 ? 0.1762 0.2486 0.1784 -0.0074 0.0195  0.0098  266  HIS B C   
5852 O  O   . HIS B 267 ? 0.1856 0.2662 0.1691 0.0611  0.0157  0.0174  266  HIS B O   
5853 C  CB  . HIS B 267 ? 0.1999 0.2199 0.1600 -0.0502 -0.0072 -0.0603 266  HIS B CB  
5854 C  CG  . HIS B 267 ? 0.2650 0.2396 0.1836 -0.0315 0.0132  -0.0608 266  HIS B CG  
5855 N  ND1 . HIS B 267 ? 0.2293 0.2732 0.1921 -0.0397 -0.0247 -0.0339 266  HIS B ND1 
5856 C  CD2 . HIS B 267 ? 0.1834 0.2198 0.1753 -0.0527 0.0442  -0.0603 266  HIS B CD2 
5857 C  CE1 . HIS B 267 ? 0.1045 0.2569 0.1972 -0.0455 -0.0357 -0.0510 266  HIS B CE1 
5858 N  NE2 . HIS B 267 ? 0.1869 0.2740 0.1818 -0.0588 0.0327  -0.0690 266  HIS B NE2 
5859 N  N   . GLU B 268 ? 0.1686 0.2518 0.1617 0.0022  -0.0208 0.0136  267  GLU B N   
5860 C  CA  . GLU B 268 ? 0.1813 0.2342 0.1766 -0.0231 0.0006  0.0113  267  GLU B CA  
5861 C  C   . GLU B 268 ? 0.1702 0.2198 0.1743 -0.0289 -0.0062 -0.0194 267  GLU B C   
5862 O  O   . GLU B 268 ? 0.1995 0.2365 0.1844 -0.0381 0.0342  -0.0329 267  GLU B O   
5863 C  CB  . GLU B 268 ? 0.1867 0.2264 0.2229 -0.0422 0.0206  -0.0291 267  GLU B CB  
5864 C  CG  . GLU B 268 ? 0.1386 0.2623 0.2560 -0.0961 0.0317  -0.0383 267  GLU B CG  
5865 C  CD  . GLU B 268 ? 0.2450 0.3368 0.3049 -0.0336 -0.0022 0.0137  267  GLU B CD  
5866 O  OE1 . GLU B 268 ? 0.2737 0.3393 0.2914 -0.0470 -0.0203 0.0606  267  GLU B OE1 
5867 O  OE2 . GLU B 268 ? 0.3548 0.3613 0.3484 -0.0317 -0.0249 0.0174  267  GLU B OE2 
5868 N  N   . THR B 269 ? 0.1489 0.1543 0.1209 -0.0092 -0.0143 -0.0021 268  THR B N   
5869 C  CA  . THR B 269 ? 0.0646 0.1530 0.1482 0.0478  -0.0040 0.0027  268  THR B CA  
5870 C  C   . THR B 269 ? 0.1124 0.1639 0.1458 0.0032  0.0222  -0.0062 268  THR B C   
5871 O  O   . THR B 269 ? 0.1980 0.1671 0.1555 0.0196  -0.0019 0.0035  268  THR B O   
5872 C  CB  . THR B 269 ? 0.1411 0.1532 0.1900 0.0099  -0.0472 0.0151  268  THR B CB  
5873 O  OG1 . THR B 269 ? 0.1603 0.1600 0.2090 0.0068  -0.0187 -0.0101 268  THR B OG1 
5874 C  CG2 . THR B 269 ? 0.1835 0.1524 0.2088 -0.0132 -0.0365 0.0354  268  THR B CG2 
5875 N  N   . THR B 270 ? 0.0992 0.1693 0.1421 0.0159  0.0215  -0.0091 269  THR B N   
5876 C  CA  . THR B 270 ? 0.1171 0.1761 0.1322 -0.0375 -0.0366 -0.0142 269  THR B CA  
5877 C  C   . THR B 270 ? 0.1293 0.1555 0.1476 -0.0264 -0.0064 -0.0337 269  THR B C   
5878 O  O   . THR B 270 ? 0.1122 0.1598 0.1718 0.0189  0.0070  -0.0105 269  THR B O   
5879 C  CB  . THR B 270 ? 0.1513 0.1642 0.1453 -0.0419 -0.0411 0.0055  269  THR B CB  
5880 O  OG1 . THR B 270 ? 0.1715 0.1956 0.1350 -0.0268 0.0038  -0.0224 269  THR B OG1 
5881 C  CG2 . THR B 270 ? 0.2203 0.1887 0.1386 -0.0171 -0.0065 0.0127  269  THR B CG2 
5882 N  N   . SER B 271 ? 0.2160 0.1545 0.1240 -0.0188 -0.0202 -0.0238 270  SER B N   
5883 C  CA  . SER B 271 ? 0.1556 0.1606 0.1100 -0.0246 0.0073  -0.0713 270  SER B CA  
5884 C  C   . SER B 271 ? 0.0613 0.1529 0.1312 0.0022  -0.0119 -0.0358 270  SER B C   
5885 O  O   . SER B 271 ? 0.1113 0.1696 0.1419 -0.0110 0.0262  -0.0406 270  SER B O   
5886 C  CB  . SER B 271 ? 0.2065 0.2187 0.1516 -0.0639 0.0130  -0.0937 270  SER B CB  
5887 O  OG  . SER B 271 ? 0.3931 0.2729 0.1896 -0.0154 0.0184  -0.0942 270  SER B OG  
5888 N  N   . GLY B 272 ? 0.1758 0.1150 0.0975 -0.0108 -0.0286 0.0061  271  GLY B N   
5889 C  CA  . GLY B 272 ? 0.1638 0.1156 0.1125 -0.0045 0.0155  0.0201  271  GLY B CA  
5890 C  C   . GLY B 272 ? 0.1756 0.1216 0.1337 0.0042  0.0278  -0.0106 271  GLY B C   
5891 O  O   . GLY B 272 ? 0.1890 0.1570 0.1204 0.0037  0.0116  -0.0051 271  GLY B O   
5892 N  N   . LEU B 273 ? 0.1364 0.1172 0.1270 0.0219  0.0225  -0.0111 272  LEU B N   
5893 C  CA  . LEU B 273 ? 0.1556 0.1291 0.1288 0.0311  -0.0095 -0.0265 272  LEU B CA  
5894 C  C   . LEU B 273 ? 0.1894 0.1461 0.0995 0.0170  -0.0006 -0.0154 272  LEU B C   
5895 O  O   . LEU B 273 ? 0.1760 0.1727 0.1065 0.0101  -0.0275 -0.0460 272  LEU B O   
5896 C  CB  . LEU B 273 ? 0.1755 0.1791 0.1195 -0.0233 -0.0099 -0.0593 272  LEU B CB  
5897 C  CG  . LEU B 273 ? 0.1489 0.1391 0.1084 -0.0386 0.0053  -0.0534 272  LEU B CG  
5898 C  CD1 . LEU B 273 ? 0.2068 0.1535 0.0928 0.0280  0.0283  -0.0501 272  LEU B CD1 
5899 C  CD2 . LEU B 273 ? 0.1728 0.1354 0.1422 -0.0710 0.0079  -0.0536 272  LEU B CD2 
5900 N  N   . LEU B 274 ? 0.1736 0.1164 0.0858 -0.0120 -0.0403 -0.0234 273  LEU B N   
5901 C  CA  . LEU B 274 ? 0.1425 0.1180 0.0989 -0.0351 -0.0020 0.0306  273  LEU B CA  
5902 C  C   . LEU B 274 ? 0.1356 0.1372 0.1135 0.0026  -0.0178 0.0071  273  LEU B C   
5903 O  O   . LEU B 274 ? 0.1102 0.1243 0.1258 0.0111  0.0021  -0.0164 273  LEU B O   
5904 C  CB  . LEU B 274 ? 0.1136 0.1007 0.1191 -0.0467 0.0380  0.0173  273  LEU B CB  
5905 C  CG  . LEU B 274 ? 0.1034 0.1105 0.1671 0.0095  0.0214  -0.0108 273  LEU B CG  
5906 C  CD1 . LEU B 274 ? 0.0963 0.1607 0.1692 0.0083  0.0141  -0.0223 273  LEU B CD1 
5907 C  CD2 . LEU B 274 ? 0.1098 0.1130 0.2056 0.0343  -0.0327 -0.0068 273  LEU B CD2 
5908 N  N   . SER B 275 ? 0.1583 0.1363 0.1047 -0.0403 -0.0075 -0.0158 274  SER B N   
5909 C  CA  . SER B 275 ? 0.1491 0.1437 0.1315 0.0022  0.0203  -0.0243 274  SER B CA  
5910 C  C   . SER B 275 ? 0.2094 0.1509 0.1117 0.0369  0.0030  -0.0288 274  SER B C   
5911 O  O   . SER B 275 ? 0.1917 0.1676 0.1215 0.0325  0.0003  -0.0315 274  SER B O   
5912 C  CB  . SER B 275 ? 0.1765 0.1615 0.1185 0.0399  0.0429  -0.0207 274  SER B CB  
5913 O  OG  . SER B 275 ? 0.1504 0.1585 0.1071 -0.0025 -0.0026 -0.0345 274  SER B OG  
5914 N  N   . PHE B 276 ? 0.2137 0.1181 0.0923 0.0153  0.0198  -0.0133 275  PHE B N   
5915 C  CA  . PHE B 276 ? 0.1346 0.1176 0.0868 0.0205  -0.0102 -0.0070 275  PHE B CA  
5916 C  C   . PHE B 276 ? 0.1539 0.1313 0.1196 0.0027  0.0235  -0.0005 275  PHE B C   
5917 O  O   . PHE B 276 ? 0.1412 0.1442 0.1150 -0.0313 0.0077  -0.0263 275  PHE B O   
5918 C  CB  . PHE B 276 ? 0.1441 0.1184 0.1159 -0.0240 -0.0125 0.0162  275  PHE B CB  
5919 C  CG  . PHE B 276 ? 0.1911 0.1360 0.1218 -0.0420 -0.0084 0.0137  275  PHE B CG  
5920 C  CD1 . PHE B 276 ? 0.1621 0.1330 0.1330 0.0034  -0.0097 -0.0163 275  PHE B CD1 
5921 C  CD2 . PHE B 276 ? 0.1664 0.1266 0.1383 0.0407  -0.0407 -0.0080 275  PHE B CD2 
5922 C  CE1 . PHE B 276 ? 0.1269 0.1264 0.1551 0.0613  -0.0379 0.0223  275  PHE B CE1 
5923 C  CE2 . PHE B 276 ? 0.1241 0.1504 0.1536 -0.0062 -0.0482 -0.0182 275  PHE B CE2 
5924 C  CZ  . PHE B 276 ? 0.1771 0.1462 0.1662 0.0205  -0.0349 0.0008  275  PHE B CZ  
5925 N  N   . ALA B 277 ? 0.1336 0.0911 0.1268 0.0460  0.0021  -0.0062 276  ALA B N   
5926 C  CA  . ALA B 277 ? 0.1209 0.0984 0.1603 -0.0019 -0.0441 -0.0178 276  ALA B CA  
5927 C  C   . ALA B 277 ? 0.1187 0.1480 0.1415 0.0150  -0.0584 -0.0425 276  ALA B C   
5928 O  O   . ALA B 277 ? 0.1254 0.1621 0.1599 0.0196  -0.0033 0.0015  276  ALA B O   
5929 C  CB  . ALA B 277 ? 0.0997 0.1021 0.1883 -0.0455 -0.0076 -0.0315 276  ALA B CB  
5930 N  N   . LEU B 278 ? 0.1636 0.1406 0.1012 -0.0429 -0.0349 -0.0394 277  LEU B N   
5931 C  CA  . LEU B 278 ? 0.1000 0.1606 0.0905 -0.0043 0.0000  -0.0175 277  LEU B CA  
5932 C  C   . LEU B 278 ? 0.1531 0.1704 0.1160 0.0077  0.0230  0.0063  277  LEU B C   
5933 O  O   . LEU B 278 ? 0.2063 0.1860 0.1304 0.0196  0.0090  -0.0076 277  LEU B O   
5934 C  CB  . LEU B 278 ? 0.1579 0.1977 0.0722 0.0483  -0.0281 -0.0302 277  LEU B CB  
5935 C  CG  . LEU B 278 ? 0.2849 0.2291 0.0991 0.0255  -0.0268 -0.0501 277  LEU B CG  
5936 C  CD1 . LEU B 278 ? 0.3683 0.2472 0.1440 0.0707  -0.0187 -0.0637 277  LEU B CD1 
5937 C  CD2 . LEU B 278 ? 0.2888 0.2484 0.0820 0.0043  -0.0308 -0.0267 277  LEU B CD2 
5938 N  N   . TYR B 279 ? 0.1004 0.1325 0.1306 -0.0155 -0.0025 0.0101  278  TYR B N   
5939 C  CA  . TYR B 279 ? 0.1272 0.1330 0.1264 -0.0132 0.0200  0.0205  278  TYR B CA  
5940 C  C   . TYR B 279 ? 0.1125 0.1465 0.1324 -0.0515 -0.0073 -0.0030 278  TYR B C   
5941 O  O   . TYR B 279 ? 0.1130 0.2038 0.1344 -0.0126 -0.0259 -0.0218 278  TYR B O   
5942 C  CB  . TYR B 279 ? 0.1390 0.1327 0.1453 -0.0058 0.0207  0.0476  278  TYR B CB  
5943 C  CG  . TYR B 279 ? 0.1355 0.1481 0.1781 -0.0327 -0.0257 -0.0170 278  TYR B CG  
5944 C  CD1 . TYR B 279 ? 0.1276 0.1380 0.2101 -0.0552 -0.0039 -0.0281 278  TYR B CD1 
5945 C  CD2 . TYR B 279 ? 0.1713 0.1541 0.1767 -0.0215 -0.0215 -0.0266 278  TYR B CD2 
5946 C  CE1 . TYR B 279 ? 0.1552 0.1100 0.2110 -0.0025 0.0051  -0.0061 278  TYR B CE1 
5947 C  CE2 . TYR B 279 ? 0.1685 0.1280 0.1833 -0.0426 0.0157  -0.0269 278  TYR B CE2 
5948 C  CZ  . TYR B 279 ? 0.1585 0.1428 0.1977 -0.0403 0.0207  -0.0119 278  TYR B CZ  
5949 O  OH  . TYR B 279 ? 0.2363 0.1893 0.1969 -0.0314 0.0466  -0.0105 278  TYR B OH  
5950 N  N   . PHE B 280 ? 0.1884 0.1264 0.1130 0.0009  0.0068  -0.0239 279  PHE B N   
5951 C  CA  . PHE B 280 ? 0.1547 0.1289 0.1157 -0.0183 -0.0474 -0.0301 279  PHE B CA  
5952 C  C   . PHE B 280 ? 0.1337 0.1447 0.1525 -0.0017 -0.0221 -0.0382 279  PHE B C   
5953 O  O   . PHE B 280 ? 0.1175 0.1574 0.1931 0.0177  0.0287  -0.0324 279  PHE B O   
5954 C  CB  . PHE B 280 ? 0.1876 0.1650 0.1268 -0.0007 -0.0364 0.0056  279  PHE B CB  
5955 C  CG  . PHE B 280 ? 0.2202 0.1613 0.1135 -0.0128 -0.0766 0.0213  279  PHE B CG  
5956 C  CD1 . PHE B 280 ? 0.2484 0.1460 0.1061 -0.0385 0.0200  0.0386  279  PHE B CD1 
5957 C  CD2 . PHE B 280 ? 0.2162 0.1599 0.1155 0.0398  -0.0157 0.0110  279  PHE B CD2 
5958 C  CE1 . PHE B 280 ? 0.2331 0.1897 0.1162 -0.0243 0.0003  0.0151  279  PHE B CE1 
5959 C  CE2 . PHE B 280 ? 0.2037 0.1916 0.1068 -0.0167 -0.0264 0.0357  279  PHE B CE2 
5960 C  CZ  . PHE B 280 ? 0.1389 0.1993 0.1334 -0.0315 0.0322  0.0208  279  PHE B CZ  
5961 N  N   . LEU B 281 ? 0.1523 0.1187 0.1658 0.0295  -0.0373 -0.0131 280  LEU B N   
5962 C  CA  . LEU B 281 ? 0.1204 0.1228 0.1867 0.0055  0.0128  -0.0097 280  LEU B CA  
5963 C  C   . LEU B 281 ? 0.1744 0.1555 0.1737 0.0010  -0.0138 -0.0061 280  LEU B C   
5964 O  O   . LEU B 281 ? 0.1647 0.1741 0.1777 0.0171  -0.0164 0.0091  280  LEU B O   
5965 C  CB  . LEU B 281 ? 0.1225 0.1420 0.2066 -0.0304 0.0425  0.0148  280  LEU B CB  
5966 C  CG  . LEU B 281 ? 0.0915 0.1461 0.2238 -0.0474 0.0311  -0.0405 280  LEU B CG  
5967 C  CD1 . LEU B 281 ? 0.1524 0.2066 0.2666 -0.0503 0.0045  -0.0004 280  LEU B CD1 
5968 C  CD2 . LEU B 281 ? 0.2182 0.1624 0.3015 -0.0283 0.0079  -0.0527 280  LEU B CD2 
5969 N  N   . VAL B 282 ? 0.1337 0.1868 0.1632 0.0010  -0.0461 -0.0118 281  VAL B N   
5970 C  CA  . VAL B 282 ? 0.1286 0.2053 0.1419 -0.0147 -0.0570 -0.0130 281  VAL B CA  
5971 C  C   . VAL B 282 ? 0.1607 0.2070 0.1734 -0.0258 -0.0287 -0.0064 281  VAL B C   
5972 O  O   . VAL B 282 ? 0.1545 0.2389 0.1962 -0.0188 -0.0021 0.0047  281  VAL B O   
5973 C  CB  . VAL B 282 ? 0.1759 0.2081 0.1518 0.0570  -0.0153 0.0172  281  VAL B CB  
5974 C  CG1 . VAL B 282 ? 0.1853 0.2053 0.1552 0.0114  0.0177  0.0106  281  VAL B CG1 
5975 C  CG2 . VAL B 282 ? 0.1277 0.2281 0.1465 0.0471  -0.0442 -0.0080 281  VAL B CG2 
5976 N  N   . LYS B 283 ? 0.1349 0.1664 0.1348 -0.0231 0.0077  -0.0143 282  LYS B N   
5977 C  CA  . LYS B 283 ? 0.1764 0.1474 0.1476 -0.0051 -0.0116 0.0085  282  LYS B CA  
5978 C  C   . LYS B 283 ? 0.1578 0.1371 0.1856 -0.0009 -0.0014 0.0039  282  LYS B C   
5979 O  O   . LYS B 283 ? 0.2028 0.1467 0.1831 -0.0073 0.0018  -0.0141 282  LYS B O   
5980 C  CB  . LYS B 283 ? 0.2359 0.1132 0.1665 -0.0211 -0.0131 -0.0200 282  LYS B CB  
5981 C  CG  . LYS B 283 ? 0.2124 0.1263 0.1878 -0.0440 -0.0443 -0.0456 282  LYS B CG  
5982 C  CD  . LYS B 283 ? 0.2189 0.1199 0.2009 -0.0699 -0.0078 -0.0519 282  LYS B CD  
5983 C  CE  . LYS B 283 ? 0.1869 0.1143 0.1847 -0.0497 -0.0242 -0.0616 282  LYS B CE  
5984 N  NZ  . LYS B 283 ? 0.1878 0.1405 0.1830 -0.0373 -0.0210 -0.0828 282  LYS B NZ  
5985 N  N   . ASN B 284 ? 0.1091 0.1231 0.1897 0.0203  -0.0002 -0.0107 283  ASN B N   
5986 C  CA  . ASN B 284 ? 0.1498 0.1452 0.1673 0.0242  -0.0302 -0.0116 283  ASN B CA  
5987 C  C   . ASN B 284 ? 0.0762 0.1534 0.1663 -0.0130 0.0213  -0.0149 283  ASN B C   
5988 O  O   . ASN B 284 ? 0.1565 0.1581 0.1627 -0.0193 0.0092  0.0036  283  ASN B O   
5989 C  CB  . ASN B 284 ? 0.1534 0.1601 0.1764 0.0482  -0.0534 -0.0098 283  ASN B CB  
5990 C  CG  . ASN B 284 ? 0.1980 0.1872 0.1690 0.0520  -0.0049 -0.0024 283  ASN B CG  
5991 O  OD1 . ASN B 284 ? 0.1935 0.1978 0.1631 0.0694  0.0276  -0.0199 283  ASN B OD1 
5992 N  ND2 . ASN B 284 ? 0.1967 0.1588 0.1607 0.0221  -0.0138 0.0029  283  ASN B ND2 
5993 N  N   . PRO B 285 ? 0.1015 0.1403 0.1712 -0.0145 -0.0064 -0.0012 284  PRO B N   
5994 C  CA  . PRO B 285 ? 0.1268 0.1519 0.1726 0.0083  -0.0373 0.0237  284  PRO B CA  
5995 C  C   . PRO B 285 ? 0.1691 0.1401 0.1542 -0.0252 0.0023  -0.0037 284  PRO B C   
5996 O  O   . PRO B 285 ? 0.1420 0.1315 0.1881 -0.0034 0.0022  0.0184  284  PRO B O   
5997 C  CB  . PRO B 285 ? 0.1360 0.1934 0.2382 -0.0345 -0.0397 0.0463  284  PRO B CB  
5998 C  CG  . PRO B 285 ? 0.1457 0.1780 0.2187 -0.0235 -0.0489 0.0622  284  PRO B CG  
5999 C  CD  . PRO B 285 ? 0.0970 0.1552 0.2019 -0.0374 -0.0112 0.0357  284  PRO B CD  
6000 N  N   . HIS B 286 ? 0.1209 0.1664 0.1523 0.0131  0.0178  -0.0136 285  HIS B N   
6001 C  CA  . HIS B 286 ? 0.1078 0.1491 0.1547 0.0148  0.0383  -0.0291 285  HIS B CA  
6002 C  C   . HIS B 286 ? 0.0951 0.1719 0.1823 -0.0128 0.0442  -0.0247 285  HIS B C   
6003 O  O   . HIS B 286 ? 0.1544 0.1931 0.1892 -0.0110 0.0226  -0.0124 285  HIS B O   
6004 C  CB  . HIS B 286 ? 0.0931 0.1784 0.1738 0.0176  0.0647  -0.0170 285  HIS B CB  
6005 C  CG  . HIS B 286 ? 0.1390 0.2066 0.1809 0.0215  0.0675  -0.0570 285  HIS B CG  
6006 N  ND1 . HIS B 286 ? 0.2084 0.2252 0.2339 0.0467  0.0611  -0.0539 285  HIS B ND1 
6007 C  CD2 . HIS B 286 ? 0.1387 0.2442 0.1768 -0.0618 0.0618  -0.0608 285  HIS B CD2 
6008 C  CE1 . HIS B 286 ? 0.1862 0.2353 0.2295 -0.0067 0.0839  -0.0361 285  HIS B CE1 
6009 N  NE2 . HIS B 286 ? 0.1299 0.2494 0.1996 -0.0528 0.0508  -0.0441 285  HIS B NE2 
6010 N  N   . VAL B 287 ? 0.1138 0.1773 0.1736 0.0323  0.0321  -0.0106 286  VAL B N   
6011 C  CA  . VAL B 287 ? 0.1161 0.1735 0.1712 0.0279  0.0150  -0.0145 286  VAL B CA  
6012 C  C   . VAL B 287 ? 0.0748 0.1508 0.1740 -0.0200 0.0207  -0.0096 286  VAL B C   
6013 O  O   . VAL B 287 ? 0.1125 0.1540 0.1823 -0.0339 0.0175  -0.0130 286  VAL B O   
6014 C  CB  . VAL B 287 ? 0.1077 0.1552 0.1760 0.0235  0.0373  -0.0235 286  VAL B CB  
6015 C  CG1 . VAL B 287 ? 0.0709 0.1361 0.1992 -0.0168 -0.0023 -0.0357 286  VAL B CG1 
6016 C  CG2 . VAL B 287 ? 0.1426 0.1493 0.1436 0.0097  0.0005  0.0313  286  VAL B CG2 
6017 N  N   . LEU B 288 ? 0.1156 0.1858 0.1605 0.0060  -0.0265 -0.0180 287  LEU B N   
6018 C  CA  . LEU B 288 ? 0.1182 0.1344 0.1633 -0.0211 -0.0088 -0.0277 287  LEU B CA  
6019 C  C   . LEU B 288 ? 0.2014 0.1512 0.1897 0.0153  -0.0050 -0.0144 287  LEU B C   
6020 O  O   . LEU B 288 ? 0.1939 0.1480 0.1839 0.0188  0.0081  -0.0067 287  LEU B O   
6021 C  CB  . LEU B 288 ? 0.1824 0.1597 0.1581 -0.0446 0.0108  -0.0774 287  LEU B CB  
6022 C  CG  . LEU B 288 ? 0.2848 0.2181 0.2057 -0.1124 -0.0203 -0.0688 287  LEU B CG  
6023 C  CD1 . LEU B 288 ? 0.3307 0.2512 0.2194 -0.0825 -0.0014 -0.0705 287  LEU B CD1 
6024 C  CD2 . LEU B 288 ? 0.4577 0.2535 0.2552 -0.1577 -0.0215 -0.0583 287  LEU B CD2 
6025 N  N   . GLN B 289 ? 0.1781 0.1362 0.2060 0.0661  -0.0235 -0.0097 288  GLN B N   
6026 C  CA  . GLN B 289 ? 0.0999 0.1547 0.2119 0.0613  -0.0285 -0.0155 288  GLN B CA  
6027 C  C   . GLN B 289 ? 0.1277 0.1659 0.1814 0.0070  -0.0711 -0.0118 288  GLN B C   
6028 O  O   . GLN B 289 ? 0.1799 0.1540 0.1615 0.0172  0.0027  -0.0048 288  GLN B O   
6029 C  CB  . GLN B 289 ? 0.1182 0.2012 0.2546 0.0847  -0.0119 0.0026  288  GLN B CB  
6030 C  CG  . GLN B 289 ? 0.1761 0.3178 0.3392 0.1158  0.0089  -0.0635 288  GLN B CG  
6031 C  CD  . GLN B 289 ? 0.5115 0.4662 0.4033 0.1548  -0.0347 -0.1197 288  GLN B CD  
6032 O  OE1 . GLN B 289 ? 0.5600 0.5303 0.4450 0.1434  0.0309  -0.1146 288  GLN B OE1 
6033 N  NE2 . GLN B 289 ? 0.6561 0.5133 0.4226 0.1541  -0.1154 -0.1196 288  GLN B NE2 
6034 N  N   . LYS B 290 ? 0.0890 0.1899 0.1549 0.0192  -0.0499 -0.0164 289  LYS B N   
6035 C  CA  . LYS B 290 ? 0.1136 0.2030 0.1290 0.0087  0.0011  -0.0449 289  LYS B CA  
6036 C  C   . LYS B 290 ? 0.1292 0.1863 0.1664 0.0098  0.0400  -0.0373 289  LYS B C   
6037 O  O   . LYS B 290 ? 0.1200 0.2056 0.1669 0.0146  -0.0092 -0.0450 289  LYS B O   
6038 C  CB  . LYS B 290 ? 0.2437 0.2543 0.1260 0.0370  0.0372  0.0202  289  LYS B CB  
6039 C  CG  . LYS B 290 ? 0.3924 0.2569 0.1327 0.0449  -0.0078 0.0093  289  LYS B CG  
6040 C  CD  . LYS B 290 ? 0.4000 0.2354 0.1064 0.0658  0.0056  0.0083  289  LYS B CD  
6041 C  CE  . LYS B 290 ? 0.3372 0.2089 0.1014 0.0608  0.0446  0.0194  289  LYS B CE  
6042 N  NZ  . LYS B 290 ? 0.2336 0.2090 0.1186 0.0550  0.0518  0.0204  289  LYS B NZ  
6043 N  N   . ALA B 291 ? 0.1157 0.1779 0.1559 0.0551  0.0511  -0.0222 290  ALA B N   
6044 C  CA  . ALA B 291 ? 0.1375 0.1440 0.1255 0.0258  0.0516  0.0054  290  ALA B CA  
6045 C  C   . ALA B 291 ? 0.1252 0.1500 0.1525 0.0283  0.0106  0.0177  290  ALA B C   
6046 O  O   . ALA B 291 ? 0.1914 0.1570 0.1639 0.0519  0.0222  0.0025  290  ALA B O   
6047 C  CB  . ALA B 291 ? 0.1878 0.1470 0.1536 0.0058  0.0255  0.0280  290  ALA B CB  
6048 N  N   . ALA B 292 ? 0.1248 0.1597 0.1614 0.0324  -0.0036 -0.0140 291  ALA B N   
6049 C  CA  . ALA B 292 ? 0.1460 0.1518 0.1466 -0.0028 -0.0310 -0.0076 291  ALA B CA  
6050 C  C   . ALA B 292 ? 0.1299 0.1420 0.1379 0.0346  0.0101  -0.0171 291  ALA B C   
6051 O  O   . ALA B 292 ? 0.1430 0.1888 0.1636 0.0050  -0.0062 -0.0028 291  ALA B O   
6052 C  CB  . ALA B 292 ? 0.1361 0.1466 0.1811 -0.0323 -0.0140 -0.0007 291  ALA B CB  
6053 N  N   . GLU B 293 ? 0.1781 0.1421 0.1276 0.0604  -0.0044 -0.0054 292  GLU B N   
6054 C  CA  . GLU B 293 ? 0.1838 0.1304 0.1413 0.0498  0.0299  -0.0228 292  GLU B CA  
6055 C  C   . GLU B 293 ? 0.1595 0.1597 0.1502 0.0018  -0.0168 0.0016  292  GLU B C   
6056 O  O   . GLU B 293 ? 0.1538 0.1451 0.1424 0.0118  0.0151  0.0010  292  GLU B O   
6057 C  CB  . GLU B 293 ? 0.1685 0.1332 0.1737 0.0614  0.0484  -0.0385 292  GLU B CB  
6058 C  CG  . GLU B 293 ? 0.1635 0.1211 0.2178 0.0427  0.0201  -0.0343 292  GLU B CG  
6059 C  CD  . GLU B 293 ? 0.2565 0.1484 0.2300 0.0204  0.0698  0.0020  292  GLU B CD  
6060 O  OE1 . GLU B 293 ? 0.2035 0.1711 0.2441 0.0195  0.0310  -0.0236 292  GLU B OE1 
6061 O  OE2 . GLU B 293 ? 0.3180 0.1460 0.2461 0.0063  -0.0152 0.0072  292  GLU B OE2 
6062 N  N   . GLU B 294 ? 0.1272 0.1826 0.1463 0.0085  -0.0243 -0.0263 293  GLU B N   
6063 C  CA  . GLU B 294 ? 0.1371 0.1824 0.1486 0.0236  -0.0258 -0.0285 293  GLU B CA  
6064 C  C   . GLU B 294 ? 0.2146 0.1715 0.1368 0.0070  -0.0214 -0.0336 293  GLU B C   
6065 O  O   . GLU B 294 ? 0.2101 0.1920 0.1280 -0.0078 -0.0238 -0.0287 293  GLU B O   
6066 C  CB  . GLU B 294 ? 0.1296 0.1718 0.1496 0.0321  -0.0653 -0.0335 293  GLU B CB  
6067 C  CG  . GLU B 294 ? 0.0931 0.1837 0.1630 0.0204  -0.0644 -0.0116 293  GLU B CG  
6068 C  CD  . GLU B 294 ? 0.1787 0.1985 0.1767 -0.0128 -0.0194 -0.0232 293  GLU B CD  
6069 O  OE1 . GLU B 294 ? 0.1732 0.1765 0.1655 -0.0371 0.0170  -0.0167 293  GLU B OE1 
6070 O  OE2 . GLU B 294 ? 0.1754 0.2163 0.1548 -0.0060 0.0196  -0.0386 293  GLU B OE2 
6071 N  N   . ALA B 295 ? 0.1638 0.1463 0.1292 0.0080  0.0377  -0.0439 294  ALA B N   
6072 C  CA  . ALA B 295 ? 0.2056 0.1441 0.1342 0.0108  0.0445  -0.0483 294  ALA B CA  
6073 C  C   . ALA B 295 ? 0.1829 0.1672 0.1577 0.0030  0.0045  -0.0074 294  ALA B C   
6074 O  O   . ALA B 295 ? 0.1910 0.1530 0.1753 0.0003  0.0478  0.0141  294  ALA B O   
6075 C  CB  . ALA B 295 ? 0.1992 0.1554 0.1525 0.0439  0.0550  -0.0191 294  ALA B CB  
6076 N  N   . ALA B 296 ? 0.1727 0.1625 0.1598 0.0452  -0.0623 -0.0171 295  ALA B N   
6077 C  CA  . ALA B 296 ? 0.1439 0.1610 0.1882 0.0202  -0.0447 -0.0032 295  ALA B CA  
6078 C  C   . ALA B 296 ? 0.2231 0.1609 0.1825 0.0434  -0.0236 0.0121  295  ALA B C   
6079 O  O   . ALA B 296 ? 0.2387 0.1949 0.1849 0.0270  -0.0429 0.0063  295  ALA B O   
6080 C  CB  . ALA B 296 ? 0.1852 0.1845 0.2072 -0.0361 -0.0385 -0.0285 295  ALA B CB  
6081 N  N   . ARG B 297 ? 0.2494 0.1502 0.1815 -0.0171 -0.0144 -0.0064 296  ARG B N   
6082 C  CA  . ARG B 297 ? 0.2512 0.1332 0.1902 -0.0056 0.0170  -0.0207 296  ARG B CA  
6083 C  C   . ARG B 297 ? 0.1574 0.1790 0.1795 0.0169  0.0028  0.0051  296  ARG B C   
6084 O  O   . ARG B 297 ? 0.2155 0.2142 0.2208 0.0091  -0.0299 0.0508  296  ARG B O   
6085 C  CB  . ARG B 297 ? 0.2505 0.1318 0.2055 0.0119  0.0269  -0.0477 296  ARG B CB  
6086 C  CG  . ARG B 297 ? 0.2473 0.1784 0.2246 0.0112  -0.0130 -0.0338 296  ARG B CG  
6087 C  CD  . ARG B 297 ? 0.2790 0.2013 0.2421 0.0528  0.0001  -0.0151 296  ARG B CD  
6088 N  NE  . ARG B 297 ? 0.2331 0.2070 0.2378 0.0612  0.0372  0.0049  296  ARG B NE  
6089 C  CZ  . ARG B 297 ? 0.2587 0.2095 0.2774 0.0168  -0.0135 -0.0203 296  ARG B CZ  
6090 N  NH1 . ARG B 297 ? 0.2683 0.2153 0.3105 -0.0042 -0.0078 -0.0594 296  ARG B NH1 
6091 N  NH2 . ARG B 297 ? 0.2779 0.1873 0.2780 0.0081  -0.0157 -0.0047 296  ARG B NH2 
6092 N  N   . VAL B 298 ? 0.1441 0.1795 0.1561 0.0868  -0.0116 0.0008  297  VAL B N   
6093 C  CA  . VAL B 298 ? 0.1277 0.2300 0.1500 0.0296  0.0332  0.0258  297  VAL B CA  
6094 C  C   . VAL B 298 ? 0.2282 0.2268 0.1523 0.0429  0.0080  -0.0077 297  VAL B C   
6095 O  O   . VAL B 298 ? 0.2606 0.2336 0.1615 0.0146  -0.0041 0.0151  297  VAL B O   
6096 C  CB  . VAL B 298 ? 0.1996 0.2375 0.1568 0.0195  0.0169  0.0146  297  VAL B CB  
6097 C  CG1 . VAL B 298 ? 0.1684 0.2469 0.1870 -0.0556 0.0155  0.0333  297  VAL B CG1 
6098 C  CG2 . VAL B 298 ? 0.2313 0.2323 0.1353 -0.0083 -0.0318 0.0148  297  VAL B CG2 
6099 N  N   . LEU B 299 ? 0.1961 0.1943 0.1396 0.0383  0.0176  -0.0424 298  LEU B N   
6100 C  CA  . LEU B 299 ? 0.2252 0.1525 0.1521 0.0452  -0.0097 -0.0246 298  LEU B CA  
6101 C  C   . LEU B 299 ? 0.2491 0.1705 0.1756 -0.0102 -0.0391 -0.0140 298  LEU B C   
6102 O  O   . LEU B 299 ? 0.2186 0.1922 0.1906 -0.0339 -0.0102 -0.0337 298  LEU B O   
6103 C  CB  . LEU B 299 ? 0.1479 0.1494 0.1861 0.0711  0.0091  -0.0039 298  LEU B CB  
6104 C  CG  . LEU B 299 ? 0.1229 0.1364 0.1971 -0.0112 -0.0313 0.0076  298  LEU B CG  
6105 C  CD1 . LEU B 299 ? 0.1625 0.1021 0.2347 -0.0459 -0.0182 -0.0260 298  LEU B CD1 
6106 C  CD2 . LEU B 299 ? 0.1783 0.1823 0.1911 -0.0408 -0.0383 0.0098  298  LEU B CD2 
6107 N  N   . VAL B 300 ? 0.2759 0.1979 0.1942 0.0272  -0.0320 0.0073  299  VAL B N   
6108 C  CA  . VAL B 300 ? 0.2624 0.2192 0.2026 0.0382  0.0151  0.0305  299  VAL B CA  
6109 C  C   . VAL B 300 ? 0.2466 0.2376 0.1974 0.0675  -0.0223 0.0219  299  VAL B C   
6110 O  O   . VAL B 300 ? 0.3215 0.2776 0.2223 0.0772  -0.0341 0.0217  299  VAL B O   
6111 C  CB  . VAL B 300 ? 0.3207 0.2830 0.2378 0.0256  0.0374  0.0190  299  VAL B CB  
6112 C  CG1 . VAL B 300 ? 0.3724 0.3042 0.2272 0.0597  0.0452  0.0062  299  VAL B CG1 
6113 C  CG2 . VAL B 300 ? 0.2353 0.2752 0.2464 -0.0076 0.0513  0.0418  299  VAL B CG2 
6114 N  N   . ASP B 301 ? 0.2073 0.2095 0.1861 -0.0224 -0.0105 0.0253  300  ASP B N   
6115 C  CA  . ASP B 301 ? 0.2604 0.2348 0.2130 -0.0250 0.0137  0.0137  300  ASP B CA  
6116 C  C   . ASP B 301 ? 0.3124 0.2554 0.1831 -0.0721 -0.0118 -0.0055 300  ASP B C   
6117 O  O   . ASP B 301 ? 0.3195 0.2630 0.1712 -0.0751 0.0114  0.0031  300  ASP B O   
6118 C  CB  . ASP B 301 ? 0.2503 0.2376 0.2445 -0.0516 -0.0214 0.0495  300  ASP B CB  
6119 C  CG  . ASP B 301 ? 0.3541 0.2374 0.2745 -0.0536 -0.0341 0.0293  300  ASP B CG  
6120 O  OD1 . ASP B 301 ? 0.4483 0.2087 0.3144 -0.0308 -0.0476 0.0034  300  ASP B OD1 
6121 O  OD2 . ASP B 301 ? 0.3983 0.2401 0.2836 -0.0893 0.0031  0.0217  300  ASP B OD2 
6122 N  N   . PRO B 302 ? 0.2871 0.2675 0.1603 -0.0265 -0.0248 0.0155  301  PRO B N   
6123 C  CA  . PRO B 302 ? 0.2906 0.2811 0.1556 -0.0187 -0.0274 0.0060  301  PRO B CA  
6124 C  C   . PRO B 302 ? 0.3141 0.2681 0.1713 -0.0515 -0.0208 0.0004  301  PRO B C   
6125 O  O   . PRO B 302 ? 0.3812 0.2290 0.2030 -0.0890 0.0119  -0.0069 301  PRO B O   
6126 C  CB  . PRO B 302 ? 0.4277 0.3065 0.1562 -0.0085 -0.0395 0.0116  301  PRO B CB  
6127 C  CG  . PRO B 302 ? 0.4836 0.3002 0.1868 -0.0215 -0.0149 -0.0026 301  PRO B CG  
6128 C  CD  . PRO B 302 ? 0.4077 0.2906 0.1833 -0.0194 -0.0186 0.0009  301  PRO B CD  
6129 N  N   . VAL B 303 ? 0.2760 0.2921 0.1752 -0.0451 -0.0288 -0.0126 302  VAL B N   
6130 C  CA  . VAL B 303 ? 0.3600 0.3187 0.2089 -0.0301 -0.0507 -0.0002 302  VAL B CA  
6131 C  C   . VAL B 303 ? 0.3610 0.2947 0.2042 0.0247  -0.0876 -0.0141 302  VAL B C   
6132 O  O   . VAL B 303 ? 0.4969 0.3189 0.2195 0.0538  -0.0882 0.0165  302  VAL B O   
6133 C  CB  . VAL B 303 ? 0.3430 0.3306 0.2400 -0.0441 0.0029  -0.0006 302  VAL B CB  
6134 C  CG1 . VAL B 303 ? 0.3237 0.3447 0.2605 -0.0213 -0.0130 0.0065  302  VAL B CG1 
6135 C  CG2 . VAL B 303 ? 0.3654 0.3565 0.2769 -0.0518 0.0670  0.0142  302  VAL B CG2 
6136 N  N   . PRO B 304 ? 0.2486 0.2802 0.1928 -0.0218 -0.0788 -0.0234 303  PRO B N   
6137 C  CA  . PRO B 304 ? 0.2316 0.2585 0.1964 -0.0143 -0.0419 0.0142  303  PRO B CA  
6138 C  C   . PRO B 304 ? 0.2187 0.2437 0.1703 -0.0146 -0.0466 0.0191  303  PRO B C   
6139 O  O   . PRO B 304 ? 0.2384 0.2777 0.1549 0.0058  -0.0368 0.0363  303  PRO B O   
6140 C  CB  . PRO B 304 ? 0.2549 0.2768 0.2266 -0.0487 -0.0243 -0.0105 303  PRO B CB  
6141 C  CG  . PRO B 304 ? 0.3003 0.2716 0.2228 -0.0844 -0.0443 -0.0344 303  PRO B CG  
6142 C  CD  . PRO B 304 ? 0.2235 0.2795 0.2150 -0.0396 -0.0388 -0.0047 303  PRO B CD  
6143 N  N   . SER B 305 ? 0.1867 0.2151 0.1684 -0.0546 -0.0218 0.0013  304  SER B N   
6144 C  CA  . SER B 305 ? 0.2245 0.1931 0.1938 -0.0276 -0.0379 -0.0187 304  SER B CA  
6145 C  C   . SER B 305 ? 0.2440 0.1782 0.1932 -0.0245 -0.0641 0.0031  304  SER B C   
6146 O  O   . SER B 305 ? 0.2166 0.1562 0.1986 -0.0153 -0.0552 0.0292  304  SER B O   
6147 C  CB  . SER B 305 ? 0.2587 0.1877 0.2160 0.0028  0.0151  -0.0137 304  SER B CB  
6148 O  OG  . SER B 305 ? 0.3123 0.1718 0.2104 -0.0360 -0.0145 -0.0269 304  SER B OG  
6149 N  N   . TYR B 306 ? 0.2269 0.1744 0.1830 -0.0316 -0.0988 -0.0224 305  TYR B N   
6150 C  CA  . TYR B 306 ? 0.1261 0.1835 0.1861 -0.0160 -0.0272 -0.0124 305  TYR B CA  
6151 C  C   . TYR B 306 ? 0.1482 0.1592 0.1828 -0.0181 0.0234  0.0061  305  TYR B C   
6152 O  O   . TYR B 306 ? 0.1931 0.1866 0.1796 -0.0217 -0.0031 -0.0185 305  TYR B O   
6153 C  CB  . TYR B 306 ? 0.1357 0.2394 0.1998 -0.0130 -0.0428 -0.0280 305  TYR B CB  
6154 C  CG  . TYR B 306 ? 0.2184 0.3094 0.2419 -0.0758 -0.0147 -0.0177 305  TYR B CG  
6155 C  CD1 . TYR B 306 ? 0.2276 0.3097 0.2551 -0.1070 -0.0107 -0.0004 305  TYR B CD1 
6156 C  CD2 . TYR B 306 ? 0.2775 0.3346 0.2667 -0.0231 -0.0031 -0.0142 305  TYR B CD2 
6157 C  CE1 . TYR B 306 ? 0.2635 0.3490 0.2910 -0.0773 -0.0361 0.0360  305  TYR B CE1 
6158 C  CE2 . TYR B 306 ? 0.3533 0.3665 0.2870 -0.0428 0.0021  0.0256  305  TYR B CE2 
6159 C  CZ  . TYR B 306 ? 0.3167 0.3974 0.3102 -0.0599 -0.0509 0.0665  305  TYR B CZ  
6160 O  OH  . TYR B 306 ? 0.3420 0.4571 0.3730 -0.0980 -0.0982 0.1110  305  TYR B OH  
6161 N  N   . LYS B 307 ? 0.2078 0.1487 0.1949 -0.0155 0.0369  -0.0216 306  LYS B N   
6162 C  CA  . LYS B 307 ? 0.1612 0.1531 0.2455 -0.0417 0.0307  0.0100  306  LYS B CA  
6163 C  C   . LYS B 307 ? 0.1876 0.1166 0.2279 -0.0103 0.0054  0.0013  306  LYS B C   
6164 O  O   . LYS B 307 ? 0.2118 0.1255 0.2368 -0.0140 -0.0431 0.0000  306  LYS B O   
6165 C  CB  . LYS B 307 ? 0.3180 0.2244 0.3254 -0.1076 -0.0072 0.0281  306  LYS B CB  
6166 C  CG  . LYS B 307 ? 0.5015 0.3096 0.3909 -0.1270 -0.0467 0.0517  306  LYS B CG  
6167 C  CD  . LYS B 307 ? 0.6670 0.3914 0.4392 -0.1052 -0.0440 0.0330  306  LYS B CD  
6168 C  CE  . LYS B 307 ? 0.7643 0.5019 0.4749 -0.0724 -0.0302 0.0350  306  LYS B CE  
6169 N  NZ  . LYS B 307 ? 0.8591 0.5703 0.4955 -0.0852 -0.0250 0.0417  306  LYS B NZ  
6170 N  N   . GLN B 308 ? 0.1944 0.1130 0.2248 -0.0034 -0.0182 -0.0099 307  GLN B N   
6171 C  CA  . GLN B 308 ? 0.2133 0.1541 0.1921 -0.0201 -0.0655 0.0096  307  GLN B CA  
6172 C  C   . GLN B 308 ? 0.1622 0.1588 0.1701 0.0398  -0.0345 -0.0036 307  GLN B C   
6173 O  O   . GLN B 308 ? 0.2336 0.1584 0.1791 0.0019  -0.0178 -0.0531 307  GLN B O   
6174 C  CB  . GLN B 308 ? 0.2573 0.1691 0.1422 0.0110  -0.0423 0.0121  307  GLN B CB  
6175 C  CG  . GLN B 308 ? 0.2306 0.1894 0.1664 0.0277  -0.0427 0.0076  307  GLN B CG  
6176 C  CD  . GLN B 308 ? 0.2474 0.2214 0.2107 0.0497  -0.0257 0.0216  307  GLN B CD  
6177 O  OE1 . GLN B 308 ? 0.2838 0.2568 0.1893 0.0489  -0.0291 0.0098  307  GLN B OE1 
6178 N  NE2 . GLN B 308 ? 0.2790 0.2368 0.2323 0.0792  -0.0133 0.0365  307  GLN B NE2 
6179 N  N   . VAL B 309 ? 0.1843 0.1573 0.1664 0.0365  0.0334  -0.0075 308  VAL B N   
6180 C  CA  . VAL B 309 ? 0.1643 0.1641 0.1441 0.0209  0.0116  -0.0021 308  VAL B CA  
6181 C  C   . VAL B 309 ? 0.1554 0.1634 0.1376 -0.0508 0.0167  0.0044  308  VAL B C   
6182 O  O   . VAL B 309 ? 0.2028 0.1484 0.1492 -0.0005 -0.0358 0.0041  308  VAL B O   
6183 C  CB  . VAL B 309 ? 0.2392 0.1801 0.1469 -0.0236 0.0037  -0.0007 308  VAL B CB  
6184 C  CG1 . VAL B 309 ? 0.2537 0.1625 0.1709 0.0036  0.0211  -0.0013 308  VAL B CG1 
6185 C  CG2 . VAL B 309 ? 0.1923 0.1943 0.1394 -0.0847 0.0470  0.0137  308  VAL B CG2 
6186 N  N   . LYS B 310 ? 0.1774 0.1474 0.1481 -0.0202 -0.0302 -0.0200 309  LYS B N   
6187 C  CA  . LYS B 310 ? 0.1577 0.1994 0.1920 -0.0737 0.0108  -0.0322 309  LYS B CA  
6188 C  C   . LYS B 310 ? 0.1428 0.1935 0.1931 -0.0420 -0.0125 -0.0348 309  LYS B C   
6189 O  O   . LYS B 310 ? 0.2161 0.2201 0.1960 0.0226  -0.0179 -0.0177 309  LYS B O   
6190 C  CB  . LYS B 310 ? 0.1697 0.2297 0.2337 -0.0797 -0.0081 -0.0051 309  LYS B CB  
6191 C  CG  . LYS B 310 ? 0.2296 0.2578 0.2935 -0.0798 0.0218  0.0528  309  LYS B CG  
6192 C  CD  . LYS B 310 ? 0.3653 0.2870 0.3669 -0.0292 -0.0064 0.0899  309  LYS B CD  
6193 C  CE  . LYS B 310 ? 0.5984 0.3201 0.4012 0.0171  -0.0225 0.1029  309  LYS B CE  
6194 N  NZ  . LYS B 310 ? 0.6898 0.3336 0.4095 0.0388  -0.0844 0.1132  309  LYS B NZ  
6195 N  N   . GLN B 311 ? 0.1123 0.1702 0.1648 -0.0100 -0.0053 -0.0207 310  GLN B N   
6196 C  CA  . GLN B 311 ? 0.1107 0.1305 0.1869 0.0225  0.0016  0.0062  310  GLN B CA  
6197 C  C   . GLN B 311 ? 0.1936 0.1482 0.1853 -0.0169 0.0037  -0.0023 310  GLN B C   
6198 O  O   . GLN B 311 ? 0.2484 0.1490 0.1999 0.0116  0.0380  -0.0028 310  GLN B O   
6199 C  CB  . GLN B 311 ? 0.2268 0.1102 0.1903 0.0089  0.0445  0.0025  310  GLN B CB  
6200 C  CG  . GLN B 311 ? 0.3441 0.1458 0.2169 0.0405  0.0593  -0.0055 310  GLN B CG  
6201 C  CD  . GLN B 311 ? 0.4181 0.1857 0.2339 0.0601  0.0477  -0.0067 310  GLN B CD  
6202 O  OE1 . GLN B 311 ? 0.5276 0.2000 0.2379 0.1060  0.0109  0.0149  310  GLN B OE1 
6203 N  NE2 . GLN B 311 ? 0.4285 0.2315 0.2722 0.0476  0.0837  -0.0179 310  GLN B NE2 
6204 N  N   . LEU B 312 ? 0.1890 0.1429 0.1667 -0.0391 -0.0267 -0.0010 311  LEU B N   
6205 C  CA  . LEU B 312 ? 0.1973 0.1277 0.1244 -0.0276 -0.0184 0.0211  311  LEU B CA  
6206 C  C   . LEU B 312 ? 0.1704 0.1511 0.1326 0.0100  0.0004  0.0055  311  LEU B C   
6207 O  O   . LEU B 312 ? 0.1906 0.1745 0.1609 -0.0169 0.0112  0.0111  311  LEU B O   
6208 C  CB  . LEU B 312 ? 0.1482 0.1191 0.0955 0.0296  -0.0169 0.0172  311  LEU B CB  
6209 C  CG  . LEU B 312 ? 0.1456 0.1484 0.1216 0.0457  -0.0149 -0.0109 311  LEU B CG  
6210 C  CD1 . LEU B 312 ? 0.2372 0.1628 0.1419 0.0346  -0.0002 -0.0201 311  LEU B CD1 
6211 C  CD2 . LEU B 312 ? 0.1291 0.1788 0.1522 0.0578  0.0252  0.0472  311  LEU B CD2 
6212 N  N   . LYS B 313 ? 0.2090 0.1596 0.1314 -0.0116 0.0043  -0.0137 312  LYS B N   
6213 C  CA  A LYS B 313 ? 0.2073 0.1223 0.1261 -0.0042 0.0003  -0.0211 312  LYS B CA  
6214 C  CA  B LYS B 313 ? 0.2158 0.1354 0.1441 -0.0058 -0.0251 -0.0123 312  LYS B CA  
6215 C  C   . LYS B 313 ? 0.2692 0.1211 0.1507 0.0002  -0.0400 -0.0245 312  LYS B C   
6216 O  O   . LYS B 313 ? 0.2146 0.0908 0.1547 -0.0143 -0.0028 -0.0271 312  LYS B O   
6217 C  CB  A LYS B 313 ? 0.2948 0.1105 0.1337 0.0036  -0.0114 -0.0467 312  LYS B CB  
6218 C  CB  B LYS B 313 ? 0.2444 0.1340 0.1706 -0.0016 -0.0676 -0.0257 312  LYS B CB  
6219 C  CG  A LYS B 313 ? 0.3394 0.1310 0.1580 -0.0017 0.0132  -0.0576 312  LYS B CG  
6220 C  CG  B LYS B 313 ? 0.2642 0.1301 0.2049 -0.0115 -0.0692 -0.0513 312  LYS B CG  
6221 C  CD  A LYS B 313 ? 0.4196 0.1461 0.2009 0.0133  -0.0269 -0.0271 312  LYS B CD  
6222 C  CD  B LYS B 313 ? 0.3316 0.1656 0.2470 0.0168  -0.0980 -0.0717 312  LYS B CD  
6223 C  CE  A LYS B 313 ? 0.4539 0.1400 0.2239 0.0622  -0.0425 0.0129  312  LYS B CE  
6224 C  CE  B LYS B 313 ? 0.3694 0.2266 0.2793 0.0421  -0.0810 -0.0618 312  LYS B CE  
6225 N  NZ  A LYS B 313 ? 0.3576 0.1658 0.2500 0.0479  -0.0578 0.0824  312  LYS B NZ  
6226 N  NZ  B LYS B 313 ? 0.4760 0.2755 0.3128 0.0280  -0.0825 -0.0603 312  LYS B NZ  
6227 N  N   . TYR B 314 ? 0.1603 0.1335 0.1333 -0.0483 -0.0228 -0.0222 313  TYR B N   
6228 C  CA  . TYR B 314 ? 0.0991 0.1628 0.1526 -0.0250 0.0121  -0.0409 313  TYR B CA  
6229 C  C   . TYR B 314 ? 0.1465 0.1267 0.1460 0.0296  0.0293  -0.0110 313  TYR B C   
6230 O  O   . TYR B 314 ? 0.1573 0.1765 0.1458 0.0063  0.0026  -0.0113 313  TYR B O   
6231 C  CB  . TYR B 314 ? 0.0751 0.1740 0.1598 -0.0064 0.0105  -0.0298 313  TYR B CB  
6232 C  CG  . TYR B 314 ? 0.1328 0.1649 0.1600 -0.0255 0.0460  -0.0115 313  TYR B CG  
6233 C  CD1 . TYR B 314 ? 0.2050 0.1464 0.1775 -0.0261 0.0549  0.0180  313  TYR B CD1 
6234 C  CD2 . TYR B 314 ? 0.1494 0.1234 0.1890 -0.0273 -0.0030 0.0195  313  TYR B CD2 
6235 C  CE1 . TYR B 314 ? 0.1395 0.1059 0.2013 -0.0346 0.0663  -0.0109 313  TYR B CE1 
6236 C  CE2 . TYR B 314 ? 0.1365 0.1498 0.1626 -0.0326 0.0303  0.0051  313  TYR B CE2 
6237 C  CZ  . TYR B 314 ? 0.1812 0.1232 0.1772 -0.0417 0.0557  -0.0048 313  TYR B CZ  
6238 O  OH  . TYR B 314 ? 0.1518 0.1390 0.1968 0.0095  0.0048  -0.0435 313  TYR B OH  
6239 N  N   . VAL B 315 ? 0.1487 0.1310 0.1278 0.0405  0.0482  -0.0299 314  VAL B N   
6240 C  CA  . VAL B 315 ? 0.1349 0.1583 0.1257 -0.0197 0.0269  -0.0165 314  VAL B CA  
6241 C  C   . VAL B 315 ? 0.1750 0.1609 0.1431 -0.0065 -0.0200 -0.0204 314  VAL B C   
6242 O  O   . VAL B 315 ? 0.1291 0.1428 0.1408 -0.0107 0.0133  -0.0180 314  VAL B O   
6243 C  CB  . VAL B 315 ? 0.1176 0.1634 0.1407 0.0306  -0.0021 -0.0062 314  VAL B CB  
6244 C  CG1 . VAL B 315 ? 0.1835 0.1517 0.1190 0.0085  0.0169  -0.0170 314  VAL B CG1 
6245 C  CG2 . VAL B 315 ? 0.1005 0.1693 0.1832 0.0370  -0.0377 0.0077  314  VAL B CG2 
6246 N  N   . GLY B 316 ? 0.1379 0.2008 0.1371 -0.0012 -0.0475 -0.0141 315  GLY B N   
6247 C  CA  . GLY B 316 ? 0.1325 0.2117 0.1317 -0.0490 -0.0271 -0.0001 315  GLY B CA  
6248 C  C   . GLY B 316 ? 0.1774 0.2165 0.1286 -0.0226 0.0072  0.0230  315  GLY B C   
6249 O  O   . GLY B 316 ? 0.1924 0.1860 0.1350 0.0169  0.0059  0.0161  315  GLY B O   
6250 N  N   . MET B 317 ? 0.0915 0.2154 0.1329 -0.0251 -0.0069 -0.0182 316  MET B N   
6251 C  CA  . MET B 317 ? 0.1250 0.2131 0.1410 -0.0001 0.0410  -0.0373 316  MET B CA  
6252 C  C   . MET B 317 ? 0.1804 0.1654 0.1342 0.0101  0.0413  -0.0207 316  MET B C   
6253 O  O   . MET B 317 ? 0.1872 0.1363 0.1486 -0.0259 0.0230  -0.0156 316  MET B O   
6254 C  CB  . MET B 317 ? 0.1390 0.2197 0.1535 -0.0329 -0.0051 -0.0766 316  MET B CB  
6255 C  CG  . MET B 317 ? 0.1034 0.2174 0.1770 -0.0005 -0.0042 -0.1156 316  MET B CG  
6256 S  SD  . MET B 317 ? 0.2153 0.2907 0.2165 0.0445  0.0103  -0.0930 316  MET B SD  
6257 C  CE  . MET B 317 ? 0.2526 0.3013 0.2238 0.0118  0.0048  -0.0303 316  MET B CE  
6258 N  N   . VAL B 318 ? 0.1236 0.1436 0.1274 0.0642  0.0044  -0.0301 317  VAL B N   
6259 C  CA  . VAL B 318 ? 0.1162 0.1341 0.1141 0.0493  -0.0045 -0.0481 317  VAL B CA  
6260 C  C   . VAL B 318 ? 0.1393 0.1553 0.1446 -0.0035 0.0070  -0.0306 317  VAL B C   
6261 O  O   . VAL B 318 ? 0.1436 0.1699 0.1711 0.0024  0.0130  -0.0258 317  VAL B O   
6262 C  CB  . VAL B 318 ? 0.1396 0.1265 0.1220 0.0599  -0.0092 -0.0524 317  VAL B CB  
6263 C  CG1 . VAL B 318 ? 0.1396 0.1398 0.1512 0.0171  0.0075  -0.0089 317  VAL B CG1 
6264 C  CG2 . VAL B 318 ? 0.2103 0.0992 0.1493 0.0076  0.0229  -0.0620 317  VAL B CG2 
6265 N  N   . LEU B 319 ? 0.0700 0.1407 0.1435 0.0300  0.0133  -0.0318 318  LEU B N   
6266 C  CA  . LEU B 319 ? 0.1158 0.1566 0.1101 -0.0058 0.0284  -0.0111 318  LEU B CA  
6267 C  C   . LEU B 319 ? 0.1402 0.1756 0.1220 -0.0057 -0.0208 -0.0035 318  LEU B C   
6268 O  O   . LEU B 319 ? 0.1086 0.1743 0.1362 -0.0071 -0.0005 -0.0034 318  LEU B O   
6269 C  CB  . LEU B 319 ? 0.1877 0.1720 0.0985 -0.0149 -0.0085 0.0058  318  LEU B CB  
6270 C  CG  . LEU B 319 ? 0.1917 0.1503 0.1040 -0.0022 0.0152  -0.0126 318  LEU B CG  
6271 C  CD1 . LEU B 319 ? 0.2556 0.1432 0.1159 -0.0414 0.0559  0.0301  318  LEU B CD1 
6272 C  CD2 . LEU B 319 ? 0.2003 0.1538 0.0962 -0.0047 -0.0270 -0.0480 318  LEU B CD2 
6273 N  N   . ASN B 320 ? 0.1064 0.1750 0.1153 -0.0124 -0.0342 -0.0037 319  ASN B N   
6274 C  CA  . ASN B 320 ? 0.1601 0.1421 0.1273 -0.0238 -0.0278 -0.0141 319  ASN B CA  
6275 C  C   . ASN B 320 ? 0.1524 0.1381 0.1297 0.0041  -0.0087 -0.0014 319  ASN B C   
6276 O  O   . ASN B 320 ? 0.1719 0.1438 0.1165 0.0296  0.0289  0.0126  319  ASN B O   
6277 C  CB  . ASN B 320 ? 0.1520 0.1739 0.1600 -0.0696 -0.0368 -0.0462 319  ASN B CB  
6278 C  CG  . ASN B 320 ? 0.2226 0.2178 0.2213 -0.0657 -0.0304 -0.0407 319  ASN B CG  
6279 O  OD1 . ASN B 320 ? 0.2023 0.2473 0.2277 -0.0747 0.0160  -0.0016 319  ASN B OD1 
6280 N  ND2 . ASN B 320 ? 0.2886 0.2392 0.2542 -0.0469 -0.0512 -0.0320 319  ASN B ND2 
6281 N  N   . GLU B 321 ? 0.1275 0.1551 0.1169 0.0204  0.0207  -0.0069 320  GLU B N   
6282 C  CA  . GLU B 321 ? 0.0826 0.1368 0.1436 0.0154  0.0237  0.0009  320  GLU B CA  
6283 C  C   . GLU B 321 ? 0.1867 0.1571 0.1449 0.0145  0.0158  -0.0138 320  GLU B C   
6284 O  O   . GLU B 321 ? 0.1834 0.0836 0.1742 -0.0091 0.0320  -0.0147 320  GLU B O   
6285 C  CB  . GLU B 321 ? 0.1603 0.1530 0.1230 0.0234  0.0199  0.0017  320  GLU B CB  
6286 C  CG  . GLU B 321 ? 0.1464 0.1735 0.1195 0.0148  0.0155  -0.0144 320  GLU B CG  
6287 C  CD  . GLU B 321 ? 0.1158 0.1657 0.1393 0.0044  0.0133  -0.0195 320  GLU B CD  
6288 O  OE1 . GLU B 321 ? 0.1546 0.1652 0.1263 0.0062  -0.0165 -0.0140 320  GLU B OE1 
6289 O  OE2 . GLU B 321 ? 0.1581 0.1799 0.1417 -0.0470 0.0379  -0.0059 320  GLU B OE2 
6290 N  N   . ALA B 322 ? 0.1429 0.1852 0.1268 -0.0109 -0.0258 -0.0407 321  ALA B N   
6291 C  CA  . ALA B 322 ? 0.1507 0.1422 0.1033 -0.0314 -0.0102 -0.0301 321  ALA B CA  
6292 C  C   . ALA B 322 ? 0.1412 0.1521 0.1278 0.0240  -0.0145 -0.0308 321  ALA B C   
6293 O  O   . ALA B 322 ? 0.1583 0.1725 0.1624 0.0383  -0.0334 -0.0013 321  ALA B O   
6294 C  CB  . ALA B 322 ? 0.1518 0.1406 0.1003 0.0075  -0.0187 -0.0327 321  ALA B CB  
6295 N  N   . LEU B 323 ? 0.1004 0.1698 0.1306 -0.0190 -0.0203 -0.0106 322  LEU B N   
6296 C  CA  . LEU B 323 ? 0.0562 0.1703 0.1292 -0.0297 0.0158  0.0132  322  LEU B CA  
6297 C  C   . LEU B 323 ? 0.1099 0.1806 0.1129 0.0310  0.0004  0.0071  322  LEU B C   
6298 O  O   . LEU B 323 ? 0.1591 0.2083 0.1413 0.0409  0.0001  0.0229  322  LEU B O   
6299 C  CB  . LEU B 323 ? 0.0839 0.1943 0.1441 -0.0250 0.0505  0.0117  322  LEU B CB  
6300 C  CG  . LEU B 323 ? 0.0828 0.1811 0.1462 -0.0029 0.0604  0.0045  322  LEU B CG  
6301 C  CD1 . LEU B 323 ? 0.0837 0.2053 0.1872 -0.0414 0.0253  0.0409  322  LEU B CD1 
6302 C  CD2 . LEU B 323 ? 0.1135 0.2094 0.1526 0.0592  0.0497  -0.0065 322  LEU B CD2 
6303 N  N   . ARG B 324 ? 0.1206 0.1941 0.0887 -0.0198 0.0141  -0.0032 323  ARG B N   
6304 C  CA  . ARG B 324 ? 0.1244 0.1806 0.0982 -0.0171 0.0174  -0.0430 323  ARG B CA  
6305 C  C   . ARG B 324 ? 0.1261 0.1817 0.1277 -0.0103 0.0088  -0.0227 323  ARG B C   
6306 O  O   . ARG B 324 ? 0.1573 0.2109 0.1134 0.0105  -0.0215 -0.0180 323  ARG B O   
6307 C  CB  . ARG B 324 ? 0.1570 0.2074 0.0905 -0.0034 0.0493  -0.0306 323  ARG B CB  
6308 C  CG  . ARG B 324 ? 0.0864 0.1855 0.0978 0.0193  0.0201  0.0028  323  ARG B CG  
6309 C  CD  . ARG B 324 ? 0.0842 0.1710 0.1180 0.0290  0.0446  -0.0155 323  ARG B CD  
6310 N  NE  . ARG B 324 ? 0.0778 0.1718 0.1493 0.0223  0.0426  -0.0224 323  ARG B NE  
6311 C  CZ  . ARG B 324 ? 0.0876 0.1916 0.1421 -0.0393 -0.0087 -0.0069 323  ARG B CZ  
6312 N  NH1 . ARG B 324 ? 0.1798 0.1682 0.1644 -0.0067 0.0210  -0.0058 323  ARG B NH1 
6313 N  NH2 . ARG B 324 ? 0.1193 0.1790 0.1289 -0.0089 -0.0231 -0.0176 323  ARG B NH2 
6314 N  N   . LEU B 325 ? 0.1518 0.1761 0.1356 -0.0104 -0.0157 -0.0255 324  LEU B N   
6315 C  CA  . LEU B 325 ? 0.1006 0.1881 0.1395 -0.0056 0.0066  -0.0293 324  LEU B CA  
6316 C  C   . LEU B 325 ? 0.1589 0.1775 0.1344 0.0027  0.0365  0.0003  324  LEU B C   
6317 O  O   . LEU B 325 ? 0.1417 0.1900 0.1435 0.0107  0.0368  0.0249  324  LEU B O   
6318 C  CB  . LEU B 325 ? 0.0839 0.2033 0.1467 0.0560  -0.0018 -0.0248 324  LEU B CB  
6319 C  CG  . LEU B 325 ? 0.1467 0.1839 0.1625 0.0771  0.0001  0.0188  324  LEU B CG  
6320 C  CD1 . LEU B 325 ? 0.1657 0.2145 0.2094 0.0512  -0.0023 0.0289  324  LEU B CD1 
6321 C  CD2 . LEU B 325 ? 0.1946 0.1797 0.1579 0.0351  0.0313  0.0290  324  LEU B CD2 
6322 N  N   . TRP B 326 ? 0.1039 0.1783 0.1271 -0.0029 -0.0033 -0.0219 325  TRP B N   
6323 C  CA  . TRP B 326 ? 0.1271 0.1630 0.1204 0.0025  -0.0423 -0.0378 325  TRP B CA  
6324 C  C   . TRP B 326 ? 0.1473 0.1702 0.1215 0.0048  -0.0375 -0.0246 325  TRP B C   
6325 O  O   . TRP B 326 ? 0.1482 0.2202 0.1411 -0.0366 -0.0049 -0.0190 325  TRP B O   
6326 C  CB  . TRP B 326 ? 0.1642 0.1642 0.1150 -0.0383 -0.0252 -0.0147 325  TRP B CB  
6327 C  CG  . TRP B 326 ? 0.1275 0.1607 0.1487 -0.0167 -0.0548 -0.0291 325  TRP B CG  
6328 C  CD1 . TRP B 326 ? 0.2085 0.1521 0.1566 -0.0062 -0.0398 -0.0394 325  TRP B CD1 
6329 C  CD2 . TRP B 326 ? 0.1913 0.1411 0.1804 0.0010  -0.0134 -0.0132 325  TRP B CD2 
6330 N  NE1 . TRP B 326 ? 0.1638 0.1088 0.1819 -0.0158 -0.0167 -0.0084 325  TRP B NE1 
6331 C  CE2 . TRP B 326 ? 0.2037 0.1237 0.1831 -0.0210 -0.0014 -0.0136 325  TRP B CE2 
6332 C  CE3 . TRP B 326 ? 0.1545 0.1381 0.1731 -0.0267 -0.0146 0.0115  325  TRP B CE3 
6333 C  CZ2 . TRP B 326 ? 0.2393 0.1251 0.1727 -0.0026 -0.0302 -0.0060 325  TRP B CZ2 
6334 C  CZ3 . TRP B 326 ? 0.2126 0.1201 0.2022 -0.0542 0.0055  0.0023  325  TRP B CZ3 
6335 C  CH2 . TRP B 326 ? 0.2243 0.1426 0.1938 -0.0361 -0.0058 0.0111  325  TRP B CH2 
6336 N  N   . PRO B 327 ? 0.1764 0.1893 0.1262 0.0368  0.0127  -0.0023 326  PRO B N   
6337 C  CA  . PRO B 327 ? 0.1004 0.1741 0.1257 0.0037  0.0011  -0.0241 326  PRO B CA  
6338 C  C   . PRO B 327 ? 0.1364 0.1565 0.1187 0.0141  -0.0120 -0.0289 326  PRO B C   
6339 O  O   . PRO B 327 ? 0.1512 0.1503 0.1604 0.0189  0.0137  -0.0010 326  PRO B O   
6340 C  CB  . PRO B 327 ? 0.1329 0.1784 0.1219 -0.0431 -0.0097 -0.0200 326  PRO B CB  
6341 C  CG  . PRO B 327 ? 0.0674 0.1789 0.1252 0.0318  -0.0009 0.0161  326  PRO B CG  
6342 C  CD  . PRO B 327 ? 0.0911 0.1852 0.1073 0.0389  -0.0242 -0.0069 326  PRO B CD  
6343 N  N   . THR B 328 ? 0.1622 0.1373 0.0682 0.0399  -0.0073 -0.0203 327  THR B N   
6344 C  CA  . THR B 328 ? 0.0979 0.1440 0.0830 0.0254  0.0169  -0.0062 327  THR B CA  
6345 C  C   . THR B 328 ? 0.0948 0.1529 0.1006 -0.0065 -0.0168 -0.0019 327  THR B C   
6346 O  O   . THR B 328 ? 0.2032 0.1905 0.1160 -0.0066 -0.0261 -0.0184 327  THR B O   
6347 C  CB  . THR B 328 ? 0.1109 0.1349 0.1093 -0.0404 -0.0090 0.0233  327  THR B CB  
6348 O  OG1 . THR B 328 ? 0.1371 0.1622 0.1540 -0.0397 -0.0116 -0.0262 327  THR B OG1 
6349 C  CG2 . THR B 328 ? 0.1485 0.1113 0.1171 -0.0128 -0.0349 0.0134  327  THR B CG2 
6350 N  N   . ALA B 329 ? 0.0774 0.1521 0.1270 0.0004  -0.0502 -0.0026 328  ALA B N   
6351 C  CA  . ALA B 329 ? 0.0531 0.1802 0.1409 -0.0146 0.0228  0.0075  328  ALA B CA  
6352 C  C   . ALA B 329 ? 0.1405 0.1815 0.1093 -0.0427 0.0319  -0.0111 328  ALA B C   
6353 O  O   . ALA B 329 ? 0.2244 0.2177 0.1071 -0.0137 -0.0003 0.0011  328  ALA B O   
6354 C  CB  . ALA B 329 ? 0.1121 0.1940 0.1508 -0.0179 0.0114  0.0056  328  ALA B CB  
6355 N  N   . PRO B 330 ? 0.1631 0.1638 0.1262 -0.0009 0.0131  -0.0585 329  PRO B N   
6356 C  CA  . PRO B 330 ? 0.1605 0.1603 0.1262 -0.0213 -0.0119 -0.0346 329  PRO B CA  
6357 C  C   . PRO B 330 ? 0.1394 0.1575 0.1451 0.0205  -0.0111 -0.0166 329  PRO B C   
6358 O  O   . PRO B 330 ? 0.1553 0.1624 0.1282 0.0050  -0.0181 0.0031  329  PRO B O   
6359 C  CB  . PRO B 330 ? 0.1109 0.1912 0.1586 -0.0461 -0.0047 -0.0585 329  PRO B CB  
6360 C  CG  . PRO B 330 ? 0.1688 0.1694 0.1722 -0.0018 0.0348  -0.0473 329  PRO B CG  
6361 C  CD  . PRO B 330 ? 0.1493 0.1486 0.1541 0.0031  0.0136  -0.0491 329  PRO B CD  
6362 N  N   . ALA B 331 ? 0.1351 0.1446 0.1505 0.0325  -0.0279 0.0050  330  ALA B N   
6363 C  CA  . ALA B 331 ? 0.0931 0.1074 0.1426 0.0119  -0.0313 0.0418  330  ALA B CA  
6364 C  C   . ALA B 331 ? 0.1485 0.1555 0.1262 0.0304  -0.0252 0.0172  330  ALA B C   
6365 O  O   . ALA B 331 ? 0.2225 0.1779 0.1040 0.0175  -0.0156 0.0321  330  ALA B O   
6366 C  CB  . ALA B 331 ? 0.1113 0.0997 0.1570 -0.0021 -0.0180 0.0315  330  ALA B CB  
6367 N  N   . PHE B 332 ? 0.0711 0.1767 0.1360 -0.0153 0.0029  -0.0266 331  PHE B N   
6368 C  CA  . PHE B 332 ? 0.1013 0.1593 0.1564 -0.0001 -0.0408 0.0118  331  PHE B CA  
6369 C  C   . PHE B 332 ? 0.1746 0.2107 0.1776 0.0019  -0.0832 0.0033  331  PHE B C   
6370 O  O   . PHE B 332 ? 0.1971 0.2012 0.1915 0.0295  -0.0598 0.0491  331  PHE B O   
6371 C  CB  . PHE B 332 ? 0.1780 0.1434 0.1594 0.0294  0.0089  0.0224  331  PHE B CB  
6372 C  CG  . PHE B 332 ? 0.1474 0.1412 0.1716 0.0368  -0.0028 0.0418  331  PHE B CG  
6373 C  CD1 . PHE B 332 ? 0.1509 0.1645 0.1850 0.0466  0.0185  0.0092  331  PHE B CD1 
6374 C  CD2 . PHE B 332 ? 0.1704 0.1510 0.1833 0.0092  -0.0199 0.0251  331  PHE B CD2 
6375 C  CE1 . PHE B 332 ? 0.2385 0.1747 0.1486 -0.0035 -0.0104 0.0029  331  PHE B CE1 
6376 C  CE2 . PHE B 332 ? 0.1960 0.1842 0.1879 -0.0198 -0.0242 -0.0178 331  PHE B CE2 
6377 C  CZ  . PHE B 332 ? 0.2130 0.1731 0.1709 -0.0249 -0.0088 -0.0224 331  PHE B CZ  
6378 N  N   . SER B 333 ? 0.1182 0.1831 0.1897 0.0296  -0.0472 0.0092  332  SER B N   
6379 C  CA  . SER B 333 ? 0.0933 0.1647 0.1837 0.0431  -0.0452 0.0285  332  SER B CA  
6380 C  C   . SER B 333 ? 0.1031 0.1523 0.1530 -0.0050 -0.0299 0.0216  332  SER B C   
6381 O  O   . SER B 333 ? 0.1474 0.1460 0.1395 -0.0087 -0.0103 0.0157  332  SER B O   
6382 C  CB  . SER B 333 ? 0.1293 0.1435 0.1958 0.0405  -0.0286 0.0477  332  SER B CB  
6383 O  OG  . SER B 333 ? 0.1345 0.1709 0.2547 0.0033  -0.0171 0.0718  332  SER B OG  
6384 N  N   . LEU B 334 ? 0.1496 0.1912 0.1476 -0.0012 -0.0338 0.0256  333  LEU B N   
6385 C  CA  . LEU B 334 ? 0.1163 0.1603 0.1540 0.0179  0.0034  0.0188  333  LEU B CA  
6386 C  C   . LEU B 334 ? 0.0749 0.1994 0.1537 0.0348  -0.0377 0.0003  333  LEU B C   
6387 O  O   . LEU B 334 ? 0.1910 0.2336 0.1464 -0.0031 -0.0525 -0.0164 333  LEU B O   
6388 C  CB  . LEU B 334 ? 0.1852 0.1740 0.1875 0.0420  -0.0059 0.0459  333  LEU B CB  
6389 C  CG  . LEU B 334 ? 0.2735 0.1497 0.1967 0.0501  0.0232  0.0375  333  LEU B CG  
6390 C  CD1 . LEU B 334 ? 0.3556 0.2108 0.2067 0.0514  0.0132  0.0287  333  LEU B CD1 
6391 C  CD2 . LEU B 334 ? 0.1382 0.1497 0.1709 -0.0246 -0.0139 0.0214  333  LEU B CD2 
6392 N  N   . TYR B 335 ? 0.1486 0.2000 0.1595 0.0519  -0.0782 0.0001  334  TYR B N   
6393 C  CA  . TYR B 335 ? 0.1508 0.2219 0.1431 0.0180  -0.0251 0.0019  334  TYR B CA  
6394 C  C   . TYR B 335 ? 0.1773 0.2239 0.1453 -0.0175 -0.0279 0.0086  334  TYR B C   
6395 O  O   . TYR B 335 ? 0.1548 0.2179 0.1462 0.0292  0.0062  0.0048  334  TYR B O   
6396 C  CB  . TYR B 335 ? 0.1226 0.2306 0.1378 0.0254  0.0363  0.0013  334  TYR B CB  
6397 C  CG  . TYR B 335 ? 0.1629 0.2349 0.1643 -0.0116 -0.0098 -0.0029 334  TYR B CG  
6398 C  CD1 . TYR B 335 ? 0.1392 0.2103 0.1599 0.0143  0.0189  0.0007  334  TYR B CD1 
6399 C  CD2 . TYR B 335 ? 0.1747 0.2515 0.1657 0.0224  -0.0219 0.0033  334  TYR B CD2 
6400 C  CE1 . TYR B 335 ? 0.1065 0.2405 0.1920 0.0209  0.0036  0.0233  334  TYR B CE1 
6401 C  CE2 . TYR B 335 ? 0.1735 0.2543 0.1798 -0.0050 -0.0159 0.0403  334  TYR B CE2 
6402 C  CZ  . TYR B 335 ? 0.1615 0.2593 0.2098 -0.0123 0.0000  0.0419  334  TYR B CZ  
6403 O  OH  . TYR B 335 ? 0.2066 0.2809 0.2351 -0.0294 -0.0300 0.0486  334  TYR B OH  
6404 N  N   . ALA B 336 ? 0.1942 0.2362 0.1074 -0.0467 -0.0435 0.0113  335  ALA B N   
6405 C  CA  . ALA B 336 ? 0.2221 0.2805 0.1124 -0.0607 0.0022  0.0307  335  ALA B CA  
6406 C  C   . ALA B 336 ? 0.1949 0.2808 0.1579 0.0110  0.0055  0.0365  335  ALA B C   
6407 O  O   . ALA B 336 ? 0.1205 0.3041 0.1804 -0.0067 -0.0202 0.0418  335  ALA B O   
6408 C  CB  . ALA B 336 ? 0.1640 0.3258 0.1271 -0.0940 0.0083  0.0370  335  ALA B CB  
6409 N  N   . LYS B 337 ? 0.1573 0.2371 0.1714 -0.0048 -0.0033 0.0450  336  LYS B N   
6410 C  CA  . LYS B 337 ? 0.1715 0.2748 0.1898 -0.0071 -0.0290 0.0646  336  LYS B CA  
6411 C  C   . LYS B 337 ? 0.2241 0.3067 0.2107 -0.0034 -0.0312 0.0453  336  LYS B C   
6412 O  O   . LYS B 337 ? 0.2463 0.3209 0.2424 0.0368  -0.0217 0.0211  336  LYS B O   
6413 C  CB  . LYS B 337 ? 0.1948 0.2795 0.1870 -0.0347 -0.0104 0.0724  336  LYS B CB  
6414 C  CG  . LYS B 337 ? 0.2223 0.2890 0.2155 -0.1028 -0.0130 0.0789  336  LYS B CG  
6415 C  CD  . LYS B 337 ? 0.2554 0.3140 0.2466 -0.1232 -0.0630 0.0508  336  LYS B CD  
6416 C  CE  . LYS B 337 ? 0.1882 0.3635 0.3063 -0.1294 -0.0305 0.0441  336  LYS B CE  
6417 N  NZ  . LYS B 337 ? 0.1910 0.3994 0.3161 -0.1326 -0.0366 0.0815  336  LYS B NZ  
6418 N  N   . GLU B 338 ? 0.2366 0.3193 0.1859 -0.0412 -0.0270 0.0421  337  GLU B N   
6419 C  CA  . GLU B 338 ? 0.2266 0.3449 0.1740 -0.0703 -0.0458 0.0451  337  GLU B CA  
6420 C  C   . GLU B 338 ? 0.1923 0.3681 0.1647 -0.0366 -0.0773 0.0514  337  GLU B C   
6421 O  O   . GLU B 338 ? 0.2053 0.3677 0.1652 0.0094  -0.0799 0.0508  337  GLU B O   
6422 C  CB  . GLU B 338 ? 0.2492 0.3773 0.2114 -0.0702 -0.0364 0.0497  337  GLU B CB  
6423 C  CG  . GLU B 338 ? 0.2369 0.4150 0.2725 -0.0803 -0.0746 0.0385  337  GLU B CG  
6424 C  CD  . GLU B 338 ? 0.3079 0.4536 0.3260 -0.0729 -0.0607 0.0361  337  GLU B CD  
6425 O  OE1 . GLU B 338 ? 0.2579 0.4575 0.3319 -0.0058 -0.0717 0.0253  337  GLU B OE1 
6426 O  OE2 . GLU B 338 ? 0.3181 0.4827 0.3575 -0.1023 -0.0690 0.0413  337  GLU B OE2 
6427 N  N   . ASP B 339 ? 0.2725 0.3843 0.1567 -0.0030 -0.0541 0.0486  338  ASP B N   
6428 C  CA  . ASP B 339 ? 0.2124 0.4066 0.1821 0.0264  -0.0144 0.0627  338  ASP B CA  
6429 C  C   . ASP B 339 ? 0.2152 0.4324 0.2041 -0.0076 0.0082  0.0357  338  ASP B C   
6430 O  O   . ASP B 339 ? 0.2582 0.4502 0.2284 -0.0065 -0.0018 0.0186  338  ASP B O   
6431 C  CB  . ASP B 339 ? 0.2459 0.4069 0.1763 0.0031  -0.0654 0.0978  338  ASP B CB  
6432 C  CG  . ASP B 339 ? 0.3123 0.3970 0.2112 0.0230  -0.1001 0.1060  338  ASP B CG  
6433 O  OD1 . ASP B 339 ? 0.2976 0.4095 0.2326 -0.0130 -0.1151 0.1098  338  ASP B OD1 
6434 O  OD2 . ASP B 339 ? 0.3780 0.4291 0.2231 0.0813  -0.0732 0.1058  338  ASP B OD2 
6435 N  N   . THR B 340 ? 0.1952 0.4364 0.1728 -0.0299 -0.0092 0.0367  339  THR B N   
6436 C  CA  . THR B 340 ? 0.2042 0.4161 0.1783 -0.0237 -0.0109 0.0194  339  THR B CA  
6437 C  C   . THR B 340 ? 0.2006 0.4342 0.2042 0.0056  0.0011  -0.0010 339  THR B C   
6438 O  O   . THR B 340 ? 0.2854 0.4399 0.2685 -0.0111 0.0271  0.0091  339  THR B O   
6439 C  CB  . THR B 340 ? 0.2440 0.3963 0.1845 -0.0462 -0.0351 -0.0090 339  THR B CB  
6440 O  OG1 . THR B 340 ? 0.3189 0.3709 0.1957 -0.0127 -0.0013 -0.0095 339  THR B OG1 
6441 C  CG2 . THR B 340 ? 0.2143 0.4136 0.1879 -0.0029 -0.0694 -0.0110 339  THR B CG2 
6442 N  N   . VAL B 341 ? 0.2154 0.4398 0.1635 0.0413  -0.0175 0.0120  340  VAL B N   
6443 C  CA  . VAL B 341 ? 0.2420 0.4319 0.1588 0.0730  -0.0137 0.0215  340  VAL B CA  
6444 C  C   . VAL B 341 ? 0.2615 0.4162 0.1763 0.0042  -0.0358 0.0087  340  VAL B C   
6445 O  O   . VAL B 341 ? 0.2960 0.4331 0.2161 0.0071  -0.0521 -0.0114 340  VAL B O   
6446 C  CB  . VAL B 341 ? 0.2723 0.4674 0.1694 0.0539  0.0312  0.0339  340  VAL B CB  
6447 C  CG1 . VAL B 341 ? 0.3594 0.4810 0.1794 0.0288  0.0627  0.0355  340  VAL B CG1 
6448 C  CG2 . VAL B 341 ? 0.3924 0.4740 0.1513 0.0885  -0.0057 0.0605  340  VAL B CG2 
6449 N  N   . LEU B 342 ? 0.3194 0.3859 0.1412 0.0051  -0.0098 0.0182  341  LEU B N   
6450 C  CA  . LEU B 342 ? 0.3103 0.3669 0.1490 0.0370  -0.0077 0.0015  341  LEU B CA  
6451 C  C   . LEU B 342 ? 0.3704 0.3647 0.1570 0.0543  -0.0254 0.0061  341  LEU B C   
6452 O  O   . LEU B 342 ? 0.3555 0.3726 0.1685 0.0916  -0.0270 0.0116  341  LEU B O   
6453 C  CB  . LEU B 342 ? 0.3603 0.3439 0.1479 0.0080  -0.0060 0.0066  341  LEU B CB  
6454 C  CG  . LEU B 342 ? 0.3072 0.3028 0.1622 0.0011  -0.0394 0.0294  341  LEU B CG  
6455 C  CD1 . LEU B 342 ? 0.3035 0.2909 0.1691 0.0080  -0.0588 0.0199  341  LEU B CD1 
6456 C  CD2 . LEU B 342 ? 0.3407 0.2713 0.1441 -0.0113 -0.0103 0.0098  341  LEU B CD2 
6457 N  N   . GLY B 343 ? 0.3734 0.3463 0.1553 0.0787  -0.0304 0.0145  342  GLY B N   
6458 C  CA  . GLY B 343 ? 0.4001 0.3473 0.1657 0.0284  0.0080  0.0083  342  GLY B CA  
6459 C  C   . GLY B 343 ? 0.3617 0.3498 0.1771 0.0172  0.0012  0.0154  342  GLY B C   
6460 O  O   . GLY B 343 ? 0.3412 0.3535 0.1990 0.0406  0.0078  0.0014  342  GLY B O   
6461 N  N   . GLY B 344 ? 0.2848 0.3213 0.1703 0.0173  -0.0796 0.0272  343  GLY B N   
6462 C  CA  . GLY B 344 ? 0.2727 0.3452 0.1834 0.0039  -0.0389 0.0265  343  GLY B CA  
6463 C  C   . GLY B 344 ? 0.3203 0.3842 0.1861 -0.0074 -0.0092 0.0275  343  GLY B C   
6464 O  O   . GLY B 344 ? 0.4381 0.4111 0.2063 -0.0138 -0.0093 0.0209  343  GLY B O   
6465 N  N   . GLU B 345 ? 0.2621 0.3859 0.2070 -0.0827 -0.0016 0.0026  344  GLU B N   
6466 C  CA  . GLU B 345 ? 0.2724 0.4121 0.2211 -0.0148 0.0458  -0.0065 344  GLU B CA  
6467 C  C   . GLU B 345 ? 0.3345 0.3656 0.2010 0.0278  0.0340  0.0084  344  GLU B C   
6468 O  O   . GLU B 345 ? 0.3269 0.3535 0.1889 -0.0238 0.0347  0.0022  344  GLU B O   
6469 C  CB  . GLU B 345 ? 0.3149 0.5073 0.2638 -0.0218 0.0601  -0.0290 344  GLU B CB  
6470 C  CG  . GLU B 345 ? 0.3342 0.5854 0.3316 -0.0032 0.0342  -0.0358 344  GLU B CG  
6471 C  CD  . GLU B 345 ? 0.4165 0.6574 0.3700 -0.0318 0.0067  -0.0548 344  GLU B CD  
6472 O  OE1 . GLU B 345 ? 0.4147 0.6510 0.3538 -0.0240 -0.0408 -0.0190 344  GLU B OE1 
6473 O  OE2 . GLU B 345 ? 0.4783 0.7063 0.4309 -0.0490 0.0013  -0.0712 344  GLU B OE2 
6474 N  N   . TYR B 346 ? 0.2812 0.3531 0.1750 0.0358  -0.0021 0.0238  345  TYR B N   
6475 C  CA  . TYR B 346 ? 0.1821 0.3938 0.1582 0.0557  0.0166  0.0433  345  TYR B CA  
6476 C  C   . TYR B 346 ? 0.2163 0.3809 0.1721 0.0106  0.0469  0.0670  345  TYR B C   
6477 O  O   . TYR B 346 ? 0.2661 0.3585 0.1896 -0.0351 0.0547  0.0544  345  TYR B O   
6478 C  CB  . TYR B 346 ? 0.2328 0.4249 0.1796 0.0564  -0.0340 0.0415  345  TYR B CB  
6479 C  CG  . TYR B 346 ? 0.2300 0.4247 0.1796 0.0277  0.0205  0.0348  345  TYR B CG  
6480 C  CD1 . TYR B 346 ? 0.2932 0.4361 0.1870 0.0258  0.0139  0.0175  345  TYR B CD1 
6481 C  CD2 . TYR B 346 ? 0.2805 0.4083 0.1636 0.0118  0.0104  0.0274  345  TYR B CD2 
6482 C  CE1 . TYR B 346 ? 0.2509 0.4489 0.1989 0.0211  0.0139  0.0222  345  TYR B CE1 
6483 C  CE2 . TYR B 346 ? 0.3339 0.4272 0.1634 -0.0006 0.0090  0.0103  345  TYR B CE2 
6484 C  CZ  . TYR B 346 ? 0.3146 0.4640 0.2083 -0.0156 0.0109  0.0057  345  TYR B CZ  
6485 O  OH  . TYR B 346 ? 0.3300 0.4945 0.2344 -0.0577 0.0079  -0.0060 345  TYR B OH  
6486 N  N   . PRO B 347 ? 0.2995 0.3846 0.2065 0.0148  0.0449  0.0817  346  PRO B N   
6487 C  CA  . PRO B 347 ? 0.3028 0.3774 0.2180 0.0084  0.0355  0.0748  346  PRO B CA  
6488 C  C   . PRO B 347 ? 0.2476 0.3623 0.2243 -0.0223 0.0218  0.0839  346  PRO B C   
6489 O  O   . PRO B 347 ? 0.3199 0.3752 0.2603 -0.0509 0.0257  0.0721  346  PRO B O   
6490 C  CB  . PRO B 347 ? 0.3436 0.4007 0.2112 0.0404  0.0527  0.0835  346  PRO B CB  
6491 C  CG  . PRO B 347 ? 0.3957 0.4202 0.2016 0.0042  0.0409  0.1146  346  PRO B CG  
6492 C  CD  . PRO B 347 ? 0.3470 0.4134 0.1739 0.0020  0.0405  0.1220  346  PRO B CD  
6493 N  N   . LEU B 348 ? 0.2345 0.3483 0.2204 -0.0127 0.0004  0.0912  347  LEU B N   
6494 C  CA  . LEU B 348 ? 0.1958 0.3412 0.2003 0.0390  -0.0293 0.0880  347  LEU B CA  
6495 C  C   . LEU B 348 ? 0.2203 0.3588 0.2179 0.0238  -0.0110 0.0786  347  LEU B C   
6496 O  O   . LEU B 348 ? 0.2082 0.3857 0.2213 -0.0030 -0.0335 0.0752  347  LEU B O   
6497 C  CB  . LEU B 348 ? 0.1949 0.3225 0.1982 0.0316  -0.0654 0.0954  347  LEU B CB  
6498 C  CG  . LEU B 348 ? 0.1822 0.3041 0.2024 -0.0364 -0.0611 0.0733  347  LEU B CG  
6499 C  CD1 . LEU B 348 ? 0.1941 0.3045 0.1680 -0.0299 -0.0122 0.0918  347  LEU B CD1 
6500 C  CD2 . LEU B 348 ? 0.1242 0.3065 0.2256 -0.0742 -0.0102 0.0519  347  LEU B CD2 
6501 N  N   . GLU B 349 ? 0.1497 0.3248 0.2304 0.0590  -0.0084 0.0859  348  GLU B N   
6502 C  CA  . GLU B 349 ? 0.1593 0.3330 0.2403 0.0269  -0.0361 0.1076  348  GLU B CA  
6503 C  C   . GLU B 349 ? 0.1115 0.3096 0.2323 0.0302  -0.0474 0.0561  348  GLU B C   
6504 O  O   . GLU B 349 ? 0.1450 0.2961 0.2446 0.0215  -0.0617 0.0573  348  GLU B O   
6505 C  CB  . GLU B 349 ? 0.2669 0.3908 0.2569 0.0275  -0.0424 0.1582  348  GLU B CB  
6506 C  CG  . GLU B 349 ? 0.4980 0.4404 0.2948 0.0093  -0.0020 0.1646  348  GLU B CG  
6507 C  CD  . GLU B 349 ? 0.7418 0.4918 0.3282 -0.0137 0.0135  0.1643  348  GLU B CD  
6508 O  OE1 . GLU B 349 ? 0.8684 0.5028 0.3600 0.0168  0.0664  0.1451  348  GLU B OE1 
6509 O  OE2 . GLU B 349 ? 0.7782 0.5405 0.3646 -0.0490 -0.0520 0.1597  348  GLU B OE2 
6510 N  N   . LYS B 350 ? 0.1443 0.3388 0.2423 0.0311  0.0069  0.0698  349  LYS B N   
6511 C  CA  . LYS B 350 ? 0.1059 0.3601 0.2187 0.0193  0.0126  0.0633  349  LYS B CA  
6512 C  C   . LYS B 350 ? 0.2014 0.3415 0.2279 0.0256  -0.0203 0.0426  349  LYS B C   
6513 O  O   . LYS B 350 ? 0.2119 0.3239 0.2234 0.0219  -0.0297 0.0439  349  LYS B O   
6514 C  CB  . LYS B 350 ? 0.1346 0.3944 0.2507 -0.0277 -0.0079 0.0862  349  LYS B CB  
6515 C  CG  . LYS B 350 ? 0.1140 0.4108 0.2881 -0.0139 -0.0167 0.0699  349  LYS B CG  
6516 C  CD  . LYS B 350 ? 0.1821 0.4105 0.3071 -0.0098 0.0031  0.0661  349  LYS B CD  
6517 C  CE  . LYS B 350 ? 0.2331 0.4324 0.3664 -0.0156 -0.0145 0.0240  349  LYS B CE  
6518 N  NZ  . LYS B 350 ? 0.3685 0.4408 0.3866 -0.0271 -0.0340 0.0034  349  LYS B NZ  
6519 N  N   . GLY B 351 ? 0.1411 0.3161 0.2060 0.0159  -0.0155 0.0454  350  GLY B N   
6520 C  CA  . GLY B 351 ? 0.1355 0.2747 0.2232 -0.0143 -0.0303 0.0300  350  GLY B CA  
6521 C  C   . GLY B 351 ? 0.1254 0.2473 0.2277 -0.0219 -0.0327 0.0296  350  GLY B C   
6522 O  O   . GLY B 351 ? 0.1555 0.2417 0.2391 0.0169  -0.0405 -0.0014 350  GLY B O   
6523 N  N   . ASP B 352 ? 0.1652 0.2421 0.2094 0.0098  0.0369  0.0637  351  ASP B N   
6524 C  CA  . ASP B 352 ? 0.1366 0.2513 0.1956 0.0375  0.0719  0.0840  351  ASP B CA  
6525 C  C   . ASP B 352 ? 0.1590 0.2534 0.2013 -0.0392 0.0077  0.0746  351  ASP B C   
6526 O  O   . ASP B 352 ? 0.2255 0.2307 0.2072 -0.0192 -0.0355 0.0637  351  ASP B O   
6527 C  CB  . ASP B 352 ? 0.1599 0.2724 0.1960 0.0148  0.0738  0.0926  351  ASP B CB  
6528 C  CG  . ASP B 352 ? 0.2035 0.2983 0.2133 0.0233  0.0242  0.0847  351  ASP B CG  
6529 O  OD1 . ASP B 352 ? 0.2341 0.2596 0.2105 0.0356  0.0192  0.0782  351  ASP B OD1 
6530 O  OD2 . ASP B 352 ? 0.2126 0.3265 0.2381 0.0398  0.0120  0.0923  351  ASP B OD2 
6531 N  N   . GLU B 353 ? 0.2170 0.2544 0.1967 -0.0355 -0.0379 0.0587  352  GLU B N   
6532 C  CA  . GLU B 353 ? 0.1627 0.2530 0.1777 -0.0091 -0.0113 0.0302  352  GLU B CA  
6533 C  C   . GLU B 353 ? 0.2138 0.2241 0.1730 -0.0002 -0.0154 0.0512  352  GLU B C   
6534 O  O   . GLU B 353 ? 0.2268 0.2322 0.2055 -0.0121 0.0026  0.0367  352  GLU B O   
6535 C  CB  . GLU B 353 ? 0.2245 0.3250 0.1744 0.1282  -0.0305 -0.0292 352  GLU B CB  
6536 C  CG  . GLU B 353 ? 0.3788 0.3922 0.2502 0.1326  -0.0598 -0.0435 352  GLU B CG  
6537 C  CD  . GLU B 353 ? 0.4822 0.4436 0.3252 0.1680  -0.0740 -0.0596 352  GLU B CD  
6538 O  OE1 . GLU B 353 ? 0.3684 0.4790 0.3278 0.1400  -0.1764 -0.0740 352  GLU B OE1 
6539 O  OE2 . GLU B 353 ? 0.6131 0.4489 0.3747 0.2347  -0.0358 -0.0520 352  GLU B OE2 
6540 N  N   . LEU B 354 ? 0.1718 0.1977 0.1651 0.0441  -0.0529 0.0320  353  LEU B N   
6541 C  CA  . LEU B 354 ? 0.1341 0.2198 0.1565 0.0102  -0.0346 0.0001  353  LEU B CA  
6542 C  C   . LEU B 354 ? 0.1767 0.2167 0.1637 0.0042  -0.0860 -0.0081 353  LEU B C   
6543 O  O   . LEU B 354 ? 0.1906 0.2244 0.1853 0.0138  -0.0380 0.0038  353  LEU B O   
6544 C  CB  . LEU B 354 ? 0.1825 0.2116 0.1560 -0.0157 -0.0595 0.0162  353  LEU B CB  
6545 C  CG  . LEU B 354 ? 0.1976 0.2170 0.1671 -0.0096 -0.0385 0.0211  353  LEU B CG  
6546 C  CD1 . LEU B 354 ? 0.2693 0.2084 0.1962 0.0302  -0.0035 -0.0003 353  LEU B CD1 
6547 C  CD2 . LEU B 354 ? 0.2649 0.2585 0.1651 -0.0269 0.0022  0.0693  353  LEU B CD2 
6548 N  N   . MET B 355 ? 0.1299 0.2046 0.1481 -0.0188 -0.0804 -0.0015 354  MET B N   
6549 C  CA  . MET B 355 ? 0.1212 0.1850 0.1383 -0.0258 -0.0721 0.0212  354  MET B CA  
6550 C  C   . MET B 355 ? 0.1617 0.1840 0.1573 0.0010  -0.0355 0.0493  354  MET B C   
6551 O  O   . MET B 355 ? 0.1958 0.1740 0.1693 -0.0204 0.0178  0.0315  354  MET B O   
6552 C  CB  . MET B 355 ? 0.1326 0.2105 0.1625 -0.0481 -0.0225 0.0002  354  MET B CB  
6553 C  CG  . MET B 355 ? 0.1883 0.2319 0.2061 -0.0392 0.0074  0.0185  354  MET B CG  
6554 S  SD  . MET B 355 ? 0.1946 0.2222 0.2068 -0.0055 0.0280  -0.0198 354  MET B SD  
6555 C  CE  . MET B 355 ? 0.1906 0.2593 0.1875 0.0060  -0.0177 0.0477  354  MET B CE  
6556 N  N   . VAL B 356 ? 0.1637 0.1725 0.1666 0.0484  -0.0213 0.0190  355  VAL B N   
6557 C  CA  . VAL B 356 ? 0.1266 0.1754 0.1617 0.0309  -0.0413 0.0310  355  VAL B CA  
6558 C  C   . VAL B 356 ? 0.0569 0.1483 0.1443 0.0155  0.0339  0.0227  355  VAL B C   
6559 O  O   . VAL B 356 ? 0.1872 0.1839 0.1340 -0.0185 0.0371  0.0232  355  VAL B O   
6560 C  CB  . VAL B 356 ? 0.1208 0.2261 0.1719 0.0230  -0.0442 0.0293  355  VAL B CB  
6561 C  CG1 . VAL B 356 ? 0.1178 0.2295 0.1836 0.0453  -0.0658 0.0243  355  VAL B CG1 
6562 C  CG2 . VAL B 356 ? 0.1424 0.2551 0.1737 -0.0283 -0.0327 -0.0076 355  VAL B CG2 
6563 N  N   . LEU B 357 ? 0.0616 0.1686 0.1578 0.0253  0.0173  0.0062  356  LEU B N   
6564 C  CA  . LEU B 357 ? 0.1250 0.1845 0.1549 -0.0182 0.0209  0.0073  356  LEU B CA  
6565 C  C   . LEU B 357 ? 0.1554 0.1749 0.1425 0.0080  -0.0128 -0.0059 356  LEU B C   
6566 O  O   . LEU B 357 ? 0.1506 0.1641 0.1427 0.0043  0.0081  -0.0082 356  LEU B O   
6567 C  CB  . LEU B 357 ? 0.2698 0.2531 0.1750 -0.1211 0.0569  -0.0036 356  LEU B CB  
6568 C  CG  . LEU B 357 ? 0.3770 0.3022 0.2113 -0.1458 0.1212  -0.0346 356  LEU B CG  
6569 C  CD1 . LEU B 357 ? 0.4179 0.3332 0.2134 -0.1920 0.1217  -0.0858 356  LEU B CD1 
6570 C  CD2 . LEU B 357 ? 0.3904 0.2848 0.2262 -0.1663 0.1182  -0.0451 356  LEU B CD2 
6571 N  N   . ILE B 358 ? 0.1216 0.1718 0.1342 0.0029  -0.0231 -0.0093 357  ILE B N   
6572 C  CA  . ILE B 358 ? 0.1072 0.1341 0.1337 0.0036  0.0144  0.0259  357  ILE B CA  
6573 C  C   . ILE B 358 ? 0.1394 0.1551 0.1372 0.0059  0.0232  -0.0244 357  ILE B C   
6574 O  O   . ILE B 358 ? 0.1480 0.1933 0.1307 0.0065  0.0268  0.0036  357  ILE B O   
6575 C  CB  . ILE B 358 ? 0.0938 0.1141 0.1649 0.0243  0.0469  0.0285  357  ILE B CB  
6576 C  CG1 . ILE B 358 ? 0.1046 0.1236 0.1531 0.0295  0.0667  0.0486  357  ILE B CG1 
6577 C  CG2 . ILE B 358 ? 0.1274 0.1254 0.1570 0.0148  -0.0278 -0.0060 357  ILE B CG2 
6578 C  CD1 . ILE B 358 ? 0.1031 0.1267 0.1632 0.0118  0.0723  0.0232  357  ILE B CD1 
6579 N  N   . PRO B 359 ? 0.1529 0.1747 0.1346 0.0114  0.0039  -0.0252 358  PRO B N   
6580 C  CA  . PRO B 359 ? 0.1337 0.1462 0.1340 -0.0068 0.0257  -0.0018 358  PRO B CA  
6581 C  C   . PRO B 359 ? 0.1013 0.1283 0.1468 0.0214  0.0080  -0.0075 358  PRO B C   
6582 O  O   . PRO B 359 ? 0.1585 0.1302 0.1664 0.0323  0.0288  -0.0059 358  PRO B O   
6583 C  CB  . PRO B 359 ? 0.1011 0.1580 0.1331 0.0003  0.0209  -0.0204 358  PRO B CB  
6584 C  CG  . PRO B 359 ? 0.0993 0.1613 0.1305 -0.0129 0.0297  -0.0315 358  PRO B CG  
6585 C  CD  . PRO B 359 ? 0.1284 0.1856 0.1229 0.0267  -0.0147 -0.0379 358  PRO B CD  
6586 N  N   . GLN B 360 ? 0.2246 0.0953 0.1490 -0.0148 -0.0319 0.0193  359  GLN B N   
6587 C  CA  . GLN B 360 ? 0.2055 0.1553 0.1797 -0.0019 0.0148  0.0509  359  GLN B CA  
6588 C  C   . GLN B 360 ? 0.1145 0.1745 0.1652 -0.0103 -0.0158 0.0497  359  GLN B C   
6589 O  O   . GLN B 360 ? 0.1455 0.1773 0.1451 -0.0077 0.0088  0.0235  359  GLN B O   
6590 C  CB  . GLN B 360 ? 0.1426 0.1503 0.2252 0.0174  0.0197  0.0433  359  GLN B CB  
6591 C  CG  . GLN B 360 ? 0.2101 0.2075 0.2277 -0.0296 -0.0085 0.0309  359  GLN B CG  
6592 C  CD  . GLN B 360 ? 0.2239 0.1868 0.2609 -0.0617 0.0115  0.0065  359  GLN B CD  
6593 O  OE1 . GLN B 360 ? 0.2503 0.1791 0.2908 0.0168  0.0243  -0.0128 359  GLN B OE1 
6594 N  NE2 . GLN B 360 ? 0.2615 0.2124 0.2854 -0.0086 0.0285  -0.0089 359  GLN B NE2 
6595 N  N   . LEU B 361 ? 0.1595 0.1433 0.1693 -0.0065 -0.0032 0.0656  360  LEU B N   
6596 C  CA  . LEU B 361 ? 0.1731 0.1904 0.1522 0.0034  0.0133  0.0399  360  LEU B CA  
6597 C  C   . LEU B 361 ? 0.1197 0.1947 0.1256 0.0256  0.0078  0.0270  360  LEU B C   
6598 O  O   . LEU B 361 ? 0.1417 0.2349 0.1417 -0.0055 0.0397  0.0011  360  LEU B O   
6599 C  CB  . LEU B 361 ? 0.1533 0.1896 0.1327 0.0030  0.0326  0.0552  360  LEU B CB  
6600 C  CG  . LEU B 361 ? 0.1642 0.1850 0.0963 -0.0191 0.0583  0.0372  360  LEU B CG  
6601 C  CD1 . LEU B 361 ? 0.1638 0.1996 0.0812 0.0051  0.0407  0.0394  360  LEU B CD1 
6602 C  CD2 . LEU B 361 ? 0.1381 0.1916 0.1243 -0.0265 0.0626  0.0392  360  LEU B CD2 
6603 N  N   . HIS B 362 ? 0.1545 0.1841 0.1024 0.0177  -0.0073 0.0499  361  HIS B N   
6604 C  CA  . HIS B 362 ? 0.1721 0.2055 0.1071 0.0351  0.0146  0.0217  361  HIS B CA  
6605 C  C   . HIS B 362 ? 0.1823 0.1951 0.1177 -0.0226 0.0442  0.0124  361  HIS B C   
6606 O  O   . HIS B 362 ? 0.2194 0.2020 0.1502 -0.0224 0.0288  -0.0092 361  HIS B O   
6607 C  CB  . HIS B 362 ? 0.1469 0.1868 0.1039 0.0174  -0.0239 0.0014  361  HIS B CB  
6608 C  CG  . HIS B 362 ? 0.1174 0.1744 0.1188 -0.0013 -0.0284 -0.0208 361  HIS B CG  
6609 N  ND1 . HIS B 362 ? 0.1371 0.1857 0.1026 0.0145  0.0050  -0.0286 361  HIS B ND1 
6610 C  CD2 . HIS B 362 ? 0.1946 0.1572 0.1537 -0.0519 -0.0144 -0.0187 361  HIS B CD2 
6611 C  CE1 . HIS B 362 ? 0.1063 0.1435 0.1351 -0.0148 -0.0181 -0.0426 361  HIS B CE1 
6612 N  NE2 . HIS B 362 ? 0.1479 0.1660 0.1467 0.0021  -0.0202 -0.0348 361  HIS B NE2 
6613 N  N   . ARG B 363 ? 0.1313 0.1578 0.1191 -0.0411 0.0489  0.0046  362  ARG B N   
6614 C  CA  . ARG B 363 ? 0.1382 0.1664 0.1301 -0.0179 0.0024  -0.0123 362  ARG B CA  
6615 C  C   . ARG B 363 ? 0.1764 0.1841 0.1577 0.0073  0.0301  -0.0183 362  ARG B C   
6616 O  O   . ARG B 363 ? 0.1253 0.2104 0.1880 0.0210  0.0052  -0.0359 362  ARG B O   
6617 C  CB  . ARG B 363 ? 0.1463 0.1778 0.1194 -0.0103 0.0047  0.0000  362  ARG B CB  
6618 C  CG  . ARG B 363 ? 0.1924 0.1827 0.1162 -0.0048 0.0469  0.0031  362  ARG B CG  
6619 C  CD  . ARG B 363 ? 0.2159 0.1764 0.1137 -0.0389 -0.0100 0.0034  362  ARG B CD  
6620 N  NE  . ARG B 363 ? 0.2134 0.1862 0.1344 -0.0643 0.0109  0.0046  362  ARG B NE  
6621 C  CZ  . ARG B 363 ? 0.1484 0.1529 0.1327 0.0324  -0.0370 0.0319  362  ARG B CZ  
6622 N  NH1 . ARG B 363 ? 0.1162 0.1615 0.1694 0.0121  -0.0039 0.0132  362  ARG B NH1 
6623 N  NH2 . ARG B 363 ? 0.1695 0.1545 0.1475 -0.0137 -0.0132 0.0403  362  ARG B NH2 
6624 N  N   . ASP B 364 ? 0.1840 0.1991 0.1226 0.0061  0.0454  -0.0102 363  ASP B N   
6625 C  CA  . ASP B 364 ? 0.1778 0.1919 0.1137 0.0023  0.0040  -0.0260 363  ASP B CA  
6626 C  C   . ASP B 364 ? 0.1826 0.1732 0.1434 -0.0022 0.0598  -0.0119 363  ASP B C   
6627 O  O   . ASP B 364 ? 0.2111 0.1448 0.1586 0.0047  0.0518  -0.0077 363  ASP B O   
6628 C  CB  . ASP B 364 ? 0.1708 0.2200 0.1097 -0.0270 -0.0059 -0.0108 363  ASP B CB  
6629 C  CG  . ASP B 364 ? 0.2136 0.2208 0.1420 -0.0009 0.0105  0.0137  363  ASP B CG  
6630 O  OD1 . ASP B 364 ? 0.1672 0.2551 0.1602 0.0039  0.0198  0.0369  363  ASP B OD1 
6631 O  OD2 . ASP B 364 ? 0.2755 0.2131 0.1325 0.0094  0.0070  -0.0208 363  ASP B OD2 
6632 N  N   . LYS B 365 ? 0.1737 0.1707 0.1538 0.0350  0.0516  -0.0157 364  LYS B N   
6633 C  CA  . LYS B 365 ? 0.1942 0.2096 0.1754 -0.0088 0.0222  -0.0190 364  LYS B CA  
6634 C  C   . LYS B 365 ? 0.1912 0.2139 0.1745 -0.0052 0.0042  -0.0309 364  LYS B C   
6635 O  O   . LYS B 365 ? 0.2130 0.2064 0.1674 0.0322  0.0332  -0.0083 364  LYS B O   
6636 C  CB  . LYS B 365 ? 0.1736 0.2415 0.2150 -0.0267 -0.0050 -0.0114 364  LYS B CB  
6637 C  CG  . LYS B 365 ? 0.1824 0.2526 0.2701 -0.0766 -0.0005 -0.0237 364  LYS B CG  
6638 C  CD  . LYS B 365 ? 0.2261 0.3286 0.3257 -0.1142 0.0453  -0.0396 364  LYS B CD  
6639 C  CE  . LYS B 365 ? 0.2980 0.3808 0.3778 -0.1874 0.0793  -0.0454 364  LYS B CE  
6640 N  NZ  . LYS B 365 ? 0.4149 0.4221 0.4324 -0.1329 0.1060  -0.0550 364  LYS B NZ  
6641 N  N   . THR B 366 ? 0.2273 0.2275 0.1668 -0.0089 0.0485  -0.0320 365  THR B N   
6642 C  CA  . THR B 366 ? 0.2560 0.2459 0.1667 -0.0361 0.0202  -0.0322 365  THR B CA  
6643 C  C   . THR B 366 ? 0.2178 0.2392 0.1653 -0.0018 0.0597  -0.0294 365  THR B C   
6644 O  O   . THR B 366 ? 0.2713 0.2469 0.1862 -0.0160 0.0319  -0.0420 365  THR B O   
6645 C  CB  . THR B 366 ? 0.2287 0.2853 0.1748 -0.0265 0.0240  -0.0250 365  THR B CB  
6646 O  OG1 . THR B 366 ? 0.2929 0.3285 0.1800 0.0590  0.0018  0.0010  365  THR B OG1 
6647 C  CG2 . THR B 366 ? 0.2944 0.2972 0.1977 -0.0380 0.0372  -0.0519 365  THR B CG2 
6648 N  N   . ILE B 367 ? 0.2056 0.2482 0.1527 -0.0012 0.0864  -0.0126 366  ILE B N   
6649 C  CA  . ILE B 367 ? 0.1799 0.2279 0.1644 0.0308  0.0267  -0.0062 366  ILE B CA  
6650 C  C   . ILE B 367 ? 0.2019 0.2430 0.1766 0.0374  0.0309  -0.0204 366  ILE B C   
6651 O  O   . ILE B 367 ? 0.3037 0.2581 0.1720 0.0453  0.0432  -0.0499 366  ILE B O   
6652 C  CB  . ILE B 367 ? 0.1772 0.2266 0.1521 0.0112  0.0397  0.0087  366  ILE B CB  
6653 C  CG1 . ILE B 367 ? 0.1336 0.2245 0.1809 -0.0310 -0.0362 -0.0312 366  ILE B CG1 
6654 C  CG2 . ILE B 367 ? 0.2154 0.2339 0.1687 0.0587  -0.0137 0.0051  366  ILE B CG2 
6655 C  CD1 . ILE B 367 ? 0.2248 0.2405 0.1739 -0.0234 -0.0672 -0.0567 366  ILE B CD1 
6656 N  N   . TRP B 368 ? 0.1504 0.2683 0.1544 0.0289  0.0197  -0.0225 367  TRP B N   
6657 C  CA  . TRP B 368 ? 0.2060 0.2457 0.1644 0.0327  0.0530  -0.0184 367  TRP B CA  
6658 C  C   . TRP B 368 ? 0.3056 0.2695 0.1868 0.0281  0.0470  -0.0117 367  TRP B C   
6659 O  O   . TRP B 368 ? 0.3217 0.2958 0.2155 0.0482  0.0574  0.0004  367  TRP B O   
6660 C  CB  . TRP B 368 ? 0.1883 0.2166 0.1797 0.0140  0.0684  -0.0151 367  TRP B CB  
6661 C  CG  . TRP B 368 ? 0.1477 0.1989 0.1683 0.0311  0.0688  0.0165  367  TRP B CG  
6662 C  CD1 . TRP B 368 ? 0.1811 0.1977 0.1505 -0.0045 0.0543  -0.0042 367  TRP B CD1 
6663 C  CD2 . TRP B 368 ? 0.2198 0.1933 0.1381 -0.0174 0.0229  0.0108  367  TRP B CD2 
6664 N  NE1 . TRP B 368 ? 0.2040 0.1752 0.1285 -0.0101 0.0258  0.0037  367  TRP B NE1 
6665 C  CE2 . TRP B 368 ? 0.2607 0.1740 0.1369 0.0104  -0.0102 -0.0068 367  TRP B CE2 
6666 C  CE3 . TRP B 368 ? 0.2819 0.1785 0.1413 -0.0088 0.0271  -0.0185 367  TRP B CE3 
6667 C  CZ2 . TRP B 368 ? 0.2388 0.1485 0.1335 0.0167  -0.0582 -0.0097 367  TRP B CZ2 
6668 C  CZ3 . TRP B 368 ? 0.2710 0.1368 0.1622 0.0122  -0.0149 0.0006  367  TRP B CZ3 
6669 C  CH2 . TRP B 368 ? 0.2126 0.1477 0.1641 0.0183  -0.0575 0.0036  367  TRP B CH2 
6670 N  N   . GLY B 369 ? 0.2615 0.2844 0.1760 0.0040  0.0693  -0.0285 368  GLY B N   
6671 C  CA  . GLY B 369 ? 0.2211 0.2971 0.1878 0.0378  0.0736  -0.0435 368  GLY B CA  
6672 C  C   . GLY B 369 ? 0.1405 0.3493 0.2028 0.0501  0.0613  -0.0268 368  GLY B C   
6673 O  O   . GLY B 369 ? 0.2455 0.3596 0.2395 0.1242  0.0168  -0.0496 368  GLY B O   
6674 N  N   . ASP B 370 ? 0.1777 0.3987 0.2044 -0.0550 0.0671  -0.0390 369  ASP B N   
6675 C  CA  . ASP B 370 ? 0.3242 0.4154 0.2204 -0.1172 0.0765  -0.0460 369  ASP B CA  
6676 C  C   . ASP B 370 ? 0.3371 0.3762 0.2146 -0.1406 0.0355  -0.0427 369  ASP B C   
6677 O  O   . ASP B 370 ? 0.4836 0.3717 0.2646 -0.1603 0.0202  -0.0170 369  ASP B O   
6678 C  CB  . ASP B 370 ? 0.4769 0.4607 0.2490 -0.1907 0.0591  -0.0654 369  ASP B CB  
6679 C  CG  . ASP B 370 ? 0.7448 0.4807 0.2940 -0.1504 0.0417  -0.0408 369  ASP B CG  
6680 O  OD1 . ASP B 370 ? 0.8124 0.4295 0.3068 -0.1306 0.0175  0.0066  369  ASP B OD1 
6681 O  OD2 . ASP B 370 ? 0.8530 0.5192 0.3324 -0.1431 0.0400  -0.0538 369  ASP B OD2 
6682 N  N   . ASP B 371 ? 0.2499 0.3621 0.1711 -0.0568 0.0289  -0.0043 370  ASP B N   
6683 C  CA  . ASP B 371 ? 0.2571 0.3460 0.2293 0.0007  0.0460  0.0132  370  ASP B CA  
6684 C  C   . ASP B 371 ? 0.2428 0.3124 0.2232 0.0705  0.0500  0.0064  370  ASP B C   
6685 O  O   . ASP B 371 ? 0.2363 0.3025 0.2242 0.0917  0.0303  0.0002  370  ASP B O   
6686 C  CB  . ASP B 371 ? 0.2500 0.3276 0.2614 0.0220  0.0329  0.0246  370  ASP B CB  
6687 C  CG  . ASP B 371 ? 0.3925 0.3460 0.3005 0.0821  0.0162  -0.0025 370  ASP B CG  
6688 O  OD1 . ASP B 371 ? 0.3500 0.3400 0.3081 0.0638  0.0679  -0.0299 370  ASP B OD1 
6689 O  OD2 . ASP B 371 ? 0.4607 0.3791 0.3093 0.0454  -0.0084 0.0174  370  ASP B OD2 
6690 N  N   . VAL B 372 ? 0.2596 0.2742 0.2307 0.0889  0.0170  -0.0012 371  VAL B N   
6691 C  CA  . VAL B 372 ? 0.2168 0.2514 0.2251 0.0609  -0.0459 0.0100  371  VAL B CA  
6692 C  C   . VAL B 372 ? 0.2177 0.2699 0.2216 0.0313  -0.0618 0.0176  371  VAL B C   
6693 O  O   . VAL B 372 ? 0.1770 0.2658 0.2160 0.0063  -0.0088 0.0352  371  VAL B O   
6694 C  CB  . VAL B 372 ? 0.3214 0.2350 0.2638 0.0447  -0.0643 0.0278  371  VAL B CB  
6695 C  CG1 . VAL B 372 ? 0.4841 0.2826 0.2764 0.0042  -0.0619 0.0240  371  VAL B CG1 
6696 C  CG2 . VAL B 372 ? 0.2817 0.2463 0.2983 0.1203  -0.0463 0.0393  371  VAL B CG2 
6697 N  N   . GLU B 373 ? 0.1565 0.2487 0.2275 0.0270  -0.0097 -0.0039 372  GLU B N   
6698 C  CA  . GLU B 373 ? 0.1052 0.2259 0.2490 -0.0018 -0.0600 -0.0051 372  GLU B CA  
6699 C  C   . GLU B 373 ? 0.1401 0.1978 0.2394 0.0080  -0.0307 0.0023  372  GLU B C   
6700 O  O   . GLU B 373 ? 0.1982 0.1980 0.2424 -0.0050 -0.0167 0.0104  372  GLU B O   
6701 C  CB  . GLU B 373 ? 0.1573 0.2185 0.2856 0.0130  -0.0454 0.0024  372  GLU B CB  
6702 C  CG  . GLU B 373 ? 0.1882 0.2463 0.3306 0.0007  0.0055  0.0237  372  GLU B CG  
6703 C  CD  . GLU B 373 ? 0.2744 0.2723 0.3802 0.0252  0.0129  -0.0061 372  GLU B CD  
6704 O  OE1 . GLU B 373 ? 0.3396 0.2904 0.3932 0.0284  0.1042  -0.0121 372  GLU B OE1 
6705 O  OE2 . GLU B 373 ? 0.2194 0.3032 0.4250 0.0155  0.0049  -0.0302 372  GLU B OE2 
6706 N  N   . GLU B 374 ? 0.1731 0.1851 0.2309 0.0739  -0.0112 0.0056  373  GLU B N   
6707 C  CA  . GLU B 374 ? 0.1326 0.1902 0.2205 0.0403  0.0446  0.0106  373  GLU B CA  
6708 C  C   . GLU B 374 ? 0.2121 0.1954 0.1668 0.0094  0.0333  -0.0032 373  GLU B C   
6709 O  O   . GLU B 374 ? 0.1931 0.1660 0.1686 -0.0121 0.0438  0.0146  373  GLU B O   
6710 C  CB  . GLU B 374 ? 0.2063 0.2373 0.2678 0.0483  0.1109  -0.0038 373  GLU B CB  
6711 C  CG  . GLU B 374 ? 0.1765 0.2913 0.3013 0.0232  0.1262  -0.0093 373  GLU B CG  
6712 C  CD  . GLU B 374 ? 0.2805 0.3011 0.3864 -0.0576 0.1323  -0.0204 373  GLU B CD  
6713 O  OE1 . GLU B 374 ? 0.2731 0.3063 0.3696 -0.0265 0.0921  -0.0495 373  GLU B OE1 
6714 O  OE2 . GLU B 374 ? 0.3424 0.3152 0.4453 -0.0890 0.0954  -0.0355 373  GLU B OE2 
6715 N  N   . PHE B 375 ? 0.1926 0.1745 0.1244 -0.0087 0.0089  0.0105  374  PHE B N   
6716 C  CA  . PHE B 375 ? 0.1743 0.1724 0.0901 0.0179  0.0098  -0.0076 374  PHE B CA  
6717 C  C   . PHE B 375 ? 0.2250 0.1861 0.1171 0.0337  0.0077  -0.0256 374  PHE B C   
6718 O  O   . PHE B 375 ? 0.1578 0.2002 0.1457 0.0446  0.0027  -0.0285 374  PHE B O   
6719 C  CB  . PHE B 375 ? 0.1399 0.1998 0.1076 0.0075  0.0277  -0.0100 374  PHE B CB  
6720 C  CG  . PHE B 375 ? 0.0751 0.2095 0.1153 -0.0112 0.0161  0.0051  374  PHE B CG  
6721 C  CD1 . PHE B 375 ? 0.0810 0.2092 0.1093 0.0410  0.0193  -0.0254 374  PHE B CD1 
6722 C  CD2 . PHE B 375 ? 0.1455 0.2258 0.1225 -0.0235 0.0142  -0.0282 374  PHE B CD2 
6723 C  CE1 . PHE B 375 ? 0.1268 0.2442 0.0839 0.0277  -0.0007 -0.0284 374  PHE B CE1 
6724 C  CE2 . PHE B 375 ? 0.1436 0.1962 0.1417 0.0573  0.0421  -0.0486 374  PHE B CE2 
6725 C  CZ  . PHE B 375 ? 0.1980 0.2101 0.1217 0.0583  0.0349  -0.0414 374  PHE B CZ  
6726 N  N   . ARG B 376 ? 0.2054 0.1818 0.1339 0.0009  0.0116  -0.0430 375  ARG B N   
6727 C  CA  . ARG B 376 ? 0.1601 0.1733 0.1250 0.0111  0.0533  -0.0070 375  ARG B CA  
6728 C  C   . ARG B 376 ? 0.1778 0.1963 0.1096 0.0202  0.0263  -0.0063 375  ARG B C   
6729 O  O   . ARG B 376 ? 0.1811 0.2006 0.1262 -0.0101 -0.0323 -0.0100 375  ARG B O   
6730 C  CB  . ARG B 376 ? 0.1389 0.2190 0.1342 -0.0447 0.0525  0.0413  375  ARG B CB  
6731 C  CG  . ARG B 376 ? 0.2274 0.2364 0.1830 -0.0711 0.0970  0.0034  375  ARG B CG  
6732 C  CD  . ARG B 376 ? 0.2046 0.2834 0.2447 -0.0381 0.0886  0.0356  375  ARG B CD  
6733 N  NE  . ARG B 376 ? 0.2722 0.3186 0.2873 0.0042  0.0676  0.0087  375  ARG B NE  
6734 C  CZ  . ARG B 376 ? 0.2887 0.3336 0.2983 -0.0214 0.1017  -0.0262 375  ARG B CZ  
6735 N  NH1 . ARG B 376 ? 0.2997 0.2971 0.2542 -0.0377 0.0863  -0.0509 375  ARG B NH1 
6736 N  NH2 . ARG B 376 ? 0.2739 0.3479 0.3230 -0.0251 0.1290  -0.0360 375  ARG B NH2 
6737 N  N   . PRO B 377 ? 0.1853 0.2006 0.0837 -0.0268 0.0366  -0.0262 376  PRO B N   
6738 C  CA  . PRO B 377 ? 0.1561 0.1801 0.0852 -0.0295 0.0293  -0.0488 376  PRO B CA  
6739 C  C   . PRO B 377 ? 0.2012 0.1807 0.1154 -0.0642 0.0289  -0.0324 376  PRO B C   
6740 O  O   . PRO B 377 ? 0.1924 0.1798 0.1343 -0.0152 0.0008  -0.0469 376  PRO B O   
6741 C  CB  . PRO B 377 ? 0.1518 0.1816 0.0701 -0.0307 -0.0088 -0.0426 376  PRO B CB  
6742 C  CG  . PRO B 377 ? 0.1729 0.2213 0.0922 0.0000  -0.0105 -0.0072 376  PRO B CG  
6743 C  CD  . PRO B 377 ? 0.1994 0.2310 0.0737 0.0104  0.0289  -0.0160 376  PRO B CD  
6744 N  N   . GLU B 378 ? 0.2169 0.1669 0.1238 -0.0186 0.0163  -0.0455 377  GLU B N   
6745 C  CA  . GLU B 378 ? 0.1758 0.1855 0.1478 -0.0347 0.0195  -0.0232 377  GLU B CA  
6746 C  C   . GLU B 378 ? 0.2524 0.1766 0.1411 0.0032  0.0153  -0.0232 377  GLU B C   
6747 O  O   . GLU B 378 ? 0.3043 0.1900 0.1606 0.0032  -0.0248 -0.0325 377  GLU B O   
6748 C  CB  . GLU B 378 ? 0.0725 0.2137 0.1714 -0.0162 0.0030  -0.0348 377  GLU B CB  
6749 C  CG  . GLU B 378 ? 0.1295 0.1951 0.1754 0.0056  -0.0221 -0.0360 377  GLU B CG  
6750 C  CD  . GLU B 378 ? 0.2058 0.1947 0.1471 0.0227  -0.0065 0.0041  377  GLU B CD  
6751 O  OE1 . GLU B 378 ? 0.1889 0.1962 0.1575 0.0332  0.0172  -0.0099 377  GLU B OE1 
6752 O  OE2 . GLU B 378 ? 0.1820 0.1900 0.1662 -0.0075 0.0146  0.0050  377  GLU B OE2 
6753 N  N   . ARG B 379 ? 0.2537 0.1353 0.1319 -0.0146 -0.0456 0.0127  378  ARG B N   
6754 C  CA  . ARG B 379 ? 0.3089 0.1501 0.1435 -0.0203 -0.0563 0.0063  378  ARG B CA  
6755 C  C   . ARG B 379 ? 0.2443 0.1993 0.1461 -0.0381 -0.0711 -0.0571 378  ARG B C   
6756 O  O   . ARG B 379 ? 0.2109 0.2829 0.1647 -0.0458 -0.0710 -0.0532 378  ARG B O   
6757 C  CB  . ARG B 379 ? 0.3867 0.1470 0.1793 -0.0483 -0.0360 0.0584  378  ARG B CB  
6758 C  CG  . ARG B 379 ? 0.3899 0.1499 0.1799 -0.0230 -0.0001 0.0640  378  ARG B CG  
6759 C  CD  . ARG B 379 ? 0.3397 0.1403 0.1719 0.0772  0.0163  0.0262  378  ARG B CD  
6760 N  NE  . ARG B 379 ? 0.2969 0.1875 0.1808 0.0561  0.0048  -0.0084 378  ARG B NE  
6761 C  CZ  . ARG B 379 ? 0.2590 0.2339 0.1652 0.0578  0.0283  -0.0063 378  ARG B CZ  
6762 N  NH1 . ARG B 379 ? 0.2993 0.2441 0.1363 0.0525  0.0259  0.0054  378  ARG B NH1 
6763 N  NH2 . ARG B 379 ? 0.1605 0.2357 0.1947 0.0439  -0.0200 -0.0383 378  ARG B NH2 
6764 N  N   . PHE B 380 ? 0.2249 0.1950 0.1555 -0.0431 -0.0052 -0.0344 379  PHE B N   
6765 C  CA  . PHE B 380 ? 0.2377 0.2046 0.1849 0.0158  0.0036  -0.0227 379  PHE B CA  
6766 C  C   . PHE B 380 ? 0.2635 0.2282 0.2241 -0.0086 -0.0195 -0.0155 379  PHE B C   
6767 O  O   . PHE B 380 ? 0.2124 0.2289 0.2339 -0.0018 -0.0079 0.0139  379  PHE B O   
6768 C  CB  . PHE B 380 ? 0.2003 0.2061 0.1922 0.0042  -0.0412 -0.0141 379  PHE B CB  
6769 C  CG  . PHE B 380 ? 0.1031 0.1786 0.1828 -0.0168 -0.0397 -0.0524 379  PHE B CG  
6770 C  CD1 . PHE B 380 ? 0.1629 0.1884 0.1555 -0.0165 -0.0163 -0.0185 379  PHE B CD1 
6771 C  CD2 . PHE B 380 ? 0.1864 0.2158 0.1710 -0.0136 0.0287  -0.0723 379  PHE B CD2 
6772 C  CE1 . PHE B 380 ? 0.1502 0.1832 0.1366 -0.0144 0.0030  -0.0384 379  PHE B CE1 
6773 C  CE2 . PHE B 380 ? 0.1270 0.2330 0.1499 -0.0349 -0.0037 -0.0615 379  PHE B CE2 
6774 C  CZ  . PHE B 380 ? 0.1025 0.2227 0.1359 -0.0436 -0.0267 -0.0494 379  PHE B CZ  
6775 N  N   . GLU B 381 ? 0.2953 0.1991 0.2331 0.0179  -0.0422 -0.0418 380  GLU B N   
6776 C  CA  . GLU B 381 ? 0.3641 0.2239 0.3055 -0.0283 -0.0601 -0.0665 380  GLU B CA  
6777 C  C   . GLU B 381 ? 0.4645 0.2554 0.3170 -0.0487 -0.0921 -0.0666 380  GLU B C   
6778 O  O   . GLU B 381 ? 0.4998 0.2578 0.3376 -0.0932 -0.0702 -0.0439 380  GLU B O   
6779 C  CB  . GLU B 381 ? 0.4007 0.2711 0.3970 0.0073  -0.0260 -0.0835 380  GLU B CB  
6780 C  CG  . GLU B 381 ? 0.5417 0.3304 0.4957 0.0889  0.0307  -0.1017 380  GLU B CG  
6781 C  CD  . GLU B 381 ? 0.6122 0.3787 0.5832 0.1073  0.0129  -0.0855 380  GLU B CD  
6782 O  OE1 . GLU B 381 ? 0.6118 0.4013 0.6117 0.0986  0.0801  -0.0993 380  GLU B OE1 
6783 O  OE2 . GLU B 381 ? 0.6852 0.3991 0.6488 0.1014  -0.0550 -0.0536 380  GLU B OE2 
6784 N  N   . ASN B 382 ? 0.4726 0.3098 0.2845 -0.0423 -0.1321 -0.0918 381  ASN B N   
6785 C  CA  . ASN B 382 ? 0.4713 0.3952 0.3040 -0.0587 -0.1614 -0.1009 381  ASN B CA  
6786 C  C   . ASN B 382 ? 0.4543 0.4033 0.3234 -0.0799 -0.1124 -0.0782 381  ASN B C   
6787 O  O   . ASN B 382 ? 0.4000 0.3410 0.3143 -0.0776 -0.0816 -0.0744 381  ASN B O   
6788 C  CB  . ASN B 382 ? 0.5597 0.4487 0.3021 -0.0655 -0.1506 -0.1182 381  ASN B CB  
6789 C  CG  . ASN B 382 ? 0.7380 0.4703 0.3322 -0.0877 -0.1463 -0.1214 381  ASN B CG  
6790 O  OD1 . ASN B 382 ? 0.7496 0.4744 0.3709 -0.0752 -0.1380 -0.0976 381  ASN B OD1 
6791 N  ND2 . ASN B 382 ? 0.7709 0.4928 0.3117 -0.0753 -0.1409 -0.1237 381  ASN B ND2 
6792 N  N   . PRO B 383 ? 0.4557 0.4562 0.3451 -0.0876 -0.1049 -0.0290 382  PRO B N   
6793 C  CA  . PRO B 383 ? 0.4622 0.4724 0.3666 -0.0430 -0.1067 -0.0132 382  PRO B CA  
6794 C  C   . PRO B 383 ? 0.3983 0.4569 0.3697 -0.0402 -0.1331 -0.0179 382  PRO B C   
6795 O  O   . PRO B 383 ? 0.2912 0.4463 0.4065 -0.0052 -0.1001 -0.0160 382  PRO B O   
6796 C  CB  . PRO B 383 ? 0.5376 0.4774 0.3897 -0.0286 -0.0866 0.0131  382  PRO B CB  
6797 C  CG  . PRO B 383 ? 0.4970 0.4932 0.4023 -0.0737 -0.0708 0.0071  382  PRO B CG  
6798 C  CD  . PRO B 383 ? 0.4463 0.4879 0.3864 -0.0969 -0.1090 -0.0091 382  PRO B CD  
6799 N  N   . SER B 384 ? 0.4576 0.4336 0.3558 -0.1307 -0.1690 -0.0379 383  SER B N   
6800 C  CA  . SER B 384 ? 0.5201 0.4087 0.3580 -0.1171 -0.2075 -0.0434 383  SER B CA  
6801 C  C   . SER B 384 ? 0.5773 0.3444 0.3476 -0.0695 -0.1784 -0.0564 383  SER B C   
6802 O  O   . SER B 384 ? 0.6990 0.3563 0.3348 -0.0800 -0.2007 -0.0580 383  SER B O   
6803 C  CB  . SER B 384 ? 0.5589 0.4183 0.3818 -0.1556 -0.2070 -0.0322 383  SER B CB  
6804 O  OG  . SER B 384 ? 0.7044 0.4717 0.4160 -0.1094 -0.2457 -0.0331 383  SER B OG  
6805 N  N   . ALA B 385 ? 0.5118 0.3111 0.3582 -0.0504 -0.1077 -0.0802 384  ALA B N   
6806 C  CA  . ALA B 385 ? 0.4920 0.3172 0.3618 -0.0257 -0.0007 -0.0641 384  ALA B CA  
6807 C  C   . ALA B 385 ? 0.4902 0.3267 0.3548 -0.0174 0.0528  -0.0612 384  ALA B C   
6808 O  O   . ALA B 385 ? 0.5181 0.3273 0.3296 -0.0521 0.1199  -0.0587 384  ALA B O   
6809 C  CB  . ALA B 385 ? 0.5515 0.3416 0.3896 -0.0012 -0.0228 -0.0505 384  ALA B CB  
6810 N  N   . ILE B 386 ? 0.4348 0.3184 0.3701 -0.0057 0.0412  -0.0450 385  ILE B N   
6811 C  CA  . ILE B 386 ? 0.3949 0.2568 0.3871 0.0185  -0.0045 -0.0272 385  ILE B CA  
6812 C  C   . ILE B 386 ? 0.4367 0.2596 0.3512 -0.0292 -0.0133 -0.0268 385  ILE B C   
6813 O  O   . ILE B 386 ? 0.4233 0.2544 0.3375 -0.0116 -0.0129 0.0092  385  ILE B O   
6814 C  CB  . ILE B 386 ? 0.3454 0.2402 0.4229 -0.0440 -0.0597 -0.0083 385  ILE B CB  
6815 C  CG1 . ILE B 386 ? 0.3917 0.2523 0.4790 -0.0623 -0.0040 -0.0073 385  ILE B CG1 
6816 C  CG2 . ILE B 386 ? 0.3742 0.2284 0.4384 -0.0624 -0.0721 -0.0007 385  ILE B CG2 
6817 C  CD1 . ILE B 386 ? 0.3317 0.2743 0.4906 -0.0758 -0.0011 -0.0160 385  ILE B CD1 
6818 N  N   . PRO B 387 ? 0.4363 0.2504 0.3455 -0.0325 0.0014  -0.0376 386  PRO B N   
6819 C  CA  . PRO B 387 ? 0.4123 0.2651 0.3048 0.0315  -0.0079 -0.0349 386  PRO B CA  
6820 C  C   . PRO B 387 ? 0.3757 0.2699 0.2845 0.0025  -0.0502 -0.0367 386  PRO B C   
6821 O  O   . PRO B 387 ? 0.3620 0.2217 0.2310 0.0274  -0.0418 -0.0631 386  PRO B O   
6822 C  CB  . PRO B 387 ? 0.4308 0.2774 0.3150 0.0473  0.0054  -0.0569 386  PRO B CB  
6823 C  CG  . PRO B 387 ? 0.4264 0.2587 0.3109 0.0161  0.0173  -0.0877 386  PRO B CG  
6824 C  CD  . PRO B 387 ? 0.4664 0.2405 0.3420 -0.0128 0.0383  -0.0679 386  PRO B CD  
6825 N  N   . GLN B 388 ? 0.2110 0.2980 0.3052 0.0007  -0.0587 -0.0403 387  GLN B N   
6826 C  CA  . GLN B 388 ? 0.2947 0.3313 0.3098 -0.0542 -0.0965 -0.0537 387  GLN B CA  
6827 C  C   . GLN B 388 ? 0.3266 0.3296 0.2455 -0.0964 -0.0823 -0.0112 387  GLN B C   
6828 O  O   . GLN B 388 ? 0.2750 0.3648 0.2047 -0.0848 -0.0366 -0.0218 387  GLN B O   
6829 C  CB  . GLN B 388 ? 0.2617 0.3749 0.3845 -0.0615 -0.0639 -0.0864 387  GLN B CB  
6830 C  CG  . GLN B 388 ? 0.4070 0.4111 0.4189 -0.0827 -0.1025 -0.0862 387  GLN B CG  
6831 C  CD  . GLN B 388 ? 0.5640 0.4655 0.4594 -0.0743 -0.0676 -0.0485 387  GLN B CD  
6832 O  OE1 . GLN B 388 ? 0.6513 0.4849 0.4635 -0.0751 -0.0987 -0.0531 387  GLN B OE1 
6833 N  NE2 . GLN B 388 ? 0.5553 0.4700 0.4782 -0.0853 -0.0577 -0.0240 387  GLN B NE2 
6834 N  N   . HIS B 389 ? 0.2875 0.3175 0.2108 -0.0948 -0.1221 0.0131  388  HIS B N   
6835 C  CA  . HIS B 389 ? 0.2206 0.3052 0.1893 -0.0608 -0.0658 0.0129  388  HIS B CA  
6836 C  C   . HIS B 389 ? 0.2389 0.2796 0.1666 -0.0321 -0.0358 0.0041  388  HIS B C   
6837 O  O   . HIS B 389 ? 0.2677 0.2927 0.2041 -0.0118 -0.0237 0.0134  388  HIS B O   
6838 C  CB  . HIS B 389 ? 0.1966 0.3381 0.2194 -0.0874 -0.0474 0.0206  388  HIS B CB  
6839 C  CG  . HIS B 389 ? 0.2916 0.3572 0.2324 -0.0413 -0.0555 0.0136  388  HIS B CG  
6840 N  ND1 . HIS B 389 ? 0.3477 0.3550 0.2541 -0.0525 -0.0614 0.0129  388  HIS B ND1 
6841 C  CD2 . HIS B 389 ? 0.3624 0.3793 0.2380 -0.0053 -0.0547 0.0216  388  HIS B CD2 
6842 C  CE1 . HIS B 389 ? 0.3443 0.3849 0.2564 -0.0007 -0.1030 0.0368  388  HIS B CE1 
6843 N  NE2 . HIS B 389 ? 0.3315 0.3765 0.2260 -0.0001 -0.0845 0.0457  388  HIS B NE2 
6844 N  N   . ALA B 390 ? 0.2075 0.2559 0.1515 -0.0090 -0.0390 -0.0003 389  ALA B N   
6845 C  CA  . ALA B 390 ? 0.2318 0.2164 0.1387 -0.0137 0.0202  -0.0405 389  ALA B CA  
6846 C  C   . ALA B 390 ? 0.2771 0.2000 0.1355 0.0132  0.0067  -0.0079 389  ALA B C   
6847 O  O   . ALA B 390 ? 0.2746 0.1858 0.1554 -0.0027 0.0182  -0.0296 389  ALA B O   
6848 C  CB  . ALA B 390 ? 0.2932 0.2379 0.1730 0.0283  0.0593  -0.0741 389  ALA B CB  
6849 N  N   . PHE B 391 ? 0.2181 0.2034 0.1244 0.0033  0.0145  0.0377  390  PHE B N   
6850 C  CA  . PHE B 391 ? 0.1944 0.2131 0.1127 0.0051  0.0021  0.0148  390  PHE B CA  
6851 C  C   . PHE B 391 ? 0.1394 0.2018 0.1369 -0.0280 0.0188  0.0032  390  PHE B C   
6852 O  O   . PHE B 391 ? 0.1565 0.1990 0.1600 -0.0487 0.0174  0.0154  390  PHE B O   
6853 C  CB  . PHE B 391 ? 0.1950 0.2186 0.1221 0.0239  -0.0417 0.0075  390  PHE B CB  
6854 C  CG  . PHE B 391 ? 0.1127 0.1951 0.1217 0.0229  -0.0526 -0.0144 390  PHE B CG  
6855 C  CD1 . PHE B 391 ? 0.1344 0.1489 0.1435 -0.0397 -0.0475 -0.0301 390  PHE B CD1 
6856 C  CD2 . PHE B 391 ? 0.1730 0.2096 0.1252 0.0119  -0.0284 -0.0095 390  PHE B CD2 
6857 C  CE1 . PHE B 391 ? 0.1721 0.1823 0.1549 -0.0175 -0.0048 0.0013  390  PHE B CE1 
6858 C  CE2 . PHE B 391 ? 0.1113 0.1920 0.1587 0.0222  -0.0211 0.0098  390  PHE B CE2 
6859 C  CZ  . PHE B 391 ? 0.1750 0.2065 0.1718 0.0438  -0.0234 0.0116  390  PHE B CZ  
6860 N  N   . LYS B 392 ? 0.1415 0.1881 0.1406 -0.0305 0.0057  -0.0003 391  LYS B N   
6861 C  CA  . LYS B 392 ? 0.1215 0.1832 0.1300 -0.0094 -0.0201 0.0022  391  LYS B CA  
6862 C  C   . LYS B 392 ? 0.1928 0.1704 0.1469 -0.0413 -0.0107 0.0068  391  LYS B C   
6863 O  O   . LYS B 392 ? 0.1475 0.1411 0.1503 -0.0455 0.0051  0.0144  391  LYS B O   
6864 C  CB  . LYS B 392 ? 0.1849 0.1817 0.1063 -0.0151 -0.0461 -0.0013 391  LYS B CB  
6865 C  CG  . LYS B 392 ? 0.2219 0.2488 0.1316 -0.0824 0.0079  -0.0305 391  LYS B CG  
6866 C  CD  . LYS B 392 ? 0.2008 0.3386 0.1707 -0.0025 0.0318  -0.0569 391  LYS B CD  
6867 C  CE  . LYS B 392 ? 0.1676 0.3615 0.2106 -0.0002 0.0157  -0.0600 391  LYS B CE  
6868 N  NZ  . LYS B 392 ? 0.2275 0.3442 0.2356 -0.0093 -0.0381 -0.0603 391  LYS B NZ  
6869 N  N   . PRO B 393 ? 0.1553 0.1618 0.1243 0.0130  -0.0156 0.0043  392  PRO B N   
6870 C  CA  . PRO B 393 ? 0.1319 0.1803 0.1371 0.0218  -0.0023 0.0033  392  PRO B CA  
6871 C  C   . PRO B 393 ? 0.1199 0.1642 0.1357 -0.0008 0.0245  -0.0164 392  PRO B C   
6872 O  O   . PRO B 393 ? 0.1146 0.1351 0.1430 -0.0060 0.0261  -0.0121 392  PRO B O   
6873 C  CB  . PRO B 393 ? 0.1395 0.1176 0.1337 0.0635  -0.0228 0.0051  392  PRO B CB  
6874 C  CG  . PRO B 393 ? 0.1793 0.1573 0.1450 -0.0082 -0.0019 -0.0104 392  PRO B CG  
6875 C  CD  . PRO B 393 ? 0.1948 0.1370 0.1022 0.0281  -0.0274 0.0287  392  PRO B CD  
6876 N  N   A HIS B 394 ? 0.1306 0.1732 0.1363 -0.0193 -0.0194 0.0066  393  HIS B N   
6877 N  N   B HIS B 394 ? 0.1254 0.1540 0.1337 -0.0122 0.0024  -0.0109 393  HIS B N   
6878 C  CA  A HIS B 394 ? 0.1781 0.1747 0.1591 -0.0663 -0.0320 0.0006  393  HIS B CA  
6879 C  CA  B HIS B 394 ? 0.1327 0.1407 0.1350 -0.0364 -0.0138 -0.0164 393  HIS B CA  
6880 C  C   A HIS B 394 ? 0.1883 0.1324 0.1348 -0.0484 -0.0226 -0.0015 393  HIS B C   
6881 C  C   B HIS B 394 ? 0.1588 0.1407 0.1263 -0.0434 -0.0267 -0.0090 393  HIS B C   
6882 O  O   A HIS B 394 ? 0.1992 0.1371 0.1365 0.0029  0.0025  -0.0396 393  HIS B O   
6883 O  O   B HIS B 394 ? 0.1895 0.1520 0.1283 -0.0334 -0.0114 -0.0127 393  HIS B O   
6884 C  CB  A HIS B 394 ? 0.1482 0.2130 0.1734 -0.0356 -0.0590 0.0348  393  HIS B CB  
6885 C  CB  B HIS B 394 ? 0.0860 0.1249 0.1384 -0.0231 -0.0133 -0.0133 393  HIS B CB  
6886 C  CG  A HIS B 394 ? 0.1412 0.2272 0.1982 -0.0708 -0.0729 0.0206  393  HIS B CG  
6887 C  CG  B HIS B 394 ? 0.1227 0.1054 0.1482 0.0116  0.0170  -0.0291 393  HIS B CG  
6888 N  ND1 A HIS B 394 ? 0.2156 0.2285 0.2198 -0.0247 0.0028  -0.0016 393  HIS B ND1 
6889 N  ND1 B HIS B 394 ? 0.1131 0.1014 0.1645 0.0283  0.0289  -0.0413 393  HIS B ND1 
6890 C  CD2 A HIS B 394 ? 0.2731 0.2195 0.1952 -0.0417 -0.0957 0.0380  393  HIS B CD2 
6891 C  CD2 B HIS B 394 ? 0.1154 0.1061 0.1604 0.0145  0.0105  -0.0256 393  HIS B CD2 
6892 C  CE1 A HIS B 394 ? 0.2652 0.2339 0.2059 -0.0385 -0.0240 0.0155  393  HIS B CE1 
6893 C  CE1 B HIS B 394 ? 0.1376 0.1077 0.1726 0.0073  0.0327  -0.0371 393  HIS B CE1 
6894 N  NE2 A HIS B 394 ? 0.3029 0.2272 0.2095 -0.0454 -0.0611 0.0120  393  HIS B NE2 
6895 N  NE2 B HIS B 394 ? 0.1530 0.1025 0.1715 -0.0180 0.0266  -0.0418 393  HIS B NE2 
6896 N  N   . GLY B 395 ? 0.1572 0.1396 0.1240 -0.0478 -0.0490 0.0041  394  GLY B N   
6897 C  CA  . GLY B 395 ? 0.1971 0.1496 0.1274 -0.0245 -0.0866 -0.0066 394  GLY B CA  
6898 C  C   . GLY B 395 ? 0.2352 0.1540 0.1431 -0.0498 -0.0681 -0.0025 394  GLY B C   
6899 O  O   . GLY B 395 ? 0.1818 0.1657 0.1586 -0.0222 -0.0295 0.0004  394  GLY B O   
6900 N  N   . ASN B 396 ? 0.1841 0.1581 0.1187 -0.0323 -0.0705 0.0201  395  ASN B N   
6901 C  CA  . ASN B 396 ? 0.1926 0.1737 0.1354 -0.0168 -0.0579 0.0084  395  ASN B CA  
6902 C  C   . ASN B 396 ? 0.2212 0.1726 0.1500 -0.0538 -0.0468 -0.0111 395  ASN B C   
6903 O  O   . ASN B 396 ? 0.1714 0.1790 0.1637 -0.0349 -0.0238 0.0098  395  ASN B O   
6904 C  CB  . ASN B 396 ? 0.2099 0.1881 0.1101 0.0040  -0.0259 0.0211  395  ASN B CB  
6905 C  CG  . ASN B 396 ? 0.2270 0.2089 0.1496 -0.0285 -0.0576 0.0146  395  ASN B CG  
6906 O  OD1 . ASN B 396 ? 0.2271 0.2056 0.1524 -0.0185 -0.0484 -0.0085 395  ASN B OD1 
6907 N  ND2 . ASN B 396 ? 0.1540 0.2416 0.1614 -0.0168 -0.0586 0.0056  395  ASN B ND2 
6908 N  N   . GLY B 397 ? 0.1714 0.1559 0.1494 -0.0496 -0.0628 -0.0397 396  GLY B N   
6909 C  CA  . GLY B 397 ? 0.1512 0.1691 0.1370 -0.0494 -0.0297 -0.0631 396  GLY B CA  
6910 C  C   . GLY B 397 ? 0.0727 0.1521 0.1547 -0.0042 -0.0059 -0.0469 396  GLY B C   
6911 O  O   . GLY B 397 ? 0.1941 0.1786 0.1578 -0.0098 -0.0009 -0.0174 396  GLY B O   
6912 N  N   . GLN B 398 ? 0.1073 0.1409 0.1649 0.0003  0.0093  -0.0508 397  GLN B N   
6913 C  CA  . GLN B 398 ? 0.1191 0.1653 0.1758 0.0317  -0.0034 -0.0204 397  GLN B CA  
6914 C  C   . GLN B 398 ? 0.1654 0.1477 0.1609 -0.0305 -0.0229 -0.0055 397  GLN B C   
6915 O  O   . GLN B 398 ? 0.1783 0.1618 0.1678 -0.0018 -0.0103 -0.0002 397  GLN B O   
6916 C  CB  . GLN B 398 ? 0.1667 0.1681 0.1811 -0.0419 -0.0230 0.0133  397  GLN B CB  
6917 C  CG  . GLN B 398 ? 0.1585 0.1943 0.1991 -0.0038 -0.0568 0.0234  397  GLN B CG  
6918 C  CD  . GLN B 398 ? 0.2008 0.2275 0.2164 0.0054  -0.0522 0.0107  397  GLN B CD  
6919 O  OE1 . GLN B 398 ? 0.2128 0.2429 0.2297 -0.0061 -0.0625 -0.0003 397  GLN B OE1 
6920 N  NE2 . GLN B 398 ? 0.1917 0.2402 0.2135 0.0297  -0.0392 -0.0153 397  GLN B NE2 
6921 N  N   . ARG B 399 ? 0.1356 0.1291 0.1634 -0.0124 -0.0401 0.0006  398  ARG B N   
6922 C  CA  . ARG B 399 ? 0.1289 0.1305 0.1715 0.0052  -0.0329 0.0255  398  ARG B CA  
6923 C  C   . ARG B 399 ? 0.1344 0.1388 0.1637 -0.0209 -0.0222 0.0026  398  ARG B C   
6924 O  O   . ARG B 399 ? 0.1410 0.1394 0.1717 0.0149  -0.0087 -0.0436 398  ARG B O   
6925 C  CB  . ARG B 399 ? 0.1364 0.1441 0.1807 0.0139  -0.0328 0.0392  398  ARG B CB  
6926 C  CG  . ARG B 399 ? 0.1446 0.1571 0.1687 -0.0009 -0.0142 0.0244  398  ARG B CG  
6927 C  CD  . ARG B 399 ? 0.1124 0.1721 0.1442 -0.0292 -0.0261 0.0017  398  ARG B CD  
6928 N  NE  . ARG B 399 ? 0.1360 0.1319 0.1265 -0.0099 -0.0367 0.0187  398  ARG B NE  
6929 C  CZ  . ARG B 399 ? 0.1392 0.1384 0.1217 0.0189  -0.0467 0.0200  398  ARG B CZ  
6930 N  NH1 . ARG B 399 ? 0.0925 0.1571 0.1476 0.0102  -0.0154 0.0654  398  ARG B NH1 
6931 N  NH2 . ARG B 399 ? 0.1596 0.1198 0.1266 0.0201  -0.0404 -0.0025 398  ARG B NH2 
6932 N  N   . ALA B 400 ? 0.1124 0.1635 0.1645 -0.0034 -0.0274 0.0136  399  ALA B N   
6933 C  CA  . ALA B 400 ? 0.1443 0.1756 0.1197 0.0329  -0.0037 0.0071  399  ALA B CA  
6934 C  C   . ALA B 400 ? 0.1529 0.1863 0.1304 0.0303  -0.0503 -0.0158 399  ALA B C   
6935 O  O   . ALA B 400 ? 0.1379 0.2266 0.1668 0.0200  -0.0149 -0.0339 399  ALA B O   
6936 C  CB  . ALA B 400 ? 0.1304 0.1685 0.1496 0.0732  -0.0311 0.0123  399  ALA B CB  
6937 N  N   . CYS B 401 ? 0.0990 0.1773 0.1092 0.0072  -0.0516 -0.0331 400  CYS B N   
6938 C  CA  . CYS B 401 ? 0.1105 0.1557 0.1103 -0.0492 -0.0423 -0.0169 400  CYS B CA  
6939 C  C   . CYS B 401 ? 0.0935 0.1707 0.1241 -0.0151 0.0121  0.0081  400  CYS B C   
6940 O  O   . CYS B 401 ? 0.1417 0.1578 0.1628 0.0018  0.0315  0.0134  400  CYS B O   
6941 C  CB  . CYS B 401 ? 0.1084 0.1689 0.1307 -0.0462 -0.0165 0.0124  400  CYS B CB  
6942 S  SG  . CYS B 401 ? 0.1502 0.2187 0.1219 -0.0219 -0.0168 0.0293  400  CYS B SG  
6943 N  N   . ILE B 402 ? 0.1359 0.1639 0.1200 -0.0414 0.0038  0.0228  401  ILE B N   
6944 C  CA  . ILE B 402 ? 0.1452 0.1461 0.1490 -0.0257 -0.0005 0.0276  401  ILE B CA  
6945 C  C   . ILE B 402 ? 0.1540 0.1205 0.1662 -0.0334 -0.0076 0.0107  401  ILE B C   
6946 O  O   . ILE B 402 ? 0.1801 0.1345 0.2081 -0.0162 0.0023  0.0176  401  ILE B O   
6947 C  CB  . ILE B 402 ? 0.1228 0.1782 0.1553 -0.0289 0.0034  0.0058  401  ILE B CB  
6948 C  CG1 . ILE B 402 ? 0.0537 0.1711 0.1776 0.0316  0.0052  0.0027  401  ILE B CG1 
6949 C  CG2 . ILE B 402 ? 0.1504 0.1743 0.1377 -0.0387 0.0090  0.0014  401  ILE B CG2 
6950 C  CD1 . ILE B 402 ? 0.0853 0.1998 0.2055 0.0213  0.0149  0.0214  401  ILE B CD1 
6951 N  N   . GLY B 403 ? 0.1359 0.1647 0.1683 0.0153  -0.0108 0.0187  402  GLY B N   
6952 C  CA  . GLY B 403 ? 0.1013 0.1924 0.1351 0.0369  -0.0422 0.0298  402  GLY B CA  
6953 C  C   . GLY B 403 ? 0.1401 0.1788 0.1415 -0.0039 -0.0330 0.0005  402  GLY B C   
6954 O  O   . GLY B 403 ? 0.2003 0.1581 0.1487 0.0167  -0.0073 -0.0046 402  GLY B O   
6955 N  N   . GLN B 404 ? 0.1729 0.1960 0.1093 0.0014  0.0189  -0.0013 403  GLN B N   
6956 C  CA  . GLN B 404 ? 0.1800 0.1787 0.1233 -0.0180 0.0210  0.0120  403  GLN B CA  
6957 C  C   . GLN B 404 ? 0.2031 0.1771 0.1556 -0.0175 -0.0219 0.0023  403  GLN B C   
6958 O  O   . GLN B 404 ? 0.1867 0.1828 0.1979 0.0036  -0.0270 0.0129  403  GLN B O   
6959 C  CB  . GLN B 404 ? 0.2758 0.2223 0.1372 0.0658  0.0933  0.0318  403  GLN B CB  
6960 C  CG  . GLN B 404 ? 0.3615 0.2448 0.1705 0.0475  0.1067  0.0086  403  GLN B CG  
6961 C  CD  . GLN B 404 ? 0.3843 0.2998 0.2205 0.0888  0.0926  -0.0317 403  GLN B CD  
6962 O  OE1 . GLN B 404 ? 0.4166 0.3016 0.2037 0.1247  -0.0332 -0.0052 403  GLN B OE1 
6963 N  NE2 . GLN B 404 ? 0.4046 0.3310 0.2554 0.0829  0.0650  -0.1008 403  GLN B NE2 
6964 N  N   A GLN B 405 ? 0.2422 0.1498 0.1408 -0.0430 0.0050  0.0053  404  GLN B N   
6965 N  N   B GLN B 405 ? 0.2360 0.1603 0.1457 -0.0589 -0.0008 -0.0054 404  GLN B N   
6966 C  CA  A GLN B 405 ? 0.2620 0.1236 0.1520 -0.0408 -0.0245 0.0130  404  GLN B CA  
6967 C  CA  B GLN B 405 ? 0.2218 0.1441 0.1716 -0.0679 -0.0731 -0.0058 404  GLN B CA  
6968 C  C   A GLN B 405 ? 0.2583 0.1153 0.1525 -0.0165 -0.0428 0.0092  404  GLN B C   
6969 C  C   B GLN B 405 ? 0.2318 0.1171 0.1586 -0.0125 -0.0682 0.0009  404  GLN B C   
6970 O  O   A GLN B 405 ? 0.2869 0.1082 0.1609 -0.0180 -0.0193 0.0008  404  GLN B O   
6971 O  O   B GLN B 405 ? 0.2363 0.1032 0.1700 0.0068  -0.0302 -0.0032 404  GLN B O   
6972 C  CB  A GLN B 405 ? 0.3983 0.1313 0.1676 -0.0341 -0.0450 -0.0003 404  GLN B CB  
6973 C  CB  B GLN B 405 ? 0.3350 0.2075 0.2245 -0.0799 -0.1116 -0.0319 404  GLN B CB  
6974 C  CG  A GLN B 405 ? 0.5173 0.1444 0.1825 -0.0185 -0.0358 0.0186  404  GLN B CG  
6975 C  CG  B GLN B 405 ? 0.4674 0.2566 0.2716 -0.0836 -0.1558 -0.0327 404  GLN B CG  
6976 C  CD  A GLN B 405 ? 0.5958 0.1569 0.1977 0.0307  0.0351  0.0165  404  GLN B CD  
6977 C  CD  B GLN B 405 ? 0.5681 0.3234 0.3208 -0.0584 -0.1356 -0.0475 404  GLN B CD  
6978 O  OE1 A GLN B 405 ? 0.6558 0.2024 0.2141 0.0230  0.0834  0.0363  404  GLN B OE1 
6979 O  OE1 B GLN B 405 ? 0.5046 0.3683 0.3503 -0.0085 -0.1290 -0.0399 404  GLN B OE1 
6980 N  NE2 A GLN B 405 ? 0.6725 0.1705 0.2228 0.0300  0.0165  0.0001  404  GLN B NE2 
6981 N  NE2 B GLN B 405 ? 0.6496 0.3457 0.3362 -0.0988 -0.1122 -0.0381 404  GLN B NE2 
6982 N  N   . PHE B 406 ? 0.2371 0.1239 0.1628 -0.0078 -0.0426 0.0145  405  PHE B N   
6983 C  CA  . PHE B 406 ? 0.1450 0.1375 0.1675 -0.0123 -0.0550 -0.0274 405  PHE B CA  
6984 C  C   . PHE B 406 ? 0.0651 0.1556 0.1453 0.0061  -0.0093 -0.0166 405  PHE B C   
6985 O  O   . PHE B 406 ? 0.1163 0.1920 0.1536 0.0008  -0.0178 -0.0025 405  PHE B O   
6986 C  CB  . PHE B 406 ? 0.0998 0.2012 0.1631 -0.0200 -0.0214 -0.0150 405  PHE B CB  
6987 C  CG  . PHE B 406 ? 0.1318 0.2171 0.1612 0.0019  0.0361  -0.0126 405  PHE B CG  
6988 C  CD1 . PHE B 406 ? 0.1266 0.2199 0.1621 -0.0001 -0.0048 -0.0030 405  PHE B CD1 
6989 C  CD2 . PHE B 406 ? 0.1881 0.2190 0.1411 0.0185  0.0115  0.0150  405  PHE B CD2 
6990 C  CE1 . PHE B 406 ? 0.1287 0.2324 0.1571 -0.0010 -0.0071 0.0078  405  PHE B CE1 
6991 C  CE2 . PHE B 406 ? 0.1551 0.2320 0.1513 -0.0491 -0.0432 -0.0189 405  PHE B CE2 
6992 C  CZ  . PHE B 406 ? 0.1464 0.2604 0.1625 -0.0196 0.0023  -0.0275 405  PHE B CZ  
6993 N  N   . ALA B 407 ? 0.0941 0.1569 0.1163 -0.0490 -0.0274 -0.0066 406  ALA B N   
6994 C  CA  . ALA B 407 ? 0.1405 0.1613 0.1207 -0.0090 -0.0674 0.0086  406  ALA B CA  
6995 C  C   . ALA B 407 ? 0.2003 0.1661 0.1224 0.0291  -0.0397 -0.0203 406  ALA B C   
6996 O  O   . ALA B 407 ? 0.1770 0.1677 0.1179 0.0123  -0.0312 -0.0175 406  ALA B O   
6997 C  CB  . ALA B 407 ? 0.1533 0.1255 0.1225 0.0225  -0.0326 0.0317  406  ALA B CB  
6998 N  N   . LEU B 408 ? 0.1875 0.1433 0.1286 -0.0133 0.0459  -0.0355 407  LEU B N   
6999 C  CA  . LEU B 408 ? 0.2231 0.1646 0.0930 -0.0372 0.0124  -0.0166 407  LEU B CA  
7000 C  C   . LEU B 408 ? 0.1459 0.1831 0.1319 0.0017  0.0233  -0.0111 407  LEU B C   
7001 O  O   . LEU B 408 ? 0.1594 0.1907 0.1511 -0.0190 -0.0011 -0.0402 407  LEU B O   
7002 C  CB  . LEU B 408 ? 0.2692 0.2298 0.0878 -0.0672 -0.0069 0.0321  407  LEU B CB  
7003 C  CG  . LEU B 408 ? 0.3363 0.2782 0.1383 -0.0537 -0.0286 -0.0022 407  LEU B CG  
7004 C  CD1 . LEU B 408 ? 0.4223 0.3088 0.1604 0.0421  -0.0310 -0.0225 407  LEU B CD1 
7005 C  CD2 . LEU B 408 ? 0.3961 0.3183 0.1851 -0.1176 0.0256  -0.0073 407  LEU B CD2 
7006 N  N   . HIS B 409 ? 0.1655 0.1589 0.1132 0.0114  0.0153  0.0178  408  HIS B N   
7007 C  CA  . HIS B 409 ? 0.1906 0.1827 0.1161 0.0025  -0.0145 0.0077  408  HIS B CA  
7008 C  C   . HIS B 409 ? 0.1697 0.1657 0.1261 0.0087  -0.0668 0.0031  408  HIS B C   
7009 O  O   . HIS B 409 ? 0.1351 0.1458 0.1392 -0.0064 -0.0574 0.0218  408  HIS B O   
7010 C  CB  . HIS B 409 ? 0.1548 0.1688 0.1261 0.0168  -0.0260 0.0133  408  HIS B CB  
7011 C  CG  . HIS B 409 ? 0.1706 0.1267 0.1306 -0.0142 -0.0131 0.0062  408  HIS B CG  
7012 N  ND1 . HIS B 409 ? 0.2094 0.1521 0.1615 -0.0045 -0.0130 0.0165  408  HIS B ND1 
7013 C  CD2 . HIS B 409 ? 0.1731 0.1310 0.1434 0.0087  -0.0431 0.0154  408  HIS B CD2 
7014 C  CE1 . HIS B 409 ? 0.2314 0.1890 0.1612 0.0463  -0.0353 -0.0051 408  HIS B CE1 
7015 N  NE2 . HIS B 409 ? 0.2217 0.1703 0.1462 0.0171  -0.0687 -0.0232 408  HIS B NE2 
7016 N  N   . GLU B 410 ? 0.1901 0.1545 0.1200 -0.0280 0.0051  -0.0470 409  GLU B N   
7017 C  CA  . GLU B 410 ? 0.1373 0.1606 0.1348 -0.0426 -0.0048 -0.0557 409  GLU B CA  
7018 C  C   . GLU B 410 ? 0.1496 0.1558 0.1589 -0.0283 0.0194  -0.0171 409  GLU B C   
7019 O  O   . GLU B 410 ? 0.1496 0.1585 0.1537 -0.0173 0.0143  -0.0073 409  GLU B O   
7020 C  CB  . GLU B 410 ? 0.1955 0.1819 0.1576 -0.0098 -0.0136 -0.0320 409  GLU B CB  
7021 C  CG  . GLU B 410 ? 0.1310 0.1802 0.1972 0.0159  -0.0053 -0.0513 409  GLU B CG  
7022 C  CD  . GLU B 410 ? 0.2168 0.2225 0.2447 -0.0082 0.0120  -0.0254 409  GLU B CD  
7023 O  OE1 . GLU B 410 ? 0.2564 0.2565 0.2554 0.0458  0.0004  -0.0157 409  GLU B OE1 
7024 O  OE2 . GLU B 410 ? 0.2015 0.2084 0.2912 -0.0337 0.0159  -0.0466 409  GLU B OE2 
7025 N  N   . ALA B 411 ? 0.1243 0.1349 0.1584 -0.0216 0.0418  -0.0065 410  ALA B N   
7026 C  CA  . ALA B 411 ? 0.1386 0.1060 0.1567 -0.0036 0.0365  0.0321  410  ALA B CA  
7027 C  C   . ALA B 411 ? 0.1739 0.1143 0.1577 0.0223  -0.0049 0.0074  410  ALA B C   
7028 O  O   . ALA B 411 ? 0.1537 0.1300 0.1416 -0.0129 -0.0022 0.0050  410  ALA B O   
7029 C  CB  . ALA B 411 ? 0.1948 0.1095 0.1579 -0.0412 -0.0098 0.0307  410  ALA B CB  
7030 N  N   . THR B 412 ? 0.1765 0.0998 0.1610 -0.0008 -0.0074 -0.0110 411  THR B N   
7031 C  CA  . THR B 412 ? 0.1562 0.1304 0.1410 -0.0072 0.0201  -0.0081 411  THR B CA  
7032 C  C   . THR B 412 ? 0.1799 0.1440 0.1498 -0.0144 0.0047  -0.0061 411  THR B C   
7033 O  O   . THR B 412 ? 0.1802 0.1490 0.1469 0.0291  0.0026  -0.0260 411  THR B O   
7034 C  CB  . THR B 412 ? 0.1563 0.0947 0.1430 0.0071  -0.0029 0.0001  411  THR B CB  
7035 O  OG1 . THR B 412 ? 0.1698 0.1118 0.1464 -0.0121 -0.0106 0.0259  411  THR B OG1 
7036 C  CG2 . THR B 412 ? 0.1586 0.1087 0.1941 0.0168  -0.0138 -0.0191 411  THR B CG2 
7037 N  N   . LEU B 413 ? 0.1941 0.1684 0.1180 -0.0167 -0.0233 -0.0049 412  LEU B N   
7038 C  CA  . LEU B 413 ? 0.1482 0.1668 0.1118 -0.0251 -0.0032 0.0063  412  LEU B CA  
7039 C  C   . LEU B 413 ? 0.1459 0.1812 0.1233 -0.0081 -0.0281 -0.0181 412  LEU B C   
7040 O  O   . LEU B 413 ? 0.1697 0.1981 0.1478 0.0265  -0.0162 -0.0142 412  LEU B O   
7041 C  CB  . LEU B 413 ? 0.0978 0.1851 0.1257 0.0027  0.0296  0.0171  412  LEU B CB  
7042 C  CG  . LEU B 413 ? 0.1813 0.2306 0.1650 0.0751  0.0413  0.0314  412  LEU B CG  
7043 C  CD1 . LEU B 413 ? 0.2078 0.2359 0.1851 0.1080  0.0135  0.0097  412  LEU B CD1 
7044 C  CD2 . LEU B 413 ? 0.2834 0.2554 0.1724 0.0573  0.0699  0.0407  412  LEU B CD2 
7045 N  N   . VAL B 414 ? 0.1385 0.1682 0.1334 -0.0015 -0.0206 -0.0092 413  VAL B N   
7046 C  CA  . VAL B 414 ? 0.0928 0.1848 0.1886 0.0217  -0.0039 -0.0522 413  VAL B CA  
7047 C  C   . VAL B 414 ? 0.1364 0.1746 0.1715 -0.0088 -0.0646 -0.0259 413  VAL B C   
7048 O  O   . VAL B 414 ? 0.1515 0.1842 0.1649 0.0036  -0.0462 -0.0183 413  VAL B O   
7049 C  CB  . VAL B 414 ? 0.0838 0.2005 0.2199 0.0288  -0.0201 -0.0921 413  VAL B CB  
7050 C  CG1 . VAL B 414 ? 0.1914 0.2435 0.2774 0.0524  -0.0752 -0.0873 413  VAL B CG1 
7051 C  CG2 . VAL B 414 ? 0.1222 0.2536 0.2456 0.0430  0.0201  -0.1017 413  VAL B CG2 
7052 N  N   . LEU B 415 ? 0.1914 0.1705 0.1401 0.0019  -0.0174 -0.0508 414  LEU B N   
7053 C  CA  . LEU B 415 ? 0.1267 0.1860 0.1230 0.0280  0.0056  -0.0190 414  LEU B CA  
7054 C  C   . LEU B 415 ? 0.1603 0.1628 0.1524 0.0232  0.0094  -0.0050 414  LEU B C   
7055 O  O   . LEU B 415 ? 0.1726 0.1567 0.1332 -0.0070 -0.0034 0.0103  414  LEU B O   
7056 C  CB  . LEU B 415 ? 0.1190 0.2142 0.1560 0.0351  0.0240  0.0283  414  LEU B CB  
7057 C  CG  . LEU B 415 ? 0.1126 0.2207 0.1371 -0.0204 -0.0116 0.0034  414  LEU B CG  
7058 C  CD1 . LEU B 415 ? 0.1375 0.1822 0.1795 -0.0353 -0.0428 -0.0349 414  LEU B CD1 
7059 C  CD2 . LEU B 415 ? 0.1948 0.2299 0.1148 -0.0442 0.0037  0.0463  414  LEU B CD2 
7060 N  N   . GLY B 416 ? 0.1761 0.1075 0.1395 0.0291  0.0085  -0.0142 415  GLY B N   
7061 C  CA  . GLY B 416 ? 0.1402 0.1354 0.1067 -0.0013 -0.0159 0.0096  415  GLY B CA  
7062 C  C   . GLY B 416 ? 0.2168 0.1432 0.1058 0.0162  -0.0119 0.0205  415  GLY B C   
7063 O  O   . GLY B 416 ? 0.2311 0.1419 0.1124 0.0307  0.0122  0.0070  415  GLY B O   
7064 N  N   . MET B 417 ? 0.1566 0.1422 0.1041 -0.0316 0.0002  -0.0148 416  MET B N   
7065 C  CA  . MET B 417 ? 0.1856 0.1709 0.1141 -0.0118 0.0276  -0.0313 416  MET B CA  
7066 C  C   . MET B 417 ? 0.1961 0.1842 0.1382 -0.0164 0.0081  -0.0121 416  MET B C   
7067 O  O   . MET B 417 ? 0.1715 0.1886 0.1335 -0.0184 0.0101  -0.0023 416  MET B O   
7068 C  CB  . MET B 417 ? 0.1161 0.1673 0.1281 -0.0204 0.0081  -0.0406 416  MET B CB  
7069 C  CG  . MET B 417 ? 0.1638 0.2159 0.1740 0.0052  0.0915  -0.0446 416  MET B CG  
7070 S  SD  . MET B 417 ? 0.2233 0.2343 0.2202 -0.0108 0.0472  -0.0447 416  MET B SD  
7071 C  CE  . MET B 417 ? 0.2759 0.2908 0.1801 -0.0257 0.0589  -0.0504 416  MET B CE  
7072 N  N   . MET B 418 ? 0.1607 0.1529 0.1465 -0.0047 0.0278  -0.0378 417  MET B N   
7073 C  CA  . MET B 418 ? 0.1312 0.1527 0.1815 0.0036  -0.0016 -0.0265 417  MET B CA  
7074 C  C   . MET B 418 ? 0.1669 0.1948 0.1698 0.0325  0.0168  -0.0284 417  MET B C   
7075 O  O   . MET B 418 ? 0.1655 0.2134 0.1702 0.0108  0.0193  -0.0087 417  MET B O   
7076 C  CB  . MET B 418 ? 0.1265 0.0963 0.2233 0.0025  -0.0243 -0.0418 417  MET B CB  
7077 C  CG  . MET B 418 ? 0.1684 0.1059 0.2253 0.0440  0.0242  -0.0367 417  MET B CG  
7078 S  SD  . MET B 418 ? 0.2369 0.1580 0.2688 0.0397  0.0343  0.0421  417  MET B SD  
7079 C  CE  . MET B 418 ? 0.2428 0.1477 0.2458 -0.0537 -0.0040 0.0080  417  MET B CE  
7080 N  N   . LEU B 419 ? 0.1797 0.2005 0.1477 0.0287  0.0357  -0.0447 418  LEU B N   
7081 C  CA  . LEU B 419 ? 0.1979 0.1921 0.1123 0.0483  0.0232  -0.0153 418  LEU B CA  
7082 C  C   . LEU B 419 ? 0.2356 0.2079 0.1376 0.0032  0.0214  -0.0103 418  LEU B C   
7083 O  O   . LEU B 419 ? 0.2828 0.2076 0.1355 -0.0032 -0.0101 0.0085  418  LEU B O   
7084 C  CB  . LEU B 419 ? 0.2327 0.1859 0.0960 0.0251  -0.0113 -0.0010 418  LEU B CB  
7085 C  CG  . LEU B 419 ? 0.2503 0.1925 0.1361 -0.0402 -0.0292 0.0265  418  LEU B CG  
7086 C  CD1 . LEU B 419 ? 0.3484 0.2092 0.1052 0.0619  -0.0222 0.0248  418  LEU B CD1 
7087 C  CD2 . LEU B 419 ? 0.2601 0.2121 0.2140 -0.0612 -0.0098 0.0676  418  LEU B CD2 
7088 N  N   . LYS B 420 ? 0.1740 0.1914 0.1290 -0.0268 0.0381  -0.0086 419  LYS B N   
7089 C  CA  . LYS B 420 ? 0.1692 0.1536 0.1289 0.0273  -0.0136 -0.0077 419  LYS B CA  
7090 C  C   . LYS B 420 ? 0.2255 0.1603 0.1419 0.0083  -0.0125 -0.0404 419  LYS B C   
7091 O  O   . LYS B 420 ? 0.2143 0.1905 0.1459 -0.0162 -0.0008 -0.0199 419  LYS B O   
7092 C  CB  . LYS B 420 ? 0.1920 0.1297 0.1379 0.0088  0.0107  0.0222  419  LYS B CB  
7093 C  CG  . LYS B 420 ? 0.1785 0.1506 0.1409 -0.0613 0.0388  0.0296  419  LYS B CG  
7094 C  CD  . LYS B 420 ? 0.2475 0.1417 0.1381 -0.0787 0.0028  0.0400  419  LYS B CD  
7095 C  CE  . LYS B 420 ? 0.1864 0.1523 0.1658 -0.0921 0.0171  0.0267  419  LYS B CE  
7096 N  NZ  . LYS B 420 ? 0.1697 0.1776 0.1824 -0.0718 0.0281  0.0108  419  LYS B NZ  
7097 N  N   . HIS B 421 ? 0.1698 0.1431 0.1397 -0.0054 -0.0043 -0.0502 420  HIS B N   
7098 C  CA  . HIS B 421 ? 0.1709 0.1383 0.1251 0.0269  0.0199  -0.0709 420  HIS B CA  
7099 C  C   . HIS B 421 ? 0.1781 0.1603 0.1473 0.0090  -0.0207 -0.0238 420  HIS B C   
7100 O  O   . HIS B 421 ? 0.1911 0.1582 0.1583 0.0149  -0.0449 -0.0341 420  HIS B O   
7101 C  CB  . HIS B 421 ? 0.2113 0.1485 0.1347 -0.0060 0.0300  -0.0292 420  HIS B CB  
7102 C  CG  . HIS B 421 ? 0.2372 0.1769 0.1524 0.0037  0.0050  -0.0181 420  HIS B CG  
7103 N  ND1 . HIS B 421 ? 0.2667 0.1861 0.1594 -0.0033 -0.0116 -0.0155 420  HIS B ND1 
7104 C  CD2 . HIS B 421 ? 0.2403 0.1604 0.1584 -0.0005 -0.0026 -0.0120 420  HIS B CD2 
7105 C  CE1 . HIS B 421 ? 0.2658 0.2019 0.1600 0.0052  -0.0092 -0.0163 420  HIS B CE1 
7106 N  NE2 . HIS B 421 ? 0.2504 0.1993 0.1606 0.0209  0.0051  -0.0216 420  HIS B NE2 
7107 N  N   . PHE B 422 ? 0.1867 0.1868 0.1593 0.0021  -0.0114 -0.0154 421  PHE B N   
7108 C  CA  . PHE B 422 ? 0.1284 0.2128 0.1699 -0.0378 0.0357  -0.0426 421  PHE B CA  
7109 C  C   . PHE B 422 ? 0.0956 0.2259 0.1703 -0.0253 0.0380  -0.0377 421  PHE B C   
7110 O  O   . PHE B 422 ? 0.1743 0.2335 0.1564 -0.0067 -0.0203 -0.0407 421  PHE B O   
7111 C  CB  . PHE B 422 ? 0.1349 0.1827 0.1569 -0.0258 0.0290  -0.0345 421  PHE B CB  
7112 C  CG  . PHE B 422 ? 0.1645 0.1758 0.1356 -0.0017 0.0364  -0.0277 421  PHE B CG  
7113 C  CD1 . PHE B 422 ? 0.2455 0.1597 0.1265 0.0277  0.0070  -0.0369 421  PHE B CD1 
7114 C  CD2 . PHE B 422 ? 0.1651 0.1684 0.1621 0.0303  -0.0017 -0.0005 421  PHE B CD2 
7115 C  CE1 . PHE B 422 ? 0.1745 0.1510 0.1667 0.0556  0.0104  -0.0216 421  PHE B CE1 
7116 C  CE2 . PHE B 422 ? 0.1779 0.1793 0.1631 0.0061  -0.0056 -0.0100 421  PHE B CE2 
7117 C  CZ  . PHE B 422 ? 0.1726 0.1637 0.1683 0.0339  -0.0429 -0.0148 421  PHE B CZ  
7118 N  N   . ASP B 423 ? 0.0754 0.2165 0.1997 0.0034  0.0238  -0.0083 422  ASP B N   
7119 C  CA  . ASP B 423 ? 0.1400 0.2193 0.2262 0.0329  0.0308  -0.0123 422  ASP B CA  
7120 C  C   . ASP B 423 ? 0.2151 0.2029 0.2089 0.0253  0.0384  0.0098  422  ASP B C   
7121 O  O   . ASP B 423 ? 0.3420 0.2075 0.2224 0.0125  0.0570  0.0191  422  ASP B O   
7122 C  CB  . ASP B 423 ? 0.1726 0.2584 0.2631 0.0338  0.0014  -0.0320 422  ASP B CB  
7123 C  CG  . ASP B 423 ? 0.2367 0.3215 0.3072 0.0736  -0.0248 -0.0545 422  ASP B CG  
7124 O  OD1 . ASP B 423 ? 0.2807 0.3407 0.3527 0.0679  -0.0624 -0.0767 422  ASP B OD1 
7125 O  OD2 . ASP B 423 ? 0.3690 0.3600 0.3491 0.0823  -0.0119 -0.0563 422  ASP B OD2 
7126 N  N   . PHE B 424 ? 0.2098 0.1990 0.1874 0.0162  0.0214  0.0178  423  PHE B N   
7127 C  CA  . PHE B 424 ? 0.1772 0.1968 0.1957 0.0431  0.0080  0.0092  423  PHE B CA  
7128 C  C   . PHE B 424 ? 0.2627 0.1965 0.2060 0.0269  0.0575  -0.0083 423  PHE B C   
7129 O  O   . PHE B 424 ? 0.3083 0.2056 0.2230 0.0327  0.1050  -0.0338 423  PHE B O   
7130 C  CB  . PHE B 424 ? 0.1307 0.2227 0.2061 -0.0066 -0.0024 -0.0024 423  PHE B CB  
7131 C  CG  . PHE B 424 ? 0.1125 0.2223 0.2011 0.0098  0.0136  -0.0010 423  PHE B CG  
7132 C  CD1 . PHE B 424 ? 0.1613 0.2319 0.2190 0.0623  0.0295  -0.0079 423  PHE B CD1 
7133 C  CD2 . PHE B 424 ? 0.2051 0.2204 0.1969 -0.0018 -0.0432 -0.0051 423  PHE B CD2 
7134 C  CE1 . PHE B 424 ? 0.1934 0.2289 0.2015 0.0018  -0.0032 0.0036  423  PHE B CE1 
7135 C  CE2 . PHE B 424 ? 0.2351 0.2222 0.2030 0.0127  -0.0303 0.0030  423  PHE B CE2 
7136 C  CZ  . PHE B 424 ? 0.2169 0.2182 0.2034 0.0320  -0.0375 -0.0097 423  PHE B CZ  
7137 N  N   . GLU B 425 ? 0.2112 0.1769 0.2322 -0.0070 0.0333  0.0169  424  GLU B N   
7138 C  CA  . GLU B 425 ? 0.1608 0.2044 0.2744 -0.0032 -0.0039 0.0436  424  GLU B CA  
7139 C  C   . GLU B 425 ? 0.1664 0.2050 0.2559 0.0139  0.0172  0.0404  424  GLU B C   
7140 O  O   . GLU B 425 ? 0.1804 0.2370 0.2522 0.0028  0.0232  0.0150  424  GLU B O   
7141 C  CB  . GLU B 425 ? 0.1899 0.2367 0.3199 0.0020  -0.0307 0.0407  424  GLU B CB  
7142 C  CG  . GLU B 425 ? 0.2032 0.3171 0.3655 0.0320  -0.0944 0.0499  424  GLU B CG  
7143 C  CD  . GLU B 425 ? 0.3138 0.4048 0.4269 -0.0091 -0.0990 0.0448  424  GLU B CD  
7144 O  OE1 . GLU B 425 ? 0.3087 0.4490 0.3939 -0.0067 -0.1542 0.0652  424  GLU B OE1 
7145 O  OE2 . GLU B 425 ? 0.3084 0.4245 0.4759 0.0339  -0.0506 0.0301  424  GLU B OE2 
7146 N  N   . ASP B 426 ? 0.1686 0.1946 0.2202 0.0085  0.0103  0.0661  425  ASP B N   
7147 C  CA  . ASP B 426 ? 0.1689 0.2088 0.2162 -0.0400 -0.0030 0.0363  425  ASP B CA  
7148 C  C   . ASP B 426 ? 0.1369 0.2390 0.2071 -0.0240 -0.0395 0.0242  425  ASP B C   
7149 O  O   . ASP B 426 ? 0.1537 0.2468 0.2225 -0.0136 -0.0294 0.0357  425  ASP B O   
7150 C  CB  . ASP B 426 ? 0.1704 0.2221 0.2162 -0.0444 0.0273  0.0236  425  ASP B CB  
7151 C  CG  . ASP B 426 ? 0.1609 0.2388 0.2079 -0.0160 0.0293  -0.0035 425  ASP B CG  
7152 O  OD1 . ASP B 426 ? 0.1685 0.2517 0.2021 0.0035  -0.0043 -0.0294 425  ASP B OD1 
7153 O  OD2 . ASP B 426 ? 0.1778 0.2260 0.2272 0.0299  0.0316  -0.0196 425  ASP B OD2 
7154 N  N   . HIS B 427 ? 0.1693 0.2552 0.2333 -0.0187 -0.0418 0.0170  426  HIS B N   
7155 C  CA  . HIS B 427 ? 0.1757 0.2841 0.2100 -0.0189 0.0148  0.0024  426  HIS B CA  
7156 C  C   . HIS B 427 ? 0.1686 0.2706 0.2328 -0.0327 -0.0164 -0.0172 426  HIS B C   
7157 O  O   . HIS B 427 ? 0.1779 0.3111 0.2747 -0.0266 -0.0628 -0.0040 426  HIS B O   
7158 C  CB  . HIS B 427 ? 0.1492 0.2834 0.1975 -0.0064 0.0225  0.0079  426  HIS B CB  
7159 C  CG  . HIS B 427 ? 0.1242 0.2906 0.2042 -0.0149 0.0127  -0.0038 426  HIS B CG  
7160 N  ND1 . HIS B 427 ? 0.1805 0.2936 0.2215 -0.0355 0.0161  -0.0012 426  HIS B ND1 
7161 C  CD2 . HIS B 427 ? 0.1519 0.3142 0.1992 -0.0124 -0.0028 0.0020  426  HIS B CD2 
7162 C  CE1 . HIS B 427 ? 0.2525 0.3114 0.2276 -0.0411 -0.0022 0.0075  426  HIS B CE1 
7163 N  NE2 . HIS B 427 ? 0.2042 0.3139 0.2155 -0.0539 -0.0097 0.0021  426  HIS B NE2 
7164 N  N   . THR B 428 ? 0.1586 0.2303 0.1918 0.0044  -0.0256 -0.0276 427  THR B N   
7165 C  CA  . THR B 428 ? 0.1480 0.2178 0.2118 -0.0153 -0.0389 -0.0167 427  THR B CA  
7166 C  C   . THR B 428 ? 0.1789 0.2021 0.2231 0.0123  -0.0577 0.0189  427  THR B C   
7167 O  O   . THR B 428 ? 0.2291 0.1459 0.2794 -0.0247 -0.0144 -0.0169 427  THR B O   
7168 C  CB  . THR B 428 ? 0.1554 0.2342 0.1923 -0.0206 -0.0504 -0.0384 427  THR B CB  
7169 O  OG1 . THR B 428 ? 0.1484 0.2558 0.2164 0.0025  -0.0419 -0.0503 427  THR B OG1 
7170 C  CG2 . THR B 428 ? 0.1391 0.2328 0.1631 -0.0620 0.0187  -0.0079 427  THR B CG2 
7171 N  N   . ASN B 429 ? 0.1701 0.2197 0.1875 0.0155  -0.0497 0.0097  428  ASN B N   
7172 C  CA  . ASN B 429 ? 0.1054 0.2493 0.2077 -0.0146 0.0037  0.0090  428  ASN B CA  
7173 C  C   . ASN B 429 ? 0.1298 0.2174 0.2153 -0.0473 -0.0257 -0.0035 428  ASN B C   
7174 O  O   . ASN B 429 ? 0.1466 0.2612 0.2525 -0.0064 -0.0152 -0.0027 428  ASN B O   
7175 C  CB  . ASN B 429 ? 0.1456 0.2847 0.2130 -0.0123 0.0429  0.0123  428  ASN B CB  
7176 C  CG  . ASN B 429 ? 0.2711 0.3380 0.3007 -0.0411 0.0304  0.0489  428  ASN B CG  
7177 O  OD1 . ASN B 429 ? 0.2940 0.3333 0.3248 0.0186  0.0076  0.0199  428  ASN B OD1 
7178 N  ND2 . ASN B 429 ? 0.3452 0.3984 0.3459 -0.0385 0.0125  0.0673  428  ASN B ND2 
7179 N  N   . TYR B 430 ? 0.0703 0.1853 0.2222 -0.0294 -0.0047 0.0089  429  TYR B N   
7180 C  CA  . TYR B 430 ? 0.0727 0.1826 0.2278 0.0050  0.0301  -0.0116 429  TYR B CA  
7181 C  C   . TYR B 430 ? 0.1500 0.1755 0.2365 -0.0090 -0.0160 0.0221  429  TYR B C   
7182 O  O   . TYR B 430 ? 0.1920 0.1809 0.2192 -0.0339 -0.0145 0.0032  429  TYR B O   
7183 C  CB  . TYR B 430 ? 0.1216 0.1815 0.2341 -0.0093 0.0110  -0.0145 429  TYR B CB  
7184 C  CG  . TYR B 430 ? 0.0900 0.1771 0.2218 0.0137  -0.0139 -0.0219 429  TYR B CG  
7185 C  CD1 . TYR B 430 ? 0.1197 0.1321 0.2108 -0.0099 0.0169  0.0086  429  TYR B CD1 
7186 C  CD2 . TYR B 430 ? 0.0869 0.1754 0.2233 -0.0138 -0.0335 -0.0236 429  TYR B CD2 
7187 C  CE1 . TYR B 430 ? 0.1197 0.1453 0.2048 -0.0399 -0.0328 0.0000  429  TYR B CE1 
7188 C  CE2 . TYR B 430 ? 0.1291 0.1313 0.2200 0.0424  0.0147  -0.0134 429  TYR B CE2 
7189 C  CZ  . TYR B 430 ? 0.1540 0.1449 0.2141 0.0043  0.0197  -0.0253 429  TYR B CZ  
7190 O  OH  . TYR B 430 ? 0.1984 0.1334 0.2074 0.0107  0.0057  -0.0186 429  TYR B OH  
7191 N  N   . GLU B 431 ? 0.1465 0.1408 0.2556 -0.0286 -0.0205 0.0783  430  GLU B N   
7192 C  CA  . GLU B 431 ? 0.1068 0.1679 0.2697 -0.0047 -0.0273 0.0527  430  GLU B CA  
7193 C  C   . GLU B 431 ? 0.1140 0.1720 0.2440 -0.0305 -0.0069 0.0173  430  GLU B C   
7194 O  O   . GLU B 431 ? 0.1675 0.1640 0.2558 -0.0062 0.0070  0.0175  430  GLU B O   
7195 C  CB  . GLU B 431 ? 0.2564 0.2172 0.3130 -0.0660 -0.0199 0.0765  430  GLU B CB  
7196 C  CG  . GLU B 431 ? 0.4445 0.2493 0.4029 -0.0890 -0.0050 0.0978  430  GLU B CG  
7197 C  CD  . GLU B 431 ? 0.7332 0.3189 0.4735 -0.0951 -0.0271 0.0882  430  GLU B CD  
7198 O  OE1 . GLU B 431 ? 0.8129 0.3318 0.5142 -0.1283 -0.0499 0.0658  430  GLU B OE1 
7199 O  OE2 . GLU B 431 ? 0.8694 0.3384 0.5020 -0.1143 -0.0046 0.0932  430  GLU B OE2 
7200 N  N   . LEU B 432 ? 0.1374 0.1430 0.2217 -0.0378 -0.0077 -0.0043 431  LEU B N   
7201 C  CA  . LEU B 432 ? 0.1581 0.1658 0.2017 -0.0546 -0.0212 -0.0237 431  LEU B CA  
7202 C  C   . LEU B 432 ? 0.1323 0.1608 0.2030 -0.0557 0.0093  0.0000  431  LEU B C   
7203 O  O   . LEU B 432 ? 0.1805 0.1717 0.2186 -0.0261 0.0240  0.0160  431  LEU B O   
7204 C  CB  . LEU B 432 ? 0.1392 0.1971 0.2105 -0.0139 -0.0621 -0.0470 431  LEU B CB  
7205 C  CG  . LEU B 432 ? 0.1686 0.1977 0.2099 -0.0021 -0.0153 -0.0544 431  LEU B CG  
7206 C  CD1 . LEU B 432 ? 0.1560 0.1636 0.2515 0.0054  0.0198  -0.0330 431  LEU B CD1 
7207 C  CD2 . LEU B 432 ? 0.2843 0.2137 0.2067 0.0529  0.0101  -0.0766 431  LEU B CD2 
7208 N  N   . ASP B 433 ? 0.0787 0.1363 0.2006 0.0007  -0.0021 -0.0116 432  ASP B N   
7209 C  CA  . ASP B 433 ? 0.1505 0.1641 0.1883 -0.0213 0.0016  -0.0301 432  ASP B CA  
7210 C  C   . ASP B 433 ? 0.1453 0.1923 0.2059 0.0075  -0.0280 -0.0289 432  ASP B C   
7211 O  O   . ASP B 433 ? 0.1703 0.2024 0.2243 -0.0069 -0.0166 -0.0425 432  ASP B O   
7212 C  CB  . ASP B 433 ? 0.1573 0.1932 0.2090 0.0089  -0.0463 -0.0478 432  ASP B CB  
7213 C  CG  . ASP B 433 ? 0.2447 0.2058 0.2202 0.0146  -0.0392 -0.0523 432  ASP B CG  
7214 O  OD1 . ASP B 433 ? 0.2271 0.2167 0.2351 0.0188  0.0010  -0.0388 432  ASP B OD1 
7215 O  OD2 . ASP B 433 ? 0.2996 0.2185 0.2416 0.0535  -0.0717 -0.0478 432  ASP B OD2 
7216 N  N   . ILE B 434 ? 0.0621 0.1736 0.1874 -0.0221 -0.0346 -0.0021 433  ILE B N   
7217 C  CA  . ILE B 434 ? 0.0572 0.1797 0.1626 -0.0149 0.0013  -0.0284 433  ILE B CA  
7218 C  C   . ILE B 434 ? 0.1387 0.1861 0.1833 -0.0232 0.0012  -0.0083 433  ILE B C   
7219 O  O   . ILE B 434 ? 0.2340 0.1788 0.1921 -0.0193 0.0029  0.0164  433  ILE B O   
7220 C  CB  . ILE B 434 ? 0.0830 0.1748 0.1726 0.0289  -0.0164 -0.0625 433  ILE B CB  
7221 C  CG1 . ILE B 434 ? 0.1447 0.1729 0.1443 0.0285  -0.0055 -0.0626 433  ILE B CG1 
7222 C  CG2 . ILE B 434 ? 0.0918 0.1778 0.1793 0.0267  -0.0098 -0.0534 433  ILE B CG2 
7223 C  CD1 . ILE B 434 ? 0.1438 0.1785 0.1313 -0.0197 0.0376  -0.0545 433  ILE B CD1 
7224 N  N   . LYS B 435 ? 0.1225 0.2008 0.1657 0.0094  0.0453  -0.0164 434  LYS B N   
7225 C  CA  . LYS B 435 ? 0.1329 0.2026 0.1582 0.0328  0.0227  -0.0267 434  LYS B CA  
7226 C  C   . LYS B 435 ? 0.0795 0.1805 0.1757 -0.0044 -0.0405 -0.0072 434  LYS B C   
7227 O  O   . LYS B 435 ? 0.1584 0.1683 0.2017 -0.0250 -0.0251 -0.0256 434  LYS B O   
7228 C  CB  . LYS B 435 ? 0.1952 0.2224 0.1534 0.0427  0.0033  -0.0480 434  LYS B CB  
7229 C  CG  . LYS B 435 ? 0.2513 0.2570 0.1547 0.0615  0.0778  -0.0379 434  LYS B CG  
7230 C  CD  . LYS B 435 ? 0.2944 0.2695 0.2188 0.0715  0.0632  -0.0236 434  LYS B CD  
7231 C  CE  . LYS B 435 ? 0.3991 0.2980 0.2894 0.0643  0.0023  -0.0348 434  LYS B CE  
7232 N  NZ  . LYS B 435 ? 0.3797 0.3326 0.3175 0.0545  -0.0081 -0.0289 434  LYS B NZ  
7233 N  N   . GLU B 436 ? 0.1367 0.1664 0.1564 0.0193  -0.0496 0.0066  435  GLU B N   
7234 C  CA  . GLU B 436 ? 0.1028 0.1787 0.1393 0.0162  -0.0037 -0.0016 435  GLU B CA  
7235 C  C   . GLU B 436 ? 0.1108 0.1643 0.1492 0.0112  0.0100  -0.0410 435  GLU B C   
7236 O  O   . GLU B 436 ? 0.2043 0.1402 0.1916 0.0282  0.0170  -0.0424 435  GLU B O   
7237 C  CB  . GLU B 436 ? 0.1557 0.1649 0.1335 0.0271  0.0029  0.0123  435  GLU B CB  
7238 C  CG  . GLU B 436 ? 0.1586 0.1741 0.1485 -0.0046 0.0506  0.0116  435  GLU B CG  
7239 C  CD  . GLU B 436 ? 0.1127 0.1363 0.1734 -0.0368 0.0305  0.0097  435  GLU B CD  
7240 O  OE1 . GLU B 436 ? 0.1528 0.1348 0.1698 -0.0268 0.0016  -0.0168 435  GLU B OE1 
7241 O  OE2 . GLU B 436 ? 0.1399 0.1463 0.2018 -0.0465 0.0292  -0.0080 435  GLU B OE2 
7242 N  N   . THR B 437 ? 0.1176 0.1906 0.1487 0.0086  -0.0078 -0.0345 436  THR B N   
7243 C  CA  . THR B 437 ? 0.1551 0.1885 0.1435 -0.0224 -0.0008 -0.0458 436  THR B CA  
7244 C  C   . THR B 437 ? 0.1374 0.2044 0.1789 0.0045  -0.0186 -0.0486 436  THR B C   
7245 O  O   . THR B 437 ? 0.2114 0.2278 0.2030 -0.0117 0.0019  -0.0416 436  THR B O   
7246 C  CB  . THR B 437 ? 0.1946 0.1809 0.1504 -0.0071 -0.0484 -0.0433 436  THR B CB  
7247 O  OG1 . THR B 437 ? 0.1979 0.2038 0.1748 -0.0098 0.0158  0.0127  436  THR B OG1 
7248 C  CG2 . THR B 437 ? 0.1450 0.2196 0.1388 0.0011  -0.0635 -0.0392 436  THR B CG2 
7249 N  N   . LEU B 438 ? 0.1200 0.1917 0.1401 0.0284  -0.0586 -0.0433 437  LEU B N   
7250 C  CA  . LEU B 438 ? 0.1124 0.1756 0.1905 0.0753  -0.0154 -0.0334 437  LEU B CA  
7251 C  C   . LEU B 438 ? 0.1786 0.1826 0.1956 0.0637  0.0026  -0.0271 437  LEU B C   
7252 O  O   . LEU B 438 ? 0.1845 0.1562 0.1876 0.0247  0.0370  -0.0317 437  LEU B O   
7253 C  CB  . LEU B 438 ? 0.1480 0.1805 0.2024 0.0886  -0.0021 -0.0449 437  LEU B CB  
7254 C  CG  . LEU B 438 ? 0.1308 0.1998 0.1957 0.0385  0.0088  0.0000  437  LEU B CG  
7255 C  CD1 . LEU B 438 ? 0.1638 0.2244 0.1955 0.0493  0.0211  0.0158  437  LEU B CD1 
7256 C  CD2 . LEU B 438 ? 0.2369 0.1718 0.1760 0.0590  -0.0755 -0.0228 437  LEU B CD2 
7257 N  N   . THR B 439 ? 0.2157 0.1605 0.1997 0.0464  0.0130  0.0271  438  THR B N   
7258 C  CA  . THR B 439 ? 0.1008 0.1642 0.1785 -0.0513 0.0531  -0.0040 438  THR B CA  
7259 C  C   . THR B 439 ? 0.1028 0.1568 0.1594 -0.0325 0.0167  -0.0061 438  THR B C   
7260 O  O   . THR B 439 ? 0.1461 0.1504 0.1736 -0.0255 0.0233  -0.0215 438  THR B O   
7261 C  CB  . THR B 439 ? 0.1713 0.2170 0.1501 -0.1090 0.0108  -0.0388 438  THR B CB  
7262 O  OG1 . THR B 439 ? 0.2175 0.2535 0.1294 -0.0550 0.0079  -0.0499 438  THR B OG1 
7263 C  CG2 . THR B 439 ? 0.2092 0.2039 0.1695 -0.0355 0.0258  -0.0100 438  THR B CG2 
7264 N  N   . LEU B 440 ? 0.1494 0.1594 0.1539 -0.0058 -0.0422 0.0036  439  LEU B N   
7265 C  CA  . LEU B 440 ? 0.1564 0.1667 0.1231 0.0288  -0.0623 0.0219  439  LEU B CA  
7266 C  C   . LEU B 440 ? 0.0956 0.1790 0.1492 0.0142  -0.0591 -0.0024 439  LEU B C   
7267 O  O   . LEU B 440 ? 0.1918 0.1647 0.1771 0.0043  -0.0352 -0.0304 439  LEU B O   
7268 C  CB  . LEU B 440 ? 0.1796 0.1793 0.1271 0.0137  -0.0176 -0.0061 439  LEU B CB  
7269 C  CG  . LEU B 440 ? 0.1429 0.1586 0.1418 0.0288  -0.0032 0.0073  439  LEU B CG  
7270 C  CD1 . LEU B 440 ? 0.1654 0.1595 0.1463 0.0455  0.0168  0.0084  439  LEU B CD1 
7271 C  CD2 . LEU B 440 ? 0.1631 0.1508 0.1611 0.0318  0.0253  -0.0179 439  LEU B CD2 
7272 N  N   . LYS B 441 ? 0.0944 0.1760 0.1600 0.0060  -0.0549 -0.0187 440  LYS B N   
7273 C  CA  . LYS B 441 ? 0.1144 0.1843 0.1765 0.0273  -0.0300 -0.0165 440  LYS B CA  
7274 C  C   . LYS B 441 ? 0.1593 0.1845 0.2003 0.0411  -0.0211 -0.0270 440  LYS B C   
7275 O  O   . LYS B 441 ? 0.1688 0.1708 0.2056 -0.0020 -0.0308 -0.0269 440  LYS B O   
7276 C  CB  . LYS B 441 ? 0.2138 0.2074 0.2040 0.0125  0.0169  0.0117  440  LYS B CB  
7277 C  CG  . LYS B 441 ? 0.2659 0.2723 0.2454 0.0417  0.0597  0.0060  440  LYS B CG  
7278 C  CD  . LYS B 441 ? 0.3175 0.3241 0.3061 0.0491  0.0593  0.0141  440  LYS B CD  
7279 C  CE  . LYS B 441 ? 0.4464 0.3652 0.3591 0.0201  0.1082  -0.0219 440  LYS B CE  
7280 N  NZ  . LYS B 441 ? 0.4684 0.3718 0.3986 -0.0263 0.1159  -0.0748 440  LYS B NZ  
7281 N  N   . PRO B 442 ? 0.1439 0.1640 0.1895 0.0116  -0.0103 -0.0658 441  PRO B N   
7282 C  CA  . PRO B 442 ? 0.1145 0.1776 0.1992 0.0184  0.0174  -0.0586 441  PRO B CA  
7283 C  C   . PRO B 442 ? 0.1642 0.1924 0.2067 0.0059  -0.0252 -0.0498 441  PRO B C   
7284 O  O   . PRO B 442 ? 0.2042 0.2239 0.2109 -0.0100 -0.0435 -0.0250 441  PRO B O   
7285 C  CB  . PRO B 442 ? 0.1668 0.1560 0.1991 0.0277  0.0091  -0.0677 441  PRO B CB  
7286 C  CG  . PRO B 442 ? 0.1941 0.1303 0.1999 0.0267  -0.0193 -0.0534 441  PRO B CG  
7287 C  CD  . PRO B 442 ? 0.1248 0.1419 0.1813 0.0735  -0.0274 -0.0306 441  PRO B CD  
7288 N  N   . GLU B 443 ? 0.1519 0.1383 0.2070 -0.0099 -0.0250 -0.0342 442  GLU B N   
7289 C  CA  . GLU B 443 ? 0.1940 0.1323 0.2285 0.0422  -0.0162 -0.0683 442  GLU B CA  
7290 C  C   . GLU B 443 ? 0.1372 0.1507 0.1905 0.0346  -0.0728 -0.0420 442  GLU B C   
7291 O  O   . GLU B 443 ? 0.1443 0.1662 0.1840 -0.0158 -0.0118 -0.0216 442  GLU B O   
7292 C  CB  . GLU B 443 ? 0.1926 0.1585 0.2551 0.0826  -0.0447 -0.0733 442  GLU B CB  
7293 C  CG  . GLU B 443 ? 0.3209 0.1669 0.3127 0.0820  -0.0275 -0.0930 442  GLU B CG  
7294 C  CD  . GLU B 443 ? 0.4888 0.2207 0.3349 0.1043  -0.0393 -0.0893 442  GLU B CD  
7295 O  OE1 . GLU B 443 ? 0.4617 0.2174 0.3391 0.0789  -0.0453 -0.0441 442  GLU B OE1 
7296 O  OE2 . GLU B 443 ? 0.6622 0.2744 0.3741 0.1326  -0.0574 -0.0784 442  GLU B OE2 
7297 N  N   . GLY B 444 ? 0.1841 0.1625 0.2092 -0.0031 -0.1168 -0.0078 443  GLY B N   
7298 C  CA  . GLY B 444 ? 0.1831 0.1844 0.2022 -0.0030 -0.0797 0.0006  443  GLY B CA  
7299 C  C   . GLY B 444 ? 0.2146 0.2094 0.1815 -0.0022 -0.0184 -0.0141 443  GLY B C   
7300 O  O   . GLY B 444 ? 0.2029 0.2546 0.1743 0.0194  -0.0303 -0.0452 443  GLY B O   
7301 N  N   . PHE B 445 ? 0.2237 0.1266 0.1866 0.0029  -0.0184 -0.0233 444  PHE B N   
7302 C  CA  . PHE B 445 ? 0.1997 0.1371 0.1747 0.0266  0.0136  -0.0089 444  PHE B CA  
7303 C  C   . PHE B 445 ? 0.1702 0.1545 0.1875 -0.0162 -0.0148 0.0090  444  PHE B C   
7304 O  O   . PHE B 445 ? 0.1676 0.1643 0.1655 -0.0273 -0.0051 -0.0150 444  PHE B O   
7305 C  CB  . PHE B 445 ? 0.2256 0.1475 0.1747 0.0373  -0.0074 -0.0175 444  PHE B CB  
7306 C  CG  . PHE B 445 ? 0.1836 0.1589 0.1631 0.0575  -0.0016 0.0045  444  PHE B CG  
7307 C  CD1 . PHE B 445 ? 0.2108 0.1684 0.1554 0.0838  0.0314  0.0478  444  PHE B CD1 
7308 C  CD2 . PHE B 445 ? 0.1943 0.1796 0.1440 0.0157  0.0404  0.0201  444  PHE B CD2 
7309 C  CE1 . PHE B 445 ? 0.1772 0.1797 0.1508 0.0214  0.0094  0.0323  444  PHE B CE1 
7310 C  CE2 . PHE B 445 ? 0.1129 0.1854 0.1527 0.0027  0.0148  -0.0007 444  PHE B CE2 
7311 C  CZ  . PHE B 445 ? 0.1247 0.1912 0.1735 -0.0027 0.0039  0.0016  444  PHE B CZ  
7312 N  N   . VAL B 446 ? 0.1562 0.1690 0.1917 0.0071  -0.0169 0.0385  445  VAL B N   
7313 C  CA  . VAL B 446 ? 0.1893 0.1652 0.2034 0.0131  -0.0362 0.0120  445  VAL B CA  
7314 C  C   . VAL B 446 ? 0.2001 0.1859 0.1991 0.0315  -0.0477 0.0302  445  VAL B C   
7315 O  O   . VAL B 446 ? 0.2405 0.1877 0.2020 0.0137  -0.0069 0.0583  445  VAL B O   
7316 C  CB  . VAL B 446 ? 0.1698 0.1688 0.2288 0.0443  0.0474  -0.0261 445  VAL B CB  
7317 C  CG1 . VAL B 446 ? 0.2033 0.2016 0.2346 0.0243  -0.0041 -0.0491 445  VAL B CG1 
7318 C  CG2 . VAL B 446 ? 0.1981 0.1319 0.2567 0.0452  0.0344  -0.0107 445  VAL B CG2 
7319 N  N   . VAL B 447 ? 0.1284 0.1461 0.2029 0.0176  -0.0542 0.0092  446  VAL B N   
7320 C  CA  . VAL B 447 ? 0.1750 0.1925 0.1708 0.0232  -0.0393 -0.0084 446  VAL B CA  
7321 C  C   . VAL B 447 ? 0.1234 0.2105 0.1729 0.0461  -0.0175 -0.0045 446  VAL B C   
7322 O  O   . VAL B 447 ? 0.1755 0.2132 0.1891 0.0170  -0.0208 -0.0238 446  VAL B O   
7323 C  CB  . VAL B 447 ? 0.1477 0.1900 0.1565 -0.0157 0.0222  0.0118  446  VAL B CB  
7324 C  CG1 . VAL B 447 ? 0.2619 0.1780 0.1544 -0.0098 -0.0183 0.0170  446  VAL B CG1 
7325 C  CG2 . VAL B 447 ? 0.1513 0.2006 0.1298 0.0394  0.0239  -0.0214 446  VAL B CG2 
7326 N  N   . LYS B 448 ? 0.1626 0.2206 0.1479 0.0454  -0.0562 -0.0096 447  LYS B N   
7327 C  CA  . LYS B 448 ? 0.1718 0.2217 0.1776 -0.0015 -0.0608 -0.0165 447  LYS B CA  
7328 C  C   . LYS B 448 ? 0.2337 0.2040 0.1818 0.0005  -0.0141 -0.0337 447  LYS B C   
7329 O  O   . LYS B 448 ? 0.2460 0.1833 0.1824 -0.0043 0.0019  -0.0303 447  LYS B O   
7330 C  CB  . LYS B 448 ? 0.1955 0.2616 0.1881 -0.0456 -0.0459 -0.0529 447  LYS B CB  
7331 C  CG  . LYS B 448 ? 0.2091 0.3062 0.2062 -0.0920 -0.0833 -0.0241 447  LYS B CG  
7332 C  CD  . LYS B 448 ? 0.2252 0.3087 0.2439 -0.1401 -0.0573 -0.0004 447  LYS B CD  
7333 C  CE  . LYS B 448 ? 0.2668 0.4031 0.2602 -0.1484 -0.0926 0.0085  447  LYS B CE  
7334 N  NZ  . LYS B 448 ? 0.3790 0.4568 0.2731 -0.1463 -0.0743 0.0369  447  LYS B NZ  
7335 N  N   . ALA B 449 ? 0.2515 0.1901 0.1750 0.0025  0.0180  -0.0290 448  ALA B N   
7336 C  CA  . ALA B 449 ? 0.2451 0.1743 0.2161 0.0262  0.0276  -0.0036 448  ALA B CA  
7337 C  C   . ALA B 449 ? 0.4260 0.1935 0.2265 0.0622  0.0034  -0.0081 448  ALA B C   
7338 O  O   . ALA B 449 ? 0.6810 0.2125 0.2185 0.1159  0.0154  -0.0154 448  ALA B O   
7339 C  CB  . ALA B 449 ? 0.2775 0.2097 0.2454 -0.0100 0.0306  -0.0082 448  ALA B CB  
7340 N  N   . LYS B 450 ? 0.2661 0.1939 0.2614 -0.0263 -0.0567 0.0305  449  LYS B N   
7341 C  CA  . LYS B 450 ? 0.2615 0.2415 0.3065 0.0145  -0.0849 0.0296  449  LYS B CA  
7342 C  C   . LYS B 450 ? 0.2633 0.2181 0.2283 -0.0326 -0.0615 0.0332  449  LYS B C   
7343 O  O   . LYS B 450 ? 0.2865 0.2615 0.1787 -0.0068 -0.0481 0.0422  449  LYS B O   
7344 C  CB  . LYS B 450 ? 0.2970 0.3190 0.4025 0.0792  -0.0973 0.0225  449  LYS B CB  
7345 C  CG  . LYS B 450 ? 0.4483 0.3764 0.4886 0.0814  -0.0576 -0.0020 449  LYS B CG  
7346 C  CD  . LYS B 450 ? 0.5240 0.4164 0.5411 0.0818  -0.0395 -0.0193 449  LYS B CD  
7347 C  CE  . LYS B 450 ? 0.6144 0.4284 0.5730 0.0964  -0.0123 -0.0263 449  LYS B CE  
7348 N  NZ  . LYS B 450 ? 0.7285 0.4648 0.5856 0.0735  0.0134  -0.0389 449  LYS B NZ  
7349 N  N   . SER B 451 ? 0.2399 0.1868 0.1812 -0.0045 -0.0612 0.0089  450  SER B N   
7350 C  CA  . SER B 451 ? 0.2406 0.2004 0.1857 -0.0137 -0.0069 0.0015  450  SER B CA  
7351 C  C   . SER B 451 ? 0.2184 0.2004 0.2080 0.0279  -0.0257 0.0010  450  SER B C   
7352 O  O   . SER B 451 ? 0.2308 0.2487 0.2427 0.0465  -0.0192 -0.0016 450  SER B O   
7353 C  CB  . SER B 451 ? 0.2537 0.2333 0.1900 0.0138  -0.0115 0.0018  450  SER B CB  
7354 O  OG  . SER B 451 ? 0.2937 0.2479 0.1896 0.0170  -0.0189 -0.0027 450  SER B OG  
7355 N  N   . LYS B 452 ? 0.2121 0.1381 0.2038 0.0230  -0.0598 -0.0203 451  LYS B N   
7356 C  CA  . LYS B 452 ? 0.3012 0.1886 0.2230 0.0528  -0.0323 -0.0017 451  LYS B CA  
7357 C  C   . LYS B 452 ? 0.2933 0.2293 0.2558 0.0891  -0.0265 0.0117  451  LYS B C   
7358 O  O   . LYS B 452 ? 0.2721 0.2448 0.2966 0.1157  0.0208  0.0059  451  LYS B O   
7359 C  CB  . LYS B 452 ? 0.2663 0.2185 0.2423 0.0357  0.0370  -0.0009 451  LYS B CB  
7360 C  CG  . LYS B 452 ? 0.3164 0.2702 0.2660 0.0095  0.0280  -0.0013 451  LYS B CG  
7361 C  CD  . LYS B 452 ? 0.2895 0.3432 0.2942 0.0102  0.0911  0.0012  451  LYS B CD  
7362 C  CE  . LYS B 452 ? 0.2343 0.4165 0.3445 0.0277  0.1616  -0.0185 451  LYS B CE  
7363 N  NZ  . LYS B 452 ? 0.4398 0.4668 0.3900 0.0107  0.1468  -0.0171 451  LYS B NZ  
7364 N  N   . LYS B 453 ? 0.2625 0.2648 0.2173 0.0606  -0.0531 0.0082  452  LYS B N   
7365 C  CA  . LYS B 453 ? 0.3021 0.2740 0.2432 0.0733  -0.1310 0.0382  452  LYS B CA  
7366 C  C   . LYS B 453 ? 0.3124 0.2746 0.2458 0.0712  -0.0890 0.0512  452  LYS B C   
7367 O  O   . LYS B 453 ? 0.3373 0.2757 0.2532 0.0534  -0.0896 0.0468  452  LYS B O   
7368 C  CB  . LYS B 453 ? 0.3836 0.3168 0.2518 0.0568  -0.1322 0.0181  452  LYS B CB  
7369 C  CG  . LYS B 453 ? 0.4452 0.3797 0.3093 0.0453  -0.0759 -0.0020 452  LYS B CG  
7370 C  CD  . LYS B 453 ? 0.5509 0.4159 0.3420 0.0218  -0.1142 -0.0232 452  LYS B CD  
7371 C  CE  . LYS B 453 ? 0.6159 0.4449 0.3517 0.0228  -0.1310 -0.0282 452  LYS B CE  
7372 N  NZ  . LYS B 453 ? 0.6812 0.4764 0.3600 0.0092  -0.1505 -0.0335 452  LYS B NZ  
7373 N  N   . ILE B 454 ? 0.2484 0.2618 0.2197 0.0394  -0.0219 0.0416  453  ILE B N   
7374 C  CA  . ILE B 454 ? 0.2528 0.2679 0.2412 0.0275  -0.0136 0.0229  453  ILE B CA  
7375 C  C   . ILE B 454 ? 0.2946 0.2792 0.2384 0.0269  -0.0341 0.0365  453  ILE B C   
7376 O  O   . ILE B 454 ? 0.3068 0.2808 0.2043 -0.0015 -0.0427 0.0041  453  ILE B O   
7377 C  CB  . ILE B 454 ? 0.2427 0.2849 0.2569 0.0113  -0.0293 0.0023  453  ILE B CB  
7378 C  CG1 . ILE B 454 ? 0.2673 0.3285 0.2620 0.0179  -0.0451 0.0069  453  ILE B CG1 
7379 C  CG2 . ILE B 454 ? 0.2203 0.2815 0.2663 -0.0139 -0.0469 -0.0266 453  ILE B CG2 
7380 C  CD1 . ILE B 454 ? 0.3052 0.3600 0.2836 0.0288  0.0043  -0.0121 453  ILE B CD1 
7381 N  N   . PRO B 455 ? 0.3415 0.2798 0.2889 0.0535  -0.0017 0.0862  454  PRO B N   
7382 C  CA  . PRO B 455 ? 0.3604 0.2950 0.2924 0.0461  -0.0134 0.1013  454  PRO B CA  
7383 C  C   . PRO B 455 ? 0.3384 0.3126 0.2855 0.0217  -0.0218 0.0388  454  PRO B C   
7384 O  O   . PRO B 455 ? 0.3213 0.3218 0.2895 0.0288  0.0132  -0.0182 454  PRO B O   
7385 C  CB  . PRO B 455 ? 0.4479 0.2895 0.3102 0.0373  0.0012  0.1368  454  PRO B CB  
7386 C  CG  . PRO B 455 ? 0.4483 0.3033 0.3227 0.0596  0.0143  0.1217  454  PRO B CG  
7387 C  CD  . PRO B 455 ? 0.3945 0.2892 0.3155 0.0507  0.0271  0.1266  454  PRO B CD  
7388 N  N   . LEU B 456 ? 0.3136 0.2993 0.2628 0.0249  -0.0033 0.0215  455  LEU B N   
7389 C  CA  . LEU B 456 ? 0.3596 0.2966 0.2675 0.0298  -0.0363 0.0434  455  LEU B CA  
7390 C  C   . LEU B 456 ? 0.4570 0.3332 0.2839 -0.0105 -0.0474 0.0649  455  LEU B C   
7391 O  O   . LEU B 456 ? 0.5077 0.3405 0.2627 -0.0132 -0.0447 0.1144  455  LEU B O   
7392 C  CB  . LEU B 456 ? 0.4212 0.2625 0.2653 0.0537  -0.0693 0.0338  455  LEU B CB  
7393 C  CG  . LEU B 456 ? 0.4006 0.2197 0.2226 0.1304  -0.0858 0.0041  455  LEU B CG  
7394 C  CD1 . LEU B 456 ? 0.4131 0.1912 0.2343 0.1164  -0.0428 -0.0245 455  LEU B CD1 
7395 C  CD2 . LEU B 456 ? 0.3696 0.2388 0.1966 0.1121  -0.0477 -0.0425 455  LEU B CD2 
7396 O  OXT . LEU B 456 ? 0.5498 0.3615 0.2999 -0.0177 0.0073  0.0406  455  LEU B OXT 
7397 C  CHA . HEM C .   ? 0.1332 0.1383 0.1080 -0.0030 0.0270  0.0157  501  HEM A CHA 
7398 C  CHB . HEM C .   ? 0.1807 0.1429 0.1409 0.0047  -0.0342 -0.0259 501  HEM A CHB 
7399 C  CHC . HEM C .   ? 0.1844 0.1731 0.1314 -0.0139 0.0384  -0.0213 501  HEM A CHC 
7400 C  CHD . HEM C .   ? 0.1690 0.1461 0.1269 -0.0025 -0.0275 -0.0408 501  HEM A CHD 
7401 C  C1A . HEM C .   ? 0.1048 0.1611 0.1202 -0.0142 0.0319  0.0118  501  HEM A C1A 
7402 C  C2A . HEM C .   ? 0.1360 0.1336 0.1198 -0.0028 -0.0178 -0.0031 501  HEM A C2A 
7403 C  C3A . HEM C .   ? 0.1284 0.1143 0.1175 0.0245  0.0122  0.0054  501  HEM A C3A 
7404 C  C4A . HEM C .   ? 0.1455 0.1204 0.1267 0.0151  0.0052  -0.0287 501  HEM A C4A 
7405 C  CMA . HEM C .   ? 0.1283 0.1256 0.1268 0.0252  0.0513  -0.0165 501  HEM A CMA 
7406 C  CAA . HEM C .   ? 0.1390 0.1287 0.1171 -0.0028 -0.0053 -0.0098 501  HEM A CAA 
7407 C  CBA . HEM C .   ? 0.1905 0.1003 0.1310 0.0052  0.0124  -0.0027 501  HEM A CBA 
7408 C  CGA . HEM C .   ? 0.1045 0.1099 0.1243 0.0145  0.0057  0.0033  501  HEM A CGA 
7409 O  O1A . HEM C .   ? 0.2220 0.1156 0.1304 -0.0546 -0.0475 -0.0104 501  HEM A O1A 
7410 O  O2A . HEM C .   ? 0.1549 0.1338 0.1120 -0.0138 -0.0378 -0.0136 501  HEM A O2A 
7411 C  C1B . HEM C .   ? 0.1361 0.1440 0.1418 0.0400  0.0180  -0.0428 501  HEM A C1B 
7412 C  C2B . HEM C .   ? 0.1088 0.1131 0.1503 -0.0059 0.0207  -0.0145 501  HEM A C2B 
7413 C  C3B . HEM C .   ? 0.1866 0.1181 0.1551 -0.0306 0.0228  0.0002  501  HEM A C3B 
7414 C  C4B . HEM C .   ? 0.1753 0.1408 0.1429 -0.0222 -0.0005 -0.0161 501  HEM A C4B 
7415 C  CMB . HEM C .   ? 0.1369 0.1664 0.1709 -0.0159 0.0357  0.0084  501  HEM A CMB 
7416 C  CAB . HEM C .   ? 0.1587 0.1132 0.1756 -0.0739 -0.0109 0.0273  501  HEM A CAB 
7417 C  CBB . HEM C .   ? 0.1893 0.1277 0.1577 -0.0737 -0.0157 -0.0044 501  HEM A CBB 
7418 C  C1C . HEM C .   ? 0.1665 0.1932 0.1163 -0.0174 -0.0120 -0.0216 501  HEM A C1C 
7419 C  C2C . HEM C .   ? 0.2085 0.2168 0.1129 -0.0183 0.0216  -0.0364 501  HEM A C2C 
7420 C  C3C . HEM C .   ? 0.2080 0.1872 0.1131 -0.0007 0.0188  -0.0312 501  HEM A C3C 
7421 C  C4C . HEM C .   ? 0.1433 0.1781 0.1218 -0.0099 -0.0229 -0.0307 501  HEM A C4C 
7422 C  CMC . HEM C .   ? 0.2569 0.2228 0.1323 -0.0268 0.0559  -0.0639 501  HEM A CMC 
7423 C  CAC . HEM C .   ? 0.2220 0.1307 0.1258 0.0433  0.0105  -0.0590 501  HEM A CAC 
7424 C  CBC . HEM C .   ? 0.2153 0.1390 0.1459 0.0727  0.0155  -0.0478 501  HEM A CBC 
7425 C  C1D . HEM C .   ? 0.1248 0.1452 0.1338 -0.0064 0.0288  -0.0605 501  HEM A C1D 
7426 C  C2D . HEM C .   ? 0.1306 0.1591 0.1384 0.0177  0.0110  -0.0473 501  HEM A C2D 
7427 C  C3D . HEM C .   ? 0.1181 0.1273 0.1489 0.0006  0.0399  -0.0603 501  HEM A C3D 
7428 C  C4D . HEM C .   ? 0.1361 0.1196 0.1218 -0.0169 0.0569  -0.0267 501  HEM A C4D 
7429 C  CMD . HEM C .   ? 0.1270 0.1442 0.1363 -0.0375 0.0661  -0.0351 501  HEM A CMD 
7430 C  CAD . HEM C .   ? 0.1391 0.1445 0.1492 -0.0174 -0.0531 -0.0217 501  HEM A CAD 
7431 C  CBD . HEM C .   ? 0.1423 0.1732 0.1473 0.0035  -0.0242 -0.0189 501  HEM A CBD 
7432 C  CGD . HEM C .   ? 0.1429 0.1898 0.1658 0.0071  0.0017  -0.0010 501  HEM A CGD 
7433 O  O1D . HEM C .   ? 0.1054 0.1923 0.1682 -0.0132 -0.0167 -0.0018 501  HEM A O1D 
7434 O  O2D . HEM C .   ? 0.1146 0.2195 0.1678 -0.0308 0.0094  -0.0158 501  HEM A O2D 
7435 N  NA  . HEM C .   ? 0.1323 0.1521 0.1471 0.0024  -0.0009 -0.0153 501  HEM A NA  
7436 N  NB  . HEM C .   ? 0.1772 0.1413 0.1368 -0.0011 0.0213  -0.0302 501  HEM A NB  
7437 N  NC  . HEM C .   ? 0.1361 0.1730 0.1405 0.0022  0.0170  -0.0322 501  HEM A NC  
7438 N  ND  . HEM C .   ? 0.1413 0.1481 0.1433 0.0241  0.0133  -0.0640 501  HEM A ND  
7439 FE FE  A HEM C .   ? 0.1233 0.1729 0.1542 -0.0209 0.0085  -0.0565 501  HEM A FE  
7440 FE FE  B HEM C .   ? 0.1700 0.1806 0.1583 -0.0005 0.0320  -0.0401 501  HEM A FE  
7441 C  CAF A SYN D .   ? 0.2683 0.2980 0.2440 -0.0805 0.0563  0.0890  502  SYN A CAF 
7442 C  CAD A SYN D .   ? 0.2581 0.3284 0.2539 -0.1001 0.0353  0.0500  502  SYN A CAD 
7443 C  CAC A SYN D .   ? 0.2692 0.3454 0.2464 -0.1286 0.0468  0.0473  502  SYN A CAC 
7444 C  CAE A SYN D .   ? 0.3223 0.3538 0.2600 -0.1244 0.0470  0.0507  502  SYN A CAE 
7445 C  CAG A SYN D .   ? 0.3258 0.3205 0.2520 -0.1050 0.0408  0.0878  502  SYN A CAG 
7446 C  CAH A SYN D .   ? 0.2740 0.2896 0.2417 -0.0726 0.0597  0.1174  502  SYN A CAH 
7447 C  CAB A SYN D .   ? 0.1098 0.2392 0.2400 -0.0193 -0.0179 0.1432  502  SYN A CAB 
7448 C  CAA A SYN D .   ? 0.2563 0.2581 0.2459 -0.0296 -0.0309 0.1487  502  SYN A CAA 
7449 O  O1  A OXY E .   ? 0.0980 0.1711 0.1518 -0.0512 0.0252  -0.0808 503  OXY A O1  
7450 O  O2  A OXY E .   ? 0.1744 0.2027 0.1727 -0.0981 0.0521  -0.0803 503  OXY A O2  
7451 C  C1  . D0L F .   ? 0.3963 0.1791 0.2496 0.0195  0.0150  -0.0221 504  D0L A C1  
7452 C  C2  . D0L F .   ? 0.3171 0.1528 0.2296 0.0429  -0.0166 -0.0057 504  D0L A C2  
7453 C  C15 . D0L F .   ? 0.3623 0.3034 0.2865 0.0522  0.0641  -0.0032 504  D0L A C15 
7454 C  C14 . D0L F .   ? 0.3068 0.3236 0.2492 0.0437  0.0370  0.0102  504  D0L A C14 
7455 C  C7  . D0L F .   ? 0.2474 0.1532 0.2123 0.0367  -0.0017 -0.0086 504  D0L A C7  
7456 C  C12 . D0L F .   ? 0.2594 0.2571 0.2296 0.0532  -0.0571 -0.0130 504  D0L A C12 
7457 C  C10 . D0L F .   ? 0.2102 0.2209 0.1898 0.0322  0.0208  -0.0035 504  D0L A C10 
7458 C  C3  . D0L F .   ? 0.3970 0.1779 0.2560 0.0273  -0.0441 -0.0368 504  D0L A C3  
7459 C  C13 . D0L F .   ? 0.3260 0.2679 0.2376 0.0867  -0.0730 0.0056  504  D0L A C13 
7460 C  C11 . D0L F .   ? 0.2189 0.2326 0.2194 0.0854  -0.0062 -0.0141 504  D0L A C11 
7461 C  C6  . D0L F .   ? 0.4035 0.1830 0.2694 0.0611  0.0183  -0.0157 504  D0L A C6  
7462 C  C8  . D0L F .   ? 0.1906 0.1776 0.1947 0.0409  0.0002  -0.0235 504  D0L A C8  
7463 C  C5  . D0L F .   ? 0.4169 0.1939 0.2764 0.0656  0.0179  -0.0253 504  D0L A C5  
7464 C  C9  . D0L F .   ? 0.2329 0.1931 0.1858 0.0388  0.0089  -0.0121 504  D0L A C9  
7465 C  C4  . D0L F .   ? 0.4353 0.2043 0.2735 0.0404  -0.0286 -0.0052 504  D0L A C4  
7466 O  O2  . D0L F .   ? 0.2595 0.1779 0.1689 0.0166  0.0292  0.0034  504  D0L A O2  
7467 O  O3  . D0L F .   ? 0.2547 0.2285 0.1852 0.0278  0.0446  0.0396  504  D0L A O3  
7468 O  O1  . D0L F .   ? 0.2632 0.2066 0.1752 0.0224  -0.0087 0.0158  504  D0L A O1  
7469 N  N2  . D0L F .   ? 0.2788 0.3000 0.2547 0.0594  0.0272  -0.0003 504  D0L A N2  
7470 C  C16 . D0L F .   ? 0.4803 0.3370 0.3290 0.0389  0.0761  0.0080  504  D0L A C16 
7471 C  C17 . D0L F .   ? 0.5263 0.3701 0.3486 0.1235  0.0777  0.0475  504  D0L A C17 
7472 C  C18 . D0L F .   ? 0.5849 0.4060 0.3731 0.1313  0.0336  0.0760  504  D0L A C18 
7473 C  C19 . D0L F .   ? 0.5778 0.4425 0.3872 0.1368  0.0247  0.0709  504  D0L A C19 
7474 C  C20 . D0L F .   ? 0.6005 0.4822 0.4140 0.1054  0.0347  0.0796  504  D0L A C20 
7475 C  C21 . D0L F .   ? 0.6726 0.5002 0.4378 0.1046  0.0227  0.0630  504  D0L A C21 
7476 N  N1  . D0L F .   ? 0.1536 0.1906 0.1925 0.0344  0.0083  -0.0271 504  D0L A N1  
7477 C  C1  . GOL G .   ? 0.2705 0.5905 0.4385 -0.0656 0.0356  0.0374  505  GOL A C1  
7478 O  O1  . GOL G .   ? 0.2391 0.5450 0.4127 -0.0483 0.0509  0.0174  505  GOL A O1  
7479 C  C2  . GOL G .   ? 0.4087 0.6476 0.4619 -0.0955 0.0004  0.0492  505  GOL A C2  
7480 O  O2  . GOL G .   ? 0.4928 0.6873 0.4527 -0.1141 -0.0821 0.0460  505  GOL A O2  
7481 C  C3  . GOL G .   ? 0.3953 0.6633 0.4919 -0.0747 -0.0007 0.0801  505  GOL A C3  
7482 O  O3  . GOL G .   ? 0.4686 0.6914 0.5151 -0.0283 0.0071  0.1251  505  GOL A O3  
7483 C  CHA . HEM H .   ? 0.1653 0.1403 0.1231 -0.0047 0.0040  -0.0283 501  HEM B CHA 
7484 C  CHB . HEM H .   ? 0.1344 0.1427 0.1352 0.0105  -0.0137 0.0113  501  HEM B CHB 
7485 C  CHC . HEM H .   ? 0.1666 0.2026 0.1197 0.0070  0.0295  0.0032  501  HEM B CHC 
7486 C  CHD . HEM H .   ? 0.1181 0.1754 0.1299 0.0374  -0.0553 0.0330  501  HEM B CHD 
7487 C  C1A . HEM H .   ? 0.0889 0.1566 0.1397 -0.0008 0.0497  0.0019  501  HEM B C1A 
7488 C  C2A . HEM H .   ? 0.1133 0.1324 0.1167 0.0410  0.0049  0.0200  501  HEM B C2A 
7489 C  C3A . HEM H .   ? 0.1468 0.1186 0.1179 0.0250  0.0255  0.0138  501  HEM B C3A 
7490 C  C4A . HEM H .   ? 0.1882 0.1576 0.1338 0.0102  0.0264  0.0154  501  HEM B C4A 
7491 C  CMA . HEM H .   ? 0.2411 0.1133 0.1180 -0.0337 0.0106  -0.0091 501  HEM B CMA 
7492 C  CAA . HEM H .   ? 0.1344 0.1395 0.1126 -0.0046 0.0206  0.0068  501  HEM B CAA 
7493 C  CBA . HEM H .   ? 0.2228 0.1302 0.1634 0.0209  -0.0130 0.0047  501  HEM B CBA 
7494 C  CGA . HEM H .   ? 0.1795 0.0952 0.1684 0.0156  0.0099  0.0040  501  HEM B CGA 
7495 O  O1A . HEM H .   ? 0.1580 0.0856 0.1784 0.0209  -0.0486 0.0337  501  HEM B O1A 
7496 O  O2A . HEM H .   ? 0.1634 0.1158 0.1727 0.0469  0.0110  0.0191  501  HEM B O2A 
7497 C  C1B . HEM H .   ? 0.1555 0.1736 0.1344 -0.0170 -0.0169 0.0128  501  HEM B C1B 
7498 C  C2B . HEM H .   ? 0.0981 0.1915 0.1305 0.0037  -0.0012 -0.0149 501  HEM B C2B 
7499 C  C3B . HEM H .   ? 0.0937 0.1682 0.1341 -0.0198 0.0051  -0.0212 501  HEM B C3B 
7500 C  C4B . HEM H .   ? 0.1083 0.1704 0.1261 0.0293  -0.0101 0.0018  501  HEM B C4B 
7501 C  CMB . HEM H .   ? 0.0646 0.2335 0.1217 0.0112  0.0115  -0.0315 501  HEM B CMB 
7502 C  CAB . HEM H .   ? 0.1037 0.1450 0.1546 0.0611  -0.0054 -0.0460 501  HEM B CAB 
7503 C  CBB . HEM H .   ? 0.1845 0.1737 0.1425 0.0591  -0.0329 -0.0449 501  HEM B CBB 
7504 C  C1C . HEM H .   ? 0.1035 0.1966 0.1157 -0.0162 -0.0053 -0.0019 501  HEM B C1C 
7505 C  C2C . HEM H .   ? 0.1420 0.2021 0.1049 -0.0183 -0.0260 0.0321  501  HEM B C2C 
7506 C  C3C . HEM H .   ? 0.1741 0.1691 0.1369 -0.0175 -0.0363 0.0064  501  HEM B C3C 
7507 C  C4C . HEM H .   ? 0.0965 0.1997 0.1332 -0.0131 -0.0487 -0.0012 501  HEM B C4C 
7508 C  CMC . HEM H .   ? 0.1720 0.2008 0.1030 -0.0237 -0.0427 0.0474  501  HEM B CMC 
7509 C  CAC . HEM H .   ? 0.2351 0.1369 0.1839 -0.0277 -0.0321 0.0364  501  HEM B CAC 
7510 C  CBC . HEM H .   ? 0.2408 0.1321 0.2116 -0.0585 -0.0049 0.0140  501  HEM B CBC 
7511 C  C1D . HEM H .   ? 0.1795 0.1696 0.1111 0.0401  -0.0162 0.0316  501  HEM B C1D 
7512 C  C2D . HEM H .   ? 0.1794 0.1589 0.0953 0.0305  0.0422  0.0509  501  HEM B C2D 
7513 C  C3D . HEM H .   ? 0.1937 0.1613 0.1304 0.0191  -0.0064 0.0255  501  HEM B C3D 
7514 C  C4D . HEM H .   ? 0.1522 0.1538 0.1247 0.0149  0.0010  0.0080  501  HEM B C4D 
7515 C  CMD . HEM H .   ? 0.1153 0.1650 0.0947 0.0123  0.0454  0.0465  501  HEM B CMD 
7516 C  CAD . HEM H .   ? 0.1793 0.1783 0.1330 0.0110  -0.0466 -0.0048 501  HEM B CAD 
7517 C  CBD . HEM H .   ? 0.0988 0.1884 0.1586 0.0223  -0.0405 0.0044  501  HEM B CBD 
7518 C  CGD . HEM H .   ? 0.1239 0.1757 0.1792 -0.0690 -0.0529 0.0050  501  HEM B CGD 
7519 O  O1D . HEM H .   ? 0.1596 0.1706 0.1733 0.0089  -0.0094 -0.0126 501  HEM B O1D 
7520 O  O2D . HEM H .   ? 0.1128 0.1651 0.1806 -0.0246 -0.0213 -0.0052 501  HEM B O2D 
7521 N  NA  . HEM H .   ? 0.1358 0.1742 0.1480 0.0225  0.0073  0.0131  501  HEM B NA  
7522 N  NB  . HEM H .   ? 0.1332 0.1570 0.1303 -0.0130 -0.0142 0.0021  501  HEM B NB  
7523 N  NC  . HEM H .   ? 0.1037 0.1854 0.1322 -0.0533 0.0014  -0.0180 501  HEM B NC  
7524 N  ND  . HEM H .   ? 0.1214 0.1656 0.1326 0.0095  -0.0296 0.0067  501  HEM B ND  
7525 FE FE  A HEM H .   ? 0.1238 0.1823 0.1442 0.0167  -0.0036 0.0165  501  HEM B FE  
7526 FE FE  B HEM H .   ? 0.1606 0.1884 0.1513 0.0085  0.0045  0.0189  501  HEM B FE  
7527 C  CAF A SYN I .   ? 0.2217 0.2533 0.2833 0.0316  0.0336  -0.0425 502  SYN B CAF 
7528 C  CAD A SYN I .   ? 0.2439 0.2794 0.2840 0.0344  0.0435  -0.0172 502  SYN B CAD 
7529 C  CAC A SYN I .   ? 0.1593 0.2899 0.2689 0.0398  0.0413  -0.0221 502  SYN B CAC 
7530 C  CAE A SYN I .   ? 0.2005 0.3058 0.2792 -0.0149 0.0172  -0.0372 502  SYN B CAE 
7531 C  CAG A SYN I .   ? 0.1879 0.2616 0.2846 -0.0679 0.0355  -0.0590 502  SYN B CAG 
7532 C  CAH A SYN I .   ? 0.2381 0.2267 0.2835 -0.0491 0.0453  -0.0723 502  SYN B CAH 
7533 C  CAB A SYN I .   ? 0.1697 0.1705 0.2836 -0.0632 -0.0077 -0.0850 502  SYN B CAB 
7534 C  CAA A SYN I .   ? 0.3107 0.1390 0.2650 -0.0215 -0.0280 -0.0960 502  SYN B CAA 
7535 O  O1  A OXY J .   ? 0.1292 0.1444 0.1315 0.0559  -0.0514 0.0135  503  OXY B O1  
7536 O  O2  A OXY J .   ? 0.2109 0.1816 0.1271 0.0731  -0.0416 0.0124  503  OXY B O2  
7537 C  C1  . D0L K .   ? 0.2324 0.2706 0.2219 0.0054  -0.0208 0.0553  504  D0L B C1  
7538 C  C2  . D0L K .   ? 0.2820 0.2485 0.2187 -0.0253 -0.0021 0.0511  504  D0L B C2  
7539 C  C15 . D0L K .   ? 0.3618 0.3428 0.3098 0.0823  0.0620  -0.0167 504  D0L B C15 
7540 C  C14 . D0L K .   ? 0.2669 0.3908 0.2120 -0.0093 0.0801  -0.0092 504  D0L B C14 
7541 C  C7  . D0L K .   ? 0.2554 0.2239 0.2277 -0.0392 -0.0199 0.0541  504  D0L B C7  
7542 C  C12 . D0L K .   ? 0.1338 0.3358 0.1653 -0.0901 -0.0131 0.0080  504  D0L B C12 
7543 C  C10 . D0L K .   ? 0.1271 0.2394 0.1578 -0.0032 -0.0303 0.0135  504  D0L B C10 
7544 C  C3  . D0L K .   ? 0.3142 0.2510 0.2117 0.0160  -0.0456 0.0275  504  D0L B C3  
7545 C  C13 . D0L K .   ? 0.3096 0.3720 0.1760 -0.1053 0.0295  -0.0118 504  D0L B C13 
7546 C  C11 . D0L K .   ? 0.0846 0.2699 0.1929 -0.0408 -0.0289 0.0109  504  D0L B C11 
7547 C  C6  . D0L K .   ? 0.2572 0.2594 0.2213 0.0091  0.0098  0.0387  504  D0L B C6  
7548 C  C8  . D0L K .   ? 0.1935 0.2082 0.2064 -0.0128 0.0032  0.0438  504  D0L B C8  
7549 C  C5  . D0L K .   ? 0.2553 0.2281 0.2102 0.0595  -0.0181 0.0398  504  D0L B C5  
7550 C  C9  . D0L K .   ? 0.2160 0.2118 0.1922 -0.0572 -0.0120 0.0332  504  D0L B C9  
7551 C  C4  . D0L K .   ? 0.3341 0.2238 0.2259 0.0310  -0.0136 0.0217  504  D0L B C4  
7552 O  O2  . D0L K .   ? 0.2011 0.2224 0.1711 0.0361  -0.0148 0.0048  504  D0L B O2  
7553 O  O3  . D0L K .   ? 0.2594 0.2191 0.1484 0.0095  0.0402  -0.0260 504  D0L B O3  
7554 O  O1  . D0L K .   ? 0.2156 0.2055 0.1800 -0.0316 0.0007  0.0053  504  D0L B O1  
7555 N  N2  . D0L K .   ? 0.2184 0.3394 0.2296 0.0508  0.0299  -0.0184 504  D0L B N2  
7556 C  C16 . D0L K .   ? 0.3847 0.3610 0.3446 0.0901  0.0885  -0.0698 504  D0L B C16 
7557 C  C17 . D0L K .   ? 0.4725 0.3768 0.3637 -0.0012 0.1039  -0.1275 504  D0L B C17 
7558 C  C18 . D0L K .   ? 0.4969 0.3852 0.3754 -0.0443 0.0732  -0.1609 504  D0L B C18 
7559 C  C19 . D0L K .   ? 0.4265 0.3946 0.4126 -0.0883 0.0642  -0.1713 504  D0L B C19 
7560 C  C20 . D0L K .   ? 0.4025 0.4005 0.4274 -0.0320 0.0939  -0.1884 504  D0L B C20 
7561 C  C21 . D0L K .   ? 0.5254 0.4222 0.4753 -0.0586 0.0527  -0.1647 504  D0L B C21 
7562 N  N1  . D0L K .   ? 0.1381 0.2254 0.1717 -0.0285 -0.0009 0.0264  504  D0L B N1  
7563 C  C1  . GOL L .   ? 0.4644 0.7611 0.6779 -0.2099 -0.0692 -0.0880 505  GOL B C1  
7564 O  O1  . GOL L .   ? 0.4629 0.7705 0.7099 -0.2098 -0.0113 -0.0751 505  GOL B O1  
7565 C  C2  . GOL L .   ? 0.3744 0.7635 0.6621 -0.1454 -0.1198 -0.0786 505  GOL B C2  
7566 O  O2  . GOL L .   ? 0.3591 0.7780 0.6456 -0.1277 -0.1146 -0.0646 505  GOL B O2  
7567 C  C3  . GOL L .   ? 0.3565 0.7389 0.6482 -0.1009 -0.1683 -0.0852 505  GOL B C3  
7568 O  O3  . GOL L .   ? 0.2747 0.6874 0.6149 -0.0349 -0.1922 -0.0518 505  GOL B O3  
7569 C  C1  . GOL M .   ? 0.4717 0.4276 0.3743 0.0546  -0.0558 -0.0049 506  GOL B C1  
7570 O  O1  . GOL M .   ? 0.4273 0.3780 0.3229 0.0695  -0.0685 0.0226  506  GOL B O1  
7571 C  C2  . GOL M .   ? 0.5607 0.4504 0.3934 0.0404  -0.1035 -0.0140 506  GOL B C2  
7572 O  O2  . GOL M .   ? 0.5167 0.4791 0.4345 0.0316  -0.1065 -0.0335 506  GOL B O2  
7573 C  C3  . GOL M .   ? 0.6292 0.4178 0.3975 0.0168  -0.1109 0.0046  506  GOL B C3  
7574 O  O3  . GOL M .   ? 0.6850 0.3901 0.3990 -0.0334 -0.0866 0.0160  506  GOL B O3  
7575 C  C1  . GOL N .   ? 0.2888 0.3326 0.4972 0.0157  -0.0477 -0.1442 507  GOL B C1  
7576 O  O1  . GOL N .   ? 0.3699 0.3507 0.5148 0.0609  -0.0403 -0.1028 507  GOL B O1  
7577 C  C2  . GOL N .   ? 0.2722 0.3200 0.4841 0.0630  -0.0554 -0.1731 507  GOL B C2  
7578 O  O2  . GOL N .   ? 0.2429 0.3083 0.4785 0.1027  -0.1365 -0.1401 507  GOL B O2  
7579 C  C3  . GOL N .   ? 0.2389 0.3113 0.4581 0.0429  0.0327  -0.1918 507  GOL B C3  
7580 O  O3  . GOL N .   ? 0.3319 0.3546 0.5277 0.0270  0.1202  -0.1996 507  GOL B O3  
7582 O  O   . HOH O .   ? 0.4771 0.6852 0.5195 -0.1534 -0.0045 0.2705  601  HOH A O   
7583 O  O   . HOH O .   ? 0.2698 0.6623 0.3433 -0.0349 -0.1046 -0.1186 602  HOH A O   
7584 O  O   . HOH O .   ? 0.5462 0.6777 0.5683 0.3285  -0.1861 -0.1369 603  HOH A O   
7585 O  O   . HOH O .   ? 0.3926 0.9469 0.7346 0.1005  0.1658  0.3420  604  HOH A O   
7586 O  O   . HOH O .   ? 0.4802 0.2750 0.3005 -0.0472 -0.0310 -0.0311 605  HOH A O   
7587 O  O   . HOH O .   ? 0.5667 0.5859 0.7263 0.3077  0.1853  0.0634  606  HOH A O   
7588 O  O   . HOH O .   ? 0.7002 0.5247 0.6396 -0.2086 -0.1476 0.2988  607  HOH A O   
7589 O  O   B HOH O .   ? 0.1669 0.1846 0.1536 0.0340  -0.0019 -0.0594 608  HOH A O   
7590 O  O   . HOH O .   ? 0.4165 0.3127 0.2524 0.1352  0.1420  0.0986  609  HOH A O   
7591 O  O   . HOH O .   ? 0.3685 1.0250 0.3764 0.2489  0.0029  -0.0674 610  HOH A O   
7592 O  O   . HOH O .   ? 0.7713 0.6853 0.4660 0.0760  0.0740  -0.1735 611  HOH A O   
7593 O  O   . HOH O .   ? 0.6482 0.4426 0.3218 -0.2672 -0.1368 0.1383  612  HOH A O   
7594 O  O   . HOH O .   ? 0.3488 0.8071 0.2801 -0.1396 -0.0458 0.1005  613  HOH A O   
7595 O  O   . HOH O .   ? 0.2537 0.2258 0.1658 0.0497  -0.0387 -0.0460 614  HOH A O   
7596 O  O   . HOH O .   ? 0.7234 0.8172 0.5340 0.0127  0.1881  0.1158  615  HOH A O   
7597 O  O   . HOH O .   ? 0.2910 0.5163 0.4510 0.0128  0.1404  -0.1728 616  HOH A O   
7598 O  O   . HOH O .   ? 0.6940 0.4655 0.2593 -0.0752 -0.1608 0.0463  617  HOH A O   
7599 O  O   . HOH O .   ? 0.3546 1.0716 0.5880 0.0291  -0.0708 -0.2006 618  HOH A O   
7600 O  O   . HOH O .   ? 0.8494 0.6059 0.9232 0.3476  -0.0773 -0.1047 619  HOH A O   
7601 O  O   . HOH O .   ? 0.1859 0.1641 0.1043 -0.0225 0.0049  -0.0053 620  HOH A O   
7602 O  O   . HOH O .   ? 0.3825 0.4192 0.6262 0.0493  -0.0989 -0.0216 621  HOH A O   
7603 O  O   . HOH O .   ? 1.0493 0.3007 0.4511 0.0438  0.2760  -0.0068 622  HOH A O   
7604 O  O   . HOH O .   ? 0.1268 0.3952 0.2284 0.0767  0.0136  0.0217  623  HOH A O   
7605 O  O   . HOH O .   ? 0.4591 0.3648 0.4768 0.0362  -0.1683 -0.0355 624  HOH A O   
7606 O  O   . HOH O .   ? 0.7608 0.3447 0.7256 -0.0629 0.4428  -0.0682 625  HOH A O   
7607 O  O   . HOH O .   ? 0.5037 0.4492 0.3838 0.0453  0.2183  -0.1118 626  HOH A O   
7608 O  O   . HOH O .   ? 0.3005 0.3964 0.2459 -0.1327 -0.0692 0.0158  627  HOH A O   
7609 O  O   . HOH O .   ? 0.4432 0.4784 0.4136 0.0494  0.1243  0.1815  628  HOH A O   
7610 O  O   . HOH O .   ? 0.1847 0.4803 0.2440 0.0495  0.0269  0.0849  629  HOH A O   
7611 O  O   . HOH O .   ? 0.5949 0.4051 0.3969 0.1621  0.1981  0.1505  630  HOH A O   
7612 O  O   . HOH O .   ? 0.2373 0.6572 0.4585 0.1030  0.0185  0.0406  631  HOH A O   
7613 O  O   . HOH O .   ? 0.3304 0.2463 0.2892 -0.0329 0.0702  -0.0868 632  HOH A O   
7614 O  O   . HOH O .   ? 0.5753 0.7516 0.4901 -0.0735 -0.0927 -0.2984 633  HOH A O   
7615 O  O   . HOH O .   ? 0.6515 0.4093 0.9143 -0.1485 -0.1092 0.1317  634  HOH A O   
7616 O  O   . HOH O .   ? 0.3410 0.8474 0.3291 0.1731  0.0909  0.1903  635  HOH A O   
7617 O  O   . HOH O .   ? 0.1892 0.2624 0.1914 -0.0561 0.0159  -0.0309 636  HOH A O   
7618 O  O   . HOH O .   ? 0.5212 0.5156 0.4647 -0.0210 -0.0677 0.2253  637  HOH A O   
7619 O  O   . HOH O .   ? 0.4206 0.5351 0.2145 0.0626  0.0132  0.0395  638  HOH A O   
7620 O  O   . HOH O .   ? 0.4245 0.3417 0.4190 -0.0051 0.0172  -0.0403 639  HOH A O   
7621 O  O   . HOH O .   ? 0.2449 0.3895 0.2678 -0.0889 0.0192  0.0183  640  HOH A O   
7622 O  O   . HOH O .   ? 0.2712 0.2488 0.2685 0.0209  -0.0459 0.0352  641  HOH A O   
7623 O  O   . HOH O .   ? 0.3180 0.4729 0.2087 0.1191  -0.0856 -0.0063 642  HOH A O   
7624 O  O   . HOH O .   ? 0.8069 0.2425 0.4187 0.0303  0.2077  0.0541  643  HOH A O   
7625 O  O   . HOH O .   ? 0.2996 0.3217 0.1686 0.1044  0.0056  -0.0215 644  HOH A O   
7626 O  O   . HOH O .   ? 0.3997 1.0548 0.6575 0.1599  0.0641  0.3386  645  HOH A O   
7627 O  O   . HOH O .   ? 0.2785 0.1982 0.1957 0.0008  -0.0878 -0.0136 646  HOH A O   
7628 O  O   . HOH O .   ? 0.9192 0.4996 0.3292 0.2823  -0.1350 -0.1107 647  HOH A O   
7629 O  O   . HOH O .   ? 0.2404 0.3388 0.2483 -0.0374 -0.0255 0.0709  648  HOH A O   
7630 O  O   . HOH O .   ? 0.3702 0.4172 0.4701 0.0444  0.0826  0.2100  649  HOH A O   
7631 O  O   . HOH O .   ? 0.2429 0.4884 0.5136 0.1268  0.0908  0.2095  650  HOH A O   
7632 O  O   . HOH O .   ? 0.8444 0.4708 0.5144 0.1036  0.3341  -0.0436 651  HOH A O   
7633 O  O   . HOH O .   ? 0.5372 0.4883 0.3411 0.2368  -0.1113 -0.1814 652  HOH A O   
7634 O  O   . HOH O .   ? 0.2485 0.3583 0.2708 -0.0573 -0.0644 0.0159  653  HOH A O   
7635 O  O   . HOH O .   ? 0.5168 0.6704 0.7459 -0.2451 0.0948  0.1440  654  HOH A O   
7636 O  O   . HOH O .   ? 0.3420 0.3498 0.4631 -0.0405 -0.1231 0.1473  655  HOH A O   
7637 O  O   . HOH O .   ? 0.3708 0.7801 0.4975 -0.0989 -0.0890 0.2822  656  HOH A O   
7638 O  O   . HOH O .   ? 0.4701 0.3760 0.2498 0.0761  -0.0327 -0.0576 657  HOH A O   
7639 O  O   . HOH O .   ? 0.1727 0.2625 0.1377 0.0474  0.0044  -0.0236 658  HOH A O   
7640 O  O   . HOH O .   ? 0.4176 0.4915 0.2219 0.0220  0.0242  -0.0536 659  HOH A O   
7641 O  O   . HOH O .   ? 0.4101 0.2184 0.1469 0.1296  -0.0007 0.0044  660  HOH A O   
7642 O  O   . HOH O .   ? 0.2993 0.2639 0.3267 0.0521  -0.0142 0.0562  661  HOH A O   
7643 O  O   . HOH O .   ? 0.7036 0.3840 0.3138 0.2772  -0.0386 -0.0501 662  HOH A O   
7644 O  O   . HOH O .   ? 0.7441 0.6124 0.6047 -0.2682 -0.2031 0.0769  663  HOH A O   
7645 O  O   . HOH O .   ? 0.2226 0.2205 0.1961 0.0077  -0.0108 -0.0088 664  HOH A O   
7646 O  O   . HOH O .   ? 0.4424 0.2142 0.3456 0.0543  0.0205  -0.0273 665  HOH A O   
7647 O  O   . HOH O .   ? 0.7408 0.7002 0.5508 -0.0927 0.1336  -0.1373 666  HOH A O   
7648 O  O   . HOH O .   ? 0.2266 0.5300 0.6248 0.0200  0.0930  0.2157  667  HOH A O   
7649 O  O   . HOH O .   ? 0.6581 0.5328 0.6402 0.0980  -0.0047 0.1535  668  HOH A O   
7650 O  O   . HOH O .   ? 0.7135 0.5220 0.5752 -0.3322 0.0493  -0.0278 669  HOH A O   
7651 O  O   . HOH O .   ? 0.1718 0.2003 0.1256 0.0234  -0.0256 -0.0192 670  HOH A O   
7652 O  O   . HOH O .   ? 0.2430 0.5428 0.4158 -0.0097 -0.0416 0.1602  671  HOH A O   
7653 O  O   . HOH O .   ? 0.2161 0.1512 0.2093 0.0693  0.0089  0.0493  672  HOH A O   
7654 O  O   . HOH O .   ? 0.3141 0.3371 0.1702 -0.0241 -0.0537 0.0404  673  HOH A O   
7655 O  O   . HOH O .   ? 0.1913 0.3280 0.1904 0.0596  0.0478  0.1036  674  HOH A O   
7656 O  O   . HOH O .   ? 0.2872 0.5739 0.6258 0.0895  -0.1774 0.0284  675  HOH A O   
7657 O  O   . HOH O .   ? 0.1492 0.1712 0.1486 -0.0258 0.0125  0.0059  676  HOH A O   
7658 O  O   . HOH O .   ? 0.3014 0.1878 0.1480 0.0488  0.0874  0.0356  677  HOH A O   
7659 O  O   . HOH O .   ? 0.1785 0.2957 0.2658 0.0745  0.0313  0.0502  678  HOH A O   
7660 O  O   . HOH O .   ? 0.9662 0.6338 0.5230 -0.0404 0.0612  0.0438  679  HOH A O   
7661 O  O   . HOH O .   ? 0.2950 0.8070 0.7964 0.0839  0.0926  -0.2003 680  HOH A O   
7662 O  O   . HOH O .   ? 0.4322 0.3186 0.1924 0.0189  -0.0700 0.1001  681  HOH A O   
7663 O  O   . HOH O .   ? 0.6414 1.1553 0.3592 0.3535  0.0805  0.0659  682  HOH A O   
7664 O  O   . HOH O .   ? 0.7337 0.3061 0.2142 0.0187  -0.0819 0.0398  683  HOH A O   
7665 O  O   . HOH O .   ? 0.2529 0.3830 0.3371 -0.0481 0.0453  0.0274  684  HOH A O   
7666 O  O   . HOH O .   ? 0.3222 0.2998 0.3121 -0.0497 -0.1245 0.0114  685  HOH A O   
7667 O  O   . HOH O .   ? 0.5396 0.6962 0.4500 0.3283  0.2071  0.2607  686  HOH A O   
7668 O  O   . HOH O .   ? 0.4794 0.4562 0.8729 -0.1854 -0.1927 0.2518  687  HOH A O   
7669 O  O   . HOH O .   ? 0.2822 0.4020 0.7335 -0.1065 0.0770  -0.0247 688  HOH A O   
7670 O  O   . HOH O .   ? 0.3036 0.1939 0.2437 0.0159  -0.0029 -0.0208 689  HOH A O   
7671 O  O   . HOH O .   ? 0.3747 0.7834 0.4001 0.0894  -0.1465 0.0971  690  HOH A O   
7672 O  O   . HOH O .   ? 0.2359 0.5010 0.2460 0.0201  0.0057  0.0227  691  HOH A O   
7673 O  O   . HOH O .   ? 0.5605 0.3525 0.2765 -0.2202 -0.0896 -0.0089 692  HOH A O   
7674 O  O   . HOH O .   ? 0.7166 0.4794 0.2492 0.0798  0.0476  -0.0635 693  HOH A O   
7675 O  O   . HOH O .   ? 0.1958 0.3761 0.3893 -0.0878 0.0868  -0.0043 694  HOH A O   
7676 O  O   . HOH O .   ? 0.3281 0.3995 0.4354 0.0210  0.0040  -0.0535 695  HOH A O   
7677 O  O   . HOH O .   ? 0.2306 0.1233 0.1599 -0.0266 -0.0015 0.0117  696  HOH A O   
7678 O  O   . HOH O .   ? 1.0777 0.4397 0.6071 0.1893  0.2687  0.0413  697  HOH A O   
7679 O  O   . HOH O .   ? 0.4424 0.4510 0.5407 0.0399  -0.1090 -0.1274 698  HOH A O   
7680 O  O   . HOH O .   ? 0.7050 0.6194 0.4077 0.1293  -0.1900 0.0329  699  HOH A O   
7681 O  O   . HOH O .   ? 0.2255 0.7187 0.6184 -0.0933 0.0857  0.0571  700  HOH A O   
7682 O  O   . HOH O .   ? 0.4301 0.6607 0.5557 -0.1417 0.0949  0.0489  701  HOH A O   
7683 O  O   . HOH O .   ? 0.2843 0.6022 0.3766 -0.1348 0.0467  0.1562  702  HOH A O   
7684 O  O   . HOH O .   ? 0.6839 0.4118 0.5996 -0.1423 0.1837  -0.0217 703  HOH A O   
7685 O  O   . HOH O .   ? 0.3399 0.6163 0.3913 0.0940  0.0836  0.1579  704  HOH A O   
7686 O  O   . HOH O .   ? 0.4917 0.5046 0.4054 0.2114  -0.0058 0.0113  705  HOH A O   
7687 O  O   . HOH O .   ? 0.4016 0.6203 0.3039 -0.1461 -0.1138 0.0920  706  HOH A O   
7688 O  O   . HOH O .   ? 0.4975 0.4663 0.6033 -0.0485 -0.0267 0.1136  707  HOH A O   
7689 O  O   . HOH O .   ? 0.3923 0.4570 0.2125 0.1284  0.0247  0.0079  708  HOH A O   
7690 O  O   . HOH O .   ? 0.3469 0.3815 0.4173 0.1480  -0.0877 -0.0435 709  HOH A O   
7691 O  O   . HOH O .   ? 0.7752 0.5374 0.3385 -0.2049 0.1382  -0.1180 710  HOH A O   
7692 O  O   . HOH O .   ? 0.4385 0.2878 0.2025 -0.1067 -0.1065 0.0267  711  HOH A O   
7693 O  O   . HOH O .   ? 0.2001 0.1453 0.1344 -0.0150 -0.0095 -0.0099 712  HOH A O   
7694 O  O   . HOH O .   ? 0.8337 0.3501 0.2347 0.0868  -0.1004 0.0026  713  HOH A O   
7695 O  O   . HOH O .   ? 0.3050 0.4173 0.2288 -0.0531 0.0947  0.0206  714  HOH A O   
7696 O  O   . HOH O .   ? 0.2847 0.6713 0.3095 0.1420  0.0684  0.1400  715  HOH A O   
7697 O  O   . HOH O .   ? 0.5542 0.5896 0.3487 -0.3226 -0.1742 0.1828  716  HOH A O   
7698 O  O   . HOH O .   ? 0.3385 0.8421 0.3460 0.1595  -0.0294 0.1566  717  HOH A O   
7699 O  O   . HOH O .   ? 0.2395 0.4406 0.1918 -0.0581 -0.0141 0.0458  718  HOH A O   
7700 O  O   . HOH O .   ? 0.4550 0.1759 0.3540 -0.0895 -0.0854 0.0644  719  HOH A O   
7701 O  O   . HOH O .   ? 0.6088 0.5389 0.4587 0.2519  0.2566  0.1089  720  HOH A O   
7702 O  O   . HOH O .   ? 0.4810 0.4252 0.5354 -0.1596 -0.2629 0.0557  721  HOH A O   
7703 O  O   . HOH O .   ? 0.8858 0.5605 0.2953 -0.0433 -0.1536 -0.0092 722  HOH A O   
7704 O  O   . HOH O .   ? 0.2554 0.4369 0.3291 0.1163  -0.0414 0.0823  723  HOH A O   
7705 O  O   . HOH O .   ? 0.3993 0.4517 0.6232 -0.0826 0.2672  -0.1349 724  HOH A O   
7706 O  O   . HOH O .   ? 0.3494 0.3506 0.3293 0.0137  0.0458  0.1455  725  HOH A O   
7707 O  O   . HOH O .   ? 0.4282 0.4466 0.4168 0.1420  0.2132  0.0010  726  HOH A O   
7708 O  O   . HOH O .   ? 0.1152 0.2333 0.1413 0.0292  -0.0120 -0.0257 727  HOH A O   
7709 O  O   . HOH O .   ? 0.3410 0.3017 0.5041 0.1635  0.0814  0.0153  728  HOH A O   
7710 O  O   . HOH O .   ? 0.1868 0.2700 0.1497 -0.0127 0.0295  0.0258  729  HOH A O   
7711 O  O   . HOH O .   ? 0.2274 0.4660 0.2446 0.0376  0.0419  0.0622  730  HOH A O   
7712 O  O   . HOH O .   ? 0.2363 0.6439 0.1734 -0.1205 -0.0107 -0.0064 731  HOH A O   
7713 O  O   . HOH O .   ? 0.2729 0.3083 0.2004 0.1441  0.0474  -0.0244 732  HOH A O   
7714 O  O   . HOH O .   ? 0.5601 0.8403 0.6327 -0.0428 -0.0565 -0.0293 733  HOH A O   
7715 O  O   . HOH O .   ? 0.1899 0.3020 0.3385 0.0025  0.0073  0.0477  734  HOH A O   
7716 O  O   . HOH O .   ? 0.3489 0.2478 0.1618 0.0624  0.0822  -0.0089 735  HOH A O   
7717 O  O   . HOH O .   ? 0.2875 0.2040 0.2150 0.0622  0.0772  0.0706  736  HOH A O   
7718 O  O   . HOH O .   ? 0.6320 0.4616 0.2874 0.0654  -0.0257 -0.0986 737  HOH A O   
7719 O  O   . HOH O .   ? 0.2995 0.3277 0.2110 0.0542  -0.0518 -0.0965 738  HOH A O   
7720 O  O   . HOH O .   ? 0.3401 0.4475 0.1931 -0.0153 -0.0641 0.0886  739  HOH A O   
7721 O  O   . HOH O .   ? 0.4347 0.3957 0.1821 -0.0517 -0.0774 -0.0042 740  HOH A O   
7722 O  O   . HOH O .   ? 0.6404 0.4288 0.3600 -0.1457 -0.0869 -0.1561 741  HOH A O   
7723 O  O   . HOH O .   ? 0.6970 0.4112 0.5727 0.0461  0.3489  0.1204  742  HOH A O   
7724 O  O   . HOH O .   ? 0.2241 0.3055 0.1902 0.0557  0.0666  0.0593  743  HOH A O   
7725 O  O   . HOH O .   ? 0.4600 0.2732 0.6348 -0.0324 -0.1089 -0.1742 744  HOH A O   
7726 O  O   . HOH O .   ? 0.1655 0.1281 0.1354 -0.0298 -0.0057 -0.0061 745  HOH A O   
7727 O  O   . HOH O .   ? 0.2159 0.7016 0.5625 -0.0416 0.0246  0.0870  746  HOH A O   
7728 O  O   . HOH O .   ? 0.2378 0.3287 0.2230 -0.0281 0.0237  0.0515  747  HOH A O   
7729 O  O   . HOH O .   ? 0.2397 0.2255 0.1668 0.0617  -0.0043 0.0191  748  HOH A O   
7730 O  O   . HOH O .   ? 0.2260 0.2846 0.3154 -0.0050 -0.0176 -0.0626 749  HOH A O   
7731 O  O   . HOH O .   ? 0.2610 0.2076 0.1375 0.0748  0.0521  0.0439  750  HOH A O   
7732 O  O   . HOH O .   ? 0.3675 0.2690 0.3769 0.0254  -0.0212 -0.0460 751  HOH A O   
7733 O  O   . HOH O .   ? 0.1951 0.1222 0.1795 -0.0301 -0.0268 0.0179  752  HOH A O   
7734 O  O   . HOH O .   ? 0.2460 0.2199 0.2461 0.1046  0.0235  0.0460  753  HOH A O   
7735 O  O   . HOH O .   ? 0.2825 0.4018 0.3308 0.0448  0.0070  0.0436  754  HOH A O   
7736 O  O   . HOH O .   ? 0.2511 0.4107 0.2080 0.1140  0.0122  0.0386  755  HOH A O   
7737 O  O   . HOH O .   ? 0.6887 0.4608 0.6592 -0.1159 0.0176  0.0111  756  HOH A O   
7738 O  O   . HOH O .   ? 0.1568 0.3153 0.2549 0.0302  0.0000  0.0398  757  HOH A O   
7739 O  O   . HOH O .   ? 0.4761 0.3870 0.3462 -0.1098 -0.0628 -0.1516 758  HOH A O   
7740 O  O   . HOH O .   ? 0.1758 0.1415 0.1482 0.0564  0.0039  0.0254  759  HOH A O   
7741 O  O   . HOH O .   ? 0.3822 1.1863 0.3161 0.2382  0.0134  0.0471  760  HOH A O   
7742 O  O   . HOH O .   ? 0.8638 0.4571 0.5793 0.0847  -0.1100 0.2311  761  HOH A O   
7743 O  O   . HOH O .   ? 0.7930 0.6077 0.5220 0.3575  -0.1578 0.0256  762  HOH A O   
7744 O  O   . HOH O .   ? 0.2642 0.3409 0.2088 0.0530  -0.0317 -0.1100 763  HOH A O   
7745 O  O   . HOH O .   ? 0.2098 0.4827 0.3590 0.0086  0.0245  0.0241  764  HOH A O   
7746 O  O   A HOH O .   ? 0.4439 0.2199 0.5611 -0.0518 -0.1162 0.1394  765  HOH A O   
7747 O  O   . HOH O .   ? 0.7386 0.4577 0.3218 -0.1555 -0.0822 0.0696  766  HOH A O   
7748 O  O   . HOH O .   ? 0.3124 0.3219 0.3214 -0.0644 0.0232  -0.1371 767  HOH A O   
7749 O  O   . HOH O .   ? 0.6358 0.2210 0.2967 0.0459  0.0020  0.0878  768  HOH A O   
7750 O  O   . HOH O .   ? 0.4287 0.1848 0.3365 -0.0665 0.0935  0.0130  769  HOH A O   
7751 O  O   . HOH O .   ? 0.3554 0.4405 0.3797 -0.0023 -0.1480 -0.0416 770  HOH A O   
7752 O  O   . HOH O .   ? 0.7299 0.2879 0.3680 -0.0146 0.1285  -0.0001 771  HOH A O   
7753 O  O   . HOH O .   ? 0.2409 0.2149 0.2364 0.0293  -0.0040 -0.0135 772  HOH A O   
7754 O  O   . HOH O .   ? 0.5188 0.3208 0.1942 0.0019  -0.0270 0.0224  773  HOH A O   
7755 O  O   . HOH O .   ? 0.2076 0.2952 0.2605 -0.0663 -0.0785 0.0664  774  HOH A O   
7756 O  O   . HOH O .   ? 0.7996 0.2744 0.8552 -0.0985 0.0991  0.1044  775  HOH A O   
7757 O  O   . HOH O .   ? 0.3634 0.3233 0.2384 0.0603  0.0680  0.0201  776  HOH A O   
7758 O  O   . HOH O .   ? 0.6802 0.3331 0.3424 0.0934  -0.2013 0.0112  777  HOH A O   
7759 O  O   . HOH O .   ? 0.3999 0.3782 0.7467 0.1229  -0.1522 0.0925  778  HOH A O   
7760 O  O   . HOH O .   ? 0.1880 0.2192 0.2235 -0.0343 0.0585  -0.0420 779  HOH A O   
7761 O  O   . HOH O .   ? 0.6008 0.5400 0.4863 0.0765  0.1759  0.0100  780  HOH A O   
7762 O  O   . HOH O .   ? 0.4726 0.4183 0.3236 0.1750  -0.0144 -0.0304 781  HOH A O   
7763 O  O   . HOH O .   ? 0.1911 0.2242 0.6986 0.0057  -0.0224 -0.1423 782  HOH A O   
7764 O  O   . HOH O .   ? 0.3147 0.8595 0.3098 -0.0542 0.0824  0.0694  783  HOH A O   
7765 O  O   . HOH O .   ? 0.2686 0.2954 0.4451 0.0572  0.0666  0.0849  784  HOH A O   
7766 O  O   . HOH O .   ? 0.4032 0.2547 0.2010 0.0739  -0.0166 -0.0494 785  HOH A O   
7767 O  O   . HOH O .   ? 0.3640 0.8150 0.7198 0.1994  -0.1334 -0.2399 786  HOH A O   
7768 O  O   . HOH O .   ? 0.2948 0.2952 0.4410 0.0091  0.1392  -0.0200 787  HOH A O   
7769 O  O   . HOH O .   ? 0.3200 0.2881 0.2540 -0.1551 -0.0104 0.0677  788  HOH A O   
7770 O  O   . HOH O .   ? 0.3503 0.5454 0.2148 -0.1585 -0.0422 0.0691  789  HOH A O   
7771 O  O   . HOH O .   ? 0.4035 0.5532 0.3290 -0.0571 0.0321  -0.1395 790  HOH A O   
7772 O  O   . HOH O .   ? 0.2273 0.1895 0.1950 -0.0237 0.0004  -0.0223 791  HOH A O   
7773 O  O   . HOH O .   ? 0.3727 0.3511 0.5322 0.1064  0.0358  -0.0489 792  HOH A O   
7774 O  O   . HOH O .   ? 0.4200 0.4349 0.3466 -0.0611 -0.0374 -0.0337 793  HOH A O   
7775 O  O   . HOH O .   ? 0.6882 0.5591 0.8193 0.2177  -0.2129 0.1315  794  HOH A O   
7776 O  O   . HOH O .   ? 0.2517 0.2540 0.1993 0.0606  0.0286  -0.0059 795  HOH A O   
7777 O  O   . HOH O .   ? 0.1687 0.1476 0.1493 0.0295  0.0307  0.0416  796  HOH A O   
7778 O  O   . HOH O .   ? 0.5003 0.3590 0.5427 0.0956  0.1341  0.0996  797  HOH A O   
7779 O  O   . HOH O .   ? 0.1583 0.1903 0.1692 -0.0358 -0.0118 -0.0289 798  HOH A O   
7780 O  O   . HOH O .   ? 0.3679 0.4512 0.5891 0.0216  -0.0214 -0.0194 799  HOH A O   
7781 O  O   . HOH O .   ? 0.1705 0.2541 0.1142 0.0363  0.0011  -0.0039 800  HOH A O   
7782 O  O   . HOH O .   ? 0.3979 0.6298 0.3187 -0.0616 -0.0095 0.1904  801  HOH A O   
7783 O  O   . HOH O .   ? 0.4795 0.3183 0.2429 0.0561  -0.0820 0.0659  802  HOH A O   
7784 O  O   . HOH O .   ? 0.6678 0.6217 0.6181 0.3201  0.0796  0.0548  803  HOH A O   
7785 O  O   . HOH O .   ? 0.1844 0.2201 0.1981 -0.0143 -0.0013 0.0230  804  HOH A O   
7786 O  O   . HOH O .   ? 0.2494 0.3047 0.1530 -0.0393 -0.0760 0.0276  805  HOH A O   
7787 O  O   . HOH O .   ? 0.1987 0.1286 0.2013 -0.0169 0.0032  0.0162  806  HOH A O   
7788 O  O   . HOH O .   ? 0.6689 0.5343 0.5065 0.0761  -0.1386 0.2093  807  HOH A O   
7789 O  O   . HOH O .   ? 0.8597 0.6061 0.3077 -0.0265 -0.2003 -0.0603 808  HOH A O   
7790 O  O   . HOH O .   ? 0.4494 0.6289 0.9564 0.1761  0.2703  0.3715  809  HOH A O   
7791 O  O   . HOH O .   ? 0.5342 0.4531 0.5883 -0.1084 -0.3176 0.1575  810  HOH A O   
7792 O  O   . HOH O .   ? 0.6898 0.4154 0.4709 -0.1868 0.0783  -0.1214 811  HOH A O   
7793 O  O   . HOH O .   ? 0.6446 0.9201 0.3388 -0.0510 0.0093  0.2372  812  HOH A O   
7794 O  O   . HOH O .   ? 0.4622 0.2960 0.2167 -0.0138 0.1078  0.0300  813  HOH A O   
7795 O  O   . HOH O .   ? 0.4976 0.4335 0.2473 0.2054  -0.0608 -0.0459 814  HOH A O   
7796 O  O   . HOH O .   ? 0.3057 0.3657 0.4023 0.0501  -0.0900 0.0251  815  HOH A O   
7797 O  O   . HOH O .   ? 0.4984 0.5862 0.4960 0.1678  0.1208  0.2593  816  HOH A O   
7798 O  O   . HOH O .   ? 0.4076 0.3447 0.3579 0.0162  -0.1301 -0.0001 817  HOH A O   
7799 O  O   . HOH O .   ? 0.3553 0.2458 0.5769 -0.0046 -0.1366 0.0397  818  HOH A O   
7800 O  O   . HOH O .   ? 0.2878 0.3162 0.5127 0.0395  -0.0112 0.1078  819  HOH A O   
7801 O  O   . HOH O .   ? 0.3442 0.6008 0.4794 -0.2020 -0.1409 0.2753  820  HOH A O   
7802 O  O   . HOH O .   ? 0.6941 0.6195 0.6497 0.1934  -0.2037 0.0746  821  HOH A O   
7803 O  O   . HOH O .   ? 0.3344 0.5120 0.2045 -0.0040 0.0784  0.0918  822  HOH A O   
7804 O  O   . HOH O .   ? 0.6023 0.6119 0.4726 0.2120  -0.1414 0.0348  823  HOH A O   
7805 O  O   . HOH O .   ? 0.3998 0.5033 0.7123 0.1456  -0.1248 -0.0001 824  HOH A O   
7806 O  O   . HOH O .   ? 0.2047 0.5853 0.3153 -0.0359 0.0603  0.1273  825  HOH A O   
7807 O  O   . HOH O .   ? 0.2476 0.5948 0.7436 0.0374  0.0754  0.2557  826  HOH A O   
7808 O  O   . HOH O .   ? 0.3630 0.2491 0.3288 0.0110  0.0017  -0.0109 827  HOH A O   
7809 O  O   . HOH O .   ? 0.4800 0.4415 0.3437 0.2172  0.1975  0.1531  828  HOH A O   
7810 O  O   . HOH O .   ? 0.7122 0.2908 0.3259 0.1526  0.1082  0.0259  829  HOH A O   
7811 O  O   . HOH O .   ? 0.4011 0.5406 0.3256 -0.0347 0.1420  -0.1202 830  HOH A O   
7812 O  O   . HOH O .   ? 0.9956 0.4692 0.6500 -0.0016 0.0910  -0.0495 831  HOH A O   
7813 O  O   . HOH O .   ? 0.4396 0.3961 0.2699 -0.0510 -0.0161 0.0415  832  HOH A O   
7814 O  O   . HOH O .   ? 0.3617 0.5152 0.7394 -0.1117 -0.1152 0.2387  833  HOH A O   
7815 O  O   . HOH O .   ? 0.5641 0.7580 0.4584 -0.2651 -0.0173 -0.0431 834  HOH A O   
7816 O  O   . HOH O .   ? 0.5832 0.6373 0.6026 0.1085  -0.2034 0.1411  835  HOH A O   
7817 O  O   . HOH O .   ? 0.3872 0.3356 0.2920 -0.1144 -0.0060 0.0381  836  HOH A O   
7818 O  O   . HOH O .   ? 0.5564 0.5751 0.2864 0.0893  0.0709  0.0497  837  HOH A O   
7819 O  O   . HOH O .   ? 0.2253 0.6738 0.2954 0.1242  0.0303  0.1617  838  HOH A O   
7820 O  O   . HOH O .   ? 0.6574 0.3771 0.2736 -0.0280 -0.0617 0.0774  839  HOH A O   
7821 O  O   . HOH O .   ? 0.4429 0.2725 0.1711 -0.0295 0.0043  0.0282  840  HOH A O   
7822 O  O   . HOH O .   ? 0.7662 0.5364 0.6449 -0.0258 0.0254  -0.3488 841  HOH A O   
7823 O  O   . HOH O .   ? 0.5814 0.6166 0.3904 0.2618  0.0915  0.0772  842  HOH A O   
7824 O  O   . HOH O .   ? 0.4677 0.6535 0.5084 0.0279  0.2881  0.0454  843  HOH A O   
7825 O  O   . HOH O .   ? 0.8637 0.4811 0.5561 0.1656  0.3132  -0.0535 844  HOH A O   
7826 O  O   . HOH O .   ? 0.4753 0.6675 0.6315 -0.3184 0.0268  0.0752  845  HOH A O   
7827 O  O   . HOH O .   ? 0.4098 0.8060 0.2569 0.0624  -0.0287 -0.1108 846  HOH A O   
7828 O  O   . HOH O .   ? 0.2828 0.2599 0.7488 -0.0626 -0.0034 0.1136  847  HOH A O   
7829 O  O   . HOH O .   ? 0.3840 0.3880 0.2400 0.0506  -0.1048 0.0517  848  HOH A O   
7830 O  O   . HOH O .   ? 0.2560 0.8391 0.3162 0.0831  0.0537  -0.0274 849  HOH A O   
7831 O  O   . HOH O .   ? 0.3613 0.2827 0.3547 -0.0045 0.1161  -0.0098 850  HOH A O   
7832 O  O   . HOH O .   ? 0.8549 0.5406 0.7156 0.1058  -0.0848 0.0467  851  HOH A O   
7833 O  O   B HOH O .   ? 0.2468 0.2709 0.1942 -0.0994 -0.0465 -0.0727 852  HOH A O   
7834 O  O   . HOH O .   ? 0.5720 0.4338 0.9571 -0.0026 0.2528  0.2515  853  HOH A O   
7835 O  O   . HOH O .   ? 0.4974 0.7071 0.4627 -0.1370 0.1904  -0.2606 854  HOH A O   
7836 O  O   . HOH O .   ? 0.4830 0.8634 0.2889 0.2532  -0.0672 0.0150  855  HOH A O   
7837 O  O   . HOH O .   ? 0.2634 0.2039 0.2275 -0.0102 -0.0131 -0.0343 856  HOH A O   
7838 O  O   . HOH O .   ? 0.2462 0.4047 0.4161 -0.0060 -0.0100 -0.0323 857  HOH A O   
7839 O  O   . HOH O .   ? 0.1895 0.2000 0.1311 0.0084  -0.0252 0.0302  858  HOH A O   
7840 O  O   . HOH O .   ? 0.2395 0.5382 0.2558 0.0388  0.0616  0.0084  859  HOH A O   
7841 O  O   . HOH O .   ? 0.1888 0.2424 0.2268 0.0247  0.0204  0.0361  860  HOH A O   
7842 O  O   . HOH O .   ? 0.3294 0.6297 0.5886 -0.0902 0.0204  0.3138  861  HOH A O   
7843 O  O   . HOH O .   ? 0.6035 0.6890 0.7306 0.0284  0.3201  0.2632  862  HOH A O   
7844 O  O   . HOH O .   ? 0.2249 0.1326 0.1695 0.0030  0.0052  -0.0167 863  HOH A O   
7845 O  O   . HOH O .   ? 0.2688 0.4303 0.4344 -0.1865 0.0407  -0.0573 864  HOH A O   
7846 O  O   . HOH O .   ? 0.3157 0.2313 0.3003 -0.0063 0.0116  0.0073  865  HOH A O   
7847 O  O   . HOH O .   ? 0.4996 0.4992 0.2969 -0.1461 -0.0441 0.1888  866  HOH A O   
7848 O  O   . HOH O .   ? 0.2915 0.2790 0.4381 0.0429  -0.0014 -0.0069 867  HOH A O   
7849 O  O   . HOH O .   ? 0.6533 0.7371 0.5073 0.3628  0.0739  0.0483  868  HOH A O   
7850 O  O   . HOH O .   ? 0.2601 0.5091 0.3170 -0.0009 0.0683  -0.0442 869  HOH A O   
7851 O  O   . HOH O .   ? 0.4863 0.8158 0.6089 0.2571  0.2363  0.3168  870  HOH A O   
7852 O  O   . HOH O .   ? 0.5661 0.3720 0.2701 0.2379  0.1442  0.0692  871  HOH A O   
7853 O  O   . HOH O .   ? 0.3709 0.4350 1.1489 -0.0511 -0.0920 0.2169  872  HOH A O   
7854 O  O   . HOH O .   ? 0.2503 0.1640 0.2438 0.0771  -0.0331 -0.0339 873  HOH A O   
7855 O  O   . HOH O .   ? 0.2885 0.1117 0.1797 0.0560  -0.0002 0.0458  874  HOH A O   
7856 O  O   . HOH O .   ? 0.5170 0.4554 0.5437 -0.1660 -0.0647 -0.0220 875  HOH A O   
7857 O  O   . HOH O .   ? 0.7093 0.5239 0.2511 -0.1904 -0.0036 -0.0653 876  HOH A O   
7858 O  O   . HOH O .   ? 0.2900 0.7578 0.3927 -0.1409 0.0428  0.1109  877  HOH A O   
7859 O  O   . HOH O .   ? 0.3697 0.2612 0.5324 -0.0207 0.0269  0.1426  878  HOH A O   
7860 O  O   . HOH O .   ? 0.2883 0.6607 0.2767 0.0510  0.0780  -0.0356 879  HOH A O   
7861 O  O   . HOH O .   ? 0.8814 0.2708 0.5783 0.0381  0.3023  0.0295  880  HOH A O   
7862 O  O   . HOH O .   ? 0.5737 0.6101 0.6297 0.0519  -0.3028 -0.0744 881  HOH A O   
7863 O  O   . HOH O .   ? 0.8085 0.3859 0.5427 0.1999  -0.1194 0.0611  882  HOH A O   
7864 O  O   . HOH O .   ? 0.6210 0.4284 0.8908 0.1133  0.2650  -0.1488 883  HOH A O   
7865 O  O   . HOH O .   ? 0.4631 0.6962 0.5134 0.0659  0.1534  0.1227  884  HOH A O   
7866 O  O   . HOH O .   ? 0.6599 0.2301 0.4202 0.0344  0.2440  -0.0146 885  HOH A O   
7867 O  O   . HOH O .   ? 0.4678 0.1291 0.3486 -0.0426 0.0439  0.0179  886  HOH A O   
7868 O  O   . HOH O .   ? 0.8583 0.3133 0.4459 0.1268  -0.0462 -0.0259 887  HOH A O   
7869 O  O   . HOH O .   ? 0.2955 0.4157 0.3493 0.1007  -0.0948 0.0323  888  HOH A O   
7870 O  O   . HOH O .   ? 0.4817 0.4394 0.3899 0.1657  -0.0015 -0.1960 889  HOH A O   
7871 O  O   . HOH O .   ? 0.6307 0.6873 0.3807 0.0542  0.1340  -0.0620 890  HOH A O   
7872 O  O   . HOH O .   ? 0.2590 0.4448 0.9801 0.0184  0.0743  0.0937  891  HOH A O   
7873 O  O   . HOH O .   ? 0.7257 0.5035 0.6567 0.2283  0.0092  -0.0579 892  HOH A O   
7874 O  O   . HOH O .   ? 0.4808 0.2651 0.6399 -0.0391 0.3248  -0.0398 893  HOH A O   
7875 O  O   . HOH O .   ? 0.5387 0.6663 0.2882 0.3333  0.0918  0.0698  894  HOH A O   
7876 O  O   . HOH O .   ? 0.7673 0.4851 0.2989 0.0904  0.1182  0.1478  895  HOH A O   
7877 O  O   . HOH O .   ? 0.6030 0.8650 0.7355 0.2736  -0.2014 0.2022  896  HOH A O   
7878 O  O   . HOH O .   ? 0.3804 0.2897 0.3294 0.1025  0.0035  0.0998  897  HOH A O   
7879 O  O   . HOH O .   ? 0.3834 0.1873 0.3300 0.0475  -0.1118 -0.0385 898  HOH A O   
7880 O  O   . HOH O .   ? 0.3929 0.9633 0.5998 0.2446  -0.1244 -0.0185 899  HOH A O   
7881 O  O   . HOH O .   ? 0.5435 0.3270 0.2945 0.1925  -0.0204 -0.0329 900  HOH A O   
7882 O  O   . HOH O .   ? 0.7239 0.6560 0.9211 0.3140  0.2606  -0.0787 901  HOH A O   
7883 O  O   . HOH O .   ? 0.2956 0.2353 0.2983 -0.0476 -0.0132 0.0645  902  HOH A O   
7884 O  O   . HOH O .   ? 0.4197 0.2689 0.1939 0.0796  -0.1014 -0.0484 903  HOH A O   
7885 O  O   . HOH O .   ? 0.2591 0.5924 0.6511 -0.0186 -0.0556 0.2865  904  HOH A O   
7886 O  O   . HOH O .   ? 0.2920 0.8070 0.5618 0.0896  0.0656  0.3887  905  HOH A O   
7887 O  O   . HOH O .   ? 0.4702 0.4799 0.7041 -0.0416 -0.3297 0.0178  906  HOH A O   
7888 O  O   . HOH O .   ? 0.4141 0.1776 0.5321 -0.0438 0.0453  0.0478  907  HOH A O   
7889 O  O   . HOH O .   ? 0.4728 0.6475 0.4557 0.1217  0.0137  -0.0384 908  HOH A O   
7890 O  O   . HOH O .   ? 0.3412 0.7569 0.3663 -0.1515 0.0299  0.1180  909  HOH A O   
7891 O  O   . HOH O .   ? 0.4170 0.5513 0.7522 -0.1598 -0.0783 0.0603  910  HOH A O   
7892 O  O   . HOH O .   ? 0.8232 0.4754 0.3812 0.1406  -0.1291 -0.1875 911  HOH A O   
7893 O  O   . HOH O .   ? 0.5306 0.6043 0.3398 0.0932  0.0572  -0.0234 912  HOH A O   
7894 O  O   . HOH O .   ? 0.6175 0.7283 0.4207 0.1684  -0.2231 -0.1341 913  HOH A O   
7895 O  O   . HOH O .   ? 0.8369 0.3077 0.6035 0.0146  0.3496  -0.0544 914  HOH A O   
7896 O  O   . HOH O .   ? 0.4747 0.3590 0.2308 -0.0484 0.0010  0.0795  915  HOH A O   
7897 O  O   . HOH O .   ? 0.8810 0.3274 0.6627 -0.1050 0.2481  -0.1493 916  HOH A O   
7898 O  O   . HOH O .   ? 0.6424 0.6663 0.7771 0.0030  0.0806  -0.0415 917  HOH A O   
7899 O  O   . HOH O .   ? 0.2219 0.2117 0.1446 0.0238  -0.0379 0.0011  918  HOH A O   
7900 O  O   . HOH O .   ? 0.8598 0.4158 0.3679 0.0333  0.1588  0.1433  919  HOH A O   
7901 O  O   . HOH O .   ? 0.9606 0.3143 0.8470 -0.0958 0.1481  0.0168  920  HOH A O   
7902 O  O   . HOH O .   ? 0.3472 0.4097 0.5297 -0.0669 0.0519  0.0168  921  HOH A O   
7903 O  O   . HOH O .   ? 0.5882 0.3759 0.7325 -0.1677 -0.3490 0.2090  922  HOH A O   
7904 O  O   . HOH O .   ? 0.4674 0.5298 0.3748 -0.1900 -0.0032 -0.1405 923  HOH A O   
7905 O  O   . HOH O .   ? 0.7682 0.8732 0.4179 0.1408  0.2583  -0.0903 924  HOH A O   
7906 O  O   . HOH O .   ? 0.8399 0.3344 0.8938 0.2123  0.1188  0.0071  925  HOH A O   
7907 O  O   . HOH O .   ? 0.4200 1.2280 0.3284 -0.0181 -0.0486 0.0228  926  HOH A O   
7908 O  O   . HOH O .   ? 0.6229 0.5833 0.3144 0.1067  -0.0614 -0.0231 927  HOH A O   
7909 O  O   . HOH O .   ? 0.2531 0.8145 0.3660 0.0584  -0.0210 -0.1766 928  HOH A O   
7910 O  O   . HOH O .   ? 0.4073 0.5403 0.7918 0.0794  0.1625  0.1727  929  HOH A O   
7911 O  O   . HOH O .   ? 1.1272 0.5430 0.3698 -0.2436 0.1497  -0.1126 930  HOH A O   
7912 O  O   . HOH O .   ? 0.8566 0.4704 0.2858 -0.3475 -0.0319 0.0212  931  HOH A O   
7913 O  O   . HOH O .   ? 0.2763 0.7175 0.5904 0.0848  0.0887  0.0286  932  HOH A O   
7914 O  O   . HOH O .   ? 0.7743 0.3655 0.4755 -0.2152 -0.3237 0.1373  933  HOH A O   
7915 O  O   . HOH O .   ? 0.4144 0.4574 0.3824 -0.1679 0.1160  -0.1787 934  HOH A O   
7916 O  O   . HOH O .   ? 0.4109 0.7696 0.4992 0.2367  0.1077  -0.0957 935  HOH A O   
7917 O  O   . HOH O .   ? 0.3912 0.6694 0.4250 -0.0101 0.1082  -0.1702 936  HOH A O   
7918 O  O   . HOH O .   ? 0.6537 0.8056 0.4404 0.2822  0.0186  0.0348  937  HOH A O   
7919 O  O   . HOH O .   ? 1.0297 0.3312 0.3933 -0.1223 0.0343  0.0739  938  HOH A O   
7920 O  O   . HOH O .   ? 0.5662 0.2183 0.4844 0.0252  -0.0564 -0.0315 939  HOH A O   
7921 O  O   . HOH O .   ? 0.7708 0.6973 0.5765 0.4302  -0.0519 -0.1023 940  HOH A O   
7922 O  O   . HOH O .   ? 0.5207 0.3560 0.6171 -0.0564 -0.1900 0.0667  941  HOH A O   
7923 O  O   . HOH O .   ? 0.4716 0.5633 0.8431 -0.0500 0.2130  0.1259  942  HOH A O   
7924 O  O   . HOH O .   ? 0.2282 0.1524 0.1438 0.0145  -0.0320 -0.0543 943  HOH A O   
7925 O  O   . HOH O .   ? 0.5910 0.4955 0.7394 0.1565  -0.1981 -0.0880 944  HOH A O   
7926 O  O   . HOH O .   ? 0.7716 0.6214 0.5830 0.1275  0.0786  -0.0290 945  HOH A O   
7927 O  O   . HOH O .   ? 0.4888 0.6176 0.2618 0.2198  0.1246  0.1037  946  HOH A O   
7928 O  O   . HOH O .   ? 0.3776 0.7656 0.7443 -0.0369 0.2756  -0.0533 947  HOH A O   
7929 O  O   . HOH O .   ? 0.2986 0.7845 0.3960 -0.1221 0.0107  -0.1811 948  HOH A O   
7930 O  O   . HOH O .   ? 0.5690 0.5955 0.5133 0.2665  0.1734  0.2768  949  HOH A O   
7931 O  O   . HOH O .   ? 0.5860 0.4197 1.0167 0.1224  -0.2267 -0.1458 950  HOH A O   
7932 O  O   . HOH O .   ? 0.2666 0.4219 0.4022 -0.0096 -0.0994 0.0303  951  HOH A O   
7933 O  O   . HOH O .   ? 0.6802 0.6485 0.4083 -0.2754 -0.0229 0.1168  952  HOH A O   
7934 O  O   . HOH O .   ? 0.7149 0.8195 0.2283 -0.1059 -0.0550 0.0177  953  HOH A O   
7935 O  O   . HOH O .   ? 0.7101 0.2482 0.5175 0.1103  -0.1210 -0.0161 954  HOH A O   
7936 O  O   . HOH O .   ? 0.4759 0.6176 0.7586 0.2236  0.1420  0.0999  955  HOH A O   
7937 O  O   . HOH O .   ? 0.5299 0.4611 0.7482 -0.2372 -0.1445 -0.0918 956  HOH A O   
7938 O  O   . HOH O .   ? 0.7931 0.3769 0.6321 -0.0852 -0.0566 0.1331  957  HOH A O   
7939 O  O   . HOH O .   ? 0.4545 0.8002 0.3733 0.2005  -0.1447 -0.1436 958  HOH A O   
7940 O  O   . HOH O .   ? 0.6324 0.7408 0.4320 -0.1916 0.1910  -0.1999 959  HOH A O   
7941 O  O   . HOH O .   ? 0.5933 0.2119 0.2120 0.0597  0.1301  -0.0057 960  HOH A O   
7942 O  O   . HOH O .   ? 0.4337 0.6927 0.6225 -0.0610 -0.1460 -0.2969 961  HOH A O   
7943 O  O   . HOH O .   ? 0.4244 0.7257 0.5116 -0.1900 -0.0257 0.1878  962  HOH A O   
7944 O  O   . HOH O .   ? 0.4776 0.6314 0.6333 0.1591  0.1379  0.0253  963  HOH A O   
7945 O  O   . HOH O .   ? 0.5085 0.4627 0.4549 -0.1318 0.0380  0.0071  964  HOH A O   
7946 O  O   . HOH O .   ? 0.5357 0.8669 0.4763 -0.1925 -0.1282 0.2877  965  HOH A O   
7947 O  O   . HOH O .   ? 0.6398 0.6362 0.4834 0.3380  0.1589  0.1744  966  HOH A O   
7948 O  O   . HOH O .   ? 0.5476 0.3688 0.7105 -0.2402 -0.0880 0.0285  967  HOH A O   
7949 O  O   . HOH O .   ? 0.7266 0.5531 0.3276 -0.1161 -0.0270 -0.0606 968  HOH A O   
7950 O  O   . HOH O .   ? 0.8077 0.5194 0.5257 0.0097  -0.2147 0.0470  969  HOH A O   
7951 O  O   . HOH O .   ? 0.4953 0.7242 0.4585 0.1147  -0.0698 0.0191  970  HOH A O   
7952 O  O   . HOH O .   ? 0.3291 0.6273 0.5182 -0.0609 0.0399  -0.1986 971  HOH A O   
7953 O  O   . HOH O .   ? 0.6343 0.4642 0.3643 0.3183  -0.0082 -0.0053 972  HOH A O   
7954 O  O   . HOH O .   ? 0.5552 0.7073 1.0230 0.0147  -0.0700 0.4826  973  HOH A O   
7955 O  O   . HOH O .   ? 0.8309 0.3813 0.3598 0.1917  0.0376  0.0068  974  HOH A O   
7956 O  O   . HOH O .   ? 0.7400 0.5304 0.6590 0.3387  -0.1649 -0.0152 975  HOH A O   
7957 O  O   . HOH O .   ? 0.3047 0.8104 0.4576 0.1852  -0.0375 0.1080  976  HOH A O   
7958 O  O   . HOH O .   ? 0.5365 0.6360 0.6305 0.1603  -0.0294 0.1278  977  HOH A O   
7959 O  O   . HOH O .   ? 0.6531 0.3473 0.5013 -0.0567 -0.1275 -0.1831 978  HOH A O   
7960 O  O   . HOH O .   ? 0.3997 0.5891 0.3261 0.1949  0.0800  0.2113  979  HOH A O   
7961 O  O   . HOH O .   ? 0.3673 0.2882 0.4952 0.0655  0.0181  0.0593  980  HOH A O   
7962 O  O   . HOH O .   ? 0.4390 0.4039 0.2696 0.1004  -0.0131 0.0905  981  HOH A O   
7963 O  O   . HOH O .   ? 0.3634 0.4055 1.0245 -0.0303 0.1599  -0.0540 982  HOH A O   
7964 O  O   . HOH O .   ? 0.5185 0.3219 0.4146 -0.0747 -0.1558 0.0687  983  HOH A O   
7965 O  O   . HOH O .   ? 0.3471 0.3826 0.4485 0.0320  -0.1476 0.0021  984  HOH A O   
7966 O  O   . HOH O .   ? 0.2728 0.5543 0.4785 0.0834  0.0997  0.1902  985  HOH A O   
7967 O  O   . HOH O .   ? 0.3166 0.7935 0.5739 -0.1043 0.0330  0.2326  986  HOH A O   
7968 O  O   . HOH O .   ? 0.3109 0.3682 0.5761 -0.0381 0.1838  -0.0775 987  HOH A O   
7969 O  O   . HOH O .   ? 0.6161 0.5463 0.4181 0.1832  0.1111  -0.1488 988  HOH A O   
7970 O  O   . HOH O .   ? 0.3930 0.2718 0.3211 0.0167  0.0112  0.0572  989  HOH A O   
7971 O  O   . HOH O .   ? 0.6080 0.7096 0.8666 0.2139  -0.1537 -0.0629 990  HOH A O   
7972 O  O   . HOH O .   ? 0.8766 0.5585 0.2303 0.0963  0.0416  -0.0136 991  HOH A O   
7973 O  O   . HOH O .   ? 0.2702 0.2893 0.4039 -0.0095 -0.1444 0.0276  992  HOH A O   
7974 O  O   . HOH O .   ? 0.5495 0.6052 0.7457 -0.1173 -0.0735 0.1378  993  HOH A O   
7975 O  O   . HOH O .   ? 0.7172 0.7941 0.5311 0.2760  -0.0776 -0.2370 994  HOH A O   
7976 O  O   . HOH O .   ? 0.5743 0.7817 0.7970 -0.0452 0.1825  -0.1652 995  HOH A O   
7977 O  O   . HOH O .   ? 0.4513 0.6261 0.5951 -0.0910 0.0629  -0.0775 996  HOH A O   
7978 O  O   . HOH O .   ? 0.3216 0.2851 0.2475 -0.0150 -0.0631 0.0441  997  HOH A O   
7979 O  O   . HOH O .   ? 0.3573 0.7022 0.5572 0.1998  -0.0720 0.0068  998  HOH A O   
7980 O  O   . HOH O .   ? 0.3882 1.0351 0.3218 -0.0759 -0.0209 0.1926  999  HOH A O   
7981 O  O   . HOH O .   ? 0.4777 0.7796 0.6676 -0.1570 0.2484  -0.1950 1000 HOH A O   
7982 O  O   . HOH O .   ? 0.7408 0.5783 0.7391 0.1865  -0.0145 0.0779  1001 HOH A O   
7983 O  O   . HOH O .   ? 0.5580 0.7890 0.4042 -0.2633 -0.1493 0.1329  1002 HOH A O   
7984 O  O   . HOH O .   ? 0.4490 0.1946 0.3992 0.0206  -0.0416 0.0208  1003 HOH A O   
7985 O  O   . HOH O .   ? 0.4931 0.7367 0.8119 0.3243  0.0861  -0.0925 1004 HOH A O   
7986 O  O   . HOH O .   ? 0.5715 0.6200 0.5405 -0.3161 -0.1313 0.2254  1005 HOH A O   
7987 O  O   . HOH O .   ? 0.3591 0.8413 0.7937 0.1050  -0.0535 0.3420  1006 HOH A O   
7988 O  O   . HOH O .   ? 0.7582 0.4148 0.5226 -0.0241 -0.1373 -0.0926 1007 HOH A O   
7989 O  O   . HOH O .   ? 0.4101 0.3871 0.3533 0.1429  -0.1195 0.0112  1008 HOH A O   
7990 O  O   . HOH O .   ? 0.5220 0.5700 0.6424 0.0775  -0.0045 0.0922  1009 HOH A O   
7991 O  O   . HOH O .   ? 0.8438 0.3637 0.3514 -0.0869 -0.0506 0.0065  1010 HOH A O   
7992 O  O   . HOH O .   ? 0.4497 0.2717 0.3823 0.0959  0.0118  0.0275  1011 HOH A O   
7993 O  O   . HOH P .   ? 0.3926 0.5159 0.5939 0.0318  -0.0094 -0.1000 601  HOH B O   
7994 O  O   B HOH P .   ? 0.1932 0.1926 0.1696 0.0088  -0.0218 0.0161  602  HOH B O   
7995 O  O   . HOH P .   ? 0.6863 0.5576 0.6472 0.1956  0.1526  0.2346  603  HOH B O   
7996 O  O   . HOH P .   ? 0.6192 0.6745 0.4617 0.1257  0.0115  0.1882  604  HOH B O   
7997 O  O   . HOH P .   ? 0.8720 0.7826 0.4813 0.0581  -0.0346 0.3413  605  HOH B O   
7998 O  O   . HOH P .   ? 0.2744 0.2947 0.2094 0.0324  0.0115  0.0091  606  HOH B O   
7999 O  O   . HOH P .   ? 0.3245 0.5096 0.3245 -0.0003 -0.0636 -0.0774 607  HOH B O   
8000 O  O   . HOH P .   ? 0.2719 0.5086 0.4421 0.0602  -0.0613 -0.1009 608  HOH B O   
8001 O  O   . HOH P .   ? 0.4515 0.2472 0.5836 0.0372  0.1745  0.0873  609  HOH B O   
8002 O  O   . HOH P .   ? 0.2960 0.5355 0.2288 -0.2003 0.0625  -0.1307 610  HOH B O   
8003 O  O   . HOH P .   ? 0.5377 0.4736 0.5862 0.1099  -0.1469 0.2217  611  HOH B O   
8004 O  O   . HOH P .   ? 1.0743 0.4055 0.5326 -0.0110 0.2163  0.0096  612  HOH B O   
8005 O  O   . HOH P .   ? 0.2095 0.2860 0.1802 0.0248  -0.0095 -0.0133 613  HOH B O   
8006 O  O   . HOH P .   ? 0.5201 1.0159 0.3916 0.0519  -0.0924 0.0160  614  HOH B O   
8007 O  O   . HOH P .   ? 0.5343 0.3396 0.6041 -0.1325 -0.3265 0.1314  615  HOH B O   
8008 O  O   . HOH P .   ? 0.7188 0.2571 0.4148 -0.1321 -0.1633 0.0687  616  HOH B O   
8009 O  O   . HOH P .   ? 0.3872 0.3347 0.2642 -0.0393 0.0297  0.0059  617  HOH B O   
8010 O  O   . HOH P .   ? 0.3565 0.5175 0.4165 -0.1616 -0.1643 0.2139  618  HOH B O   
8011 O  O   . HOH P .   ? 0.4025 0.7409 0.5503 0.2155  -0.1484 -0.3341 619  HOH B O   
8012 O  O   . HOH P .   ? 0.4073 0.2955 0.6969 0.0306  -0.0813 -0.0683 620  HOH B O   
8013 O  O   . HOH P .   ? 0.8704 0.2889 0.4847 -0.1385 0.2587  -0.0570 621  HOH B O   
8014 O  O   . HOH P .   ? 0.3663 0.8368 0.4894 0.2148  -0.1444 -0.1712 622  HOH B O   
8015 O  O   . HOH P .   ? 0.2784 0.2980 0.2171 0.0882  -0.0502 -0.1004 623  HOH B O   
8016 O  O   . HOH P .   ? 0.2132 0.3042 0.2379 -0.0285 -0.0342 0.0250  624  HOH B O   
8017 O  O   . HOH P .   ? 0.5809 0.5188 0.9071 0.0041  -0.0617 -0.0191 625  HOH B O   
8018 O  O   . HOH P .   ? 0.2927 0.2537 0.4079 -0.0175 0.0930  -0.0774 626  HOH B O   
8019 O  O   . HOH P .   ? 0.3702 0.3937 0.5723 0.1028  0.0226  -0.0114 627  HOH B O   
8020 O  O   . HOH P .   ? 0.2801 0.8422 0.3447 0.0780  -0.0556 -0.2312 628  HOH B O   
8021 O  O   . HOH P .   ? 0.3531 0.3872 0.4901 -0.0759 -0.0040 -0.0132 629  HOH B O   
8022 O  O   . HOH P .   ? 0.6337 0.2722 0.6976 -0.0480 -0.2745 0.0504  630  HOH B O   
8023 O  O   . HOH P .   ? 0.8889 0.6164 0.2866 0.2872  -0.0961 -0.0299 631  HOH B O   
8024 O  O   . HOH P .   ? 0.7464 0.2385 0.7850 -0.1332 -0.0217 -0.0606 632  HOH B O   
8025 O  O   . HOH P .   ? 0.6996 0.3432 0.8215 -0.1241 0.0478  0.2048  633  HOH B O   
8026 O  O   . HOH P .   ? 0.7391 0.4089 0.2331 0.3014  -0.0320 -0.0181 634  HOH B O   
8027 O  O   . HOH P .   ? 0.5994 0.3845 0.5376 0.0892  -0.1794 0.0353  635  HOH B O   
8028 O  O   . HOH P .   ? 0.4899 0.5247 0.7048 0.1871  0.0009  0.0727  636  HOH B O   
8029 O  O   . HOH P .   ? 0.2589 0.5522 0.3453 -0.1122 -0.0215 0.0159  637  HOH B O   
8030 O  O   . HOH P .   ? 0.4272 0.4267 0.9502 0.0152  0.2521  0.1584  638  HOH B O   
8031 O  O   . HOH P .   ? 0.2269 0.2805 0.2463 0.0512  0.0046  0.1001  639  HOH B O   
8032 O  O   . HOH P .   ? 0.7326 0.3093 0.3663 0.0033  0.0364  0.0587  640  HOH B O   
8033 O  O   . HOH P .   ? 0.1481 0.2806 0.1715 -0.0235 0.0107  0.0497  641  HOH B O   
8034 O  O   . HOH P .   ? 0.6308 0.2338 0.6241 0.1568  -0.0041 -0.0566 642  HOH B O   
8035 O  O   . HOH P .   ? 0.2809 0.4295 0.8980 -0.0349 0.0129  -0.2891 643  HOH B O   
8036 O  O   . HOH P .   ? 0.8038 0.5834 0.4875 -0.1734 -0.2007 -0.1744 644  HOH B O   
8037 O  O   . HOH P .   ? 0.3961 0.5220 0.5166 0.1356  0.0876  0.2945  645  HOH B O   
8038 O  O   . HOH P .   ? 0.3576 0.2566 0.2557 -0.0466 -0.0355 -0.0539 646  HOH B O   
8039 O  O   . HOH P .   ? 0.1900 0.2731 0.2397 -0.0365 -0.0167 0.0019  647  HOH B O   
8040 O  O   . HOH P .   ? 0.1346 0.2277 0.2214 -0.0090 -0.0391 -0.0050 648  HOH B O   
8041 O  O   . HOH P .   ? 0.1448 0.1710 0.1541 0.0145  -0.0245 -0.0088 649  HOH B O   
8042 O  O   . HOH P .   ? 0.2869 0.4759 0.8102 0.0600  0.0151  0.2415  650  HOH B O   
8043 O  O   . HOH P .   ? 0.1749 0.2838 0.1279 -0.0333 -0.0255 0.0376  651  HOH B O   
8044 O  O   . HOH P .   ? 0.2081 0.2036 0.5609 0.0186  -0.0413 0.0815  652  HOH B O   
8045 O  O   . HOH P .   ? 0.1527 0.2083 0.1742 0.0466  0.0344  -0.0360 653  HOH B O   
8046 O  O   . HOH P .   ? 0.7409 0.7018 0.5075 0.3963  0.2727  0.2569  654  HOH B O   
8047 O  O   . HOH P .   ? 0.5296 0.3183 0.3262 0.0414  0.1572  -0.0891 655  HOH B O   
8048 O  O   . HOH P .   ? 0.2704 0.5361 0.7109 0.0446  0.0258  -0.3030 656  HOH B O   
8049 O  O   . HOH P .   ? 0.1708 0.3844 0.2385 -0.0697 0.0274  -0.0105 657  HOH B O   
8050 O  O   . HOH P .   ? 0.3345 0.3023 0.3689 -0.0250 -0.0131 -0.0737 658  HOH B O   
8051 O  O   . HOH P .   ? 0.4150 0.3969 0.4924 -0.0089 0.0637  -0.1497 659  HOH B O   
8052 O  O   . HOH P .   ? 0.1927 0.2626 0.2626 -0.0707 0.0105  -0.0651 660  HOH B O   
8053 O  O   . HOH P .   ? 0.6728 0.4725 0.2916 -0.2283 0.0880  0.0310  661  HOH B O   
8054 O  O   . HOH P .   ? 0.5965 0.5817 0.6217 0.0949  0.0885  -0.1298 662  HOH B O   
8055 O  O   . HOH P .   ? 0.5214 0.2453 0.5864 0.0871  -0.2896 -0.0972 663  HOH B O   
8056 O  O   . HOH P .   ? 0.2759 0.4659 0.2755 0.0266  -0.0426 0.1491  664  HOH B O   
8057 O  O   . HOH P .   ? 0.9077 0.3823 0.5130 0.0818  -0.1635 0.0122  665  HOH B O   
8058 O  O   . HOH P .   ? 0.2220 0.3806 0.3468 0.0692  0.0632  0.0214  666  HOH B O   
8059 O  O   . HOH P .   ? 0.3801 0.6864 0.3766 -0.0196 -0.0672 0.0788  667  HOH B O   
8060 O  O   . HOH P .   ? 0.2584 0.2793 0.2283 -0.0701 -0.0064 -0.0515 668  HOH B O   
8061 O  O   . HOH P .   ? 0.3883 0.3304 0.3236 0.1225  -0.0532 -0.0518 669  HOH B O   
8062 O  O   . HOH P .   ? 0.2898 0.1616 0.1965 0.0374  -0.0401 0.0242  670  HOH B O   
8063 O  O   . HOH P .   ? 0.7379 0.5450 0.5045 -0.3237 0.2065  -0.0423 671  HOH B O   
8064 O  O   . HOH P .   ? 0.2123 0.4389 0.1874 0.0061  0.0163  -0.0427 672  HOH B O   
8065 O  O   . HOH P .   ? 0.3453 0.2517 0.5534 0.0068  -0.0420 -0.1864 673  HOH B O   
8066 O  O   . HOH P .   ? 0.2932 0.4729 0.4466 -0.1140 0.1200  -0.2032 674  HOH B O   
8067 O  O   . HOH P .   ? 0.3655 0.7364 0.2719 -0.0111 -0.0571 0.0609  675  HOH B O   
8068 O  O   . HOH P .   ? 0.2354 0.2378 0.4649 0.0230  -0.1026 -0.0335 676  HOH B O   
8069 O  O   . HOH P .   ? 0.4278 0.2391 0.3989 0.0591  0.0047  0.0723  677  HOH B O   
8070 O  O   . HOH P .   ? 0.2699 0.1719 0.2793 -0.0091 -0.0085 -0.0186 678  HOH B O   
8071 O  O   . HOH P .   ? 0.5690 0.3635 0.9157 0.0677  -0.2407 0.1329  679  HOH B O   
8072 O  O   . HOH P .   ? 0.1368 0.2026 0.2433 -0.0320 -0.0023 0.0389  680  HOH B O   
8073 O  O   . HOH P .   ? 0.8639 0.5492 0.9503 -0.1216 0.3412  -0.1540 681  HOH B O   
8074 O  O   . HOH P .   ? 0.1954 0.3786 0.5987 -0.0462 -0.0268 -0.1402 682  HOH B O   
8075 O  O   . HOH P .   ? 0.2622 0.2976 0.1978 -0.0713 -0.0168 0.0117  683  HOH B O   
8076 O  O   . HOH P .   ? 0.3200 0.2436 0.3164 0.0480  0.1011  -0.0263 684  HOH B O   
8077 O  O   . HOH P .   ? 0.2820 0.5161 0.3675 -0.1001 0.0254  0.0804  685  HOH B O   
8078 O  O   . HOH P .   ? 0.2300 0.1785 0.6405 0.0056  0.0928  0.0677  686  HOH B O   
8079 O  O   . HOH P .   ? 0.2083 0.3317 0.1921 0.0630  0.0307  -0.0401 687  HOH B O   
8080 O  O   . HOH P .   ? 0.2122 0.2414 0.1807 0.0057  0.0419  0.0161  688  HOH B O   
8081 O  O   . HOH P .   ? 0.2505 0.2705 0.3625 0.0233  -0.0757 -0.0493 689  HOH B O   
8082 O  O   . HOH P .   ? 0.6833 0.6203 0.3283 0.0050  -0.1481 0.0412  690  HOH B O   
8083 O  O   . HOH P .   ? 0.2130 0.2503 0.3197 -0.0277 -0.0323 -0.0229 691  HOH B O   
8084 O  O   . HOH P .   ? 0.3379 0.2856 0.2883 0.0414  -0.0666 -0.0147 692  HOH B O   
8085 O  O   . HOH P .   ? 0.4466 0.6104 0.7980 0.2325  -0.0101 -0.2325 693  HOH B O   
8086 O  O   . HOH P .   ? 0.1985 0.2610 0.1351 0.0573  -0.0152 -0.0133 694  HOH B O   
8087 O  O   . HOH P .   ? 0.5282 0.4239 0.2030 -0.1511 -0.0067 0.0254  695  HOH B O   
8088 O  O   . HOH P .   ? 0.2193 0.4287 0.6176 0.0755  0.0643  0.2200  696  HOH B O   
8089 O  O   . HOH P .   ? 0.1729 0.2196 0.2106 0.0098  0.0254  0.0118  697  HOH B O   
8090 O  O   . HOH P .   ? 0.2943 0.2576 0.5156 0.0099  0.0674  -0.0093 698  HOH B O   
8091 O  O   . HOH P .   ? 0.3489 0.2262 0.5455 -0.0934 -0.0596 -0.0262 699  HOH B O   
8092 O  O   . HOH P .   ? 0.3746 0.3041 0.9203 0.0127  -0.2004 0.1142  700  HOH B O   
8093 O  O   . HOH P .   ? 0.2666 0.2318 0.4418 -0.0811 0.0458  -0.1455 701  HOH B O   
8094 O  O   . HOH P .   ? 0.2592 0.3227 0.5240 0.1209  0.0370  0.1417  702  HOH B O   
8095 O  O   . HOH P .   ? 0.1581 0.2731 0.1437 0.0035  0.0033  0.0043  703  HOH B O   
8096 O  O   . HOH P .   ? 0.1467 0.2140 0.4642 -0.0092 -0.0055 0.1020  704  HOH B O   
8097 O  O   . HOH P .   ? 0.4151 0.4349 0.3962 -0.1014 -0.1221 0.2117  705  HOH B O   
8098 O  O   . HOH P .   ? 0.2343 0.4420 0.5993 -0.1152 0.1044  -0.0756 706  HOH B O   
8099 O  O   . HOH P .   ? 0.6225 0.2227 0.5218 -0.0573 0.2731  -0.0293 707  HOH B O   
8100 O  O   . HOH P .   ? 0.2210 0.4881 0.2771 -0.0801 -0.0302 0.0049  708  HOH B O   
8101 O  O   . HOH P .   ? 0.7653 0.4435 0.3088 -0.1445 -0.0498 0.0002  709  HOH B O   
8102 O  O   . HOH P .   ? 0.7321 0.7447 0.4585 -0.0472 0.2986  -0.1474 710  HOH B O   
8103 O  O   A HOH P .   ? 0.3841 0.2711 0.7250 0.0587  -0.0093 -0.1102 711  HOH B O   
8104 O  O   . HOH P .   ? 0.2088 0.1727 0.1534 -0.0486 0.0431  -0.0026 712  HOH B O   
8105 O  O   . HOH P .   ? 0.5717 0.4149 0.3044 0.0790  0.0564  -0.0822 713  HOH B O   
8106 O  O   . HOH P .   ? 0.2745 0.3404 0.2151 -0.0112 0.0440  -0.0101 714  HOH B O   
8107 O  O   . HOH P .   ? 0.2201 0.3107 0.3261 -0.0081 0.1124  -0.0217 715  HOH B O   
8108 O  O   . HOH P .   ? 0.2871 0.4235 0.1694 -0.0142 0.0177  -0.0027 716  HOH B O   
8109 O  O   . HOH P .   ? 0.6071 0.5111 0.3702 0.0741  -0.1429 -0.1284 717  HOH B O   
8110 O  O   . HOH P .   ? 0.3293 0.3531 0.2736 -0.0025 -0.0004 0.0208  718  HOH B O   
8111 O  O   . HOH P .   ? 0.1636 0.2429 0.2107 0.0356  -0.0168 -0.0104 719  HOH B O   
8112 O  O   . HOH P .   ? 0.1623 0.2287 0.1179 -0.0112 -0.0341 -0.0263 720  HOH B O   
8113 O  O   . HOH P .   ? 0.5910 0.3747 0.7880 -0.0109 0.3986  0.0181  721  HOH B O   
8114 O  O   . HOH P .   ? 0.2815 0.8436 0.4523 -0.1763 0.0033  0.0869  722  HOH B O   
8115 O  O   . HOH P .   ? 0.2708 0.2304 0.3112 0.0403  0.0669  -0.0824 723  HOH B O   
8116 O  O   . HOH P .   ? 0.2263 0.2329 0.2271 0.0324  0.0495  0.0191  724  HOH B O   
8117 O  O   . HOH P .   ? 0.5306 0.4529 0.2726 0.2461  0.1005  0.1293  725  HOH B O   
8118 O  O   . HOH P .   ? 0.3946 0.3483 0.2730 -0.0755 -0.0075 0.0287  726  HOH B O   
8119 O  O   . HOH P .   ? 0.7641 0.4153 0.4578 -0.0655 0.2316  -0.1761 727  HOH B O   
8120 O  O   . HOH P .   ? 0.1589 0.2014 0.2769 -0.0356 -0.0245 0.0334  728  HOH B O   
8121 O  O   . HOH P .   ? 0.3402 0.3924 0.4417 0.0629  0.1062  0.1932  729  HOH B O   
8122 O  O   . HOH P .   ? 0.1518 0.2107 0.1707 0.0290  -0.0020 -0.0433 730  HOH B O   
8123 O  O   . HOH P .   ? 0.1479 0.1799 0.2146 -0.0264 0.0087  -0.0295 731  HOH B O   
8124 O  O   . HOH P .   ? 0.3257 0.6040 0.4427 0.0651  -0.0723 -0.0195 732  HOH B O   
8125 O  O   . HOH P .   ? 0.2926 0.8561 0.4758 0.1631  -0.0214 0.1387  733  HOH B O   
8126 O  O   . HOH P .   ? 0.2716 0.2891 0.3170 -0.0195 0.0015  -0.0027 734  HOH B O   
8127 O  O   . HOH P .   ? 0.2990 0.3622 0.2472 -0.0647 0.0623  0.0798  735  HOH B O   
8128 O  O   . HOH P .   ? 0.4366 0.5442 0.2565 -0.0988 0.0211  0.0821  736  HOH B O   
8129 O  O   . HOH P .   ? 0.5543 0.6912 0.3879 -0.2184 0.0844  -0.0242 737  HOH B O   
8130 O  O   . HOH P .   ? 0.2982 0.3803 0.3718 0.0719  0.0445  0.1150  738  HOH B O   
8131 O  O   . HOH P .   ? 0.2104 0.2163 0.1880 -0.0148 0.0266  0.0088  739  HOH B O   
8132 O  O   . HOH P .   ? 0.2921 0.6559 0.2990 0.1708  -0.0950 -0.1758 740  HOH B O   
8133 O  O   . HOH P .   ? 0.1348 0.1891 0.1286 0.0014  -0.0123 -0.0012 741  HOH B O   
8134 O  O   . HOH P .   ? 0.3065 0.4759 0.5478 0.0989  0.0834  -0.0619 742  HOH B O   
8135 O  O   . HOH P .   ? 0.1498 0.2396 0.1294 -0.0718 -0.0125 -0.0017 743  HOH B O   
8136 O  O   . HOH P .   ? 0.7345 0.2333 0.3933 -0.0484 0.2392  -0.0513 744  HOH B O   
8137 O  O   . HOH P .   ? 0.3247 0.2530 0.2619 0.0033  0.0543  -0.0115 745  HOH B O   
8138 O  O   . HOH P .   ? 0.5099 0.5494 0.3024 0.2003  0.0447  0.0291  746  HOH B O   
8139 O  O   . HOH P .   ? 0.2948 0.2372 0.2154 0.0774  0.0288  -0.0332 747  HOH B O   
8140 O  O   . HOH P .   ? 0.3164 0.2635 0.2448 -0.1109 -0.0077 0.0258  748  HOH B O   
8141 O  O   . HOH P .   ? 0.2854 0.3375 0.5683 -0.0431 -0.0049 -0.0761 749  HOH B O   
8142 O  O   . HOH P .   ? 0.3098 0.2882 0.1765 0.0269  0.0093  0.0059  750  HOH B O   
8143 O  O   . HOH P .   ? 0.2281 0.1901 0.1856 0.0235  0.0010  -0.0585 751  HOH B O   
8144 O  O   . HOH P .   ? 0.2566 0.2486 0.3183 -0.0632 -0.0086 -0.0347 752  HOH B O   
8145 O  O   . HOH P .   ? 0.2397 0.5641 0.5866 0.0543  -0.1267 0.1219  753  HOH B O   
8146 O  O   . HOH P .   ? 0.2830 0.6269 0.1847 0.0469  -0.0130 -0.0202 754  HOH B O   
8147 O  O   . HOH P .   ? 0.1779 0.3247 0.2059 -0.0046 -0.0041 -0.0226 755  HOH B O   
8148 O  O   . HOH P .   ? 0.3986 0.5292 0.3743 0.1083  0.0055  0.1966  756  HOH B O   
8149 O  O   . HOH P .   ? 0.6380 0.5777 0.5054 0.1979  0.2927  0.0927  757  HOH B O   
8150 O  O   . HOH P .   ? 0.4236 0.3245 0.6659 -0.1341 -0.1181 -0.0006 758  HOH B O   
8151 O  O   . HOH P .   ? 0.1832 0.1440 0.1820 0.0058  0.0052  0.0168  759  HOH B O   
8152 O  O   . HOH P .   ? 0.1601 0.2044 0.1147 -0.0262 0.0321  -0.0044 760  HOH B O   
8153 O  O   . HOH P .   ? 0.4631 0.2465 0.2968 -0.0502 -0.0026 -0.0265 761  HOH B O   
8154 O  O   . HOH P .   ? 0.5593 0.5168 0.3586 0.2834  0.1302  0.0743  762  HOH B O   
8155 O  O   . HOH P .   ? 0.3321 0.2723 0.2396 -0.0023 0.0274  -0.0250 763  HOH B O   
8156 O  O   . HOH P .   ? 0.2110 0.1839 0.1558 -0.0165 -0.0344 0.0056  764  HOH B O   
8157 O  O   . HOH P .   ? 0.5447 0.4377 0.3676 -0.0428 -0.0151 -0.0447 765  HOH B O   
8158 O  O   . HOH P .   ? 0.4435 0.3637 0.8187 0.0143  -0.3280 -0.0373 766  HOH B O   
8159 O  O   . HOH P .   ? 0.4119 0.7286 0.7180 -0.2145 -0.2070 0.3540  767  HOH B O   
8160 O  O   . HOH P .   ? 0.1999 0.2573 0.1900 -0.0356 -0.0579 0.0101  768  HOH B O   
8161 O  O   . HOH P .   ? 0.7523 0.6607 0.1929 0.0216  0.0378  0.0151  769  HOH B O   
8162 O  O   . HOH P .   ? 0.2718 0.2123 0.2397 -0.0100 0.0228  -0.0241 770  HOH B O   
8163 O  O   . HOH P .   ? 0.2726 0.2126 0.2013 0.0620  0.0024  -0.0071 771  HOH B O   
8164 O  O   . HOH P .   ? 0.2242 0.2619 0.3250 -0.0674 -0.0318 0.0963  772  HOH B O   
8165 O  O   . HOH P .   ? 0.3382 0.4032 0.8352 0.0965  0.2013  0.2836  773  HOH B O   
8166 O  O   . HOH P .   ? 0.4242 0.4436 0.5307 -0.1958 -0.0673 0.2120  774  HOH B O   
8167 O  O   . HOH P .   ? 0.7664 0.5113 0.5003 0.0881  -0.0598 -0.2841 775  HOH B O   
8168 O  O   . HOH P .   ? 0.8591 0.6129 0.3531 0.3373  0.1242  0.0013  776  HOH B O   
8169 O  O   . HOH P .   ? 0.1912 0.1852 0.1746 -0.0046 -0.0222 -0.0251 777  HOH B O   
8170 O  O   . HOH P .   ? 0.2660 0.1748 0.2383 -0.0294 0.0262  0.0061  778  HOH B O   
8171 O  O   . HOH P .   ? 0.3809 0.8976 0.5354 -0.2172 -0.1340 0.3693  779  HOH B O   
8172 O  O   . HOH P .   ? 0.7581 0.4844 0.5534 -0.1401 0.1342  -0.1435 780  HOH B O   
8173 O  O   . HOH P .   ? 0.1862 0.2555 0.1953 0.0184  -0.0049 -0.0407 781  HOH B O   
8174 O  O   . HOH P .   ? 0.2059 0.2574 0.3315 -0.0421 -0.0011 -0.0103 782  HOH B O   
8175 O  O   . HOH P .   ? 0.2969 0.5373 0.3296 -0.1795 -0.0375 -0.0482 783  HOH B O   
8176 O  O   . HOH P .   ? 1.0159 0.5526 0.6176 0.1859  -0.1568 0.2292  784  HOH B O   
8177 O  O   . HOH P .   ? 0.2927 0.3091 0.3488 -0.0163 -0.0165 -0.0410 785  HOH B O   
8178 O  O   . HOH P .   ? 0.1759 0.2402 0.1594 -0.0307 -0.0265 -0.0408 786  HOH B O   
8179 O  O   . HOH P .   ? 0.2338 0.2508 0.3695 -0.1146 -0.0705 0.0063  787  HOH B O   
8180 O  O   . HOH P .   ? 0.1729 0.1735 0.2402 -0.0143 0.0264  -0.0284 788  HOH B O   
8181 O  O   . HOH P .   ? 0.4593 0.7113 0.5038 -0.0664 -0.2665 0.1029  789  HOH B O   
8182 O  O   . HOH P .   ? 0.8616 0.4562 0.4933 -0.0666 -0.0504 -0.0353 790  HOH B O   
8183 O  O   . HOH P .   ? 0.2508 0.2141 0.3421 0.0232  0.0461  0.0593  791  HOH B O   
8184 O  O   . HOH P .   ? 0.3171 0.4271 0.5368 -0.0361 0.0802  0.1320  792  HOH B O   
8185 O  O   . HOH P .   ? 0.7861 0.3553 0.4962 0.0765  -0.0393 -0.0066 793  HOH B O   
8186 O  O   . HOH P .   ? 0.1894 0.2236 0.1569 0.0173  -0.0111 0.0373  794  HOH B O   
8187 O  O   . HOH P .   ? 0.9455 0.5914 0.7032 0.2836  0.0353  -0.2649 795  HOH B O   
8188 O  O   . HOH P .   ? 0.1574 0.3016 0.2001 0.0122  -0.0105 -0.0556 796  HOH B O   
8189 O  O   . HOH P .   ? 0.6266 0.4811 0.3885 -0.2082 -0.2314 0.1751  797  HOH B O   
8190 O  O   . HOH P .   ? 0.2122 0.3064 0.2661 -0.0102 0.0108  -0.0866 798  HOH B O   
8191 O  O   . HOH P .   ? 0.2337 0.2434 0.1916 -0.0497 -0.0004 -0.0318 799  HOH B O   
8192 O  O   . HOH P .   ? 0.5626 0.3503 0.4961 -0.0248 -0.2450 -0.0201 800  HOH B O   
8193 O  O   . HOH P .   ? 0.1013 0.1907 0.1851 0.0324  0.0060  0.0012  801  HOH B O   
8194 O  O   . HOH P .   ? 0.2575 0.2377 0.3019 -0.0466 -0.0178 0.0338  802  HOH B O   
8195 O  O   . HOH P .   ? 0.3052 0.4038 0.4607 -0.0872 0.0009  -0.1638 803  HOH B O   
8196 O  O   . HOH P .   ? 0.6422 0.7973 0.5978 0.4015  0.1177  0.0262  804  HOH B O   
8197 O  O   . HOH P .   ? 0.7883 0.5557 0.5107 -0.0403 0.1983  -0.1635 805  HOH B O   
8198 O  O   . HOH P .   ? 0.2586 0.4934 0.3707 -0.0638 0.0794  -0.1634 806  HOH B O   
8199 O  O   . HOH P .   ? 0.2261 0.2106 0.1712 0.0039  -0.0482 -0.0483 807  HOH B O   
8200 O  O   . HOH P .   ? 0.2042 0.1513 0.1792 0.0365  -0.0269 -0.0020 808  HOH B O   
8201 O  O   . HOH P .   ? 0.2896 0.4099 0.9311 0.0401  0.1627  0.0110  809  HOH B O   
8202 O  O   . HOH P .   ? 0.4029 0.2706 0.3330 -0.0226 0.0447  -0.0214 810  HOH B O   
8203 O  O   . HOH P .   ? 0.5532 0.8396 0.5093 -0.2013 -0.1040 -0.2458 811  HOH B O   
8204 O  O   . HOH P .   ? 0.1794 0.1435 0.2378 -0.0033 -0.0146 0.0813  812  HOH B O   
8205 O  O   . HOH P .   ? 0.4442 0.4436 0.3369 0.0396  -0.0192 0.1180  813  HOH B O   
8206 O  O   . HOH P .   ? 0.4780 0.7575 0.3924 -0.1830 -0.0841 0.1869  814  HOH B O   
8207 O  O   . HOH P .   ? 0.3436 0.3616 0.6773 -0.0455 0.0706  0.2315  815  HOH B O   
8208 O  O   . HOH P .   ? 0.1913 0.2438 0.2233 0.0384  -0.0036 0.0395  816  HOH B O   
8209 O  O   . HOH P .   ? 0.1904 0.2324 0.1711 -0.0483 -0.0062 -0.0671 817  HOH B O   
8210 O  O   . HOH P .   ? 0.5204 0.5498 0.6782 -0.0392 0.0543  -0.2445 818  HOH B O   
8211 O  O   . HOH P .   ? 1.0076 0.2641 0.6869 0.0636  -0.0367 -0.0097 819  HOH B O   
8212 O  O   . HOH P .   ? 0.4068 0.3495 0.1996 -0.0375 0.0076  -0.0030 820  HOH B O   
8213 O  O   . HOH P .   ? 0.7398 0.4367 0.7684 0.1990  -0.2957 -0.2509 821  HOH B O   
8214 O  O   . HOH P .   ? 0.8219 0.5516 0.5703 -0.0816 0.2062  -0.0754 822  HOH B O   
8215 O  O   . HOH P .   ? 0.8734 0.6287 0.8490 0.2444  0.1969  0.0893  823  HOH B O   
8216 O  O   . HOH P .   ? 0.2024 0.1841 0.1296 -0.0447 0.0079  -0.0059 824  HOH B O   
8217 O  O   . HOH P .   ? 0.1414 0.1671 0.1564 -0.0108 0.0418  0.0093  825  HOH B O   
8218 O  O   . HOH P .   ? 0.2919 0.5565 0.8688 -0.0365 -0.0304 -0.1314 826  HOH B O   
8219 O  O   . HOH P .   ? 0.2436 0.2308 0.2350 -0.0141 -0.0103 -0.0360 827  HOH B O   
8220 O  O   . HOH P .   ? 0.9106 0.7378 0.3098 -0.1455 0.0419  -0.0976 828  HOH B O   
8221 O  O   . HOH P .   ? 0.2939 0.5494 0.4199 0.1372  -0.0118 0.0193  829  HOH B O   
8222 O  O   . HOH P .   ? 0.6666 0.6360 0.7456 0.3095  0.3201  0.1766  830  HOH B O   
8223 O  O   . HOH P .   ? 0.2412 0.1957 0.3321 0.0104  0.0528  0.0548  831  HOH B O   
8224 O  O   . HOH P .   ? 0.2417 0.3776 0.3742 0.0838  0.0491  0.1200  832  HOH B O   
8225 O  O   . HOH P .   ? 0.3787 0.6399 0.3799 0.1287  -0.0543 0.1239  833  HOH B O   
8226 O  O   . HOH P .   ? 0.4326 0.4636 0.2206 0.0657  -0.0813 -0.1422 834  HOH B O   
8227 O  O   . HOH P .   ? 0.3448 0.3739 0.2918 -0.0111 0.0963  -0.0483 835  HOH B O   
8228 O  O   . HOH P .   ? 0.4107 0.2529 0.2259 0.0324  0.1289  -0.0027 836  HOH B O   
8229 O  O   . HOH P .   ? 0.1978 0.3861 0.5968 0.0305  -0.0513 -0.2460 837  HOH B O   
8230 O  O   . HOH P .   ? 0.3760 0.4548 0.7213 -0.0328 -0.0468 0.2366  838  HOH B O   
8231 O  O   . HOH P .   ? 0.3942 0.2473 0.6472 0.0527  0.0852  0.0266  839  HOH B O   
8232 O  O   . HOH P .   ? 0.8366 0.2938 0.7565 0.0021  -0.1151 -0.1731 840  HOH B O   
8233 O  O   . HOH P .   ? 0.2357 0.4707 0.2490 -0.1368 -0.0525 0.0644  841  HOH B O   
8234 O  O   . HOH P .   ? 0.5715 0.1682 0.5986 0.0869  0.0060  -0.0033 842  HOH B O   
8235 O  O   . HOH P .   ? 0.4571 0.8356 0.2408 -0.0179 0.0508  -0.0439 843  HOH B O   
8236 O  O   . HOH P .   ? 0.5769 0.6142 0.3251 0.1119  -0.0886 0.1554  844  HOH B O   
8237 O  O   . HOH P .   ? 0.4715 0.8091 0.7695 0.1157  0.1730  0.1418  845  HOH B O   
8238 O  O   . HOH P .   ? 0.6097 0.5614 0.5448 0.0623  -0.0921 -0.1105 846  HOH B O   
8239 O  O   . HOH P .   ? 0.5274 0.4406 0.4356 -0.1568 0.0158  -0.0126 847  HOH B O   
8240 O  O   . HOH P .   ? 0.4551 0.3188 0.6404 -0.0942 0.1076  -0.0506 848  HOH B O   
8241 O  O   . HOH P .   ? 0.2668 0.8710 0.3520 -0.1463 -0.0021 -0.0858 849  HOH B O   
8242 O  O   . HOH P .   ? 0.6552 0.3800 0.7039 0.0944  0.1710  0.2013  850  HOH B O   
8243 O  O   . HOH P .   ? 0.6930 0.4785 0.6424 -0.2844 -0.0813 0.1014  851  HOH B O   
8244 O  O   . HOH P .   ? 0.7199 0.4797 0.5251 0.0283  0.3518  -0.0410 852  HOH B O   
8245 O  O   . HOH P .   ? 0.3551 0.6142 0.4293 -0.0748 0.1091  -0.0336 853  HOH B O   
8246 O  O   . HOH P .   ? 0.3431 0.3184 0.2575 0.0683  -0.0263 -0.0240 854  HOH B O   
8247 O  O   . HOH P .   ? 0.3993 0.3680 0.4730 -0.0113 0.0870  0.1246  855  HOH B O   
8248 O  O   . HOH P .   ? 0.2384 0.2699 0.2032 -0.0496 0.0099  -0.0405 856  HOH B O   
8249 O  O   . HOH P .   ? 0.1602 0.1485 0.2002 0.0054  -0.0368 -0.0051 857  HOH B O   
8250 O  O   . HOH P .   ? 0.3714 0.5267 0.4186 0.0754  0.0654  0.2000  858  HOH B O   
8251 O  O   . HOH P .   ? 0.6037 0.4537 0.3962 -0.1004 0.1150  -0.2188 859  HOH B O   
8252 O  O   . HOH P .   ? 0.3682 0.8446 0.5684 -0.0131 0.1304  0.1142  860  HOH B O   
8253 O  O   . HOH P .   ? 0.2316 0.5136 0.2535 0.0457  -0.0119 -0.0358 861  HOH B O   
8254 O  O   . HOH P .   ? 0.8081 0.4657 0.6417 -0.1877 0.1327  -0.2670 862  HOH B O   
8255 O  O   . HOH P .   ? 0.4725 0.4675 0.2185 -0.0894 0.0201  -0.0121 863  HOH B O   
8256 O  O   . HOH P .   ? 0.1768 0.2865 0.2230 -0.0652 0.0314  0.0602  864  HOH B O   
8257 O  O   . HOH P .   ? 0.4184 0.5454 0.2619 -0.1011 -0.0394 0.1405  865  HOH B O   
8258 O  O   . HOH P .   ? 0.3282 0.3976 0.2311 -0.0100 0.0227  0.0028  866  HOH B O   
8259 O  O   . HOH P .   ? 0.3770 0.8405 0.2348 0.1828  -0.0125 -0.0644 867  HOH B O   
8260 O  O   . HOH P .   ? 0.2896 0.3260 0.2063 0.0738  -0.0062 -0.0344 868  HOH B O   
8261 O  O   . HOH P .   ? 0.7403 0.5910 0.3071 -0.0140 -0.1098 -0.1508 869  HOH B O   
8262 O  O   . HOH P .   ? 0.3138 0.9378 0.3508 -0.0206 0.0784  -0.0059 870  HOH B O   
8263 O  O   . HOH P .   ? 0.4603 0.4376 0.4381 -0.0851 0.0656  -0.1211 871  HOH B O   
8264 O  O   . HOH P .   ? 0.3320 0.4074 0.7429 0.0581  -0.2127 -0.1767 872  HOH B O   
8265 O  O   . HOH P .   ? 0.2786 0.2073 0.2963 0.0044  0.0210  0.0180  873  HOH B O   
8266 O  O   . HOH P .   ? 1.0139 0.3913 0.3272 0.1755  0.0574  -0.0561 874  HOH B O   
8267 O  O   . HOH P .   ? 0.5630 0.3077 0.4057 0.0692  -0.2656 -0.0730 875  HOH B O   
8268 O  O   . HOH P .   ? 0.7645 0.3975 0.6020 -0.0459 -0.0352 0.1341  876  HOH B O   
8269 O  O   . HOH P .   ? 0.3403 0.3034 0.3220 0.0604  -0.0203 0.0511  877  HOH B O   
8270 O  O   . HOH P .   ? 0.3764 0.3331 0.4525 -0.0803 0.0743  -0.0240 878  HOH B O   
8271 O  O   . HOH P .   ? 0.2378 0.3563 0.2979 -0.0551 0.0276  0.0544  879  HOH B O   
8272 O  O   . HOH P .   ? 0.3749 0.3610 0.6129 0.0462  0.1046  -0.0797 880  HOH B O   
8273 O  O   . HOH P .   ? 0.3542 0.2624 0.4572 -0.1012 -0.1587 -0.0400 881  HOH B O   
8274 O  O   . HOH P .   ? 0.3490 0.3208 0.5505 0.0440  0.0248  -0.0598 882  HOH B O   
8275 O  O   . HOH P .   ? 0.5598 0.2140 0.5215 0.0809  0.1536  -0.0083 883  HOH B O   
8276 O  O   . HOH P .   ? 0.4458 0.3306 0.7059 -0.1418 -0.0356 -0.0704 884  HOH B O   
8277 O  O   . HOH P .   ? 0.3813 0.4435 0.2752 0.0955  -0.0847 -0.0374 885  HOH B O   
8278 O  O   . HOH P .   ? 0.3537 0.3326 0.4543 0.1097  -0.0211 0.0254  886  HOH B O   
8279 O  O   . HOH P .   ? 0.5429 0.4562 0.3358 -0.0942 0.0021  0.1328  887  HOH B O   
8280 O  O   . HOH P .   ? 0.3451 0.3318 0.2438 0.0811  -0.0820 -0.0548 888  HOH B O   
8281 O  O   . HOH P .   ? 0.4028 0.4509 0.4099 0.1736  0.1240  0.0435  889  HOH B O   
8282 O  O   . HOH P .   ? 0.2432 0.5299 0.2930 -0.0151 -0.0450 0.0734  890  HOH B O   
8283 O  O   . HOH P .   ? 0.7483 0.7920 0.6223 -0.0906 0.2030  0.0584  891  HOH B O   
8284 O  O   . HOH P .   ? 0.6023 0.1891 0.2750 0.0616  0.2036  0.0286  892  HOH B O   
8285 O  O   . HOH P .   ? 0.3661 0.6830 0.5809 -0.2115 0.0516  -0.2553 893  HOH B O   
8286 O  O   . HOH P .   ? 0.2724 0.3625 0.2356 -0.0218 -0.0713 0.1029  894  HOH B O   
8287 O  O   . HOH P .   ? 0.2631 0.1551 0.3082 -0.0195 -0.0028 0.0475  895  HOH B O   
8288 O  O   . HOH P .   ? 0.5883 0.5074 0.5177 -0.0920 -0.0207 0.1475  896  HOH B O   
8289 O  O   . HOH P .   ? 0.9185 0.3234 0.3351 -0.1573 0.0414  -0.0724 897  HOH B O   
8290 O  O   . HOH P .   ? 0.4771 0.2661 0.2311 -0.0851 -0.1184 -0.0250 898  HOH B O   
8291 O  O   . HOH P .   ? 0.4690 0.3503 0.2334 -0.0068 -0.0124 -0.1024 899  HOH B O   
8292 O  O   . HOH P .   ? 0.2618 0.1898 0.2487 0.0075  0.0658  0.0355  900  HOH B O   
8293 O  O   . HOH P .   ? 0.3131 0.1883 0.4527 -0.0582 -0.0302 -0.0545 901  HOH B O   
8294 O  O   . HOH P .   ? 0.3978 0.2517 0.4726 0.0317  0.2369  0.0934  902  HOH B O   
8295 O  O   . HOH P .   ? 0.3736 0.6236 0.4420 -0.1300 -0.0612 0.2061  903  HOH B O   
8296 O  O   . HOH P .   ? 0.6577 0.5120 0.6372 0.1019  0.1543  0.1878  904  HOH B O   
8297 O  O   . HOH P .   ? 0.7722 0.8387 0.5203 0.4486  -0.0036 0.1245  905  HOH B O   
8298 O  O   . HOH P .   ? 0.2742 0.1995 0.2867 -0.0261 -0.0797 -0.0510 906  HOH B O   
8299 O  O   . HOH P .   ? 0.4568 0.2577 0.2607 -0.0220 0.0066  0.0653  907  HOH B O   
8300 O  O   . HOH P .   ? 0.3320 0.5620 0.2964 -0.1052 0.0698  -0.1465 908  HOH B O   
8301 O  O   . HOH P .   ? 0.2773 0.3178 0.4128 -0.0904 -0.0510 0.0561  909  HOH B O   
8302 O  O   . HOH P .   ? 0.2565 0.2429 0.2302 0.0358  0.0395  0.0243  910  HOH B O   
8303 O  O   . HOH P .   ? 0.4524 0.4432 0.5087 -0.1680 -0.2595 0.1633  911  HOH B O   
8304 O  O   . HOH P .   ? 0.2762 0.3444 0.2605 -0.1378 0.0497  -0.0271 912  HOH B O   
8305 O  O   . HOH P .   ? 0.5923 0.2056 0.2594 0.0513  0.0588  -0.0396 913  HOH B O   
8306 O  O   . HOH P .   ? 1.0447 0.3481 0.5789 -0.0381 0.3063  0.0619  914  HOH B O   
8307 O  O   . HOH P .   ? 0.6686 0.5287 0.3211 0.2010  0.0230  0.0922  915  HOH B O   
8308 O  O   . HOH P .   ? 0.2918 0.2929 0.5060 -0.0308 0.1965  0.0474  916  HOH B O   
8309 O  O   . HOH P .   ? 0.2255 0.5602 0.6853 0.0343  0.0236  -0.2301 917  HOH B O   
8310 O  O   . HOH P .   ? 0.4385 0.4106 0.8152 0.1634  -0.1500 -0.2276 918  HOH B O   
8311 O  O   . HOH P .   ? 0.8697 0.5724 0.3848 -0.0947 0.1900  0.1447  919  HOH B O   
8312 O  O   . HOH P .   ? 0.3159 0.4802 0.7066 0.0029  -0.0054 -0.3375 920  HOH B O   
8313 O  O   . HOH P .   ? 0.2473 0.3762 0.6202 -0.0186 -0.0904 -0.0132 921  HOH B O   
8314 O  O   . HOH P .   ? 0.2846 0.3554 0.2894 -0.0153 0.1043  0.0502  922  HOH B O   
8315 O  O   . HOH P .   ? 0.6564 0.6719 0.3445 0.3641  0.1034  0.0285  923  HOH B O   
8316 O  O   . HOH P .   ? 0.5205 0.6105 0.9556 -0.0938 0.1803  -0.2988 924  HOH B O   
8317 O  O   . HOH P .   ? 0.7516 0.3356 0.7870 -0.2074 -0.0645 -0.1370 925  HOH B O   
8318 O  O   . HOH P .   ? 0.2995 0.2168 0.3676 0.0489  0.0830  0.0549  926  HOH B O   
8319 O  O   . HOH P .   ? 0.4829 0.3446 0.2894 -0.1212 0.1435  -0.0572 927  HOH B O   
8320 O  O   . HOH P .   ? 0.7124 0.2395 0.5692 0.0449  -0.0417 0.0086  928  HOH B O   
8321 O  O   . HOH P .   ? 0.6004 0.6268 0.7807 -0.1448 -0.1354 0.1859  929  HOH B O   
8322 O  O   . HOH P .   ? 0.4149 0.4035 0.8681 0.0646  -0.0960 0.2406  930  HOH B O   
8323 O  O   . HOH P .   ? 0.3571 0.5601 0.8315 0.1082  0.1960  0.3462  931  HOH B O   
8324 O  O   . HOH P .   ? 0.4076 1.1605 0.5715 -0.1282 0.1344  -0.1331 932  HOH B O   
8325 O  O   . HOH P .   ? 0.4301 0.3655 0.8151 -0.0691 -0.2998 0.0254  933  HOH B O   
8326 O  O   . HOH P .   ? 0.5250 0.3596 0.4454 0.1534  -0.0242 -0.1243 934  HOH B O   
8327 O  O   . HOH P .   ? 0.5194 0.4871 0.6019 0.0199  -0.2222 0.2296  935  HOH B O   
8328 O  O   . HOH P .   ? 0.6393 0.3938 0.2731 0.2589  -0.1561 -0.0983 936  HOH B O   
8329 O  O   B HOH P .   ? 0.1864 0.1941 0.1865 0.0261  -0.1086 -0.0334 937  HOH B O   
8330 O  O   . HOH P .   ? 0.4967 0.4722 0.6098 0.1738  -0.2753 -0.2190 938  HOH B O   
8331 O  O   . HOH P .   ? 0.5129 0.5272 0.6841 0.0105  -0.1930 -0.3004 939  HOH B O   
8332 O  O   . HOH P .   ? 0.5023 0.2215 0.5365 0.0020  0.0680  -0.1528 940  HOH B O   
8333 O  O   . HOH P .   ? 0.3236 0.7124 0.5319 -0.1663 -0.0646 0.0712  941  HOH B O   
8334 O  O   . HOH P .   ? 0.3907 0.5269 0.7253 -0.0809 -0.2705 -0.0179 942  HOH B O   
8335 O  O   . HOH P .   ? 0.4529 0.7261 0.6937 0.0819  -0.0026 -0.1925 943  HOH B O   
8336 O  O   . HOH P .   ? 0.6255 0.6955 0.2205 -0.1326 -0.0269 0.0344  944  HOH B O   
8337 O  O   . HOH P .   ? 0.3551 0.9980 0.6452 0.1284  0.1320  0.2679  945  HOH B O   
8338 O  O   . HOH P .   ? 0.3593 0.5924 0.4559 -0.2330 -0.1231 0.1869  946  HOH B O   
8339 O  O   . HOH P .   ? 0.3140 0.1970 0.2961 -0.0874 0.0901  -0.0323 947  HOH B O   
8340 O  O   . HOH P .   ? 0.6769 0.5109 0.6723 0.2075  -0.2792 -0.2131 948  HOH B O   
8341 O  O   . HOH P .   ? 0.3723 0.2646 0.5155 -0.0420 -0.1235 0.1341  949  HOH B O   
8342 O  O   . HOH P .   ? 0.9203 0.2967 0.5880 -0.0894 0.3011  -0.0054 950  HOH B O   
8343 O  O   . HOH P .   ? 0.3572 0.4075 0.5615 0.1286  0.1771  0.1893  951  HOH B O   
8344 O  O   . HOH P .   ? 0.4425 0.5416 0.5284 -0.0036 0.2533  0.1477  952  HOH B O   
8345 O  O   . HOH P .   ? 0.4551 0.6623 0.5210 -0.1860 -0.1964 0.0049  953  HOH B O   
8346 O  O   . HOH P .   ? 0.4936 0.5761 0.8552 -0.2476 0.1916  0.0252  954  HOH B O   
8347 O  O   . HOH P .   ? 0.3070 0.7902 0.3082 0.0920  0.0466  0.1504  955  HOH B O   
8348 O  O   . HOH P .   ? 0.8717 0.6998 0.5967 0.4418  -0.0757 -0.1497 956  HOH B O   
8349 O  O   . HOH P .   ? 0.6157 0.7555 0.9288 -0.1682 -0.0679 -0.0473 957  HOH B O   
8350 O  O   . HOH P .   ? 0.1928 0.2651 0.2456 0.0399  -0.0417 0.0157  958  HOH B O   
8351 O  O   . HOH P .   ? 0.3050 0.3945 0.4913 -0.0003 0.0131  -0.1112 959  HOH B O   
8352 O  O   . HOH P .   ? 0.6437 0.5749 0.4546 -0.0128 -0.0325 -0.0466 960  HOH B O   
8353 O  O   . HOH P .   ? 0.4137 0.6109 0.4411 -0.1900 0.0322  -0.0619 961  HOH B O   
8354 O  O   . HOH P .   ? 0.6804 0.4493 0.5661 0.2094  -0.0024 0.1818  962  HOH B O   
8355 O  O   . HOH P .   ? 0.5764 0.6132 0.4075 -0.1706 0.1281  -0.1027 963  HOH B O   
8356 O  O   . HOH P .   ? 0.6030 0.7497 0.5356 -0.1952 0.2162  -0.0521 964  HOH B O   
8357 O  O   . HOH P .   ? 0.3361 0.6101 0.5479 -0.1475 0.0981  0.1293  965  HOH B O   
8358 O  O   . HOH P .   ? 0.3484 0.5774 0.2949 -0.0025 0.0432  0.0137  966  HOH B O   
8359 O  O   . HOH P .   ? 0.2997 0.4550 0.6235 -0.0060 0.0319  0.2085  967  HOH B O   
8360 O  O   . HOH P .   ? 0.3499 0.3646 0.2466 0.0596  0.0138  0.0278  968  HOH B O   
8361 O  O   . HOH P .   ? 0.6763 0.5739 0.8033 0.0040  0.2463  -0.1187 969  HOH B O   
8362 O  O   . HOH P .   ? 0.6139 0.3181 0.4479 0.0078  -0.2131 -0.0138 970  HOH B O   
8363 O  O   . HOH P .   ? 0.4274 0.4483 0.2714 0.0938  0.0320  0.0249  971  HOH B O   
8364 O  O   . HOH P .   ? 0.7362 0.6199 0.5516 -0.2295 -0.1307 -0.1037 972  HOH B O   
8365 O  O   . HOH P .   ? 0.4085 0.7666 0.7361 -0.1832 0.1398  0.0674  973  HOH B O   
8366 O  O   . HOH P .   ? 0.5437 0.4766 0.5387 -0.2513 0.0018  -0.1094 974  HOH B O   
8367 O  O   . HOH P .   ? 0.6226 0.6776 0.6442 0.3565  0.0872  0.2010  975  HOH B O   
8368 O  O   . HOH P .   ? 0.4448 0.4362 0.5952 -0.0952 0.1986  0.0596  976  HOH B O   
8369 O  O   . HOH P .   ? 0.9256 0.6152 0.3906 -0.1393 -0.0790 0.2208  977  HOH B O   
8370 O  O   . HOH P .   ? 0.5064 0.7599 0.5781 -0.1856 -0.1818 0.3322  978  HOH B O   
8371 O  O   . HOH P .   ? 0.5110 0.3999 0.4493 0.2335  -0.1963 -0.1587 979  HOH B O   
8372 O  O   . HOH P .   ? 0.4111 0.3929 0.5407 0.0107  -0.1361 0.0259  980  HOH B O   
8373 O  O   . HOH P .   ? 0.6339 0.6598 0.4557 0.3761  -0.1195 -0.1411 981  HOH B O   
8374 O  O   . HOH P .   ? 0.3314 0.5620 0.6122 -0.1303 0.1736  -0.3138 982  HOH B O   
8375 O  O   . HOH P .   ? 0.2723 0.5839 0.5087 0.0623  0.1035  -0.0791 983  HOH B O   
8376 O  O   . HOH P .   ? 0.5479 0.8959 0.6096 0.0136  0.0394  0.2608  984  HOH B O   
8377 O  O   . HOH P .   ? 0.7356 0.7333 0.6954 -0.0206 0.2347  -0.0614 985  HOH B O   
8378 O  O   . HOH P .   ? 0.4833 0.5807 0.9040 -0.1512 0.1986  -0.0895 986  HOH B O   
8379 O  O   . HOH P .   ? 0.5629 0.8410 0.5209 -0.0001 -0.1063 0.0318  987  HOH B O   
8380 O  O   . HOH P .   ? 0.8714 0.5275 0.4852 0.0449  0.0474  0.0194  988  HOH B O   
8381 O  O   . HOH P .   ? 0.2581 0.1610 0.1616 -0.0074 -0.0211 0.0131  989  HOH B O   
8382 O  O   . HOH P .   ? 0.6970 0.4838 0.3960 0.0050  0.1586  -0.0164 990  HOH B O   
8383 O  O   . HOH P .   ? 0.5705 0.3771 0.7293 -0.0673 0.2605  -0.0827 991  HOH B O   
8384 O  O   . HOH P .   ? 0.3927 0.6099 0.4322 0.2043  -0.1252 -0.1900 992  HOH B O   
8385 O  O   . HOH P .   ? 0.4941 0.8167 0.3782 -0.2822 -0.0491 -0.0932 993  HOH B O   
8386 O  O   . HOH P .   ? 0.6230 0.3448 0.5427 0.1383  -0.2757 -0.0876 994  HOH B O   
8387 O  O   . HOH P .   ? 0.5755 0.7649 0.3431 -0.1856 0.0630  0.0176  995  HOH B O   
8388 O  O   . HOH P .   ? 0.6348 0.8345 0.7720 0.0637  0.0353  -0.0692 996  HOH B O   
8389 O  O   . HOH P .   ? 0.5415 0.7515 0.4986 0.1144  0.0053  0.1363  997  HOH B O   
8390 O  O   . HOH P .   ? 0.5465 0.3983 0.1771 -0.1374 0.0603  -0.0119 998  HOH B O   
8391 O  O   . HOH P .   ? 0.7430 0.6807 0.5648 0.3719  -0.0473 0.1428  999  HOH B O   
8392 O  O   . HOH P .   ? 0.6553 0.7805 0.3928 -0.1987 -0.0648 0.0113  1000 HOH B O   
8393 O  O   . HOH P .   ? 0.2919 0.6089 0.4059 0.1760  -0.1071 -0.2499 1001 HOH B O   
8394 O  O   . HOH P .   ? 0.3300 0.5812 0.5261 0.0960  -0.0097 0.0965  1002 HOH B O   
8395 O  O   . HOH P .   ? 0.5375 0.4305 0.9462 0.1064  -0.0989 0.2478  1003 HOH B O   
8396 O  O   . HOH P .   ? 0.4884 0.5042 0.2699 -0.1900 0.0178  0.0488  1004 HOH B O   
8397 O  O   . HOH P .   ? 0.5036 0.3285 0.5966 -0.1516 0.1216  0.0091  1005 HOH B O   
8398 O  O   . HOH P .   ? 1.0082 0.4684 0.5471 -0.2115 -0.1452 0.0596  1006 HOH B O   
8399 O  O   . HOH P .   ? 0.3970 0.7737 0.4234 -0.0162 0.0092  -0.2203 1007 HOH B O   
8400 O  O   . HOH P .   ? 0.3076 0.8093 0.2739 0.0703  -0.0494 -0.1654 1008 HOH B O   
8401 O  O   . HOH P .   ? 0.6014 0.2195 0.6422 0.0856  0.0096  -0.0153 1009 HOH B O   
8402 O  O   . HOH P .   ? 0.4334 0.6565 0.4722 0.0468  -0.0317 0.1648  1010 HOH B O   
8403 O  O   . HOH P .   ? 0.5576 0.7623 0.6627 0.1151  -0.2617 0.0387  1011 HOH B O   
8404 O  O   . HOH P .   ? 0.3610 0.8722 0.9383 0.1266  0.1996  0.1845  1012 HOH B O   
8405 O  O   . HOH P .   ? 0.5298 0.4925 0.7135 -0.0457 0.0164  0.2880  1013 HOH B O   
8406 O  O   . HOH P .   ? 0.6153 0.3651 0.4368 -0.0064 -0.1655 -0.0438 1014 HOH B O   
8407 O  O   . HOH P .   ? 0.2344 0.4189 0.5111 -0.0872 -0.0978 0.0033  1015 HOH B O   
8408 O  O   . HOH P .   ? 1.0218 0.4289 0.4729 0.2085  0.1494  0.1572  1016 HOH B O   
8409 O  O   . HOH P .   ? 0.4874 0.5652 0.6819 0.1461  -0.0921 0.0655  1017 HOH B O   
8410 O  O   . HOH P .   ? 0.3544 0.2700 0.4165 -0.0428 -0.0788 -0.1539 1018 HOH B O   
8411 O  O   . HOH P .   ? 1.0226 0.4137 0.6105 -0.1002 -0.0957 0.1254  1019 HOH B O   
8412 O  O   . HOH P .   ? 0.5808 0.4924 0.7691 0.0904  -0.1591 0.0524  1020 HOH B O   
8413 O  O   . HOH P .   ? 0.2473 0.6194 0.4366 -0.0038 -0.0841 -0.0120 1021 HOH B O   
8414 O  O   . HOH P .   ? 0.2383 0.3123 0.3880 -0.0406 -0.1536 0.0699  1022 HOH B O   
8415 O  O   . HOH P .   ? 0.5339 0.4565 0.2927 -0.0127 -0.1683 -0.0379 1023 HOH B O   
8416 O  O   . HOH P .   ? 0.8750 0.4507 0.6188 0.2085  -0.0700 -0.1684 1024 HOH B O   
8417 O  O   . HOH P .   ? 0.8512 0.5046 0.5646 -0.0556 0.1672  0.0254  1025 HOH B O   
8418 O  O   . HOH P .   ? 0.2977 0.3686 0.3798 0.0909  -0.0576 -0.2134 1026 HOH B O   
8419 O  O   . HOH P .   ? 0.3924 0.4200 0.3419 -0.0007 0.0800  0.1097  1027 HOH B O   
8420 O  O   . HOH P .   ? 0.3429 0.3306 0.7166 0.0659  -0.0310 0.1223  1028 HOH B O   
8421 O  O   . HOH P .   ? 0.3646 1.0589 0.5516 0.1455  -0.1022 -0.1231 1029 HOH B O   
8422 O  O   . HOH P .   ? 0.5657 0.2785 0.7742 0.0073  0.0386  -0.1930 1030 HOH B O   
8423 O  O   . HOH P .   ? 0.5021 0.8475 0.4876 -0.0128 0.1605  0.0868  1031 HOH B O   
8424 O  O   . HOH P .   ? 0.6133 1.0386 0.5089 0.0530  -0.0598 0.1725  1032 HOH B O   
8425 O  O   . HOH P .   ? 0.4144 0.3748 0.4665 -0.0004 0.0102  0.0928  1033 HOH B O   
8426 O  O   . HOH P .   ? 0.5471 0.4132 0.6852 -0.1307 0.0672  -0.0896 1034 HOH B O   
8427 O  O   . HOH P .   ? 0.4635 0.3132 0.5463 -0.0909 0.0231  0.1109  1035 HOH B O   
8428 O  O   . HOH P .   ? 0.7296 0.2748 0.6964 -0.0469 0.2995  0.0362  1036 HOH B O   
8429 O  O   . HOH P .   ? 0.2283 0.3636 0.2599 0.0257  -0.0508 0.0225  1037 HOH B O   
8430 O  O   . HOH P .   ? 0.3014 0.3461 0.3312 0.0978  -0.0669 -0.0148 1038 HOH B O   
8431 O  O   . HOH P .   ? 0.6556 0.5107 0.3413 -0.0837 0.0533  0.2163  1039 HOH B O   
8432 O  O   . HOH P .   ? 0.6285 0.5032 0.7301 -0.2316 -0.2440 -0.0621 1040 HOH B O   
8433 O  O   . HOH P .   ? 0.6824 0.5868 0.4411 -0.1658 0.2266  0.0921  1041 HOH B O   
8434 O  O   . HOH P .   ? 0.3792 0.6058 0.3309 0.1075  0.0800  0.1803  1042 HOH B O   
8435 O  O   . HOH P .   ? 0.6288 0.4885 0.5408 0.0838  0.2342  0.0707  1043 HOH B O   
8436 O  O   . HOH P .   ? 0.5744 0.4870 0.3714 -0.0648 0.1606  0.0383  1044 HOH B O   
8437 O  O   . HOH P .   ? 0.3769 0.4874 0.3282 0.0026  -0.0671 -0.1841 1045 HOH B O   
8438 O  O   . HOH P .   ? 0.4583 0.4533 1.0050 -0.0482 0.0910  -0.2648 1046 HOH B O   
8439 O  O   . HOH P .   ? 0.3704 0.8096 0.4666 0.2404  -0.1101 -0.2650 1047 HOH B O   
8440 O  O   . HOH P .   ? 0.5163 0.4809 0.7757 0.1016  0.3288  -0.0249 1048 HOH B O   
8441 O  O   . HOH P .   ? 0.5332 0.5222 1.0058 0.1312  0.3003  0.2995  1049 HOH B O   
8442 O  O   . HOH P .   ? 0.8643 0.5509 0.6964 0.0173  0.0872  -0.1351 1050 HOH B O   
8443 O  O   . HOH P .   ? 0.2767 0.5295 0.6712 -0.0463 -0.0493 -0.0147 1051 HOH B O   
8444 O  O   . HOH P .   ? 0.4272 0.7023 0.9585 0.0809  0.2639  0.1630  1052 HOH B O   
8445 O  O   . HOH P .   ? 0.5683 0.5826 0.4297 0.1643  -0.0073 0.0532  1053 HOH B O   
8446 O  O   . HOH P .   ? 0.2319 0.4784 0.3597 0.0236  -0.0740 -0.0823 1054 HOH B O   
8447 O  O   . HOH P .   ? 0.4622 0.6249 0.6009 0.1984  -0.1457 0.0144  1055 HOH B O   
8448 O  O   . HOH P .   ? 0.4603 0.5287 0.5322 0.0818  0.0750  0.0416  1056 HOH B O   
8449 O  O   . HOH P .   ? 0.7139 0.5034 0.7533 -0.0528 0.1221  -0.1796 1057 HOH B O   
8450 O  O   . HOH P .   ? 0.7180 0.4519 0.5122 -0.0457 -0.3097 -0.0206 1058 HOH B O   
8451 O  O   . HOH P .   ? 0.2780 0.4255 0.3786 -0.0800 -0.0826 -0.0577 1059 HOH B O   
8452 O  O   . HOH P .   ? 0.4413 0.6955 0.5188 -0.1739 0.1159  0.2061  1060 HOH B O   
8453 O  O   . HOH P .   ? 0.3971 0.5083 0.6099 0.1471  -0.2510 -0.1879 1061 HOH B O   
8454 O  O   . HOH P .   ? 0.6188 0.4334 0.7149 -0.2115 0.1859  -0.2076 1062 HOH B O   
8455 O  O   . HOH P .   ? 0.4113 0.7531 0.6907 0.0443  -0.2383 -0.2438 1063 HOH B O   
8456 O  O   . HOH P .   ? 0.4714 0.4091 0.8535 -0.0806 -0.0028 -0.0352 1064 HOH B O   
8457 O  O   . HOH P .   ? 0.1978 0.4115 0.3467 -0.0013 -0.0211 0.1016  1065 HOH B O   
8458 O  O   . HOH P .   ? 0.8092 0.3815 0.9815 0.0946  -0.2054 0.1868  1066 HOH B O   
8459 O  O   . HOH P .   ? 0.9272 0.2640 0.6309 -0.0215 0.0247  -0.1112 1067 HOH B O   
8460 O  O   . HOH P .   ? 1.0686 0.7182 0.4196 -0.0741 -0.0147 0.1355  1068 HOH B O   
8461 O  O   . HOH P .   ? 0.5014 0.2872 0.4819 0.0322  -0.0048 0.0594  1069 HOH B O   
# 
